CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  uwu  ***

elNémo ID: 22022820254074740

Job options:

ID        	=	 22022820254074740
JOBID     	=	 uwu
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER uwu

HEADER    TRANSFERASE                             18-SEP-18   6HOU              
TITLE     HUMAN PROTEIN KINASE CK2 ALPHA IN COMPLEX WITH VANILLIN               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN (RESIDUES 1-337);                            
COMPND   5 SYNONYM: CK II ALPHA;                                                
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE DOMAIN, TRANSFERASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BATTISTUTTA,G.LOLLI                                                 
REVDAT   3   13-MAY-20 6HOU    1       JRNL   HETSYN                            
REVDAT   2   13-NOV-19 6HOU    1       JRNL                                     
REVDAT   1   02-OCT-19 6HOU    0                                                
JRNL        AUTH   G.COZZA,F.ZONTA,A.DALLE VEDOVE,A.VENERANDO,S.DALL'ACQUA,     
JRNL        AUTH 2 R.BATTISTUTTA,M.RUZZENE,G.LOLLI                              
JRNL        TITL   BIOCHEMICAL AND CELLULAR MECHANISM OF PROTEIN KINASE CK2     
JRNL        TITL 2 INHIBITION BY DECEPTIVE CURCUMIN.                            
JRNL        REF    FEBS J.                       V. 287  1850 2020              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   31661600                                                     
JRNL        DOI    10.1111/FEBS.15111                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 29332                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1497                            
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 36.5251 -  4.0016    1.00     2632   143  0.1471 0.1810        
REMARK   3     2  4.0016 -  3.1768    0.99     2542   138  0.1459 0.1814        
REMARK   3     3  3.1768 -  2.7754    0.99     2527   132  0.1733 0.1778        
REMARK   3     4  2.7754 -  2.5217    0.99     2539   132  0.1841 0.2250        
REMARK   3     5  2.5217 -  2.3410    1.00     2536   138  0.1805 0.2107        
REMARK   3     6  2.3410 -  2.2030    1.00     2509   144  0.1821 0.2309        
REMARK   3     7  2.2030 -  2.0926    1.00     2536   122  0.1840 0.2522        
REMARK   3     8  2.0926 -  2.0016    0.99     2504   148  0.2020 0.2307        
REMARK   3     9  2.0016 -  1.9245    1.00     2502   126  0.2142 0.2562        
REMARK   3    10  1.9245 -  1.8581    0.99     2519   151  0.2323 0.3167        
REMARK   3    11  1.8581 -  1.8000    0.99     2489   123  0.2400 0.3049        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.004           2891                                  
REMARK   3   ANGLE     :  0.841           3917                                  
REMARK   3   CHIRALITY :  0.034            406                                  
REMARK   3   PLANARITY :  0.004            502                                  
REMARK   3   DIHEDRAL  : 14.147           1094                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 44 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9751  -0.8893 -10.8854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1885 T22:   0.1090                                     
REMARK   3      T33:   0.2877 T12:  -0.0503                                     
REMARK   3      T13:   0.0597 T23:   0.1098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9930 L22:  -0.2483                                     
REMARK   3      L33:   1.2843 L12:  -0.1431                                     
REMARK   3      L13:  -0.0912 L23:   0.1766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2590 S12:  -0.1949 S13:  -0.1948                       
REMARK   3      S21:   0.0602 S22:   0.1404 S23:   0.1181                       
REMARK   3      S31:   0.2258 S32:  -0.0738 S33:  -0.1403                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 108 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -28.3140   9.9342 -13.4968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1174 T22:   0.1862                                     
REMARK   3      T33:   0.1701 T12:   0.0009                                     
REMARK   3      T13:  -0.0197 T23:   0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6789 L22:   0.5907                                     
REMARK   3      L33:   0.4127 L12:  -0.7934                                     
REMARK   3      L13:   0.3163 L23:  -0.4155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0370 S12:  -0.0793 S13:  -0.1038                       
REMARK   3      S21:  -0.0426 S22:  -0.0621 S23:   0.1196                       
REMARK   3      S31:   0.1093 S32:  -0.0735 S33:  -0.0059                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5867  18.2680  -8.2470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1364 T22:   0.1915                                     
REMARK   3      T33:   0.1201 T12:  -0.0235                                     
REMARK   3      T13:   0.0118 T23:   0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6850 L22:   0.3399                                     
REMARK   3      L33:   1.6350 L12:   0.5442                                     
REMARK   3      L13:  -0.4094 L23:   1.2172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0331 S12:  -0.3785 S13:   0.1961                       
REMARK   3      S21:  -0.2630 S22:   0.1910 S23:   0.3159                       
REMARK   3      S31:  -0.2257 S32:   0.2109 S33:   0.0761                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 226 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6905   8.1114 -16.4842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.1018                                     
REMARK   3      T33:   0.1224 T12:  -0.0111                                     
REMARK   3      T13:  -0.0113 T23:   0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1293 L22:   0.7194                                     
REMARK   3      L33:   0.7030 L12:  -0.0975                                     
REMARK   3      L13:  -0.5134 L23:  -0.1976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0563 S12:  -0.1239 S13:  -0.0933                       
REMARK   3      S21:  -0.0917 S22:   0.0633 S23:   0.1347                       
REMARK   3      S31:   0.0091 S32:  -0.0057 S33:   0.0132                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 280 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4909   9.2250 -29.0005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1839 T22:   0.0947                                     
REMARK   3      T33:   0.1186 T12:  -0.0185                                     
REMARK   3      T13:  -0.0142 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1805 L22:   0.7416                                     
REMARK   3      L33:   1.4700 L12:   0.6716                                     
REMARK   3      L13:  -0.4998 L23:   0.6453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1758 S12:   0.1766 S13:   0.0478                       
REMARK   3      S21:  -0.1772 S22:   0.0381 S23:  -0.0044                       
REMARK   3      S31:  -0.0519 S32:   0.1117 S33:  -0.1591                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 281 THROUGH 330 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4445  15.2150 -10.0477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1161 T22:   0.2334                                     
REMARK   3      T33:   0.1243 T12:  -0.0161                                     
REMARK   3      T13:  -0.0053 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7018 L22:   0.6874                                     
REMARK   3      L33:   1.0299 L12:   0.0120                                     
REMARK   3      L13:  -0.7137 L23:  -0.2778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0383 S12:  -0.3823 S13:   0.0594                       
REMARK   3      S21:  -0.0105 S22:  -0.0293 S23:   0.0051                       
REMARK   3      S31:  -0.0567 S32:   0.2618 S33:  -0.0354                       
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 6HOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011983.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29389                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3Q04                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG4000, 0.2 M LITHIUM SULFATE, PH   
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       23.27150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 430 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     GLY A   335                                                      
REMARK 465     SER A   336                                                      
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    ASP A 156       43.91   -149.06                                   
REMARK 500    ASP A 175       76.12     50.23                                   
REMARK 500    ALA A 193      159.81     60.59                                   
REMARK 500    ASP A 210     -159.62   -157.14                                   
REMARK 500    HIS A 234       70.51   -106.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue V55 A 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6HOP   RELATED DB: PDB                                   
REMARK 900 6HOP CONTAINS THE SAME PROTEIN COMPLEXED WITH ADDITIONAL LIGANDS     
REMARK 900 RELATED ID: 6HOQ   RELATED DB: PDB                                   
REMARK 900 6HOQ CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT LIGAND     
REMARK 900 RELATED ID: 6HOR   RELATED DB: PDB                                   
REMARK 900 6HOR CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT LIGAND     
REMARK 900 RELATED ID: 6HOT   RELATED DB: PDB                                   
REMARK 900 6HOT CONTAINS THE SAME PROTEIN COMPLEXED WITH A DIFFERENT LIGAND     
DBREF  6HOU A    1   336  UNP    P68400   CSK21_HUMAN      1    336             
SEQRES   1 A  336  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  336  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  336  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  336  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  336  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  336  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  336  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  336  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  336  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  336  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  336  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  336  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  336  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  336  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  336  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  336  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  336  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  336  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  336  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  336  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  336  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  336  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  336  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  336  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  336  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  336  THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER                  
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    V55  A 403      11                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     V55 4-HYDROXY-3-METHOXYBENZALDEHYDE                                  
HETSYN     V55 P-VANILLIN                                                       
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  V55    C8 H8 O3                                                     
FORMUL   5  HOH   *282(H2 O)                                                    
HELIX    1 AA1 PRO A   20  ASP A   25  1                                   6    
HELIX    2 AA2 TYR A   26  HIS A   29  5                                   4    
HELIX    3 AA3 ASN A   35  ASP A   37  5                                   3    
HELIX    4 AA4 LYS A   74  ARG A   89  1                                  16    
HELIX    5 AA5 ASP A  120  TYR A  125  1                                   6    
HELIX    6 AA6 THR A  129  MET A  150  1                                  22    
HELIX    7 AA7 LYS A  158  HIS A  160  5                                   3    
HELIX    8 AA8 ASP A  175  ALA A  179  5                                   5    
HELIX    9 AA9 SER A  194  LYS A  198  5                                   5    
HELIX   10 AB1 GLY A  199  VAL A  204  1                                   6    
HELIX   11 AB2 TYR A  211  PHE A  227  1                                  17    
HELIX   12 AB3 ASP A  237  GLY A  250  1                                  14    
HELIX   13 AB4 GLY A  250  TYR A  261  1                                  12    
HELIX   14 AB5 ASP A  266  ILE A  272  5                                   7    
HELIX   15 AB6 ARG A  280  VAL A  285  5                                   6    
HELIX   16 AB7 ASN A  289  VAL A  293  5                                   5    
HELIX   17 AB8 SER A  294  LEU A  305  1                                  12    
HELIX   18 AB9 ASP A  308  ARG A  312  5                                   5    
HELIX   19 AC1 THR A  314  GLU A  320  1                                   7    
HELIX   20 AC2 HIS A  321  TYR A  325  5                                   5    
SHEET    1 AA1 5 TYR A  39  ARG A  47  0                                        
SHEET    2 AA1 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
SHEET    3 AA1 5 LYS A  64  LEU A  70 -1  O  VAL A  67   N  PHE A  54           
SHEET    4 AA1 5 PRO A 109  GLU A 114 -1  O  PHE A 113   N  VAL A  66           
SHEET    5 AA1 5 LEU A  97  LYS A 102 -1  N  VAL A 101   O  ALA A 110           
SHEET    1 AA2 2 ILE A 152  MET A 153  0                                        
SHEET    2 AA2 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1 AA3 2 VAL A 162  ASP A 165  0                                        
SHEET    2 AA3 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
CISPEP   1 GLU A  230    PRO A  231          0        -2.77                     
SITE     1 AC1  5 ARG A  80  ARG A 155  ASN A 189  VAL A 192                    
SITE     2 AC1  5 HOH A 520                                                     
SITE     1 AC2  8 ASP A 253  ARG A 278  ARG A 306  TYR A 307                    
SITE     2 AC2  8 ASP A 308  HOH A 559  HOH A 562  HOH A 576                    
SITE     1 AC3  5 LYS A  68  PHE A 113  ILE A 174  ASP A 175                    
SITE     2 AC3  5 HOH A 527                                                     
CRYST1   58.225   46.543   63.411  90.00 111.74  90.00 P 1 21 1      2          
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      0.017175  0.000000  0.006850        0.00000                         
SCALE2      0.000000  0.021486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016978        0.00000                         
ATOM      1  N   GLY A   3       1.654 -13.280 -30.189  1.00 37.02           N  
ANISOU    1  N   GLY A   3     4801   4365   4902   -159    235     46       N  
ATOM      2  CA  GLY A   3       0.644 -12.401 -29.628  1.00 37.81           C  
ANISOU    2  CA  GLY A   3     4894   4399   5074   -258    245    112       C  
ATOM      3  C   GLY A   3       1.205 -11.493 -28.551  1.00 37.42           C  
ANISOU    3  C   GLY A   3     4836   4452   4931   -204    226    179       C  
ATOM      4  O   GLY A   3       2.376 -11.602 -28.194  1.00 35.23           O  
ANISOU    4  O   GLY A   3     4559   4296   4530    -88    212    177       O  
ATOM      5  N   PRO A   4       0.370 -10.586 -28.024  1.00 38.75           N  
ANISOU    5  N   PRO A   4     4993   4579   5153   -287    224    233       N  
ATOM      6  CA  PRO A   4       0.825  -9.639 -26.999  1.00 35.93           C  
ANISOU    6  CA  PRO A   4     4622   4316   4714   -249    204    289       C  
ATOM      7  C   PRO A   4       1.107 -10.327 -25.666  1.00 32.95           C  
ANISOU    7  C   PRO A   4     4331   3882   4307    -89    287    348       C  
ATOM      8  O   PRO A   4       0.453 -11.314 -25.326  1.00 34.04           O  
ANISOU    8  O   PRO A   4     4551   3853   4531    -44    372    375       O  
ATOM      9  CB  PRO A   4      -0.351  -8.658 -26.865  1.00 37.89           C  
ANISOU    9  CB  PRO A   4     4846   4500   5051   -379    190    324       C  
ATOM     10  CG  PRO A   4      -1.295  -8.982 -28.003  1.00 40.17           C  
ANISOU   10  CG  PRO A   4     5116   4700   5449   -494    188    280       C  
ATOM     11  CD  PRO A   4      -1.059 -10.419 -28.335  1.00 40.29           C  
ANISOU   11  CD  PRO A   4     5186   4640   5484   -416    244    241       C  
ATOM     12  N   VAL A   5       2.087  -9.816 -24.931  1.00 28.29           N  
ANISOU   12  N   VAL A   5     3721   3437   3592     -6    265    369       N  
ATOM     13  CA  VAL A   5       2.367 -10.305 -23.589  1.00 26.68           C  
ANISOU   13  CA  VAL A   5     3584   3207   3347    147    341    433       C  
ATOM     14  C   VAL A   5       1.253  -9.842 -22.656  1.00 24.55           C  
ANISOU   14  C   VAL A   5     3340   2824   3165    105    382    502       C  
ATOM     15  O   VAL A   5       0.858  -8.680 -22.706  1.00 24.68           O  
ANISOU   15  O   VAL A   5     3298   2882   3196     -6    328    503       O  
ATOM     16  CB  VAL A   5       3.727  -9.801 -23.077  1.00 24.32           C  
ANISOU   16  CB  VAL A   5     3240   3121   2879    239    302    428       C  
ATOM     17  CG1 VAL A   5       3.975 -10.270 -21.650  1.00 24.93           C  
ANISOU   17  CG1 VAL A   5     3378   3183   2909    402    383    498       C  
ATOM     18  CG2 VAL A   5       4.853 -10.259 -24.008  1.00 25.36           C  
ANISOU   18  CG2 VAL A   5     3340   3385   2910    284    257    356       C  
ATOM     19  N   PRO A   6       0.729 -10.749 -21.817  1.00 22.94           N  
ANISOU   19  N   PRO A   6     3222   2475   3019    194    479    563       N  
ATOM     20  CA  PRO A   6      -0.340 -10.358 -20.889  1.00 23.12           C  
ANISOU   20  CA  PRO A   6     3264   2401   3118    161    521    630       C  
ATOM     21  C   PRO A   6       0.135  -9.398 -19.802  1.00 23.18           C  
ANISOU   21  C   PRO A   6     3233   2542   3033    212    500    667       C  
ATOM     22  O   PRO A   6       1.323  -9.335 -19.511  1.00 26.45           O  
ANISOU   22  O   PRO A   6     3626   3104   3320    311    483    655       O  
ATOM     23  CB  PRO A   6      -0.783 -11.694 -20.275  1.00 26.71           C  
ANISOU   23  CB  PRO A   6     3822   2689   3636    260    631    686       C  
ATOM     24  CG  PRO A   6       0.374 -12.618 -20.474  1.00 27.27           C  
ANISOU   24  CG  PRO A   6     3929   2809   3621    397    648    663       C  
ATOM     25  CD  PRO A   6       1.007 -12.196 -21.769  1.00 26.41           C  
ANISOU   25  CD  PRO A   6     3748   2821   3466    320    554    570       C  
ATOM     26  N   SER A   7      -0.803  -8.667 -19.210  1.00 21.68           N  
ANISOU   26  N   SER A   7     3030   2304   2905    147    503    705       N  
ATOM     27  CA  SER A   7      -0.500  -7.714 -18.147  1.00 20.21           C  
ANISOU   27  CA  SER A   7     2804   2230   2644    185    486    733       C  
ATOM     28  C   SER A   7      -1.484  -7.857 -16.989  1.00 21.13           C  
ANISOU   28  C   SER A   7     2960   2243   2826    221    558    810       C  
ATOM     29  O   SER A   7      -2.625  -8.271 -17.194  1.00 22.36           O  
ANISOU   29  O   SER A   7     3151   2246   3099    157    595    831       O  
ATOM     30  CB  SER A   7      -0.538  -6.278 -18.687  1.00 18.98           C  
ANISOU   30  CB  SER A   7     2569   2163   2478     49    387    686       C  
ATOM     31  OG  SER A   7      -0.236  -5.339 -17.667  1.00 19.81           O  
ANISOU   31  OG  SER A   7     2639   2373   2514     81    369    704       O  
ATOM     32  N   ARG A   8      -1.029  -7.528 -15.780  1.00 21.71           N  
ANISOU   32  N   ARG A   8     3020   2413   2818    323    577    848       N  
ATOM     33  CA  ARG A   8      -1.890  -7.460 -14.592  1.00 20.79           C  
ANISOU   33  CA  ARG A   8     2919   2235   2745    357    634    919       C  
ATOM     34  C   ARG A   8      -1.638  -6.163 -13.837  1.00 21.96           C  
ANISOU   34  C   ARG A   8     2998   2522   2825    353    584    908       C  
ATOM     35  O   ARG A   8      -0.504  -5.678 -13.802  1.00 23.67           O  
ANISOU   35  O   ARG A   8     3170   2896   2926    390    540    869       O  
ATOM     36  CB  ARG A   8      -1.632  -8.631 -13.639  1.00 26.29           C  
ANISOU   36  CB  ARG A   8     3680   2898   3410    522    734    993       C  
ATOM     37  CG  ARG A   8      -1.811 -10.008 -14.227  1.00 33.06           C  
ANISOU   37  CG  ARG A   8     4622   3608   4333    547    795   1008       C  
ATOM     38  CD  ARG A   8      -3.278 -10.391 -14.350  1.00 36.30           C  
ANISOU   38  CD  ARG A   8     5064   3846   4883    445    828   1022       C  
ATOM     39  NE  ARG A   8      -3.410 -11.750 -14.869  1.00 36.31           N  
ANISOU   39  NE  ARG A   8     5134   3726   4936    460    875   1005       N  
ATOM     40  CZ  ARG A   8      -3.300 -12.066 -16.154  1.00 36.51           C  
ANISOU   40  CZ  ARG A   8     5182   3685   5005    395    858    961       C  
ATOM     41  NH1 ARG A   8      -3.067 -11.122 -17.059  1.00 30.27           N  
ANISOU   41  NH1 ARG A   8     4328   2971   4202    297    776    903       N  
ATOM     42  NH2 ARG A   8      -3.419 -13.328 -16.539  1.00 39.83           N  
ANISOU   42  NH2 ARG A   8     5667   3995   5471    415    904    944       N  
ATOM     43  N   ALA A   9      -2.682  -5.617 -13.217  1.00 16.73           N  
ANISOU   43  N   ALA A   9     2324   1806   2227    309    591    939       N  
ATOM     44  CA  ALA A   9      -2.515  -4.486 -12.311  1.00 17.47           C  
ANISOU   44  CA  ALA A   9     2358   2018   2260    324    557    933       C  
ATOM     45  C   ALA A   9      -1.536  -4.882 -11.210  1.00 19.44           C  
ANISOU   45  C   ALA A   9     2604   2392   2392    489    607    966       C  
ATOM     46  O   ALA A   9      -1.532  -6.022 -10.761  1.00 21.24           O  
ANISOU   46  O   ALA A   9     2884   2566   2619    597    690   1028       O  
ATOM     47  CB  ALA A   9      -3.851  -4.060 -11.715  1.00 17.71           C  
ANISOU   47  CB  ALA A   9     2385   1965   2379    277    571    968       C  
ATOM     48  N   ARG A  10      -0.694  -3.951 -10.785  1.00 20.73           N  
ANISOU   48  N   ARG A  10     2704   2723   2450    508    559    924       N  
ATOM     49  CA  ARG A  10       0.275  -4.275  -9.748  1.00 21.74           C  
ANISOU   49  CA  ARG A  10     2814   2994   2451    666    605    949       C  
ATOM     50  C   ARG A  10      -0.348  -4.154  -8.360  1.00 20.51           C  
ANISOU   50  C   ARG A  10     2644   2846   2303    740    657   1008       C  
ATOM     51  O   ARG A  10       0.234  -4.597  -7.369  1.00 21.51           O  
ANISOU   51  O   ARG A  10     2761   3073   2339    887    715   1050       O  
ATOM     52  CB  ARG A  10       1.508  -3.379  -9.875  1.00 26.01           C  
ANISOU   52  CB  ARG A  10     3287   3731   2865    653    536    873       C  
ATOM     53  CG  ARG A  10       2.227  -3.539 -11.203  1.00 32.87           C  
ANISOU   53  CG  ARG A  10     4161   4620   3708    591    484    817       C  
ATOM     54  CD  ARG A  10       3.673  -3.106 -11.100  1.00 40.43           C  
ANISOU   54  CD  ARG A  10     5059   5800   4504    635    448    761       C  
ATOM     55  NE  ARG A  10       3.789  -1.744 -10.592  1.00 47.24           N  
ANISOU   55  NE  ARG A  10     5854   6768   5326    569    394    716       N  
ATOM     56  CZ  ARG A  10       4.921  -1.209 -10.148  1.00 50.86           C  
ANISOU   56  CZ  ARG A  10     6250   7433   5641    607    371    669       C  
ATOM     57  NH1 ARG A  10       6.038  -1.922 -10.155  1.00 54.34           N  
ANISOU   57  NH1 ARG A  10     6683   8007   5956    719    397    664       N  
ATOM     58  NH2 ARG A  10       4.935   0.038  -9.700  1.00 51.26           N  
ANISOU   58  NH2 ARG A  10     6247   7560   5670    535    324    623       N  
ATOM     59  N   VAL A  11      -1.542  -3.568  -8.295  1.00 18.52           N  
ANISOU   59  N   VAL A  11     2386   2496   2154    644    638   1013       N  
ATOM     60  CA  VAL A  11      -2.271  -3.439  -7.034  1.00 19.62           C  
ANISOU   60  CA  VAL A  11     2507   2639   2308    704    683   1068       C  
ATOM     61  C   VAL A  11      -3.754  -3.726  -7.244  1.00 21.04           C  
ANISOU   61  C   VAL A  11     2727   2639   2627    626    706   1111       C  
ATOM     62  O   VAL A  11      -4.244  -3.670  -8.373  1.00 21.77           O  
ANISOU   62  O   VAL A  11     2845   2623   2803    505    668   1079       O  
ATOM     63  CB  VAL A  11      -2.119  -2.030  -6.416  1.00 22.08           C  
ANISOU   63  CB  VAL A  11     2740   3082   2569    676    621   1010       C  
ATOM     64  CG1 VAL A  11      -0.687  -1.801  -5.956  1.00 26.79           C  
ANISOU   64  CG1 VAL A  11     3287   3879   3015    766    614    973       C  
ATOM     65  CG2 VAL A  11      -2.539  -0.966  -7.402  1.00 22.32           C  
ANISOU   65  CG2 VAL A  11     2758   3057   2667    511    528    939       C  
ATOM     66  N   TYR A  12      -4.453  -4.039  -6.154  1.00 20.62           N  
ANISOU   66  N   TYR A  12     2674   2570   2593    696    768   1179       N  
ATOM     67  CA  TYR A  12      -5.885  -4.326  -6.196  1.00 23.92           C  
ANISOU   67  CA  TYR A  12     3106   2851   3130    614    775   1173       C  
ATOM     68  C   TYR A  12      -6.223  -5.324  -7.292  1.00 23.47           C  
ANISOU   68  C   TYR A  12     3112   2655   3152    541    782   1147       C  
ATOM     69  O   TYR A  12      -7.265  -5.221  -7.932  1.00 23.96           O  
ANISOU   69  O   TYR A  12     3180   2622   3301    423    748   1108       O  
ATOM     70  CB  TYR A  12      -6.682  -3.041  -6.416  1.00 21.58           C  
ANISOU   70  CB  TYR A  12     2773   2544   2884    504    708   1145       C  
ATOM     71  CG  TYR A  12      -6.407  -1.955  -5.403  1.00 22.13           C  
ANISOU   71  CG  TYR A  12     2774   2754   2879    558    682   1138       C  
ATOM     72  CD1 TYR A  12      -6.441  -2.221  -4.040  1.00 24.49           C  
ANISOU   72  CD1 TYR A  12     3045   3134   3127    682    743   1197       C  
ATOM     73  CD2 TYR A  12      -6.109  -0.663  -5.813  1.00 19.64           C  
ANISOU   73  CD2 TYR A  12     2417   2499   2548    477    589   1050       C  
ATOM     74  CE1 TYR A  12      -6.191  -1.221  -3.110  1.00 25.59           C  
ANISOU   74  CE1 TYR A  12     3109   3416   3197    725    710   1159       C  
ATOM     75  CE2 TYR A  12      -5.857   0.342  -4.895  1.00 20.74           C  
ANISOU   75  CE2 TYR A  12     2490   2766   2623    515    557   1012       C  
ATOM     76  CZ  TYR A  12      -5.898   0.056  -3.544  1.00 21.74           C  
ANISOU   76  CZ  TYR A  12     2584   2978   2698    640    617   1062       C  
ATOM     77  OH  TYR A  12      -5.649   1.056  -2.629  1.00 23.55           O  
ANISOU   77  OH  TYR A  12     2742   3343   2863    678    584   1016       O  
ATOM     78  N   THR A  13      -5.330  -6.278  -7.517  1.00 24.03           N  
ANISOU   78  N   THR A  13     3224   2725   3180    617    823   1162       N  
ATOM     79  CA  THR A  13      -5.439  -7.157  -8.673  1.00 24.90           C  
ANISOU   79  CA  THR A  13     3393   2717   3351    554    825   1134       C  
ATOM     80  C   THR A  13      -6.687  -8.041  -8.613  1.00 25.28           C  
ANISOU   80  C   THR A  13     3469   2646   3488    500    855   1127       C  
ATOM     81  O   THR A  13      -7.395  -8.191  -9.608  1.00 24.69           O  
ANISOU   81  O   THR A  13     3412   2483   3485    383    820   1079       O  
ATOM     82  CB  THR A  13      -4.193  -8.057  -8.813  1.00 24.08           C  
ANISOU   82  CB  THR A  13     3332   2643   3175    671    871   1159       C  
ATOM     83  OG1 THR A  13      -3.004  -7.258  -8.717  1.00 25.64           O  
ANISOU   83  OG1 THR A  13     3494   2991   3257    735    842   1166       O  
ATOM     84  CG2 THR A  13      -4.203  -8.768 -10.152  1.00 19.96           C  
ANISOU   84  CG2 THR A  13     2865   2007   2711    600    863   1125       C  
ATOM     85  N   ASP A  14      -6.959  -8.607  -7.442  1.00 24.21           N  
ANISOU   85  N   ASP A  14     3334   2526   3339    585    916   1175       N  
ATOM     86  CA  ASP A  14      -8.031  -9.589  -7.292  1.00 28.45           C  
ANISOU   86  CA  ASP A  14     3904   2963   3944    546    953   1182       C  
ATOM     87  C   ASP A  14      -9.177  -9.115  -6.406  1.00 27.94           C  
ANISOU   87  C   ASP A  14     3794   2917   3903    518    950   1198       C  
ATOM     88  O   ASP A  14      -9.840  -9.928  -5.759  1.00 27.50           O  
ANISOU   88  O   ASP A  14     3756   2822   3870    537   1000   1233       O  
ATOM     89  CB  ASP A  14      -7.476 -10.897  -6.717  1.00 33.33           C  
ANISOU   89  CB  ASP A  14     4571   3561   4531    663   1038   1234       C  
ATOM     90  CG  ASP A  14      -6.467 -11.555  -7.631  1.00 38.81           C  
ANISOU   90  CG  ASP A  14     5320   4219   5205    696   1049   1220       C  
ATOM     91  OD1 ASP A  14      -6.885 -12.110  -8.668  1.00 43.18           O  
ANISOU   91  OD1 ASP A  14     5916   4666   5824    605   1035   1181       O  
ATOM     92  OD2 ASP A  14      -5.263 -11.527  -7.307  1.00 37.91           O  
ANISOU   92  OD2 ASP A  14     5205   4194   5004    817   1071   1246       O  
ATOM     93  N  AVAL A  15      -9.412  -7.811  -6.371  0.29 26.71           N  
ANISOU   93  N  AVAL A  15     3584   2822   3743    475    892   1175       N  
ATOM     94  N  BVAL A  15      -9.403  -7.804  -6.381  0.71 26.77           N  
ANISOU   94  N  BVAL A  15     3592   2829   3750    474    891   1175       N  
ATOM     95  CA AVAL A  15     -10.475  -7.272  -5.533  0.29 26.39           C  
ANISOU   95  CA AVAL A  15     3499   2807   3720    457    887   1191       C  
ATOM     96  CA BVAL A  15     -10.475  -7.217  -5.579  0.71 26.10           C  
ANISOU   96  CA BVAL A  15     3461   2771   3684    453    883   1188       C  
ATOM     97  C  AVAL A  15     -11.850  -7.793  -5.952  0.29 27.08           C  
ANISOU   97  C  AVAL A  15     3609   2801   3879    352    879   1167       C  
ATOM     98  C  BVAL A  15     -11.833  -7.799  -5.958  0.71 27.20           C  
ANISOU   98  C  BVAL A  15     3624   2816   3894    353    879   1167       C  
ATOM     99  O  AVAL A  15     -12.663  -8.144  -5.101  0.29 27.40           O  
ANISOU   99  O  AVAL A  15     3639   2841   3932    369    916   1205       O  
ATOM    100  O  BVAL A  15     -12.611  -8.202  -5.092  0.71 27.45           O  
ANISOU  100  O  BVAL A  15     3648   2846   3937    374    919   1207       O  
ATOM    101  CB AVAL A  15     -10.474  -5.742  -5.563  0.29 24.89           C  
ANISOU  101  CB AVAL A  15     3253   2688   3517    424    821   1167       C  
ATOM    102  CB BVAL A  15     -10.512  -5.678  -5.728  0.71 25.08           C  
ANISOU  102  CB BVAL A  15     3279   2705   3547    408    813   1158       C  
ATOM    103  CG1AVAL A  15      -9.409  -5.197  -4.623  0.29 24.21           C  
ANISOU  103  CG1AVAL A  15     3127   2728   3343    547    840   1208       C  
ATOM    104  CG1BVAL A  15     -11.862  -5.115  -5.293  0.71 23.92           C  
ANISOU  104  CG1BVAL A  15     3095   2555   3439    355    793   1156       C  
ATOM    105  CG2AVAL A  15     -10.222  -5.267  -6.965  0.29 24.89           C  
ANISOU  105  CG2AVAL A  15     3269   2647   3540    324    754   1103       C  
ATOM    106  CG2BVAL A  15      -9.381  -5.043  -4.930  0.71 24.05           C  
ANISOU  106  CG2BVAL A  15     3110   2697   3330    522    824   1194       C  
ATOM    107  N   ASN A  16     -12.100  -7.862  -7.258  1.00 27.64           N  
ANISOU  107  N   ASN A  16     3706   2806   3989    246    832   1104       N  
ATOM    108  CA  ASN A  16     -13.378  -8.369  -7.758  1.00 29.27           C  
ANISOU  108  CA  ASN A  16     3933   2941   4248    145    820   1075       C  
ATOM    109  C   ASN A  16     -13.473  -9.887  -7.707  1.00 32.27           C  
ANISOU  109  C   ASN A  16     4371   3243   4647    162    884   1103       C  
ATOM    110  O   ASN A  16     -14.570 -10.446  -7.614  1.00 33.18           O  
ANISOU  110  O   ASN A  16     4500   3313   4794    107    898   1107       O  
ATOM    111  CB  ASN A  16     -13.623  -7.884  -9.187  1.00 28.14           C  
ANISOU  111  CB  ASN A  16     3792   2773   4129     31    745    996       C  
ATOM    112  CG  ASN A  16     -14.039  -6.430  -9.238  1.00 27.31           C  
ANISOU  112  CG  ASN A  16     3635   2725   4018    -12    681    966       C  
ATOM    113  OD1 ASN A  16     -14.843  -5.976  -8.421  1.00 28.01           O  
ANISOU  113  OD1 ASN A  16     3690   2844   4109     -4    687    989       O  
ATOM    114  ND2 ASN A  16     -13.484  -5.685 -10.188  1.00 21.96           N  
ANISOU  114  ND2 ASN A  16     2949   2062   3332    -56    621    917       N  
ATOM    115  N   THR A  17     -12.324 -10.550  -7.764  1.00 33.56           N  
ANISOU  115  N   THR A  17     4571   3391   4788    240    924   1124       N  
ATOM    116  CA  THR A  17     -12.278 -12.003  -7.689  1.00 35.62           C  
ANISOU  116  CA  THR A  17     4895   3573   5067    271    990   1156       C  
ATOM    117  C   THR A  17     -12.888 -12.492  -6.380  1.00 34.51           C  
ANISOU  117  C   THR A  17     4752   3439   4923    323   1050   1225       C  
ATOM    118  O   THR A  17     -13.580 -13.508  -6.348  1.00 37.96           O  
ANISOU  118  O   THR A  17     5230   3797   5394    288   1086   1242       O  
ATOM    119  CB  THR A  17     -10.833 -12.533  -7.804  1.00 38.09           C  
ANISOU  119  CB  THR A  17     5245   3885   5341    374   1029   1176       C  
ATOM    120  OG1 THR A  17     -10.135 -11.828  -8.839  1.00 39.26           O  
ANISOU  120  OG1 THR A  17     5382   4057   5480    340    971   1124       O  
ATOM    121  CG2 THR A  17     -10.831 -14.023  -8.104  1.00 39.86           C  
ANISOU  121  CG2 THR A  17     5546   4003   5596    382   1085   1191       C  
ATOM    122  N   HIS A  18     -12.650 -11.749  -5.306  1.00 31.43           N  
ANISOU  122  N   HIS A  18     4309   3145   4490    404   1061   1265       N  
ATOM    123  CA  HIS A  18     -13.071 -12.190  -3.980  1.00 34.25           C  
ANISOU  123  CA  HIS A  18     4654   3525   4834    473   1123   1338       C  
ATOM    124  C   HIS A  18     -14.282 -11.427  -3.441  1.00 33.59           C  
ANISOU  124  C   HIS A  18     4514   3483   4765    419   1096   1342       C  
ATOM    125  O   HIS A  18     -14.737 -11.682  -2.325  1.00 34.05           O  
ANISOU  125  O   HIS A  18     4552   3572   4814    470   1141   1405       O  
ATOM    126  CB  HIS A  18     -11.895 -12.083  -3.014  1.00 34.23           C  
ANISOU  126  CB  HIS A  18     4629   3617   4761    627   1168   1392       C  
ATOM    127  CG  HIS A  18     -10.695 -12.865  -3.452  1.00 34.86           C  
ANISOU  127  CG  HIS A  18     4764   3667   4813    696   1202   1395       C  
ATOM    128  ND1 HIS A  18     -10.633 -14.239  -3.361  1.00 36.99           N  
ANISOU  128  ND1 HIS A  18     5103   3853   5098    730   1267   1432       N  
ATOM    129  CD2 HIS A  18      -9.526 -12.471  -4.005  1.00 33.81           C  
ANISOU  129  CD2 HIS A  18     4633   3577   4637    739   1180   1367       C  
ATOM    130  CE1 HIS A  18      -9.468 -14.656  -3.824  1.00 36.22           C  
ANISOU  130  CE1 HIS A  18     5046   3750   4966    798   1286   1426       C  
ATOM    131  NE2 HIS A  18      -8.777 -13.604  -4.222  1.00 35.03           N  
ANISOU  131  NE2 HIS A  18     4854   3680   4777    805   1233   1387       N  
ATOM    132  N   ARG A  19     -14.801 -10.494  -4.234  1.00 32.01           N  
ANISOU  132  N   ARG A  19     4287   3287   4586    321   1022   1278       N  
ATOM    133  CA  ARG A  19     -16.110  -9.902  -3.958  1.00 32.68           C  
ANISOU  133  CA  ARG A  19     4331   3394   4692    253    996   1273       C  
ATOM    134  C   ARG A  19     -17.189 -10.932  -4.283  1.00 34.24           C  
ANISOU  134  C   ARG A  19     4574   3505   4930    165   1015   1272       C  
ATOM    135  O   ARG A  19     -16.962 -11.825  -5.098  1.00 34.06           O  
ANISOU  135  O   ARG A  19     4610   3402   4928    127   1023   1248       O  
ATOM    136  CB  ARG A  19     -16.340  -8.629  -4.785  1.00 31.91           C  
ANISOU  136  CB  ARG A  19     4198   3323   4601    177    913   1204       C  
ATOM    137  CG  ARG A  19     -15.547  -7.406  -4.356  1.00 33.71           C  
ANISOU  137  CG  ARG A  19     4373   3644   4793    246    887   1209       C  
ATOM    138  CD  ARG A  19     -16.288  -6.544  -3.346  1.00 36.55           C  
ANISOU  138  CD  ARG A  19     4667   4079   5143    273    885   1243       C  
ATOM    139  NE  ARG A  19     -15.465  -5.419  -2.905  1.00 38.40           N  
ANISOU  139  NE  ARG A  19     4852   4404   5336    344    862   1252       N  
ATOM    140  CZ  ARG A  19     -15.818  -4.556  -1.957  1.00 40.24           C  
ANISOU  140  CZ  ARG A  19     5020   4723   5548    392    860   1287       C  
ATOM    141  NH1 ARG A  19     -16.988  -4.680  -1.345  1.00 41.13           N  
ANISOU  141  NH1 ARG A  19     5106   4844   5677    379    879   1319       N  
ATOM    142  NH2 ARG A  19     -14.999  -3.570  -1.622  1.00 41.05           N  
ANISOU  142  NH2 ARG A  19     5082   4909   5606    454    838   1292       N  
ATOM    143  N   PRO A  20     -18.370 -10.814  -3.656  1.00 35.98           N  
ANISOU  143  N   PRO A  20     4767   3747   5158    130   1023   1299       N  
ATOM    144  CA  PRO A  20     -19.479 -11.650  -4.127  1.00 37.42           C  
ANISOU  144  CA  PRO A  20     4989   3857   5373     24   1031   1287       C  
ATOM    145  C   PRO A  20     -19.874 -11.230  -5.539  1.00 39.00           C  
ANISOU  145  C   PRO A  20     5194   4032   5592    -90    961   1198       C  
ATOM    146  O   PRO A  20     -19.704 -10.062  -5.885  1.00 36.65           O  
ANISOU  146  O   PRO A  20     4854   3788   5282    -95    905   1155       O  
ATOM    147  CB  PRO A  20     -20.595 -11.369  -3.115  1.00 36.55           C  
ANISOU  147  CB  PRO A  20     4833   3800   5255     17   1049   1335       C  
ATOM    148  CG  PRO A  20     -20.265 -10.034  -2.545  1.00 38.31           C  
ANISOU  148  CG  PRO A  20     4982   4122   5451     88   1021   1340       C  
ATOM    149  CD  PRO A  20     -18.763  -9.941  -2.537  1.00 37.89           C  
ANISOU  149  CD  PRO A  20     4937   4084   5376    184   1027   1342       C  
ATOM    150  N   ARG A  21     -20.389 -12.158  -6.340  1.00 39.26           N  
ANISOU  150  N   ARG A  21     5276   3990   5650   -177    963   1172       N  
ATOM    151  CA  ARG A  21     -20.617 -11.877  -7.755  1.00 39.39           C  
ANISOU  151  CA  ARG A  21     5297   3992   5679   -273    900   1089       C  
ATOM    152  C   ARG A  21     -21.611 -10.730  -7.969  1.00 39.00           C  
ANISOU  152  C   ARG A  21     5193   4008   5616   -337    845   1050       C  
ATOM    153  O   ARG A  21     -21.495  -9.982  -8.941  1.00 36.24           O  
ANISOU  153  O   ARG A  21     4828   3681   5261   -377    783    986       O  
ATOM    154  CB  ARG A  21     -21.084 -13.141  -8.481  1.00 42.22           C  
ANISOU  154  CB  ARG A  21     5711   4265   6067   -352    919   1076       C  
ATOM    155  CG  ARG A  21     -21.855 -12.895  -9.774  1.00 47.33           C  
ANISOU  155  CG  ARG A  21     6347   4917   6719   -468    858   1002       C  
ATOM    156  CD  ARG A  21     -21.942 -14.143 -10.638  1.00 52.56           C  
ANISOU  156  CD  ARG A  21     7061   5494   7415   -528    874    984       C  
ATOM    157  NE  ARG A  21     -21.698 -15.356  -9.867  1.00 58.50           N  
ANISOU  157  NE  ARG A  21     7867   6170   8189   -483    952   1050       N  
ATOM    158  CZ  ARG A  21     -21.003 -16.399 -10.312  1.00 63.28           C  
ANISOU  158  CZ  ARG A  21     8529   6688   8825   -464    984   1051       C  
ATOM    159  NH1 ARG A  21     -20.471 -16.377 -11.527  1.00 63.50           N  
ANISOU  159  NH1 ARG A  21     8562   6700   8864   -487    946    988       N  
ATOM    160  NH2 ARG A  21     -20.833 -17.462  -9.536  1.00 65.69           N  
ANISOU  160  NH2 ARG A  21     8888   6923   9147   -419   1058   1116       N  
ATOM    161  N   GLU A  22     -22.559 -10.569  -7.045  1.00 37.80           N  
ANISOU  161  N   GLU A  22     5012   3893   5458   -341    870   1093       N  
ATOM    162  CA  GLU A  22     -23.511  -9.455  -7.097  1.00 38.05           C  
ANISOU  162  CA  GLU A  22     4989   3992   5477   -386    829   1065       C  
ATOM    163  C   GLU A  22     -22.798  -8.108  -7.266  1.00 32.53           C  
ANISOU  163  C   GLU A  22     4249   3344   4767   -337    778   1034       C  
ATOM    164  O   GLU A  22     -23.337  -7.185  -7.875  1.00 31.64           O  
ANISOU  164  O   GLU A  22     4106   3266   4649   -387    727    985       O  
ATOM    165  CB  GLU A  22     -24.385  -9.431  -5.831  1.00 43.39           C  
ANISOU  165  CB  GLU A  22     5631   4711   6145   -366    874   1132       C  
ATOM    166  CG  GLU A  22     -23.957  -8.391  -4.789  1.00 50.91           C  
ANISOU  166  CG  GLU A  22     6522   5737   7083   -261    875   1173       C  
ATOM    167  CD  GLU A  22     -24.884  -8.312  -3.585  1.00 58.25           C  
ANISOU  167  CD  GLU A  22     7405   6726   8001   -240    915   1240       C  
ATOM    168  OE1 GLU A  22     -26.115  -8.211  -3.776  1.00 59.61           O  
ANISOU  168  OE1 GLU A  22     7560   6919   8171   -324    908   1226       O  
ATOM    169  OE2 GLU A  22     -24.374  -8.337  -2.443  1.00 60.89           O  
ANISOU  169  OE2 GLU A  22     7716   7098   8322   -137    953   1309       O  
ATOM    170  N   TYR A  23     -21.576  -8.013  -6.748  1.00 31.42           N  
ANISOU  170  N   TYR A  23     4108   3208   4620   -239    794   1064       N  
ATOM    171  CA  TYR A  23     -20.845  -6.752  -6.738  1.00 28.58           C  
ANISOU  171  CA  TYR A  23     3709   2901   4249   -189    751   1047       C  
ATOM    172  C   TYR A  23     -20.438  -6.287  -8.129  1.00 26.13           C  
ANISOU  172  C   TYR A  23     3415   2576   3939   -249    685    968       C  
ATOM    173  O   TYR A  23     -20.545  -5.103  -8.441  1.00 25.24           O  
ANISOU  173  O   TYR A  23     3267   2502   3822   -264    633    934       O  
ATOM    174  CB  TYR A  23     -19.601  -6.867  -5.858  1.00 25.81           C  
ANISOU  174  CB  TYR A  23     3355   2569   3881    -73    789   1100       C  
ATOM    175  CG  TYR A  23     -18.790  -5.591  -5.774  1.00 23.52           C  
ANISOU  175  CG  TYR A  23     3025   2338   3575    -23    748   1089       C  
ATOM    176  CD1 TYR A  23     -19.119  -4.600  -4.864  1.00 23.73           C  
ANISOU  176  CD1 TYR A  23     2989   2436   3592     23    744   1124       C  
ATOM    177  CD2 TYR A  23     -17.687  -5.384  -6.597  1.00 22.30           C  
ANISOU  177  CD2 TYR A  23     2891   2170   3411    -24    715   1048       C  
ATOM    178  CE1 TYR A  23     -18.387  -3.436  -4.777  1.00 22.43           C  
ANISOU  178  CE1 TYR A  23     2789   2323   3413     64    706   1117       C  
ATOM    179  CE2 TYR A  23     -16.955  -4.219  -6.522  1.00 17.49           C  
ANISOU  179  CE2 TYR A  23     2247   1613   2785     11    677   1041       C  
ATOM    180  CZ  TYR A  23     -17.306  -3.250  -5.605  1.00 23.26           C  
ANISOU  180  CZ  TYR A  23     2920   2408   3509     53    673   1075       C  
ATOM    181  OH  TYR A  23     -16.582  -2.084  -5.512  1.00 23.64           O  
ANISOU  181  OH  TYR A  23     2935   2507   3540     84    635   1071       O  
ATOM    182  N   TRP A  24     -19.948  -7.207  -8.953  1.00 25.57           N  
ANISOU  182  N   TRP A  24     3393   2449   3873   -277    688    943       N  
ATOM    183  CA  TRP A  24     -19.399  -6.826 -10.254  1.00 25.92           C  
ANISOU  183  CA  TRP A  24     3449   2488   3912   -322    629    877       C  
ATOM    184  C   TRP A  24     -20.261  -7.287 -11.425  1.00 27.08           C  
ANISOU  184  C   TRP A  24     3615   2609   4063   -427    602    825       C  
ATOM    185  O   TRP A  24     -20.101  -6.807 -12.543  1.00 27.45           O  
ANISOU  185  O   TRP A  24     3661   2670   4098   -474    547    768       O  
ATOM    186  CB  TRP A  24     -17.974  -7.371 -10.414  1.00 25.40           C  
ANISOU  186  CB  TRP A  24     3414   2394   3844   -265    647    887       C  
ATOM    187  CG  TRP A  24     -17.840  -8.828 -10.092  1.00 24.80           C  
ANISOU  187  CG  TRP A  24     3384   2256   3785   -238    714    928       C  
ATOM    188  CD1 TRP A  24     -17.351  -9.370  -8.939  1.00 27.75           C  
ANISOU  188  CD1 TRP A  24     3768   2624   4154   -144    781    998       C  
ATOM    189  CD2 TRP A  24     -18.202  -9.930 -10.931  1.00 27.23           C  
ANISOU  189  CD2 TRP A  24     3734   2498   4115   -303    723    906       C  
ATOM    190  NE1 TRP A  24     -17.385 -10.742  -9.009  1.00 30.78           N  
ANISOU  190  NE1 TRP A  24     4204   2934   4558   -146    832   1020       N  
ATOM    191  CE2 TRP A  24     -17.902 -11.110 -10.223  1.00 30.76           C  
ANISOU  191  CE2 TRP A  24     4222   2889   4576   -246    797    963       C  
ATOM    192  CE3 TRP A  24     -18.746 -10.034 -12.216  1.00 28.71           C  
ANISOU  192  CE3 TRP A  24     3928   2671   4311   -400    677    845       C  
ATOM    193  CZ2 TRP A  24     -18.133 -12.378 -10.754  1.00 33.69           C  
ANISOU  193  CZ2 TRP A  24     4644   3181   4977   -287    827    960       C  
ATOM    194  CZ3 TRP A  24     -18.973 -11.292 -12.742  1.00 30.43           C  
ANISOU  194  CZ3 TRP A  24     4187   2819   4557   -440    706    842       C  
ATOM    195  CH2 TRP A  24     -18.665 -12.448 -12.012  1.00 33.27           C  
ANISOU  195  CH2 TRP A  24     4591   3112   4937   -386    780    898       C  
ATOM    196  N   ASP A  25     -21.170  -8.222 -11.173  1.00 31.16           N  
ANISOU  196  N   ASP A  25     4150   3095   4594   -463    642    848       N  
ATOM    197  CA  ASP A  25     -22.063  -8.712 -12.218  1.00 30.38           C  
ANISOU  197  CA  ASP A  25     4063   2981   4498   -564    621    806       C  
ATOM    198  C   ASP A  25     -23.207  -7.724 -12.435  1.00 29.66           C  
ANISOU  198  C   ASP A  25     3929   2949   4390   -619    587    777       C  
ATOM    199  O   ASP A  25     -24.334  -7.963 -11.997  1.00 31.11           O  
ANISOU  199  O   ASP A  25     4102   3145   4575   -658    612    797       O  
ATOM    200  CB  ASP A  25     -22.606 -10.096 -11.849  1.00 31.84           C  
ANISOU  200  CB  ASP A  25     4282   3106   4710   -587    682    847       C  
ATOM    201  CG  ASP A  25     -23.448 -10.715 -12.951  1.00 34.08           C  
ANISOU  201  CG  ASP A  25     4567   3360   5022   -682    683    812       C  
ATOM    202  OD1 ASP A  25     -23.321 -10.292 -14.118  1.00 33.76           O  
ANISOU  202  OD1 ASP A  25     4509   3336   4983   -716    639    757       O  
ATOM    203  OD2 ASP A  25     -24.247 -11.624 -12.641  1.00 36.49           O  
ANISOU  203  OD2 ASP A  25     4888   3630   5346   -724    728    841       O  
ATOM    204  N   TYR A  26     -22.913  -6.617 -13.114  1.00 27.89           N  
ANISOU  204  N   TYR A  26     3682   2764   4150   -621    533    731       N  
ATOM    205  CA  TYR A  26     -23.875  -5.528 -13.255  1.00 28.34           C  
ANISOU  205  CA  TYR A  26     3701   2878   4190   -655    502    705       C  
ATOM    206  C   TYR A  26     -25.033  -5.859 -14.194  1.00 30.78           C  
ANISOU  206  C   TYR A  26     3996   3194   4507   -744    501    676       C  
ATOM    207  O   TYR A  26     -26.092  -5.234 -14.118  1.00 31.04           O  
ANISOU  207  O   TYR A  26     3997   3273   4523   -778    494    665       O  
ATOM    208  CB  TYR A  26     -23.167  -4.252 -13.727  1.00 25.26           C  
ANISOU  208  CB  TYR A  26     3296   2520   3783   -629    448    666       C  
ATOM    209  CG  TYR A  26     -22.397  -4.380 -15.028  1.00 26.67           C  
ANISOU  209  CG  TYR A  26     3487   2682   3966   -651    420    625       C  
ATOM    210  CD1 TYR A  26     -21.038  -4.667 -15.027  1.00 27.46           C  
ANISOU  210  CD1 TYR A  26     3612   2758   4065   -607    418    632       C  
ATOM    211  CD2 TYR A  26     -23.024  -4.189 -16.253  1.00 27.70           C  
ANISOU  211  CD2 TYR A  26     3600   2829   4095   -716    397    580       C  
ATOM    212  CE1 TYR A  26     -20.327  -4.769 -16.214  1.00 29.05           C  
ANISOU  212  CE1 TYR A  26     3822   2952   4266   -629    392    596       C  
ATOM    213  CE2 TYR A  26     -22.321  -4.292 -17.441  1.00 29.34           C  
ANISOU  213  CE2 TYR A  26     3815   3031   4303   -735    372    545       C  
ATOM    214  CZ  TYR A  26     -20.978  -4.581 -17.413  1.00 31.58           C  
ANISOU  214  CZ  TYR A  26     4123   3289   4586   -693    369    553       C  
ATOM    215  OH  TYR A  26     -20.283  -4.683 -18.593  1.00 39.62           O  
ANISOU  215  OH  TYR A  26     5145   4308   5602   -715    344    518       O  
ATOM    216  N   GLU A  27     -24.839  -6.837 -15.072  1.00 33.27           N  
ANISOU  216  N   GLU A  27     4330   3466   4846   -782    510    663       N  
ATOM    217  CA  GLU A  27     -25.894  -7.243 -15.999  1.00 38.47           C  
ANISOU  217  CA  GLU A  27     4969   4134   5513   -867    508    638       C  
ATOM    218  C   GLU A  27     -27.106  -7.809 -15.258  1.00 38.50           C  
ANISOU  218  C   GLU A  27     4966   4145   5520   -910    550    674       C  
ATOM    219  O   GLU A  27     -28.225  -7.786 -15.772  1.00 38.10           O  
ANISOU  219  O   GLU A  27     4881   4131   5462   -982    543    659       O  
ATOM    220  CB  GLU A  27     -25.362  -8.273 -17.000  1.00 42.40           C  
ANISOU  220  CB  GLU A  27     5487   4578   6046   -890    515    620       C  
ATOM    221  CG  GLU A  27     -24.646  -7.659 -18.196  1.00 47.23           C  
ANISOU  221  CG  GLU A  27     6087   5211   6648   -889    465    572       C  
ATOM    222  CD  GLU A  27     -23.812  -8.673 -18.964  1.00 53.89           C  
ANISOU  222  CD  GLU A  27     6955   5997   7525   -890    476    559       C  
ATOM    223  OE1 GLU A  27     -22.670  -8.954 -18.540  1.00 54.28           O  
ANISOU  223  OE1 GLU A  27     7039   6007   7577   -831    488    576       O  
ATOM    224  OE2 GLU A  27     -24.302  -9.192 -19.991  1.00 57.98           O  
ANISOU  224  OE2 GLU A  27     7455   6508   8065   -947    475    532       O  
ATOM    225  N   SER A  28     -26.876  -8.304 -14.045  1.00 37.92           N  
ANISOU  225  N   SER A  28     4917   4041   5450   -867    591    726       N  
ATOM    226  CA  SER A  28     -27.931  -8.919 -13.247  1.00 37.81           C  
ANISOU  226  CA  SER A  28     4900   4032   5434   -908    636    768       C  
ATOM    227  C   SER A  28     -28.505  -7.959 -12.215  1.00 35.62           C  
ANISOU  227  C   SER A  28     4593   3824   5118   -885    634    786       C  
ATOM    228  O   SER A  28     -29.377  -8.327 -11.432  1.00 35.29           O  
ANISOU  228  O   SER A  28     4543   3803   5064   -916    670    823       O  
ATOM    229  CB  SER A  28     -27.403 -10.168 -12.541  1.00 40.52           C  
ANISOU  229  CB  SER A  28     5293   4299   5805   -877    691    819       C  
ATOM    230  OG  SER A  28     -27.005 -11.150 -13.481  1.00 44.46           O  
ANISOU  230  OG  SER A  28     5821   4728   6344   -904    702    800       O  
ATOM    231  N   HIS A  29     -28.012  -6.727 -12.213  1.00 33.86           N  
ANISOU  231  N   HIS A  29     4351   3636   4877   -832    595    760       N  
ATOM    232  CA  HIS A  29     -28.443  -5.738 -11.232  1.00 31.70           C  
ANISOU  232  CA  HIS A  29     4031   3410   4603   -785    608    785       C  
ATOM    233  C   HIS A  29     -29.908  -5.369 -11.436  1.00 31.74           C  
ANISOU  233  C   HIS A  29     3992   3478   4589   -858    611    766       C  
ATOM    234  O   HIS A  29     -30.356  -5.191 -12.563  1.00 32.05           O  
ANISOU  234  O   HIS A  29     4027   3543   4608   -925    578    712       O  
ATOM    235  CB  HIS A  29     -27.561  -4.490 -11.314  1.00 30.80           C  
ANISOU  235  CB  HIS A  29     3898   3308   4498   -711    565    766       C  
ATOM    236  CG  HIS A  29     -27.922  -3.434 -10.318  1.00 30.50           C  
ANISOU  236  CG  HIS A  29     3798   3314   4475   -652    570    804       C  
ATOM    237  ND1 HIS A  29     -27.822  -3.633  -8.958  1.00 29.29           N  
ANISOU  237  ND1 HIS A  29     3626   3169   4335   -586    614    877       N  
ATOM    238  CD2 HIS A  29     -28.377  -2.170 -10.482  1.00 31.91           C  
ANISOU  238  CD2 HIS A  29     3925   3537   4662   -643    535    788       C  
ATOM    239  CE1 HIS A  29     -28.207  -2.539  -8.327  1.00 30.25           C  
ANISOU  239  CE1 HIS A  29     3681   3344   4468   -541    602    906       C  
ATOM    240  NE2 HIS A  29     -28.548  -1.634  -9.227  1.00 32.65           N  
ANISOU  240  NE2 HIS A  29     3964   3665   4775   -575    553    854       N  
ATOM    241  N   VAL A  30     -30.662  -5.265 -10.349  1.00 31.93           N  
ANISOU  241  N   VAL A  30     3978   3538   4616   -844    654    813       N  
ATOM    242  CA  VAL A  30     -32.055  -4.849 -10.458  1.00 31.87           C  
ANISOU  242  CA  VAL A  30     3916   3603   4589   -907    664    796       C  
ATOM    243  C   VAL A  30     -32.222  -3.417  -9.956  1.00 31.39           C  
ANISOU  243  C   VAL A  30     3784   3593   4549   -834    646    810       C  
ATOM    244  O   VAL A  30     -32.037  -3.138  -8.773  1.00 32.36           O  
ANISOU  244  O   VAL A  30     3873   3733   4689   -757    664    875       O  
ATOM    245  CB  VAL A  30     -32.994  -5.786  -9.679  1.00 34.70           C  
ANISOU  245  CB  VAL A  30     4270   3984   4930   -962    723    840       C  
ATOM    246  CG1 VAL A  30     -34.438  -5.317  -9.810  1.00 36.74           C  
ANISOU  246  CG1 VAL A  30     4464   4334   5162  -1029    739    814       C  
ATOM    247  CG2 VAL A  30     -32.854  -7.205 -10.187  1.00 36.60           C  
ANISOU  247  CG2 VAL A  30     4573   4170   5165  -1035    730    843       C  
ATOM    248  N   VAL A  31     -32.575  -2.516 -10.867  1.00 29.77           N  
ANISOU  248  N   VAL A  31     3549   3419   4343   -855    605    757       N  
ATOM    249  CA  VAL A  31     -32.675  -1.098 -10.543  1.00 32.57           C  
ANISOU  249  CA  VAL A  31     3831   3817   4728   -785    569    778       C  
ATOM    250  C   VAL A  31     -33.864  -0.811  -9.636  1.00 36.00           C  
ANISOU  250  C   VAL A  31     4180   4339   5159   -781    598    828       C  
ATOM    251  O   VAL A  31     -34.991  -1.216  -9.922  1.00 36.08           O  
ANISOU  251  O   VAL A  31     4169   4398   5142   -858    630    800       O  
ATOM    252  CB  VAL A  31     -32.792  -0.238 -11.820  1.00 33.29           C  
ANISOU  252  CB  VAL A  31     3910   3916   4821   -810    517    713       C  
ATOM    253  CG1 VAL A  31     -33.045   1.225 -11.468  1.00 33.09           C  
ANISOU  253  CG1 VAL A  31     3803   3940   4831   -747    469    749       C  
ATOM    254  CG2 VAL A  31     -31.537  -0.375 -12.670  1.00 33.54           C  
ANISOU  254  CG2 VAL A  31     4015   3881   4848   -802    483    669       C  
ATOM    255  N   GLU A  32     -33.608  -0.116  -8.534  1.00 39.03           N  
ANISOU  255  N   GLU A  32     4509   4757   5562   -691    586    901       N  
ATOM    256  CA  GLU A  32     -34.687   0.316  -7.655  1.00 43.78           C  
ANISOU  256  CA  GLU A  32     5012   5474   6148   -673    600    957       C  
ATOM    257  C   GLU A  32     -35.061   1.761  -7.966  1.00 38.29           C  
ANISOU  257  C   GLU A  32     4232   4847   5468   -643    534    960       C  
ATOM    258  O   GLU A  32     -34.262   2.680  -7.759  1.00 36.73           O  
ANISOU  258  O   GLU A  32     4020   4632   5303   -573    486    988       O  
ATOM    259  CB  GLU A  32     -34.283   0.157  -6.192  1.00 51.16           C  
ANISOU  259  CB  GLU A  32     5924   6438   7077   -591    629   1043       C  
ATOM    260  CG  GLU A  32     -35.143  -0.844  -5.438  1.00 59.10           C  
ANISOU  260  CG  GLU A  32     6919   7496   8042   -628    696   1074       C  
ATOM    261  CD  GLU A  32     -34.383  -1.542  -4.329  1.00 64.22           C  
ANISOU  261  CD  GLU A  32     7600   8116   8686   -566    737   1140       C  
ATOM    262  OE1 GLU A  32     -33.961  -0.855  -3.375  1.00 66.90           O  
ANISOU  262  OE1 GLU A  32     7881   8516   9022   -463    725   1203       O  
ATOM    263  OE2 GLU A  32     -34.209  -2.777  -4.414  1.00 64.68           O  
ANISOU  263  OE2 GLU A  32     7737   8100   8739   -617    782   1128       O  
ATOM    264  N   TRP A  33     -36.278   1.952  -8.471  1.00 30.90           N  
ANISOU  264  N   TRP A  33     3239   3995   4507   -699    530    931       N  
ATOM    265  CA  TRP A  33     -36.703   3.251  -8.984  1.00 28.93           C  
ANISOU  265  CA  TRP A  33     2911   3815   4266   -681    461    926       C  
ATOM    266  C   TRP A  33     -37.315   4.142  -7.907  1.00 28.22           C  
ANISOU  266  C   TRP A  33     2736   3867   4120   -579    418    945       C  
ATOM    267  O   TRP A  33     -38.079   3.677  -7.059  1.00 25.40           O  
ANISOU  267  O   TRP A  33     2326   3612   3714   -580    462    978       O  
ATOM    268  CB  TRP A  33     -37.714   3.068 -10.124  1.00 28.85           C  
ANISOU  268  CB  TRP A  33     2891   3843   4229   -766    465    854       C  
ATOM    269  CG  TRP A  33     -37.232   2.177 -11.234  1.00 31.40           C  
ANISOU  269  CG  TRP A  33     3322   4046   4563   -836    494    773       C  
ATOM    270  CD1 TRP A  33     -37.438   0.832 -11.355  1.00 34.90           C  
ANISOU  270  CD1 TRP A  33     3827   4450   4983   -908    568    732       C  
ATOM    271  CD2 TRP A  33     -36.464   2.568 -12.378  1.00 31.81           C  
ANISOU  271  CD2 TRP A  33     3429   4019   4640   -839    449    721       C  
ATOM    272  NE1 TRP A  33     -36.842   0.362 -12.503  1.00 34.31           N  
ANISOU  272  NE1 TRP A  33     3836   4290   4910   -955    571    658       N  
ATOM    273  CE2 TRP A  33     -36.239   1.409 -13.148  1.00 33.26           C  
ANISOU  273  CE2 TRP A  33     3697   4136   4802   -910    500    649       C  
ATOM    274  CE3 TRP A  33     -35.940   3.785 -12.824  1.00 30.77           C  
ANISOU  274  CE3 TRP A  33     3280   3871   4540   -791    371    729       C  
ATOM    275  CZ2 TRP A  33     -35.517   1.433 -14.340  1.00 34.56           C  
ANISOU  275  CZ2 TRP A  33     3925   4240   4968   -927    475    586       C  
ATOM    276  CZ3 TRP A  33     -35.222   3.805 -14.007  1.00 33.56           C  
ANISOU  276  CZ3 TRP A  33     3702   4149   4899   -810    348    666       C  
ATOM    277  CH2 TRP A  33     -35.018   2.637 -14.751  1.00 33.85           C  
ANISOU  277  CH2 TRP A  33     3815   4140   4906   -873    401    595       C  
ATOM    278  N   GLY A  34     -36.979   5.428  -7.951  1.00 27.10           N  
ANISOU  278  N   GLY A  34     2602   3727   3969   -479    323    898       N  
ATOM    279  CA  GLY A  34     -37.609   6.409  -7.089  1.00 26.87           C  
ANISOU  279  CA  GLY A  34     2515   3825   3870   -360    259    871       C  
ATOM    280  C   GLY A  34     -38.809   7.035  -7.778  1.00 25.72           C  
ANISOU  280  C   GLY A  34     2315   3781   3677   -367    215    820       C  
ATOM    281  O   GLY A  34     -39.282   6.526  -8.796  1.00 24.37           O  
ANISOU  281  O   GLY A  34     2137   3604   3519   -475    251    814       O  
ATOM    282  N   ASN A  35     -39.304   8.136  -7.220  1.00 26.55           N  
ANISOU  282  N   ASN A  35     2379   3984   3723   -246    139    780       N  
ATOM    283  CA  ASN A  35     -40.448   8.847  -7.788  1.00 28.85           C  
ANISOU  283  CA  ASN A  35     2619   4386   3957   -224     90    730       C  
ATOM    284  C   ASN A  35     -40.017  10.023  -8.658  1.00 25.90           C  
ANISOU  284  C   ASN A  35     2296   3930   3613   -172      3    683       C  
ATOM    285  O   ASN A  35     -39.457  10.992  -8.151  1.00 22.56           O  
ANISOU  285  O   ASN A  35     1905   3470   3196    -62    -66    658       O  
ATOM    286  CB  ASN A  35     -41.369   9.352  -6.677  1.00 36.15           C  
ANISOU  286  CB  ASN A  35     3464   5482   4789   -115     57    712       C  
ATOM    287  CG  ASN A  35     -42.231   8.256  -6.087  1.00 43.48           C  
ANISOU  287  CG  ASN A  35     4319   6536   5665   -185    139    754       C  
ATOM    288  OD1 ASN A  35     -41.880   7.078  -6.130  1.00 44.89           O  
ANISOU  288  OD1 ASN A  35     4521   6649   5887   -295    226    808       O  
ATOM    289  ND2 ASN A  35     -43.377   8.643  -5.538  1.00 46.69           N  
ANISOU  289  ND2 ASN A  35     4638   7127   5975   -121    112    728       N  
ATOM    290  N   GLN A  36     -40.296   9.950  -9.959  1.00 24.89           N  
ANISOU  290  N   GLN A  36     2174   3780   3503   -253      7    669       N  
ATOM    291  CA  GLN A  36     -39.834  10.979 -10.890  1.00 25.35           C  
ANISOU  291  CA  GLN A  36     2285   3751   3594   -218    -68    637       C  
ATOM    292  C   GLN A  36     -40.456  12.340 -10.597  1.00 23.27           C  
ANISOU  292  C   GLN A  36     2003   3567   3272    -76   -160    590       C  
ATOM    293  O   GLN A  36     -39.863  13.377 -10.907  1.00 20.61           O  
ANISOU  293  O   GLN A  36     1726   3140   2966    -11   -233    568       O  
ATOM    294  CB  GLN A  36     -40.122  10.566 -12.343  1.00 29.37           C  
ANISOU  294  CB  GLN A  36     2789   4248   4124   -333    -40    634       C  
ATOM    295  CG  GLN A  36     -41.556  10.787 -12.803  1.00 35.54           C  
ANISOU  295  CG  GLN A  36     3489   5190   4824   -328    -47    603       C  
ATOM    296  CD  GLN A  36     -41.770  12.161 -13.418  1.00 37.39           C  
ANISOU  296  CD  GLN A  36     3738   5431   5036   -229   -141    567       C  
ATOM    297  OE1 GLN A  36     -40.855  12.740 -14.009  1.00 41.13           O  
ANISOU  297  OE1 GLN A  36     4284   5773   5570   -219   -185    568       O  
ATOM    298  NE2 GLN A  36     -42.971  12.698 -13.260  1.00 42.91           N  
ANISOU  298  NE2 GLN A  36     4370   6287   5645   -152   -172    536       N  
ATOM    299  N   ASP A  37     -41.644  12.334  -9.996  1.00 23.14           N  
ANISOU  299  N   ASP A  37     1904   3718   3169    -29   -156    576       N  
ATOM    300  CA  ASP A  37     -42.345  13.568  -9.668  1.00 22.64           C  
ANISOU  300  CA  ASP A  37     1816   3747   3040    116   -241    527       C  
ATOM    301  C   ASP A  37     -41.706  14.295  -8.485  1.00 23.88           C  
ANISOU  301  C   ASP A  37     2005   3866   3205    240   -295    510       C  
ATOM    302  O   ASP A  37     -42.116  15.401  -8.146  1.00 23.47           O  
ANISOU  302  O   ASP A  37     1947   3863   3109    372   -372    463       O  
ATOM    303  CB  ASP A  37     -43.818  13.280  -9.372  1.00 29.47           C  
ANISOU  303  CB  ASP A  37     2574   4824   3799    128   -219    514       C  
ATOM    304  CG  ASP A  37     -44.001  12.210  -8.320  1.00 34.70           C  
ANISOU  304  CG  ASP A  37     3182   5564   4436     79   -145    550       C  
ATOM    305  OD1 ASP A  37     -43.730  11.026  -8.619  1.00 34.85           O  
ANISOU  305  OD1 ASP A  37     3208   5535   4498    -61    -59    594       O  
ATOM    306  OD2 ASP A  37     -44.425  12.556  -7.198  1.00 39.38           O  
ANISOU  306  OD2 ASP A  37     3727   6270   4966    182   -173    535       O  
ATOM    307  N   ASP A  38     -40.698  13.681  -7.864  1.00 22.38           N  
ANISOU  307  N   ASP A  38     1847   3590   3067    202   -253    544       N  
ATOM    308  CA  ASP A  38     -39.964  14.345  -6.793  1.00 22.70           C  
ANISOU  308  CA  ASP A  38     1915   3592   3118    310   -300    523       C  
ATOM    309  C   ASP A  38     -39.052  15.439  -7.342  1.00 24.61           C  
ANISOU  309  C   ASP A  38     2249   3683   3419    352   -374    491       C  
ATOM    310  O   ASP A  38     -38.593  16.297  -6.595  1.00 24.63           O  
ANISOU  310  O   ASP A  38     2277   3657   3423    455   -432    453       O  
ATOM    311  CB  ASP A  38     -39.112  13.351  -5.995  1.00 26.59           C  
ANISOU  311  CB  ASP A  38     2414   4048   3644    260   -230    572       C  
ATOM    312  CG  ASP A  38     -39.923  12.541  -5.009  1.00 30.37           C  
ANISOU  312  CG  ASP A  38     2802   4682   4054    262   -173    600       C  
ATOM    313  OD1 ASP A  38     -41.119  12.855  -4.821  1.00 28.70           O  
ANISOU  313  OD1 ASP A  38     2519   4620   3764    313   -197    573       O  
ATOM    314  OD2 ASP A  38     -39.353  11.603  -4.410  1.00 29.74           O  
ANISOU  314  OD2 ASP A  38     2722   4580   3996    215   -105    652       O  
ATOM    315  N   TYR A  39     -38.777  15.402  -8.644  1.00 21.89           N  
ANISOU  315  N   TYR A  39     1952   3242   3122    267   -371    505       N  
ATOM    316  CA  TYR A  39     -37.756  16.273  -9.215  1.00 24.06           C  
ANISOU  316  CA  TYR A  39     2319   3362   3460    278   -430    489       C  
ATOM    317  C   TYR A  39     -38.272  17.138 -10.328  1.00 26.70           C  
ANISOU  317  C   TYR A  39     2676   3679   3789    298   -487    469       C  
ATOM    318  O   TYR A  39     -39.029  16.701 -11.188  1.00 27.15           O  
ANISOU  318  O   TYR A  39     2694   3798   3823    238   -457    485       O  
ATOM    319  CB  TYR A  39     -36.576  15.442  -9.717  1.00 21.84           C  
ANISOU  319  CB  TYR A  39     2087   2960   3253    156   -376    532       C  
ATOM    320  CG  TYR A  39     -36.075  14.523  -8.648  1.00 23.01           C  
ANISOU  320  CG  TYR A  39     2213   3127   3402    141   -313    560       C  
ATOM    321  CD1 TYR A  39     -36.469  13.195  -8.611  1.00 23.73           C  
ANISOU  321  CD1 TYR A  39     2258   3276   3484     54   -224    605       C  
ATOM    322  CD2 TYR A  39     -35.248  14.998  -7.640  1.00 21.40           C  
ANISOU  322  CD2 TYR A  39     2034   2890   3205    218   -342    540       C  
ATOM    323  CE1 TYR A  39     -36.039  12.361  -7.624  1.00 22.42           C  
ANISOU  323  CE1 TYR A  39     2076   3127   3317     48   -165    640       C  
ATOM    324  CE2 TYR A  39     -34.812  14.170  -6.641  1.00 21.30           C  
ANISOU  324  CE2 TYR A  39     1996   2910   3187    215   -284    570       C  
ATOM    325  CZ  TYR A  39     -35.210  12.851  -6.638  1.00 22.94           C  
ANISOU  325  CZ  TYR A  39     2162   3168   3385    133   -195    624       C  
ATOM    326  OH  TYR A  39     -34.782  12.008  -5.647  1.00 24.66           O  
ANISOU  326  OH  TYR A  39     2360   3414   3597    135   -133    664       O  
ATOM    327  N   GLN A  40     -37.835  18.384 -10.310  1.00 29.35           N  
ANISOU  327  N   GLN A  40     3077   3929   4145    384   -568    434       N  
ATOM    328  CA  GLN A  40     -38.298  19.347 -11.297  1.00 31.03           C  
ANISOU  328  CA  GLN A  40     3323   4117   4352    424   -629    420       C  
ATOM    329  C   GLN A  40     -37.121  19.997 -12.017  1.00 28.41           C  
ANISOU  329  C   GLN A  40     3091   3607   4095    387   -669    427       C  
ATOM    330  O   GLN A  40     -36.290  20.663 -11.395  1.00 29.77           O  
ANISOU  330  O   GLN A  40     3322   3689   4300    434   -710    401       O  
ATOM    331  CB  GLN A  40     -39.180  20.410 -10.652  1.00 36.90           C  
ANISOU  331  CB  GLN A  40     4050   4939   5032    584   -698    367       C  
ATOM    332  CG  GLN A  40     -40.501  19.804 -10.162  1.00 46.35           C  
ANISOU  332  CG  GLN A  40     5137   6336   6139    614   -662    361       C  
ATOM    333  CD  GLN A  40     -41.680  20.744 -10.324  1.00 54.06           C  
ANISOU  333  CD  GLN A  40     6089   7412   7040    742   -724    322       C  
ATOM    334  OE1 GLN A  40     -41.489  21.936 -10.616  1.00 57.84           O  
ANISOU  334  OE1 GLN A  40     6641   7798   7538    829   -800    296       O  
ATOM    335  NE2 GLN A  40     -42.920  20.203 -10.182  1.00 53.59           N  
ANISOU  335  NE2 GLN A  40     5927   7545   6891    752   -691    319       N  
ATOM    336  N   LEU A  41     -37.070  19.807 -13.335  1.00 25.47           N  
ANISOU  336  N   LEU A  41     2733   3196   3747    300   -656    461       N  
ATOM    337  CA  LEU A  41     -36.002  20.347 -14.164  1.00 24.97           C  
ANISOU  337  CA  LEU A  41     2756   2979   3750    249   -691    478       C  
ATOM    338  C   LEU A  41     -36.103  21.865 -14.159  1.00 24.82           C  
ANISOU  338  C   LEU A  41     2804   2896   3730    364   -782    447       C  
ATOM    339  O   LEU A  41     -37.190  22.419 -14.311  1.00 22.39           O  
ANISOU  339  O   LEU A  41     2473   2663   3370    455   -815    431       O  
ATOM    340  CB  LEU A  41     -36.099  19.781 -15.581  1.00 26.31           C  
ANISOU  340  CB  LEU A  41     2909   3153   3934    138   -656    519       C  
ATOM    341  CG  LEU A  41     -36.073  18.250 -15.642  1.00 25.16           C  
ANISOU  341  CG  LEU A  41     2701   3066   3793     21   -563    544       C  
ATOM    342  CD1 LEU A  41     -36.174  17.767 -17.083  1.00 26.94           C  
ANISOU  342  CD1 LEU A  41     2907   3298   4032    -85   -534    574       C  
ATOM    343  CD2 LEU A  41     -34.824  17.684 -14.960  1.00 21.73           C  
ANISOU  343  CD2 LEU A  41     2302   2549   3407    -29   -532    553       C  
ATOM    344  N   VAL A  42     -34.971  22.529 -13.959  1.00 25.74           N  
ANISOU  344  N   VAL A  42     3005   2874   3901    362   -822    435       N  
ATOM    345  CA  VAL A  42     -34.932  23.985 -13.871  1.00 26.27           C  
ANISOU  345  CA  VAL A  42     3151   2853   3978    464   -908    402       C  
ATOM    346  C   VAL A  42     -34.258  24.581 -15.094  1.00 26.03           C  
ANISOU  346  C   VAL A  42     3201   2692   3998    399   -941    438       C  
ATOM    347  O   VAL A  42     -34.766  25.516 -15.712  1.00 25.50           O  
ANISOU  347  O   VAL A  42     3174   2592   3922    463   -994    443       O  
ATOM    348  CB  VAL A  42     -34.186  24.457 -12.613  1.00 28.31           C  
ANISOU  348  CB  VAL A  42     3447   3055   4255    518   -935    349       C  
ATOM    349  CG1 VAL A  42     -34.050  25.971 -12.609  1.00 31.24           C  
ANISOU  349  CG1 VAL A  42     3912   3310   4647    608  -1022    311       C  
ATOM    350  CG2 VAL A  42     -34.907  23.985 -11.370  1.00 31.16           C  
ANISOU  350  CG2 VAL A  42     3724   3556   4559    597   -910    314       C  
ATOM    351  N   ARG A  43     -33.099  24.036 -15.440  1.00 27.68           N  
ANISOU  351  N   ARG A  43     3431   2830   4255    275   -911    466       N  
ATOM    352  CA  ARG A  43     -32.421  24.466 -16.650  1.00 30.51           C  
ANISOU  352  CA  ARG A  43     3853   3082   4657    196   -936    507       C  
ATOM    353  C   ARG A  43     -31.463  23.398 -17.150  1.00 26.33           C  
ANISOU  353  C   ARG A  43     3303   2541   4159     51   -879    542       C  
ATOM    354  O   ARG A  43     -30.897  22.634 -16.364  1.00 22.45           O  
ANISOU  354  O   ARG A  43     2788   2070   3673     18   -836    527       O  
ATOM    355  CB  ARG A  43     -31.677  25.782 -16.419  1.00 36.74           C  
ANISOU  355  CB  ARG A  43     4749   3726   5485    236  -1009    482       C  
ATOM    356  CG  ARG A  43     -30.629  25.739 -15.327  1.00 40.99           C  
ANISOU  356  CG  ARG A  43     5312   4217   6047    220  -1005    438       C  
ATOM    357  CD  ARG A  43     -29.932  27.089 -15.207  1.00 47.36           C  
ANISOU  357  CD  ARG A  43     6226   4877   6891    246  -1077    409       C  
ATOM    358  NE  ARG A  43     -28.672  26.995 -14.474  1.00 50.62           N  
ANISOU  358  NE  ARG A  43     6663   5241   7330    190  -1069    375       N  
ATOM    359  CZ  ARG A  43     -27.507  27.444 -14.930  1.00 53.94           C  
ANISOU  359  CZ  ARG A  43     7155   5550   7790    100  -1091    385       C  
ATOM    360  NH1 ARG A  43     -27.434  28.023 -16.122  1.00 55.64           N  
ANISOU  360  NH1 ARG A  43     7412   5726   8003     47  -1101    419       N  
ATOM    361  NH2 ARG A  43     -26.413  27.315 -14.193  1.00 54.74           N  
ANISOU  361  NH2 ARG A  43     7265   5632   7902     56  -1080    348       N  
ATOM    362  N   LYS A  44     -31.309  23.345 -18.470  1.00 26.01           N  
ANISOU  362  N   LYS A  44     3270   2478   4135    -29   -880    589       N  
ATOM    363  CA  LYS A  44     -30.386  22.419 -19.109  1.00 27.31           C  
ANISOU  363  CA  LYS A  44     3419   2629   4328   -165   -834    621       C  
ATOM    364  C   LYS A  44     -28.964  22.926 -18.951  1.00 25.88           C  
ANISOU  364  C   LYS A  44     3315   2329   4189   -213   -867    615       C  
ATOM    365  O   LYS A  44     -28.681  24.096 -19.216  1.00 25.22           O  
ANISOU  365  O   LYS A  44     3307   2152   4124   -190   -931    617       O  
ATOM    366  CB  LYS A  44     -30.730  22.240 -20.589  1.00 31.04           C  
ANISOU  366  CB  LYS A  44     3864   3133   4798   -229   -828    668       C  
ATOM    367  CG  LYS A  44     -29.998  21.093 -21.269  1.00 32.21           C  
ANISOU  367  CG  LYS A  44     3974   3297   4966   -363   -773    692       C  
ATOM    368  CD  LYS A  44     -30.819  20.626 -22.464  1.00 36.61           C  
ANISOU  368  CD  LYS A  44     4464   3944   5502   -404   -746    720       C  
ATOM    369  CE  LYS A  44     -30.990  21.752 -23.496  1.00 41.09           C  
ANISOU  369  CE  LYS A  44     5069   4474   6069   -382   -809    755       C  
ATOM    370  NZ  LYS A  44     -32.122  21.473 -24.462  1.00 42.32           N  
ANISOU  370  NZ  LYS A  44     5147   4747   6184   -380   -788    773       N  
ATOM    371  N   LEU A  45     -28.072  22.047 -18.506  1.00 24.24           N  
ANISOU  371  N   LEU A  45     2356   3342   3510    256   -271    557       N  
ATOM    372  CA  LEU A  45     -26.680  22.430 -18.281  1.00 26.99           C  
ANISOU  372  CA  LEU A  45     2687   3655   3914    265   -277    608       C  
ATOM    373  C   LEU A  45     -25.761  22.001 -19.426  1.00 30.58           C  
ANISOU  373  C   LEU A  45     3178   4118   4322    296   -244    672       C  
ATOM    374  O   LEU A  45     -24.789  22.688 -19.747  1.00 33.74           O  
ANISOU  374  O   LEU A  45     3572   4482   4763    300   -228    714       O  
ATOM    375  CB  LEU A  45     -26.174  21.841 -16.964  1.00 27.59           C  
ANISOU  375  CB  LEU A  45     2796   3722   3966    229   -285    560       C  
ATOM    376  CG  LEU A  45     -26.800  22.402 -15.688  1.00 30.14           C  
ANISOU  376  CG  LEU A  45     3104   4035   4314    201   -308    475       C  
ATOM    377  CD1 LEU A  45     -26.244  21.694 -14.472  1.00 29.03           C  
ANISOU  377  CD1 LEU A  45     2995   3905   4130    179   -311    439       C  
ATOM    378  CD2 LEU A  45     -26.557  23.899 -15.587  1.00 32.63           C  
ANISOU  378  CD2 LEU A  45     3355   4296   4747    214   -341    477       C  
ATOM    379  N   GLY A  46     -26.066  20.865 -20.040  1.00 30.03           N  
ANISOU  379  N   GLY A  46     3142   4098   4169    320   -235    677       N  
ATOM    380  CA  GLY A  46     -25.250  20.370 -21.129  1.00 31.73           C  
ANISOU  380  CA  GLY A  46     3395   4333   4328    360   -206    722       C  
ATOM    381  C   GLY A  46     -25.792  19.108 -21.760  1.00 30.98           C  
ANISOU  381  C   GLY A  46     3336   4289   4144    393   -213    704       C  
ATOM    382  O   GLY A  46     -26.654  18.429 -21.193  1.00 29.52           O  
ANISOU  382  O   GLY A  46     3168   4110   3938    361   -234    646       O  
ATOM    383  N   ARG A  47     -25.289  18.809 -22.952  1.00 31.89           N  
ANISOU  383  N   ARG A  47     3481   4432   4203    444   -190    728       N  
ATOM    384  CA  ARG A  47     -25.633  17.585 -23.655  1.00 34.56           C  
ANISOU  384  CA  ARG A  47     3861   4816   4455    489   -206    701       C  
ATOM    385  C   ARG A  47     -24.358  16.924 -24.151  1.00 35.95           C  
ANISOU  385  C   ARG A  47     4079   4999   4582    526   -179    726       C  
ATOM    386  O   ARG A  47     -23.624  17.497 -24.955  1.00 38.46           O  
ANISOU  386  O   ARG A  47     4389   5328   4895    553   -141    767       O  
ATOM    387  CB  ARG A  47     -26.574  17.855 -24.831  1.00 35.41           C  
ANISOU  387  CB  ARG A  47     3958   4968   4528    533   -213    683       C  
ATOM    388  CG  ARG A  47     -26.805  16.627 -25.702  1.00 38.34           C  
ANISOU  388  CG  ARG A  47     4373   5386   4809    594   -239    644       C  
ATOM    389  CD  ARG A  47     -27.429  16.971 -27.051  1.00 40.37           C  
ANISOU  389  CD  ARG A  47     4622   5696   5020    651   -239    633       C  
ATOM    390  NE  ARG A  47     -28.817  17.406 -26.939  1.00 40.74           N  
ANISOU  390  NE  ARG A  47     4632   5753   5095    628   -270    600       N  
ATOM    391  CZ  ARG A  47     -29.502  17.990 -27.920  1.00 39.38           C  
ANISOU  391  CZ  ARG A  47     4440   5620   4903    662   -267    597       C  
ATOM    392  NH1 ARG A  47     -28.928  18.222 -29.093  1.00 38.09           N  
ANISOU  392  NH1 ARG A  47     4287   5497   4690    722   -233    629       N  
ATOM    393  NH2 ARG A  47     -30.762  18.356 -27.718  1.00 36.63           N  
ANISOU  393  NH2 ARG A  47     4056   5278   4585    635   -295    567       N  
ATOM    394  N   GLY A  48     -24.091  15.726 -23.654  1.00 36.95           N  
ANISOU  394  N   GLY A  48     4245   5121   4675    525   -197    707       N  
ATOM    395  CA  GLY A  48     -22.931  14.976 -24.085  1.00 37.51           C  
ANISOU  395  CA  GLY A  48     4359   5198   4697    563   -174    722       C  
ATOM    396  C   GLY A  48     -23.340  13.929 -25.095  1.00 37.67           C  
ANISOU  396  C   GLY A  48     4419   5259   4633    633   -200    678       C  
ATOM    397  O   GLY A  48     -24.463  13.933 -25.594  1.00 37.98           O  
ANISOU  397  O   GLY A  48     4449   5327   4654    655   -234    639       O  
ATOM    398  N   LYS A  49     -22.427  13.015 -25.392  1.00 38.12           N  
ANISOU  398  N   LYS A  49     4520   5321   4642    672   -190    678       N  
ATOM    399  CA  LYS A  49     -22.709  11.956 -26.348  1.00 37.78           C  
ANISOU  399  CA  LYS A  49     4520   5315   4521    751   -223    624       C  
ATOM    400  C   LYS A  49     -23.689  10.930 -25.767  1.00 33.78           C  
ANISOU  400  C   LYS A  49     4036   4787   4014    740   -292    561       C  
ATOM    401  O   LYS A  49     -24.412  10.262 -26.507  1.00 33.38           O  
ANISOU  401  O   LYS A  49     4012   4747   3923    780   -339    479       O  
ATOM    402  CB  LYS A  49     -21.401  11.279 -26.770  1.00 42.30           C  
ANISOU  402  CB  LYS A  49     5129   5897   5047    797   -192    639       C  
ATOM    403  CG  LYS A  49     -21.564  10.126 -27.744  1.00 48.09           C  
ANISOU  403  CG  LYS A  49     5910   6666   5695    891   -230    572       C  
ATOM    404  CD  LYS A  49     -20.236   9.449 -28.048  1.00 51.32           C  
ANISOU  404  CD  LYS A  49     6352   7085   6063    936   -194    590       C  
ATOM    405  CE  LYS A  49     -20.439   8.247 -28.959  1.00 53.85           C  
ANISOU  405  CE  LYS A  49     6725   7437   6300   1040   -243    507       C  
ATOM    406  NZ  LYS A  49     -21.204   8.622 -30.183  1.00 55.50           N  
ANISOU  406  NZ  LYS A  49     6921   7715   6451   1109   -259    465       N  
ATOM    407  N   TYR A  50     -23.734  10.824 -24.440  1.00 28.56           N  
ANISOU  407  N   TYR A  50     3374   4057   3419    635   -282    556       N  
ATOM    408  CA  TYR A  50     -24.499   9.753 -23.801  1.00 29.13           C  
ANISOU  408  CA  TYR A  50     3480   4067   3522    567   -317    472       C  
ATOM    409  C   TYR A  50     -25.598  10.225 -22.854  1.00 26.63           C  
ANISOU  409  C   TYR A  50     3129   3716   3271    466   -321    448       C  
ATOM    410  O   TYR A  50     -26.332   9.402 -22.295  1.00 22.68           O  
ANISOU  410  O   TYR A  50     2642   3168   2806    407   -346    395       O  
ATOM    411  CB  TYR A  50     -23.552   8.824 -23.037  1.00 33.34           C  
ANISOU  411  CB  TYR A  50     4049   4556   4063    545   -302    489       C  
ATOM    412  CG  TYR A  50     -22.567   8.104 -23.928  1.00 37.26           C  
ANISOU  412  CG  TYR A  50     4587   5079   4493    646   -304    498       C  
ATOM    413  CD1 TYR A  50     -21.216   8.420 -23.905  1.00 39.23           C  
ANISOU  413  CD1 TYR A  50     4831   5359   4717    689   -259    587       C  
ATOM    414  CD2 TYR A  50     -22.996   7.113 -24.801  1.00 39.36           C  
ANISOU  414  CD2 TYR A  50     4893   5341   4723    704   -357    414       C  
ATOM    415  CE1 TYR A  50     -20.317   7.761 -24.720  1.00 42.87           C  
ANISOU  415  CE1 TYR A  50     5327   5849   5111    786   -255    596       C  
ATOM    416  CE2 TYR A  50     -22.109   6.452 -25.620  1.00 42.50           C  
ANISOU  416  CE2 TYR A  50     5330   5768   5051    810   -362    412       C  
ATOM    417  CZ  TYR A  50     -20.770   6.778 -25.577  1.00 45.28           C  
ANISOU  417  CZ  TYR A  50     5677   6159   5370    856   -308    509       C  
ATOM    418  OH  TYR A  50     -19.885   6.114 -26.397  1.00 48.44           O  
ANISOU  418  OH  TYR A  50     6114   6589   5703    951   -301    501       O  
ATOM    419  N   SER A  51     -25.712  11.536 -22.665  1.00 24.78           N  
ANISOU  419  N   SER A  51     2848   3507   3061    452   -295    492       N  
ATOM    420  CA  SER A  51     -26.708  12.057 -21.736  1.00 21.58           C  
ANISOU  420  CA  SER A  51     2409   3079   2711    369   -296    469       C  
ATOM    421  C   SER A  51     -26.992  13.539 -21.934  1.00 21.76           C  
ANISOU  421  C   SER A  51     2379   3132   2758    377   -281    502       C  
ATOM    422  O   SER A  51     -26.258  14.246 -22.631  1.00 19.81           O  
ANISOU  422  O   SER A  51     2112   2918   2497    438   -264    562       O  
ATOM    423  CB  SER A  51     -26.260  11.824 -20.288  1.00 23.25           C  
ANISOU  423  CB  SER A  51     2622   3254   2956    302   -272    486       C  
ATOM    424  OG  SER A  51     -25.099  12.581 -19.977  1.00 21.82           O  
ANISOU  424  OG  SER A  51     2426   3084   2782    317   -242    549       O  
ATOM    425  N   GLU A  52     -28.080  13.985 -21.316  1.00 20.32           N  
ANISOU  425  N   GLU A  52     2168   2938   2615    319   -288    468       N  
ATOM    426  CA  GLU A  52     -28.374  15.396 -21.133  1.00 25.37           C  
ANISOU  426  CA  GLU A  52     2755   3589   3296    310   -274    492       C  
ATOM    427  C   GLU A  52     -28.377  15.694 -19.645  1.00 25.35           C  
ANISOU  427  C   GLU A  52     2738   3559   3335    245   -261    483       C  
ATOM    428  O   GLU A  52     -28.919  14.924 -18.852  1.00 24.78           O  
ANISOU  428  O   GLU A  52     2681   3473   3261    197   -265    446       O  
ATOM    429  CB  GLU A  52     -29.726  15.774 -21.745  1.00 26.56           C  
ANISOU  429  CB  GLU A  52     2881   3762   3450    313   -295    456       C  
ATOM    430  CG  GLU A  52     -29.692  16.006 -23.242  1.00 32.76           C  
ANISOU  430  CG  GLU A  52     3659   4594   4194    395   -304    478       C  
ATOM    431  CD  GLU A  52     -30.921  16.742 -23.742  1.00 38.11           C  
ANISOU  431  CD  GLU A  52     4296   5299   4886    399   -318    459       C  
ATOM    432  OE1 GLU A  52     -31.999  16.603 -23.124  1.00 38.29           O  
ANISOU  432  OE1 GLU A  52     4312   5302   4935    339   -332    409       O  
ATOM    433  OE2 GLU A  52     -30.806  17.462 -24.754  1.00 43.37           O  
ANISOU  433  OE2 GLU A  52     4933   6011   5537    465   -312    505       O  
ATOM    434  N   VAL A  53     -27.783  16.819 -19.270  1.00 22.73           N  
ANISOU  434  N   VAL A  53     2371   3221   3045    249   -248    518       N  
ATOM    435  CA  VAL A  53     -27.617  17.149 -17.863  1.00 22.43           C  
ANISOU  435  CA  VAL A  53     2320   3164   3038    203   -243    501       C  
ATOM    436  C   VAL A  53     -28.399  18.403 -17.499  1.00 21.49           C  
ANISOU  436  C   VAL A  53     2152   3044   2970    192   -251    476       C  
ATOM    437  O   VAL A  53     -28.281  19.440 -18.157  1.00 21.45           O  
ANISOU  437  O   VAL A  53     2110   3032   3007    222   -255    507       O  
ATOM    438  CB  VAL A  53     -26.133  17.333 -17.515  1.00 21.49           C  
ANISOU  438  CB  VAL A  53     2201   3028   2936    216   -235    548       C  
ATOM    439  CG1 VAL A  53     -25.975  17.788 -16.076  1.00 23.52           C  
ANISOU  439  CG1 VAL A  53     2440   3273   3222    180   -240    518       C  
ATOM    440  CG2 VAL A  53     -25.386  16.028 -17.744  1.00 18.52           C  
ANISOU  440  CG2 VAL A  53     1876   2655   2508    228   -225    569       C  
ATOM    441  N   PHE A  54     -29.198  18.291 -16.444  1.00 19.58           N  
ANISOU  441  N   PHE A  54     1906   2810   2724    153   -251    426       N  
ATOM    442  CA  PHE A  54     -30.068  19.374 -16.010  1.00 23.05           C  
ANISOU  442  CA  PHE A  54     2303   3254   3202    148   -259    391       C  
ATOM    443  C   PHE A  54     -29.819  19.772 -14.567  1.00 24.37           C  
ANISOU  443  C   PHE A  54     2457   3422   3380    134   -262    355       C  
ATOM    444  O   PHE A  54     -29.542  18.927 -13.714  1.00 24.92           O  
ANISOU  444  O   PHE A  54     2550   3509   3409    116   -252    349       O  
ATOM    445  CB  PHE A  54     -31.536  18.972 -16.161  1.00 20.96           C  
ANISOU  445  CB  PHE A  54     2034   3015   2914    129   -257    360       C  
ATOM    446  CG  PHE A  54     -31.950  18.692 -17.572  1.00 22.38           C  
ANISOU  446  CG  PHE A  54     2221   3200   3082    149   -265    378       C  
ATOM    447  CD1 PHE A  54     -31.670  17.471 -18.163  1.00 20.64           C  
ANISOU  447  CD1 PHE A  54     2041   2979   2821    153   -270    387       C  
ATOM    448  CD2 PHE A  54     -32.648  19.643 -18.304  1.00 22.90           C  
ANISOU  448  CD2 PHE A  54     2250   3275   3176    171   -272    379       C  
ATOM    449  CE1 PHE A  54     -32.064  17.210 -19.467  1.00 23.28           C  
ANISOU  449  CE1 PHE A  54     2382   3327   3135    184   -286    389       C  
ATOM    450  CE2 PHE A  54     -33.042  19.388 -19.604  1.00 21.69           C  
ANISOU  450  CE2 PHE A  54     2100   3140   3000    200   -282    393       C  
ATOM    451  CZ  PHE A  54     -32.750  18.171 -20.185  1.00 24.19           C  
ANISOU  451  CZ  PHE A  54     2460   3462   3268    209   -292    392       C  
ATOM    452  N   GLU A  55     -29.921  21.066 -14.295  1.00 23.33           N  
ANISOU  452  N   GLU A  55     2284   3275   3306    149   -280    331       N  
ATOM    453  CA  GLU A  55     -30.099  21.505 -12.926  1.00 24.06           C  
ANISOU  453  CA  GLU A  55     2361   3383   3398    148   -292    271       C  
ATOM    454  C   GLU A  55     -31.564  21.297 -12.577  1.00 22.38           C  
ANISOU  454  C   GLU A  55     2139   3216   3148    139   -276    237       C  
ATOM    455  O   GLU A  55     -32.440  21.540 -13.400  1.00 23.36           O  
ANISOU  455  O   GLU A  55     2249   3340   3288    139   -273    244       O  
ATOM    456  CB  GLU A  55     -29.696  22.963 -12.746  1.00 29.05           C  
ANISOU  456  CB  GLU A  55     2949   3971   4116    171   -327    245       C  
ATOM    457  CG  GLU A  55     -29.947  23.492 -11.348  1.00 34.50           C  
ANISOU  457  CG  GLU A  55     3624   4684   4802    186   -350    163       C  
ATOM    458  CD  GLU A  55     -29.412  24.893 -11.157  1.00 40.90           C  
ANISOU  458  CD  GLU A  55     4391   5433   5715    210   -400    127       C  
ATOM    459  OE1 GLU A  55     -28.179  25.077 -11.247  1.00 43.53           O  
ANISOU  459  OE1 GLU A  55     4718   5719   6101    209   -424    156       O  
ATOM    460  OE2 GLU A  55     -30.225  25.810 -10.928  1.00 44.32           O  
ANISOU  460  OE2 GLU A  55     4792   5861   6185    231   -419     72       O  
ATOM    461  N   ALA A  56     -31.827  20.827 -11.365  1.00 23.82           N  
ANISOU  461  N   ALA A  56     2324   3446   3278    136   -265    208       N  
ATOM    462  CA  ALA A  56     -33.193  20.562 -10.948  1.00 24.79           C  
ANISOU  462  CA  ALA A  56     2430   3623   3367    131   -245    192       C  
ATOM    463  C   ALA A  56     -33.382  20.839  -9.466  1.00 23.93           C  
ANISOU  463  C   ALA A  56     2302   3573   3219    159   -242    144       C  
ATOM    464  O   ALA A  56     -32.431  21.140  -8.747  1.00 24.12           O  
ANISOU  464  O   ALA A  56     2330   3595   3238    180   -262    116       O  
ATOM    465  CB  ALA A  56     -33.578  19.127 -11.267  1.00 25.59           C  
ANISOU  465  CB  ALA A  56     2553   3737   3431     95   -219    240       C  
ATOM    466  N   ILE A  57     -34.626  20.729  -9.022  1.00 24.09           N  
ANISOU  466  N   ILE A  57     2296   3651   3207    166   -220    137       N  
ATOM    467  CA  ILE A  57     -34.958  20.883  -7.621  1.00 26.20           C  
ANISOU  467  CA  ILE A  57     2539   3997   3417    207   -210    100       C  
ATOM    468  C   ILE A  57     -35.662  19.627  -7.142  1.00 26.64           C  
ANISOU  468  C   ILE A  57     2584   4119   3418    189   -165    162       C  
ATOM    469  O   ILE A  57     -36.567  19.121  -7.803  1.00 26.45           O  
ANISOU  469  O   ILE A  57     2549   4087   3413    154   -148    205       O  
ATOM    470  CB  ILE A  57     -35.859  22.110  -7.379  1.00 31.05           C  
ANISOU  470  CB  ILE A  57     3117   4633   4047    251   -224     37       C  
ATOM    471  CG1 ILE A  57     -35.096  23.398  -7.685  1.00 39.05           C  
ANISOU  471  CG1 ILE A  57     4129   5573   5134    273   -276    -24       C  
ATOM    472  CG2 ILE A  57     -36.356  22.135  -5.948  1.00 30.72           C  
ANISOU  472  CG2 ILE A  57     3048   4697   3928    308   -207      4       C  
ATOM    473  CD1 ILE A  57     -35.939  24.645  -7.532  1.00 44.04           C  
ANISOU  473  CD1 ILE A  57     4725   6209   5798    318   -296    -90       C  
ATOM    474  N   ASN A  58     -35.209  19.111  -6.008  1.00 26.74           N  
ANISOU  474  N   ASN A  58     2596   4195   3369    212   -148    172       N  
ATOM    475  CA  ASN A  58     -35.903  18.051  -5.297  1.00 26.24           C  
ANISOU  475  CA  ASN A  58     2505   4210   3257    209   -100    240       C  
ATOM    476  C   ASN A  58     -36.986  18.701  -4.452  1.00 27.69           C  
ANISOU  476  C   ASN A  58     2638   4488   3395    268    -83    212       C  
ATOM    477  O   ASN A  58     -36.679  19.367  -3.472  1.00 33.08           O  
ANISOU  477  O   ASN A  58     3313   5234   4024    336    -94    151       O  
ATOM    478  CB  ASN A  58     -34.909  17.267  -4.433  1.00 27.98           C  
ANISOU  478  CB  ASN A  58     2738   4468   3426    219    -86    271       C  
ATOM    479  CG  ASN A  58     -35.539  16.089  -3.705  1.00 29.04           C  
ANISOU  479  CG  ASN A  58     2835   4680   3521    216    -33    364       C  
ATOM    480  OD1 ASN A  58     -36.754  15.998  -3.563  1.00 29.26           O  
ANISOU  480  OD1 ASN A  58     2816   4754   3547    221     -6    398       O  
ATOM    481  ND2 ASN A  58     -34.694  15.192  -3.209  1.00 31.02           N  
ANISOU  481  ND2 ASN A  58     3098   4945   3745    210    -16    413       N  
ATOM    482  N   ILE A  59     -38.248  18.527  -4.826  1.00 27.89           N  
ANISOU  482  N   ILE A  59     2629   4527   3442    249    -61    252       N  
ATOM    483  CA  ILE A  59     -39.315  19.253  -4.147  1.00 28.81           C  
ANISOU  483  CA  ILE A  59     2696   4731   3519    311    -44    226       C  
ATOM    484  C   ILE A  59     -39.713  18.620  -2.812  1.00 31.75           C  
ANISOU  484  C   ILE A  59     3022   5236   3807    362      6    284       C  
ATOM    485  O   ILE A  59     -40.575  19.143  -2.112  1.00 33.07           O  
ANISOU  485  O   ILE A  59     3144   5498   3923    429     27    270       O  
ATOM    486  CB  ILE A  59     -40.564  19.385  -5.039  1.00 29.15           C  
ANISOU  486  CB  ILE A  59     2712   4746   3618    277    -39    251       C  
ATOM    487  CG1 ILE A  59     -41.182  18.018  -5.325  1.00 28.95           C  
ANISOU  487  CG1 ILE A  59     2660   4718   3622    215     -8    361       C  
ATOM    488  CG2 ILE A  59     -40.215  20.102  -6.336  1.00 29.05           C  
ANISOU  488  CG2 ILE A  59     2737   4622   3680    242    -84    200       C  
ATOM    489  CD1 ILE A  59     -42.500  18.101  -6.081  1.00 30.23           C  
ANISOU  489  CD1 ILE A  59     2785   4865   3837    185     -6    388       C  
ATOM    490  N   THR A  60     -39.078  17.511  -2.442  1.00 32.08           N  
ANISOU  490  N   THR A  60     3070   5290   3830    339     29    354       N  
ATOM    491  CA  THR A  60     -39.335  16.922  -1.131  1.00 35.19           C  
ANISOU  491  CA  THR A  60     3413   5819   4138    396     80    422       C  
ATOM    492  C   THR A  60     -38.471  17.590  -0.061  1.00 39.75           C  
ANISOU  492  C   THR A  60     4005   6475   4621    487     62    338       C  
ATOM    493  O   THR A  60     -38.708  17.415   1.135  1.00 41.91           O  
ANISOU  493  O   THR A  60     4234   6889   4799    567    100    368       O  
ATOM    494  CB  THR A  60     -39.080  15.400  -1.113  1.00 36.01           C  
ANISOU  494  CB  THR A  60     3506   5908   4269    338    114    546       C  
ATOM    495  OG1 THR A  60     -37.679  15.138  -1.273  1.00 36.78           O  
ANISOU  495  OG1 THR A  60     3664   5942   4370    314     87    518       O  
ATOM    496  CG2 THR A  60     -39.865  14.712  -2.218  1.00 36.44           C  
ANISOU  496  CG2 THR A  60     3547   5870   4430    248    114    613       C  
ATOM    497  N   ASN A  61     -37.472  18.357  -0.491  1.00 40.34           N  
ANISOU  497  N   ASN A  61     4136   6464   4726    479      2    235       N  
ATOM    498  CA  ASN A  61     -36.626  19.092   0.445  1.00 39.82           C  
ANISOU  498  CA  ASN A  61     4085   6455   4591    562    -34    136       C  
ATOM    499  C   ASN A  61     -36.224  20.470  -0.073  1.00 41.35           C  
ANISOU  499  C   ASN A  61     4310   6557   4843    572   -106      5       C  
ATOM    500  O   ASN A  61     -35.482  21.195   0.588  1.00 44.75           O  
ANISOU  500  O   ASN A  61     4752   7009   5243    634   -155    -94       O  
ATOM    501  CB  ASN A  61     -35.374  18.276   0.787  1.00 39.18           C  
ANISOU  501  CB  ASN A  61     4031   6371   4486    544    -34    172       C  
ATOM    502  CG  ASN A  61     -34.562  17.897  -0.441  1.00 39.19           C  
ANISOU  502  CG  ASN A  61     4084   6220   4586    444    -58    194       C  
ATOM    503  OD1 ASN A  61     -34.739  18.463  -1.520  1.00 38.30           O  
ANISOU  503  OD1 ASN A  61     3991   6005   4554    400    -87    160       O  
ATOM    504  ND2 ASN A  61     -33.643  16.949  -0.272  1.00 40.24           N  
ANISOU  504  ND2 ASN A  61     4236   6346   4707    417    -44    253       N  
ATOM    505  N   ASN A  62     -36.716  20.818  -1.261  1.00 39.26           N  
ANISOU  505  N   ASN A  62     4055   6192   4671    512   -117      7       N  
ATOM    506  CA  ASN A  62     -36.375  22.075  -1.929  1.00 38.98           C  
ANISOU  506  CA  ASN A  62     4041   6056   4716    510   -181    -91       C  
ATOM    507  C   ASN A  62     -34.869  22.265  -2.105  1.00 39.02           C  
ANISOU  507  C   ASN A  62     4085   5978   4763    490   -232   -130       C  
ATOM    508  O   ASN A  62     -34.378  23.394  -2.146  1.00 41.07           O  
ANISOU  508  O   ASN A  62     4349   6181   5076    518   -294   -225       O  
ATOM    509  CB  ASN A  62     -36.969  23.262  -1.170  1.00 42.04           C  
ANISOU  509  CB  ASN A  62     4398   6506   5068    607   -207   -196       C  
ATOM    510  CG  ASN A  62     -38.420  23.509  -1.530  1.00 44.76           C  
ANISOU  510  CG  ASN A  62     4708   6876   5424    611   -174   -171       C  
ATOM    511  OD1 ASN A  62     -39.017  22.754  -2.298  1.00 42.28           O  
ANISOU  511  OD1 ASN A  62     4388   6537   5141    541   -133    -74       O  
ATOM    512  ND2 ASN A  62     -39.001  24.560  -0.963  1.00 47.45           N  
ANISOU  512  ND2 ASN A  62     5023   7267   5740    698   -195   -262       N  
ATOM    513  N   GLU A  63     -34.152  21.148  -2.216  1.00 37.17           N  
ANISOU  513  N   GLU A  63     3875   5734   4516    441   -208    -52       N  
ATOM    514  CA  GLU A  63     -32.714  21.144  -2.474  1.00 41.48           C  
ANISOU  514  CA  GLU A  63     4455   6203   5101    414   -247    -65       C  
ATOM    515  C   GLU A  63     -32.427  21.154  -3.971  1.00 36.86           C  
ANISOU  515  C   GLU A  63     3896   5493   4618    339   -257    -25       C  
ATOM    516  O   GLU A  63     -33.158  20.544  -4.752  1.00 34.80           O  
ANISOU  516  O   GLU A  63     3637   5215   4372    294   -220     41       O  
ATOM    517  CB  GLU A  63     -32.057  19.914  -1.853  1.00 46.46           C  
ANISOU  517  CB  GLU A  63     5097   6890   5664    406   -213      4       C  
ATOM    518  CG  GLU A  63     -31.747  20.014  -0.372  1.00 54.04           C  
ANISOU  518  CG  GLU A  63     6039   7969   6526    490   -221    -45       C  
ATOM    519  CD  GLU A  63     -30.662  19.039   0.034  1.00 59.43           C  
ANISOU  519  CD  GLU A  63     6741   8672   7170    475   -207     12       C  
ATOM    520  OE1 GLU A  63     -31.007  17.925   0.485  1.00 60.00           O  
ANISOU  520  OE1 GLU A  63     6797   8821   7180    473   -146    105       O  
ATOM    521  OE2 GLU A  63     -29.467  19.378  -0.106  1.00 63.28           O  
ANISOU  521  OE2 GLU A  63     7253   9095   7697    465   -257    -29       O  
ATOM    522  N   LYS A  64     -31.361  21.835  -4.378  1.00 34.66           N  
ANISOU  522  N   LYS A  64     3632   5128   4408    332   -308    -62       N  
ATOM    523  CA  LYS A  64     -30.893  21.718  -5.753  1.00 32.72           C  
ANISOU  523  CA  LYS A  64     3408   4782   4242    273   -310     -6       C  
ATOM    524  C   LYS A  64     -30.255  20.353  -5.960  1.00 29.05           C  
ANISOU  524  C   LYS A  64     2976   4318   3743    232   -275     77       C  
ATOM    525  O   LYS A  64     -29.535  19.863  -5.090  1.00 28.13           O  
ANISOU  525  O   LYS A  64     2868   4245   3576    247   -273     80       O  
ATOM    526  CB  LYS A  64     -29.887  22.820  -6.098  1.00 37.17           C  
ANISOU  526  CB  LYS A  64     3965   5257   4900    281   -372    -49       C  
ATOM    527  CG  LYS A  64     -30.489  24.207  -6.235  1.00 41.34           C  
ANISOU  527  CG  LYS A  64     4459   5749   5499    311   -411   -120       C  
ATOM    528  CD  LYS A  64     -29.454  25.177  -6.779  1.00 45.51           C  
ANISOU  528  CD  LYS A  64     4971   6171   6149    306   -470   -132       C  
ATOM    529  CE  LYS A  64     -29.956  26.610  -6.742  1.00 48.92           C  
ANISOU  529  CE  LYS A  64     5362   6558   6668    342   -519   -210       C  
ATOM    530  NZ  LYS A  64     -28.861  27.565  -7.066  1.00 50.39           N  
ANISOU  530  NZ  LYS A  64     5519   6635   6990    339   -585   -221       N  
ATOM    531  N   VAL A  65     -30.532  19.735  -7.105  1.00 25.52           N  
ANISOU  531  N   VAL A  65     2547   3828   3323    186   -251    141       N  
ATOM    532  CA  VAL A  65     -29.860  18.500  -7.492  1.00 22.41           C  
ANISOU  532  CA  VAL A  65     2187   3415   2912    150   -227    212       C  
ATOM    533  C   VAL A  65     -29.456  18.570  -8.956  1.00 21.80           C  
ANISOU  533  C   VAL A  65     2130   3258   2895    126   -238    245       C  
ATOM    534  O   VAL A  65     -29.789  19.521  -9.661  1.00 22.10           O  
ANISOU  534  O   VAL A  65     2152   3261   2986    133   -258    224       O  
ATOM    535  CB  VAL A  65     -30.747  17.258  -7.283  1.00 21.20           C  
ANISOU  535  CB  VAL A  65     2032   3309   2714    128   -182    264       C  
ATOM    536  CG1 VAL A  65     -31.029  17.039  -5.806  1.00 23.34           C  
ANISOU  536  CG1 VAL A  65     2277   3677   2916    161   -161    257       C  
ATOM    537  CG2 VAL A  65     -32.043  17.392  -8.078  1.00 19.79           C  
ANISOU  537  CG2 VAL A  65     1837   3118   2565    110   -176    266       C  
ATOM    538  N   VAL A  66     -28.736  17.558  -9.413  1.00 22.78           N  
ANISOU  538  N   VAL A  66     2288   3359   3009    105   -223    299       N  
ATOM    539  CA  VAL A  66     -28.417  17.443 -10.823  1.00 23.26           C  
ANISOU  539  CA  VAL A  66     2369   3363   3105     95   -228    335       C  
ATOM    540  C   VAL A  66     -29.100  16.203 -11.373  1.00 23.28           C  
ANISOU  540  C   VAL A  66     2394   3368   3084     70   -207    367       C  
ATOM    541  O   VAL A  66     -29.069  15.138 -10.754  1.00 22.14           O  
ANISOU  541  O   VAL A  66     2261   3244   2908     53   -187    390       O  
ATOM    542  CB  VAL A  66     -26.894  17.371 -11.062  1.00 23.21           C  
ANISOU  542  CB  VAL A  66     2384   3323   3113    103   -237    370       C  
ATOM    543  CG1 VAL A  66     -26.593  16.917 -12.480  1.00 26.61           C  
ANISOU  543  CG1 VAL A  66     2839   3717   3554    106   -231    418       C  
ATOM    544  CG2 VAL A  66     -26.255  18.723 -10.785  1.00 24.54           C  
ANISOU  544  CG2 VAL A  66     2519   3467   3337    125   -272    341       C  
ATOM    545  N   VAL A  67     -29.741  16.352 -12.525  1.00 21.28           N  
ANISOU  545  N   VAL A  67     2140   3092   2854     69   -215    368       N  
ATOM    546  CA  VAL A  67     -30.398  15.229 -13.164  1.00 20.56           C  
ANISOU  546  CA  VAL A  67     2067   2992   2754     48   -211    384       C  
ATOM    547  C   VAL A  67     -29.736  14.913 -14.491  1.00 19.76           C  
ANISOU  547  C   VAL A  67     1998   2855   2655     68   -224    404       C  
ATOM    548  O   VAL A  67     -29.664  15.761 -15.379  1.00 19.74           O  
ANISOU  548  O   VAL A  67     1985   2844   2669     95   -235    405       O  
ATOM    549  CB  VAL A  67     -31.891  15.499 -13.400  1.00 20.32           C  
ANISOU  549  CB  VAL A  67     2004   2977   2738     36   -216    361       C  
ATOM    550  CG1 VAL A  67     -32.513  14.318 -14.122  1.00 21.25           C  
ANISOU  550  CG1 VAL A  67     2138   3076   2862     14   -226    372       C  
ATOM    551  CG2 VAL A  67     -32.595  15.753 -12.074  1.00 22.22           C  
ANISOU  551  CG2 VAL A  67     2209   3267   2965     29   -198    347       C  
ATOM    552  N   LYS A  68     -29.267  13.677 -14.615  1.00 18.25           N  
ANISOU  552  N   LYS A  68     1841   2646   2446     60   -221    425       N  
ATOM    553  CA  LYS A  68     -28.592  13.199 -15.814  1.00 17.81           C  
ANISOU  553  CA  LYS A  68     1822   2566   2379     92   -233    440       C  
ATOM    554  C   LYS A  68     -29.485  12.204 -16.543  1.00 18.25           C  
ANISOU  554  C   LYS A  68     1893   2605   2438     83   -256    417       C  
ATOM    555  O   LYS A  68     -29.617  11.053 -16.125  1.00 16.25           O  
ANISOU  555  O   LYS A  68     1652   2329   2192     55   -258    420       O  
ATOM    556  CB  LYS A  68     -27.257  12.551 -15.431  1.00 18.82           C  
ANISOU  556  CB  LYS A  68     1981   2682   2488     99   -219    475       C  
ATOM    557  CG  LYS A  68     -26.426  11.997 -16.577  1.00 18.90           C  
ANISOU  557  CG  LYS A  68     2029   2675   2477    144   -227    494       C  
ATOM    558  CD  LYS A  68     -25.137  11.399 -15.998  1.00 23.67           C  
ANISOU  558  CD  LYS A  68     2659   3270   3066    147   -208    533       C  
ATOM    559  CE  LYS A  68     -24.241  10.779 -17.054  1.00 30.78           C  
ANISOU  559  CE  LYS A  68     3597   4160   3937    201   -211    556       C  
ATOM    560  NZ  LYS A  68     -22.994  10.222 -16.438  1.00 34.51           N  
ANISOU  560  NZ  LYS A  68     4091   4625   4398    203   -190    598       N  
ATOM    561  N   ILE A  69     -30.118  12.649 -17.621  1.00 17.82           N  
ANISOU  561  N   ILE A  69     1829   2557   2384    108   -278    394       N  
ATOM    562  CA  ILE A  69     -31.025  11.783 -18.362  1.00 18.59           C  
ANISOU  562  CA  ILE A  69     1936   2639   2490    103   -314    359       C  
ATOM    563  C   ILE A  69     -30.257  11.064 -19.461  1.00 21.55           C  
ANISOU  563  C   ILE A  69     2357   3000   2832    157   -337    351       C  
ATOM    564  O   ILE A  69     -29.761  11.690 -20.401  1.00 21.38           O  
ANISOU  564  O   ILE A  69     2340   3006   2776    217   -337    362       O  
ATOM    565  CB  ILE A  69     -32.191  12.574 -18.961  1.00 16.80           C  
ANISOU  565  CB  ILE A  69     1675   2436   2275    108   -332    332       C  
ATOM    566  CG1 ILE A  69     -32.914  13.354 -17.857  1.00 17.62           C  
ANISOU  566  CG1 ILE A  69     1733   2558   2404     66   -307    338       C  
ATOM    567  CG2 ILE A  69     -33.145  11.646 -19.687  1.00 20.67           C  
ANISOU  567  CG2 ILE A  69     2169   2905   2780    101   -380    289       C  
ATOM    568  CD1 ILE A  69     -34.110  14.134 -18.353  1.00 16.75           C  
ANISOU  568  CD1 ILE A  69     1585   2471   2309     68   -321    316       C  
ATOM    569  N   LEU A  70     -30.148   9.746 -19.325  1.00 20.88           N  
ANISOU  569  N   LEU A  70     2300   2874   2761    141   -355    337       N  
ATOM    570  CA  LEU A  70     -29.327   8.951 -20.231  1.00 23.68           C  
ANISOU  570  CA  LEU A  70     2702   3213   3082    199   -378    323       C  
ATOM    571  C   LEU A  70     -29.946   8.834 -21.614  1.00 27.31           C  
ANISOU  571  C   LEU A  70     3170   3685   3520    253   -430    266       C  
ATOM    572  O   LEU A  70     -31.147   8.604 -21.747  1.00 28.29           O  
ANISOU  572  O   LEU A  70     3273   3793   3682    221   -468    222       O  
ATOM    573  CB  LEU A  70     -29.095   7.557 -19.646  1.00 20.27           C  
ANISOU  573  CB  LEU A  70     2295   2723   2685    167   -388    321       C  
ATOM    574  CG  LEU A  70     -28.522   7.564 -18.227  1.00 19.42           C  
ANISOU  574  CG  LEU A  70     2175   2614   2591    119   -338    380       C  
ATOM    575  CD1 LEU A  70     -28.281   6.152 -17.730  1.00 22.47           C  
ANISOU  575  CD1 LEU A  70     2579   2943   3016     93   -345    390       C  
ATOM    576  CD2 LEU A  70     -27.235   8.374 -18.175  1.00 21.37           C  
ANISOU  576  CD2 LEU A  70     2433   2898   2788    159   -299    423       C  
ATOM    577  N   LYS A  71     -29.122   9.004 -22.642  1.00 30.03           N  
ANISOU  577  N   LYS A  71     3542   4068   3801    340   -432    270       N  
ATOM    578  CA  LYS A  71     -29.555   8.746 -24.008  1.00 31.39           C  
ANISOU  578  CA  LYS A  71     3728   4265   3933    412   -485    210       C  
ATOM    579  C   LYS A  71     -29.706   7.246 -24.183  1.00 31.56           C  
ANISOU  579  C   LYS A  71     3787   4224   3979    413   -544    141       C  
ATOM    580  O   LYS A  71     -29.038   6.476 -23.488  1.00 25.13           O  
ANISOU  580  O   LYS A  71     2996   3361   3190    386   -530    160       O  
ATOM    581  CB  LYS A  71     -28.557   9.304 -25.025  1.00 35.21           C  
ANISOU  581  CB  LYS A  71     4224   4820   4333    520   -464    248       C  
ATOM    582  CG  LYS A  71     -28.612  10.809 -25.222  1.00 36.50           C  
ANISOU  582  CG  LYS A  71     4339   5043   4486    535   -424    310       C  
ATOM    583  CD  LYS A  71     -27.593  11.234 -26.264  1.00 41.72           C  
ANISOU  583  CD  LYS A  71     5003   5777   5073    649   -402    366       C  
ATOM    584  CE  LYS A  71     -27.555  12.742 -26.439  1.00 44.58           C  
ANISOU  584  CE  LYS A  71     5305   6187   5445    663   -361    446       C  
ATOM    585  NZ  LYS A  71     -26.349  13.158 -27.215  1.00 46.63           N  
ANISOU  585  NZ  LYS A  71     5559   6501   5656    752   -320    526       N  
ATOM    586  N   PRO A  72     -30.598   6.824 -25.096  1.00 38.31           N  
ANISOU  586  N   PRO A  72     4644   5076   4835    443   -616     58       N  
ATOM    587  CA  PRO A  72     -30.782   5.403 -25.414  1.00 42.48           C  
ANISOU  587  CA  PRO A  72     5205   5536   5401    454   -691    -24       C  
ATOM    588  C   PRO A  72     -29.464   4.694 -25.724  1.00 47.87           C  
ANISOU  588  C   PRO A  72     5943   6214   6032    529   -686    -26       C  
ATOM    589  O   PRO A  72     -28.763   5.012 -26.686  1.00 50.09           O  
ANISOU  589  O   PRO A  72     6248   6569   6215    638   -680    -26       O  
ATOM    590  CB  PRO A  72     -31.698   5.441 -26.637  1.00 42.20           C  
ANISOU  590  CB  PRO A  72     5163   5533   5339    513   -768   -112       C  
ATOM    591  CG  PRO A  72     -32.525   6.667 -26.416  1.00 40.98           C  
ANISOU  591  CG  PRO A  72     4954   5426   5191    468   -733    -69       C  
ATOM    592  CD  PRO A  72     -31.592   7.671 -25.782  1.00 38.42           C  
ANISOU  592  CD  PRO A  72     4622   5144   4831    461   -637     35       C  
ATOM    593  N   VAL A  73     -29.138   3.728 -24.876  1.00 51.86           N  
ANISOU  593  N   VAL A  73     6463   6636   6606    473   -685    -16       N  
ATOM    594  CA  VAL A  73     -27.873   3.008 -24.929  1.00 55.23           C  
ANISOU  594  CA  VAL A  73     6939   7048   6999    529   -672     -5       C  
ATOM    595  C   VAL A  73     -28.128   1.613 -24.377  1.00 57.34           C  
ANISOU  595  C   VAL A  73     7215   7198   7374    472   -720    -44       C  
ATOM    596  O   VAL A  73     -29.068   1.437 -23.604  1.00 59.17           O  
ANISOU  596  O   VAL A  73     7403   7373   7705    372   -731    -33       O  
ATOM    597  CB  VAL A  73     -26.773   3.748 -24.128  1.00 54.95           C  
ANISOU  597  CB  VAL A  73     6899   7054   6927    512   -575    109       C  
ATOM    598  CG1 VAL A  73     -26.094   2.836 -23.105  1.00 54.77           C  
ANISOU  598  CG1 VAL A  73     6892   6961   6958    462   -551    147       C  
ATOM    599  CG2 VAL A  73     -25.749   4.359 -25.074  1.00 54.21           C  
ANISOU  599  CG2 VAL A  73     6825   7050   6720    628   -546    138       C  
ATOM    600  N   LYS A  74     -27.319   0.629 -24.775  1.00 57.48           N  
ANISOU  600  N   LYS A  74     7282   7180   7378    538   -750    -83       N  
ATOM    601  CA  LYS A  74     -27.582  -0.760 -24.403  1.00 59.87           C  
ANISOU  601  CA  LYS A  74     7590   7359   7799    494   -810   -127       C  
ATOM    602  C   LYS A  74     -27.709  -0.887 -22.892  1.00 59.92           C  
ANISOU  602  C   LYS A  74     7554   7313   7899    371   -752    -28       C  
ATOM    603  O   LYS A  74     -27.055  -0.167 -22.130  1.00 58.19           O  
ANISOU  603  O   LYS A  74     7327   7151   7633    346   -663     68       O  
ATOM    604  CB  LYS A  74     -26.493  -1.697 -24.931  1.00 62.24           C  
ANISOU  604  CB  LYS A  74     7951   7633   8063    589   -834   -169       C  
ATOM    605  CG  LYS A  74     -25.116  -1.446 -24.361  1.00 63.10           C  
ANISOU  605  CG  LYS A  74     8082   7787   8108    606   -739    -66       C  
ATOM    606  CD  LYS A  74     -24.029  -1.932 -25.299  1.00 64.54           C  
ANISOU  606  CD  LYS A  74     8325   7999   8200    742   -755   -109       C  
ATOM    607  CE  LYS A  74     -22.838  -0.983 -25.281  1.00 64.24           C  
ANISOU  607  CE  LYS A  74     8293   8070   8045    793   -659     -6       C  
ATOM    608  NZ  LYS A  74     -23.099   0.343 -25.915  1.00 64.52           N  
ANISOU  608  NZ  LYS A  74     8305   8218   7994    832   -634     16       N  
ATOM    609  N   LYS A  75     -28.581  -1.791 -22.469  1.00 61.87           N  
ANISOU  609  N   LYS A  75     7768   7457   8284    297   -806    -50       N  
ATOM    610  CA  LYS A  75     -29.003  -1.851 -21.077  1.00 61.69           C  
ANISOU  610  CA  LYS A  75     7686   7400   8352    184   -755     49       C  
ATOM    611  C   LYS A  75     -27.831  -2.087 -20.125  1.00 58.07           C  
ANISOU  611  C   LYS A  75     7242   6946   7876    173   -676    144       C  
ATOM    612  O   LYS A  75     -27.809  -1.539 -19.024  1.00 57.79           O  
ANISOU  612  O   LYS A  75     7169   6953   7836    113   -601    239       O  
ATOM    613  CB  LYS A  75     -30.069  -2.939 -20.899  1.00 63.92           C  
ANISOU  613  CB  LYS A  75     7923   7561   8803    118   -834     19       C  
ATOM    614  CG  LYS A  75     -30.567  -3.119 -19.470  1.00 65.43           C  
ANISOU  614  CG  LYS A  75     8042   7723   9096      9   -780    137       C  
ATOM    615  CD  LYS A  75     -31.243  -1.862 -18.958  1.00 66.11           C  
ANISOU  615  CD  LYS A  75     8084   7905   9131    -33   -720    191       C  
ATOM    616  CE  LYS A  75     -31.859  -2.074 -17.591  1.00 66.35           C  
ANISOU  616  CE  LYS A  75     8035   7919   9256   -126   -672    304       C  
ATOM    617  NZ  LYS A  75     -32.328  -0.799 -16.982  1.00 63.25           N  
ANISOU  617  NZ  LYS A  75     7606   7633   8793   -152   -603    356       N  
ATOM    618  N   LYS A  76     -26.850  -2.877 -20.552  1.00 54.85           N  
ANISOU  618  N   LYS A  76     6887   6502   7452    238   -695    114       N  
ATOM    619  CA  LYS A  76     -25.748  -3.232 -19.662  1.00 52.76           C  
ANISOU  619  CA  LYS A  76     6634   6233   7180    228   -626    204       C  
ATOM    620  C   LYS A  76     -24.812  -2.051 -19.384  1.00 48.16           C  
ANISOU  620  C   LYS A  76     6065   5767   6468    254   -538    272       C  
ATOM    621  O   LYS A  76     -24.231  -1.971 -18.305  1.00 46.81           O  
ANISOU  621  O   LYS A  76     5877   5614   6295    214   -470    364       O  
ATOM    622  CB  LYS A  76     -24.961  -4.421 -20.225  1.00 55.19           C  
ANISOU  622  CB  LYS A  76     6994   6466   7510    297   -673    151       C  
ATOM    623  CG  LYS A  76     -24.286  -4.183 -21.561  1.00 56.31           C  
ANISOU  623  CG  LYS A  76     7200   6663   7530    424   -702     68       C  
ATOM    624  CD  LYS A  76     -23.564  -5.445 -22.013  1.00 56.96           C  
ANISOU  624  CD  LYS A  76     7332   6667   7642    494   -751     12       C  
ATOM    625  CE  LYS A  76     -22.402  -5.768 -21.089  1.00 56.80           C  
ANISOU  625  CE  LYS A  76     7320   6644   7617    479   -672    118       C  
ATOM    626  NZ  LYS A  76     -21.676  -6.997 -21.508  1.00 58.01           N  
ANISOU  626  NZ  LYS A  76     7521   6719   7803    551   -717     68       N  
ATOM    627  N   LYS A  77     -24.671  -1.129 -20.333  1.00 43.42           N  
ANISOU  627  N   LYS A  77     5488   5244   5766    323   -541    231       N  
ATOM    628  CA  LYS A  77     -23.865   0.061 -20.073  1.00 40.36           C  
ANISOU  628  CA  LYS A  77     5099   4954   5281    340   -465    302       C  
ATOM    629  C   LYS A  77     -24.563   0.974 -19.063  1.00 34.80           C  
ANISOU  629  C   LYS A  77     4339   4286   4600    253   -422    356       C  
ATOM    630  O   LYS A  77     -23.918   1.573 -18.195  1.00 29.53           O  
ANISOU  630  O   LYS A  77     3656   3662   3901    230   -359    431       O  
ATOM    631  CB  LYS A  77     -23.570   0.836 -21.356  1.00 40.82           C  
ANISOU  631  CB  LYS A  77     5184   5089   5238    438   -476    262       C  
ATOM    632  CG  LYS A  77     -22.928   2.190 -21.072  1.00 42.37           C  
ANISOU  632  CG  LYS A  77     5361   5374   5365    443   -405    342       C  
ATOM    633  CD  LYS A  77     -22.296   2.838 -22.285  1.00 44.13           C  
ANISOU  633  CD  LYS A  77     5603   5674   5491    552   -401    339       C  
ATOM    634  CE  LYS A  77     -21.807   4.231 -21.920  1.00 45.49           C  
ANISOU  634  CE  LYS A  77     5739   5916   5631    539   -338    425       C  
ATOM    635  NZ  LYS A  77     -21.036   4.878 -23.013  1.00 47.53           N  
ANISOU  635  NZ  LYS A  77     6002   6252   5806    647   -322    456       N  
ATOM    636  N   ILE A  78     -25.884   1.074 -19.179  1.00 29.67           N  
ANISOU  636  N   ILE A  78     3655   3616   4003    211   -462    314       N  
ATOM    637  CA  ILE A  78     -26.674   1.841 -18.228  1.00 26.64           C  
ANISOU  637  CA  ILE A  78     3214   3264   3643    136   -426    360       C  
ATOM    638  C   ILE A  78     -26.586   1.208 -16.848  1.00 24.41           C  
ANISOU  638  C   ILE A  78     2901   2952   3422     69   -387    435       C  
ATOM    639  O   ILE A  78     -26.358   1.894 -15.854  1.00 22.54           O  
ANISOU  639  O   ILE A  78     2637   2771   3155     41   -329    497       O  
ATOM    640  CB  ILE A  78     -28.156   1.932 -18.654  1.00 31.15           C  
ANISOU  640  CB  ILE A  78     3752   3816   4269    105   -479    305       C  
ATOM    641  CG1 ILE A  78     -28.293   2.687 -19.977  1.00 33.26           C  
ANISOU  641  CG1 ILE A  78     4042   4132   4465    175   -511    238       C  
ATOM    642  CG2 ILE A  78     -28.981   2.606 -17.573  1.00 31.32           C  
ANISOU  642  CG2 ILE A  78     3711   3871   4318     32   -438    358       C  
ATOM    643  CD1 ILE A  78     -29.709   2.675 -20.527  1.00 34.61           C  
ANISOU  643  CD1 ILE A  78     4182   4282   4686    154   -574    175       C  
ATOM    644  N   LYS A  79     -26.773  -0.110 -16.795  1.00 25.24           N  
ANISOU  644  N   LYS A  79     3006   2969   3615     51   -424    429       N  
ATOM    645  CA  LYS A  79     -26.629  -0.855 -15.551  1.00 25.55           C  
ANISOU  645  CA  LYS A  79     3011   2978   3719     -3   -387    514       C  
ATOM    646  C   LYS A  79     -25.210  -0.780 -15.012  1.00 24.82           C  
ANISOU  646  C   LYS A  79     2948   2927   3557     26   -328    572       C  
ATOM    647  O   LYS A  79     -25.005  -0.762 -13.801  1.00 24.90           O  
ANISOU  647  O   LYS A  79     2923   2969   3568    -11   -273    654       O  
ATOM    648  CB  LYS A  79     -27.026  -2.320 -15.741  1.00 30.25           C  
ANISOU  648  CB  LYS A  79     3598   3456   4441    -23   -446    497       C  
ATOM    649  CG  LYS A  79     -28.510  -2.539 -15.953  1.00 35.39           C  
ANISOU  649  CG  LYS A  79     4197   4056   5195    -72   -504    465       C  
ATOM    650  CD  LYS A  79     -28.864  -4.006 -15.736  1.00 41.58           C  
ANISOU  650  CD  LYS A  79     4947   4714   6136   -111   -552    484       C  
ATOM    651  CE  LYS A  79     -30.337  -4.176 -15.423  1.00 47.56           C  
ANISOU  651  CE  LYS A  79     5623   5433   7016   -183   -583    509       C  
ATOM    652  NZ  LYS A  79     -30.805  -5.576 -15.629  1.00 51.66           N  
ANISOU  652  NZ  LYS A  79     6110   5806   7714   -213   -663    496       N  
ATOM    653  N   ARG A  80     -24.230  -0.749 -15.908  1.00 23.31           N  
ANISOU  653  N   ARG A  80     2816   2740   3300     98   -339    533       N  
ATOM    654  CA  ARG A  80     -22.838  -0.681 -15.481  1.00 22.82           C  
ANISOU  654  CA  ARG A  80     2780   2715   3176    128   -287    590       C  
ATOM    655  C   ARG A  80     -22.607   0.578 -14.657  1.00 21.09           C  
ANISOU  655  C   ARG A  80     2532   2588   2894    107   -230    641       C  
ATOM    656  O   ARG A  80     -22.095   0.510 -13.539  1.00 20.67           O  
ANISOU  656  O   ARG A  80     2457   2561   2834     82   -184    710       O  
ATOM    657  CB  ARG A  80     -21.891  -0.713 -16.681  1.00 23.63           C  
ANISOU  657  CB  ARG A  80     2944   2822   3212    219   -306    545       C  
ATOM    658  CG  ARG A  80     -20.428  -0.872 -16.307  1.00 22.08           C  
ANISOU  658  CG  ARG A  80     2772   2649   2967    253   -258    609       C  
ATOM    659  CD  ARG A  80     -19.555  -0.962 -17.544  1.00 22.33           C  
ANISOU  659  CD  ARG A  80     2858   2692   2932    353   -276    571       C  
ATOM    660  NE  ARG A  80     -19.555   0.294 -18.289  1.00 21.21           N  
ANISOU  660  NE  ARG A  80     2715   2627   2717    395   -271    556       N  
ATOM    661  CZ  ARG A  80     -19.017   0.447 -19.495  1.00 22.65           C  
ANISOU  661  CZ  ARG A  80     2932   2843   2831    492   -285    527       C  
ATOM    662  NH1 ARG A  80     -18.446  -0.583 -20.106  1.00 24.26           N  
ANISOU  662  NH1 ARG A  80     3182   3013   3024    562   -310    496       N  
ATOM    663  NH2 ARG A  80     -19.053   1.630 -20.090  1.00 22.73           N  
ANISOU  663  NH2 ARG A  80     2927   2925   2785    525   -275    533       N  
ATOM    664  N   GLU A  81     -23.002   1.723 -15.208  1.00 21.63           N  
ANISOU  664  N   GLU A  81     2595   2703   2918    121   -238    602       N  
ATOM    665  CA  GLU A  81     -22.811   2.996 -14.526  1.00 17.72           C  
ANISOU  665  CA  GLU A  81     2072   2284   2376    107   -198    635       C  
ATOM    666  C   GLU A  81     -23.579   3.016 -13.202  1.00 19.91           C  
ANISOU  666  C   GLU A  81     2296   2582   2688     43   -173    672       C  
ATOM    667  O   GLU A  81     -23.057   3.445 -12.181  1.00 18.35           O  
ANISOU  667  O   GLU A  81     2078   2436   2459     33   -134    718       O  
ATOM    668  CB  GLU A  81     -23.241   4.168 -15.418  1.00 17.14           C  
ANISOU  668  CB  GLU A  81     1996   2246   2270    134   -216    589       C  
ATOM    669  CG  GLU A  81     -23.036   5.526 -14.757  1.00 19.23           C  
ANISOU  669  CG  GLU A  81     2228   2574   2504    122   -184    614       C  
ATOM    670  CD  GLU A  81     -23.355   6.699 -15.663  1.00 19.45           C  
ANISOU  670  CD  GLU A  81     2249   2630   2511    151   -200    582       C  
ATOM    671  OE1 GLU A  81     -23.667   6.485 -16.855  1.00 20.92           O  
ANISOU  671  OE1 GLU A  81     2456   2801   2691    190   -231    543       O  
ATOM    672  OE2 GLU A  81     -23.288   7.847 -15.178  1.00 18.53           O  
ANISOU  672  OE2 GLU A  81     2102   2553   2388    141   -184    594       O  
ATOM    673  N   ILE A  82     -24.815   2.534 -13.221  1.00 19.76           N  
ANISOU  673  N   ILE A  82     2248   2526   2733      5   -198    654       N  
ATOM    674  CA  ILE A  82     -25.632   2.511 -12.009  1.00 18.76           C  
ANISOU  674  CA  ILE A  82     2062   2429   2638    -46   -170    702       C  
ATOM    675  C   ILE A  82     -24.995   1.666 -10.908  1.00 19.33           C  
ANISOU  675  C   ILE A  82     2118   2503   2722    -59   -131    783       C  
ATOM    676  O   ILE A  82     -24.879   2.110  -9.763  1.00 19.34           O  
ANISOU  676  O   ILE A  82     2085   2579   2686    -67    -88    831       O  
ATOM    677  CB  ILE A  82     -27.053   1.983 -12.301  1.00 19.55           C  
ANISOU  677  CB  ILE A  82     2127   2479   2824    -85   -208    683       C  
ATOM    678  CG1 ILE A  82     -27.837   3.015 -13.113  1.00 19.44           C  
ANISOU  678  CG1 ILE A  82     2112   2487   2787    -76   -236    615       C  
ATOM    679  CG2 ILE A  82     -27.776   1.661 -11.002  1.00 22.82           C  
ANISOU  679  CG2 ILE A  82     2470   2920   3280   -131   -171    761       C  
ATOM    680  CD1 ILE A  82     -29.210   2.531 -13.585  1.00 20.14           C  
ANISOU  680  CD1 ILE A  82     2168   2524   2960   -109   -284    586       C  
ATOM    681  N   LYS A  83     -24.568   0.456 -11.256  1.00 19.56           N  
ANISOU  681  N   LYS A  83     2173   2457   2803    -54   -148    796       N  
ATOM    682  CA  LYS A  83     -23.983  -0.446 -10.272  1.00 21.97           C  
ANISOU  682  CA  LYS A  83     2459   2758   3132    -66   -111    881       C  
ATOM    683  C   LYS A  83     -22.685   0.133  -9.719  1.00 21.38           C  
ANISOU  683  C   LYS A  83     2406   2755   2964    -34    -69    910       C  
ATOM    684  O   LYS A  83     -22.410   0.046  -8.526  1.00 20.39           O  
ANISOU  684  O   LYS A  83     2244   2686   2817    -43    -25    980       O  
ATOM    685  CB  LYS A  83     -23.728  -1.826 -10.878  1.00 24.53           C  
ANISOU  685  CB  LYS A  83     2810   2973   3538    -60   -145    878       C  
ATOM    686  CG  LYS A  83     -23.211  -2.853  -9.870  1.00 24.10           C  
ANISOU  686  CG  LYS A  83     2727   2903   3527    -75   -107    978       C  
ATOM    687  CD  LYS A  83     -24.219  -3.083  -8.749  1.00 28.84           C  
ANISOU  687  CD  LYS A  83     3242   3532   4186   -125    -76   1063       C  
ATOM    688  CE  LYS A  83     -23.663  -4.016  -7.687  1.00 30.74           C  
ANISOU  688  CE  LYS A  83     3445   3776   4458   -131    -29   1178       C  
ATOM    689  NZ  LYS A  83     -24.681  -4.354  -6.652  1.00 31.46           N  
ANISOU  689  NZ  LYS A  83     3441   3897   4614   -171      3   1279       N  
ATOM    690  N   ILE A  84     -21.898   0.744 -10.595  1.00 19.38           N  
ANISOU  690  N   ILE A  84     2204   2505   2656      8    -84    859       N  
ATOM    691  CA  ILE A  84     -20.642   1.346 -10.178  1.00 17.02           C  
ANISOU  691  CA  ILE A  84     1918   2264   2282     37    -54    886       C  
ATOM    692  C   ILE A  84     -20.891   2.514  -9.219  1.00 18.58           C  
ANISOU  692  C   ILE A  84     2074   2551   2433     24    -32    891       C  
ATOM    693  O   ILE A  84     -20.227   2.632  -8.192  1.00 20.36           O  
ANISOU  693  O   ILE A  84     2282   2833   2622     28     -2    936       O  
ATOM    694  CB  ILE A  84     -19.823   1.795 -11.409  1.00 18.33           C  
ANISOU  694  CB  ILE A  84     2137   2416   2411     89    -75    843       C  
ATOM    695  CG1 ILE A  84     -19.170   0.563 -12.048  1.00 21.38           C  
ANISOU  695  CG1 ILE A  84     2567   2735   2821    121    -86    851       C  
ATOM    696  CG2 ILE A  84     -18.777   2.825 -11.021  1.00 16.09           C  
ANISOU  696  CG2 ILE A  84     1849   2197   2066    110    -52    866       C  
ATOM    697  CD1 ILE A  84     -18.416   0.829 -13.329  1.00 22.96           C  
ANISOU  697  CD1 ILE A  84     2816   2930   2979    188   -104    816       C  
ATOM    698  N   LEU A  85     -21.867   3.360  -9.536  1.00 16.61           N  
ANISOU  698  N   LEU A  85     1808   2315   2187     13    -52    839       N  
ATOM    699  CA  LEU A  85     -22.186   4.494  -8.673  1.00 16.15           C  
ANISOU  699  CA  LEU A  85     1710   2336   2088      8    -39    829       C  
ATOM    700  C   LEU A  85     -22.671   4.033  -7.298  1.00 16.68           C  
ANISOU  700  C   LEU A  85     1726   2457   2153    -11     -4    886       C  
ATOM    701  O   LEU A  85     -22.332   4.633  -6.278  1.00 16.62           O  
ANISOU  701  O   LEU A  85     1693   2529   2091      4     15    896       O  
ATOM    702  CB  LEU A  85     -23.238   5.386  -9.326  1.00 16.61           C  
ANISOU  702  CB  LEU A  85     1759   2392   2159      1    -65    767       C  
ATOM    703  CG  LEU A  85     -22.797   6.278 -10.484  1.00 16.41           C  
ANISOU  703  CG  LEU A  85     1766   2349   2121     31    -92    720       C  
ATOM    704  CD1 LEU A  85     -24.022   6.828 -11.202  1.00 15.95           C  
ANISOU  704  CD1 LEU A  85     1695   2280   2086     21   -117    668       C  
ATOM    705  CD2 LEU A  85     -21.920   7.415  -9.976  1.00 13.07           C  
ANISOU  705  CD2 LEU A  85     1331   1973   1660     51    -86    718       C  
ATOM    706  N   GLU A  86     -23.453   2.959  -7.267  1.00 20.57           N  
ANISOU  706  N   GLU A  86     2199   2910   2709    -39      1    925       N  
ATOM    707  CA  GLU A  86     -23.947   2.432  -5.997  1.00 23.21           C  
ANISOU  707  CA  GLU A  86     2471   3299   3047    -52     40   1002       C  
ATOM    708  C   GLU A  86     -22.820   1.778  -5.196  1.00 22.53           C  
ANISOU  708  C   GLU A  86     2385   3241   2933    -35     74   1073       C  
ATOM    709  O   GLU A  86     -22.729   1.964  -3.983  1.00 20.54           O  
ANISOU  709  O   GLU A  86     2091   3086   2626    -17    109   1119       O  
ATOM    710  CB  GLU A  86     -25.101   1.452  -6.236  1.00 24.71           C  
ANISOU  710  CB  GLU A  86     2626   3426   3337    -91     32   1038       C  
ATOM    711  CG  GLU A  86     -26.409   2.178  -6.560  1.00 25.28           C  
ANISOU  711  CG  GLU A  86     2671   3509   3424   -108     12    991       C  
ATOM    712  CD  GLU A  86     -27.595   1.253  -6.798  1.00 28.57           C  
ANISOU  712  CD  GLU A  86     3044   3860   3952   -150     -3   1028       C  
ATOM    713  OE1 GLU A  86     -27.486   0.032  -6.548  1.00 29.88           O  
ANISOU  713  OE1 GLU A  86     3188   3974   4192   -169      5   1102       O  
ATOM    714  OE2 GLU A  86     -28.646   1.762  -7.242  1.00 28.72           O  
ANISOU  714  OE2 GLU A  86     3045   3875   3993   -166    -27    986       O  
ATOM    715  N   ASN A  87     -21.948   1.036  -5.872  1.00 22.07           N  
ANISOU  715  N   ASN A  87     2375   3107   2904    -31     63   1080       N  
ATOM    716  CA  ASN A  87     -20.773   0.466  -5.212  1.00 21.60           C  
ANISOU  716  CA  ASN A  87     2321   3072   2816    -11     93   1144       C  
ATOM    717  C   ASN A  87     -19.880   1.514  -4.550  1.00 22.30           C  
ANISOU  717  C   ASN A  87     2411   3254   2808     22    102   1127       C  
ATOM    718  O   ASN A  87     -19.357   1.288  -3.455  1.00 22.58           O  
ANISOU  718  O   ASN A  87     2418   3361   2801     39    135   1187       O  
ATOM    719  CB  ASN A  87     -19.930  -0.340  -6.204  1.00 22.96           C  
ANISOU  719  CB  ASN A  87     2551   3146   3028     -2     74   1138       C  
ATOM    720  CG  ASN A  87     -20.571  -1.658  -6.586  1.00 23.24           C  
ANISOU  720  CG  ASN A  87     2577   3083   3171    -28     62   1168       C  
ATOM    721  OD1 ASN A  87     -21.554  -2.085  -5.981  1.00 24.47           O  
ANISOU  721  OD1 ASN A  87     2673   3243   3381    -59     75   1219       O  
ATOM    722  ND2 ASN A  87     -20.002  -2.319  -7.586  1.00 22.94           N  
ANISOU  722  ND2 ASN A  87     2593   2955   3170    -11     33   1139       N  
ATOM    723  N   LEU A  88     -19.708   2.652  -5.222  1.00 18.33           N  
ANISOU  723  N   LEU A  88     1938   2748   2279     33     70   1046       N  
ATOM    724  CA  LEU A  88     -18.772   3.688  -4.790  1.00 18.46           C  
ANISOU  724  CA  LEU A  88     1957   2827   2231     61     62   1020       C  
ATOM    725  C   LEU A  88     -19.389   4.781  -3.925  1.00 21.58           C  
ANISOU  725  C   LEU A  88     2309   3310   2580     71     56    978       C  
ATOM    726  O   LEU A  88     -18.677   5.655  -3.427  1.00 22.85           O  
ANISOU  726  O   LEU A  88     2464   3522   2696     96     40    947       O  
ATOM    727  CB  LEU A  88     -18.126   4.348  -6.012  1.00 17.78           C  
ANISOU  727  CB  LEU A  88     1916   2684   2156     72     29    969       C  
ATOM    728  CG  LEU A  88     -17.274   3.436  -6.893  1.00 20.72           C  
ANISOU  728  CG  LEU A  88     2335   2986   2553     84     32   1001       C  
ATOM    729  CD1 LEU A  88     -16.762   4.196  -8.116  1.00 22.74           C  
ANISOU  729  CD1 LEU A  88     2624   3207   2811    108      4    960       C  
ATOM    730  CD2 LEU A  88     -16.118   2.860  -6.079  1.00 18.79           C  
ANISOU  730  CD2 LEU A  88     2087   2769   2283     98     58   1051       C  
ATOM    731  N   ARG A  89     -20.707   4.744  -3.761  1.00 18.76           N  
ANISOU  731  N   ARG A  89     1921   2969   2240     55     64    974       N  
ATOM    732  CA  ARG A  89     -21.409   5.805  -3.046  1.00 21.91           C  
ANISOU  732  CA  ARG A  89     2281   3450   2594     74     58    926       C  
ATOM    733  C   ARG A  89     -20.870   5.978  -1.630  1.00 23.61           C  
ANISOU  733  C   ARG A  89     2462   3779   2731    115     74    947       C  
ATOM    734  O   ARG A  89     -20.693   5.002  -0.896  1.00 23.16           O  
ANISOU  734  O   ARG A  89     2380   3762   2656    123    114   1031       O  
ATOM    735  CB  ARG A  89     -22.912   5.515  -3.016  1.00 24.22           C  
ANISOU  735  CB  ARG A  89     2537   3748   2918     53     74    942       C  
ATOM    736  CG  ARG A  89     -23.748   6.610  -2.372  1.00 26.83           C  
ANISOU  736  CG  ARG A  89     2828   4164   3201     79     68    890       C  
ATOM    737  CD  ARG A  89     -25.201   6.525  -2.835  1.00 27.19           C  
ANISOU  737  CD  ARG A  89     2850   4185   3298     51     71    891       C  
ATOM    738  NE  ARG A  89     -25.727   5.165  -2.753  1.00 27.61           N  
ANISOU  738  NE  ARG A  89     2874   4210   3406     21    104    987       N  
ATOM    739  CZ  ARG A  89     -26.698   4.691  -3.528  1.00 28.69           C  
ANISOU  739  CZ  ARG A  89     3003   4274   3625    -20     93    996       C  
ATOM    740  NH1 ARG A  89     -27.249   5.465  -4.455  1.00 25.66           N  
ANISOU  740  NH1 ARG A  89     2641   3847   3261    -32     57    917       N  
ATOM    741  NH2 ARG A  89     -27.116   3.440  -3.382  1.00 29.68           N  
ANISOU  741  NH2 ARG A  89     3094   4365   3819    -48    115   1088       N  
ATOM    742  N   GLY A  90     -20.584   7.223  -1.261  1.00 22.95           N  
ANISOU  742  N   GLY A  90     2373   3744   2604    146     39    868       N  
ATOM    743  CA  GLY A  90     -20.062   7.526   0.060  1.00 22.97           C  
ANISOU  743  CA  GLY A  90     2344   3860   2524    197     39    863       C  
ATOM    744  C   GLY A  90     -18.545   7.546   0.123  1.00 22.95           C  
ANISOU  744  C   GLY A  90     2364   3844   2512    207     18    867       C  
ATOM    745  O   GLY A  90     -17.963   7.953   1.129  1.00 24.98           O  
ANISOU  745  O   GLY A  90     2598   4188   2704    251      1    843       O  
ATOM    746  N   GLY A  91     -17.895   7.105  -0.949  1.00 19.16           N  
ANISOU  746  N   GLY A  91     1928   3261   2092    172     16    895       N  
ATOM    747  CA  GLY A  91     -16.444   7.144  -1.009  1.00 20.60           C  
ANISOU  747  CA  GLY A  91     2130   3425   2273    181     -2    907       C  
ATOM    748  C   GLY A  91     -15.964   8.578  -1.113  1.00 19.61           C  
ANISOU  748  C   GLY A  91     2000   3292   2160    195    -65    819       C  
ATOM    749  O   GLY A  91     -16.727   9.463  -1.484  1.00 17.66           O  
ANISOU  749  O   GLY A  91     1747   3024   1939    190    -92    753       O  
ATOM    750  N   PRO A  92     -14.692   8.818  -0.774  1.00 19.27           N  
ANISOU  750  N   PRO A  92     1953   3261   2109    212    -92    822       N  
ATOM    751  CA  PRO A  92     -14.105  10.160  -0.781  1.00 16.98           C  
ANISOU  751  CA  PRO A  92     1646   2954   1851    224   -162    746       C  
ATOM    752  C   PRO A  92     -14.176  10.817  -2.153  1.00 17.52           C  
ANISOU  752  C   PRO A  92     1733   2917   2006    196   -183    730       C  
ATOM    753  O   PRO A  92     -13.600  10.291  -3.109  1.00 19.19           O  
ANISOU  753  O   PRO A  92     1973   3065   2253    179   -161    793       O  
ATOM    754  CB  PRO A  92     -12.643   9.911  -0.381  1.00 15.42           C  
ANISOU  754  CB  PRO A  92     1444   2772   1644    237   -176    787       C  
ATOM    755  CG  PRO A  92     -12.633   8.570   0.254  1.00 23.02           C  
ANISOU  755  CG  PRO A  92     2411   3796   2539    246   -114    867       C  
ATOM    756  CD  PRO A  92     -13.705   7.784  -0.426  1.00 21.24           C  
ANISOU  756  CD  PRO A  92     2210   3530   2332    218    -61    906       C  
ATOM    757  N   ASN A  93     -14.891  11.938  -2.236  1.00 16.67           N  
ANISOU  757  N   ASN A  93     1606   2799   1929    199   -223    649       N  
ATOM    758  CA  ASN A  93     -14.937  12.779  -3.433  1.00 18.92           C  
ANISOU  758  CA  ASN A  93     1894   2995   2301    181   -249    633       C  
ATOM    759  C   ASN A  93     -15.542  12.083  -4.647  1.00 18.75           C  
ANISOU  759  C   ASN A  93     1909   2922   2294    157   -202    683       C  
ATOM    760  O   ASN A  93     -15.331  12.502  -5.781  1.00 21.46           O  
ANISOU  760  O   ASN A  93     2259   3198   2696    150   -211    699       O  
ATOM    761  CB  ASN A  93     -13.537  13.298  -3.764  1.00 18.80           C  
ANISOU  761  CB  ASN A  93     1864   2930   2349    182   -289    659       C  
ATOM    762  CG  ASN A  93     -12.994  14.208  -2.678  1.00 22.13           C  
ANISOU  762  CG  ASN A  93     2243   3385   2782    204   -359    588       C  
ATOM    763  OD1 ASN A  93     -13.758  14.906  -2.004  1.00 24.62           O  
ANISOU  763  OD1 ASN A  93     2536   3736   3081    223   -393    497       O  
ATOM    764  ND2 ASN A  93     -11.683  14.196  -2.490  1.00 19.50           N  
ANISOU  764  ND2 ASN A  93     1895   3042   2473    208   -385    625       N  
ATOM    765  N   ILE A  94     -16.301  11.021  -4.394  1.00 18.22           N  
ANISOU  765  N   ILE A  94     1859   2887   2176    150   -154    708       N  
ATOM    766  CA  ILE A  94     -17.088  10.366  -5.431  1.00 17.03           C  
ANISOU  766  CA  ILE A  94     1739   2690   2044    129   -122    734       C  
ATOM    767  C   ILE A  94     -18.449  11.048  -5.486  1.00 17.34           C  
ANISOU  767  C   ILE A  94     1760   2737   2092    123   -133    672       C  
ATOM    768  O   ILE A  94     -19.085  11.222  -4.446  1.00 16.72           O  
ANISOU  768  O   ILE A  94     1654   2726   1973    134   -132    640       O  
ATOM    769  CB  ILE A  94     -17.277   8.856  -5.140  1.00 17.93           C  
ANISOU  769  CB  ILE A  94     1871   2819   2123    119    -73    795       C  
ATOM    770  CG1 ILE A  94     -15.923   8.171  -4.896  1.00 20.72           C  
ANISOU  770  CG1 ILE A  94     2238   3174   2460    131    -60    857       C  
ATOM    771  CG2 ILE A  94     -18.074   8.175  -6.258  1.00 19.48           C  
ANISOU  771  CG2 ILE A  94     2096   2954   2352    100    -57    808       C  
ATOM    772  CD1 ILE A  94     -15.012   8.154  -6.103  1.00 16.81           C  
ANISOU  772  CD1 ILE A  94     1773   2611   2003    137    -66    887       C  
ATOM    773  N   ILE A  95     -18.885  11.456  -6.676  1.00 15.68           N  
ANISOU  773  N   ILE A  95     1561   2468   1927    113   -143    659       N  
ATOM    774  CA  ILE A  95     -20.190  12.094  -6.813  1.00 16.08           C  
ANISOU  774  CA  ILE A  95     1595   2525   1991    107   -152    605       C  
ATOM    775  C   ILE A  95     -21.254  11.142  -6.269  1.00 18.05           C  
ANISOU  775  C   ILE A  95     1841   2815   2204     93   -117    620       C  
ATOM    776  O   ILE A  95     -21.208   9.932  -6.507  1.00 16.29           O  
ANISOU  776  O   ILE A  95     1639   2572   1977     79    -88    674       O  
ATOM    777  CB  ILE A  95     -20.494  12.495  -8.288  1.00 16.96           C  
ANISOU  777  CB  ILE A  95     1720   2573   2152    103   -162    603       C  
ATOM    778  CG1 ILE A  95     -21.698  13.441  -8.357  1.00 17.95           C  
ANISOU  778  CG1 ILE A  95     1818   2705   2297    100   -180    544       C  
ATOM    779  CG2 ILE A  95     -20.702  11.277  -9.178  1.00 15.93           C  
ANISOU  779  CG2 ILE A  95     1627   2410   2016     93   -136    645       C  
ATOM    780  CD1 ILE A  95     -21.389  14.830  -7.851  1.00 19.81           C  
ANISOU  780  CD1 ILE A  95     2017   2945   2564    118   -221    493       C  
ATOM    781  N   THR A  96     -22.185  11.691  -5.495  1.00 19.73           N  
ANISOU  781  N   THR A  96     2019   3083   2394    103   -120    577       N  
ATOM    782  CA  THR A  96     -23.181  10.886  -4.805  1.00 17.50           C  
ANISOU  782  CA  THR A  96     1717   2855   2079     97    -83    606       C  
ATOM    783  C   THR A  96     -24.433  10.707  -5.648  1.00 18.74           C  
ANISOU  783  C   THR A  96     1873   2973   2274     70    -77    603       C  
ATOM    784  O   THR A  96     -25.084  11.683  -6.024  1.00 19.08           O  
ANISOU  784  O   THR A  96     1905   3010   2336     74    -99    549       O  
ATOM    785  CB  THR A  96     -23.580  11.515  -3.455  1.00 20.49           C  
ANISOU  785  CB  THR A  96     2052   3334   2399    135    -85    567       C  
ATOM    786  OG1 THR A  96     -22.447  11.527  -2.579  1.00 22.60           O  
ANISOU  786  OG1 THR A  96     2316   3647   2622    164    -94    569       O  
ATOM    787  CG2 THR A  96     -24.706  10.722  -2.804  1.00 24.32           C  
ANISOU  787  CG2 THR A  96     2503   3883   2853    135    -40    616       C  
ATOM    788  N   LEU A  97     -24.757   9.457  -5.953  1.00 18.54           N  
ANISOU  788  N   LEU A  97     1857   2918   2269     42    -52    661       N  
ATOM    789  CA  LEU A  97     -26.015   9.148  -6.617  1.00 16.81           C  
ANISOU  789  CA  LEU A  97     1628   2666   2092     15    -52    660       C  
ATOM    790  C   LEU A  97     -27.126   9.167  -5.578  1.00 19.01           C  
ANISOU  790  C   LEU A  97     1852   3024   2349     20    -27    677       C  
ATOM    791  O   LEU A  97     -27.155   8.331  -4.673  1.00 22.22           O  
ANISOU  791  O   LEU A  97     2230   3475   2736     22      8    742       O  
ATOM    792  CB  LEU A  97     -25.950   7.789  -7.314  1.00 16.65           C  
ANISOU  792  CB  LEU A  97     1634   2576   2118    -13    -48    708       C  
ATOM    793  CG  LEU A  97     -27.233   7.315  -8.002  1.00 17.40           C  
ANISOU  793  CG  LEU A  97     1714   2627   2270    -44    -59    705       C  
ATOM    794  CD1 LEU A  97     -27.576   8.212  -9.178  1.00 18.36           C  
ANISOU  794  CD1 LEU A  97     1857   2716   2405    -38    -94    638       C  
ATOM    795  CD2 LEU A  97     -27.104   5.870  -8.453  1.00 16.69           C  
ANISOU  795  CD2 LEU A  97     1642   2464   2234    -67    -63    748       C  
ATOM    796  N   ALA A  98     -28.029  10.129  -5.701  1.00 17.76           N  
ANISOU  796  N   ALA A  98     1671   2885   2190     27    -40    625       N  
ATOM    797  CA  ALA A  98     -29.099  10.296  -4.724  1.00 21.89           C  
ANISOU  797  CA  ALA A  98     2139   3495   2684     45    -14    638       C  
ATOM    798  C   ALA A  98     -30.342   9.474  -5.065  1.00 21.92           C  
ANISOU  798  C   ALA A  98     2111   3476   2742      7      1    691       C  
ATOM    799  O   ALA A  98     -31.043   9.004  -4.168  1.00 22.83           O  
ANISOU  799  O   ALA A  98     2171   3659   2843     15     38    753       O  
ATOM    800  CB  ALA A  98     -29.464  11.767  -4.598  1.00 25.10           C  
ANISOU  800  CB  ALA A  98     2533   3938   3065     79    -38    555       C  
ATOM    801  N   ASP A  99     -30.612   9.302  -6.355  1.00 19.78           N  
ANISOU  801  N   ASP A  99     1869   3114   2535    -29    -29    669       N  
ATOM    802  CA  ASP A  99     -31.839   8.633  -6.792  1.00 21.13           C  
ANISOU  802  CA  ASP A  99     2006   3251   2770    -67    -30    703       C  
ATOM    803  C   ASP A  99     -31.733   8.203  -8.246  1.00 21.80           C  
ANISOU  803  C   ASP A  99     2137   3230   2916    -96    -73    673       C  
ATOM    804  O   ASP A  99     -30.856   8.667  -8.984  1.00 18.90           O  
ANISOU  804  O   ASP A  99     1822   2829   2531    -80    -96    624       O  
ATOM    805  CB  ASP A  99     -33.053   9.556  -6.621  1.00 22.45           C  
ANISOU  805  CB  ASP A  99     2129   3472   2927    -55    -27    675       C  
ATOM    806  CG  ASP A  99     -34.344   8.798  -6.307  1.00 24.42           C  
ANISOU  806  CG  ASP A  99     2313   3739   3228    -82     -7    749       C  
ATOM    807  OD1 ASP A  99     -34.407   7.565  -6.513  1.00 22.89           O  
ANISOU  807  OD1 ASP A  99     2109   3485   3102   -121     -9    810       O  
ATOM    808  OD2 ASP A  99     -35.318   9.456  -5.877  1.00 26.37           O  
ANISOU  808  OD2 ASP A  99     2512   4052   3454    -63      9    746       O  
ATOM    809  N   ILE A 100     -32.632   7.309  -8.644  1.00 21.94           N  
ANISOU  809  N   ILE A 100     2129   3200   3008   -134    -86    704       N  
ATOM    810  CA  ILE A 100     -32.779   6.891 -10.031  1.00 20.68           C  
ANISOU  810  CA  ILE A 100     2004   2948   2906   -154   -137    662       C  
ATOM    811  C   ILE A 100     -34.261   6.884 -10.355  1.00 20.95           C  
ANISOU  811  C   ILE A 100     1989   2973   2999   -183   -158    660       C  
ATOM    812  O   ILE A 100     -35.037   6.220  -9.667  1.00 20.87           O  
ANISOU  812  O   ILE A 100     1918   2973   3040   -210   -139    730       O  
ATOM    813  CB  ILE A 100     -32.218   5.485 -10.299  1.00 21.53           C  
ANISOU  813  CB  ILE A 100     2134   2977   3068   -173   -153    694       C  
ATOM    814  CG1 ILE A 100     -30.811   5.322  -9.721  1.00 22.51           C  
ANISOU  814  CG1 ILE A 100     2293   3121   3139   -148   -123    720       C  
ATOM    815  CG2 ILE A 100     -32.232   5.184 -11.793  1.00 21.75           C  
ANISOU  815  CG2 ILE A 100     2207   2921   3134   -172   -215    627       C  
ATOM    816  CD1 ILE A 100     -30.362   3.872  -9.666  1.00 23.44           C  
ANISOU  816  CD1 ILE A 100     2418   3172   3318   -167   -126    772       C  
ATOM    817  N   VAL A 101     -34.656   7.627 -11.382  1.00 19.88           N  
ANISOU  817  N   VAL A 101     1872   2822   2859   -174   -193    591       N  
ATOM    818  CA  VAL A 101     -36.056   7.659 -11.786  1.00 20.22           C  
ANISOU  818  CA  VAL A 101     1869   2856   2958   -200   -218    585       C  
ATOM    819  C   VAL A 101     -36.199   7.406 -13.282  1.00 21.79           C  
ANISOU  819  C   VAL A 101     2105   2983   3193   -201   -284    519       C  
ATOM    820  O   VAL A 101     -35.241   7.538 -14.048  1.00 20.31           O  
ANISOU  820  O   VAL A 101     1979   2773   2967   -168   -302    474       O  
ATOM    821  CB  VAL A 101     -36.723   9.004 -11.437  1.00 22.15           C  
ANISOU  821  CB  VAL A 101     2083   3179   3155   -179   -194    566       C  
ATOM    822  CG1 VAL A 101     -36.631   9.276  -9.939  1.00 21.64           C  
ANISOU  822  CG1 VAL A 101     1980   3200   3042   -161   -135    619       C  
ATOM    823  CG2 VAL A 101     -36.089  10.138 -12.238  1.00 19.18           C  
ANISOU  823  CG2 VAL A 101     1757   2806   2726   -140   -210    494       C  
ATOM    824  N   LYS A 102     -37.405   7.036 -13.691  1.00 22.16           N  
ANISOU  824  N   LYS A 102     2108   3000   3313   -233   -321    516       N  
ATOM    825  CA  LYS A 102     -37.679   6.783 -15.093  1.00 22.94           C  
ANISOU  825  CA  LYS A 102     2233   3039   3443   -228   -393    445       C  
ATOM    826  C   LYS A 102     -38.224   8.057 -15.718  1.00 21.90           C  
ANISOU  826  C   LYS A 102     2099   2958   3263   -201   -398    398       C  
ATOM    827  O   LYS A 102     -39.322   8.494 -15.370  1.00 21.30           O  
ANISOU  827  O   LYS A 102     1966   2917   3211   -222   -387    419       O  
ATOM    828  CB  LYS A 102     -38.674   5.629 -15.236  1.00 29.39           C  
ANISOU  828  CB  LYS A 102     3001   3785   4382   -278   -445    463       C  
ATOM    829  CG  LYS A 102     -38.767   5.020 -16.624  1.00 38.90           C  
ANISOU  829  CG  LYS A 102     4239   4912   5628   -267   -535    378       C  
ATOM    830  CD  LYS A 102     -38.637   3.497 -16.561  1.00 46.18           C  
ANISOU  830  CD  LYS A 102     5154   5733   6659   -300   -580    393       C  
ATOM    831  CE  LYS A 102     -39.362   2.915 -15.346  1.00 50.82           C  
ANISOU  831  CE  LYS A 102     5654   6310   7346   -363   -547    504       C  
ATOM    832  NZ  LYS A 102     -39.288   1.424 -15.289  1.00 53.00           N  
ANISOU  832  NZ  LYS A 102     5910   6473   7755   -399   -594    530       N  
ATOM    833  N   ASP A 103     -37.469   8.673 -16.624  1.00 20.01           N  
ANISOU  833  N   ASP A 103     1916   2728   2961   -151   -411    345       N  
ATOM    834  CA  ASP A 103     -37.969   9.893 -17.250  1.00 20.20           C  
ANISOU  834  CA  ASP A 103     1929   2798   2947   -123   -414    311       C  
ATOM    835  C   ASP A 103     -39.101   9.549 -18.207  1.00 20.77           C  
ANISOU  835  C   ASP A 103     1977   2844   3069   -135   -478    270       C  
ATOM    836  O   ASP A 103     -38.940   8.702 -19.083  1.00 21.71           O  
ANISOU  836  O   ASP A 103     2126   2914   3210   -123   -537    226       O  
ATOM    837  CB  ASP A 103     -36.871  10.655 -17.990  1.00 21.64           C  
ANISOU  837  CB  ASP A 103     2164   3000   3058    -63   -407    284       C  
ATOM    838  CG  ASP A 103     -37.374  11.969 -18.564  1.00 24.14           C  
ANISOU  838  CG  ASP A 103     2460   3364   3348    -33   -405    265       C  
ATOM    839  OD1 ASP A 103     -37.471  12.955 -17.801  1.00 23.75           O  
ANISOU  839  OD1 ASP A 103     2384   3352   3287    -36   -362    287       O  
ATOM    840  OD2 ASP A 103     -37.679  12.019 -19.774  1.00 23.58           O  
ANISOU  840  OD2 ASP A 103     2398   3294   3269     -2   -447    227       O  
ATOM    841  N   PRO A 104     -40.251  10.216 -18.044  1.00 21.00           N  
ANISOU  841  N   PRO A 104     1952   2910   3117   -152   -471    280       N  
ATOM    842  CA  PRO A 104     -41.432   9.922 -18.866  1.00 24.88           C  
ANISOU  842  CA  PRO A 104     2409   3381   3662   -168   -534    246       C  
ATOM    843  C   PRO A 104     -41.252  10.275 -20.340  1.00 23.73           C  
ANISOU  843  C   PRO A 104     2302   3245   3470   -111   -584    175       C  
ATOM    844  O   PRO A 104     -41.889   9.653 -21.190  1.00 27.32           O  
ANISOU  844  O   PRO A 104     2748   3668   3965   -113   -658    127       O  
ATOM    845  CB  PRO A 104     -42.525  10.792 -18.233  1.00 25.01           C  
ANISOU  845  CB  PRO A 104     2360   3452   3689   -189   -497    283       C  
ATOM    846  CG  PRO A 104     -41.785  11.902 -17.566  1.00 25.14           C  
ANISOU  846  CG  PRO A 104     2396   3525   3632   -156   -428    302       C  
ATOM    847  CD  PRO A 104     -40.514  11.278 -17.058  1.00 21.76           C  
ANISOU  847  CD  PRO A 104     2014   3070   3184   -153   -407    319       C  
ATOM    848  N   VAL A 105     -40.409  11.256 -20.644  1.00 21.02           N  
ANISOU  848  N   VAL A 105     1994   2947   3047    -56   -548    173       N  
ATOM    849  CA  VAL A 105     -40.249  11.697 -22.024  1.00 20.96           C  
ANISOU  849  CA  VAL A 105     2010   2967   2985     10   -584    126       C  
ATOM    850  C   VAL A 105     -39.237  10.842 -22.775  1.00 22.70           C  
ANISOU  850  C   VAL A 105     2291   3160   3174     57   -621     88       C  
ATOM    851  O   VAL A 105     -39.525  10.344 -23.858  1.00 24.10           O  
ANISOU  851  O   VAL A 105     2480   3332   3344     94   -689     27       O  
ATOM    852  CB  VAL A 105     -39.823  13.176 -22.104  1.00 22.05           C  
ANISOU  852  CB  VAL A 105     2146   3165   3067     53   -530    154       C  
ATOM    853  CG1 VAL A 105     -39.571  13.573 -23.552  1.00 21.28           C  
ANISOU  853  CG1 VAL A 105     2067   3107   2913    132   -560    126       C  
ATOM    854  CG2 VAL A 105     -40.903  14.070 -21.491  1.00 23.16           C  
ANISOU  854  CG2 VAL A 105     2227   3336   3237     21   -501    178       C  
ATOM    855  N   SER A 106     -38.055  10.666 -22.194  1.00 20.55           N  
ANISOU  855  N   SER A 106     2055   2873   2879     61   -578    120       N  
ATOM    856  CA  SER A 106     -37.004   9.889 -22.840  1.00 22.36           C  
ANISOU  856  CA  SER A 106     2342   3081   3073    112   -605     92       C  
ATOM    857  C   SER A 106     -37.255   8.393 -22.733  1.00 26.74           C  
ANISOU  857  C   SER A 106     2906   3557   3696     76   -663     55       C  
ATOM    858  O   SER A 106     -36.718   7.615 -23.523  1.00 30.42           O  
ANISOU  858  O   SER A 106     3417   4000   4143    126   -712      3       O  
ATOM    859  CB  SER A 106     -35.646  10.213 -22.221  1.00 20.16           C  
ANISOU  859  CB  SER A 106     2093   2812   2754    127   -540    146       C  
ATOM    860  OG  SER A 106     -35.604   9.727 -20.897  1.00 21.98           O  
ANISOU  860  OG  SER A 106     2312   3005   3033     59   -509    184       O  
ATOM    861  N   ARG A 107     -38.068   8.007 -21.747  1.00 24.57           N  
ANISOU  861  N   ARG A 107     2585   3244   3506     -5   -657     87       N  
ATOM    862  CA  ARG A 107     -38.313   6.605 -21.393  1.00 25.68           C  
ANISOU  862  CA  ARG A 107     2717   3299   3742    -54   -702     79       C  
ATOM    863  C   ARG A 107     -37.025   5.887 -20.972  1.00 27.59           C  
ANISOU  863  C   ARG A 107     3007   3504   3971    -43   -677    101       C  
ATOM    864  O   ARG A 107     -36.933   4.661 -21.045  1.00 30.46           O  
ANISOU  864  O   ARG A 107     3381   3789   4403    -56   -728     77       O  
ATOM    865  CB  ARG A 107     -38.980   5.862 -22.554  1.00 30.75           C  
ANISOU  865  CB  ARG A 107     3360   3896   4427    -33   -808    -11       C  
ATOM    866  CG  ARG A 107     -40.068   6.674 -23.259  1.00 35.84           C  
ANISOU  866  CG  ARG A 107     3968   4593   5057    -21   -837    -44       C  
ATOM    867  CD  ARG A 107     -40.713   5.880 -24.376  1.00 40.13           C  
ANISOU  867  CD  ARG A 107     4511   5093   5644      3   -954   -143       C  
ATOM    868  NE  ARG A 107     -41.785   5.023 -23.887  1.00 43.52           N  
ANISOU  868  NE  ARG A 107     4878   5439   6219    -82  -1007   -136       N  
ATOM    869  CZ  ARG A 107     -42.025   3.799 -24.338  1.00 43.77           C  
ANISOU  869  CZ  ARG A 107     4909   5377   6345    -90  -1109   -205       C  
ATOM    870  NH1 ARG A 107     -41.253   3.278 -25.280  1.00 44.38           N  
ANISOU  870  NH1 ARG A 107     5052   5439   6371    -10  -1169   -298       N  
ATOM    871  NH2 ARG A 107     -43.026   3.094 -23.837  1.00 43.50           N  
ANISOU  871  NH2 ARG A 107     4802   5263   6462   -173  -1154   -180       N  
ATOM    872  N   THR A 108     -36.039   6.659 -20.519  1.00 23.36           N  
ANISOU  872  N   THR A 108     2495   3020   3358    -18   -604    147       N  
ATOM    873  CA  THR A 108     -34.754   6.113 -20.076  1.00 24.01           C  
ANISOU  873  CA  THR A 108     2621   3081   3420     -5   -573    176       C  
ATOM    874  C   THR A 108     -34.502   6.474 -18.613  1.00 26.51           C  
ANISOU  874  C   THR A 108     2910   3422   3740    -52   -496    258       C  
ATOM    875  O   THR A 108     -35.201   7.323 -18.067  1.00 25.61           O  
ANISOU  875  O   THR A 108     2752   3353   3625    -77   -464    284       O  
ATOM    876  CB  THR A 108     -33.597   6.648 -20.941  1.00 24.12           C  
ANISOU  876  CB  THR A 108     2690   3139   3335     81   -561    157       C  
ATOM    877  OG1 THR A 108     -33.497   8.069 -20.773  1.00 23.58           O  
ANISOU  877  OG1 THR A 108     2603   3142   3214     93   -508    193       O  
ATOM    878  CG2 THR A 108     -33.829   6.317 -22.412  1.00 26.88           C  
ANISOU  878  CG2 THR A 108     3066   3487   3660    147   -636     74       C  
ATOM    879  N   PRO A 109     -33.505   5.835 -17.972  1.00 28.84           N  
ANISOU  879  N   PRO A 109     2878   3768   4313   -169   -512    665       N  
ATOM    880  CA  PRO A 109     -33.218   6.230 -16.589  1.00 25.72           C  
ANISOU  880  CA  PRO A 109     2467   3383   3922   -135   -471    624       C  
ATOM    881  C   PRO A 109     -32.627   7.627 -16.485  1.00 24.48           C  
ANISOU  881  C   PRO A 109     2344   3134   3823    -31   -596    646       C  
ATOM    882  O   PRO A 109     -31.784   8.014 -17.296  1.00 24.34           O  
ANISOU  882  O   PRO A 109     2430   3014   3804    -22   -668    751       O  
ATOM    883  CB  PRO A 109     -32.197   5.180 -16.121  1.00 23.75           C  
ANISOU  883  CB  PRO A 109     2318   3116   3589   -223   -330    728       C  
ATOM    884  CG  PRO A 109     -32.365   4.033 -17.058  1.00 27.50           C  
ANISOU  884  CG  PRO A 109     2825   3604   4020   -317   -264    775       C  
ATOM    885  CD  PRO A 109     -32.739   4.639 -18.369  1.00 28.83           C  
ANISOU  885  CD  PRO A 109     2972   3741   4240   -280   -400    779       C  
ATOM    886  N   ALA A 110     -33.082   8.376 -15.489  1.00 21.72           N  
ANISOU  886  N   ALA A 110     1909   2824   3521     34   -615    536       N  
ATOM    887  CA  ALA A 110     -32.504   9.667 -15.161  1.00 18.73           C  
ANISOU  887  CA  ALA A 110     1561   2364   3193    122   -702    544       C  
ATOM    888  C   ALA A 110     -31.835   9.534 -13.806  1.00 19.83           C  
ANISOU  888  C   ALA A 110     1701   2540   3296     91   -593    541       C  
ATOM    889  O   ALA A 110     -32.482   9.183 -12.815  1.00 20.43           O  
ANISOU  889  O   ALA A 110     1681   2717   3366     66   -514    441       O  
ATOM    890  CB  ALA A 110     -33.568  10.756 -15.144  1.00 21.25           C  
ANISOU  890  CB  ALA A 110     1775   2693   3605    233   -823    413       C  
ATOM    891  N   LEU A 111     -30.528   9.768 -13.770  1.00 17.23           N  
ANISOU  891  N   LEU A 111     1480   2137   2931     85   -584    644       N  
ATOM    892  CA  LEU A 111     -29.773   9.657 -12.534  1.00 17.75           C  
ANISOU  892  CA  LEU A 111     1549   2245   2950     63   -487    649       C  
ATOM    893  C   LEU A 111     -29.809  10.989 -11.798  1.00 20.62           C  
ANISOU  893  C   LEU A 111     1855   2599   3380    138   -539    565       C  
ATOM    894  O   LEU A 111     -29.591  12.048 -12.398  1.00 21.55           O  
ANISOU  894  O   LEU A 111     2018   2622   3549    199   -644    574       O  
ATOM    895  CB  LEU A 111     -28.329   9.235 -12.820  1.00 18.17           C  
ANISOU  895  CB  LEU A 111     1732   2247   2926     22   -447    781       C  
ATOM    896  CG  LEU A 111     -28.127   7.980 -13.679  1.00 20.60           C  
ANISOU  896  CG  LEU A 111     2109   2542   3174    -51   -402    874       C  
ATOM    897  CD1 LEU A 111     -26.642   7.681 -13.860  1.00 19.73           C  
ANISOU  897  CD1 LEU A 111     2115   2393   2989    -82   -364    962       C  
ATOM    898  CD2 LEU A 111     -28.847   6.777 -13.081  1.00 21.37           C  
ANISOU  898  CD2 LEU A 111     2158   2732   3229   -108   -285    842       C  
ATOM    899  N   VAL A 112     -30.104  10.945 -10.504  1.00 18.71           N  
ANISOU  899  N   VAL A 112     1521   2453   3135    126   -462    479       N  
ATOM    900  CA  VAL A 112     -30.141  12.165  -9.707  1.00 17.57           C  
ANISOU  900  CA  VAL A 112     1307   2311   3057    185   -494    388       C  
ATOM    901  C   VAL A 112     -28.903  12.240  -8.832  1.00 20.02           C  
ANISOU  901  C   VAL A 112     1661   2645   3301    159   -412    436       C  
ATOM    902  O   VAL A 112     -28.632  11.322  -8.052  1.00 19.50           O  
ANISOU  902  O   VAL A 112     1590   2665   3154     99   -304    458       O  
ATOM    903  CB  VAL A 112     -31.392  12.232  -8.826  1.00 18.06           C  
ANISOU  903  CB  VAL A 112     1212   2478   3172    187   -472    229       C  
ATOM    904  CG1 VAL A 112     -31.494  13.594  -8.142  1.00 21.24           C  
ANISOU  904  CG1 VAL A 112     1537   2870   3662    254   -518    126       C  
ATOM    905  CG2 VAL A 112     -32.625  11.974  -9.666  1.00 17.86           C  
ANISOU  905  CG2 VAL A 112     1132   2462   3192    206   -539    166       C  
ATOM    906  N   PHE A 113     -28.151  13.327  -8.963  1.00 19.71           N  
ANISOU  906  N   PHE A 113     1671   2532   3287    202   -462    448       N  
ATOM    907  CA  PHE A 113     -26.913  13.487  -8.195  1.00 18.57           C  
ANISOU  907  CA  PHE A 113     1559   2423   3073    179   -386    480       C  
ATOM    908  C   PHE A 113     -26.979  14.661  -7.227  1.00 22.31           C  
ANISOU  908  C   PHE A 113     1946   2926   3606    212   -378    371       C  
ATOM    909  O   PHE A 113     -27.787  15.580  -7.392  1.00 21.20           O  
ANISOU  909  O   PHE A 113     1751   2733   3570    269   -456    285       O  
ATOM    910  CB  PHE A 113     -25.716  13.688  -9.125  1.00 19.09           C  
ANISOU  910  CB  PHE A 113     1768   2394   3090    173   -419    580       C  
ATOM    911  CG  PHE A 113     -25.442  12.526 -10.033  1.00 19.86           C  
ANISOU  911  CG  PHE A 113     1953   2469   3125    129   -414    689       C  
ATOM    912  CD1 PHE A 113     -24.740  11.422  -9.572  1.00 19.49           C  
ANISOU  912  CD1 PHE A 113     1931   2497   2978     85   -318    751       C  
ATOM    913  CD2 PHE A 113     -25.860  12.548 -11.352  1.00 22.83           C  
ANISOU  913  CD2 PHE A 113     2387   2747   3540    136   -506    728       C  
ATOM    914  CE1 PHE A 113     -24.471  10.354 -10.409  1.00 19.71           C  
ANISOU  914  CE1 PHE A 113     2038   2496   2954     45   -309    845       C  
ATOM    915  CE2 PHE A 113     -25.603  11.482 -12.193  1.00 20.47           C  
ANISOU  915  CE2 PHE A 113     2159   2432   3187     84   -493    822       C  
ATOM    916  CZ  PHE A 113     -24.903  10.386 -11.724  1.00 18.03           C  
ANISOU  916  CZ  PHE A 113     1873   2192   2787     38   -392    878       C  
ATOM    917  N   GLU A 114     -26.111  14.625  -6.220  1.00 22.74           N  
ANISOU  917  N   GLU A 114     1983   3066   3590    180   -285    370       N  
ATOM    918  CA  GLU A 114     -25.867  15.787  -5.381  1.00 23.41           C  
ANISOU  918  CA  GLU A 114     2001   3177   3716    198   -264    278       C  
ATOM    919  C   GLU A 114     -25.447  16.960  -6.262  1.00 27.41           C  
ANISOU  919  C   GLU A 114     2600   3542   4271    241   -343    283       C  
ATOM    920  O   GLU A 114     -24.802  16.776  -7.300  1.00 26.87           O  
ANISOU  920  O   GLU A 114     2663   3389   4158    233   -382    377       O  
ATOM    921  CB  GLU A 114     -24.782  15.486  -4.341  1.00 23.25           C  
ANISOU  921  CB  GLU A 114     1968   3277   3588    154   -152    295       C  
ATOM    922  CG  GLU A 114     -23.422  15.202  -4.959  1.00 23.86           C  
ANISOU  922  CG  GLU A 114     2177   3325   3564    142   -141    399       C  
ATOM    923  CD  GLU A 114     -22.320  15.006  -3.931  1.00 28.43           C  
ANISOU  923  CD  GLU A 114     2733   4038   4032    117    -40    399       C  
ATOM    924  OE1 GLU A 114     -22.217  15.821  -2.992  1.00 32.15           O  
ANISOU  924  OE1 GLU A 114     3115   4581   4522    113      7    308       O  
ATOM    925  OE2 GLU A 114     -21.550  14.038  -4.072  1.00 24.74           O  
ANISOU  925  OE2 GLU A 114     2334   3608   3459    105     -9    486       O  
ATOM    926  N   HIS A 115     -25.816  18.166  -5.857  1.00 28.87           N  
ANISOU  926  N   HIS A 115     2724   3698   4548    280   -365    179       N  
ATOM    927  CA  HIS A 115     -25.455  19.350  -6.619  1.00 33.49           C  
ANISOU  927  CA  HIS A 115     3414   4135   5175    319   -433    178       C  
ATOM    928  C   HIS A 115     -24.087  19.871  -6.183  1.00 33.23           C  
ANISOU  928  C   HIS A 115     3433   4130   5062    272   -346    177       C  
ATOM    929  O   HIS A 115     -23.832  20.015  -4.994  1.00 33.31           O  
ANISOU  929  O   HIS A 115     3338   4264   5055    244   -251    108       O  
ATOM    930  CB  HIS A 115     -26.516  20.437  -6.449  1.00 37.05           C  
ANISOU  930  CB  HIS A 115     3788   4524   5764    395   -501     62       C  
ATOM    931  CG  HIS A 115     -26.176  21.724  -7.130  1.00 40.87           C  
ANISOU  931  CG  HIS A 115     4398   4842   6291    440   -563     56       C  
ATOM    932  ND1 HIS A 115     -25.611  22.793  -6.466  1.00 42.52           N  
ANISOU  932  ND1 HIS A 115     4602   5041   6513    428   -499    -18       N  
ATOM    933  CD2 HIS A 115     -26.317  22.117  -8.418  1.00 42.43           C  
ANISOU  933  CD2 HIS A 115     4739   4872   6510    489   -679    116       C  
ATOM    934  CE1 HIS A 115     -25.419  23.785  -7.314  1.00 43.51           C  
ANISOU  934  CE1 HIS A 115     4875   4991   6667    467   -568     -4       C  
ATOM    935  NE2 HIS A 115     -25.839  23.401  -8.507  1.00 44.30           N  
ANISOU  935  NE2 HIS A 115     5071   4990   6770    507   -683     81       N  
ATOM    936  N   VAL A 116     -23.211  20.139  -7.145  1.00 35.86           N  
ANISOU  936  N   VAL A 116     3925   4360   5342    253   -373    243       N  
ATOM    937  CA  VAL A 116     -21.927  20.776  -6.857  1.00 39.70           C  
ANISOU  937  CA  VAL A 116     4468   4865   5750    202   -293    217       C  
ATOM    938  C   VAL A 116     -21.857  22.146  -7.527  1.00 42.92           C  
ANISOU  938  C   VAL A 116     4997   5101   6210    221   -346    181       C  
ATOM    939  O   VAL A 116     -21.948  22.252  -8.748  1.00 43.18           O  
ANISOU  939  O   VAL A 116     5170   4987   6250    234   -440    247       O  
ATOM    940  CB  VAL A 116     -20.731  19.919  -7.329  1.00 39.71           C  
ANISOU  940  CB  VAL A 116     4563   4911   5615    141   -256    304       C  
ATOM    941  CG1 VAL A 116     -19.416  20.611  -6.989  1.00 41.06           C  
ANISOU  941  CG1 VAL A 116     4778   5127   5698     85   -167    248       C  
ATOM    942  CG2 VAL A 116     -20.776  18.539  -6.694  1.00 38.14           C  
ANISOU  942  CG2 VAL A 116     4271   4863   5357    132   -206    350       C  
ATOM    943  N   ASN A 117     -21.705  23.191  -6.720  1.00 47.46           N  
ANISOU  943  N   ASN A 117     5523   5692   6819    219   -281     76       N  
ATOM    944  CA  ASN A 117     -21.617  24.558  -7.230  1.00 51.66           C  
ANISOU  944  CA  ASN A 117     6180   6052   7397    235   -312     32       C  
ATOM    945  C   ASN A 117     -20.283  24.814  -7.927  1.00 51.10           C  
ANISOU  945  C   ASN A 117     6287   5925   7203    149   -272     64       C  
ATOM    946  O   ASN A 117     -19.344  25.326  -7.321  1.00 52.37           O  
ANISOU  946  O   ASN A 117     6444   6158   7296     83   -156    -10       O  
ATOM    947  CB  ASN A 117     -21.820  25.559  -6.092  1.00 55.18           C  
ANISOU  947  CB  ASN A 117     6512   6541   7914    246   -235   -101       C  
ATOM    948  CG  ASN A 117     -21.998  26.976  -6.587  1.00 59.37           C  
ANISOU  948  CG  ASN A 117     7171   6871   8517    284   -278   -150       C  
ATOM    949  OD1 ASN A 117     -22.505  27.201  -7.685  1.00 60.92           O  
ANISOU  949  OD1 ASN A 117     7502   6890   8755    344   -405    -90       O  
ATOM    950  ND2 ASN A 117     -21.581  27.944  -5.776  1.00 61.65           N  
ANISOU  950  ND2 ASN A 117     7424   7184   8815    249   -170   -260       N  
ATOM    951  N   ASN A 118     -20.220  24.469  -9.208  1.00 50.47           N  
ANISOU  951  N   ASN A 118     6358   5727   7093    142   -365    162       N  
ATOM    952  CA  ASN A 118     -18.971  24.454  -9.970  1.00 51.67           C  
ANISOU  952  CA  ASN A 118     6672   5844   7117     44   -333    194       C  
ATOM    953  C   ASN A 118     -18.616  25.773 -10.657  1.00 52.28           C  
ANISOU  953  C   ASN A 118     6948   5731   7185     10   -347    159       C  
ATOM    954  O   ASN A 118     -19.498  26.546 -11.033  1.00 51.92           O  
ANISOU  954  O   ASN A 118     6967   5522   7240     86   -437    161       O  
ATOM    955  CB  ASN A 118     -19.054  23.357 -11.032  1.00 52.83           C  
ANISOU  955  CB  ASN A 118     6882   5962   7229     34   -421    314       C  
ATOM    956  CG  ASN A 118     -17.720  23.064 -11.694  1.00 55.10           C  
ANISOU  956  CG  ASN A 118     7296   6262   7379    -79   -379    337       C  
ATOM    957  OD1 ASN A 118     -16.661  23.161 -11.074  1.00 56.05           O  
ANISOU  957  OD1 ASN A 118     7391   6501   7406   -145   -264    267       O  
ATOM    958  ND2 ASN A 118     -17.769  22.718 -12.976  1.00 56.03           N  
ANISOU  958  ND2 ASN A 118     7546   6264   7479   -106   -472    425       N  
ATOM    959  N   THR A 119     -17.318  26.018 -10.827  1.00 52.08           N  
ANISOU  959  N   THR A 119     7028   5728   7032   -106   -257    121       N  
ATOM    960  CA  THR A 119     -16.852  27.042 -11.762  1.00 54.16           C  
ANISOU  960  CA  THR A 119     7529   5799   7251   -172   -272    107       C  
ATOM    961  C   THR A 119     -16.134  26.377 -12.934  1.00 52.96           C  
ANISOU  961  C   THR A 119     7517   5616   6991   -264   -312    182       C  
ATOM    962  O   THR A 119     -15.406  25.399 -12.746  1.00 51.52           O  
ANISOU  962  O   THR A 119     7253   5599   6723   -317   -258    187       O  
ATOM    963  CB  THR A 119     -15.908  28.069 -11.098  1.00 57.03           C  
ANISOU  963  CB  THR A 119     7928   6197   7545   -259   -120    -28       C  
ATOM    964  OG1 THR A 119     -15.102  27.423 -10.105  1.00 56.91           O  
ANISOU  964  OG1 THR A 119     7741   6434   7448   -306      4    -91       O  
ATOM    965  CG2 THR A 119     -16.708  29.188 -10.444  1.00 58.57           C  
ANISOU  965  CG2 THR A 119     8089   6303   7861   -179   -110    -97       C  
ATOM    966  N   ASP A 120     -16.356  26.910 -14.136  1.00 54.41           N  
ANISOU  966  N   ASP A 120     7913   5584   7176   -280   -410    237       N  
ATOM    967  CA  ASP A 120     -15.761  26.391 -15.369  1.00 55.59           C  
ANISOU  967  CA  ASP A 120     8154   5746   7222   -362   -436    290       C  
ATOM    968  C   ASP A 120     -14.255  26.192 -15.196  1.00 52.21           C  
ANISOU  968  C   ASP A 120     7770   5420   6648   -517   -317    212       C  
ATOM    969  O   ASP A 120     -13.562  27.074 -14.687  1.00 53.42           O  
ANISOU  969  O   ASP A 120     7996   5557   6744   -597   -210    101       O  
ATOM    970  CB  ASP A 120     -16.054  27.345 -16.534  1.00 60.71           C  
ANISOU  970  CB  ASP A 120     8914   6300   7854   -341   -477    297       C  
ATOM    971  CG  ASP A 120     -15.582  26.806 -17.878  1.00 65.59           C  
ANISOU  971  CG  ASP A 120     9559   6990   8372   -401   -500    330       C  
ATOM    972  OD1 ASP A 120     -15.065  25.670 -17.935  1.00 66.60           O  
ANISOU  972  OD1 ASP A 120     9610   7242   8452   -445   -483    343       O  
ATOM    973  OD2 ASP A 120     -15.733  27.528 -18.887  1.00 68.11           O  
ANISOU  973  OD2 ASP A 120     9979   7237   8661   -402   -537    337       O  
ATOM    974  N   PHE A 121     -13.756  25.029 -15.608  1.00 49.11           N  
ANISOU  974  N   PHE A 121     7316   5154   6190   -556   -323    252       N  
ATOM    975  CA  PHE A 121     -12.369  24.670 -15.335  1.00 49.73           C  
ANISOU  975  CA  PHE A 121     7401   5363   6132   -688   -215    168       C  
ATOM    976  C   PHE A 121     -11.391  25.589 -16.062  1.00 51.50           C  
ANISOU  976  C   PHE A 121     7743   5590   6235   -775   -153     75       C  
ATOM    977  O   PHE A 121     -10.323  25.895 -15.534  1.00 50.87           O  
ANISOU  977  O   PHE A 121     7675   5604   6049   -876    -30    -45       O  
ATOM    978  CB  PHE A 121     -12.103  23.196 -15.695  1.00 47.70           C  
ANISOU  978  CB  PHE A 121     7049   5233   5842   -688   -248    234       C  
ATOM    979  CG  PHE A 121     -11.885  22.940 -17.164  1.00 48.04           C  
ANISOU  979  CG  PHE A 121     7122   5292   5837   -687   -302    250       C  
ATOM    980  CD1 PHE A 121     -12.949  22.619 -17.995  1.00 49.92           C  
ANISOU  980  CD1 PHE A 121     7321   5486   6159   -595   -398    332       C  
ATOM    981  CD2 PHE A 121     -10.612  22.995 -17.711  1.00 47.79           C  
ANISOU  981  CD2 PHE A 121     7150   5341   5667   -786   -246    169       C  
ATOM    982  CE1 PHE A 121     -12.745  22.372 -19.348  1.00 49.30           C  
ANISOU  982  CE1 PHE A 121     7269   5432   6032   -615   -435    331       C  
ATOM    983  CE2 PHE A 121     -10.405  22.754 -19.057  1.00 48.20           C  
ANISOU  983  CE2 PHE A 121     7233   5409   5673   -792   -295    183       C  
ATOM    984  CZ  PHE A 121     -11.471  22.442 -19.876  1.00 47.86           C  
ANISOU  984  CZ  PHE A 121     7153   5312   5718   -713   -390    262       C  
ATOM    985  N   LYS A 122     -11.760  26.042 -17.258  1.00 53.67           N  
ANISOU  985  N   LYS A 122     8092   5784   6516   -738   -229    123       N  
ATOM    986  CA  LYS A 122     -10.881  26.913 -18.040  1.00 57.98           C  
ANISOU  986  CA  LYS A 122     8762   6328   6939   -821   -180     59       C  
ATOM    987  C   LYS A 122     -10.608  28.223 -17.314  1.00 58.95           C  
ANISOU  987  C   LYS A 122     8964   6391   7043   -861    -80    -33       C  
ATOM    988  O   LYS A 122      -9.495  28.748 -17.359  1.00 58.24           O  
ANISOU  988  O   LYS A 122     8931   6373   6824   -961     28   -121       O  
ATOM    989  CB  LYS A 122     -11.470  27.199 -19.420  1.00 61.08           C  
ANISOU  989  CB  LYS A 122     9226   6636   7345   -780   -283    129       C  
ATOM    990  CG  LYS A 122     -10.811  26.386 -20.533  1.00 63.94           C  
ANISOU  990  CG  LYS A 122     9582   7103   7611   -830   -307    140       C  
ATOM    991  CD  LYS A 122      -9.289  26.517 -20.470  1.00 65.95           C  
ANISOU  991  CD  LYS A 122     9881   7469   7708   -945   -189     50       C  
ATOM    992  CE  LYS A 122      -8.587  25.497 -21.354  1.00 64.71           C  
ANISOU  992  CE  LYS A 122     9686   7431   7469   -980   -203     61       C  
ATOM    993  NZ  LYS A 122      -7.370  26.068 -22.001  1.00 66.06           N  
ANISOU  993  NZ  LYS A 122     9955   7657   7490  -1080   -115     12       N  
ATOM    994  N   GLN A 123     -11.628  28.749 -16.647  1.00 58.90           N  
ANISOU  994  N   GLN A 123     8950   6262   7167   -779   -109    -14       N  
ATOM    995  CA  GLN A 123     -11.453  29.939 -15.833  1.00 60.03           C  
ANISOU  995  CA  GLN A 123     9148   6351   7310   -808     -6   -114       C  
ATOM    996  C   GLN A 123     -10.734  29.580 -14.535  1.00 56.54           C  
ANISOU  996  C   GLN A 123     8602   6058   6823   -882    133   -231       C  
ATOM    997  O   GLN A 123      -9.829  30.293 -14.101  1.00 56.35           O  
ANISOU  997  O   GLN A 123     8593   6116   6702   -969    274   -353       O  
ATOM    998  CB  GLN A 123     -12.804  30.594 -15.541  1.00 64.62           C  
ANISOU  998  CB  GLN A 123     9743   6757   8055   -682    -83    -66       C  
ATOM    999  CG  GLN A 123     -12.968  31.060 -14.106  1.00 68.71           C  
ANISOU  999  CG  GLN A 123    10211   7259   8639   -675     16   -167       C  
ATOM   1000  CD  GLN A 123     -14.383  31.502 -13.801  1.00 73.71           C  
ANISOU 1000  CD  GLN A 123    10830   7728   9449   -523    -81   -117       C  
ATOM   1001  OE1 GLN A 123     -15.341  31.013 -14.405  1.00 75.50           O  
ANISOU 1001  OE1 GLN A 123    11022   7904   9760   -410   -227      2       O  
ATOM   1002  NE2 GLN A 123     -14.526  32.422 -12.853  1.00 74.72           N  
ANISOU 1002  NE2 GLN A 123    10963   7795   9630   -513     11   -223       N  
ATOM   1003  N   LEU A 124     -11.130  28.460 -13.933  1.00 52.44           N  
ANISOU 1003  N   LEU A 124     7963   5595   6365   -850    100   -196       N  
ATOM   1004  CA  LEU A 124     -10.564  28.035 -12.660  1.00 47.34           C  
ANISOU 1004  CA  LEU A 124     7110   5198   5680   -853    224   -294       C  
ATOM   1005  C   LEU A 124      -9.085  27.697 -12.782  1.00 43.77           C  
ANISOU 1005  C   LEU A 124     6670   4912   5050   -999    328   -406       C  
ATOM   1006  O   LEU A 124      -8.280  28.124 -11.956  1.00 40.14           O  
ANISOU 1006  O   LEU A 124     6138   4609   4505  -1058    474   -555       O  
ATOM   1007  CB  LEU A 124     -11.325  26.830 -12.105  1.00 46.13           C  
ANISOU 1007  CB  LEU A 124     6736   5171   5621   -710    150   -189       C  
ATOM   1008  CG  LEU A 124     -10.897  26.389 -10.703  1.00 47.52           C  
ANISOU 1008  CG  LEU A 124     6676   5617   5765   -677    263   -269       C  
ATOM   1009  CD1 LEU A 124     -11.624  27.198  -9.646  1.00 49.65           C  
ANISOU 1009  CD1 LEU A 124     6841   5885   6137   -603    311   -317       C  
ATOM   1010  CD2 LEU A 124     -11.142  24.903 -10.504  1.00 47.28           C  
ANISOU 1010  CD2 LEU A 124     6492   5722   5751   -593    201   -167       C  
ATOM   1011  N   TYR A 125      -8.727  26.947 -13.824  1.00 43.77           N  
ANISOU 1011  N   TYR A 125     6721   4914   4997  -1025    252   -330       N  
ATOM   1012  CA  TYR A 125      -7.346  26.488 -14.023  1.00 46.27           C  
ANISOU 1012  CA  TYR A 125     6972   5433   5175  -1091    333   -386       C  
ATOM   1013  C   TYR A 125      -6.371  27.629 -14.266  1.00 51.44           C  
ANISOU 1013  C   TYR A 125     7674   6115   5757  -1160    449   -446       C  
ATOM   1014  O   TYR A 125      -5.167  27.422 -14.423  1.00 52.80           O  
ANISOU 1014  O   TYR A 125     7760   6420   5882  -1215    519   -470       O  
ATOM   1015  CB  TYR A 125      -7.266  25.512 -15.199  1.00 44.54           C  
ANISOU 1015  CB  TYR A 125     6783   5200   4940  -1078    228   -274       C  
ATOM   1016  CG  TYR A 125      -7.702  24.107 -14.871  1.00 42.04           C  
ANISOU 1016  CG  TYR A 125     6366   4940   4669  -1040    152   -219       C  
ATOM   1017  CD1 TYR A 125      -8.522  23.846 -13.782  1.00 42.32           C  
ANISOU 1017  CD1 TYR A 125     6264   5015   4800   -938    144   -190       C  
ATOM   1018  CD2 TYR A 125      -7.271  23.035 -15.639  1.00 41.27           C  
ANISOU 1018  CD2 TYR A 125     6239   4908   4533  -1038    104   -158       C  
ATOM   1019  CE1 TYR A 125      -8.916  22.560 -13.478  1.00 40.77           C  
ANISOU 1019  CE1 TYR A 125     5914   4923   4653   -829     89    -88       C  
ATOM   1020  CE2 TYR A 125      -7.657  21.746 -15.343  1.00 40.14           C  
ANISOU 1020  CE2 TYR A 125     6006   4813   4431  -1009     38    -96       C  
ATOM   1021  CZ  TYR A 125      -8.478  21.514 -14.262  1.00 40.38           C  
ANISOU 1021  CZ  TYR A 125     5884   4904   4556   -868     38    -41       C  
ATOM   1022  OH  TYR A 125      -8.860  20.229 -13.969  1.00 40.82           O  
ANISOU 1022  OH  TYR A 125     5803   5050   4656   -763     -7     59       O  
ATOM   1023  N   GLN A 126      -6.902  28.836 -14.291  1.00 52.46           N  
ANISOU 1023  N   GLN A 126     7923   6095   5913  -1156    458   -459       N  
ATOM   1024  CA  GLN A 126      -6.144  29.992 -14.696  1.00 55.27           C  
ANISOU 1024  CA  GLN A 126     8368   6436   6197  -1231    551   -493       C  
ATOM   1025  C   GLN A 126      -5.898  30.905 -13.498  1.00 53.23           C  
ANISOU 1025  C   GLN A 126     8036   6236   5954  -1262    691   -606       C  
ATOM   1026  O   GLN A 126      -5.087  31.830 -13.556  1.00 53.80           O  
ANISOU 1026  O   GLN A 126     8134   6331   5977  -1345    797   -647       O  
ATOM   1027  CB  GLN A 126      -6.905  30.686 -15.812  1.00 60.45           C  
ANISOU 1027  CB  GLN A 126     9221   6880   6866  -1196    442   -411       C  
ATOM   1028  CG  GLN A 126      -6.258  31.857 -16.451  1.00 66.19           C  
ANISOU 1028  CG  GLN A 126    10084   7565   7499  -1275    517   -431       C  
ATOM   1029  CD  GLN A 126      -6.972  32.206 -17.722  1.00 71.20           C  
ANISOU 1029  CD  GLN A 126    10885   8028   8139  -1231    380   -339       C  
ATOM   1030  OE1 GLN A 126      -7.079  31.382 -18.629  1.00 71.16           O  
ANISOU 1030  OE1 GLN A 126    10878   8036   8122  -1208    278   -264       O  
ATOM   1031  NE2 GLN A 126      -7.550  33.386 -17.763  1.00 75.39           N  
ANISOU 1031  NE2 GLN A 126    11542   8400   8704  -1208    371   -342       N  
ATOM   1032  N   THR A 127      -6.587  30.613 -12.399  1.00 50.89           N  
ANISOU 1032  N   THR A 127     7632   5974   5731  -1202    694   -655       N  
ATOM   1033  CA  THR A 127      -6.401  31.353 -11.157  1.00 51.46           C  
ANISOU 1033  CA  THR A 127     7586   6139   5826  -1218    824   -766       C  
ATOM   1034  C   THR A 127      -5.868  30.447 -10.050  1.00 47.92           C  
ANISOU 1034  C   THR A 127     6868   5945   5394  -1190    855   -817       C  
ATOM   1035  O   THR A 127      -5.567  30.913  -8.950  1.00 48.85           O  
ANISOU 1035  O   THR A 127     6833   6180   5549  -1188    928   -892       O  
ATOM   1036  CB  THR A 127      -7.711  31.994 -10.677  1.00 53.90           C  
ANISOU 1036  CB  THR A 127     7966   6276   6239  -1148    804   -792       C  
ATOM   1037  OG1 THR A 127      -8.453  31.045  -9.900  1.00 55.07           O  
ANISOU 1037  OG1 THR A 127     7981   6485   6459  -1076    765   -813       O  
ATOM   1038  CG2 THR A 127      -8.550  32.456 -11.861  1.00 54.47           C  
ANISOU 1038  CG2 THR A 127     8262   6066   6367  -1102    664   -677       C  
ATOM   1039  N   LEU A 128      -5.764  29.153 -10.342  1.00 42.14           N  
ANISOU 1039  N   LEU A 128     6074   5291   4645  -1150    770   -761       N  
ATOM   1040  CA  LEU A 128      -5.270  28.191  -9.361  1.00 38.24           C  
ANISOU 1040  CA  LEU A 128     5332   5024   4173  -1075    751   -778       C  
ATOM   1041  C   LEU A 128      -3.835  28.507  -8.967  1.00 31.60           C  
ANISOU 1041  C   LEU A 128     4360   4300   3347  -1109    772   -827       C  
ATOM   1042  O   LEU A 128      -2.961  28.653  -9.822  1.00 29.32           O  
ANISOU 1042  O   LEU A 128     4126   3974   3038  -1186    775   -817       O  
ATOM   1043  CB  LEU A 128      -5.355  26.761  -9.900  1.00 40.79           C  
ANISOU 1043  CB  LEU A 128     5641   5388   4471  -1024    654   -699       C  
ATOM   1044  CG  LEU A 128      -6.731  26.092  -9.965  1.00 41.44           C  
ANISOU 1044  CG  LEU A 128     5795   5413   4538   -970    603   -649       C  
ATOM   1045  CD1 LEU A 128      -6.575  24.604 -10.234  1.00 40.36           C  
ANISOU 1045  CD1 LEU A 128     5583   5377   4374   -914    521   -564       C  
ATOM   1046  CD2 LEU A 128      -7.531  26.332  -8.690  1.00 41.29           C  
ANISOU 1046  CD2 LEU A 128     5629   5471   4588   -874    654   -666       C  
ATOM   1047  N   THR A 129      -3.608  28.629  -7.664  1.00 29.07           N  
ANISOU 1047  N   THR A 129     3875   4111   3061  -1051    780   -876       N  
ATOM   1048  CA  THR A 129      -2.271  28.840  -7.131  1.00 27.92           C  
ANISOU 1048  CA  THR A 129     3611   4077   2922  -1093    783   -937       C  
ATOM   1049  C   THR A 129      -1.525  27.514  -7.079  1.00 28.03           C  
ANISOU 1049  C   THR A 129     3507   4225   2918  -1061    711   -928       C  
ATOM   1050  O   THR A 129      -2.118  26.456  -7.298  1.00 29.16           O  
ANISOU 1050  O   THR A 129     3660   4366   3054   -944    644   -840       O  
ATOM   1051  CB  THR A 129      -2.311  29.448  -5.717  1.00 27.71           C  
ANISOU 1051  CB  THR A 129     3464   4140   2923  -1088    816  -1011       C  
ATOM   1052  OG1 THR A 129      -2.954  28.529  -4.832  1.00 26.39           O  
ANISOU 1052  OG1 THR A 129     3195   4066   2764   -941    753   -959       O  
ATOM   1053  CG2 THR A 129      -3.074  30.770  -5.708  1.00 27.80           C  
ANISOU 1053  CG2 THR A 129     3582   4019   2960  -1111    896  -1026       C  
ATOM   1054  N   ASP A 130      -0.227  27.574  -6.792  1.00 25.22           N  
ANISOU 1054  N   ASP A 130     3038   3989   2554  -1165    726  -1022       N  
ATOM   1055  CA  ASP A 130       0.565  26.367  -6.577  1.00 26.49           C  
ANISOU 1055  CA  ASP A 130     3068   4302   2697  -1123    656  -1030       C  
ATOM   1056  C   ASP A 130      -0.077  25.504  -5.491  1.00 26.11           C  
ANISOU 1056  C   ASP A 130     2932   4345   2642   -961    587   -980       C  
ATOM   1057  O   ASP A 130      -0.210  24.285  -5.643  1.00 25.89           O  
ANISOU 1057  O   ASP A 130     2885   4352   2601   -860    523   -907       O  
ATOM   1058  CB  ASP A 130       2.004  26.726  -6.195  1.00 29.73           C  
ANISOU 1058  CB  ASP A 130     3345   4854   3097  -1254    683  -1161       C  
ATOM   1059  CG  ASP A 130       2.828  25.511  -5.803  1.00 33.25           C  
ANISOU 1059  CG  ASP A 130     3637   5480   3517  -1190    604  -1180       C  
ATOM   1060  OD1 ASP A 130       2.621  24.430  -6.390  1.00 30.59           O  
ANISOU 1060  OD1 ASP A 130     3328   5121   3173  -1102    553  -1097       O  
ATOM   1061  OD2 ASP A 130       3.692  25.638  -4.908  1.00 35.50           O  
ANISOU 1061  OD2 ASP A 130     3774   5930   3785  -1227    590  -1281       O  
ATOM   1062  N   TYR A 131      -0.494  26.141  -4.403  1.00 23.18           N  
ANISOU 1062  N   TYR A 131     2516   4008   2284   -943    606  -1013       N  
ATOM   1063  CA  TYR A 131      -1.126  25.407  -3.319  1.00 24.21           C  
ANISOU 1063  CA  TYR A 131     2570   4223   2407   -806    554   -960       C  
ATOM   1064  C   TYR A 131      -2.458  24.783  -3.757  1.00 25.36           C  
ANISOU 1064  C   TYR A 131     2807   4256   2572   -685    541   -826       C  
ATOM   1065  O   TYR A 131      -2.747  23.634  -3.407  1.00 25.18           O  
ANISOU 1065  O   TYR A 131     2738   4291   2537   -579    487   -751       O  
ATOM   1066  CB  TYR A 131      -1.338  26.312  -2.103  1.00 24.04           C  
ANISOU 1066  CB  TYR A 131     2486   4251   2397   -829    585  -1027       C  
ATOM   1067  CG  TYR A 131      -1.833  25.556  -0.896  1.00 26.63           C  
ANISOU 1067  CG  TYR A 131     2725   4684   2709   -712    531   -980       C  
ATOM   1068  CD1 TYR A 131      -0.955  24.854  -0.081  1.00 25.68           C  
ANISOU 1068  CD1 TYR A 131     2481   4745   2533   -692    465  -1017       C  
ATOM   1069  CD2 TYR A 131      -3.183  25.528  -0.582  1.00 26.18           C  
ANISOU 1069  CD2 TYR A 131     2707   4550   2691   -624    548   -895       C  
ATOM   1070  CE1 TYR A 131      -1.410  24.152   1.021  1.00 28.65           C  
ANISOU 1070  CE1 TYR A 131     2793   5212   2882   -591    418   -966       C  
ATOM   1071  CE2 TYR A 131      -3.649  24.829   0.514  1.00 30.62           C  
ANISOU 1071  CE2 TYR A 131     3192   5201   3239   -535    507   -848       C  
ATOM   1072  CZ  TYR A 131      -2.758  24.144   1.314  1.00 32.90           C  
ANISOU 1072  CZ  TYR A 131     3379   5661   3462   -521    442   -881       C  
ATOM   1073  OH  TYR A 131      -3.224  23.449   2.405  1.00 35.45           O  
ANISOU 1073  OH  TYR A 131     3642   6068   3759   -438    403   -829       O  
ATOM   1074  N   ASP A 132      -3.263  25.528  -4.514  1.00 26.14           N  
ANISOU 1074  N   ASP A 132     3034   4200   2698   -702    591   -796       N  
ATOM   1075  CA  ASP A 132      -4.542  25.004  -5.011  1.00 25.82           C  
ANISOU 1075  CA  ASP A 132     3059   4085   2666   -630    586   -703       C  
ATOM   1076  C   ASP A 132      -4.353  23.717  -5.817  1.00 25.16           C  
ANISOU 1076  C   ASP A 132     2998   4010   2551   -595    525   -634       C  
ATOM   1077  O   ASP A 132      -5.104  22.755  -5.655  1.00 23.83           O  
ANISOU 1077  O   ASP A 132     2795   3876   2382   -515    497   -556       O  
ATOM   1078  CB  ASP A 132      -5.259  26.027  -5.894  1.00 25.82           C  
ANISOU 1078  CB  ASP A 132     3195   3946   2670   -735    657   -743       C  
ATOM   1079  CG  ASP A 132      -5.877  27.166  -5.113  1.00 27.91           C  
ANISOU 1079  CG  ASP A 132     3437   4186   2980   -752    731   -802       C  
ATOM   1080  OD1 ASP A 132      -6.193  26.998  -3.912  1.00 25.69           O  
ANISOU 1080  OD1 ASP A 132     3029   3999   2735   -666    719   -787       O  
ATOM   1081  OD2 ASP A 132      -6.056  28.243  -5.722  1.00 31.45           O  
ANISOU 1081  OD2 ASP A 132     4016   4503   3432   -854    802   -860       O  
ATOM   1082  N   ILE A 133      -3.357  23.711  -6.699  1.00 23.42           N  
ANISOU 1082  N   ILE A 133     2830   3756   2314   -661    509   -660       N  
ATOM   1083  CA  ILE A 133      -3.130  22.565  -7.573  1.00 21.83           C  
ANISOU 1083  CA  ILE A 133     2657   3548   2092   -641    454   -604       C  
ATOM   1084  C   ILE A 133      -2.773  21.326  -6.761  1.00 24.63           C  
ANISOU 1084  C   ILE A 133     2892   4026   2440   -533    404   -567       C  
ATOM   1085  O   ILE A 133      -3.298  20.242  -7.004  1.00 22.20           O  
ANISOU 1085  O   ILE A 133     2595   3715   2123   -461    367   -483       O  
ATOM   1086  CB  ILE A 133      -2.015  22.836  -8.591  1.00 25.95           C  
ANISOU 1086  CB  ILE A 133     3223   4029   2606   -756    460   -654       C  
ATOM   1087  CG1 ILE A 133      -2.394  23.999  -9.508  1.00 27.74           C  
ANISOU 1087  CG1 ILE A 133     3604   4103   2835   -867    508   -667       C  
ATOM   1088  CG2 ILE A 133      -1.735  21.587  -9.424  1.00 23.17           C  
ANISOU 1088  CG2 ILE A 133     2883   3678   2243   -730    403   -600       C  
ATOM   1089  CD1 ILE A 133      -1.255  24.451 -10.403  1.00 27.57           C  
ANISOU 1089  CD1 ILE A 133     3617   4051   2808  -1010    546   -715       C  
ATOM   1090  N   ARG A 134      -1.880  21.490  -5.791  1.00 23.26           N  
ANISOU 1090  N   ARG A 134     2591   3991   2256   -556    402   -651       N  
ATOM   1091  CA  ARG A 134      -1.505  20.377  -4.929  1.00 23.08           C  
ANISOU 1091  CA  ARG A 134     2452   4110   2209   -467    347   -632       C  
ATOM   1092  C   ARG A 134      -2.709  19.871  -4.144  1.00 21.10           C  
ANISOU 1092  C   ARG A 134     2197   3848   1970   -355    338   -534       C  
ATOM   1093  O   ARG A 134      -2.943  18.664  -4.052  1.00 20.28           O  
ANISOU 1093  O   ARG A 134     2078   3769   1857   -267    298   -454       O  
ATOM   1094  CB  ARG A 134      -0.390  20.795  -3.978  1.00 20.29           C  
ANISOU 1094  CB  ARG A 134     1964   3918   1830   -516    338   -746       C  
ATOM   1095  CG  ARG A 134       0.805  21.420  -4.676  1.00 20.38           C  
ANISOU 1095  CG  ARG A 134     1956   3949   1840   -653    365   -854       C  
ATOM   1096  CD  ARG A 134       1.982  21.518  -3.743  1.00 21.78           C  
ANISOU 1096  CD  ARG A 134     1974   4318   1984   -685    340   -962       C  
ATOM   1097  NE  ARG A 134       3.013  22.415  -4.255  1.00 20.96           N  
ANISOU 1097  NE  ARG A 134     1842   4233   1890   -845    390  -1080       N  
ATOM   1098  CZ  ARG A 134       4.306  22.294  -3.985  1.00 20.32           C  
ANISOU 1098  CZ  ARG A 134     1620   4319   1783   -895    370  -1182       C  
ATOM   1099  NH1 ARG A 134       4.735  21.294  -3.224  1.00 22.85           N  
ANISOU 1099  NH1 ARG A 134     1822   4800   2059   -782    293  -1176       N  
ATOM   1100  NH2 ARG A 134       5.170  23.161  -4.493  1.00 20.96           N  
ANISOU 1100  NH2 ARG A 134     1694   4393   1877  -1044    435  -1277       N  
ATOM   1101  N   PHE A 135      -3.470  20.805  -3.580  1.00 20.02           N  
ANISOU 1101  N   PHE A 135     2071   3674   1863   -365    383   -543       N  
ATOM   1102  CA  PHE A 135      -4.648  20.461  -2.792  1.00 20.33           C  
ANISOU 1102  CA  PHE A 135     2090   3703   1932   -279    388   -460       C  
ATOM   1103  C   PHE A 135      -5.651  19.646  -3.608  1.00 21.60           C  
ANISOU 1103  C   PHE A 135     2301   3798   2107   -237    382   -357       C  
ATOM   1104  O   PHE A 135      -6.109  18.589  -3.171  1.00 21.26           O  
ANISOU 1104  O   PHE A 135     2217   3798   2064   -162    349   -278       O  
ATOM   1105  CB  PHE A 135      -5.315  21.732  -2.254  1.00 20.94           C  
ANISOU 1105  CB  PHE A 135     2167   3738   2053   -311    448   -499       C  
ATOM   1106  CG  PHE A 135      -6.526  21.471  -1.405  1.00 26.26           C  
ANISOU 1106  CG  PHE A 135     2798   4405   2776   -240    458   -427       C  
ATOM   1107  CD1 PHE A 135      -6.397  21.220  -0.047  1.00 29.92           C  
ANISOU 1107  CD1 PHE A 135     3167   4989   3212   -216    429   -448       C  
ATOM   1108  CD2 PHE A 135      -7.798  21.482  -1.962  1.00 27.12           C  
ANISOU 1108  CD2 PHE A 135     2910   4468   2926   -237    484   -380       C  
ATOM   1109  CE1 PHE A 135      -7.517  20.982   0.736  1.00 29.03           C  
ANISOU 1109  CE1 PHE A 135     3017   4866   3146   -167    438   -389       C  
ATOM   1110  CE2 PHE A 135      -8.916  21.239  -1.182  1.00 28.66           C  
ANISOU 1110  CE2 PHE A 135     3035   4673   3181   -186    488   -327       C  
ATOM   1111  CZ  PHE A 135      -8.772  20.990   0.167  1.00 27.53           C  
ANISOU 1111  CZ  PHE A 135     2845   4576   3038   -148    470   -323       C  
ATOM   1112  N   TYR A 136      -5.980  20.130  -4.799  1.00 19.26           N  
ANISOU 1112  N   TYR A 136     2085   3428   1804   -308    407   -367       N  
ATOM   1113  CA  TYR A 136      -7.010  19.489  -5.600  1.00 19.40           C  
ANISOU 1113  CA  TYR A 136     2137   3418   1816   -303    397   -273       C  
ATOM   1114  C   TYR A 136      -6.512  18.183  -6.214  1.00 20.48           C  
ANISOU 1114  C   TYR A 136     2297   3566   1918   -268    334   -211       C  
ATOM   1115  O   TYR A 136      -7.282  17.240  -6.362  1.00 18.60           O  
ANISOU 1115  O   TYR A 136     2045   3340   1681   -218    305    -98       O  
ATOM   1116  CB  TYR A 136      -7.513  20.446  -6.682  1.00 20.71           C  
ANISOU 1116  CB  TYR A 136     2419   3485   1966   -420    439   -301       C  
ATOM   1117  CG  TYR A 136      -8.444  21.509  -6.142  1.00 23.08           C  
ANISOU 1117  CG  TYR A 136     2686   3753   2328   -438    505   -334       C  
ATOM   1118  CD1 TYR A 136      -9.498  21.173  -5.298  1.00 24.17           C  
ANISOU 1118  CD1 TYR A 136     2706   3910   2568   -341    481   -256       C  
ATOM   1119  CD2 TYR A 136      -8.264  22.849  -6.463  1.00 23.74           C  
ANISOU 1119  CD2 TYR A 136     2870   3734   2415   -534    559   -437       C  
ATOM   1120  CE1 TYR A 136     -10.353  22.143  -4.796  1.00 23.24           C  
ANISOU 1120  CE1 TYR A 136     2553   3718   2560   -336    504   -286       C  
ATOM   1121  CE2 TYR A 136      -9.115  23.827  -5.965  1.00 24.67           C  
ANISOU 1121  CE2 TYR A 136     2967   3763   2644   -520    583   -457       C  
ATOM   1122  CZ  TYR A 136     -10.156  23.470  -5.133  1.00 22.71           C  
ANISOU 1122  CZ  TYR A 136     2583   3544   2503   -418    553   -385       C  
ATOM   1123  OH  TYR A 136     -11.007  24.437  -4.637  1.00 25.52           O  
ANISOU 1123  OH  TYR A 136     2904   3817   2975   -403    574   -419       O  
ATOM   1124  N   MET A 137      -5.226  18.120  -6.557  1.00 20.57           N  
ANISOU 1124  N   MET A 137     2333   3573   1911   -294    314   -278       N  
ATOM   1125  CA  MET A 137      -4.626  16.861  -6.996  1.00 17.68           C  
ANISOU 1125  CA  MET A 137     1967   3224   1527   -252    263   -237       C  
ATOM   1126  C   MET A 137      -4.762  15.795  -5.912  1.00 17.87           C  
ANISOU 1126  C   MET A 137     1901   3335   1554   -139    236   -176       C  
ATOM   1127  O   MET A 137      -5.103  14.647  -6.195  1.00 18.68           O  
ANISOU 1127  O   MET A 137     2008   3441   1651    -85    202    -88       O  
ATOM   1128  CB  MET A 137      -3.147  17.054  -7.362  1.00 18.08           C  
ANISOU 1128  CB  MET A 137     2023   3271   1574   -296    256   -328       C  
ATOM   1129  CG  MET A 137      -2.925  17.622  -8.747  1.00 18.54           C  
ANISOU 1129  CG  MET A 137     2186   3229   1630   -407    261   -361       C  
ATOM   1130  SD  MET A 137      -3.317  16.421 -10.045  1.00 24.19           S  
ANISOU 1130  SD  MET A 137     2981   3879   2332   -414    206   -271       S  
ATOM   1131  CE  MET A 137      -2.182  15.113  -9.619  1.00 38.36           C  
ANISOU 1131  CE  MET A 137     4684   5761   4129   -316    178   -279       C  
ATOM   1132  N   TYR A 138      -4.498  16.181  -4.668  1.00 17.59           N  
ANISOU 1132  N   TYR A 138     1795   3362   1527   -110    246   -219       N  
ATOM   1133  CA  TYR A 138      -4.606  15.250  -3.557  1.00 16.86           C  
ANISOU 1133  CA  TYR A 138     1631   3352   1424    -17    214   -167       C  
ATOM   1134  C   TYR A 138      -6.037  14.748  -3.428  1.00 18.42           C  
ANISOU 1134  C   TYR A 138     1825   3535   1640     28    216    -57       C  
ATOM   1135  O   TYR A 138      -6.273  13.574  -3.146  1.00 18.63           O  
ANISOU 1135  O   TYR A 138     1829   3596   1653    105    183     26       O  
ATOM   1136  CB  TYR A 138      -4.148  15.907  -2.257  1.00 21.01           C  
ANISOU 1136  CB  TYR A 138     2070   3986   1926    -19    213   -240       C  
ATOM   1137  CG  TYR A 138      -3.822  14.921  -1.163  1.00 21.56           C  
ANISOU 1137  CG  TYR A 138     2056   4189   1945     70    163   -207       C  
ATOM   1138  CD1 TYR A 138      -2.672  14.146  -1.223  1.00 21.95           C  
ANISOU 1138  CD1 TYR A 138     2053   4340   1947    114    116   -230       C  
ATOM   1139  CD2 TYR A 138      -4.658  14.771  -0.066  1.00 23.86           C  
ANISOU 1139  CD2 TYR A 138     2322   4509   2237    112    166   -156       C  
ATOM   1140  CE1 TYR A 138      -2.369  13.246  -0.225  1.00 25.22           C  
ANISOU 1140  CE1 TYR A 138     2396   4878   2309    212     73   -193       C  
ATOM   1141  CE2 TYR A 138      -4.364  13.876   0.938  1.00 27.91           C  
ANISOU 1141  CE2 TYR A 138     2771   5142   2692    195    123   -120       C  
ATOM   1142  CZ  TYR A 138      -3.216  13.116   0.855  1.00 26.80           C  
ANISOU 1142  CZ  TYR A 138     2584   5099   2500    251     76   -135       C  
ATOM   1143  OH  TYR A 138      -2.914  12.220   1.854  1.00 29.81           O  
ANISOU 1143  OH  TYR A 138     2903   5600   2823    349     38    -93       O  
ATOM   1144  N   GLU A 139      -6.993  15.638  -3.659  1.00 18.25           N  
ANISOU 1144  N   GLU A 139     1820   3462   1654    -19    256    -53       N  
ATOM   1145  CA  GLU A 139      -8.401  15.275  -3.531  1.00 17.93           C  
ANISOU 1145  CA  GLU A 139     1755   3408   1649     17    261     54       C  
ATOM   1146  C   GLU A 139      -8.823  14.306  -4.633  1.00 15.47           C  
ANISOU 1146  C   GLU A 139     1492   3054   1332     31    229    172       C  
ATOM   1147  O   GLU A 139      -9.624  13.402  -4.395  1.00 16.44           O  
ANISOU 1147  O   GLU A 139     1596   3174   1477     89    210    284       O  
ATOM   1148  CB  GLU A 139      -9.284  16.524  -3.550  1.00 20.28           C  
ANISOU 1148  CB  GLU A 139     2036   3665   2004    -37    314     25       C  
ATOM   1149  CG  GLU A 139      -9.102  17.433  -2.334  1.00 24.64           C  
ANISOU 1149  CG  GLU A 139     2545   4235   2581    -47    346    -70       C  
ATOM   1150  CD  GLU A 139      -9.469  16.759  -1.018  1.00 25.00           C  
ANISOU 1150  CD  GLU A 139     2537   4329   2631     13    325    -33       C  
ATOM   1151  OE1 GLU A 139     -10.585  16.212  -0.910  1.00 25.76           O  
ANISOU 1151  OE1 GLU A 139     2605   4415   2768     44    319     50       O  
ATOM   1152  OE2 GLU A 139      -8.640  16.782  -0.083  1.00 26.16           O  
ANISOU 1152  OE2 GLU A 139     2672   4527   2742     21    315    -85       O  
ATOM   1153  N   ILE A 140      -8.296  14.497  -5.837  1.00 16.60           N  
ANISOU 1153  N   ILE A 140     1715   3144   1448    -33    219    151       N  
ATOM   1154  CA  ILE A 140      -8.574  13.577  -6.934  1.00 18.23           C  
ANISOU 1154  CA  ILE A 140     1997   3273   1656    -36    169    264       C  
ATOM   1155  C   ILE A 140      -7.974  12.208  -6.624  1.00 19.66           C  
ANISOU 1155  C   ILE A 140     2157   3481   1831     47    139    283       C  
ATOM   1156  O   ILE A 140      -8.577  11.174  -6.888  1.00 14.68           O  
ANISOU 1156  O   ILE A 140     1552   2785   1239     86    109    390       O  
ATOM   1157  CB  ILE A 140      -8.008  14.081  -8.268  1.00 17.91           C  
ANISOU 1157  CB  ILE A 140     2067   3154   1586   -144    149    218       C  
ATOM   1158  CG1 ILE A 140      -8.620  15.431  -8.648  1.00 18.97           C  
ANISOU 1158  CG1 ILE A 140     2256   3169   1780   -227    153    190       C  
ATOM   1159  CG2 ILE A 140      -8.283  13.072  -9.375  1.00 18.46           C  
ANISOU 1159  CG2 ILE A 140     2217   3104   1691   -152     75    330       C  
ATOM   1160  CD1 ILE A 140      -7.933  16.082  -9.849  1.00 16.33           C  
ANISOU 1160  CD1 ILE A 140     2052   2742   1411   -352    138    116       C  
ATOM   1161  N   LEU A 141      -6.776  12.208  -6.054  1.00 17.14           N  
ANISOU 1161  N   LEU A 141     1794   3240   1478     69    146    177       N  
ATOM   1162  CA  LEU A 141      -6.121  10.954  -5.712  1.00 16.22           C  
ANISOU 1162  CA  LEU A 141     1650   3165   1347    152    121    196       C  
ATOM   1163  C   LEU A 141      -6.936  10.146  -4.704  1.00 17.65           C  
ANISOU 1163  C   LEU A 141     1787   3377   1544    242    122    290       C  
ATOM   1164  O   LEU A 141      -6.968   8.919  -4.779  1.00 20.35           O  
ANISOU 1164  O   LEU A 141     2149   3689   1896    300    113    355       O  
ATOM   1165  CB  LEU A 141      -4.713  11.223  -5.171  1.00 14.57           C  
ANISOU 1165  CB  LEU A 141     1389   3044   1104    159    118     76       C  
ATOM   1166  CG  LEU A 141      -3.660  11.536  -6.233  1.00 16.52           C  
ANISOU 1166  CG  LEU A 141     1681   3253   1343     84    115    -12       C  
ATOM   1167  CD1 LEU A 141      -2.342  11.926  -5.570  1.00 16.76           C  
ANISOU 1167  CD1 LEU A 141     1639   3375   1353     85    111   -122       C  
ATOM   1168  CD2 LEU A 141      -3.457  10.347  -7.157  1.00 15.30           C  
ANISOU 1168  CD2 LEU A 141     1575   3052   1188    106     90     39       C  
ATOM   1169  N   LYS A 142      -7.599  10.829  -3.772  1.00 17.07           N  
ANISOU 1169  N   LYS A 142     1665   3346   1475    241    140    288       N  
ATOM   1170  CA  LYS A 142      -8.461  10.150  -2.807  1.00 19.01           C  
ANISOU 1170  CA  LYS A 142     1877   3614   1733    305    144    371       C  
ATOM   1171  C   LYS A 142      -9.551   9.378  -3.539  1.00 19.50           C  
ANISOU 1171  C   LYS A 142     1994   3562   1853    303    146    486       C  
ATOM   1172  O   LYS A 142      -9.835   8.225  -3.225  1.00 19.97           O  
ANISOU 1172  O   LYS A 142     2071   3592   1926    353    150    545       O  
ATOM   1173  CB  LYS A 142      -9.108  11.144  -1.840  1.00 20.26           C  
ANISOU 1173  CB  LYS A 142     1989   3812   1897    275    166    337       C  
ATOM   1174  CG  LYS A 142      -8.173  11.760  -0.827  1.00 24.93           C  
ANISOU 1174  CG  LYS A 142     2540   4487   2447    269    163    229       C  
ATOM   1175  CD  LYS A 142      -8.959  12.682   0.090  1.00 28.28           C  
ANISOU 1175  CD  LYS A 142     2935   4911   2899    227    196    194       C  
ATOM   1176  CE  LYS A 142      -8.047  13.506   0.975  1.00 32.76           C  
ANISOU 1176  CE  LYS A 142     3475   5530   3443    197    201     83       C  
ATOM   1177  NZ  LYS A 142      -8.840  14.466   1.789  1.00 33.92           N  
ANISOU 1177  NZ  LYS A 142     3598   5652   3637    150    244     42       N  
ATOM   1178  N   ALA A 143     -10.156  10.030  -4.522  1.00 17.78           N  
ANISOU 1178  N   ALA A 143     1818   3262   1675    234    141    510       N  
ATOM   1179  CA  ALA A 143     -11.233   9.417  -5.286  1.00 19.93           C  
ANISOU 1179  CA  ALA A 143     2153   3394   2025    212    119    607       C  
ATOM   1180  C   ALA A 143     -10.710   8.228  -6.089  1.00 19.76           C  
ANISOU 1180  C   ALA A 143     2210   3278   2020    215     94    610       C  
ATOM   1181  O   ALA A 143     -11.347   7.172  -6.140  1.00 17.89           O  
ANISOU 1181  O   ALA A 143     2012   2957   1827    226     91    655       O  
ATOM   1182  CB  ALA A 143     -11.876  10.441  -6.208  1.00 18.27           C  
ANISOU 1182  CB  ALA A 143     1976   3106   1860    138     96    636       C  
ATOM   1183  N   LEU A 144      -9.543   8.401  -6.704  1.00 18.51           N  
ANISOU 1183  N   LEU A 144     2076   3140   1819    197     81    548       N  
ATOM   1184  CA  LEU A 144      -8.982   7.361  -7.556  1.00 16.47           C  
ANISOU 1184  CA  LEU A 144     1885   2801   1571    192     57    545       C  
ATOM   1185  C   LEU A 144      -8.487   6.164  -6.742  1.00 16.63           C  
ANISOU 1185  C   LEU A 144     1886   2871   1559    277     76    548       C  
ATOM   1186  O   LEU A 144      -8.727   5.020  -7.128  1.00 17.09           O  
ANISOU 1186  O   LEU A 144     2006   2836   1650    280     67    583       O  
ATOM   1187  CB  LEU A 144      -7.850   7.917  -8.418  1.00 17.70           C  
ANISOU 1187  CB  LEU A 144     2066   2979   1681    141     40    471       C  
ATOM   1188  CG  LEU A 144      -8.265   8.846  -9.563  1.00 17.01           C  
ANISOU 1188  CG  LEU A 144     2042   2798   1622     40     11    477       C  
ATOM   1189  CD1 LEU A 144      -7.037   9.299 -10.343  1.00 17.84           C  
ANISOU 1189  CD1 LEU A 144     2179   2932   1666    -23      4    385       C  
ATOM   1190  CD2 LEU A 144      -9.247   8.147 -10.490  1.00 15.25           C  
ANISOU 1190  CD2 LEU A 144     1890   2408   1495     14    -25    541       C  
ATOM   1191  N   ASP A 145      -7.802   6.400  -5.627  1.00 15.56           N  
ANISOU 1191  N   ASP A 145     1671   2879   1361    345    100    508       N  
ATOM   1192  CA  ASP A 145      -7.408   5.251  -4.815  1.00 17.81           C  
ANISOU 1192  CA  ASP A 145     1948   3204   1614    434    115    525       C  
ATOM   1193  C   ASP A 145      -8.652   4.514  -4.346  1.00 20.36           C  
ANISOU 1193  C   ASP A 145     2311   3448   1977    438    131    604       C  
ATOM   1194  O   ASP A 145      -8.665   3.284  -4.294  1.00 22.94           O  
ANISOU 1194  O   ASP A 145     2697   3717   2301    467    133    636       O  
ATOM   1195  CB  ASP A 145      -6.561   5.638  -3.606  1.00 21.67           C  
ANISOU 1195  CB  ASP A 145     2338   3861   2036    509    128    469       C  
ATOM   1196  CG  ASP A 145      -6.100   4.414  -2.825  1.00 25.46           C  
ANISOU 1196  CG  ASP A 145     2823   4379   2474    612    141    494       C  
ATOM   1197  OD1 ASP A 145      -5.593   3.461  -3.459  1.00 23.62           O  
ANISOU 1197  OD1 ASP A 145     2650   4090   2234    634    132    501       O  
ATOM   1198  OD2 ASP A 145      -6.277   4.382  -1.592  1.00 26.25           O  
ANISOU 1198  OD2 ASP A 145     2874   4558   2543    667    158    509       O  
ATOM   1199  N   TYR A 146      -9.705   5.259  -4.024  1.00 18.70           N  
ANISOU 1199  N   TYR A 146     2071   3236   1799    402    141    629       N  
ATOM   1200  CA  TYR A 146     -10.926   4.609  -3.564  1.00 17.88           C  
ANISOU 1200  CA  TYR A 146     1999   3068   1728    395    156    690       C  
ATOM   1201  C   TYR A 146     -11.537   3.712  -4.639  1.00 19.68           C  
ANISOU 1201  C   TYR A 146     2324   3137   2015    342    136    717       C  
ATOM   1202  O   TYR A 146     -11.756   2.525  -4.393  1.00 18.48           O  
ANISOU 1202  O   TYR A 146     2232   2935   1853    357    144    743       O  
ATOM   1203  CB  TYR A 146     -11.968   5.619  -3.095  1.00 18.95           C  
ANISOU 1203  CB  TYR A 146     2072   3242   1887    365    169    709       C  
ATOM   1204  CG  TYR A 146     -13.151   4.922  -2.449  1.00 18.51           C  
ANISOU 1204  CG  TYR A 146     2038   3148   1846    359    191    763       C  
ATOM   1205  CD1 TYR A 146     -13.021   4.324  -1.204  1.00 22.80           C  
ANISOU 1205  CD1 TYR A 146     2574   3759   2328    410    217    774       C  
ATOM   1206  CD2 TYR A 146     -14.371   4.819  -3.103  1.00 20.61           C  
ANISOU 1206  CD2 TYR A 146     2339   3311   2180    300    184    797       C  
ATOM   1207  CE1 TYR A 146     -14.082   3.671  -0.609  1.00 25.12           C  
ANISOU 1207  CE1 TYR A 146     2906   4018   2621    389    241    818       C  
ATOM   1208  CE2 TYR A 146     -15.439   4.163  -2.518  1.00 20.86           C  
ANISOU 1208  CE2 TYR A 146     2393   3318   2213    286    210    835       C  
ATOM   1209  CZ  TYR A 146     -15.286   3.593  -1.266  1.00 24.15           C  
ANISOU 1209  CZ  TYR A 146     2814   3800   2560    325    241    845       C  
ATOM   1210  OH  TYR A 146     -16.337   2.940  -0.662  1.00 26.20           O  
ANISOU 1210  OH  TYR A 146     3114   4034   2807    294    273    877       O  
ATOM   1211  N   CYS A 147     -11.798   4.243  -5.832  1.00 19.70           N  
ANISOU 1211  N   CYS A 147     2349   3062   2072    276    106    704       N  
ATOM   1212  CA  CYS A 147     -12.469   3.415  -6.832  1.00 18.46           C  
ANISOU 1212  CA  CYS A 147     2271   2772   1970    225     86    717       C  
ATOM   1213  C   CYS A 147     -11.558   2.271  -7.290  1.00 18.15           C  
ANISOU 1213  C   CYS A 147     2269   2721   1905    255     85    721       C  
ATOM   1214  O   CYS A 147     -12.031   1.155  -7.522  1.00 17.95           O  
ANISOU 1214  O   CYS A 147     2288   2638   1894    253     96    756       O  
ATOM   1215  CB  CYS A 147     -12.972   4.251  -8.022  1.00 18.23           C  
ANISOU 1215  CB  CYS A 147     2256   2669   2003    156     51    702       C  
ATOM   1216  SG  CYS A 147     -11.748   5.019  -9.112  1.00 17.78           S  
ANISOU 1216  SG  CYS A 147     2217   2606   1931    122     16    652       S  
ATOM   1217  N   HIS A 148     -10.250   2.516  -7.359  1.00 16.97           N  
ANISOU 1217  N   HIS A 148     2103   2635   1710    284     74    683       N  
ATOM   1218  CA  HIS A 148      -9.319   1.437  -7.674  1.00 15.96           C  
ANISOU 1218  CA  HIS A 148     2005   2510   1550    325     72    685       C  
ATOM   1219  C   HIS A 148      -9.337   0.364  -6.585  1.00 14.67           C  
ANISOU 1219  C   HIS A 148     1854   2378   1343    406    104    725       C  
ATOM   1220  O   HIS A 148      -9.320  -0.828  -6.888  1.00 17.99           O  
ANISOU 1220  O   HIS A 148     2328   2744   1762    423    110    757       O  
ATOM   1221  CB  HIS A 148      -7.898   1.980  -7.859  1.00 15.58           C  
ANISOU 1221  CB  HIS A 148     1926   2545   1450    345     56    623       C  
ATOM   1222  CG  HIS A 148      -7.763   2.896  -9.030  1.00 15.64           C  
ANISOU 1222  CG  HIS A 148     1950   2509   1486    257     23    585       C  
ATOM   1223  ND1 HIS A 148      -6.621   3.650  -9.264  1.00 16.79           N  
ANISOU 1223  ND1 HIS A 148     2068   2733   1579    249     12    517       N  
ATOM   1224  CD2 HIS A 148      -8.605   3.188 -10.047  1.00 13.35           C  
ANISOU 1224  CD2 HIS A 148     1699   2112   1260    177      3    599       C  
ATOM   1225  CE1 HIS A 148      -6.779   4.357 -10.360  1.00 18.29           C  
ANISOU 1225  CE1 HIS A 148     2296   2857   1797    161    -14    500       C  
ATOM   1226  NE2 HIS A 148      -7.988   4.100 -10.857  1.00 15.54           N  
ANISOU 1226  NE2 HIS A 148     1993   2388   1525    121    -22    549       N  
ATOM   1227  N   SER A 149      -9.389   0.784  -5.321  1.00 16.94           N  
ANISOU 1227  N   SER A 149     2098   2747   1590    452    126    724       N  
ATOM   1228  CA  SER A 149      -9.387  -0.170  -4.205  1.00 18.00           C  
ANISOU 1228  CA  SER A 149     2256   2913   1671    528    153    764       C  
ATOM   1229  C   SER A 149     -10.691  -0.953  -4.202  1.00 19.34           C  
ANISOU 1229  C   SER A 149     2491   2983   1873    485    170    821       C  
ATOM   1230  O   SER A 149     -10.781  -2.036  -3.621  1.00 20.22           O  
ANISOU 1230  O   SER A 149     2661   3077   1945    528    190    864       O  
ATOM   1231  CB  SER A 149      -9.192   0.538  -2.861  1.00 19.52           C  
ANISOU 1231  CB  SER A 149     2381   3223   1812    575    169    746       C  
ATOM   1232  OG  SER A 149     -10.354   1.263  -2.484  1.00 20.22           O  
ANISOU 1232  OG  SER A 149     2449   3296   1936    513    178    756       O  
ATOM   1233  N   MET A 150     -11.695  -0.389  -4.863  1.00 19.44           N  
ANISOU 1233  N   MET A 150     1893   2874   2620    292    384   1217       N  
ATOM   1234  CA  MET A 150     -13.004  -1.011  -4.963  1.00 21.99           C  
ANISOU 1234  CA  MET A 150     2184   3101   3071    277    410   1274       C  
ATOM   1235  C   MET A 150     -13.159  -1.747  -6.291  1.00 21.49           C  
ANISOU 1235  C   MET A 150     2167   2833   3163    222    394   1234       C  
ATOM   1236  O   MET A 150     -14.264  -2.148  -6.664  1.00 23.80           O  
ANISOU 1236  O   MET A 150     2445   3025   3572    189    397   1240       O  
ATOM   1237  CB  MET A 150     -14.093   0.046  -4.794  1.00 18.37           C  
ANISOU 1237  CB  MET A 150     1731   2684   2564    261    382   1198       C  
ATOM   1238  CG  MET A 150     -14.105   0.674  -3.411  1.00 20.73           C  
ANISOU 1238  CG  MET A 150     1973   3185   2717    314    410   1232       C  
ATOM   1239  SD  MET A 150     -14.784  -0.418  -2.137  1.00 27.53           S  
ANISOU 1239  SD  MET A 150     2719   4124   3618    376    490   1423       S  
ATOM   1240  CE  MET A 150     -16.528  -0.331  -2.554  1.00 25.28           C  
ANISOU 1240  CE  MET A 150     2421   3730   3454    335    498   1419       C  
ATOM   1241  N   GLY A 151     -12.049  -1.919  -7.005  1.00 21.46           N  
ANISOU 1241  N   GLY A 151     2216   2778   3161    211    379   1186       N  
ATOM   1242  CA  GLY A 151     -12.038  -2.731  -8.211  1.00 21.41           C  
ANISOU 1242  CA  GLY A 151     2249   2592   3293    165    375   1145       C  
ATOM   1243  C   GLY A 151     -12.566  -2.077  -9.473  1.00 19.69           C  
ANISOU 1243  C   GLY A 151     2108   2288   3087     96    303    995       C  
ATOM   1244  O   GLY A 151     -12.945  -2.760 -10.424  1.00 19.53           O  
ANISOU 1244  O   GLY A 151     2107   2129   3185     49    297    954       O  
ATOM   1245  N   ILE A 152     -12.572  -0.751  -9.491  1.00 15.61           N  
ANISOU 1245  N   ILE A 152     1630   1855   2447     90    251    910       N  
ATOM   1246  CA  ILE A 152     -13.134  -0.011 -10.612  1.00 18.04           C  
ANISOU 1246  CA  ILE A 152     2000   2099   2755     35    185    789       C  
ATOM   1247  C   ILE A 152     -12.148   1.002 -11.186  1.00 19.74           C  
ANISOU 1247  C   ILE A 152     2289   2349   2865     26    142    691       C  
ATOM   1248  O   ILE A 152     -11.482   1.727 -10.439  1.00 19.49           O  
ANISOU 1248  O   ILE A 152     2250   2427   2728     59    147    692       O  
ATOM   1249  CB  ILE A 152     -14.434   0.701 -10.179  1.00 20.09           C  
ANISOU 1249  CB  ILE A 152     2228   2402   3003     33    167    788       C  
ATOM   1250  CG1 ILE A 152     -15.487  -0.344  -9.779  1.00 21.14           C  
ANISOU 1250  CG1 ILE A 152     2287   2485   3261     31    209    882       C  
ATOM   1251  CG2 ILE A 152     -14.937   1.657 -11.271  1.00 17.46           C  
ANISOU 1251  CG2 ILE A 152     1954   2027   2654    -13     96    675       C  
ATOM   1252  CD1 ILE A 152     -16.626   0.197  -8.928  1.00 24.97           C  
ANISOU 1252  CD1 ILE A 152     2715   3044   3727     52    219    922       C  
ATOM   1253  N   MET A 153     -12.043   1.041 -12.516  1.00 16.41           N  
ANISOU 1253  N   MET A 153     1929   1837   2468    -21    100    605       N  
ATOM   1254  CA  MET A 153     -11.278   2.094 -13.179  1.00 15.46           C  
ANISOU 1254  CA  MET A 153     1877   1741   2257    -34     59    517       C  
ATOM   1255  C   MET A 153     -12.226   3.091 -13.851  1.00 15.63           C  
ANISOU 1255  C   MET A 153     1926   1748   2264    -66      2    450       C  
ATOM   1256  O   MET A 153     -13.258   2.706 -14.403  1.00 16.23           O  
ANISOU 1256  O   MET A 153     1993   1763   2412    -97    -21    444       O  
ATOM   1257  CB  MET A 153     -10.286   1.506 -14.193  1.00 20.20           C  
ANISOU 1257  CB  MET A 153     2526   2272   2876    -54     61    476       C  
ATOM   1258  CG  MET A 153     -10.827   0.423 -15.096  1.00 18.59           C  
ANISOU 1258  CG  MET A 153     2329   1953   2781    -92     61    456       C  
ATOM   1259  SD  MET A 153      -9.545  -0.365 -16.124  1.00 22.34           S  
ANISOU 1259  SD  MET A 153     2855   2355   3279   -105     85    405       S  
ATOM   1260  CE  MET A 153     -10.531  -1.668 -16.844  1.00 20.22           C  
ANISOU 1260  CE  MET A 153     2570   1957   3158   -153     92    377       C  
ATOM   1261  N   HIS A 154     -11.882   4.375 -13.779  1.00 13.94           N  
ANISOU 1261  N   HIS A 154     1739   1590   1966    -58    -19    405       N  
ATOM   1262  CA  HIS A 154     -12.788   5.431 -14.237  1.00 14.84           C  
ANISOU 1262  CA  HIS A 154     1869   1697   2073    -75    -63    363       C  
ATOM   1263  C   HIS A 154     -12.794   5.545 -15.764  1.00 16.70           C  
ANISOU 1263  C   HIS A 154     2162   1868   2317   -117   -113    308       C  
ATOM   1264  O   HIS A 154     -13.860   5.582 -16.398  1.00 17.58           O  
ANISOU 1264  O   HIS A 154     2267   1946   2467   -141   -151    299       O  
ATOM   1265  CB  HIS A 154     -12.399   6.767 -13.595  1.00 13.83           C  
ANISOU 1265  CB  HIS A 154     1744   1640   1871    -51    -58    332       C  
ATOM   1266  CG  HIS A 154     -13.344   7.891 -13.908  1.00 12.61           C  
ANISOU 1266  CG  HIS A 154     1594   1472   1726    -57    -89    301       C  
ATOM   1267  ND1 HIS A 154     -13.285   8.608 -15.081  1.00 16.35           N  
ANISOU 1267  ND1 HIS A 154     2118   1900   2195    -81   -130    260       N  
ATOM   1268  CD2 HIS A 154     -14.373   8.409 -13.196  1.00 12.29           C  
ANISOU 1268  CD2 HIS A 154     1508   1459   1702    -36    -79    314       C  
ATOM   1269  CE1 HIS A 154     -14.240   9.527 -15.081  1.00 15.49           C  
ANISOU 1269  CE1 HIS A 154     1992   1787   2108    -73   -145    256       C  
ATOM   1270  NE2 HIS A 154     -14.908   9.430 -13.948  1.00 12.65           N  
ANISOU 1270  NE2 HIS A 154     1575   1467   1763    -46   -113    283       N  
ATOM   1271  N   ARG A 155     -11.595   5.619 -16.333  1.00 14.77           N  
ANISOU 1271  N   ARG A 155     1966   1617   2027   -123   -111    273       N  
ATOM   1272  CA  ARG A 155     -11.368   5.589 -17.779  1.00 16.14           C  
ANISOU 1272  CA  ARG A 155     2196   1746   2191   -159   -147    224       C  
ATOM   1273  C   ARG A 155     -11.798   6.858 -18.529  1.00 16.89           C  
ANISOU 1273  C   ARG A 155     2319   1849   2250   -170   -193    197       C  
ATOM   1274  O   ARG A 155     -11.781   6.879 -19.753  1.00 15.54           O  
ANISOU 1274  O   ARG A 155     2186   1659   2061   -197   -228    166       O  
ATOM   1275  CB  ARG A 155     -12.058   4.366 -18.413  1.00 13.62           C  
ANISOU 1275  CB  ARG A 155     1866   1367   1942   -191   -160    216       C  
ATOM   1276  CG  ARG A 155     -11.603   3.019 -17.827  1.00 16.18           C  
ANISOU 1276  CG  ARG A 155     2162   1658   2328   -180   -104    250       C  
ATOM   1277  CD  ARG A 155     -11.896   1.854 -18.776  1.00 15.52           C  
ANISOU 1277  CD  ARG A 155     2086   1495   2315   -223   -111    208       C  
ATOM   1278  NE  ARG A 155     -13.301   1.788 -19.159  1.00 16.93           N  
ANISOU 1278  NE  ARG A 155     2236   1654   2541   -258   -157    193       N  
ATOM   1279  CZ  ARG A 155     -13.801   0.893 -20.008  1.00 18.12           C  
ANISOU 1279  CZ  ARG A 155     2384   1746   2755   -307   -175    140       C  
ATOM   1280  NH1 ARG A 155     -13.009  -0.018 -20.571  1.00 16.06           N  
ANISOU 1280  NH1 ARG A 155     2151   1430   2521   -323   -145     91       N  
ATOM   1281  NH2 ARG A 155     -15.094   0.912 -20.296  1.00 15.48           N  
ANISOU 1281  NH2 ARG A 155     2013   1409   2459   -341   -223    129       N  
ATOM   1282  N   ASP A 156     -12.151   7.918 -17.812  1.00 15.08           N  
ANISOU 1282  N   ASP A 156     2068   1652   2011   -146   -189    209       N  
ATOM   1283  CA  ASP A 156     -12.458   9.189 -18.468  1.00 11.50           C  
ANISOU 1283  CA  ASP A 156     1635   1194   1539   -149   -221    196       C  
ATOM   1284  C   ASP A 156     -12.089  10.353 -17.556  1.00 14.66           C  
ANISOU 1284  C   ASP A 156     2024   1622   1923   -121   -190    186       C  
ATOM   1285  O   ASP A 156     -12.840  11.315 -17.413  1.00 17.39           O  
ANISOU 1285  O   ASP A 156     2352   1963   2293   -108   -196    191       O  
ATOM   1286  CB  ASP A 156     -13.939   9.246 -18.861  1.00 16.13           C  
ANISOU 1286  CB  ASP A 156     2190   1768   2169   -157   -263    218       C  
ATOM   1287  CG  ASP A 156     -14.223  10.271 -19.949  1.00 17.80           C  
ANISOU 1287  CG  ASP A 156     2426   1975   2362   -162   -305    220       C  
ATOM   1288  OD1 ASP A 156     -13.281  10.696 -20.655  1.00 17.19           O  
ANISOU 1288  OD1 ASP A 156     2398   1896   2238   -169   -304    204       O  
ATOM   1289  OD2 ASP A 156     -15.404  10.648 -20.106  1.00 18.80           O  
ANISOU 1289  OD2 ASP A 156     2518   2102   2524   -157   -335    248       O  
ATOM   1290  N   VAL A 157     -10.918  10.260 -16.933  1.00 11.47           N  
ANISOU 1290  N   VAL A 157     1627   1249   1484   -114   -154    169       N  
ATOM   1291  CA  VAL A 157     -10.427  11.354 -16.111  1.00 13.04           C  
ANISOU 1291  CA  VAL A 157     1812   1479   1662    -98   -126    138       C  
ATOM   1292  C   VAL A 157      -9.999  12.516 -17.017  1.00 18.47           C  
ANISOU 1292  C   VAL A 157     2540   2127   2349   -112   -137    113       C  
ATOM   1293  O   VAL A 157      -9.162  12.358 -17.914  1.00 17.08           O  
ANISOU 1293  O   VAL A 157     2405   1935   2148   -131   -144    111       O  
ATOM   1294  CB  VAL A 157      -9.255  10.913 -15.214  1.00 15.94           C  
ANISOU 1294  CB  VAL A 157     2166   1907   1986    -90    -91    126       C  
ATOM   1295  CG1 VAL A 157      -8.649  12.109 -14.491  1.00 13.77           C  
ANISOU 1295  CG1 VAL A 157     1878   1670   1686    -86    -68     71       C  
ATOM   1296  CG2 VAL A 157      -9.715   9.847 -14.224  1.00 17.59           C  
ANISOU 1296  CG2 VAL A 157     2325   2160   2199    -67    -72    170       C  
ATOM   1297  N   LYS A 158     -10.603  13.674 -16.783  1.00 17.09           N  
ANISOU 1297  N   LYS A 158     2349   1934   2209   -100   -131    101       N  
ATOM   1298  CA  LYS A 158     -10.307  14.891 -17.528  1.00 14.58           C  
ANISOU 1298  CA  LYS A 158     2058   1570   1914   -108   -131     93       C  
ATOM   1299  C   LYS A 158     -10.870  16.057 -16.718  1.00 15.53           C  
ANISOU 1299  C   LYS A 158     2142   1673   2086    -87   -101     63       C  
ATOM   1300  O   LYS A 158     -11.696  15.836 -15.839  1.00 12.20           O  
ANISOU 1300  O   LYS A 158     1681   1280   1675    -67    -92     59       O  
ATOM   1301  CB  LYS A 158     -10.911  14.830 -18.939  1.00 16.51           C  
ANISOU 1301  CB  LYS A 158     2329   1779   2166   -115   -174    146       C  
ATOM   1302  CG  LYS A 158     -12.426  14.685 -18.975  1.00 17.09           C  
ANISOU 1302  CG  LYS A 158     2367   1847   2278    -99   -204    184       C  
ATOM   1303  CD  LYS A 158     -12.928  14.563 -20.404  1.00 17.96           C  
ANISOU 1303  CD  LYS A 158     2498   1949   2378   -111   -255    232       C  
ATOM   1304  CE  LYS A 158     -14.447  14.479 -20.472  1.00 21.77           C  
ANISOU 1304  CE  LYS A 158     2935   2434   2902    -98   -290    272       C  
ATOM   1305  NZ  LYS A 158     -14.935  14.565 -21.890  1.00 22.67           N  
ANISOU 1305  NZ  LYS A 158     3058   2558   2996   -108   -346    320       N  
ATOM   1306  N   PRO A 159     -10.408  17.292 -16.986  1.00 18.26           N  
ANISOU 1306  N   PRO A 159     2499   1969   2470    -93    -79     39       N  
ATOM   1307  CA  PRO A 159     -10.867  18.464 -16.229  1.00 17.15           C  
ANISOU 1307  CA  PRO A 159     2324   1797   2396    -76    -40     -6       C  
ATOM   1308  C   PRO A 159     -12.393  18.589 -16.128  1.00 16.98           C  
ANISOU 1308  C   PRO A 159     2269   1758   2426    -42    -48     33       C  
ATOM   1309  O   PRO A 159     -12.909  18.906 -15.051  1.00 15.12           O  
ANISOU 1309  O   PRO A 159     1992   1539   2212    -22    -15    -13       O  
ATOM   1310  CB  PRO A 159     -10.283  19.630 -17.024  1.00 19.29           C  
ANISOU 1310  CB  PRO A 159     2617   1990   2724    -88    -22     -3       C  
ATOM   1311  CG  PRO A 159      -9.007  19.081 -17.573  1.00 17.98           C  
ANISOU 1311  CG  PRO A 159     2488   1849   2493   -119    -33     -1       C  
ATOM   1312  CD  PRO A 159      -9.286  17.631 -17.883  1.00 19.70           C  
ANISOU 1312  CD  PRO A 159     2721   2124   2640   -117    -77     43       C  
ATOM   1313  N   HIS A 160     -13.100  18.330 -17.222  1.00 17.09           N  
ANISOU 1313  N   HIS A 160     2294   1748   2452    -37    -92    115       N  
ATOM   1314  CA  HIS A 160     -14.554  18.469 -17.212  1.00 19.60           C  
ANISOU 1314  CA  HIS A 160     2571   2052   2823     -6   -104    161       C  
ATOM   1315  C   HIS A 160     -15.215  17.491 -16.248  1.00 16.73           C  
ANISOU 1315  C   HIS A 160     2172   1751   2434      2   -106    151       C  
ATOM   1316  O   HIS A 160     -16.308  17.754 -15.744  1.00 20.68           O  
ANISOU 1316  O   HIS A 160     2626   2248   2984     32    -92    162       O  
ATOM   1317  CB  HIS A 160     -15.126  18.275 -18.612  1.00 27.70           C  
ANISOU 1317  CB  HIS A 160     3609   3065   3849     -8   -162    250       C  
ATOM   1318  CG  HIS A 160     -16.619  18.376 -18.668  1.00 38.32           C  
ANISOU 1318  CG  HIS A 160     4903   4407   5249     22   -182    305       C  
ATOM   1319  ND1 HIS A 160     -17.299  19.524 -18.326  1.00 42.86           N  
ANISOU 1319  ND1 HIS A 160     5439   4930   5916     61   -145    316       N  
ATOM   1320  CD2 HIS A 160     -17.562  17.473 -19.027  1.00 42.46           C  
ANISOU 1320  CD2 HIS A 160     5403   4971   5758     17   -235    350       C  
ATOM   1321  CE1 HIS A 160     -18.598  19.326 -18.472  1.00 43.63           C  
ANISOU 1321  CE1 HIS A 160     5488   5041   6047     83   -174    374       C  
ATOM   1322  NE2 HIS A 160     -18.782  18.089 -18.898  1.00 43.95           N  
ANISOU 1322  NE2 HIS A 160     5536   5140   6024     54   -232    394       N  
ATOM   1323  N   ASN A 161     -14.559  16.367 -15.980  1.00 13.13           N  
ANISOU 1323  N   ASN A 161     1733   1349   1908    -19   -115    137       N  
ATOM   1324  CA  ASN A 161     -15.149  15.372 -15.085  1.00 14.88           C  
ANISOU 1324  CA  ASN A 161     1915   1627   2112    -10   -110    145       C  
ATOM   1325  C   ASN A 161     -14.664  15.494 -13.647  1.00 16.20           C  
ANISOU 1325  C   ASN A 161     2057   1854   2245      4    -57     85       C  
ATOM   1326  O   ASN A 161     -14.956  14.644 -12.803  1.00 15.97           O  
ANISOU 1326  O   ASN A 161     1993   1887   2188     15    -44    100       O  
ATOM   1327  CB  ASN A 161     -14.880  13.967 -15.613  1.00 15.89           C  
ANISOU 1327  CB  ASN A 161     2063   1775   2200    -36   -146    180       C  
ATOM   1328  CG  ASN A 161     -15.740  13.639 -16.816  1.00 15.72           C  
ANISOU 1328  CG  ASN A 161     2045   1721   2206    -49   -201    231       C  
ATOM   1329  OD1 ASN A 161     -16.784  14.264 -17.030  1.00 15.23           O  
ANISOU 1329  OD1 ASN A 161     1953   1639   2195    -32   -214    261       O  
ATOM   1330  ND2 ASN A 161     -15.323  12.654 -17.595  1.00 14.61           N  
ANISOU 1330  ND2 ASN A 161     1936   1582   2033    -80   -233    239       N  
ATOM   1331  N   VAL A 162     -13.913  16.553 -13.374  1.00 16.77           N  
ANISOU 1331  N   VAL A 162     2139   1912   2319      1    -26     16       N  
ATOM   1332  CA  VAL A 162     -13.517  16.855 -12.009  1.00 17.25           C  
ANISOU 1332  CA  VAL A 162     2168   2043   2343     11     21    -60       C  
ATOM   1333  C   VAL A 162     -14.172  18.162 -11.601  1.00 20.18           C  
ANISOU 1333  C   VAL A 162     2513   2372   2784     33     62   -116       C  
ATOM   1334  O   VAL A 162     -13.653  19.246 -11.870  1.00 23.04           O  
ANISOU 1334  O   VAL A 162     2891   2672   3191     21     82   -170       O  
ATOM   1335  CB  VAL A 162     -11.991  16.957 -11.851  1.00 15.91           C  
ANISOU 1335  CB  VAL A 162     2023   1907   2117    -17     29   -119       C  
ATOM   1336  CG1 VAL A 162     -11.647  17.284 -10.412  1.00 15.41           C  
ANISOU 1336  CG1 VAL A 162     1915   1937   2002     -9     71   -206       C  
ATOM   1337  CG2 VAL A 162     -11.334  15.653 -12.258  1.00 17.71           C  
ANISOU 1337  CG2 VAL A 162     2274   2169   2288    -32     -3    -61       C  
ATOM   1338  N   MET A 163     -15.330  18.045 -10.963  1.00 19.46           N  
ANISOU 1338  N   MET A 163     2375   2307   2712     67     81    -99       N  
ATOM   1339  CA  MET A 163     -16.124  19.202 -10.582  1.00 18.77           C  
ANISOU 1339  CA  MET A 163     2255   2174   2703     96    126   -145       C  
ATOM   1340  C   MET A 163     -15.645  19.817  -9.276  1.00 19.60           C  
ANISOU 1340  C   MET A 163     2334   2344   2771    100    186   -270       C  
ATOM   1341  O   MET A 163     -15.564  19.144  -8.248  1.00 22.52           O  
ANISOU 1341  O   MET A 163     2673   2833   3051    108    200   -289       O  
ATOM   1342  CB  MET A 163     -17.593  18.804 -10.474  1.00 18.93           C  
ANISOU 1342  CB  MET A 163     2231   2200   2762    132    124    -73       C  
ATOM   1343  CG  MET A 163     -18.186  18.469 -11.812  1.00 23.11           C  
ANISOU 1343  CG  MET A 163     2777   2664   3342    126     65     32       C  
ATOM   1344  SD  MET A 163     -18.886  19.966 -12.513  1.00 38.60           S  
ANISOU 1344  SD  MET A 163     4726   4508   5432    155     83     44       S  
ATOM   1345  CE  MET A 163     -20.250  20.171 -11.373  1.00 29.57           C  
ANISOU 1345  CE  MET A 163     3506   3396   4335    207    139     31       C  
ATOM   1346  N   ILE A 164     -15.329  21.105  -9.323  1.00 19.98           N  
ANISOU 1346  N   ILE A 164     2386   2315   2888     93    222   -357       N  
ATOM   1347  CA  ILE A 164     -14.773  21.784  -8.165  1.00 22.66           C  
ANISOU 1347  CA  ILE A 164     2700   2712   3197     85    277   -502       C  
ATOM   1348  C   ILE A 164     -15.621  22.977  -7.737  1.00 27.85           C  
ANISOU 1348  C   ILE A 164     3323   3301   3960    116    344   -579       C  
ATOM   1349  O   ILE A 164     -15.873  23.890  -8.526  1.00 29.22           O  
ANISOU 1349  O   ILE A 164     3508   3334   4261    122    358   -564       O  
ATOM   1350  CB  ILE A 164     -13.330  22.257  -8.445  1.00 21.83           C  
ANISOU 1350  CB  ILE A 164     2628   2583   3084     34    270   -574       C  
ATOM   1351  CG1 ILE A 164     -12.396  21.054  -8.590  1.00 21.19           C  
ANISOU 1351  CG1 ILE A 164     2570   2595   2887      9    217   -519       C  
ATOM   1352  CG2 ILE A 164     -12.839  23.172  -7.332  1.00 23.01           C  
ANISOU 1352  CG2 ILE A 164     2743   2774   3225     18    328   -747       C  
ATOM   1353  CD1 ILE A 164     -11.021  21.393  -9.196  1.00 20.48           C  
ANISOU 1353  CD1 ILE A 164     2515   2465   2802    -40    202   -552       C  
ATOM   1354  N   ASP A 165     -16.076  22.946  -6.486  1.00 28.23           N  
ANISOU 1354  N   ASP A 165     3322   3451   3952    141    389   -654       N  
ATOM   1355  CA  ASP A 165     -16.658  24.115  -5.841  1.00 32.93           C  
ANISOU 1355  CA  ASP A 165     3880   4000   4632    166    468   -770       C  
ATOM   1356  C   ASP A 165     -15.542  24.819  -5.077  1.00 34.19           C  
ANISOU 1356  C   ASP A 165     4035   4204   4754    124    503   -950       C  
ATOM   1357  O   ASP A 165     -15.242  24.473  -3.931  1.00 32.62           O  
ANISOU 1357  O   ASP A 165     3804   4165   4424    120    518  -1036       O  
ATOM   1358  CB  ASP A 165     -17.804  23.724  -4.901  1.00 34.83           C  
ANISOU 1358  CB  ASP A 165     4066   4337   4831    218    505   -760       C  
ATOM   1359  CG  ASP A 165     -18.522  24.931  -4.308  1.00 38.31           C  
ANISOU 1359  CG  ASP A 165     4466   4717   5371    252    594   -878       C  
ATOM   1360  OD1 ASP A 165     -17.967  26.051  -4.317  1.00 39.13           O  
ANISOU 1360  OD1 ASP A 165     4579   4732   5557    229    635  -1004       O  
ATOM   1361  OD2 ASP A 165     -19.653  24.754  -3.818  1.00 38.78           O  
ANISOU 1361  OD2 ASP A 165     4482   4817   5438    303    629   -846       O  
ATOM   1362  N   HIS A 166     -14.940  25.809  -5.723  1.00 34.15           N  
ANISOU 1362  N   HIS A 166     4054   4059   4862     92    517  -1003       N  
ATOM   1363  CA  HIS A 166     -13.755  26.473  -5.198  1.00 34.56           C  
ANISOU 1363  CA  HIS A 166     4102   4134   4897     37    540  -1171       C  
ATOM   1364  C   HIS A 166     -14.020  27.243  -3.903  1.00 39.38           C  
ANISOU 1364  C   HIS A 166     4659   4801   5503     44    619  -1364       C  
ATOM   1365  O   HIS A 166     -13.099  27.478  -3.120  1.00 41.06           O  
ANISOU 1365  O   HIS A 166     4852   5110   5638     -1    629  -1518       O  
ATOM   1366  CB  HIS A 166     -13.185  27.416  -6.260  1.00 34.93           C  
ANISOU 1366  CB  HIS A 166     4180   3995   5098      4    548  -1168       C  
ATOM   1367  CG  HIS A 166     -11.770  27.833  -6.006  1.00 35.68           C  
ANISOU 1367  CG  HIS A 166     4276   4111   5169    -66    550  -1301       C  
ATOM   1368  ND1 HIS A 166     -10.824  26.977  -5.485  1.00 34.74           N  
ANISOU 1368  ND1 HIS A 166     4154   4165   4881   -100    500  -1327       N  
ATOM   1369  CD2 HIS A 166     -11.139  29.014  -6.209  1.00 37.31           C  
ANISOU 1369  CD2 HIS A 166     4479   4188   5511   -109    596  -1411       C  
ATOM   1370  CE1 HIS A 166      -9.672  27.613  -5.375  1.00 35.94           C  
ANISOU 1370  CE1 HIS A 166     4298   4301   5055   -163    510  -1450       C  
ATOM   1371  NE2 HIS A 166      -9.835  28.851  -5.805  1.00 35.96           N  
ANISOU 1371  NE2 HIS A 166     4300   4117   5245   -173    569  -1508       N  
ATOM   1372  N   GLU A 167     -15.272  27.635  -3.681  1.00 42.62           N  
ANISOU 1372  N   GLU A 167     5042   5158   5994    101    675  -1360       N  
ATOM   1373  CA  GLU A 167     -15.636  28.391  -2.483  1.00 48.42           C  
ANISOU 1373  CA  GLU A 167     5725   5939   6732    114    760  -1548       C  
ATOM   1374  C   GLU A 167     -15.469  27.551  -1.223  1.00 48.31           C  
ANISOU 1374  C   GLU A 167     5677   6177   6501    116    750  -1607       C  
ATOM   1375  O   GLU A 167     -14.832  27.981  -0.262  1.00 48.29           O  
ANISOU 1375  O   GLU A 167     5652   6277   6418     75    757  -1746       O  
ATOM   1376  CB  GLU A 167     -17.076  28.909  -2.575  1.00 53.03           C  
ANISOU 1376  CB  GLU A 167     6283   6412   7454    184    825  -1509       C  
ATOM   1377  CG  GLU A 167     -17.543  29.636  -1.318  1.00 58.72           C  
ANISOU 1377  CG  GLU A 167     6958   7193   8160    196    898  -1662       C  
ATOM   1378  CD  GLU A 167     -18.802  30.459  -1.535  1.00 63.19           C  
ANISOU 1378  CD  GLU A 167     7502   7606   8900    254    965  -1627       C  
ATOM   1379  OE1 GLU A 167     -19.117  30.778  -2.701  1.00 63.03           O  
ANISOU 1379  OE1 GLU A 167     7499   7406   9045    276    963  -1514       O  
ATOM   1380  OE2 GLU A 167     -19.476  30.791  -0.536  1.00 66.03           O  
ANISOU 1380  OE2 GLU A 167     7825   8033   9229    281   1017  -1704       O  
ATOM   1381  N   HIS A 168     -16.040  26.352  -1.227  1.00 47.80           N  
ANISOU 1381  N   HIS A 168     5611   6214   6336    155    707  -1443       N  
ATOM   1382  CA  HIS A 168     -15.913  25.458  -0.083  1.00 47.73           C  
ANISOU 1382  CA  HIS A 168     5565   6448   6123    166    698  -1458       C  
ATOM   1383  C   HIS A 168     -14.811  24.435  -0.303  1.00 41.71           C  
ANISOU 1383  C   HIS A 168     4826   5788   5233    128    615  -1372       C  
ATOM   1384  O   HIS A 168     -14.701  23.467   0.449  1.00 39.26           O  
ANISOU 1384  O   HIS A 168     4487   5671   4760    144    596  -1324       O  
ATOM   1385  CB  HIS A 168     -17.238  24.757   0.200  1.00 52.43           C  
ANISOU 1385  CB  HIS A 168     6129   7098   6693    235    718  -1332       C  
ATOM   1386  CG  HIS A 168     -18.349  25.698   0.539  1.00 57.33           C  
ANISOU 1386  CG  HIS A 168     6715   7640   7427    280    807  -1415       C  
ATOM   1387  ND1 HIS A 168     -19.187  26.236  -0.415  1.00 58.35           N  
ANISOU 1387  ND1 HIS A 168     6858   7564   7747    309    822  -1338       N  
ATOM   1388  CD2 HIS A 168     -18.750  26.215   1.724  1.00 60.18           C  
ANISOU 1388  CD2 HIS A 168     7024   8103   7737    305    888  -1568       C  
ATOM   1389  CE1 HIS A 168     -20.061  27.034   0.169  1.00 60.43           C  
ANISOU 1389  CE1 HIS A 168     7079   7797   8086    352    913  -1435       C  
ATOM   1390  NE2 HIS A 168     -19.818  27.039   1.468  1.00 62.03           N  
ANISOU 1390  NE2 HIS A 168     7247   8180   8142    348    951  -1574       N  
ATOM   1391  N   ARG A 169     -14.000  24.674  -1.334  1.00 38.94           N  
ANISOU 1391  N   ARG A 169     4524   5306   4964     82    572  -1348       N  
ATOM   1392  CA  ARG A 169     -12.871  23.818  -1.682  1.00 37.15           C  
ANISOU 1392  CA  ARG A 169     4323   5149   4643     45    499  -1273       C  
ATOM   1393  C   ARG A 169     -13.285  22.351  -1.711  1.00 34.66           C  
ANISOU 1393  C   ARG A 169     4006   4931   4231     83    456  -1088       C  
ATOM   1394  O   ARG A 169     -12.629  21.487  -1.127  1.00 35.85           O  
ANISOU 1394  O   ARG A 169     4136   5249   4236     78    427  -1059       O  
ATOM   1395  CB  ARG A 169     -11.714  24.053  -0.708  1.00 39.82           C  
ANISOU 1395  CB  ARG A 169     4625   5647   4857      0    500  -1435       C  
ATOM   1396  CG  ARG A 169     -11.434  25.533  -0.479  1.00 42.88           C  
ANISOU 1396  CG  ARG A 169     5001   5945   5348    -41    554  -1644       C  
ATOM   1397  CD  ARG A 169     -10.011  25.787  -0.008  1.00 49.69           C  
ANISOU 1397  CD  ARG A 169     5843   6896   6141   -113    509  -1718       C  
ATOM   1398  NE  ARG A 169      -9.066  25.829  -1.122  1.00 54.09           N  
ANISOU 1398  NE  ARG A 169     6443   7338   6773   -157    474  -1683       N  
ATOM   1399  CZ  ARG A 169      -7.748  25.704  -0.997  1.00 55.91           C  
ANISOU 1399  CZ  ARG A 169     6658   7648   6938   -211    426  -1701       C  
ATOM   1400  NH1 ARG A 169      -7.204  25.531   0.200  1.00 57.20           N  
ANISOU 1400  NH1 ARG A 169     6762   8009   6964   -227    404  -1753       N  
ATOM   1401  NH2 ARG A 169      -6.972  25.753  -2.069  1.00 55.51           N  
ANISOU 1401  NH2 ARG A 169     6647   7482   6962   -248    401  -1659       N  
ATOM   1402  N   LYS A 170     -14.391  22.099  -2.402  1.00 31.50           N  
ANISOU 1402  N   LYS A 170     3623   4421   3925    121    455   -961       N  
ATOM   1403  CA  LYS A 170     -15.004  20.781  -2.495  1.00 31.83           C  
ANISOU 1403  CA  LYS A 170     3658   4522   3915    155    424   -790       C  
ATOM   1404  C   LYS A 170     -14.865  20.218  -3.906  1.00 25.65           C  
ANISOU 1404  C   LYS A 170     2930   3611   3203    137    360   -651       C  
ATOM   1405  O   LYS A 170     -15.075  20.929  -4.886  1.00 27.64           O  
ANISOU 1405  O   LYS A 170     3216   3704   3581    128    354   -646       O  
ATOM   1406  CB  LYS A 170     -16.477  20.872  -2.092  1.00 36.06           C  
ANISOU 1406  CB  LYS A 170     4154   5053   4495    210    473   -761       C  
ATOM   1407  CG  LYS A 170     -17.409  19.873  -2.760  1.00 38.88           C  
ANISOU 1407  CG  LYS A 170     4514   5363   4895    236    440   -577       C  
ATOM   1408  CD  LYS A 170     -18.869  20.129  -2.365  1.00 44.32           C  
ANISOU 1408  CD  LYS A 170     5154   6040   5644    289    494   -560       C  
ATOM   1409  CE  LYS A 170     -19.134  21.605  -2.072  1.00 48.82           C  
ANISOU 1409  CE  LYS A 170     5712   6540   6296    300    561   -713       C  
ATOM   1410  NZ  LYS A 170     -20.257  21.806  -1.106  1.00 52.62           N  
ANISOU 1410  NZ  LYS A 170     6129   7092   6772    355    635   -744       N  
ATOM   1411  N   LEU A 171     -14.508  18.943  -4.005  1.00 19.29           N  
ANISOU 1411  N   LEU A 171     2131   2880   2318    135    317   -539       N  
ATOM   1412  CA  LEU A 171     -14.243  18.326  -5.300  1.00 16.86           C  
ANISOU 1412  CA  LEU A 171     1876   2470   2062    114    258   -427       C  
ATOM   1413  C   LEU A 171     -15.014  17.026  -5.459  1.00 18.91           C  
ANISOU 1413  C   LEU A 171     2122   2750   2312    139    237   -280       C  
ATOM   1414  O   LEU A 171     -15.126  16.246  -4.509  1.00 20.51           O  
ANISOU 1414  O   LEU A 171     2280   3083   2429    162    255   -243       O  
ATOM   1415  CB  LEU A 171     -12.734  18.080  -5.463  1.00 19.22           C  
ANISOU 1415  CB  LEU A 171     2201   2809   2294     73    226   -452       C  
ATOM   1416  CG  LEU A 171     -12.210  17.484  -6.774  1.00 19.24           C  
ANISOU 1416  CG  LEU A 171     2259   2718   2332     48    172   -360       C  
ATOM   1417  CD1 LEU A 171     -10.800  17.986  -7.050  1.00 15.87           C  
ANISOU 1417  CD1 LEU A 171     1858   2282   1889      4    160   -433       C  
ATOM   1418  CD2 LEU A 171     -12.222  15.955  -6.736  1.00 18.30           C  
ANISOU 1418  CD2 LEU A 171     2132   2665   2156     62    148   -237       C  
ATOM   1419  N   ARG A 172     -15.542  16.793  -6.662  1.00 16.89           N  
ANISOU 1419  N   ARG A 172     1900   2371   2147    132    199   -196       N  
ATOM   1420  CA  ARG A 172     -16.232  15.546  -6.977  1.00 13.79           C  
ANISOU 1420  CA  ARG A 172     1496   1979   1766    142    173    -68       C  
ATOM   1421  C   ARG A 172     -15.812  15.004  -8.342  1.00 14.33           C  
ANISOU 1421  C   ARG A 172     1619   1955   1870    108    113     -6       C  
ATOM   1422  O   ARG A 172     -15.783  15.736  -9.338  1.00 16.82           O  
ANISOU 1422  O   ARG A 172     1973   2169   2248     91     90    -23       O  
ATOM   1423  CB  ARG A 172     -17.755  15.744  -6.953  1.00 16.11           C  
ANISOU 1423  CB  ARG A 172     1750   2234   2137    174    191    -28       C  
ATOM   1424  CG  ARG A 172     -18.321  16.094  -5.578  1.00 18.36           C  
ANISOU 1424  CG  ARG A 172     1973   2620   2382    214    258    -77       C  
ATOM   1425  CD  ARG A 172     -18.201  14.932  -4.608  1.00 20.91           C  
ANISOU 1425  CD  ARG A 172     2253   3083   2607    230    276    -14       C  
ATOM   1426  NE  ARG A 172     -18.847  15.208  -3.322  1.00 20.55           N  
ANISOU 1426  NE  ARG A 172     2144   3150   2513    273    343    -48       N  
ATOM   1427  CZ  ARG A 172     -18.225  15.724  -2.267  1.00 24.50           C  
ANISOU 1427  CZ  ARG A 172     2623   3774   2910    282    383   -152       C  
ATOM   1428  NH1 ARG A 172     -16.935  16.024  -2.332  1.00 26.34           N  
ANISOU 1428  NH1 ARG A 172     2892   4029   3087    249    359   -230       N  
ATOM   1429  NH2 ARG A 172     -18.892  15.935  -1.142  1.00 28.56           N  
ANISOU 1429  NH2 ARG A 172     3078   4400   3375    323    446   -183       N  
ATOM   1430  N   LEU A 173     -15.502  13.714  -8.382  1.00 13.50           N  
ANISOU 1430  N   LEU A 173     1514   1887   1729    101     95     69       N  
ATOM   1431  CA  LEU A 173     -15.238  13.023  -9.638  1.00 15.67           C  
ANISOU 1431  CA  LEU A 173     1835   2082   2038     70     44    124       C  
ATOM   1432  C   LEU A 173     -16.559  12.512 -10.229  1.00 15.66           C  
ANISOU 1432  C   LEU A 173     1815   2022   2114     72     21    197       C  
ATOM   1433  O   LEU A 173     -17.247  11.699  -9.608  1.00 16.44           O  
ANISOU 1433  O   LEU A 173     1864   2163   2220     88     40    256       O  
ATOM   1434  CB  LEU A 173     -14.257  11.874  -9.405  1.00 16.77           C  
ANISOU 1434  CB  LEU A 173     1977   2276   2117     62     43    163       C  
ATOM   1435  CG  LEU A 173     -13.792  11.057 -10.610  1.00 19.04           C  
ANISOU 1435  CG  LEU A 173     2312   2491   2432     31      3    203       C  
ATOM   1436  CD1 LEU A 173     -13.200  11.964 -11.683  1.00 18.30           C  
ANISOU 1436  CD1 LEU A 173     2277   2326   2348      4    -27    148       C  
ATOM   1437  CD2 LEU A 173     -12.771  10.005 -10.179  1.00 15.47           C  
ANISOU 1437  CD2 LEU A 173     1852   2096   1929     34     18    239       C  
ATOM   1438  N   ILE A 174     -16.906  12.993 -11.422  1.00 15.18           N  
ANISOU 1438  N   ILE A 174     1785   1872   2109     54    -20    199       N  
ATOM   1439  CA  ILE A 174     -18.212  12.705 -12.021  1.00 17.53           C  
ANISOU 1439  CA  ILE A 174     2056   2125   2479     53    -50    258       C  
ATOM   1440  C   ILE A 174     -18.118  11.883 -13.309  1.00 16.90           C  
ANISOU 1440  C   ILE A 174     2011   1995   2415     14   -109    293       C  
ATOM   1441  O   ILE A 174     -17.028  11.495 -13.734  1.00 14.65           O  
ANISOU 1441  O   ILE A 174     1774   1705   2087     -9   -121    275       O  
ATOM   1442  CB  ILE A 174     -18.978  14.008 -12.334  1.00 18.26           C  
ANISOU 1442  CB  ILE A 174     2138   2171   2629     74    -50    241       C  
ATOM   1443  CG1 ILE A 174     -18.247  14.815 -13.412  1.00 17.22           C  
ANISOU 1443  CG1 ILE A 174     2065   1978   2499     55    -79    214       C  
ATOM   1444  CG2 ILE A 174     -19.165  14.851 -11.067  1.00 12.57           C  
ANISOU 1444  CG2 ILE A 174     1380   1493   1903    113     16    187       C  
ATOM   1445  CD1 ILE A 174     -19.130  15.851 -14.121  1.00 14.70           C  
ANISOU 1445  CD1 ILE A 174     1732   1597   2257     74    -94    239       C  
ATOM   1446  N   ASP A 175     -19.280  11.638 -13.918  1.00 16.42           N  
ANISOU 1446  N   ASP A 175     1921   1905   2415      5   -145    336       N  
ATOM   1447  CA  ASP A 175     -19.439  10.877 -15.166  1.00 15.05           C  
ANISOU 1447  CA  ASP A 175     1767   1694   2258    -36   -207    357       C  
ATOM   1448  C   ASP A 175     -18.731   9.526 -15.168  1.00 14.20           C  
ANISOU 1448  C   ASP A 175     1676   1586   2131    -65   -203    359       C  
ATOM   1449  O   ASP A 175     -17.681   9.350 -15.805  1.00 16.45           O  
ANISOU 1449  O   ASP A 175     2019   1857   2373    -85   -216    329       O  
ATOM   1450  CB  ASP A 175     -18.975  11.699 -16.373  1.00 15.60           C  
ANISOU 1450  CB  ASP A 175     1890   1731   2304    -49   -248    336       C  
ATOM   1451  CG  ASP A 175     -19.646  11.249 -17.674  1.00 26.43           C  
ANISOU 1451  CG  ASP A 175     3260   3089   3695    -83   -318    360       C  
ATOM   1452  OD1 ASP A 175     -20.213  10.135 -17.698  1.00 29.63           O  
ANISOU 1452  OD1 ASP A 175     3632   3495   4131   -109   -335    374       O  
ATOM   1453  OD2 ASP A 175     -19.614  12.009 -18.664  1.00 28.23           O  
ANISOU 1453  OD2 ASP A 175     3513   3307   3908    -84   -354    367       O  
ATOM   1454  N   TRP A 176     -19.337   8.571 -14.470  1.00 11.76           N  
ANISOU 1454  N   TRP A 176     1313   1289   1865    -63   -179    400       N  
ATOM   1455  CA  TRP A 176     -18.826   7.211 -14.381  1.00 13.75           C  
ANISOU 1455  CA  TRP A 176     1567   1528   2129    -85   -163    418       C  
ATOM   1456  C   TRP A 176     -19.390   6.330 -15.491  1.00 15.73           C  
ANISOU 1456  C   TRP A 176     1814   1723   2439   -136   -213    414       C  
ATOM   1457  O   TRP A 176     -19.384   5.107 -15.378  1.00 17.60           O  
ANISOU 1457  O   TRP A 176     2029   1930   2727   -157   -195    434       O  
ATOM   1458  CB  TRP A 176     -19.147   6.623 -12.999  1.00 14.82           C  
ANISOU 1458  CB  TRP A 176     1639   1706   2287    -54   -101    477       C  
ATOM   1459  CG  TRP A 176     -18.444   7.392 -11.931  1.00 15.57           C  
ANISOU 1459  CG  TRP A 176     1737   1876   2303     -9    -55    463       C  
ATOM   1460  CD1 TRP A 176     -18.824   8.596 -11.398  1.00 16.36           C  
ANISOU 1460  CD1 TRP A 176     1823   2016   2378     22    -40    436       C  
ATOM   1461  CD2 TRP A 176     -17.194   7.060 -11.311  1.00 16.37           C  
ANISOU 1461  CD2 TRP A 176     1856   2024   2340      7    -19    464       C  
ATOM   1462  NE1 TRP A 176     -17.898   9.016 -10.467  1.00 16.09           N  
ANISOU 1462  NE1 TRP A 176     1796   2055   2264     50      2    407       N  
ATOM   1463  CE2 TRP A 176     -16.889   8.089 -10.397  1.00 16.51           C  
ANISOU 1463  CE2 TRP A 176     1866   2121   2287     41     11    429       C  
ATOM   1464  CE3 TRP A 176     -16.311   5.983 -11.431  1.00 15.65           C  
ANISOU 1464  CE3 TRP A 176     1778   1917   2250     -4     -7    490       C  
ATOM   1465  CZ2 TRP A 176     -15.735   8.077  -9.609  1.00 15.61           C  
ANISOU 1465  CZ2 TRP A 176     1754   2084   2091     61     43    419       C  
ATOM   1466  CZ3 TRP A 176     -15.165   5.974 -10.647  1.00 17.84           C  
ANISOU 1466  CZ3 TRP A 176     2059   2268   2454     23     29    495       C  
ATOM   1467  CH2 TRP A 176     -14.890   7.013  -9.748  1.00 15.64           C  
ANISOU 1467  CH2 TRP A 176     1768   2081   2093     54     49    459       C  
ATOM   1468  N   GLY A 177     -19.856   6.961 -16.567  1.00 16.84           N  
ANISOU 1468  N   GLY A 177     1972   1852   2574   -156   -275    388       N  
ATOM   1469  CA  GLY A 177     -20.455   6.242 -17.683  1.00 17.80           C  
ANISOU 1469  CA  GLY A 177     2084   1944   2737   -209   -333    369       C  
ATOM   1470  C   GLY A 177     -19.492   5.395 -18.503  1.00 20.19           C  
ANISOU 1470  C   GLY A 177     2442   2214   3016   -248   -343    317       C  
ATOM   1471  O   GLY A 177     -19.919   4.489 -19.224  1.00 19.40           O  
ANISOU 1471  O   GLY A 177     2326   2082   2961   -298   -376    288       O  
ATOM   1472  N   LEU A 178     -18.195   5.682 -18.411  1.00 15.25           N  
ANISOU 1472  N   LEU A 178     1877   1595   2324   -228   -314    298       N  
ATOM   1473  CA  LEU A 178     -17.199   4.869 -19.107  1.00 17.29           C  
ANISOU 1473  CA  LEU A 178     2186   1822   2563   -257   -311    251       C  
ATOM   1474  C   LEU A 178     -16.460   3.925 -18.153  1.00 18.15           C  
ANISOU 1474  C   LEU A 178     2284   1908   2706   -239   -241    277       C  
ATOM   1475  O   LEU A 178     -15.646   3.110 -18.583  1.00 18.00           O  
ANISOU 1475  O   LEU A 178     2296   1852   2693   -256   -224    246       O  
ATOM   1476  CB  LEU A 178     -16.183   5.754 -19.840  1.00 19.85           C  
ANISOU 1476  CB  LEU A 178     2580   2168   2793   -249   -326    216       C  
ATOM   1477  CG  LEU A 178     -16.679   6.472 -21.093  1.00 22.81           C  
ANISOU 1477  CG  LEU A 178     2973   2567   3127   -270   -395    195       C  
ATOM   1478  CD1 LEU A 178     -15.517   7.083 -21.864  1.00 21.75           C  
ANISOU 1478  CD1 LEU A 178     2908   2447   2907   -266   -396    168       C  
ATOM   1479  CD2 LEU A 178     -17.471   5.515 -21.972  1.00 26.61           C  
ANISOU 1479  CD2 LEU A 178     3431   3036   3643   -323   -444    158       C  
ATOM   1480  N   ALA A 179     -16.759   4.023 -16.862  1.00 18.49           N  
ANISOU 1480  N   ALA A 179     2277   1978   2770   -201   -197    339       N  
ATOM   1481  CA  ALA A 179     -16.045   3.236 -15.856  1.00 17.23           C  
ANISOU 1481  CA  ALA A 179     2098   1821   2628   -172   -130    387       C  
ATOM   1482  C   ALA A 179     -16.315   1.739 -15.982  1.00 17.19           C  
ANISOU 1482  C   ALA A 179     2060   1742   2730   -201   -106    406       C  
ATOM   1483  O   ALA A 179     -17.380   1.326 -16.439  1.00 18.23           O  
ANISOU 1483  O   ALA A 179     2159   1833   2937   -241   -135    394       O  
ATOM   1484  CB  ALA A 179     -16.407   3.723 -14.456  1.00 17.15           C  
ANISOU 1484  CB  ALA A 179     2035   1878   2602   -124    -90    449       C  
ATOM   1485  N   GLU A 180     -15.345   0.929 -15.567  1.00 15.20           N  
ANISOU 1485  N   GLU A 180     1810   1470   2495   -182    -51    436       N  
ATOM   1486  CA  GLU A 180     -15.458  -0.527 -15.664  1.00 18.11           C  
ANISOU 1486  CA  GLU A 180     2145   1749   2985   -205    -13    457       C  
ATOM   1487  C   GLU A 180     -14.828  -1.241 -14.477  1.00 18.74           C  
ANISOU 1487  C   GLU A 180     2182   1840   3098   -153     68    560       C  
ATOM   1488  O   GLU A 180     -13.916  -0.713 -13.829  1.00 18.89           O  
ANISOU 1488  O   GLU A 180     2214   1938   3024   -106     89    590       O  
ATOM   1489  CB  GLU A 180     -14.795  -1.046 -16.944  1.00 21.08           C  
ANISOU 1489  CB  GLU A 180     2580   2055   3373   -246    -30    364       C  
ATOM   1490  CG  GLU A 180     -15.744  -1.409 -18.065  1.00 24.35           C  
ANISOU 1490  CG  GLU A 180     2994   2413   3847   -316    -84    282       C  
ATOM   1491  CD  GLU A 180     -16.463  -2.737 -17.851  1.00 25.40           C  
ANISOU 1491  CD  GLU A 180     3060   2451   4142   -347    -45    305       C  
ATOM   1492  OE1 GLU A 180     -16.504  -3.246 -16.711  1.00 24.25           O  
ANISOU 1492  OE1 GLU A 180     2858   2293   4065   -309     21    412       O  
ATOM   1493  OE2 GLU A 180     -16.994  -3.273 -18.843  1.00 27.56           O  
ANISOU 1493  OE2 GLU A 180     3332   2665   4474   -412    -81    216       O  
ATOM   1494  N   PHE A 181     -15.302  -2.456 -14.217  1.00 16.61           N  
ANISOU 1494  N   PHE A 181     1855   1492   2964   -164    115    616       N  
ATOM   1495  CA  PHE A 181     -14.697  -3.330 -13.224  1.00 15.82           C  
ANISOU 1495  CA  PHE A 181     1707   1388   2917   -114    199    731       C  
ATOM   1496  C   PHE A 181     -13.399  -3.938 -13.749  1.00 17.37           C  
ANISOU 1496  C   PHE A 181     1946   1529   3127   -108    228    702       C  
ATOM   1497  O   PHE A 181     -13.347  -4.415 -14.884  1.00 19.58           O  
ANISOU 1497  O   PHE A 181     2264   1711   3467   -159    210    606       O  
ATOM   1498  CB  PHE A 181     -15.676  -4.444 -12.841  1.00 19.40           C  
ANISOU 1498  CB  PHE A 181     2078   1757   3534   -130    247    808       C  
ATOM   1499  CG  PHE A 181     -16.904  -3.952 -12.138  1.00 18.63           C  
ANISOU 1499  CG  PHE A 181     1924   1723   3431   -124    237    861       C  
ATOM   1500  CD1 PHE A 181     -18.007  -3.519 -12.860  1.00 20.09           C  
ANISOU 1500  CD1 PHE A 181     2113   1886   3635   -180    171    782       C  
ATOM   1501  CD2 PHE A 181     -16.960  -3.921 -10.754  1.00 20.56           C  
ANISOU 1501  CD2 PHE A 181     2106   2060   3647    -60    294    994       C  
ATOM   1502  CE1 PHE A 181     -19.148  -3.055 -12.215  1.00 21.00           C  
ANISOU 1502  CE1 PHE A 181     2169   2057   3752   -170    166    833       C  
ATOM   1503  CE2 PHE A 181     -18.100  -3.466 -10.103  1.00 20.07           C  
ANISOU 1503  CE2 PHE A 181     1988   2058   3578    -52    292   1039       C  
ATOM   1504  CZ  PHE A 181     -19.189  -3.027 -10.837  1.00 20.42           C  
ANISOU 1504  CZ  PHE A 181     2038   2068   3653   -106    230    959       C  
ATOM   1505  N   TYR A 182     -12.354  -3.935 -12.928  1.00 16.86           N  
ANISOU 1505  N   TYR A 182     1868   1533   3005    -46    273    782       N  
ATOM   1506  CA  TYR A 182     -11.109  -4.563 -13.335  1.00 18.26           C  
ANISOU 1506  CA  TYR A 182     2073   1659   3207    -31    309    772       C  
ATOM   1507  C   TYR A 182     -11.115  -6.052 -12.987  1.00 21.94           C  
ANISOU 1507  C   TYR A 182     2475   2023   3840    -13    393    863       C  
ATOM   1508  O   TYR A 182     -11.336  -6.436 -11.837  1.00 22.46           O  
ANISOU 1508  O   TYR A 182     2464   2155   3915     39    435    975       O  
ATOM   1509  CB  TYR A 182      -9.893  -3.889 -12.692  1.00 18.17           C  
ANISOU 1509  CB  TYR A 182     2071   1774   3060     26    315    812       C  
ATOM   1510  CG  TYR A 182      -8.629  -4.641 -13.038  1.00 18.33           C  
ANISOU 1510  CG  TYR A 182     2104   1739   3122     49    362    821       C  
ATOM   1511  CD1 TYR A 182      -8.100  -4.587 -14.320  1.00 16.40           C  
ANISOU 1511  CD1 TYR A 182     1933   1426   2872      9    337    697       C  
ATOM   1512  CD2 TYR A 182      -8.003  -5.458 -12.105  1.00 20.56           C  
ANISOU 1512  CD2 TYR A 182     2319   2040   3455    112    437    961       C  
ATOM   1513  CE1 TYR A 182      -6.955  -5.304 -14.654  1.00 17.06           C  
ANISOU 1513  CE1 TYR A 182     2024   1454   3003     33    389    702       C  
ATOM   1514  CE2 TYR A 182      -6.869  -6.178 -12.429  1.00 21.18           C  
ANISOU 1514  CE2 TYR A 182     2400   2066   3582    138    483    970       C  
ATOM   1515  CZ  TYR A 182      -6.352  -6.101 -13.704  1.00 17.24           C  
ANISOU 1515  CZ  TYR A 182     1978   1486   3087     98    464    842       C  
ATOM   1516  OH  TYR A 182      -5.222  -6.823 -14.025  1.00 20.48           O  
ANISOU 1516  OH  TYR A 182     2388   1836   3555    128    520    856       O  
ATOM   1517  N   HIS A 183     -10.871  -6.883 -13.994  1.00 19.41           N  
ANISOU 1517  N   HIS A 183     2183   1582   3612    -48    406    773       N  
ATOM   1518  CA  HIS A 183     -10.737  -8.322 -13.805  1.00 21.94           C  
ANISOU 1518  CA  HIS A 183     2446   1829   4062    -25    477    807       C  
ATOM   1519  C   HIS A 183      -9.414  -8.755 -14.417  1.00 24.99           C  
ANISOU 1519  C   HIS A 183     2870   2167   4457     -8    510    764       C  
ATOM   1520  O   HIS A 183      -9.152  -8.456 -15.587  1.00 25.32           O  
ANISOU 1520  O   HIS A 183     2988   2153   4478    -58    476    637       O  
ATOM   1521  CB  HIS A 183     -11.898  -9.085 -14.452  1.00 24.97           C  
ANISOU 1521  CB  HIS A 183     2812   2103   4574    -89    469    728       C  
ATOM   1522  CG  HIS A 183     -13.242  -8.785 -13.853  1.00 26.61           C  
ANISOU 1522  CG  HIS A 183     2969   2348   4792   -104    445    777       C  
ATOM   1523  ND1 HIS A 183     -13.672  -9.350 -12.670  1.00 27.10           N  
ANISOU 1523  ND1 HIS A 183     2940   2446   4909    -52    498    906       N  
ATOM   1524  CD2 HIS A 183     -14.250  -7.994 -14.283  1.00 25.33           C  
ANISOU 1524  CD2 HIS A 183     2828   2196   4599   -161    375    716       C  
ATOM   1525  CE1 HIS A 183     -14.888  -8.910 -12.396  1.00 26.37           C  
ANISOU 1525  CE1 HIS A 183     2819   2382   4817    -77    465    921       C  
ATOM   1526  NE2 HIS A 183     -15.264  -8.089 -13.354  1.00 25.34           N  
ANISOU 1526  NE2 HIS A 183     2754   2237   4639   -143    390    809       N  
ATOM   1527  N   PRO A 184      -8.575  -9.450 -13.632  1.00 24.53           N  
ANISOU 1527  N   PRO A 184     2755   2138   4429     63    578    870       N  
ATOM   1528  CA  PRO A 184      -7.234  -9.834 -14.087  1.00 23.76           C  
ANISOU 1528  CA  PRO A 184     2681   2007   4341     90    618    849       C  
ATOM   1529  C   PRO A 184      -7.272 -10.505 -15.452  1.00 22.70           C  
ANISOU 1529  C   PRO A 184     2595   1728   4300     31    626    701       C  
ATOM   1530  O   PRO A 184      -7.985 -11.501 -15.629  1.00 24.86           O  
ANISOU 1530  O   PRO A 184     2830   1911   4703      6    655    673       O  
ATOM   1531  CB  PRO A 184      -6.762 -10.813 -13.007  1.00 26.28           C  
ANISOU 1531  CB  PRO A 184     2899   2357   4731    168    698    992       C  
ATOM   1532  CG  PRO A 184      -7.526 -10.429 -11.797  1.00 28.49           C  
ANISOU 1532  CG  PRO A 184     3117   2749   4959    196    684   1101       C  
ATOM   1533  CD  PRO A 184      -8.870  -9.966 -12.284  1.00 25.40           C  
ANISOU 1533  CD  PRO A 184     2763   2315   4573    124    626   1017       C  
ATOM   1534  N   GLY A 185      -6.547  -9.923 -16.401  1.00 23.60           N  
ANISOU 1534  N   GLY A 185     2792   1830   4344      8    599    601       N  
ATOM   1535  CA  GLY A 185      -6.392 -10.465 -17.736  1.00 25.73           C  
ANISOU 1535  CA  GLY A 185     3114   1990   4671    -42    606    448       C  
ATOM   1536  C   GLY A 185      -7.572 -10.283 -18.676  1.00 26.61           C  
ANISOU 1536  C   GLY A 185     3266   2055   4788   -131    541    309       C  
ATOM   1537  O   GLY A 185      -7.598 -10.864 -19.763  1.00 26.50           O  
ANISOU 1537  O   GLY A 185     3285   1963   4822   -178    546    172       O  
ATOM   1538  N   GLN A 186      -8.554  -9.490 -18.265  1.00 26.77           N  
ANISOU 1538  N   GLN A 186     3280   2136   4756   -155    480    340       N  
ATOM   1539  CA  GLN A 186      -9.659  -9.147 -19.151  1.00 29.28           C  
ANISOU 1539  CA  GLN A 186     3631   2432   5062   -238    406    216       C  
ATOM   1540  C   GLN A 186      -9.175  -8.152 -20.209  1.00 27.22           C  
ANISOU 1540  C   GLN A 186     3460   2201   4683   -274    350    101       C  
ATOM   1541  O   GLN A 186      -8.346  -7.288 -19.924  1.00 24.38           O  
ANISOU 1541  O   GLN A 186     3129   1937   4196   -229    338    148       O  
ATOM   1542  CB  GLN A 186     -10.831  -8.569 -18.348  1.00 30.28           C  
ANISOU 1542  CB  GLN A 186     3714   2618   5175   -246    364    296       C  
ATOM   1543  CG  GLN A 186     -12.135  -8.414 -19.124  1.00 32.19           C  
ANISOU 1543  CG  GLN A 186     3960   2837   5432   -329    292    188       C  
ATOM   1544  CD  GLN A 186     -13.343  -8.247 -18.209  1.00 36.60           C  
ANISOU 1544  CD  GLN A 186     4451   3432   6025   -327    277    283       C  
ATOM   1545  OE1 GLN A 186     -14.142  -7.321 -18.370  1.00 40.03           O  
ANISOU 1545  OE1 GLN A 186     4892   3915   6404   -364    205    263       O  
ATOM   1546  NE2 GLN A 186     -13.480  -9.149 -17.245  1.00 36.45           N  
ANISOU 1546  NE2 GLN A 186     4358   3392   6101   -282    348    391       N  
ATOM   1547  N   GLU A 187      -9.678  -8.284 -21.432  1.00 26.87           N  
ANISOU 1547  N   GLU A 187     3453   2124   4633   -347    305    -55       N  
ATOM   1548  CA  GLU A 187      -9.346  -7.333 -22.492  1.00 26.80           C  
ANISOU 1548  CA  GLU A 187     3522   2196   4465   -373    237   -165       C  
ATOM   1549  C   GLU A 187     -10.455  -6.296 -22.626  1.00 23.77           C  
ANISOU 1549  C   GLU A 187     3141   1912   3980   -409    136   -175       C  
ATOM   1550  O   GLU A 187     -11.635  -6.647 -22.669  1.00 24.71           O  
ANISOU 1550  O   GLU A 187     3218   1993   4178   -459    107   -200       O  
ATOM   1551  CB  GLU A 187      -9.117  -8.053 -23.823  1.00 30.51           C  
ANISOU 1551  CB  GLU A 187     4031   2592   4969   -427    251   -334       C  
ATOM   1552  CG  GLU A 187      -7.886  -8.950 -23.828  1.00 35.70           C  
ANISOU 1552  CG  GLU A 187     4692   3186   5688   -377    346   -328       C  
ATOM   1553  CD  GLU A 187      -7.494  -9.404 -25.221  1.00 41.13           C  
ANISOU 1553  CD  GLU A 187     5430   3856   6343   -415    350   -498       C  
ATOM   1554  OE1 GLU A 187      -8.390  -9.571 -26.075  1.00 42.52           O  
ANISOU 1554  OE1 GLU A 187     5612   4043   6501   -483    292   -617       O  
ATOM   1555  OE2 GLU A 187      -6.282  -9.583 -25.465  1.00 42.53           O  
ANISOU 1555  OE2 GLU A 187     5635   4019   6506   -374    410   -509       O  
ATOM   1556  N   TYR A 188     -10.073  -5.021 -22.681  1.00 18.78           N  
ANISOU 1556  N   TYR A 188     2553   1400   3184   -383     85   -152       N  
ATOM   1557  CA  TYR A 188     -11.043  -3.929 -22.679  1.00 19.51           C  
ANISOU 1557  CA  TYR A 188     2642   1585   3186   -400      0   -138       C  
ATOM   1558  C   TYR A 188     -11.030  -3.134 -23.974  1.00 21.44           C  
ANISOU 1558  C   TYR A 188     2948   1905   3295   -435    -72   -238       C  
ATOM   1559  O   TYR A 188     -10.066  -3.178 -24.735  1.00 21.92           O  
ANISOU 1559  O   TYR A 188     3061   1972   3297   -432    -54   -301       O  
ATOM   1560  CB  TYR A 188     -10.782  -2.982 -21.499  1.00 19.75           C  
ANISOU 1560  CB  TYR A 188     2658   1695   3153   -338      4    -13       C  
ATOM   1561  CG  TYR A 188     -10.966  -3.641 -20.158  1.00 21.20           C  
ANISOU 1561  CG  TYR A 188     2772   1838   3445   -300     65    102       C  
ATOM   1562  CD1 TYR A 188     -12.225  -3.730 -19.581  1.00 23.16           C  
ANISOU 1562  CD1 TYR A 188     2960   2079   3759   -315     49    150       C  
ATOM   1563  CD2 TYR A 188      -9.887  -4.187 -19.470  1.00 19.71           C  
ANISOU 1563  CD2 TYR A 188     2569   1627   3294   -247    142    174       C  
ATOM   1564  CE1 TYR A 188     -12.409  -4.339 -18.360  1.00 22.87           C  
ANISOU 1564  CE1 TYR A 188     2855   2016   3817   -278    110    267       C  
ATOM   1565  CE2 TYR A 188     -10.063  -4.808 -18.246  1.00 20.91           C  
ANISOU 1565  CE2 TYR A 188     2649   1757   3540   -207    201    296       C  
ATOM   1566  CZ  TYR A 188     -11.332  -4.876 -17.696  1.00 22.45           C  
ANISOU 1566  CZ  TYR A 188     2789   1948   3794   -223    186    343       C  
ATOM   1567  OH  TYR A 188     -11.532  -5.488 -16.478  1.00 21.39           O  
ANISOU 1567  OH  TYR A 188     2579   1801   3747   -181    249    476       O  
ATOM   1568  N   ASN A 189     -12.111  -2.398 -24.206  1.00 17.95           N  
ANISOU 1568  N   ASN A 189     2492   1525   2802   -462   -151   -241       N  
ATOM   1569  CA  ASN A 189     -12.211  -1.485 -25.339  1.00 17.70           C  
ANISOU 1569  CA  ASN A 189     2507   1585   2633   -485   -224   -301       C  
ATOM   1570  C   ASN A 189     -11.213  -0.338 -25.197  1.00 16.15           C  
ANISOU 1570  C   ASN A 189     2357   1458   2321   -432   -217   -244       C  
ATOM   1571  O   ASN A 189     -11.145   0.298 -24.146  1.00 19.28           O  
ANISOU 1571  O   ASN A 189     2734   1873   2717   -389   -203   -150       O  
ATOM   1572  CB  ASN A 189     -13.642  -0.956 -25.436  1.00 22.69           C  
ANISOU 1572  CB  ASN A 189     3097   2267   3257   -515   -303   -289       C  
ATOM   1573  CG  ASN A 189     -13.871  -0.076 -26.643  1.00 29.41           C  
ANISOU 1573  CG  ASN A 189     3983   3220   3973   -537   -382   -336       C  
ATOM   1574  OD1 ASN A 189     -13.014   0.057 -27.514  1.00 30.26           O  
ANISOU 1574  OD1 ASN A 189     4146   3362   3990   -537   -378   -391       O  
ATOM   1575  ND2 ASN A 189     -15.053   0.524 -26.707  1.00 35.76           N  
ANISOU 1575  ND2 ASN A 189     4745   4077   4763   -551   -451   -306       N  
ATOM   1576  N   VAL A 190     -10.431  -0.070 -26.240  1.00 18.95           N  
ANISOU 1576  N   VAL A 190     2768   1853   2578   -438   -222   -306       N  
ATOM   1577  CA  VAL A 190      -9.438   1.001 -26.143  1.00 18.74           C  
ANISOU 1577  CA  VAL A 190     2782   1884   2456   -394   -210   -252       C  
ATOM   1578  C   VAL A 190     -10.047   2.347 -26.529  1.00 20.48           C  
ANISOU 1578  C   VAL A 190     3009   2189   2584   -395   -280   -218       C  
ATOM   1579  O   VAL A 190      -9.393   3.384 -26.420  1.00 21.48           O  
ANISOU 1579  O   VAL A 190     3160   2357   2645   -363   -273   -169       O  
ATOM   1580  CB  VAL A 190      -8.193   0.737 -27.029  1.00 18.68           C  
ANISOU 1580  CB  VAL A 190     2828   1881   2390   -392   -170   -315       C  
ATOM   1581  CG1 VAL A 190      -7.483  -0.540 -26.605  1.00 20.55           C  
ANISOU 1581  CG1 VAL A 190     3053   2024   2729   -380    -90   -337       C  
ATOM   1582  CG2 VAL A 190      -8.571   0.692 -28.515  1.00 22.60           C  
ANISOU 1582  CG2 VAL A 190     3354   2430   2802   -439   -220   -414       C  
ATOM   1583  N   ARG A 191     -11.300   2.327 -26.977  1.00 22.12           N  
ANISOU 1583  N   ARG A 191     3189   2420   2796   -431   -344   -242       N  
ATOM   1584  CA  ARG A 191     -11.999   3.555 -27.350  1.00 22.70           C  
ANISOU 1584  CA  ARG A 191     3256   2571   2796   -427   -410   -196       C  
ATOM   1585  C   ARG A 191     -12.657   4.200 -26.136  1.00 22.07           C  
ANISOU 1585  C   ARG A 191     3131   2478   2775   -395   -411   -106       C  
ATOM   1586  O   ARG A 191     -13.879   4.359 -26.079  1.00 22.20           O  
ANISOU 1586  O   ARG A 191     3102   2512   2821   -409   -459    -87       O  
ATOM   1587  CB  ARG A 191     -13.041   3.279 -28.435  1.00 26.12           C  
ANISOU 1587  CB  ARG A 191     3672   3057   3197   -478   -484   -258       C  
ATOM   1588  CG  ARG A 191     -12.443   3.015 -29.810  1.00 34.98           C  
ANISOU 1588  CG  ARG A 191     4842   4234   4217   -505   -495   -346       C  
ATOM   1589  CD  ARG A 191     -12.357   4.286 -30.652  1.00 44.01           C  
ANISOU 1589  CD  ARG A 191     6009   5485   5229   -485   -538   -294       C  
ATOM   1590  NE  ARG A 191     -13.561   4.492 -31.460  1.00 50.09           N  
ANISOU 1590  NE  ARG A 191     6741   6344   5947   -517   -627   -304       N  
ATOM   1591  CZ  ARG A 191     -14.261   5.624 -31.490  1.00 54.99           C  
ANISOU 1591  CZ  ARG A 191     7334   7024   6538   -492   -676   -206       C  
ATOM   1592  NH1 ARG A 191     -13.878   6.668 -30.763  1.00 56.73           N  
ANISOU 1592  NH1 ARG A 191     7563   7213   6779   -438   -641   -104       N  
ATOM   1593  NH2 ARG A 191     -15.341   5.714 -32.254  1.00 56.11           N  
ANISOU 1593  NH2 ARG A 191     7432   7256   6631   -520   -759   -213       N  
ATOM   1594  N   VAL A 192     -11.832   4.556 -25.160  1.00 17.85           N  
ANISOU 1594  N   VAL A 192     2605   1922   2255   -353   -355    -57       N  
ATOM   1595  CA  VAL A 192     -12.291   5.260 -23.974  1.00 21.14           C  
ANISOU 1595  CA  VAL A 192     2984   2339   2711   -319   -347     16       C  
ATOM   1596  C   VAL A 192     -11.438   6.506 -23.753  1.00 22.13           C  
ANISOU 1596  C   VAL A 192     3138   2492   2779   -284   -327     52       C  
ATOM   1597  O   VAL A 192     -10.436   6.702 -24.444  1.00 20.29           O  
ANISOU 1597  O   VAL A 192     2951   2272   2486   -285   -314     30       O  
ATOM   1598  CB  VAL A 192     -12.227   4.368 -22.722  1.00 20.45           C  
ANISOU 1598  CB  VAL A 192     2857   2203   2709   -304   -293     40       C  
ATOM   1599  CG1 VAL A 192     -13.145   3.145 -22.883  1.00 19.02           C  
ANISOU 1599  CG1 VAL A 192     2638   1977   2612   -343   -306      9       C  
ATOM   1600  CG2 VAL A 192     -10.793   3.948 -22.456  1.00 17.94           C  
ANISOU 1600  CG2 VAL A 192     2569   1867   2379   -284   -233     33       C  
ATOM   1601  N   ALA A 193     -11.842   7.326 -22.782  1.00 21.22           N  
ANISOU 1601  N   ALA A 193     2990   2383   2689   -255   -320    101       N  
ATOM   1602  CA  ALA A 193     -11.212   8.613 -22.475  1.00 19.78           C  
ANISOU 1602  CA  ALA A 193     2823   2217   2474   -227   -301    126       C  
ATOM   1603  C   ALA A 193     -11.253   9.602 -23.643  1.00 22.06           C  
ANISOU 1603  C   ALA A 193     3142   2529   2712   -232   -336    138       C  
ATOM   1604  O   ALA A 193     -11.452   9.226 -24.801  1.00 22.12           O  
ANISOU 1604  O   ALA A 193     3169   2557   2678   -256   -373    119       O  
ATOM   1605  CB  ALA A 193      -9.761   8.405 -22.015  1.00 21.42           C  
ANISOU 1605  CB  ALA A 193     3054   2423   2662   -215   -247    111       C  
ATOM   1606  N   SER A 194     -11.092  10.880 -23.322  1.00 19.54           N  
ANISOU 1606  N   SER A 194     2820   2208   2396   -208   -321    169       N  
ATOM   1607  CA ASER A 194     -10.986  11.904 -24.352  0.33 20.63           C  
ANISOU 1607  CA ASER A 194     2981   2360   2497   -205   -339    201       C  
ATOM   1608  CA BSER A 194     -10.972  11.928 -24.328  0.67 20.48           C  
ANISOU 1608  CA BSER A 194     2962   2340   2479   -204   -338    202       C  
ATOM   1609  C   SER A 194      -9.595  11.853 -24.973  1.00 19.34           C  
ANISOU 1609  C   SER A 194     2867   2205   2277   -214   -310    182       C  
ATOM   1610  O   SER A 194      -8.644  11.428 -24.328  1.00 16.13           O  
ANISOU 1610  O   SER A 194     2469   1786   1875   -214   -268    150       O  
ATOM   1611  CB ASER A 194     -11.276  13.290 -23.778  0.33 21.75           C  
ANISOU 1611  CB ASER A 194     3098   2477   2688   -176   -322    241       C  
ATOM   1612  CB BSER A 194     -11.191  13.306 -23.701  0.67 21.72           C  
ANISOU 1612  CB BSER A 194     3096   2471   2686   -175   -317    238       C  
ATOM   1613  OG ASER A 194     -12.653  13.434 -23.476  0.33 24.06           O  
ANISOU 1613  OG ASER A 194     3344   2768   3029   -163   -351    269       O  
ATOM   1614  OG BSER A 194     -10.607  14.332 -24.490  0.67 24.04           O  
ANISOU 1614  OG BSER A 194     3414   2760   2959   -169   -307    273       O  
ATOM   1615  N   ARG A 195      -9.490  12.273 -26.232  1.00 16.54           N  
ANISOU 1615  N   ARG A 195     2538   1880   1865   -220   -332    207       N  
ATOM   1616  CA  ARG A 195      -8.228  12.180 -26.981  1.00 19.73           C  
ANISOU 1616  CA  ARG A 195     2987   2303   2208   -228   -303    193       C  
ATOM   1617  C   ARG A 195      -6.990  12.619 -26.207  1.00 18.27           C  
ANISOU 1617  C   ARG A 195     2809   2084   2050   -219   -242    185       C  
ATOM   1618  O   ARG A 195      -5.997  11.898 -26.158  1.00 17.89           O  
ANISOU 1618  O   ARG A 195     2779   2038   1979   -227   -211    146       O  
ATOM   1619  CB  ARG A 195      -8.306  13.006 -28.266  1.00 21.09           C  
ANISOU 1619  CB  ARG A 195     3175   2518   2321   -224   -324    251       C  
ATOM   1620  CG  ARG A 195      -7.067  12.878 -29.148  1.00 22.97           C  
ANISOU 1620  CG  ARG A 195     3457   2787   2485   -232   -291    241       C  
ATOM   1621  CD  ARG A 195      -7.083  13.895 -30.285  1.00 26.43           C  
ANISOU 1621  CD  ARG A 195     3902   3270   2870   -219   -300    323       C  
ATOM   1622  NE  ARG A 195      -8.335  13.839 -31.031  1.00 28.44           N  
ANISOU 1622  NE  ARG A 195     4136   3588   3082   -219   -368    354       N  
ATOM   1623  CZ  ARG A 195      -8.949  14.897 -31.551  1.00 30.24           C  
ANISOU 1623  CZ  ARG A 195     4339   3841   3308   -195   -390    454       C  
ATOM   1624  NH1 ARG A 195      -8.423  16.109 -31.424  1.00 26.78           N  
ANISOU 1624  NH1 ARG A 195     3898   3356   2922   -171   -342    530       N  
ATOM   1625  NH2 ARG A 195     -10.089  14.741 -32.207  1.00 31.67           N  
ANISOU 1625  NH2 ARG A 195     4494   4096   3443   -195   -458    480       N  
ATOM   1626  N   TYR A 196      -7.054  13.799 -25.599  1.00 20.22           N  
ANISOU 1626  N   TYR A 196     3033   2300   2351   -204   -224    217       N  
ATOM   1627  CA  TYR A 196      -5.874  14.405 -24.984  1.00 18.07           C  
ANISOU 1627  CA  TYR A 196     2760   2002   2103   -203   -171    203       C  
ATOM   1628  C   TYR A 196      -5.412  13.661 -23.736  1.00 17.52           C  
ANISOU 1628  C   TYR A 196     2672   1935   2051   -204   -149    150       C  
ATOM   1629  O   TYR A 196      -4.277  13.838 -23.277  1.00 14.38           O  
ANISOU 1629  O   TYR A 196     2269   1538   1655   -209   -111    128       O  
ATOM   1630  CB  TYR A 196      -6.161  15.869 -24.644  1.00 21.91           C  
ANISOU 1630  CB  TYR A 196     3223   2446   2658   -191   -156    236       C  
ATOM   1631  CG  TYR A 196      -6.730  16.637 -25.812  1.00 23.46           C  
ANISOU 1631  CG  TYR A 196     3425   2640   2847   -180   -176    313       C  
ATOM   1632  CD1 TYR A 196      -6.150  16.544 -27.073  1.00 22.93           C  
ANISOU 1632  CD1 TYR A 196     3392   2611   2709   -187   -176    349       C  
ATOM   1633  CD2 TYR A 196      -7.859  17.433 -25.664  1.00 27.70           C  
ANISOU 1633  CD2 TYR A 196     3931   3149   3445   -159   -192    358       C  
ATOM   1634  CE1 TYR A 196      -6.667  17.236 -28.153  1.00 27.60           C  
ANISOU 1634  CE1 TYR A 196     3983   3221   3282   -172   -195    435       C  
ATOM   1635  CE2 TYR A 196      -8.387  18.132 -26.742  1.00 31.55           C  
ANISOU 1635  CE2 TYR A 196     4416   3645   3927   -142   -210    448       C  
ATOM   1636  CZ  TYR A 196      -7.787  18.027 -27.983  1.00 30.17           C  
ANISOU 1636  CZ  TYR A 196     4273   3519   3673   -148   -214    490       C  
ATOM   1637  OH  TYR A 196      -8.304  18.718 -29.056  1.00 31.09           O  
ANISOU 1637  OH  TYR A 196     4380   3663   3772   -127   -233    593       O  
ATOM   1638  N   PHE A 197      -6.280  12.808 -23.205  1.00 14.71           N  
ANISOU 1638  N   PHE A 197     2296   1586   1707   -199   -172    137       N  
ATOM   1639  CA  PHE A 197      -6.004  12.137 -21.945  1.00 13.11           C  
ANISOU 1639  CA  PHE A 197     2065   1395   1523   -192   -150    109       C  
ATOM   1640  C   PHE A 197      -5.869  10.627 -22.124  1.00 12.32           C  
ANISOU 1640  C   PHE A 197     1973   1303   1406   -197   -151     95       C  
ATOM   1641  O   PHE A 197      -5.728   9.900 -21.153  1.00 12.97           O  
ANISOU 1641  O   PHE A 197     2026   1394   1507   -185   -131     91       O  
ATOM   1642  CB  PHE A 197      -7.100  12.499 -20.929  1.00 17.70           C  
ANISOU 1642  CB  PHE A 197     2603   1973   2151   -177   -159    113       C  
ATOM   1643  CG  PHE A 197      -7.250  13.981 -20.752  1.00 16.44           C  
ANISOU 1643  CG  PHE A 197     2432   1789   2025   -171   -149    117       C  
ATOM   1644  CD1 PHE A 197      -6.484  14.659 -19.815  1.00 15.81           C  
ANISOU 1644  CD1 PHE A 197     2332   1716   1960   -171   -112     79       C  
ATOM   1645  CD2 PHE A 197      -8.093  14.708 -21.580  1.00 15.12           C  
ANISOU 1645  CD2 PHE A 197     2271   1594   1878   -166   -174    157       C  
ATOM   1646  CE1 PHE A 197      -6.583  16.034 -19.678  1.00 14.39           C  
ANISOU 1646  CE1 PHE A 197     2140   1498   1830   -169    -94     69       C  
ATOM   1647  CE2 PHE A 197      -8.200  16.074 -21.449  1.00 16.30           C  
ANISOU 1647  CE2 PHE A 197     2408   1705   2081   -157   -154    166       C  
ATOM   1648  CZ  PHE A 197      -7.438  16.740 -20.502  1.00 15.12           C  
ANISOU 1648  CZ  PHE A 197     2240   1544   1959   -160   -111    117       C  
ATOM   1649  N   LYS A 198      -5.881  10.173 -23.376  1.00 13.86           N  
ANISOU 1649  N   LYS A 198     2204   1495   1566   -212   -168     89       N  
ATOM   1650  CA  LYS A 198      -5.714   8.750 -23.688  1.00 16.49           C  
ANISOU 1650  CA  LYS A 198     2547   1821   1896   -221   -161     60       C  
ATOM   1651  C   LYS A 198      -4.311   8.264 -23.347  1.00 17.43           C  
ANISOU 1651  C   LYS A 198     2670   1943   2010   -210   -109     49       C  
ATOM   1652  O   LYS A 198      -3.326   8.870 -23.765  1.00 15.94           O  
ANISOU 1652  O   LYS A 198     2502   1768   1787   -211    -88     50       O  
ATOM   1653  CB  LYS A 198      -5.987   8.482 -25.170  1.00 14.56           C  
ANISOU 1653  CB  LYS A 198     2342   1588   1604   -243   -190     38       C  
ATOM   1654  CG  LYS A 198      -7.458   8.568 -25.566  1.00 14.48           C  
ANISOU 1654  CG  LYS A 198     2316   1585   1599   -256   -249     45       C  
ATOM   1655  CD  LYS A 198      -7.612   8.488 -27.072  1.00 13.51           C  
ANISOU 1655  CD  LYS A 198     2227   1503   1404   -278   -283     24       C  
ATOM   1656  CE  LYS A 198      -9.069   8.645 -27.499  1.00 18.48           C  
ANISOU 1656  CE  LYS A 198     2831   2160   2032   -291   -350     38       C  
ATOM   1657  NZ  LYS A 198      -9.896   7.453 -27.149  1.00 18.56           N  
ANISOU 1657  NZ  LYS A 198     2811   2142   2098   -314   -368     -7       N  
ATOM   1658  N   GLY A 199      -4.218   7.168 -22.605  1.00 16.07           N  
ANISOU 1658  N   GLY A 199     2471   1758   1878   -198    -85     48       N  
ATOM   1659  CA  GLY A 199      -2.916   6.606 -22.290  1.00 14.56           C  
ANISOU 1659  CA  GLY A 199     2273   1572   1688   -182    -35     50       C  
ATOM   1660  C   GLY A 199      -2.284   5.977 -23.517  1.00 14.17           C  
ANISOU 1660  C   GLY A 199     2266   1504   1615   -192    -15     13       C  
ATOM   1661  O   GLY A 199      -2.988   5.581 -24.438  1.00 17.30           O  
ANISOU 1661  O   GLY A 199     2689   1882   2002   -214    -40    -22       O  
ATOM   1662  N   PRO A 200      -0.943   5.880 -23.538  1.00 12.88           N  
ANISOU 1662  N   PRO A 200     2104   1353   1437   -178     30     15       N  
ATOM   1663  CA  PRO A 200      -0.231   5.192 -24.625  1.00 14.19           C  
ANISOU 1663  CA  PRO A 200     2306   1503   1584   -181     64    -24       C  
ATOM   1664  C   PRO A 200      -0.786   3.796 -24.906  1.00 16.60           C  
ANISOU 1664  C   PRO A 200     2613   1754   1940   -186     74    -63       C  
ATOM   1665  O   PRO A 200      -0.804   3.364 -26.065  1.00 16.51           O  
ANISOU 1665  O   PRO A 200     2641   1731   1901   -204     78   -123       O  
ATOM   1666  CB  PRO A 200       1.209   5.105 -24.102  1.00 12.58           C  
ANISOU 1666  CB  PRO A 200     2075   1317   1388   -155    117      2       C  
ATOM   1667  CG  PRO A 200       1.346   6.268 -23.196  1.00 15.17           C  
ANISOU 1667  CG  PRO A 200     2371   1688   1703   -154     98     38       C  
ATOM   1668  CD  PRO A 200      -0.020   6.466 -22.554  1.00 14.02           C  
ANISOU 1668  CD  PRO A 200     2211   1536   1580   -160     53     48       C  
ATOM   1669  N   GLU A 201      -1.238   3.102 -23.863  1.00 15.35           N  
ANISOU 1669  N   GLU A 201     2410   1566   1856   -171     82    -31       N  
ATOM   1670  CA  GLU A 201      -1.788   1.765 -24.046  1.00 15.29           C  
ANISOU 1670  CA  GLU A 201     2396   1489   1923   -178    100    -64       C  
ATOM   1671  C   GLU A 201      -2.997   1.784 -24.985  1.00 14.04           C  
ANISOU 1671  C   GLU A 201     2267   1321   1745   -222     45   -126       C  
ATOM   1672  O   GLU A 201      -3.149   0.895 -25.823  1.00 16.59           O  
ANISOU 1672  O   GLU A 201     2610   1603   2090   -245     58   -200       O  
ATOM   1673  CB  GLU A 201      -2.164   1.128 -22.696  1.00 15.70           C  
ANISOU 1673  CB  GLU A 201     2387   1516   2063   -152    119      2       C  
ATOM   1674  CG  GLU A 201      -3.168   1.902 -21.828  1.00 16.96           C  
ANISOU 1674  CG  GLU A 201     2517   1714   2211   -155     70     47       C  
ATOM   1675  CD  GLU A 201      -2.487   2.810 -20.818  1.00 18.13           C  
ANISOU 1675  CD  GLU A 201     2637   1936   2315   -126     74    103       C  
ATOM   1676  OE1 GLU A 201      -1.643   3.628 -21.236  1.00 16.24           O  
ANISOU 1676  OE1 GLU A 201     2424   1733   2013   -129     73     86       O  
ATOM   1677  OE2 GLU A 201      -2.783   2.696 -19.607  1.00 17.41           O  
ANISOU 1677  OE2 GLU A 201     2493   1870   2251   -102     81    162       O  
ATOM   1678  N   LEU A 202      -3.847   2.798 -24.860  1.00 12.42           N  
ANISOU 1678  N   LEU A 202     2061   1159   1501   -235    -14   -102       N  
ATOM   1679  CA  LEU A 202      -4.997   2.918 -25.756  1.00 12.65           C  
ANISOU 1679  CA  LEU A 202     2108   1198   1503   -274    -73   -148       C  
ATOM   1680  C   LEU A 202      -4.521   3.240 -27.167  1.00 17.16           C  
ANISOU 1680  C   LEU A 202     2731   1812   1978   -292    -82   -202       C  
ATOM   1681  O   LEU A 202      -5.055   2.721 -28.155  1.00 16.64           O  
ANISOU 1681  O   LEU A 202     2682   1751   1889   -325   -106   -274       O  
ATOM   1682  CB  LEU A 202      -5.964   4.004 -25.277  1.00 11.50           C  
ANISOU 1682  CB  LEU A 202     1940   1088   1341   -274   -128    -96       C  
ATOM   1683  CG  LEU A 202      -6.378   3.953 -23.805  1.00 14.31           C  
ANISOU 1683  CG  LEU A 202     2244   1427   1768   -251   -117    -36       C  
ATOM   1684  CD1 LEU A 202      -7.369   5.066 -23.494  1.00 16.98           C  
ANISOU 1684  CD1 LEU A 202     2564   1798   2090   -251   -166      0       C  
ATOM   1685  CD2 LEU A 202      -6.939   2.587 -23.438  1.00 16.02           C  
ANISOU 1685  CD2 LEU A 202     2425   1581   2079   -259    -98    -47       C  
ATOM   1686  N   LEU A 203      -3.505   4.095 -27.252  1.00 15.47           N  
ANISOU 1686  N   LEU A 203     2536   1636   1707   -270    -59   -167       N  
ATOM   1687  CA  LEU A 203      -3.050   4.618 -28.535  1.00 15.66           C  
ANISOU 1687  CA  LEU A 203     2605   1714   1632   -281    -64   -193       C  
ATOM   1688  C   LEU A 203      -2.286   3.574 -29.346  1.00 16.51           C  
ANISOU 1688  C   LEU A 203     2739   1808   1725   -286    -14   -271       C  
ATOM   1689  O   LEU A 203      -2.137   3.713 -30.559  1.00 17.74           O  
ANISOU 1689  O   LEU A 203     2932   2018   1791   -301    -20   -314       O  
ATOM   1690  CB  LEU A 203      -2.184   5.863 -28.313  1.00 15.33           C  
ANISOU 1690  CB  LEU A 203     2566   1705   1553   -259    -47   -126       C  
ATOM   1691  CG  LEU A 203      -2.913   7.016 -27.616  1.00 13.44           C  
ANISOU 1691  CG  LEU A 203     2302   1474   1330   -255    -89    -62       C  
ATOM   1692  CD1 LEU A 203      -1.950   8.133 -27.235  1.00 13.48           C  
ANISOU 1692  CD1 LEU A 203     2303   1493   1328   -239    -60    -12       C  
ATOM   1693  CD2 LEU A 203      -4.034   7.558 -28.506  1.00 15.57           C  
ANISOU 1693  CD2 LEU A 203     2584   1784   1549   -274   -151    -56       C  
ATOM   1694  N   VAL A 204      -1.794   2.533 -28.680  1.00 18.99           N  
ANISOU 1694  N   VAL A 204     3033   2054   2128   -269     41   -285       N  
ATOM   1695  CA  VAL A 204      -1.102   1.460 -29.383  1.00 17.79           C  
ANISOU 1695  CA  VAL A 204     2901   1870   1987   -270     99   -365       C  
ATOM   1696  C   VAL A 204      -1.954   0.195 -29.400  1.00 18.65           C  
ANISOU 1696  C   VAL A 204     2995   1907   2184   -296     99   -440       C  
ATOM   1697  O   VAL A 204      -1.468  -0.881 -29.748  1.00 18.87           O  
ANISOU 1697  O   VAL A 204     3028   1878   2263   -295    159   -511       O  
ATOM   1698  CB  VAL A 204       0.281   1.149 -28.759  1.00 18.95           C  
ANISOU 1698  CB  VAL A 204     3030   1985   2183   -225    178   -325       C  
ATOM   1699  CG1 VAL A 204       1.167   2.388 -28.804  1.00 19.80           C  
ANISOU 1699  CG1 VAL A 204     3148   2162   2213   -209    181   -264       C  
ATOM   1700  CG2 VAL A 204       0.148   0.621 -27.337  1.00 16.73           C  
ANISOU 1700  CG2 VAL A 204     2695   1645   2016   -200    196   -261       C  
ATOM   1701  N   ASP A 205      -3.221   0.347 -29.019  1.00 19.10           N  
ANISOU 1701  N   ASP A 205     3028   1962   2269   -320     36   -423       N  
ATOM   1702  CA  ASP A 205      -4.220  -0.721 -29.096  1.00 24.56           C  
ANISOU 1702  CA  ASP A 205     3697   2589   3044   -357     23   -494       C  
ATOM   1703  C   ASP A 205      -3.924  -1.905 -28.169  1.00 23.53           C  
ANISOU 1703  C   ASP A 205     3528   2346   3067   -335     95   -477       C  
ATOM   1704  O   ASP A 205      -4.194  -3.059 -28.518  1.00 26.41           O  
ANISOU 1704  O   ASP A 205     3884   2632   3517   -361    125   -564       O  
ATOM   1705  CB  ASP A 205      -4.350  -1.218 -30.541  1.00 30.79           C  
ANISOU 1705  CB  ASP A 205     4523   3405   3771   -400     14   -630       C  
ATOM   1706  CG  ASP A 205      -5.709  -1.827 -30.835  1.00 38.33           C  
ANISOU 1706  CG  ASP A 205     5453   4339   4771   -457    -40   -708       C  
ATOM   1707  OD1 ASP A 205      -6.519  -1.990 -29.895  1.00 38.73           O  
ANISOU 1707  OD1 ASP A 205     5458   4339   4920   -461    -59   -653       O  
ATOM   1708  OD2 ASP A 205      -5.961  -2.161 -32.013  1.00 40.93           O  
ANISOU 1708  OD2 ASP A 205     5804   4712   5035   -501    -62   -830       O  
ATOM   1709  N   TYR A 206      -3.373  -1.628 -26.992  1.00 17.74           N  
ANISOU 1709  N   TYR A 206     2764   1605   2370   -286    125   -366       N  
ATOM   1710  CA  TYR A 206      -3.163  -2.683 -26.005  1.00 16.38           C  
ANISOU 1710  CA  TYR A 206     2543   1342   2339   -256    191   -318       C  
ATOM   1711  C   TYR A 206      -4.382  -2.778 -25.095  1.00 17.99           C  
ANISOU 1711  C   TYR A 206     2697   1523   2615   -267    156   -261       C  
ATOM   1712  O   TYR A 206      -4.678  -1.841 -24.354  1.00 17.37           O  
ANISOU 1712  O   TYR A 206     2603   1509   2489   -251    116   -182       O  
ATOM   1713  CB  TYR A 206      -1.903  -2.426 -25.179  1.00 16.34           C  
ANISOU 1713  CB  TYR A 206     2519   1360   2330   -196    242   -223       C  
ATOM   1714  CG  TYR A 206      -1.571  -3.582 -24.263  1.00 18.87           C  
ANISOU 1714  CG  TYR A 206     2783   1595   2792   -156    317   -160       C  
ATOM   1715  CD1 TYR A 206      -1.057  -4.769 -24.775  1.00 21.17           C  
ANISOU 1715  CD1 TYR A 206     3076   1791   3177   -149    392   -219       C  
ATOM   1716  CD2 TYR A 206      -1.782  -3.495 -22.891  1.00 17.71           C  
ANISOU 1716  CD2 TYR A 206     2577   1466   2685   -121    318    -40       C  
ATOM   1717  CE1 TYR A 206      -0.761  -5.838 -23.946  1.00 21.98           C  
ANISOU 1717  CE1 TYR A 206     3121   1806   3426   -106    469   -146       C  
ATOM   1718  CE2 TYR A 206      -1.484  -4.559 -22.055  1.00 20.34           C  
ANISOU 1718  CE2 TYR A 206     2852   1732   3146    -78    389     38       C  
ATOM   1719  CZ  TYR A 206      -0.972  -5.723 -22.587  1.00 21.04           C  
ANISOU 1719  CZ  TYR A 206     2940   1714   3340    -69    465     -9       C  
ATOM   1720  OH  TYR A 206      -0.676  -6.786 -21.761  1.00 22.29           O  
ANISOU 1720  OH  TYR A 206     3033   1795   3640    -21    544     85       O  
ATOM   1721  N   GLN A 207      -5.083  -3.910 -25.142  1.00 19.88           N  
ANISOU 1721  N   GLN A 207     2910   1669   2977   -295    176   -305       N  
ATOM   1722  CA  GLN A 207      -6.380  -4.014 -24.479  1.00 20.29           C  
ANISOU 1722  CA  GLN A 207     2914   1700   3096   -316    140   -264       C  
ATOM   1723  C   GLN A 207      -6.324  -4.475 -23.025  1.00 20.95           C  
ANISOU 1723  C   GLN A 207     2933   1744   3285   -267    192   -134       C  
ATOM   1724  O   GLN A 207      -7.287  -4.282 -22.289  1.00 20.53           O  
ANISOU 1724  O   GLN A 207     2837   1704   3260   -272    163    -72       O  
ATOM   1725  CB  GLN A 207      -7.300  -4.964 -25.257  1.00 20.62           C  
ANISOU 1725  CB  GLN A 207     2947   1663   3223   -381    129   -379       C  
ATOM   1726  CG  GLN A 207      -7.560  -4.546 -26.696  1.00 22.70           C  
ANISOU 1726  CG  GLN A 207     3264   1992   3370   -434     66   -510       C  
ATOM   1727  CD  GLN A 207      -8.561  -5.456 -27.382  1.00 26.38           C  
ANISOU 1727  CD  GLN A 207     3710   2396   3917   -506     46   -632       C  
ATOM   1728  OE1 GLN A 207      -8.190  -6.280 -28.214  1.00 30.05           O  
ANISOU 1728  OE1 GLN A 207     4195   2807   4415   -535     84   -757       O  
ATOM   1729  NE2 GLN A 207      -9.839  -5.300 -27.046  1.00 25.15           N  
ANISOU 1729  NE2 GLN A 207     3509   2250   3795   -539    -14   -606       N  
ATOM   1730  N   MET A 208      -5.222  -5.094 -22.604  1.00 19.58           N  
ANISOU 1730  N   MET A 208     2743   1528   3167   -218    272    -85       N  
ATOM   1731  CA  MET A 208      -5.186  -5.666 -21.255  1.00 18.51           C  
ANISOU 1731  CA  MET A 208     2536   1363   3135   -168    327     50       C  
ATOM   1732  C   MET A 208      -4.678  -4.647 -20.234  1.00 17.91           C  
ANISOU 1732  C   MET A 208     2443   1409   2953   -117    309    160       C  
ATOM   1733  O   MET A 208      -3.731  -4.912 -19.484  1.00 17.70           O  
ANISOU 1733  O   MET A 208     2380   1399   2944    -59    363    250       O  
ATOM   1734  CB  MET A 208      -4.335  -6.948 -21.230  1.00 17.82           C  
ANISOU 1734  CB  MET A 208     2424   1164   3183   -134    428     66       C  
ATOM   1735  CG  MET A 208      -4.681  -7.886 -20.073  1.00 19.50           C  
ANISOU 1735  CG  MET A 208     2552   1307   3549    -98    491    196       C  
ATOM   1736  SD  MET A 208      -3.880  -9.506 -20.133  1.00 25.81           S  
ANISOU 1736  SD  MET A 208     3309   1975   4524    -58    608    211       S  
ATOM   1737  CE  MET A 208      -4.730 -10.240 -21.530  1.00 34.78           C  
ANISOU 1737  CE  MET A 208     4480   3015   5721   -146    589     13       C  
ATOM   1738  N   TYR A 209      -5.321  -3.481 -20.204  1.00 17.86           N  
ANISOU 1738  N   TYR A 209     2456   1490   2841   -139    233    148       N  
ATOM   1739  CA  TYR A 209      -4.881  -2.395 -19.331  1.00 16.22           C  
ANISOU 1739  CA  TYR A 209     2236   1397   2529   -102    212    221       C  
ATOM   1740  C   TYR A 209      -5.618  -2.435 -17.995  1.00 16.85           C  
ANISOU 1740  C   TYR A 209     2248   1511   2644    -76    216    325       C  
ATOM   1741  O   TYR A 209      -6.360  -3.376 -17.723  1.00 18.45           O  
ANISOU 1741  O   TYR A 209     2410   1641   2961    -81    244    359       O  
ATOM   1742  CB  TYR A 209      -5.061  -1.036 -20.021  1.00 16.61           C  
ANISOU 1742  CB  TYR A 209     2341   1516   2453   -133    139    154       C  
ATOM   1743  CG  TYR A 209      -6.475  -0.696 -20.446  1.00 14.88           C  
ANISOU 1743  CG  TYR A 209     2131   1290   2234   -179     77    111       C  
ATOM   1744  CD1 TYR A 209      -7.381  -0.165 -19.540  1.00 16.63           C  
ANISOU 1744  CD1 TYR A 209     2313   1554   2452   -171     50    168       C  
ATOM   1745  CD2 TYR A 209      -6.893  -0.874 -21.765  1.00 12.55           C  
ANISOU 1745  CD2 TYR A 209     1879    957   1932   -229     45     11       C  
ATOM   1746  CE1 TYR A 209      -8.672   0.163 -19.919  1.00 17.28           C  
ANISOU 1746  CE1 TYR A 209     2394   1632   2539   -209     -6    137       C  
ATOM   1747  CE2 TYR A 209      -8.200  -0.538 -22.158  1.00 14.24           C  
ANISOU 1747  CE2 TYR A 209     2090   1179   2140   -271    -19    -22       C  
ATOM   1748  CZ  TYR A 209      -9.076  -0.022 -21.224  1.00 17.08           C  
ANISOU 1748  CZ  TYR A 209     2406   1572   2509   -259    -43     46       C  
ATOM   1749  OH  TYR A 209     -10.369   0.315 -21.579  1.00 18.55           O  
ANISOU 1749  OH  TYR A 209     2581   1769   2697   -295   -104     24       O  
ATOM   1750  N   ASP A 210      -5.399  -1.434 -17.147  1.00 16.21           N  
ANISOU 1750  N   ASP A 210     2151   1541   2467    -48    194    374       N  
ATOM   1751  CA  ASP A 210      -5.959  -1.483 -15.794  1.00 17.05           C  
ANISOU 1751  CA  ASP A 210     2188   1702   2587    -15    207    476       C  
ATOM   1752  C   ASP A 210      -6.099  -0.094 -15.175  1.00 16.17           C  
ANISOU 1752  C   ASP A 210     2076   1709   2358     -9    162    473       C  
ATOM   1753  O   ASP A 210      -6.123   0.911 -15.886  1.00 16.53           O  
ANISOU 1753  O   ASP A 210     2175   1769   2335    -40    113    393       O  
ATOM   1754  CB  ASP A 210      -5.097  -2.384 -14.893  1.00 17.30           C  
ANISOU 1754  CB  ASP A 210     2157   1747   2667     44    278    587       C  
ATOM   1755  CG  ASP A 210      -3.645  -1.939 -14.826  1.00 18.88           C  
ANISOU 1755  CG  ASP A 210     2367   2023   2783     74    287    588       C  
ATOM   1756  OD1 ASP A 210      -2.771  -2.603 -15.435  1.00 21.09           O  
ANISOU 1756  OD1 ASP A 210     2662   2241   3111     83    326    576       O  
ATOM   1757  OD2 ASP A 210      -3.376  -0.922 -14.159  1.00 16.53           O  
ANISOU 1757  OD2 ASP A 210     2057   1846   2377     86    256    597       O  
ATOM   1758  N   TYR A 211      -6.190  -0.043 -13.847  1.00 15.47           N  
ANISOU 1758  N   TYR A 211     1923   1707   2247     32    182    561       N  
ATOM   1759  CA  TYR A 211      -6.316   1.222 -13.121  1.00 11.27           C  
ANISOU 1759  CA  TYR A 211     1382   1290   1609     40    149    549       C  
ATOM   1760  C   TYR A 211      -5.281   2.270 -13.534  1.00 11.55           C  
ANISOU 1760  C   TYR A 211     1462   1374   1553     28    123    476       C  
ATOM   1761  O   TYR A 211      -5.543   3.467 -13.482  1.00 14.03           O  
ANISOU 1761  O   TYR A 211     1795   1732   1804     11     86    422       O  
ATOM   1762  CB  TYR A 211      -6.172   0.998 -11.617  1.00 13.78           C  
ANISOU 1762  CB  TYR A 211     1619   1720   1895     93    186    652       C  
ATOM   1763  CG  TYR A 211      -6.910  -0.189 -11.037  1.00 15.63           C  
ANISOU 1763  CG  TYR A 211     1792   1918   2227    118    233    760       C  
ATOM   1764  CD1 TYR A 211      -6.212  -1.301 -10.586  1.00 16.68           C  
ANISOU 1764  CD1 TYR A 211     1875   2049   2415    163    292    866       C  
ATOM   1765  CD2 TYR A 211      -8.298  -0.182 -10.905  1.00 16.15           C  
ANISOU 1765  CD2 TYR A 211     1843   1954   2339    101    223    766       C  
ATOM   1766  CE1 TYR A 211      -6.866  -2.386 -10.036  1.00 19.29           C  
ANISOU 1766  CE1 TYR A 211     2143   2337   2849    188    344    978       C  
ATOM   1767  CE2 TYR A 211      -8.968  -1.267 -10.352  1.00 18.45           C  
ANISOU 1767  CE2 TYR A 211     2071   2208   2730    121    272    873       C  
ATOM   1768  CZ  TYR A 211      -8.242  -2.366  -9.916  1.00 17.96           C  
ANISOU 1768  CZ  TYR A 211     1961   2135   2726    165    335    981       C  
ATOM   1769  OH  TYR A 211      -8.890  -3.446  -9.357  1.00 19.92           O  
ANISOU 1769  OH  TYR A 211     2141   2339   3090    187    393   1100       O  
ATOM   1770  N   SER A 212      -4.091   1.810 -13.913  1.00 13.10           N  
ANISOU 1770  N   SER A 212     1669   1556   1753     39    148    480       N  
ATOM   1771  CA  SER A 212      -2.989   2.709 -14.224  1.00 13.07           C  
ANISOU 1771  CA  SER A 212     1694   1601   1672     30    132    426       C  
ATOM   1772  C   SER A 212      -3.297   3.662 -15.387  1.00 13.06           C  
ANISOU 1772  C   SER A 212     1766   1549   1648    -18     87    330       C  
ATOM   1773  O   SER A 212      -2.639   4.688 -15.532  1.00 12.44           O  
ANISOU 1773  O   SER A 212     1706   1512   1508    -31     71    286       O  
ATOM   1774  CB  SER A 212      -1.717   1.897 -14.517  1.00 13.86           C  
ANISOU 1774  CB  SER A 212     1786   1682   1796     53    174    455       C  
ATOM   1775  OG  SER A 212      -1.958   0.871 -15.464  1.00 15.39           O  
ANISOU 1775  OG  SER A 212     2012   1754   2081     42    197    444       O  
ATOM   1776  N   LEU A 213      -4.300   3.333 -16.199  1.00 12.31           N  
ANISOU 1776  N   LEU A 213     1704   1369   1604    -45     69    304       N  
ATOM   1777  CA  LEU A 213      -4.776   4.248 -17.243  1.00 14.04           C  
ANISOU 1777  CA  LEU A 213     1980   1558   1795    -85     23    233       C  
ATOM   1778  C   LEU A 213      -5.167   5.614 -16.662  1.00 13.06           C  
ANISOU 1778  C   LEU A 213     1847   1493   1621    -87     -5    219       C  
ATOM   1779  O   LEU A 213      -4.796   6.669 -17.196  1.00 12.83           O  
ANISOU 1779  O   LEU A 213     1853   1471   1552   -104    -24    176       O  
ATOM   1780  CB  LEU A 213      -5.975   3.639 -17.978  1.00 14.49           C  
ANISOU 1780  CB  LEU A 213     2053   1539   1911   -112      1    216       C  
ATOM   1781  CG  LEU A 213      -6.720   4.574 -18.933  1.00 16.05           C  
ANISOU 1781  CG  LEU A 213     2293   1726   2078   -146    -53    164       C  
ATOM   1782  CD1 LEU A 213      -5.813   5.025 -20.079  1.00 17.38           C  
ANISOU 1782  CD1 LEU A 213     2520   1892   2194   -163    -60    117       C  
ATOM   1783  CD2 LEU A 213      -7.965   3.879 -19.459  1.00 16.22           C  
ANISOU 1783  CD2 LEU A 213     2310   1694   2158   -173    -79    151       C  
ATOM   1784  N   ASP A 214      -5.906   5.589 -15.559  1.00 13.16           N  
ANISOU 1784  N   ASP A 214     1810   1548   1645    -66      0    257       N  
ATOM   1785  CA  ASP A 214      -6.356   6.812 -14.901  1.00 14.46           C  
ANISOU 1785  CA  ASP A 214     1957   1765   1771    -64    -17    234       C  
ATOM   1786  C   ASP A 214      -5.189   7.679 -14.439  1.00 13.06           C  
ANISOU 1786  C   ASP A 214     1773   1657   1531    -61     -8    202       C  
ATOM   1787  O   ASP A 214      -5.323   8.895 -14.297  1.00 12.88           O  
ANISOU 1787  O   ASP A 214     1755   1651   1486    -72    -21    153       O  
ATOM   1788  CB  ASP A 214      -7.239   6.488 -13.692  1.00 15.08           C  
ANISOU 1788  CB  ASP A 214     1975   1892   1863    -37     -1    284       C  
ATOM   1789  CG  ASP A 214      -8.562   5.843 -14.072  1.00 15.60           C  
ANISOU 1789  CG  ASP A 214     2037   1890   2000    -47    -14    310       C  
ATOM   1790  OD1 ASP A 214      -9.060   6.044 -15.210  1.00 12.95           O  
ANISOU 1790  OD1 ASP A 214     1744   1486   1689    -79    -49    273       O  
ATOM   1791  OD2 ASP A 214      -9.117   5.141 -13.197  1.00 14.68           O  
ANISOU 1791  OD2 ASP A 214     1866   1798   1913    -24     13    373       O  
ATOM   1792  N   MET A 215      -4.046   7.053 -14.186  1.00 12.87           N  
ANISOU 1792  N   MET A 215     1731   1671   1488    -45     18    228       N  
ATOM   1793  CA  MET A 215      -2.900   7.789 -13.672  1.00 13.82           C  
ANISOU 1793  CA  MET A 215     1831   1871   1550    -45     24    197       C  
ATOM   1794  C   MET A 215      -2.198   8.549 -14.802  1.00 13.38           C  
ANISOU 1794  C   MET A 215     1830   1763   1492    -79     13    142       C  
ATOM   1795  O   MET A 215      -1.644   9.631 -14.576  1.00 12.79           O  
ANISOU 1795  O   MET A 215     1748   1724   1389    -96      9     92       O  
ATOM   1796  CB  MET A 215      -1.931   6.843 -12.956  1.00 15.51           C  
ANISOU 1796  CB  MET A 215     1992   2158   1744    -11     55    258       C  
ATOM   1797  CG  MET A 215      -2.568   6.079 -11.789  1.00 16.44           C  
ANISOU 1797  CG  MET A 215     2047   2339   1860     28     73    334       C  
ATOM   1798  SD  MET A 215      -3.422   7.126 -10.585  1.00 16.99           S  
ANISOU 1798  SD  MET A 215     2076   2508   1872     31     60    297       S  
ATOM   1799  CE  MET A 215      -2.051   8.040  -9.885  1.00 17.34           C  
ANISOU 1799  CE  MET A 215     2081   2682   1823     23     55    236       C  
ATOM   1800  N   TRP A 216      -2.228   7.997 -16.015  1.00 13.04           N  
ANISOU 1800  N   TRP A 216     1837   1638   1481    -90     11    149       N  
ATOM   1801  CA  TRP A 216      -1.745   8.744 -17.170  1.00 13.92           C  
ANISOU 1801  CA  TRP A 216     2000   1704   1584   -119      2    108       C  
ATOM   1802  C   TRP A 216      -2.621   9.971 -17.395  1.00 13.69           C  
ANISOU 1802  C   TRP A 216     1991   1648   1562   -139    -25     77       C  
ATOM   1803  O   TRP A 216      -2.119  11.080 -17.595  1.00 13.27           O  
ANISOU 1803  O   TRP A 216     1946   1594   1501   -157    -24     44       O  
ATOM   1804  CB  TRP A 216      -1.719   7.898 -18.446  1.00 14.96           C  
ANISOU 1804  CB  TRP A 216     2180   1769   1734   -126      5    114       C  
ATOM   1805  CG  TRP A 216      -1.328   8.735 -19.641  1.00 14.98           C  
ANISOU 1805  CG  TRP A 216     2234   1743   1715   -153     -3     83       C  
ATOM   1806  CD1 TRP A 216      -2.167   9.461 -20.450  1.00 12.62           C  
ANISOU 1806  CD1 TRP A 216     1970   1409   1415   -172    -34     72       C  
ATOM   1807  CD2 TRP A 216      -0.002   8.962 -20.137  1.00 15.97           C  
ANISOU 1807  CD2 TRP A 216     2371   1879   1817   -159     23     74       C  
ATOM   1808  NE1 TRP A 216      -1.443  10.112 -21.416  1.00 12.87           N  
ANISOU 1808  NE1 TRP A 216     2036   1431   1422   -188    -26     63       N  
ATOM   1809  CE2 TRP A 216      -0.112   9.823 -21.246  1.00 14.00           C  
ANISOU 1809  CE2 TRP A 216     2167   1600   1553   -182     11     60       C  
ATOM   1810  CE3 TRP A 216       1.267   8.511 -19.755  1.00 15.65           C  
ANISOU 1810  CE3 TRP A 216     2301   1876   1769   -145     58     84       C  
ATOM   1811  CZ2 TRP A 216       0.996  10.241 -21.981  1.00 14.37           C  
ANISOU 1811  CZ2 TRP A 216     2232   1649   1578   -193     36     56       C  
ATOM   1812  CZ3 TRP A 216       2.370   8.938 -20.479  1.00 15.13           C  
ANISOU 1812  CZ3 TRP A 216     2252   1811   1685   -157     81     73       C  
ATOM   1813  CH2 TRP A 216       2.228   9.789 -21.581  1.00 16.53           C  
ANISOU 1813  CH2 TRP A 216     2478   1955   1849   -182     71     58       C  
ATOM   1814  N   SER A 217      -3.934   9.768 -17.376  1.00 14.18           N  
ANISOU 1814  N   SER A 217     2054   1684   1651   -134    -46     91       N  
ATOM   1815  CA  SER A 217      -4.866  10.871 -17.563  1.00 11.11           C  
ANISOU 1815  CA  SER A 217     1674   1267   1279   -144    -69     74       C  
ATOM   1816  C   SER A 217      -4.640  11.958 -16.509  1.00 12.33           C  
ANISOU 1816  C   SER A 217     1792   1465   1428   -142    -54     36       C  
ATOM   1817  O   SER A 217      -4.663  13.155 -16.823  1.00 14.05           O  
ANISOU 1817  O   SER A 217     2023   1649   1665   -156    -55      7       O  
ATOM   1818  CB  SER A 217      -6.309  10.360 -17.497  1.00 11.85           C  
ANISOU 1818  CB  SER A 217     1757   1341   1406   -135    -91    100       C  
ATOM   1819  OG  SER A 217      -6.510   9.345 -18.462  1.00 14.25           O  
ANISOU 1819  OG  SER A 217     2089   1605   1720   -146   -105    116       O  
ATOM   1820  N   LEU A 218      -4.424  11.534 -15.265  1.00 12.72           N  
ANISOU 1820  N   LEU A 218     1792   1590   1452   -123    -37     37       N  
ATOM   1821  CA  LEU A 218      -4.168  12.477 -14.178  1.00 12.39           C  
ANISOU 1821  CA  LEU A 218     1708   1609   1389   -124    -24    -17       C  
ATOM   1822  C   LEU A 218      -2.878  13.253 -14.449  1.00 14.58           C  
ANISOU 1822  C   LEU A 218     1992   1889   1657   -152    -14    -64       C  
ATOM   1823  O   LEU A 218      -2.794  14.462 -14.198  1.00 15.43           O  
ANISOU 1823  O   LEU A 218     2091   1988   1784   -171     -6   -127       O  
ATOM   1824  CB  LEU A 218      -4.078  11.756 -12.829  1.00 12.96           C  
ANISOU 1824  CB  LEU A 218     1721   1790   1415    -96     -9      3       C  
ATOM   1825  CG  LEU A 218      -3.965  12.671 -11.604  1.00 15.02           C  
ANISOU 1825  CG  LEU A 218     1931   2139   1638    -96      3    -67       C  
ATOM   1826  CD1 LEU A 218      -5.288  13.371 -11.308  1.00 14.79           C  
ANISOU 1826  CD1 LEU A 218     1898   2081   1642    -89      5    -95       C  
ATOM   1827  CD2 LEU A 218      -3.469  11.900 -10.388  1.00 15.71           C  
ANISOU 1827  CD2 LEU A 218     1954   2364   1652    -69     15    -37       C  
ATOM   1828  N   GLY A 219      -1.878  12.557 -14.979  1.00 11.16           N  
ANISOU 1828  N   GLY A 219     1574   1462   1206   -154     -9    -36       N  
ATOM   1829  CA  GLY A 219      -0.628  13.200 -15.334  1.00  9.62           C  
ANISOU 1829  CA  GLY A 219     1381   1267   1007   -182      3    -70       C  
ATOM   1830  C   GLY A 219      -0.841  14.269 -16.390  1.00 15.87           C  
ANISOU 1830  C   GLY A 219     2219   1966   1848   -207      2    -86       C  
ATOM   1831  O   GLY A 219      -0.247  15.342 -16.326  1.00 16.76           O  
ANISOU 1831  O   GLY A 219     2318   2066   1983   -235     17   -134       O  
ATOM   1832  N   CYS A 220      -1.703  13.980 -17.363  1.00 15.21           N  
ANISOU 1832  N   CYS A 220     2181   1817   1781   -199    -14    -42       N  
ATOM   1833  CA  CYS A 220      -2.013  14.950 -18.410  1.00 13.75           C  
ANISOU 1833  CA  CYS A 220     2033   1556   1636   -215    -16    -34       C  
ATOM   1834  C   CYS A 220      -2.677  16.188 -17.820  1.00 14.60           C  
ANISOU 1834  C   CYS A 220     2117   1635   1796   -218    -10    -72       C  
ATOM   1835  O   CYS A 220      -2.398  17.313 -18.236  1.00 16.20           O  
ANISOU 1835  O   CYS A 220     2324   1782   2047   -237      8    -85       O  
ATOM   1836  CB  CYS A 220      -2.917  14.330 -19.477  1.00 13.05           C  
ANISOU 1836  CB  CYS A 220     1987   1430   1541   -203    -43     18       C  
ATOM   1837  SG  CYS A 220      -2.104  13.046 -20.451  1.00 13.85           S  
ANISOU 1837  SG  CYS A 220     2124   1544   1594   -204    -40     44       S  
ATOM   1838  N   MET A 221      -3.558  15.970 -16.847  1.00 12.96           N  
ANISOU 1838  N   MET A 221     1879   1459   1585   -199    -18    -88       N  
ATOM   1839  CA  MET A 221      -4.201  17.073 -16.149  1.00 14.64           C  
ANISOU 1839  CA  MET A 221     2064   1651   1848   -198     -3   -138       C  
ATOM   1840  C   MET A 221      -3.162  17.901 -15.397  1.00 17.13           C  
ANISOU 1840  C   MET A 221     2344   1994   2171   -226     25   -223       C  
ATOM   1841  O   MET A 221      -3.146  19.131 -15.487  1.00 18.39           O  
ANISOU 1841  O   MET A 221     2498   2087   2402   -245     49   -266       O  
ATOM   1842  CB  MET A 221      -5.269  16.544 -15.185  1.00 17.51           C  
ANISOU 1842  CB  MET A 221     2396   2063   2194   -169    -11   -139       C  
ATOM   1843  CG  MET A 221      -6.492  15.981 -15.885  1.00 19.66           C  
ANISOU 1843  CG  MET A 221     2691   2296   2484   -148    -39    -68       C  
ATOM   1844  SD  MET A 221      -7.839  15.648 -14.727  1.00 20.54           S  
ANISOU 1844  SD  MET A 221     2755   2450   2598   -116    -38    -67       S  
ATOM   1845  CE  MET A 221      -7.911  17.209 -13.883  1.00 13.45           C  
ANISOU 1845  CE  MET A 221     1825   1541   1745   -118      1   -158       C  
ATOM   1846  N   LEU A 222      -2.287  17.219 -14.668  1.00 15.20           N  
ANISOU 1846  N   LEU A 222     2069   1846   1860   -230     25   -246       N  
ATOM   1847  CA  LEU A 222      -1.264  17.910 -13.895  1.00 16.21           C  
ANISOU 1847  CA  LEU A 222     2153   2024   1983   -262     43   -334       C  
ATOM   1848  C   LEU A 222      -0.393  18.777 -14.799  1.00 15.79           C  
ANISOU 1848  C   LEU A 222     2118   1891   1991   -300     62   -345       C  
ATOM   1849  O   LEU A 222      -0.162  19.952 -14.498  1.00 18.06           O  
ANISOU 1849  O   LEU A 222     2381   2141   2342   -332     87   -424       O  
ATOM   1850  CB  LEU A 222      -0.406  16.912 -13.118  1.00 14.72           C  
ANISOU 1850  CB  LEU A 222     1924   1965   1705   -254     34   -331       C  
ATOM   1851  CG  LEU A 222       0.694  17.521 -12.246  1.00 15.86           C  
ANISOU 1851  CG  LEU A 222     2007   2193   1825   -290     43   -425       C  
ATOM   1852  CD1 LEU A 222       0.096  18.352 -11.114  1.00 18.98           C  
ANISOU 1852  CD1 LEU A 222     2360   2629   2221   -297     54   -529       C  
ATOM   1853  CD2 LEU A 222       1.591  16.422 -11.700  1.00 17.32           C  
ANISOU 1853  CD2 LEU A 222     2151   2508   1921   -274     30   -388       C  
ATOM   1854  N   ALA A 223       0.069  18.209 -15.911  1.00 13.61           N  
ANISOU 1854  N   ALA A 223     1883   1585   1703   -297     56   -269       N  
ATOM   1855  CA  ALA A 223       0.959  18.931 -16.813  1.00 15.89           C  
ANISOU 1855  CA  ALA A 223     2186   1810   2041   -330     79   -262       C  
ATOM   1856  C   ALA A 223       0.277  20.200 -17.319  1.00 17.85           C  
ANISOU 1856  C   ALA A 223     2450   1944   2389   -338    100   -262       C  
ATOM   1857  O   ALA A 223       0.894  21.259 -17.393  1.00 18.55           O  
ANISOU 1857  O   ALA A 223     2518   1978   2552   -374    133   -303       O  
ATOM   1858  CB  ALA A 223       1.386  18.043 -17.981  1.00 14.15           C  
ANISOU 1858  CB  ALA A 223     2011   1585   1781   -317     72   -176       C  
ATOM   1859  N   SER A 224      -1.009  20.095 -17.639  1.00 17.67           N  
ANISOU 1859  N   SER A 224     2455   1883   2377   -305     84   -213       N  
ATOM   1860  CA  SER A 224      -1.750  21.248 -18.132  1.00 15.64           C  
ANISOU 1860  CA  SER A 224     2205   1519   2218   -301    104   -193       C  
ATOM   1861  C   SER A 224      -1.896  22.317 -17.050  1.00 16.42           C  
ANISOU 1861  C   SER A 224     2256   1588   2394   -319    137   -299       C  
ATOM   1862  O   SER A 224      -1.950  23.512 -17.349  1.00 18.51           O  
ANISOU 1862  O   SER A 224     2513   1749   2771   -332    176   -308       O  
ATOM   1863  CB  SER A 224      -3.132  20.826 -18.652  1.00 16.90           C  
ANISOU 1863  CB  SER A 224     2393   1661   2365   -259     74   -116       C  
ATOM   1864  OG  SER A 224      -3.999  20.447 -17.591  1.00 19.21           O  
ANISOU 1864  OG  SER A 224     2660   2000   2637   -238     60   -158       O  
ATOM   1865  N   MET A 225      -1.948  21.894 -15.791  1.00 15.94           N  
ANISOU 1865  N   MET A 225     2161   1619   2276   -318    127   -380       N  
ATOM   1866  CA  MET A 225      -2.140  22.844 -14.697  1.00 19.41           C  
ANISOU 1866  CA  MET A 225     2553   2050   2772   -334    158   -500       C  
ATOM   1867  C   MET A 225      -0.835  23.540 -14.304  1.00 20.34           C  
ANISOU 1867  C   MET A 225     2631   2174   2922   -392    185   -601       C  
ATOM   1868  O   MET A 225      -0.798  24.769 -14.184  1.00 22.70           O  
ANISOU 1868  O   MET A 225     2907   2381   3337   -421    229   -674       O  
ATOM   1869  CB  MET A 225      -2.747  22.147 -13.477  1.00 20.78           C  
ANISOU 1869  CB  MET A 225     2697   2339   2858   -308    139   -547       C  
ATOM   1870  CG  MET A 225      -4.188  21.680 -13.667  1.00 22.20           C  
ANISOU 1870  CG  MET A 225     2899   2500   3034   -257    122   -470       C  
ATOM   1871  SD  MET A 225      -4.862  20.865 -12.203  1.00 35.50           S  
ANISOU 1871  SD  MET A 225     4542   4324   4621   -226    111   -512       S  
ATOM   1872  CE  MET A 225      -3.600  19.656 -11.840  1.00 46.07           C  
ANISOU 1872  CE  MET A 225     5867   5801   5835   -238     82   -496       C  
ATOM   1873  N   ILE A 226       0.237  22.778 -14.102  1.00 17.29           N  
ANISOU 1873  N   ILE A 226     2231   1893   2447   -410    162   -606       N  
ATOM   1874  CA  ILE A 226       1.471  23.408 -13.634  1.00 16.02           C  
ANISOU 1874  CA  ILE A 226     2019   1757   2311   -470    181   -709       C  
ATOM   1875  C   ILE A 226       2.176  24.174 -14.756  1.00 15.23           C  
ANISOU 1875  C   ILE A 226     1934   1534   2317   -504    215   -668       C  
ATOM   1876  O   ILE A 226       2.848  25.162 -14.482  1.00 18.36           O  
ANISOU 1876  O   ILE A 226     2288   1886   2801   -558    249   -762       O  
ATOM   1877  CB  ILE A 226       2.457  22.392 -12.993  1.00 22.11           C  
ANISOU 1877  CB  ILE A 226     2754   2692   2956   -476    147   -723       C  
ATOM   1878  CG1 ILE A 226       3.046  21.431 -14.030  1.00 19.25           C  
ANISOU 1878  CG1 ILE A 226     2431   2333   2548   -458    131   -597       C  
ATOM   1879  CG2 ILE A 226       1.775  21.636 -11.853  1.00 23.02           C  
ANISOU 1879  CG2 ILE A 226     2846   2937   2965   -439    121   -747       C  
ATOM   1880  CD1 ILE A 226       4.054  20.448 -13.437  1.00 16.57           C  
ANISOU 1880  CD1 ILE A 226     2049   2143   2102   -458    105   -597       C  
ATOM   1881  N   PHE A 227       1.995  23.760 -16.011  1.00 17.28           N  
ANISOU 1881  N   PHE A 227     2459   1388   2717   -424   -202   -337       N  
ATOM   1882  CA  PHE A 227       2.634  24.451 -17.139  1.00 20.12           C  
ANISOU 1882  CA  PHE A 227     2870   1674   3100   -435   -210   -287       C  
ATOM   1883  C   PHE A 227       1.719  25.484 -17.796  1.00 21.93           C  
ANISOU 1883  C   PHE A 227     3143   1793   3398   -383   -235   -267       C  
ATOM   1884  O   PHE A 227       2.147  26.223 -18.690  1.00 21.73           O  
ANISOU 1884  O   PHE A 227     3176   1691   3390   -394   -242   -216       O  
ATOM   1885  CB  PHE A 227       3.099  23.447 -18.201  1.00 18.28           C  
ANISOU 1885  CB  PHE A 227     2650   1462   2834   -404   -261   -224       C  
ATOM   1886  CG  PHE A 227       4.196  22.537 -17.740  1.00 18.87           C  
ANISOU 1886  CG  PHE A 227     2691   1628   2851   -455   -249   -231       C  
ATOM   1887  CD1 PHE A 227       5.260  23.029 -17.002  1.00 20.06           C  
ANISOU 1887  CD1 PHE A 227     2813   1822   2988   -547   -202   -263       C  
ATOM   1888  CD2 PHE A 227       4.157  21.184 -18.034  1.00 15.80           C  
ANISOU 1888  CD2 PHE A 227     2294   1284   2423   -412   -287   -208       C  
ATOM   1889  CE1 PHE A 227       6.276  22.187 -16.570  1.00 19.74           C  
ANISOU 1889  CE1 PHE A 227     2732   1879   2888   -592   -210   -263       C  
ATOM   1890  CE2 PHE A 227       5.164  20.335 -17.605  1.00 18.31           C  
ANISOU 1890  CE2 PHE A 227     2588   1679   2690   -454   -288   -207       C  
ATOM   1891  CZ  PHE A 227       6.228  20.842 -16.872  1.00 18.94           C  
ANISOU 1891  CZ  PHE A 227     2632   1823   2742   -538   -248   -229       C  
ATOM   1892  N   ARG A 228       0.465  25.532 -17.356  1.00 21.66           N  
ANISOU 1892  N   ARG A 228     3077   1749   3403   -328   -250   -305       N  
ATOM   1893  CA  ARG A 228      -0.531  26.435 -17.931  1.00 23.84           C  
ANISOU 1893  CA  ARG A 228     3377   1923   3759   -264   -288   -292       C  
ATOM   1894  C   ARG A 228      -0.646  26.277 -19.446  1.00 24.22           C  
ANISOU 1894  C   ARG A 228     3469   1922   3812   -206   -364   -208       C  
ATOM   1895  O   ARG A 228      -0.492  27.237 -20.208  1.00 23.15           O  
ANISOU 1895  O   ARG A 228     3400   1691   3705   -200   -378   -155       O  
ATOM   1896  CB  ARG A 228      -0.218  27.887 -17.562  1.00 28.63           C  
ANISOU 1896  CB  ARG A 228     4031   2445   4402   -315   -238   -308       C  
ATOM   1897  CG  ARG A 228      -0.416  28.179 -16.092  1.00 34.16           C  
ANISOU 1897  CG  ARG A 228     4691   3188   5098   -362   -193   -387       C  
ATOM   1898  CD  ARG A 228      -1.355  29.361 -15.894  1.00 42.77           C  
ANISOU 1898  CD  ARG A 228     5790   4179   6282   -326   -194   -419       C  
ATOM   1899  NE  ARG A 228      -1.565  29.667 -14.481  1.00 47.62           N  
ANISOU 1899  NE  ARG A 228     6354   4839   6899   -371   -158   -494       N  
ATOM   1900  CZ  ARG A 228      -1.501  30.891 -13.967  1.00 50.07           C  
ANISOU 1900  CZ  ARG A 228     6689   5080   7255   -408   -127   -526       C  
ATOM   1901  NH1 ARG A 228      -1.230  31.927 -14.750  1.00 51.89           N  
ANISOU 1901  NH1 ARG A 228     7010   5184   7523   -408   -123   -487       N  
ATOM   1902  NH2 ARG A 228      -1.707  31.079 -12.670  1.00 49.83           N  
ANISOU 1902  NH2 ARG A 228     6592   5107   7233   -446    -97   -594       N  
ATOM   1903  N   LYS A 229      -0.926  25.047 -19.861  1.00 22.25           N  
ANISOU 1903  N   LYS A 229     3192   1738   3524   -168   -410   -195       N  
ATOM   1904  CA  LYS A 229      -1.122  24.707 -21.261  1.00 24.91           C  
ANISOU 1904  CA  LYS A 229     3573   2051   3842   -120   -491   -121       C  
ATOM   1905  C   LYS A 229      -2.189  23.625 -21.342  1.00 23.00           C  
ANISOU 1905  C   LYS A 229     3277   1863   3598    -60   -539   -154       C  
ATOM   1906  O   LYS A 229      -1.911  22.465 -21.050  1.00 20.97           O  
ANISOU 1906  O   LYS A 229     2993   1687   3287    -77   -515   -175       O  
ATOM   1907  CB  LYS A 229       0.186  24.227 -21.896  1.00 24.57           C  
ANISOU 1907  CB  LYS A 229     3579   2038   3717   -174   -483    -61       C  
ATOM   1908  CG  LYS A 229       0.072  23.865 -23.368  1.00 26.78           C  
ANISOU 1908  CG  LYS A 229     3920   2303   3953   -143   -560     21       C  
ATOM   1909  CD  LYS A 229       1.364  23.274 -23.907  1.00 27.81           C  
ANISOU 1909  CD  LYS A 229     4094   2479   3995   -208   -542     69       C  
ATOM   1910  CE  LYS A 229       1.289  23.066 -25.417  1.00 30.85           C  
ANISOU 1910  CE  LYS A 229     4552   2848   4320   -196   -609    154       C  
ATOM   1911  NZ  LYS A 229       0.063  22.334 -25.852  1.00 31.75           N  
ANISOU 1911  NZ  LYS A 229     4643   2976   4446   -121   -678    143       N  
ATOM   1912  N   GLU A 230      -3.410  24.001 -21.711  1.00 26.85           N  
ANISOU 1912  N   GLU A 230     3750   2305   4149      8   -603   -164       N  
ATOM   1913  CA  GLU A 230      -4.522  23.050 -21.719  1.00 31.95           C  
ANISOU 1913  CA  GLU A 230     4335   3002   4801     56   -644   -215       C  
ATOM   1914  C   GLU A 230      -5.134  22.896 -23.109  1.00 30.98           C  
ANISOU 1914  C   GLU A 230     4248   2846   4677    116   -753   -163       C  
ATOM   1915  O   GLU A 230      -5.628  23.870 -23.678  1.00 32.35           O  
ANISOU 1915  O   GLU A 230     4447   2941   4903    163   -814   -127       O  
ATOM   1916  CB  GLU A 230      -5.608  23.487 -20.734  1.00 36.34           C  
ANISOU 1916  CB  GLU A 230     4815   3555   5436     81   -628   -302       C  
ATOM   1917  CG  GLU A 230      -6.314  22.334 -20.026  1.00 38.18           C  
ANISOU 1917  CG  GLU A 230     4976   3884   5646     79   -600   -379       C  
ATOM   1918  CD  GLU A 230      -7.430  21.722 -20.861  1.00 41.32           C  
ANISOU 1918  CD  GLU A 230     5347   4290   6063    141   -685   -401       C  
ATOM   1919  OE1 GLU A 230      -7.689  20.507 -20.722  1.00 39.11           O  
ANISOU 1919  OE1 GLU A 230     5041   4089   5730    130   -660   -436       O  
ATOM   1920  OE2 GLU A 230      -8.034  22.446 -21.678  1.00 43.28           O  
ANISOU 1920  OE2 GLU A 230     5606   4465   6373    202   -777   -381       O  
ATOM   1921  N   PRO A 231      -5.114  21.668 -23.654  1.00 27.43           N  
ANISOU 1921  N   PRO A 231     3805   2454   4163    115   -774   -159       N  
ATOM   1922  CA  PRO A 231      -4.496  20.495 -23.028  1.00 23.95           C  
ANISOU 1922  CA  PRO A 231     3343   2100   3658     66   -695   -193       C  
ATOM   1923  C   PRO A 231      -2.998  20.477 -23.287  1.00 21.85           C  
ANISOU 1923  C   PRO A 231     3139   1836   3328      8   -656   -124       C  
ATOM   1924  O   PRO A 231      -2.525  21.252 -24.118  1.00 22.87           O  
ANISOU 1924  O   PRO A 231     3334   1908   3448      0   -692    -49       O  
ATOM   1925  CB  PRO A 231      -5.191  19.330 -23.724  1.00 23.64           C  
ANISOU 1925  CB  PRO A 231     3299   2098   3586     95   -741   -215       C  
ATOM   1926  CG  PRO A 231      -5.440  19.851 -25.097  1.00 26.06           C  
ANISOU 1926  CG  PRO A 231     3668   2338   3897    134   -849   -143       C  
ATOM   1927  CD  PRO A 231      -5.764  21.320 -24.930  1.00 28.68           C  
ANISOU 1927  CD  PRO A 231     3995   2596   4305    165   -877   -123       C  
ATOM   1928  N   PHE A 232      -2.264  19.618 -22.586  1.00 18.78           N  
ANISOU 1928  N   PHE A 232     2731   1515   2892    -33   -583   -149       N  
ATOM   1929  CA  PHE A 232      -0.815  19.574 -22.729  1.00 18.24           C  
ANISOU 1929  CA  PHE A 232     2706   1454   2770    -88   -549    -99       C  
ATOM   1930  C   PHE A 232      -0.412  18.876 -24.019  1.00 19.87           C  
ANISOU 1930  C   PHE A 232     2975   1663   2911    -94   -588    -38       C  
ATOM   1931  O   PHE A 232       0.294  19.449 -24.851  1.00 22.12           O  
ANISOU 1931  O   PHE A 232     3326   1913   3166   -126   -608     33       O  
ATOM   1932  CB  PHE A 232      -0.176  18.870 -21.530  1.00 19.58           C  
ANISOU 1932  CB  PHE A 232     2833   1691   2917   -123   -474   -144       C  
ATOM   1933  CG  PHE A 232       1.324  18.962 -21.509  1.00 17.97           C  
ANISOU 1933  CG  PHE A 232     2659   1495   2674   -182   -448   -106       C  
ATOM   1934  CD1 PHE A 232       1.945  20.178 -21.295  1.00 20.00           C  
ANISOU 1934  CD1 PHE A 232     2931   1714   2953   -228   -432    -92       C  
ATOM   1935  CD2 PHE A 232       2.106  17.838 -21.704  1.00 18.01           C  
ANISOU 1935  CD2 PHE A 232     2680   1542   2622   -198   -436    -90       C  
ATOM   1936  CE1 PHE A 232       3.322  20.276 -21.279  1.00 18.08           C  
ANISOU 1936  CE1 PHE A 232     2711   1489   2670   -297   -408    -65       C  
ATOM   1937  CE2 PHE A 232       3.486  17.926 -21.687  1.00 20.83           C  
ANISOU 1937  CE2 PHE A 232     3051   1928   2937   -254   -410    -58       C  
ATOM   1938  CZ  PHE A 232       4.092  19.151 -21.473  1.00 17.55           C  
ANISOU 1938  CZ  PHE A 232     2648   1481   2540   -311   -402    -48       C  
ATOM   1939  N   PHE A 233      -0.853  17.631 -24.171  1.00 14.74           N  
ANISOU 1939  N   PHE A 233     2311   1056   2232    -74   -585    -71       N  
ATOM   1940  CA  PHE A 233      -0.623  16.878 -25.395  1.00 15.23           C  
ANISOU 1940  CA  PHE A 233     2432   1126   2229    -83   -612    -27       C  
ATOM   1941  C   PHE A 233      -1.794  17.124 -26.339  1.00 17.13           C  
ANISOU 1941  C   PHE A 233     2686   1344   2480    -40   -693    -15       C  
ATOM   1942  O   PHE A 233      -2.842  16.506 -26.193  1.00 17.18           O  
ANISOU 1942  O   PHE A 233     2650   1372   2505     -4   -706    -82       O  
ATOM   1943  CB  PHE A 233      -0.481  15.384 -25.103  1.00 15.81           C  
ANISOU 1943  CB  PHE A 233     2477   1276   2256    -83   -546    -73       C  
ATOM   1944  CG  PHE A 233       0.706  15.033 -24.243  1.00 16.21           C  
ANISOU 1944  CG  PHE A 233     2510   1363   2287   -111   -475    -73       C  
ATOM   1945  CD1 PHE A 233       1.999  15.241 -24.700  1.00 18.63           C  
ANISOU 1945  CD1 PHE A 233     2837   1699   2541   -150   -449    -14       C  
ATOM   1946  CD2 PHE A 233       0.528  14.458 -22.994  1.00 14.08           C  
ANISOU 1946  CD2 PHE A 233     2200   1106   2043   -102   -437   -134       C  
ATOM   1947  CE1 PHE A 233       3.093  14.899 -23.916  1.00 14.96           C  
ANISOU 1947  CE1 PHE A 233     2343   1285   2058   -168   -391    -17       C  
ATOM   1948  CE2 PHE A 233       1.615  14.107 -22.207  1.00 14.36           C  
ANISOU 1948  CE2 PHE A 233     2216   1187   2053   -121   -383   -126       C  
ATOM   1949  CZ  PHE A 233       2.902  14.329 -22.670  1.00 14.41           C  
ANISOU 1949  CZ  PHE A 233     2232   1230   2012   -148   -363    -68       C  
ATOM   1950  N   HIS A 234      -1.611  18.028 -27.297  1.00 19.36           N  
ANISOU 1950  N   HIS A 234     3025   1587   2744    -46   -748     69       N  
ATOM   1951  CA  HIS A 234      -2.729  18.538 -28.090  1.00 21.25           C  
ANISOU 1951  CA  HIS A 234     3277   1793   3003      7   -844     94       C  
ATOM   1952  C   HIS A 234      -2.738  17.973 -29.509  1.00 20.97           C  
ANISOU 1952  C   HIS A 234     3278   1830   2861    -12   -869    150       C  
ATOM   1953  O   HIS A 234      -2.474  18.693 -30.474  1.00 21.76           O  
ANISOU 1953  O   HIS A 234     3445   1904   2917    -29   -920    244       O  
ATOM   1954  CB  HIS A 234      -2.673  20.065 -28.132  1.00 27.19           C  
ANISOU 1954  CB  HIS A 234     4072   2447   3814     20   -891    155       C  
ATOM   1955  CG  HIS A 234      -3.984  20.712 -28.459  1.00 31.74           C  
ANISOU 1955  CG  HIS A 234     4628   2983   4450    100   -984    155       C  
ATOM   1956  ND1 HIS A 234      -4.250  22.034 -28.172  1.00 33.90           N  
ANISOU 1956  ND1 HIS A 234     4896   3193   4794    129   -995    168       N  
ATOM   1957  CD2 HIS A 234      -5.101  20.221 -29.043  1.00 33.65           C  
ANISOU 1957  CD2 HIS A 234     4845   3249   4690    160  -1066    139       C  
ATOM   1958  CE1 HIS A 234      -5.476  22.329 -28.568  1.00 35.71           C  
ANISOU 1958  CE1 HIS A 234     5098   3401   5068    208  -1084    163       C  
ATOM   1959  NE2 HIS A 234      -6.014  21.246 -29.099  1.00 34.63           N  
ANISOU 1959  NE2 HIS A 234     4946   3321   4888    230  -1135    145       N  
ATOM   1960  N   GLY A 235      -3.051  16.685 -29.630  1.00 20.09           N  
ANISOU 1960  N   GLY A 235     3126   1806   2702    -18   -830     89       N  
ATOM   1961  CA  GLY A 235      -3.056  16.014 -30.919  1.00 21.18           C  
ANISOU 1961  CA  GLY A 235     3288   2025   2733    -50   -836    121       C  
ATOM   1962  C   GLY A 235      -4.301  16.287 -31.748  1.00 23.62           C  
ANISOU 1962  C   GLY A 235     3588   2354   3032     -6   -939    134       C  
ATOM   1963  O   GLY A 235      -5.380  16.559 -31.206  1.00 21.00           O  
ANISOU 1963  O   GLY A 235     3202   1996   2782     61   -990     79       O  
ATOM   1964  N   HIS A 236      -4.152  16.200 -33.067  1.00 24.70           N  
ANISOU 1964  N   HIS A 236     3770   2547   3066    -46   -970    202       N  
ATOM   1965  CA  HIS A 236      -5.260  16.454 -33.988  1.00 28.71           C  
ANISOU 1965  CA  HIS A 236     4270   3097   3542     -8  -1078    229       C  
ATOM   1966  C   HIS A 236      -6.134  15.222 -34.209  1.00 25.81           C  
ANISOU 1966  C   HIS A 236     3832   2842   3132    -14  -1054    129       C  
ATOM   1967  O   HIS A 236      -7.288  15.333 -34.638  1.00 27.73           O  
ANISOU 1967  O   HIS A 236     4033   3133   3372     32  -1142    111       O  
ATOM   1968  CB  HIS A 236      -4.725  16.956 -35.328  1.00 36.76           C  
ANISOU 1968  CB  HIS A 236     5376   4134   4455    -62  -1126    352       C  
ATOM   1969  CG  HIS A 236      -3.948  18.229 -35.226  1.00 48.09           C  
ANISOU 1969  CG  HIS A 236     6894   5455   5922    -67  -1151    452       C  
ATOM   1970  ND1 HIS A 236      -2.702  18.391 -35.791  1.00 53.15           N  
ANISOU 1970  ND1 HIS A 236     7616   6096   6482   -160  -1101    521       N  
ATOM   1971  CD2 HIS A 236      -4.235  19.402 -34.609  1.00 53.00           C  
ANISOU 1971  CD2 HIS A 236     7531   5956   6651      3  -1209    484       C  
ATOM   1972  CE1 HIS A 236      -2.259  19.610 -35.539  1.00 54.79           C  
ANISOU 1972  CE1 HIS A 236     7890   6190   6738   -154  -1127    593       C  
ATOM   1973  NE2 HIS A 236      -3.171  20.243 -34.820  1.00 54.62           N  
ANISOU 1973  NE2 HIS A 236     7831   6087   6833    -53  -1191    574       N  
ATOM   1974  N   ASP A 237      -5.574  14.051 -33.925  1.00 18.21           N  
ANISOU 1974  N   ASP A 237     2858   1924   2137    -70   -934     61       N  
ATOM   1975  CA  ASP A 237      -6.307  12.794 -33.984  1.00 19.48           C  
ANISOU 1975  CA  ASP A 237     2963   2176   2264    -88   -882    -48       C  
ATOM   1976  C   ASP A 237      -5.560  11.793 -33.107  1.00 20.58           C  
ANISOU 1976  C   ASP A 237     3100   2298   2422   -119   -746   -114       C  
ATOM   1977  O   ASP A 237      -4.588  12.165 -32.453  1.00 18.63           O  
ANISOU 1977  O   ASP A 237     2880   1982   2217   -117   -712    -75       O  
ATOM   1978  CB  ASP A 237      -6.455  12.287 -35.430  1.00 23.30           C  
ANISOU 1978  CB  ASP A 237     3462   2773   2619   -152   -894    -28       C  
ATOM   1979  CG  ASP A 237      -5.121  12.182 -36.169  1.00 28.70           C  
ANISOU 1979  CG  ASP A 237     4219   3466   3221   -233   -837     47       C  
ATOM   1980  OD1 ASP A 237      -4.145  11.650 -35.600  1.00 26.68           O  
ANISOU 1980  OD1 ASP A 237     3975   3177   2985   -259   -731     24       O  
ATOM   1981  OD2 ASP A 237      -5.055  12.613 -37.341  1.00 34.16           O  
ANISOU 1981  OD2 ASP A 237     4952   4205   3823   -274   -900    127       O  
ATOM   1982  N   ASN A 238      -5.994  10.535 -33.092  1.00 20.51           N  
ANISOU 1982  N   ASN A 238     3061   2351   2380   -148   -667   -211       N  
ATOM   1983  CA  ASN A 238      -5.411   9.564 -32.167  1.00 22.75           C  
ANISOU 1983  CA  ASN A 238     3348   2606   2692   -162   -544   -270       C  
ATOM   1984  C   ASN A 238      -3.988   9.171 -32.554  1.00 22.46           C  
ANISOU 1984  C   ASN A 238     3360   2568   2606   -209   -466   -216       C  
ATOM   1985  O   ASN A 238      -3.201   8.758 -31.703  1.00 21.51           O  
ANISOU 1985  O   ASN A 238     3247   2404   2523   -199   -389   -225       O  
ATOM   1986  CB  ASN A 238      -6.296   8.314 -32.061  1.00 24.65           C  
ANISOU 1986  CB  ASN A 238     3556   2900   2910   -186   -472   -392       C  
ATOM   1987  CG  ASN A 238      -7.603   8.581 -31.315  1.00 24.14           C  
ANISOU 1987  CG  ASN A 238     3432   2830   2910   -142   -523   -474       C  
ATOM   1988  OD1 ASN A 238      -7.729   9.574 -30.594  1.00 22.53           O  
ANISOU 1988  OD1 ASN A 238     3210   2563   2786    -87   -591   -449       O  
ATOM   1989  ND2 ASN A 238      -8.585   7.700 -31.500  1.00 23.69           N  
ANISOU 1989  ND2 ASN A 238     3340   2843   2818   -174   -485   -582       N  
ATOM   1990  N   TYR A 239      -3.651   9.309 -33.833  1.00 20.70           N  
ANISOU 1990  N   TYR A 239     3166   2399   2299   -260   -486   -161       N  
ATOM   1991  CA  TYR A 239      -2.300   9.005 -34.289  1.00 20.78           C  
ANISOU 1991  CA  TYR A 239     3215   2418   2264   -312   -412   -120       C  
ATOM   1992  C   TYR A 239      -1.356  10.150 -33.940  1.00 19.80           C  
ANISOU 1992  C   TYR A 239     3118   2231   2174   -296   -454    -31       C  
ATOM   1993  O   TYR A 239      -0.290   9.938 -33.358  1.00 18.73           O  
ANISOU 1993  O   TYR A 239     2985   2069   2064   -296   -385    -26       O  
ATOM   1994  CB  TYR A 239      -2.291   8.729 -35.794  1.00 24.85           C  
ANISOU 1994  CB  TYR A 239     3752   3023   2668   -391   -410   -105       C  
ATOM   1995  CG  TYR A 239      -3.318   7.690 -36.183  1.00 30.21           C  
ANISOU 1995  CG  TYR A 239     4399   3774   3306   -418   -371   -202       C  
ATOM   1996  CD1 TYR A 239      -4.461   8.043 -36.890  1.00 33.95           C  
ANISOU 1996  CD1 TYR A 239     4852   4317   3731   -425   -466   -204       C  
ATOM   1997  CD2 TYR A 239      -3.164   6.364 -35.806  1.00 30.79           C  
ANISOU 1997  CD2 TYR A 239     4464   3846   3390   -434   -240   -292       C  
ATOM   1998  CE1 TYR A 239      -5.408   7.096 -37.232  1.00 36.62           C  
ANISOU 1998  CE1 TYR A 239     5152   4736   4024   -461   -425   -306       C  
ATOM   1999  CE2 TYR A 239      -4.110   5.409 -36.141  1.00 34.38           C  
ANISOU 1999  CE2 TYR A 239     4895   4363   3804   -471   -190   -391       C  
ATOM   2000  CZ  TYR A 239      -5.228   5.782 -36.851  1.00 37.59           C  
ANISOU 2000  CZ  TYR A 239     5273   4853   4158   -490   -282   -403       C  
ATOM   2001  OH  TYR A 239      -6.170   4.836 -37.189  1.00 41.98           O  
ANISOU 2001  OH  TYR A 239     5797   5486   4666   -538   -228   -513       O  
ATOM   2002  N   ASP A 240      -1.759  11.366 -34.286  1.00 18.87           N  
ANISOU 2002  N   ASP A 240     3020   2091   2058   -282   -566     38       N  
ATOM   2003  CA  ASP A 240      -0.970  12.542 -33.947  1.00 18.90           C  
ANISOU 2003  CA  ASP A 240     3058   2026   2098   -276   -602    116       C  
ATOM   2004  C   ASP A 240      -0.826  12.659 -32.437  1.00 18.94           C  
ANISOU 2004  C   ASP A 240     3028   1964   2205   -220   -575     79       C  
ATOM   2005  O   ASP A 240       0.179  13.151 -31.945  1.00 19.59           O  
ANISOU 2005  O   ASP A 240     3124   2010   2309   -232   -550    112       O  
ATOM   2006  CB  ASP A 240      -1.612  13.807 -34.516  1.00 21.71           C  
ANISOU 2006  CB  ASP A 240     3448   2350   2450   -257   -728    195       C  
ATOM   2007  CG  ASP A 240      -0.789  15.041 -34.247  1.00 22.91           C  
ANISOU 2007  CG  ASP A 240     3651   2421   2634   -264   -754    274       C  
ATOM   2008  OD1 ASP A 240       0.418  15.035 -34.575  1.00 22.38           O  
ANISOU 2008  OD1 ASP A 240     3620   2368   2514   -333   -695    306       O  
ATOM   2009  OD2 ASP A 240      -1.344  16.010 -33.692  1.00 24.97           O  
ANISOU 2009  OD2 ASP A 240     3912   2602   2973   -205   -825    295       O  
ATOM   2010  N   GLN A 241      -1.828  12.189 -31.704  1.00 17.36           N  
ANISOU 2010  N   GLN A 241     2781   1757   2058   -172   -576      2       N  
ATOM   2011  CA  GLN A 241      -1.771  12.219 -30.249  1.00 16.87           C  
ANISOU 2011  CA  GLN A 241     2687   1642   2081   -131   -547    -41       C  
ATOM   2012  C   GLN A 241      -0.560  11.445 -29.730  1.00 15.53           C  
ANISOU 2012  C   GLN A 241     2518   1485   1900   -151   -446    -49       C  
ATOM   2013  O   GLN A 241       0.120  11.900 -28.816  1.00 14.51           O  
ANISOU 2013  O   GLN A 241     2379   1320   1813   -141   -433    -34       O  
ATOM   2014  CB  GLN A 241      -3.055  11.650 -29.642  1.00 18.11           C  
ANISOU 2014  CB  GLN A 241     2797   1804   2280    -95   -549   -135       C  
ATOM   2015  CG  GLN A 241      -3.115  11.753 -28.128  1.00 17.42           C  
ANISOU 2015  CG  GLN A 241     2680   1665   2276    -64   -525   -183       C  
ATOM   2016  CD  GLN A 241      -3.233  13.186 -27.642  1.00 17.55           C  
ANISOU 2016  CD  GLN A 241     2690   1613   2366    -37   -601   -151       C  
ATOM   2017  OE1 GLN A 241      -3.714  14.058 -28.361  1.00 17.35           O  
ANISOU 2017  OE1 GLN A 241     2675   1569   2347    -19   -685   -108       O  
ATOM   2018  NE2 GLN A 241      -2.789  13.436 -26.415  1.00 17.15           N  
ANISOU 2018  NE2 GLN A 241     2623   1524   2370    -34   -568   -169       N  
ATOM   2019  N   LEU A 242      -0.282  10.282 -30.313  1.00 12.77           N  
ANISOU 2019  N   LEU A 242     2173   1188   1492   -178   -372    -74       N  
ATOM   2020  CA  LEU A 242       0.864   9.497 -29.866  1.00 12.78           C  
ANISOU 2020  CA  LEU A 242     2169   1198   1487   -180   -278    -80       C  
ATOM   2021  C   LEU A 242       2.171  10.169 -30.294  1.00 11.69           C  
ANISOU 2021  C   LEU A 242     2047   1073   1320   -216   -277    -13       C  
ATOM   2022  O   LEU A 242       3.168  10.108 -29.573  1.00 13.73           O  
ANISOU 2022  O   LEU A 242     2287   1331   1600   -205   -235     -5       O  
ATOM   2023  CB  LEU A 242       0.792   8.067 -30.406  1.00 14.70           C  
ANISOU 2023  CB  LEU A 242     2417   1481   1687   -197   -190   -132       C  
ATOM   2024  CG  LEU A 242       1.905   7.112 -29.957  1.00 13.61           C  
ANISOU 2024  CG  LEU A 242     2273   1344   1554   -180    -90   -141       C  
ATOM   2025  CD1 LEU A 242       1.962   6.977 -28.437  1.00 12.34           C  
ANISOU 2025  CD1 LEU A 242     2094   1140   1456   -124    -78   -153       C  
ATOM   2026  CD2 LEU A 242       1.739   5.745 -30.607  1.00 16.94           C  
ANISOU 2026  CD2 LEU A 242     2708   1789   1939   -200      3   -198       C  
ATOM   2027  N   VAL A 243       2.160  10.813 -31.461  1.00 13.88           N  
ANISOU 2027  N   VAL A 243     2360   1370   1545   -265   -324     34       N  
ATOM   2028  CA  VAL A 243       3.342  11.529 -31.938  1.00 14.80           C  
ANISOU 2028  CA  VAL A 243     2501   1499   1624   -318   -320     93       C  
ATOM   2029  C   VAL A 243       3.662  12.693 -31.003  1.00 17.11           C  
ANISOU 2029  C   VAL A 243     2791   1735   1974   -301   -362    125       C  
ATOM   2030  O   VAL A 243       4.823  12.915 -30.659  1.00 17.12           O  
ANISOU 2030  O   VAL A 243     2780   1751   1973   -325   -321    137       O  
ATOM   2031  CB  VAL A 243       3.169  12.048 -33.385  1.00 17.77           C  
ANISOU 2031  CB  VAL A 243     2931   1901   1920   -384   -368    144       C  
ATOM   2032  CG1 VAL A 243       4.414  12.828 -33.828  1.00 16.47           C  
ANISOU 2032  CG1 VAL A 243     2800   1744   1712   -454   -355    198       C  
ATOM   2033  CG2 VAL A 243       2.916  10.881 -34.336  1.00 19.51           C  
ANISOU 2033  CG2 VAL A 243     3147   2190   2074   -419   -316    101       C  
ATOM   2034  N   ARG A 244       2.634  13.421 -30.576  1.00 14.39           N  
ANISOU 2034  N   ARG A 244     2451   1333   1684   -263   -437    129       N  
ATOM   2035  CA  ARG A 244       2.828  14.514 -29.617  1.00 14.15           C  
ANISOU 2035  CA  ARG A 244     2417   1241   1719   -250   -466    145       C  
ATOM   2036  C   ARG A 244       3.482  14.002 -28.346  1.00 13.91           C  
ANISOU 2036  C   ARG A 244     2333   1228   1725   -230   -402    101       C  
ATOM   2037  O   ARG A 244       4.402  14.621 -27.822  1.00 14.47           O  
ANISOU 2037  O   ARG A 244     2395   1298   1805   -256   -385    117       O  
ATOM   2038  CB  ARG A 244       1.500  15.192 -29.256  1.00 18.70           C  
ANISOU 2038  CB  ARG A 244     2990   1750   2364   -200   -547    135       C  
ATOM   2039  CG  ARG A 244       0.721  15.792 -30.418  1.00 27.94           C  
ANISOU 2039  CG  ARG A 244     4207   2901   3506   -200   -631    187       C  
ATOM   2040  CD  ARG A 244       1.457  16.946 -31.053  1.00 30.78           C  
ANISOU 2040  CD  ARG A 244     4638   3223   3834   -252   -659    274       C  
ATOM   2041  NE  ARG A 244       0.688  17.563 -32.133  1.00 33.36           N  
ANISOU 2041  NE  ARG A 244     5019   3526   4130   -245   -751    340       N  
ATOM   2042  CZ  ARG A 244       0.423  18.864 -32.213  1.00 35.05           C  
ANISOU 2042  CZ  ARG A 244     5285   3648   4383   -228   -822    403       C  
ATOM   2043  NH1 ARG A 244       0.862  19.694 -31.274  1.00 34.66           N  
ANISOU 2043  NH1 ARG A 244     5239   3522   4408   -229   -801    397       N  
ATOM   2044  NH2 ARG A 244      -0.275  19.339 -33.234  1.00 35.94           N  
ANISOU 2044  NH2 ARG A 244     5448   3747   4461   -213   -912    473       N  
ATOM   2045  N   ILE A 245       3.011  12.861 -27.854  1.00 11.97           N  
ANISOU 2045  N   ILE A 245     2054   1002   1493   -188   -366     47       N  
ATOM   2046  CA  ILE A 245       3.588  12.271 -26.650  1.00 12.04           C  
ANISOU 2046  CA  ILE A 245     2020   1028   1527   -162   -311     16       C  
ATOM   2047  C   ILE A 245       5.044  11.856 -26.888  1.00 14.38           C  
ANISOU 2047  C   ILE A 245     2302   1386   1777   -184   -249     37       C  
ATOM   2048  O   ILE A 245       5.921  12.155 -26.076  1.00 14.22           O  
ANISOU 2048  O   ILE A 245     2248   1387   1768   -187   -231     43       O  
ATOM   2049  CB  ILE A 245       2.759  11.062 -26.177  1.00 11.74           C  
ANISOU 2049  CB  ILE A 245     1967    989   1503   -119   -278    -42       C  
ATOM   2050  CG1 ILE A 245       1.364  11.536 -25.742  1.00 14.04           C  
ANISOU 2050  CG1 ILE A 245     2254   1231   1847   -101   -336    -82       C  
ATOM   2051  CG2 ILE A 245       3.472  10.322 -25.056  1.00 11.22           C  
ANISOU 2051  CG2 ILE A 245     1871    945   1446    -91   -219    -56       C  
ATOM   2052  CD1 ILE A 245       0.381  10.405 -25.460  1.00 15.18           C  
ANISOU 2052  CD1 ILE A 245     2394   1379   1997    -77   -303   -151       C  
ATOM   2053  N   ALA A 246       5.299  11.203 -28.017  1.00 14.67           N  
ANISOU 2053  N   ALA A 246     2358   1457   1761   -204   -215     42       N  
ATOM   2054  CA  ALA A 246       6.645  10.728 -28.339  1.00 17.33           C  
ANISOU 2054  CA  ALA A 246     2671   1855   2058   -223   -150     48       C  
ATOM   2055  C   ALA A 246       7.647  11.879 -28.503  1.00 17.71           C  
ANISOU 2055  C   ALA A 246     2720   1925   2085   -283   -164     83       C  
ATOM   2056  O   ALA A 246       8.847  11.709 -28.270  1.00 16.89           O  
ANISOU 2056  O   ALA A 246     2572   1880   1967   -291   -117     77       O  
ATOM   2057  CB  ALA A 246       6.613   9.870 -29.598  1.00 16.30           C  
ANISOU 2057  CB  ALA A 246     2563   1754   1877   -248   -106     34       C  
ATOM   2058  N   LYS A 247       7.165  13.052 -28.888  1.00 14.24           N  
ANISOU 2058  N   LYS A 247     2328   1439   1643   -325   -227    117       N  
ATOM   2059  CA  LYS A 247       8.062  14.200 -29.017  1.00 16.34           C  
ANISOU 2059  CA  LYS A 247     2610   1712   1888   -394   -232    148       C  
ATOM   2060  C   LYS A 247       8.562  14.700 -27.655  1.00 16.61           C  
ANISOU 2060  C   LYS A 247     2594   1749   1967   -382   -225    131       C  
ATOM   2061  O   LYS A 247       9.538  15.443 -27.585  1.00 20.03           O  
ANISOU 2061  O   LYS A 247     3021   2212   2379   -443   -205    137       O  
ATOM   2062  CB  LYS A 247       7.381  15.335 -29.775  1.00 21.05           C  
ANISOU 2062  CB  LYS A 247     3286   2240   2474   -437   -300    199       C  
ATOM   2063  CG  LYS A 247       7.293  15.100 -31.276  1.00 25.20           C  
ANISOU 2063  CG  LYS A 247     3864   2790   2922   -486   -303    228       C  
ATOM   2064  CD  LYS A 247       6.673  16.289 -31.988  1.00 28.26           C  
ANISOU 2064  CD  LYS A 247     4337   3108   3293   -522   -381    295       C  
ATOM   2065  CE  LYS A 247       6.680  16.085 -33.495  1.00 32.66           C  
ANISOU 2065  CE  LYS A 247     4951   3705   3755   -587   -386    330       C  
ATOM   2066  NZ  LYS A 247       5.999  17.201 -34.216  1.00 37.54           N  
ANISOU 2066  NZ  LYS A 247     5660   4254   4350   -610   -475    411       N  
ATOM   2067  N   VAL A 248       7.904  14.281 -26.577  1.00 15.91           N  
ANISOU 2067  N   VAL A 248     2471   1639   1934   -315   -236    103       N  
ATOM   2068  CA  VAL A 248       8.314  14.660 -25.227  1.00 16.97           C  
ANISOU 2068  CA  VAL A 248     2554   1790   2103   -309   -229     82       C  
ATOM   2069  C   VAL A 248       9.008  13.496 -24.503  1.00 14.39           C  
ANISOU 2069  C   VAL A 248     2160   1541   1766   -258   -181     60       C  
ATOM   2070  O   VAL A 248      10.112  13.650 -23.960  1.00 17.37           O  
ANISOU 2070  O   VAL A 248     2482   1991   2126   -275   -154     54       O  
ATOM   2071  CB  VAL A 248       7.094  15.138 -24.386  1.00 15.14           C  
ANISOU 2071  CB  VAL A 248     2332   1480   1940   -282   -277     63       C  
ATOM   2072  CG1 VAL A 248       7.519  15.552 -22.981  1.00 11.85           C  
ANISOU 2072  CG1 VAL A 248     1862   1089   1552   -293   -264     35       C  
ATOM   2073  CG2 VAL A 248       6.386  16.292 -25.072  1.00 15.21           C  
ANISOU 2073  CG2 VAL A 248     2404   1403   1971   -312   -331     90       C  
ATOM   2074  N   LEU A 249       8.366  12.330 -24.509  1.00 12.90           N  
ANISOU 2074  N   LEU A 249     1976   1337   1587   -195   -168     48       N  
ATOM   2075  CA ALEU A 249       8.892  11.159 -23.810  0.68 13.61           C  
ANISOU 2075  CA ALEU A 249     2018   1478   1674   -132   -125     37       C  
ATOM   2076  CA BLEU A 249       8.892  11.161 -23.810  0.32 14.09           C  
ANISOU 2076  CA BLEU A 249     2080   1539   1735   -132   -125     37       C  
ATOM   2077  C   LEU A 249       9.960  10.434 -24.630  1.00 15.07           C  
ANISOU 2077  C   LEU A 249     2180   1725   1820   -124    -71     41       C  
ATOM   2078  O   LEU A 249      10.713   9.606 -24.101  1.00 14.57           O  
ANISOU 2078  O   LEU A 249     2066   1715   1756    -68    -35     39       O  
ATOM   2079  CB ALEU A 249       7.759  10.190 -23.459  0.68 13.88           C  
ANISOU 2079  CB ALEU A 249     2080   1459   1735    -76   -121     17       C  
ATOM   2080  CB BLEU A 249       7.755  10.197 -23.462  0.32 14.06           C  
ANISOU 2080  CB BLEU A 249     2102   1481   1757    -76   -121     17       C  
ATOM   2081  CG ALEU A 249       7.015  10.417 -22.136  0.68 13.57           C  
ANISOU 2081  CG ALEU A 249     2034   1389   1734    -63   -149     -3       C  
ATOM   2082  CG BLEU A 249       6.677  10.710 -22.503  0.32 13.65           C  
ANISOU 2082  CG BLEU A 249     2061   1377   1749    -79   -164     -6       C  
ATOM   2083  CD1ALEU A 249       6.167  11.679 -22.163  0.68 13.33           C  
ANISOU 2083  CD1ALEU A 249     2024   1302   1737   -110   -204    -17       C  
ATOM   2084  CD1BLEU A 249       5.680   9.603 -22.187  0.32 15.20           C  
ANISOU 2084  CD1BLEU A 249     2282   1533   1958    -33   -143    -36       C  
ATOM   2085  CD2ALEU A 249       6.167   9.196 -21.783  0.68 15.06           C  
ANISOU 2085  CD2ALEU A 249     2249   1541   1932    -12   -122    -27       C  
ATOM   2086  CD2BLEU A 249       7.298  11.260 -21.229  0.32 13.43           C  
ANISOU 2086  CD2BLEU A 249     1983   1390   1728    -90   -172     -5       C  
ATOM   2087  N   GLY A 250      10.024  10.741 -25.921  1.00 14.72           N  
ANISOU 2087  N   GLY A 250     2171   1677   1745   -180    -65     47       N  
ATOM   2088  CA  GLY A 250      11.015  10.136 -26.793  1.00 14.81           C  
ANISOU 2088  CA  GLY A 250     2159   1750   1719   -191     -8     37       C  
ATOM   2089  C   GLY A 250      10.537   8.852 -27.442  1.00 16.75           C  
ANISOU 2089  C   GLY A 250     2428   1971   1965   -150     37     18       C  
ATOM   2090  O   GLY A 250       9.700   8.137 -26.887  1.00 15.82           O  
ANISOU 2090  O   GLY A 250     2328   1805   1879    -90     38     10       O  
ATOM   2091  N   THR A 251      11.085   8.541 -28.612  1.00 15.87           N  
ANISOU 2091  N   THR A 251     2319   1895   1815   -191     84      2       N  
ATOM   2092  CA  THR A 251      10.680   7.337 -29.325  1.00 15.32           C  
ANISOU 2092  CA  THR A 251     2271   1805   1743   -169    141    -27       C  
ATOM   2093  C   THR A 251      11.388   6.069 -28.849  1.00 15.47           C  
ANISOU 2093  C   THR A 251     2239   1842   1796    -80    213    -51       C  
ATOM   2094  O   THR A 251      10.838   4.982 -28.973  1.00 16.70           O  
ANISOU 2094  O   THR A 251     2422   1953   1971    -37    260    -74       O  
ATOM   2095  CB  THR A 251      10.905   7.494 -30.843  1.00 15.85           C  
ANISOU 2095  CB  THR A 251     2366   1906   1751   -263    168    -42       C  
ATOM   2096  OG1 THR A 251      12.208   8.041 -31.078  1.00 16.72           O  
ANISOU 2096  OG1 THR A 251     2432   2088   1834   -312    188    -45       O  
ATOM   2097  CG2 THR A 251       9.858   8.437 -31.435  1.00 14.62           C  
ANISOU 2097  CG2 THR A 251     2281   1713   1562   -331     95    -10       C  
ATOM   2098  N   GLU A 252      12.602   6.177 -28.311  1.00 15.90           N  
ANISOU 2098  N   GLU A 252     2221   1962   1859    -49    223    -47       N  
ATOM   2099  CA  GLU A 252      13.280   4.943 -27.906  1.00 17.16           C  
ANISOU 2099  CA  GLU A 252     2330   2134   2055     52    286    -62       C  
ATOM   2100  C   GLU A 252      12.568   4.274 -26.726  1.00 16.31           C  
ANISOU 2100  C   GLU A 252     2247   1961   1988    145    271    -36       C  
ATOM   2101  O   GLU A 252      12.471   3.048 -26.673  1.00 19.54           O  
ANISOU 2101  O   GLU A 252     2672   2324   2427    218    331    -47       O  
ATOM   2102  CB  GLU A 252      14.757   5.196 -27.583  1.00 22.60           C  
ANISOU 2102  CB  GLU A 252     2921   2925   2743     72    293    -67       C  
ATOM   2103  CG  GLU A 252      15.598   5.326 -28.857  1.00 31.23           C  
ANISOU 2103  CG  GLU A 252     3983   4081   3802     -6    348   -115       C  
ATOM   2104  CD  GLU A 252      17.076   5.574 -28.606  1.00 44.08           C  
ANISOU 2104  CD  GLU A 252     5501   5824   5424      4    362   -139       C  
ATOM   2105  OE1 GLU A 252      17.448   6.028 -27.503  1.00 46.44           O  
ANISOU 2105  OE1 GLU A 252     5749   6168   5728     42    313   -111       O  
ATOM   2106  OE2 GLU A 252      17.875   5.297 -29.526  1.00 51.37           O  
ANISOU 2106  OE2 GLU A 252     6381   6801   6335    -31    427   -193       O  
ATOM   2107  N   ASP A 253      12.037   5.060 -25.796  1.00 15.62           N  
ANISOU 2107  N   ASP A 253     2172   1862   1901    135    199     -6       N  
ATOM   2108  CA  ASP A 253      11.273   4.461 -24.700  1.00 14.44           C  
ANISOU 2108  CA  ASP A 253     2056   1652   1779    203    188     12       C  
ATOM   2109  C   ASP A 253       9.909   3.955 -25.176  1.00 16.37           C  
ANISOU 2109  C   ASP A 253     2383   1808   2028    181    209    -15       C  
ATOM   2110  O   ASP A 253       9.341   3.037 -24.583  1.00 14.53           O  
ANISOU 2110  O   ASP A 253     2189   1516   1816    235    238    -17       O  
ATOM   2111  CB  ASP A 253      11.106   5.451 -23.549  1.00 16.79           C  
ANISOU 2111  CB  ASP A 253     2335   1971   2075    186    114     37       C  
ATOM   2112  CG  ASP A 253      12.416   5.727 -22.833  1.00 22.79           C  
ANISOU 2112  CG  ASP A 253     3007   2829   2826    217     99     59       C  
ATOM   2113  OD1 ASP A 253      13.280   4.826 -22.813  1.00 22.50           O  
ANISOU 2113  OD1 ASP A 253     2926   2826   2798    296    140     66       O  
ATOM   2114  OD2 ASP A 253      12.585   6.843 -22.306  1.00 26.06           O  
ANISOU 2114  OD2 ASP A 253     3389   3287   3224    164     49     65       O  
ATOM   2115  N   LEU A 254       9.382   4.549 -26.243  1.00 15.93           N  
ANISOU 2115  N   LEU A 254     2356   1749   1948     98    194    -36       N  
ATOM   2116  CA  LEU A 254       8.140   4.053 -26.827  1.00 15.04           C  
ANISOU 2116  CA  LEU A 254     2307   1576   1830     72    215    -70       C  
ATOM   2117  C   LEU A 254       8.379   2.668 -27.408  1.00 16.61           C  
ANISOU 2117  C   LEU A 254     2521   1755   2035    104    316   -104       C  
ATOM   2118  O   LEU A 254       7.571   1.749 -27.219  1.00 14.53           O  
ANISOU 2118  O   LEU A 254     2306   1430   1785    127    361   -132       O  
ATOM   2119  CB  LEU A 254       7.608   5.001 -27.906  1.00 12.41           C  
ANISOU 2119  CB  LEU A 254     1996   1258   1460    -20    169    -76       C  
ATOM   2120  CG  LEU A 254       6.413   4.490 -28.719  1.00 15.71           C  
ANISOU 2120  CG  LEU A 254     2465   1646   1859    -56    188   -118       C  
ATOM   2121  CD1 LEU A 254       5.231   4.163 -27.813  1.00 15.74           C  
ANISOU 2121  CD1 LEU A 254     2496   1593   1892    -24    174   -141       C  
ATOM   2122  CD2 LEU A 254       6.011   5.507 -29.766  1.00 16.27           C  
ANISOU 2122  CD2 LEU A 254     2553   1744   1886   -137    127   -106       C  
ATOM   2123  N   TYR A 255       9.497   2.510 -28.106  1.00 15.95           N  
ANISOU 2123  N   TYR A 255     2396   1721   1944    101    359   -110       N  
ATOM   2124  CA  TYR A 255       9.811   1.215 -28.688  1.00 18.77           C  
ANISOU 2124  CA  TYR A 255     2759   2054   2317    133    465   -151       C  
ATOM   2125  C   TYR A 255      10.122   0.194 -27.598  1.00 21.86           C  
ANISOU 2125  C   TYR A 255     3151   2395   2759    251    505   -131       C  
ATOM   2126  O   TYR A 255       9.727  -0.965 -27.714  1.00 21.68           O  
ANISOU 2126  O   TYR A 255     3176   2301   2759    283    587   -161       O  
ATOM   2127  CB  TYR A 255      10.957   1.333 -29.695  1.00 17.94           C  
ANISOU 2127  CB  TYR A 255     2602   2020   2195     95    506   -174       C  
ATOM   2128  CG  TYR A 255      10.460   1.717 -31.075  1.00 20.31           C  
ANISOU 2128  CG  TYR A 255     2933   2345   2437    -26    512   -209       C  
ATOM   2129  CD1 TYR A 255       9.797   0.792 -31.874  1.00 24.71           C  
ANISOU 2129  CD1 TYR A 255     3534   2868   2984    -59    590   -265       C  
ATOM   2130  CD2 TYR A 255      10.629   3.003 -31.571  1.00 22.48           C  
ANISOU 2130  CD2 TYR A 255     3201   2678   2662   -113    442   -185       C  
ATOM   2131  CE1 TYR A 255       9.326   1.132 -33.127  1.00 26.44           C  
ANISOU 2131  CE1 TYR A 255     3780   3127   3139   -175    589   -294       C  
ATOM   2132  CE2 TYR A 255      10.160   3.352 -32.830  1.00 25.00           C  
ANISOU 2132  CE2 TYR A 255     3558   3023   2918   -223    439   -204       C  
ATOM   2133  CZ  TYR A 255       9.513   2.411 -33.600  1.00 26.62           C  
ANISOU 2133  CZ  TYR A 255     3797   3208   3108   -252    509   -257       C  
ATOM   2134  OH  TYR A 255       9.047   2.741 -34.852  1.00 29.84           O  
ANISOU 2134  OH  TYR A 255     4238   3657   3441   -366    502   -274       O  
ATOM   2135  N   ASP A 256      10.780   0.622 -26.522  1.00 19.93           N  
ANISOU 2135  N   ASP A 256     2859   2186   2529    311    449    -79       N  
ATOM   2136  CA  ASP A 256      11.017  -0.285 -25.401  1.00 20.42           C  
ANISOU 2136  CA  ASP A 256     2928   2203   2628    426    470    -43       C  
ATOM   2137  C   ASP A 256       9.690  -0.755 -24.818  1.00 19.01           C  
ANISOU 2137  C   ASP A 256     2841   1933   2450    422    477    -47       C  
ATOM   2138  O   ASP A 256       9.543  -1.923 -24.455  1.00 19.84           O  
ANISOU 2138  O   ASP A 256     2997   1960   2581    489    544    -44       O  
ATOM   2139  CB  ASP A 256      11.858   0.378 -24.311  1.00 19.93           C  
ANISOU 2139  CB  ASP A 256     2795   2215   2563    474    394     13       C  
ATOM   2140  CG  ASP A 256      13.328   0.448 -24.670  1.00 23.37           C  
ANISOU 2140  CG  ASP A 256     3132   2741   3007    510    409     11       C  
ATOM   2141  OD1 ASP A 256      14.085   1.095 -23.920  1.00 24.76           O  
ANISOU 2141  OD1 ASP A 256     3235   3001   3171    532    348     44       O  
ATOM   2142  OD2 ASP A 256      13.729  -0.136 -25.699  1.00 22.13           O  
ANISOU 2142  OD2 ASP A 256     2964   2577   2866    509    484    -34       O  
ATOM   2143  N   TYR A 257       8.725   0.160 -24.752  1.00 17.78           N  
ANISOU 2143  N   TYR A 257     2705   1782   2267    341    412    -58       N  
ATOM   2144  CA  TYR A 257       7.401  -0.149 -24.222  1.00 18.60           C  
ANISOU 2144  CA  TYR A 257     2883   1816   2369    321    414    -79       C  
ATOM   2145  C   TYR A 257       6.709  -1.203 -25.066  1.00 19.24           C  
ANISOU 2145  C   TYR A 257     3028   1833   2450    297    510   -140       C  
ATOM   2146  O   TYR A 257       6.285  -2.241 -24.550  1.00 20.71           O  
ANISOU 2146  O   TYR A 257     3279   1941   2650    334    575   -150       O  
ATOM   2147  CB  TYR A 257       6.535   1.115 -24.148  1.00 18.63           C  
ANISOU 2147  CB  TYR A 257     2880   1846   2353    241    326    -92       C  
ATOM   2148  CG  TYR A 257       5.089   0.881 -23.741  1.00 20.45           C  
ANISOU 2148  CG  TYR A 257     3171   2018   2581    208    328   -135       C  
ATOM   2149  CD1 TYR A 257       4.776   0.094 -22.640  1.00 20.02           C  
ANISOU 2149  CD1 TYR A 257     3164   1907   2535    249    360   -129       C  
ATOM   2150  CD2 TYR A 257       4.039   1.482 -24.433  1.00 19.40           C  
ANISOU 2150  CD2 TYR A 257     3047   1893   2433    132    294   -183       C  
ATOM   2151  CE1 TYR A 257       3.466  -0.118 -22.254  1.00 18.98           C  
ANISOU 2151  CE1 TYR A 257     3078   1737   2396    202    367   -179       C  
ATOM   2152  CE2 TYR A 257       2.710   1.281 -24.041  1.00 17.86           C  
ANISOU 2152  CE2 TYR A 257     2892   1657   2237    100    297   -237       C  
ATOM   2153  CZ  TYR A 257       2.439   0.482 -22.949  1.00 22.52           C  
ANISOU 2153  CZ  TYR A 257     3504   2216   2835    126    328   -233       C  
ATOM   2154  OH  TYR A 257       1.138   0.267 -22.538  1.00 24.69           O  
ANISOU 2154  OH  TYR A 257     3760   2515   3107     77    311   -271       O  
ATOM   2155  N   ILE A 258       6.596  -0.954 -26.367  1.00 15.65           N  
ANISOU 2155  N   ILE A 258     2561   1412   1974    226    526   -183       N  
ATOM   2156  CA  ILE A 258       5.835  -1.875 -27.201  1.00 15.86           C  
ANISOU 2156  CA  ILE A 258     2643   1394   1990    182    617   -253       C  
ATOM   2157  C   ILE A 258       6.585  -3.190 -27.375  1.00 19.92           C  
ANISOU 2157  C   ILE A 258     3176   1854   2539    247    735   -265       C  
ATOM   2158  O   ILE A 258       5.964  -4.242 -27.512  1.00 23.20           O  
ANISOU 2158  O   ILE A 258     3610   2248   2956    216    778   -283       O  
ATOM   2159  CB  ILE A 258       5.490  -1.267 -28.580  1.00 18.95           C  
ANISOU 2159  CB  ILE A 258     3016   1848   2336     80    600   -294       C  
ATOM   2160  CG1 ILE A 258       6.745  -0.991 -29.404  1.00 20.69           C  
ANISOU 2160  CG1 ILE A 258     3181   2130   2550     74    611   -279       C  
ATOM   2161  CG2 ILE A 258       4.675   0.012 -28.409  1.00 19.39           C  
ANISOU 2161  CG2 ILE A 258     3060   1941   2367     31    482   -279       C  
ATOM   2162  CD1 ILE A 258       6.434  -0.600 -30.836  1.00 25.16           C  
ANISOU 2162  CD1 ILE A 258     3746   2755   3061    -35    611   -320       C  
ATOM   2163  N   ASP A 259       7.915  -3.141 -27.341  1.00 18.32           N  
ANISOU 2163  N   ASP A 259     2912   1685   2362    314    734   -224       N  
ATOM   2164  CA  ASP A 259       8.703  -4.367 -27.406  1.00 17.59           C  
ANISOU 2164  CA  ASP A 259     2827   1537   2319    398    839   -230       C  
ATOM   2165  C   ASP A 259       8.500  -5.226 -26.157  1.00 19.84           C  
ANISOU 2165  C   ASP A 259     3145   1767   2627    464    823   -170       C  
ATOM   2166  O   ASP A 259       8.463  -6.458 -26.245  1.00 20.71           O  
ANISOU 2166  O   ASP A 259     3279   1833   2759    473    884   -174       O  
ATOM   2167  CB  ASP A 259      10.187  -4.053 -27.582  1.00 19.66           C  
ANISOU 2167  CB  ASP A 259     2993   1872   2604    454    822   -202       C  
ATOM   2168  CG  ASP A 259      10.516  -3.530 -28.969  1.00 21.86           C  
ANISOU 2168  CG  ASP A 259     3224   2230   2852    355    837   -257       C  
ATOM   2169  OD1 ASP A 259       9.643  -3.591 -29.859  1.00 20.54           O  
ANISOU 2169  OD1 ASP A 259     3102   2056   2648    255    872   -314       O  
ATOM   2170  OD2 ASP A 259      11.657  -3.064 -29.169  1.00 24.54           O  
ANISOU 2170  OD2 ASP A 259     3481   2648   3197    372    816   -245       O  
ATOM   2171  N   LYS A 260       8.374  -4.580 -25.001  1.00 20.17           N  
ANISOU 2171  N   LYS A 260     3193   1812   2658    502    746   -117       N  
ATOM   2172  CA  LYS A 260       8.174  -5.305 -23.745  1.00 21.40           C  
ANISOU 2172  CA  LYS A 260     3387   1926   2819    552    730    -61       C  
ATOM   2173  C   LYS A 260       6.909  -6.160 -23.774  1.00 23.66           C  
ANISOU 2173  C   LYS A 260     3734   2174   3081    466    767    -96       C  
ATOM   2174  O   LYS A 260       6.910  -7.297 -23.303  1.00 26.81           O  
ANISOU 2174  O   LYS A 260     4177   2521   3491    498    813    -71       O  
ATOM   2175  CB  LYS A 260       8.116  -4.339 -22.554  1.00 19.48           C  
ANISOU 2175  CB  LYS A 260     3140   1705   2556    579    639     -9       C  
ATOM   2176  CG  LYS A 260       7.550  -4.981 -21.290  1.00 21.11           C  
ANISOU 2176  CG  LYS A 260     3403   1874   2746    587    625     30       C  
ATOM   2177  CD  LYS A 260       7.734  -4.111 -20.053  1.00 21.75           C  
ANISOU 2177  CD  LYS A 260     3473   1982   2808    625    541     88       C  
ATOM   2178  CE  LYS A 260       6.961  -4.696 -18.879  1.00 23.62           C  
ANISOU 2178  CE  LYS A 260     3780   2179   3015    603    539    108       C  
ATOM   2179  NZ  LYS A 260       7.095  -3.879 -17.647  1.00 26.24           N  
ANISOU 2179  NZ  LYS A 260     4109   2539   3323    628    460    162       N  
ATOM   2180  N   TYR A 261       5.834  -5.619 -24.341  1.00 21.12           N  
ANISOU 2180  N   TYR A 261     3414   1884   2728    359    747   -153       N  
ATOM   2181  CA  TYR A 261       4.567  -6.338 -24.399  1.00 22.47           C  
ANISOU 2181  CA  TYR A 261     3621   2042   2873    276    777   -190       C  
ATOM   2182  C   TYR A 261       4.363  -6.986 -25.758  1.00 25.85           C  
ANISOU 2182  C   TYR A 261     4045   2475   3304    214    849   -245       C  
ATOM   2183  O   TYR A 261       3.259  -7.435 -26.086  1.00 24.42           O  
ANISOU 2183  O   TYR A 261     3877   2302   3100    131    872   -285       O  
ATOM   2184  CB  TYR A 261       3.410  -5.395 -24.068  1.00 18.80           C  
ANISOU 2184  CB  TYR A 261     3145   1622   2377    204    701   -216       C  
ATOM   2185  CG  TYR A 261       3.520  -4.861 -22.666  1.00 21.57           C  
ANISOU 2185  CG  TYR A 261     3505   1965   2726    248    639   -170       C  
ATOM   2186  CD1 TYR A 261       3.006  -5.578 -21.591  1.00 21.88           C  
ANISOU 2186  CD1 TYR A 261     3593   1971   2750    247    657   -151       C  
ATOM   2187  CD2 TYR A 261       4.165  -3.656 -22.407  1.00 20.93           C  
ANISOU 2187  CD2 TYR A 261     3393   1906   2653    286    571   -145       C  
ATOM   2188  CE1 TYR A 261       3.123  -5.108 -20.302  1.00 22.87           C  
ANISOU 2188  CE1 TYR A 261     3734   2090   2867    280    606   -111       C  
ATOM   2189  CE2 TYR A 261       4.286  -3.176 -21.115  1.00 21.29           C  
ANISOU 2189  CE2 TYR A 261     3447   1947   2695    320    518   -102       C  
ATOM   2190  CZ  TYR A 261       3.762  -3.907 -20.069  1.00 22.82           C  
ANISOU 2190  CZ  TYR A 261     3689   2111   2872    316    535    -87       C  
ATOM   2191  OH  TYR A 261       3.879  -3.435 -18.787  1.00 20.70           O  
ANISOU 2191  OH  TYR A 261     3436   1838   2591    342    486    -48       O  
ATOM   2192  N   ASN A 262       5.446  -7.045 -26.531  1.00 25.73           N  
ANISOU 2192  N   ASN A 262     4002   2459   3315    253    888   -250       N  
ATOM   2193  CA  ASN A 262       5.427  -7.601 -27.879  1.00 27.66           C  
ANISOU 2193  CA  ASN A 262     4236   2712   3562    191    961   -308       C  
ATOM   2194  C   ASN A 262       4.253  -7.047 -28.688  1.00 28.93           C  
ANISOU 2194  C   ASN A 262     4385   2933   3676     74    932   -363       C  
ATOM   2195  O   ASN A 262       3.519  -7.791 -29.338  1.00 30.31           O  
ANISOU 2195  O   ASN A 262     4569   3109   3839      0    982   -403       O  
ATOM   2196  CB  ASN A 262       5.403  -9.135 -27.822  1.00 29.77           C  
ANISOU 2196  CB  ASN A 262     4544   2911   3856    201   1052   -306       C  
ATOM   2197  CG  ASN A 262       6.702  -9.719 -27.260  1.00 32.29           C  
ANISOU 2197  CG  ASN A 262     4865   3175   4228    328   1082   -255       C  
ATOM   2198  OD1 ASN A 262       7.744  -9.063 -27.275  1.00 33.99           O  
ANISOU 2198  OD1 ASN A 262     5032   3418   4466    398   1052   -237       O  
ATOM   2199  ND2 ASN A 262       6.641 -10.951 -26.767  1.00 32.21           N  
ANISOU 2199  ND2 ASN A 262     4910   3090   4238    360   1144   -232       N  
ATOM   2200  N   ILE A 263       4.095  -5.726 -28.607  1.00 28.46           N  
ANISOU 2200  N   ILE A 263     4304   2919   3589     64    850   -362       N  
ATOM   2201  CA  ILE A 263       3.101  -4.956 -29.353  1.00 27.99           C  
ANISOU 2201  CA  ILE A 263     4230   2922   3485    -27    804   -407       C  
ATOM   2202  C   ILE A 263       3.708  -4.436 -30.654  1.00 30.10           C  
ANISOU 2202  C   ILE A 263     4478   3233   3725    -70    826   -444       C  
ATOM   2203  O   ILE A 263       4.880  -4.060 -30.692  1.00 30.55           O  
ANISOU 2203  O   ILE A 263     4526   3286   3797    -21    841   -429       O  
ATOM   2204  CB  ILE A 263       2.593  -3.742 -28.532  1.00 33.31           C  
ANISOU 2204  CB  ILE A 263     4898   3615   4145    -16    700   -387       C  
ATOM   2205  CG1 ILE A 263       1.949  -4.183 -27.220  1.00 35.37           C  
ANISOU 2205  CG1 ILE A 263     5172   3848   4421      9    678   -360       C  
ATOM   2206  CG2 ILE A 263       1.618  -2.887 -29.334  1.00 31.93           C  
ANISOU 2206  CG2 ILE A 263     4707   3501   3925    -96    645   -432       C  
ATOM   2207  CD1 ILE A 263       1.581  -3.016 -26.332  1.00 34.03           C  
ANISOU 2207  CD1 ILE A 263     4987   3693   4249     22    580   -343       C  
ATOM   2208  N   GLU A 264       2.913  -4.403 -31.715  1.00 28.97           N  
ANISOU 2208  N   GLU A 264     4325   3144   3538   -167    830   -494       N  
ATOM   2209  CA  GLU A 264       3.362  -3.828 -32.969  1.00 31.05           C  
ANISOU 2209  CA  GLU A 264     4577   3467   3754   -232    842   -530       C  
ATOM   2210  C   GLU A 264       2.621  -2.520 -33.246  1.00 29.97           C  
ANISOU 2210  C   GLU A 264     4447   3389   3550   -287    747   -540       C  
ATOM   2211  O   GLU A 264       1.405  -2.450 -33.095  1.00 28.48           O  
ANISOU 2211  O   GLU A 264     4252   3219   3349   -313    698   -551       O  
ATOM   2212  CB  GLU A 264       3.155  -4.837 -34.099  1.00 34.10           C  
ANISOU 2212  CB  GLU A 264     4948   3876   4132   -311    920   -578       C  
ATOM   2213  CG  GLU A 264       3.638  -4.385 -35.443  1.00 36.10           C  
ANISOU 2213  CG  GLU A 264     5184   4203   4329   -396    939   -615       C  
ATOM   2214  CD  GLU A 264       3.937  -5.554 -36.359  1.00 36.64           C  
ANISOU 2214  CD  GLU A 264     5233   4267   4420   -448   1035   -659       C  
ATOM   2215  OE1 GLU A 264       4.969  -5.495 -37.055  1.00 35.78           O  
ANISOU 2215  OE1 GLU A 264     5105   4184   4307   -469   1079   -678       O  
ATOM   2216  OE2 GLU A 264       3.153  -6.531 -36.377  1.00 36.65           O  
ANISOU 2216  OE2 GLU A 264     5240   4240   4446   -473   1070   -678       O  
ATOM   2217  N   LEU A 265       3.354  -1.473 -33.617  1.00 30.25           N  
ANISOU 2217  N   LEU A 265     4478   3466   3551   -301    699   -514       N  
ATOM   2218  CA  LEU A 265       2.711  -0.213 -33.967  1.00 30.36           C  
ANISOU 2218  CA  LEU A 265     4476   3543   3515   -350    567   -478       C  
ATOM   2219  C   LEU A 265       1.966  -0.331 -35.290  1.00 31.62           C  
ANISOU 2219  C   LEU A 265     4643   3780   3592   -460    581   -534       C  
ATOM   2220  O   LEU A 265       2.365  -1.094 -36.171  1.00 31.49           O  
ANISOU 2220  O   LEU A 265     4630   3790   3546   -518    684   -588       O  
ATOM   2221  CB  LEU A 265       3.724   0.934 -34.059  1.00 28.40           C  
ANISOU 2221  CB  LEU A 265     4197   3330   3264   -342    486   -396       C  
ATOM   2222  CG  LEU A 265       4.128   1.692 -32.795  1.00 26.85           C  
ANISOU 2222  CG  LEU A 265     3983   3094   3124   -259    409   -327       C  
ATOM   2223  CD1 LEU A 265       5.051   2.842 -33.158  1.00 28.11           C  
ANISOU 2223  CD1 LEU A 265     4117   3300   3261   -285    342   -263       C  
ATOM   2224  CD2 LEU A 265       2.907   2.196 -32.040  1.00 26.25           C  
ANISOU 2224  CD2 LEU A 265     3918   2991   3064   -239    326   -323       C  
ATOM   2225  N   ASP A 266       0.875   0.420 -35.407  1.00 29.45           N  
ANISOU 2225  N   ASP A 266     4363   3546   3281   -487    476   -526       N  
ATOM   2226  CA  ASP A 266       0.209   0.647 -36.681  1.00 29.35           C  
ANISOU 2226  CA  ASP A 266     4345   3630   3175   -586    445   -552       C  
ATOM   2227  C   ASP A 266       1.261   1.110 -37.686  1.00 28.04           C  
ANISOU 2227  C   ASP A 266     4176   3518   2958   -646    441   -506       C  
ATOM   2228  O   ASP A 266       1.991   2.066 -37.423  1.00 24.41           O  
ANISOU 2228  O   ASP A 266     3712   3045   2517   -613    368   -423       O  
ATOM   2229  CB  ASP A 266      -0.907   1.691 -36.507  1.00 30.79           C  
ANISOU 2229  CB  ASP A 266     4514   3843   3343   -573    299   -519       C  
ATOM   2230  CG  ASP A 266      -1.843   1.785 -37.707  1.00 32.07           C  
ANISOU 2230  CG  ASP A 266     4664   4113   3406   -664    261   -553       C  
ATOM   2231  OD1 ASP A 266      -1.435   1.475 -38.842  1.00 30.61           O  
ANISOU 2231  OD1 ASP A 266     4487   3997   3147   -753    312   -569       O  
ATOM   2232  OD2 ASP A 266      -3.008   2.188 -37.505  1.00 33.36           O  
ANISOU 2232  OD2 ASP A 266     4807   4304   3566   -647    175   -567       O  
ATOM   2233  N   PRO A 267       1.363   0.423 -38.838  1.00 25.86           N  
ANISOU 2233  N   PRO A 267     3904   3307   2613   -745    530   -569       N  
ATOM   2234  CA  PRO A 267       2.347   0.838 -39.847  1.00 24.79           C  
ANISOU 2234  CA  PRO A 267     3767   3232   2419   -821    535   -537       C  
ATOM   2235  C   PRO A 267       2.100   2.260 -40.338  1.00 24.25           C  
ANISOU 2235  C   PRO A 267     3709   3220   2283   -855    381   -442       C  
ATOM   2236  O   PRO A 267       2.954   2.851 -40.997  1.00 24.39           O  
ANISOU 2236  O   PRO A 267     3737   3275   2254   -913    364   -395       O  
ATOM   2237  CB  PRO A 267       2.147  -0.180 -40.978  1.00 23.54           C  
ANISOU 2237  CB  PRO A 267     3603   3140   2202   -930    648   -630       C  
ATOM   2238  CG  PRO A 267       0.802  -0.769 -40.744  1.00 23.19           C  
ANISOU 2238  CG  PRO A 267     3534   3088   2189   -910    640   -667       C  
ATOM   2239  CD  PRO A 267       0.622  -0.778 -39.257  1.00 23.62           C  
ANISOU 2239  CD  PRO A 267     3604   3041   2328   -789    626   -656       C  
ATOM   2240  N   ARG A 268       0.933   2.796 -40.005  1.00 24.70           N  
ANISOU 2240  N   ARG A 268     3767   3280   2340   -819    272   -418       N  
ATOM   2241  CA  ARG A 268       0.585   4.181 -40.292  1.00 30.62           C  
ANISOU 2241  CA  ARG A 268     4530   4057   3047   -822    116   -319       C  
ATOM   2242  C   ARG A 268       1.587   5.160 -39.667  1.00 28.95           C  
ANISOU 2242  C   ARG A 268     4332   3778   2890   -768     66   -229       C  
ATOM   2243  O   ARG A 268       1.787   6.269 -40.169  1.00 27.56           O  
ANISOU 2243  O   ARG A 268     4185   3620   2665   -802    -27   -144       O  
ATOM   2244  CB  ARG A 268      -0.826   4.463 -39.780  1.00 34.25           C  
ANISOU 2244  CB  ARG A 268     4971   4512   3530   -763     22   -326       C  
ATOM   2245  CG  ARG A 268      -1.353   5.852 -40.048  1.00 40.81           C  
ANISOU 2245  CG  ARG A 268     5814   5360   4330   -746   -143   -228       C  
ATOM   2246  CD  ARG A 268      -2.666   6.056 -39.317  1.00 46.10           C  
ANISOU 2246  CD  ARG A 268     6449   6012   5053   -667   -222   -253       C  
ATOM   2247  NE  ARG A 268      -3.439   4.817 -39.241  1.00 49.54           N  
ANISOU 2247  NE  ARG A 268     6852   6487   5482   -690   -131   -377       N  
ATOM   2248  CZ  ARG A 268      -4.609   4.624 -39.840  1.00 51.42           C  
ANISOU 2248  CZ  ARG A 268     7059   6823   5656   -727   -170   -429       C  
ATOM   2249  NH1 ARG A 268      -5.156   5.594 -40.561  1.00 53.46           N  
ANISOU 2249  NH1 ARG A 268     7312   7148   5853   -733   -310   -358       N  
ATOM   2250  NH2 ARG A 268      -5.236   3.461 -39.711  1.00 50.70           N  
ANISOU 2250  NH2 ARG A 268     6943   6761   5559   -759    -68   -553       N  
ATOM   2251  N   PHE A 269       2.218   4.740 -38.574  1.00 28.08           N  
ANISOU 2251  N   PHE A 269     4203   3592   2875   -690    130   -249       N  
ATOM   2252  CA  PHE A 269       3.185   5.579 -37.872  1.00 27.44           C  
ANISOU 2252  CA  PHE A 269     4122   3458   2845   -642     93   -180       C  
ATOM   2253  C   PHE A 269       4.542   5.652 -38.565  1.00 30.19           C  
ANISOU 2253  C   PHE A 269     4474   3844   3151   -712    152   -169       C  
ATOM   2254  O   PHE A 269       5.357   6.518 -38.236  1.00 29.33           O  
ANISOU 2254  O   PHE A 269     4369   3715   3060   -703    115   -111       O  
ATOM   2255  CB  PHE A 269       3.381   5.080 -36.441  1.00 24.75           C  
ANISOU 2255  CB  PHE A 269     3754   3040   2610   -536    136   -204       C  
ATOM   2256  CG  PHE A 269       2.235   5.397 -35.526  1.00 21.34           C  
ANISOU 2256  CG  PHE A 269     3318   2563   2229   -468     60   -201       C  
ATOM   2257  CD1 PHE A 269       1.374   4.398 -35.096  1.00 19.36           C  
ANISOU 2257  CD1 PHE A 269     3059   2294   2003   -441    112   -277       C  
ATOM   2258  CD2 PHE A 269       2.019   6.693 -35.092  1.00 21.62           C  
ANISOU 2258  CD2 PHE A 269     3359   2569   2288   -438    -56   -132       C  
ATOM   2259  CE1 PHE A 269       0.318   4.689 -34.258  1.00 21.03           C  
ANISOU 2259  CE1 PHE A 269     3262   2471   2259   -389     49   -288       C  
ATOM   2260  CE2 PHE A 269       0.967   6.990 -34.249  1.00 20.42           C  
ANISOU 2260  CE2 PHE A 269     3194   2376   2190   -378   -120   -143       C  
ATOM   2261  CZ  PHE A 269       0.116   5.990 -33.832  1.00 20.87           C  
ANISOU 2261  CZ  PHE A 269     3236   2427   2267   -356    -69   -223       C  
ATOM   2262  N   ASN A 270       4.786   4.753 -39.517  1.00 31.52           N  
ANISOU 2262  N   ASN A 270     4640   4072   3266   -791    251   -234       N  
ATOM   2263  CA  ASN A 270       6.095   4.666 -40.169  1.00 33.21           C  
ANISOU 2263  CA  ASN A 270     4846   4327   3446   -863    327   -249       C  
ATOM   2264  C   ASN A 270       6.584   5.990 -40.747  1.00 34.65           C  
ANISOU 2264  C   ASN A 270     5065   4541   3559   -938    244   -166       C  
ATOM   2265  O   ASN A 270       7.780   6.278 -40.722  1.00 34.86           O  
ANISOU 2265  O   ASN A 270     5078   4576   3591   -961    282   -161       O  
ATOM   2266  CB  ASN A 270       6.080   3.614 -41.283  1.00 35.49           C  
ANISOU 2266  CB  ASN A 270     5130   4682   3672   -960    439   -337       C  
ATOM   2267  CG  ASN A 270       6.092   2.196 -40.749  1.00 37.68           C  
ANISOU 2267  CG  ASN A 270     5376   4913   4030   -896    565   -430       C  
ATOM   2268  OD1 ASN A 270       5.681   1.261 -41.436  1.00 40.51           O  
ANISOU 2268  OD1 ASN A 270     5735   5304   4352   -959    654   -511       O  
ATOM   2269  ND2 ASN A 270       6.556   2.030 -39.519  1.00 37.93           N  
ANISOU 2269  ND2 ASN A 270     5382   4865   4164   -774    577   -416       N  
ATOM   2270  N   ASP A 271       5.667   6.803 -41.257  1.00 33.13           N  
ANISOU 2270  N   ASP A 271     4919   4367   3300   -974    133   -102       N  
ATOM   2271  CA  ASP A 271       6.073   8.046 -41.899  1.00 38.50           C  
ANISOU 2271  CA  ASP A 271     5655   5068   3904  -1053     57    -15       C  
ATOM   2272  C   ASP A 271       5.647   9.303 -41.141  1.00 37.74           C  
ANISOU 2272  C   ASP A 271     5590   4895   3854   -978    -72     80       C  
ATOM   2273  O   ASP A 271       5.726  10.406 -41.681  1.00 41.53           O  
ANISOU 2273  O   ASP A 271     6134   5374   4271  -1036   -149    165       O  
ATOM   2274  CB  ASP A 271       5.529   8.097 -43.327  1.00 46.52           C  
ANISOU 2274  CB  ASP A 271     6716   6173   4786  -1176     29     -2       C  
ATOM   2275  CG  ASP A 271       6.058   6.967 -44.190  1.00 51.99           C  
ANISOU 2275  CG  ASP A 271     7382   6947   5424  -1277    166   -103       C  
ATOM   2276  OD1 ASP A 271       7.245   6.608 -44.036  1.00 55.28           O  
ANISOU 2276  OD1 ASP A 271     7767   7360   5876  -1292    268   -153       O  
ATOM   2277  OD2 ASP A 271       5.291   6.440 -45.022  1.00 53.70           O  
ANISOU 2277  OD2 ASP A 271     7603   7236   5563  -1344    175   -138       O  
ATOM   2278  N   ILE A 272       5.208   9.153 -39.894  1.00 32.10           N  
ANISOU 2278  N   ILE A 272     4837   4111   3247   -856    -89     66       N  
ATOM   2279  CA  ILE A 272       4.834  10.323 -39.100  1.00 28.27           C  
ANISOU 2279  CA  ILE A 272     4374   3550   2819   -787   -196    141       C  
ATOM   2280  C   ILE A 272       5.496  10.368 -37.723  1.00 27.70           C  
ANISOU 2280  C   ILE A 272     4258   3416   2850   -705   -163    124       C  
ATOM   2281  O   ILE A 272       5.539  11.425 -37.089  1.00 30.11           O  
ANISOU 2281  O   ILE A 272     4581   3663   3197   -673   -229    179       O  
ATOM   2282  CB  ILE A 272       3.306  10.409 -38.905  1.00 24.64           C  
ANISOU 2282  CB  ILE A 272     3911   3070   2382   -720   -287    149       C  
ATOM   2283  CG1 ILE A 272       2.781   9.159 -38.198  1.00 22.39           C  
ANISOU 2283  CG1 ILE A 272     3566   2783   2159   -655   -219     54       C  
ATOM   2284  CG2 ILE A 272       2.613  10.595 -40.245  1.00 26.95           C  
ANISOU 2284  CG2 ILE A 272     4246   3433   2563   -797   -348    183       C  
ATOM   2285  CD1 ILE A 272       1.336   9.263 -37.740  1.00 22.18           C  
ANISOU 2285  CD1 ILE A 272     3522   2733   2173   -584   -298     42       C  
ATOM   2286  N   LEU A 273       6.023   9.238 -37.262  1.00 23.04           N  
ANISOU 2286  N   LEU A 273     3613   2841   2302   -672    -61     50       N  
ATOM   2287  CA  LEU A 273       6.530   9.155 -35.895  1.00 21.97           C  
ANISOU 2287  CA  LEU A 273     3431   2659   2259   -584    -38     37       C  
ATOM   2288  C   LEU A 273       7.913   9.787 -35.738  1.00 24.66           C  
ANISOU 2288  C   LEU A 273     3759   3015   2595   -619    -13     58       C  
ATOM   2289  O   LEU A 273       8.167  10.489 -34.759  1.00 24.36           O  
ANISOU 2289  O   LEU A 273     3708   2939   2609   -577    -49     85       O  
ATOM   2290  CB  LEU A 273       6.572   7.701 -35.429  1.00 23.47           C  
ANISOU 2290  CB  LEU A 273     3573   2850   2494   -526     58    -39       C  
ATOM   2291  CG  LEU A 273       7.057   7.502 -33.993  1.00 22.78           C  
ANISOU 2291  CG  LEU A 273     3441   2722   2493   -430     78    -46       C  
ATOM   2292  CD1 LEU A 273       6.247   8.357 -33.022  1.00 23.84           C  
ANISOU 2292  CD1 LEU A 273     3584   2799   2676   -379    -16     -9       C  
ATOM   2293  CD2 LEU A 273       6.996   6.032 -33.603  1.00 22.79           C  
ANISOU 2293  CD2 LEU A 273     3415   2710   2533   -370    169   -109       C  
ATOM   2294  N   GLY A 274       8.802   9.522 -36.689  1.00 21.42           N  
ANISOU 2294  N   GLY A 274     3349   2670   2121   -705     54     35       N  
ATOM   2295  CA  GLY A 274      10.165  10.035 -36.631  1.00 21.02           C  
ANISOU 2295  CA  GLY A 274     3278   2653   2057   -752     90     35       C  
ATOM   2296  C   GLY A 274      11.003   9.499 -35.480  1.00 20.98           C  
ANISOU 2296  C   GLY A 274     3188   2653   2130   -665    144     -6       C  
ATOM   2297  O   GLY A 274      10.641   8.507 -34.843  1.00 21.21           O  
ANISOU 2297  O   GLY A 274     3181   2660   2220   -572    173    -38       O  
ATOM   2298  N   ARG A 275      12.140  10.150 -35.230  1.00 21.26           N  
ANISOU 2298  N   ARG A 275     3195   2725   2159   -701    159     -5       N  
ATOM   2299  CA  ARG A 275      13.003   9.829 -34.093  1.00 21.23           C  
ANISOU 2299  CA  ARG A 275     3104   2744   2220   -620    194    -34       C  
ATOM   2300  C   ARG A 275      13.101  11.033 -33.159  1.00 21.89           C  
ANISOU 2300  C   ARG A 275     3191   2802   2323   -617    129      9       C  
ATOM   2301  O   ARG A 275      13.445  12.132 -33.597  1.00 22.86           O  
ANISOU 2301  O   ARG A 275     3357   2931   2396   -715    109     35       O  
ATOM   2302  CB  ARG A 275      14.406   9.417 -34.555  1.00 24.35           C  
ANISOU 2302  CB  ARG A 275     3432   3230   2590   -664    284    -96       C  
ATOM   2303  CG  ARG A 275      14.465   8.148 -35.403  1.00 25.87           C  
ANISOU 2303  CG  ARG A 275     3606   3447   2775   -665    369   -157       C  
ATOM   2304  CD  ARG A 275      15.897   7.616 -35.496  1.00 27.55           C  
ANISOU 2304  CD  ARG A 275     3723   3745   3000   -665    460   -230       C  
ATOM   2305  NE  ARG A 275      16.785   8.496 -36.256  1.00 27.95           N  
ANISOU 2305  NE  ARG A 275     3777   3869   2974   -804    479   -249       N  
ATOM   2306  CZ  ARG A 275      18.096   8.301 -36.396  1.00 30.61           C  
ANISOU 2306  CZ  ARG A 275     4025   4296   3309   -830    552   -321       C  
ATOM   2307  NH1 ARG A 275      18.682   7.260 -35.816  1.00 30.96           N  
ANISOU 2307  NH1 ARG A 275     3967   4366   3430   -710    606   -372       N  
ATOM   2308  NH2 ARG A 275      18.826   9.148 -37.112  1.00 29.58           N  
ANISOU 2308  NH2 ARG A 275     3909   4231   3098   -975    573   -343       N  
ATOM   2309  N   HIS A 276      12.809  10.827 -31.877  1.00 17.89           N  
ANISOU 2309  N   HIS A 276     2645   2266   1887   -515    104     14       N  
ATOM   2310  CA  HIS A 276      12.817  11.924 -30.913  1.00 17.57           C  
ANISOU 2310  CA  HIS A 276     2604   2200   1871   -516     50     44       C  
ATOM   2311  C   HIS A 276      13.490  11.547 -29.609  1.00 16.55           C  
ANISOU 2311  C   HIS A 276     2383   2116   1789   -437     68     20       C  
ATOM   2312  O   HIS A 276      13.246  10.478 -29.054  1.00 17.08           O  
ANISOU 2312  O   HIS A 276     2415   2176   1897   -341     85      8       O  
ATOM   2313  CB  HIS A 276      11.387  12.399 -30.628  1.00 18.26           C  
ANISOU 2313  CB  HIS A 276     2756   2191   1991   -488    -28     85       C  
ATOM   2314  CG  HIS A 276      10.657  12.839 -31.854  1.00 17.25           C  
ANISOU 2314  CG  HIS A 276     2715   2025   1814   -553    -65    119       C  
ATOM   2315  ND1 HIS A 276      10.840  14.087 -32.415  1.00 18.38           N  
ANISOU 2315  ND1 HIS A 276     2923   2148   1914   -644    -98    162       N  
ATOM   2316  CD2 HIS A 276       9.766  12.197 -32.639  1.00 18.47           C  
ANISOU 2316  CD2 HIS A 276     2904   2164   1948   -545    -74    119       C  
ATOM   2317  CE1 HIS A 276      10.083  14.192 -33.491  1.00 21.38           C  
ANISOU 2317  CE1 HIS A 276     3375   2502   2248   -681   -135    197       C  
ATOM   2318  NE2 HIS A 276       9.422  13.062 -33.653  1.00 19.15           N  
ANISOU 2318  NE2 HIS A 276     3070   2231   1976   -625   -121    168       N  
ATOM   2319  N   SER A 277      14.349  12.440 -29.133  1.00 16.00           N  
ANISOU 2319  N   SER A 277     2279   2095   1707   -486     67     16       N  
ATOM   2320  CA  SER A 277      14.950  12.301 -27.817  1.00 16.86           C  
ANISOU 2320  CA  SER A 277     2299   2259   1848   -423     69     -1       C  
ATOM   2321  C   SER A 277      13.909  12.523 -26.731  1.00 16.48           C  
ANISOU 2321  C   SER A 277     2273   2138   1851   -369     11     26       C  
ATOM   2322  O   SER A 277      12.902  13.195 -26.957  1.00 16.43           O  
ANISOU 2322  O   SER A 277     2344   2044   1856   -399    -34     52       O  
ATOM   2323  CB  SER A 277      16.081  13.308 -27.649  1.00 22.06           C  
ANISOU 2323  CB  SER A 277     2914   2998   2469   -512     86    -23       C  
ATOM   2324  OG  SER A 277      15.570  14.621 -27.812  1.00 23.60           O  
ANISOU 2324  OG  SER A 277     3193   3121   2652   -600     49      5       O  
ATOM   2325  N   ARG A 278      14.146  11.960 -25.551  1.00 16.40           N  
ANISOU 2325  N   ARG A 278     2193   2167   1871   -288     11     19       N  
ATOM   2326  CA  ARG A 278      13.326  12.292 -24.393  1.00 16.35           C  
ANISOU 2326  CA  ARG A 278     2198   2110   1904   -259    -36     32       C  
ATOM   2327  C   ARG A 278      13.719  13.690 -23.942  1.00 18.77           C  
ANISOU 2327  C   ARG A 278     2494   2439   2199   -346    -53     24       C  
ATOM   2328  O   ARG A 278      14.906  14.024 -23.920  1.00 18.61           O  
ANISOU 2328  O   ARG A 278     2414   2515   2142   -393    -23      2       O  
ATOM   2329  CB  ARG A 278      13.517  11.273 -23.267  1.00 21.64           C  
ANISOU 2329  CB  ARG A 278     2806   2823   2595   -159    -30     32       C  
ATOM   2330  CG  ARG A 278      12.522  11.413 -22.114  1.00 24.02           C  
ANISOU 2330  CG  ARG A 278     3127   3068   2931   -133    -71     39       C  
ATOM   2331  CD  ARG A 278      12.418  10.103 -21.332  1.00 28.32           C  
ANISOU 2331  CD  ARG A 278     3651   3621   3489    -30    -60     51       C  
ATOM   2332  NE  ARG A 278      11.209  10.020 -20.511  1.00 31.68           N  
ANISOU 2332  NE  ARG A 278     4120   3972   3944    -14    -88     50       N  
ATOM   2333  CZ  ARG A 278      10.395   8.966 -20.476  1.00 31.26           C  
ANISOU 2333  CZ  ARG A 278     4114   3855   3909     46    -73     53       C  
ATOM   2334  NH1 ARG A 278      10.650   7.898 -21.221  1.00 28.13           N  
ANISOU 2334  NH1 ARG A 278     3729   3450   3508     98    -28     59       N  
ATOM   2335  NH2 ARG A 278       9.323   8.974 -19.689  1.00 29.69           N  
ANISOU 2335  NH2 ARG A 278     3950   3600   3733     44    -95     39       N  
ATOM   2336  N   LYS A 279      12.730  14.512 -23.607  1.00 16.22           N  
ANISOU 2336  N   LYS A 279     2227   2026   1909   -372    -95     34       N  
ATOM   2337  CA  LYS A 279      12.983  15.892 -23.202  1.00 15.48           C  
ANISOU 2337  CA  LYS A 279     2139   1928   1816   -459   -102     23       C  
ATOM   2338  C   LYS A 279      12.952  16.035 -21.682  1.00 19.13           C  
ANISOU 2338  C   LYS A 279     2540   2424   2303   -443   -113     -1       C  
ATOM   2339  O   LYS A 279      12.314  15.237 -20.993  1.00 20.72           O  
ANISOU 2339  O   LYS A 279     2729   2612   2533   -366   -131      2       O  
ATOM   2340  CB  LYS A 279      11.954  16.832 -23.841  1.00 16.19           C  
ANISOU 2340  CB  LYS A 279     2330   1889   1933   -501   -139     47       C  
ATOM   2341  CG  LYS A 279      11.771  16.645 -25.344  1.00 16.86           C  
ANISOU 2341  CG  LYS A 279     2484   1937   1984   -517   -141     80       C  
ATOM   2342  CD  LYS A 279      13.065  16.883 -26.112  1.00 19.65           C  
ANISOU 2342  CD  LYS A 279     2827   2371   2269   -600    -91     72       C  
ATOM   2343  CE  LYS A 279      12.829  16.891 -27.618  1.00 18.50           C  
ANISOU 2343  CE  LYS A 279     2764   2185   2079   -642    -94    106       C  
ATOM   2344  NZ  LYS A 279      12.293  15.580 -28.105  1.00 12.99           N  
ANISOU 2344  NZ  LYS A 279     2059   1492   1384   -564    -95    107       N  
ATOM   2345  N   ARG A 280      13.647  17.043 -21.159  1.00 19.64           N  
ANISOU 2345  N   ARG A 280     2572   2540   2352   -526    -96    -28       N  
ATOM   2346  CA  ARG A 280      13.589  17.343 -19.727  1.00 21.69           C  
ANISOU 2346  CA  ARG A 280     2777   2837   2628   -535   -103    -58       C  
ATOM   2347  C   ARG A 280      12.413  18.276 -19.480  1.00 21.45           C  
ANISOU 2347  C   ARG A 280     2816   2674   2661   -567   -128    -66       C  
ATOM   2348  O   ARG A 280      12.146  19.163 -20.291  1.00 18.96           O  
ANISOU 2348  O   ARG A 280     2576   2268   2361   -619   -130    -55       O  
ATOM   2349  CB  ARG A 280      14.897  17.966 -19.237  1.00 24.14           C  
ANISOU 2349  CB  ARG A 280     3008   3279   2887   -617    -66    -97       C  
ATOM   2350  CG  ARG A 280      16.128  17.156 -19.628  1.00 24.16           C  
ANISOU 2350  CG  ARG A 280     2932   3418   2832   -587    -41    -98       C  
ATOM   2351  CD  ARG A 280      17.369  17.554 -18.852  1.00 24.85           C  
ANISOU 2351  CD  ARG A 280     2908   3668   2865   -648    -14   -146       C  
ATOM   2352  NE  ARG A 280      18.539  16.864 -19.387  1.00 26.55           N  
ANISOU 2352  NE  ARG A 280     3046   4010   3033   -618     12   -155       N  
ATOM   2353  CZ  ARG A 280      19.084  15.777 -18.851  1.00 27.14           C  
ANISOU 2353  CZ  ARG A 280     3024   4195   3092   -515     -3   -145       C  
ATOM   2354  NH1 ARG A 280      18.580  15.252 -17.742  1.00 24.50           N  
ANISOU 2354  NH1 ARG A 280     2670   3865   2775   -441    -42   -118       N  
ATOM   2355  NH2 ARG A 280      20.141  15.217 -19.424  1.00 28.40           N  
ANISOU 2355  NH2 ARG A 280     3109   4461   3220   -486     24   -163       N  
ATOM   2356  N   TRP A 281      11.702  18.070 -18.375  1.00 18.82           N  
ANISOU 2356  N   TRP A 281     2185   2743   2222   -230    103   -416       N  
ATOM   2357  CA  TRP A 281      10.454  18.795 -18.147  1.00 20.62           C  
ANISOU 2357  CA  TRP A 281     2455   2908   2472   -254     91   -475       C  
ATOM   2358  C   TRP A 281      10.678  20.296 -17.976  1.00 21.83           C  
ANISOU 2358  C   TRP A 281     2602   3053   2638   -333    125   -572       C  
ATOM   2359  O   TRP A 281       9.760  21.087 -18.187  1.00 20.92           O  
ANISOU 2359  O   TRP A 281     2545   2847   2557   -346    136   -618       O  
ATOM   2360  CB  TRP A 281       9.715  18.227 -16.931  1.00 21.21           C  
ANISOU 2360  CB  TRP A 281     2479   3068   2513   -245     57   -465       C  
ATOM   2361  CG  TRP A 281       9.203  16.838 -17.157  1.00 19.93           C  
ANISOU 2361  CG  TRP A 281     2343   2881   2350   -171     33   -378       C  
ATOM   2362  CD1 TRP A 281       9.709  15.680 -16.636  1.00 21.74           C  
ANISOU 2362  CD1 TRP A 281     2519   3202   2539   -130     26   -306       C  
ATOM   2363  CD2 TRP A 281       8.093  16.458 -17.977  1.00 19.74           C  
ANISOU 2363  CD2 TRP A 281     2405   2730   2364   -131     17   -352       C  
ATOM   2364  NE1 TRP A 281       8.976  14.602 -17.077  1.00 21.99           N  
ANISOU 2364  NE1 TRP A 281     2607   3162   2587    -70     14   -243       N  
ATOM   2365  CE2 TRP A 281       7.979  15.053 -17.903  1.00 21.40           C  
ANISOU 2365  CE2 TRP A 281     2616   2957   2558    -75      4   -273       C  
ATOM   2366  CE3 TRP A 281       7.179  17.170 -18.764  1.00 20.66           C  
ANISOU 2366  CE3 TRP A 281     2597   2726   2525   -137     14   -386       C  
ATOM   2367  CZ2 TRP A 281       6.988  14.346 -18.586  1.00 23.15           C  
ANISOU 2367  CZ2 TRP A 281     2912   3078   2805    -39    -13   -237       C  
ATOM   2368  CZ3 TRP A 281       6.198  16.468 -19.443  1.00 23.16           C  
ANISOU 2368  CZ3 TRP A 281     2979   2956   2864    -95    -12   -343       C  
ATOM   2369  CH2 TRP A 281       6.112  15.068 -19.352  1.00 24.02           C  
ANISOU 2369  CH2 TRP A 281     3088   3083   2954    -53    -26   -274       C  
ATOM   2370  N   GLU A 282      11.901  20.685 -17.621  1.00 22.98           N  
ANISOU 2370  N   GLU A 282     2679   3294   2759   -387    147   -601       N  
ATOM   2371  CA  GLU A 282      12.242  22.095 -17.430  1.00 25.34           C  
ANISOU 2371  CA  GLU A 282     2972   3590   3068   -476    188   -699       C  
ATOM   2372  C   GLU A 282      12.017  22.899 -18.711  1.00 24.07           C  
ANISOU 2372  C   GLU A 282     2913   3263   2969   -470    231   -720       C  
ATOM   2373  O   GLU A 282      11.827  24.112 -18.674  1.00 24.52           O  
ANISOU 2373  O   GLU A 282     2999   3267   3049   -527    274   -799       O  
ATOM   2374  CB  GLU A 282      13.698  22.240 -16.967  1.00 29.00           C  
ANISOU 2374  CB  GLU A 282     3338   4189   3492   -538    201   -717       C  
ATOM   2375  CG  GLU A 282      13.957  21.837 -15.507  1.00 32.57           C  
ANISOU 2375  CG  GLU A 282     3679   4825   3870   -569    164   -722       C  
ATOM   2376  CD  GLU A 282      14.004  20.329 -15.283  1.00 34.53           C  
ANISOU 2376  CD  GLU A 282     3887   5148   4087   -481    122   -612       C  
ATOM   2377  OE1 GLU A 282      14.206  19.913 -14.122  1.00 36.18           O  
ANISOU 2377  OE1 GLU A 282     4007   5510   4232   -493     92   -602       O  
ATOM   2378  OE2 GLU A 282      13.834  19.559 -16.255  1.00 34.09           O  
ANISOU 2378  OE2 GLU A 282     3892   4996   4066   -400    123   -536       O  
ATOM   2379  N   ARG A 283      12.043  22.195 -19.837  1.00 25.10           N  
ANISOU 2379  N   ARG A 283     3100   3312   3123   -398    225   -646       N  
ATOM   2380  CA  ARG A 283      11.744  22.745 -21.157  1.00 27.33           C  
ANISOU 2380  CA  ARG A 283     3489   3440   3458   -373    257   -646       C  
ATOM   2381  C   ARG A 283      10.437  23.553 -21.203  1.00 23.44           C  
ANISOU 2381  C   ARG A 283     3059   2852   2996   -372    263   -687       C  
ATOM   2382  O   ARG A 283      10.339  24.561 -21.903  1.00 22.39           O  
ANISOU 2382  O   ARG A 283     2990   2616   2901   -384    311   -722       O  
ATOM   2383  CB  ARG A 283      11.690  21.588 -22.168  1.00 30.83           C  
ANISOU 2383  CB  ARG A 283     3985   3825   3905   -289    233   -554       C  
ATOM   2384  CG  ARG A 283      10.862  21.834 -23.414  1.00 38.76           C  
ANISOU 2384  CG  ARG A 283     5104   4676   4947   -244    238   -538       C  
ATOM   2385  CD  ARG A 283      11.688  22.504 -24.490  1.00 42.90           C  
ANISOU 2385  CD  ARG A 283     5681   5122   5498   -251    294   -546       C  
ATOM   2386  NE  ARG A 283      12.629  21.577 -25.112  1.00 43.80           N  
ANISOU 2386  NE  ARG A 283     5798   5247   5599   -214    300   -481       N  
ATOM   2387  CZ  ARG A 283      12.408  20.937 -26.257  1.00 38.58           C  
ANISOU 2387  CZ  ARG A 283     5224   4493   4942   -151    294   -423       C  
ATOM   2388  NH1 ARG A 283      11.282  21.130 -26.930  1.00 35.67           N  
ANISOU 2388  NH1 ARG A 283     4941   4024   4587   -122    274   -420       N  
ATOM   2389  NH2 ARG A 283      13.327  20.113 -26.735  1.00 36.36           N  
ANISOU 2389  NH2 ARG A 283     4944   4222   4647   -119    312   -367       N  
ATOM   2390  N   PHE A 284       9.439  23.112 -20.449  1.00 21.18           N  
ANISOU 2390  N   PHE A 284     2753   2600   2694   -353    221   -678       N  
ATOM   2391  CA  PHE A 284       8.109  23.713 -20.525  1.00 20.28           C  
ANISOU 2391  CA  PHE A 284     2693   2400   2612   -337    223   -698       C  
ATOM   2392  C   PHE A 284       7.886  24.774 -19.457  1.00 21.92           C  
ANISOU 2392  C   PHE A 284     2870   2643   2817   -404    260   -784       C  
ATOM   2393  O   PHE A 284       6.787  25.319 -19.328  1.00 22.58           O  
ANISOU 2393  O   PHE A 284     2987   2667   2926   -391    271   -802       O  
ATOM   2394  CB  PHE A 284       7.051  22.621 -20.428  1.00 23.57           C  
ANISOU 2394  CB  PHE A 284     3114   2821   3022   -277    161   -636       C  
ATOM   2395  CG  PHE A 284       7.285  21.486 -21.386  1.00 23.00           C  
ANISOU 2395  CG  PHE A 284     3077   2718   2945   -220    130   -557       C  
ATOM   2396  CD1 PHE A 284       6.928  21.607 -22.721  1.00 22.85           C  
ANISOU 2396  CD1 PHE A 284     3146   2580   2955   -181    132   -529       C  
ATOM   2397  CD2 PHE A 284       7.874  20.305 -20.958  1.00 21.30           C  
ANISOU 2397  CD2 PHE A 284     2810   2591   2692   -205    104   -511       C  
ATOM   2398  CE1 PHE A 284       7.153  20.575 -23.614  1.00 22.02           C  
ANISOU 2398  CE1 PHE A 284     3084   2442   2839   -136    109   -464       C  
ATOM   2399  CE2 PHE A 284       8.098  19.263 -21.845  1.00 22.51           C  
ANISOU 2399  CE2 PHE A 284     3005   2704   2841   -154     89   -441       C  
ATOM   2400  CZ  PHE A 284       7.739  19.399 -23.176  1.00 22.79           C  
ANISOU 2400  CZ  PHE A 284     3136   2618   2904   -123     91   -422       C  
ATOM   2401  N   VAL A 285       8.935  25.064 -18.695  1.00 19.24           N  
ANISOU 2401  N   VAL A 285     2463   2403   2443   -477    281   -836       N  
ATOM   2402  CA  VAL A 285       8.866  26.081 -17.650  1.00 21.70           C  
ANISOU 2402  CA  VAL A 285     2748   2754   2742   -556    322   -929       C  
ATOM   2403  C   VAL A 285       9.231  27.445 -18.219  1.00 22.37           C  
ANISOU 2403  C   VAL A 285     2885   2748   2868   -594    399   -972       C  
ATOM   2404  O   VAL A 285      10.198  27.570 -18.963  1.00 25.27           O  
ANISOU 2404  O   VAL A 285     3261   3093   3247   -610    423   -971       O  
ATOM   2405  CB  VAL A 285       9.808  25.746 -16.474  1.00 22.42           C  
ANISOU 2405  CB  VAL A 285     2735   3016   2766   -622    302   -958       C  
ATOM   2406  CG1 VAL A 285       9.777  26.848 -15.422  1.00 21.74           C  
ANISOU 2406  CG1 VAL A 285     2630   2971   2661   -710    347  -1053       C  
ATOM   2407  CG2 VAL A 285       9.437  24.403 -15.869  1.00 23.36           C  
ANISOU 2407  CG2 VAL A 285     2802   3230   2846   -566    231   -886       C  
ATOM   2408  N   HIS A 286       8.446  28.461 -17.881  1.00 20.67           N  
ANISOU 2408  N   HIS A 286     2698   2480   2676   -594    438   -983       N  
ATOM   2409  CA  HIS A 286       8.741  29.827 -18.296  1.00 22.43           C  
ANISOU 2409  CA  HIS A 286     2961   2627   2933   -618    514   -998       C  
ATOM   2410  C   HIS A 286       8.251  30.813 -17.237  1.00 24.82           C  
ANISOU 2410  C   HIS A 286     3256   2945   3230   -663    560  -1045       C  
ATOM   2411  O   HIS A 286       7.677  30.409 -16.222  1.00 23.77           O  
ANISOU 2411  O   HIS A 286     3088   2878   3067   -670    531  -1062       O  
ATOM   2412  CB  HIS A 286       8.115  30.127 -19.663  1.00 22.66           C  
ANISOU 2412  CB  HIS A 286     3076   2521   3014   -535    525   -932       C  
ATOM   2413  CG  HIS A 286       6.662  29.768 -19.763  1.00 22.84           C  
ANISOU 2413  CG  HIS A 286     3131   2496   3052   -459    487   -888       C  
ATOM   2414  ND1 HIS A 286       5.690  30.361 -18.993  1.00 23.11           N  
ANISOU 2414  ND1 HIS A 286     3166   2522   3094   -459    510   -907       N  
ATOM   2415  CD2 HIS A 286       6.021  28.885 -20.571  1.00 23.01           C  
ANISOU 2415  CD2 HIS A 286     3185   2474   3085   -384    432   -828       C  
ATOM   2416  CE1 HIS A 286       4.507  29.854 -19.310  1.00 22.18           C  
ANISOU 2416  CE1 HIS A 286     3073   2360   2993   -387    471   -862       C  
ATOM   2417  NE2 HIS A 286       4.683  28.961 -20.265  1.00 20.18           N  
ANISOU 2417  NE2 HIS A 286     2839   2087   2742   -343    420   -814       N  
ATOM   2418  N   SER A 287       8.472  32.103 -17.465  1.00 24.46           N  
ANISOU 2418  N   SER A 287     3245   2836   3211   -693    637  -1066       N  
ATOM   2419  CA  SER A 287       8.208  33.095 -16.428  1.00 26.16           C  
ANISOU 2419  CA  SER A 287     3456   3067   3418   -751    695  -1120       C  
ATOM   2420  C   SER A 287       6.724  33.211 -16.058  1.00 23.55           C  
ANISOU 2420  C   SER A 287     3157   2687   3104   -695    694  -1100       C  
ATOM   2421  O   SER A 287       6.382  33.795 -15.032  1.00 24.60           O  
ANISOU 2421  O   SER A 287     3282   2843   3222   -739    733  -1145       O  
ATOM   2422  CB  SER A 287       8.752  34.463 -16.857  1.00 33.03           C  
ANISOU 2422  CB  SER A 287     4364   3868   4318   -794    788  -1145       C  
ATOM   2423  OG  SER A 287       8.249  34.845 -18.123  1.00 36.64           O  
ANISOU 2423  OG  SER A 287     4893   4203   4827   -715    808  -1082       O  
ATOM   2424  N   GLU A 288       5.840  32.640 -16.868  1.00 24.85           N  
ANISOU 2424  N   GLU A 288     3357   2786   3297   -602    652  -1034       N  
ATOM   2425  CA  GLU A 288       4.411  32.758 -16.584  1.00 26.08           C  
ANISOU 2425  CA  GLU A 288     3540   2895   3474   -547    655  -1014       C  
ATOM   2426  C   GLU A 288       3.840  31.528 -15.883  1.00 26.07           C  
ANISOU 2426  C   GLU A 288     3494   2968   3443   -528    583  -1012       C  
ATOM   2427  O   GLU A 288       2.688  31.546 -15.453  1.00 29.59           O  
ANISOU 2427  O   GLU A 288     3951   3391   3903   -493    588  -1006       O  
ATOM   2428  CB  GLU A 288       3.624  33.033 -17.866  1.00 25.60           C  
ANISOU 2428  CB  GLU A 288     3544   2720   3464   -457    660   -945       C  
ATOM   2429  CG  GLU A 288       3.822  34.431 -18.432  1.00 29.94           C  
ANISOU 2429  CG  GLU A 288     4144   3187   4045   -464    746   -943       C  
ATOM   2430  CD  GLU A 288       5.253  34.679 -18.869  1.00 31.71           C  
ANISOU 2430  CD  GLU A 288     4360   3428   4260   -520    767   -964       C  
ATOM   2431  OE1 GLU A 288       5.701  34.011 -19.827  1.00 26.92           O  
ANISOU 2431  OE1 GLU A 288     3760   2814   3654   -485    721   -923       O  
ATOM   2432  OE2 GLU A 288       5.930  35.527 -18.245  1.00 35.93           O  
ANISOU 2432  OE2 GLU A 288     4883   3983   4785   -602    833  -1023       O  
ATOM   2433  N   ASN A 289       4.633  30.466 -15.758  1.00 23.17           N  
ANISOU 2433  N   ASN A 289     3077   2691   3037   -550    523  -1016       N  
ATOM   2434  CA  ASN A 289       4.172  29.306 -15.001  1.00 20.52           C  
ANISOU 2434  CA  ASN A 289     2694   2439   2666   -539    460  -1016       C  
ATOM   2435  C   ASN A 289       5.137  28.833 -13.910  1.00 19.71           C  
ANISOU 2435  C   ASN A 289     2513   2484   2493   -613    436  -1061       C  
ATOM   2436  O   ASN A 289       4.821  27.900 -13.183  1.00 20.60           O  
ANISOU 2436  O   ASN A 289     2581   2681   2567   -605    386  -1059       O  
ATOM   2437  CB  ASN A 289       3.852  28.139 -15.952  1.00 16.83           C  
ANISOU 2437  CB  ASN A 289     2240   1942   2214   -469    393   -957       C  
ATOM   2438  CG  ASN A 289       5.080  27.608 -16.690  1.00 15.86           C  
ANISOU 2438  CG  ASN A 289     2106   1843   2076   -482    368   -943       C  
ATOM   2439  OD1 ASN A 289       6.219  27.770 -16.248  1.00 20.59           O  
ANISOU 2439  OD1 ASN A 289     2662   2520   2640   -548    382   -982       O  
ATOM   2440  ND2 ASN A 289       4.842  26.960 -17.829  1.00 18.67           N  
ANISOU 2440  ND2 ASN A 289     2503   2132   2459   -419    334   -888       N  
ATOM   2441  N   GLN A 290       6.299  29.473 -13.778  1.00 21.71           N  
ANISOU 2441  N   GLN A 290     2746   2775   2728   -683    472  -1099       N  
ATOM   2442  CA  GLN A 290       7.333  28.946 -12.878  1.00 22.59           C  
ANISOU 2442  CA  GLN A 290     2774   3042   2768   -749    440  -1132       C  
ATOM   2443  C   GLN A 290       6.911  28.951 -11.406  1.00 22.65           C  
ANISOU 2443  C   GLN A 290     2740   3142   2724   -784    438  -1167       C  
ATOM   2444  O   GLN A 290       7.433  28.174 -10.604  1.00 25.32           O  
ANISOU 2444  O   GLN A 290     3003   3621   2994   -810    390  -1171       O  
ATOM   2445  CB  GLN A 290       8.642  29.721 -13.044  1.00 29.55           C  
ANISOU 2445  CB  GLN A 290     3638   3945   3643   -824    485  -1171       C  
ATOM   2446  CG  GLN A 290       8.591  31.170 -12.610  1.00 37.42           C  
ANISOU 2446  CG  GLN A 290     4667   4897   4655   -882    570  -1224       C  
ATOM   2447  CD  GLN A 290       9.894  31.894 -12.896  1.00 44.65           C  
ANISOU 2447  CD  GLN A 290     5568   5829   5568   -957    617  -1263       C  
ATOM   2448  OE1 GLN A 290      10.301  32.786 -12.152  1.00 48.45           O  
ANISOU 2448  OE1 GLN A 290     6036   6347   6025  -1038    671  -1323       O  
ATOM   2449  NE2 GLN A 290      10.555  31.512 -13.983  1.00 46.09           N  
ANISOU 2449  NE2 GLN A 290     5755   5984   5774   -933    601  -1232       N  
ATOM   2450  N   HIS A 291       5.959  29.808 -11.056  1.00 22.09           N  
ANISOU 2450  N   HIS A 291     2717   2996   2682   -780    491  -1187       N  
ATOM   2451  CA  HIS A 291       5.427  29.849  -9.693  1.00 25.90           C  
ANISOU 2451  CA  HIS A 291     3172   3549   3120   -808    498  -1221       C  
ATOM   2452  C   HIS A 291       4.563  28.624  -9.378  1.00 26.79           C  
ANISOU 2452  C   HIS A 291     3261   3704   3213   -746    433  -1183       C  
ATOM   2453  O   HIS A 291       4.198  28.391  -8.224  1.00 26.03           O  
ANISOU 2453  O   HIS A 291     3133   3689   3070   -763    426  -1203       O  
ATOM   2454  CB  HIS A 291       4.614  31.131  -9.478  1.00 26.54           C  
ANISOU 2454  CB  HIS A 291     3318   3523   3242   -818    583  -1251       C  
ATOM   2455  CG  HIS A 291       3.361  31.196 -10.293  1.00 25.42           C  
ANISOU 2455  CG  HIS A 291     3238   3249   3170   -729    595  -1205       C  
ATOM   2456  ND1 HIS A 291       3.370  31.418 -11.655  1.00 26.93           N  
ANISOU 2456  ND1 HIS A 291     3477   3335   3419   -680    602  -1162       N  
ATOM   2457  CD2 HIS A 291       2.059  31.069  -9.944  1.00 27.99           C  
ANISOU 2457  CD2 HIS A 291     3584   3535   3514   -679    602  -1193       C  
ATOM   2458  CE1 HIS A 291       2.130  31.422 -12.107  1.00 28.73           C  
ANISOU 2458  CE1 HIS A 291     3748   3470   3697   -603    609  -1124       C  
ATOM   2459  NE2 HIS A 291       1.313  31.212 -11.088  1.00 28.38           N  
ANISOU 2459  NE2 HIS A 291     3687   3463   3633   -602    611  -1144       N  
ATOM   2460  N   LEU A 292       4.242  27.844 -10.406  1.00 25.33           N  
ANISOU 2460  N   LEU A 292     3094   3465   3064   -676    390  -1130       N  
ATOM   2461  CA  LEU A 292       3.441  26.634 -10.239  1.00 23.85           C  
ANISOU 2461  CA  LEU A 292     2885   3313   2863   -619    330  -1094       C  
ATOM   2462  C   LEU A 292       4.326  25.391 -10.256  1.00 22.64           C  
ANISOU 2462  C   LEU A 292     2667   3277   2657   -614    257  -1056       C  
ATOM   2463  O   LEU A 292       3.861  24.275  -9.997  1.00 19.83           O  
ANISOU 2463  O   LEU A 292     2279   2968   2289   -554    204   -982       O  
ATOM   2464  CB  LEU A 292       2.387  26.529 -11.341  1.00 21.64           C  
ANISOU 2464  CB  LEU A 292     2665   2896   2660   -540    328  -1049       C  
ATOM   2465  CG  LEU A 292       1.383  27.675 -11.417  1.00 23.42           C  
ANISOU 2465  CG  LEU A 292     2951   3004   2942   -524    400  -1068       C  
ATOM   2466  CD1 LEU A 292       0.412  27.464 -12.563  1.00 24.17           C  
ANISOU 2466  CD1 LEU A 292     3090   2984   3108   -438    385  -1004       C  
ATOM   2467  CD2 LEU A 292       0.640  27.812 -10.095  1.00 27.36           C  
ANISOU 2467  CD2 LEU A 292     3430   3552   3412   -541    426  -1105       C  
ATOM   2468  N   VAL A 293       5.603  25.598 -10.560  1.00 21.57           N  
ANISOU 2468  N   VAL A 293     2509   3182   2503   -660    260  -1071       N  
ATOM   2469  CA  VAL A 293       6.527  24.496 -10.777  1.00 23.98           C  
ANISOU 2469  CA  VAL A 293     2757   3584   2772   -642    201  -1014       C  
ATOM   2470  C   VAL A 293       7.571  24.419  -9.665  1.00 24.39           C  
ANISOU 2470  C   VAL A 293     2721   3811   2736   -713    188  -1050       C  
ATOM   2471  O   VAL A 293       8.046  25.436  -9.164  1.00 28.87           O  
ANISOU 2471  O   VAL A 293     3283   4394   3292   -780    236  -1102       O  
ATOM   2472  CB  VAL A 293       7.235  24.630 -12.146  1.00 26.41           C  
ANISOU 2472  CB  VAL A 293     3099   3807   3127   -629    211   -991       C  
ATOM   2473  CG1 VAL A 293       8.135  23.434 -12.415  1.00 27.11           C  
ANISOU 2473  CG1 VAL A 293     3132   3981   3186   -591    159   -909       C  
ATOM   2474  CG2 VAL A 293       6.210  24.773 -13.252  1.00 23.93           C  
ANISOU 2474  CG2 VAL A 293     2872   3328   2892   -559    222   -953       C  
ATOM   2475  N   SER A 294       7.914  23.195  -9.289  1.00 23.07           N  
ANISOU 2475  N   SER A 294     2486   3761   2520   -671    130   -976       N  
ATOM   2476  CA  SER A 294       8.923  22.923  -8.278  1.00 24.10           C  
ANISOU 2476  CA  SER A 294     2520   4080   2558   -723    105   -989       C  
ATOM   2477  C   SER A 294       9.574  21.595  -8.651  1.00 25.66           C  
ANISOU 2477  C   SER A 294     2665   4343   2742   -648     57   -875       C  
ATOM   2478  O   SER A 294       9.028  20.874  -9.493  1.00 24.85           O  
ANISOU 2478  O   SER A 294     2611   4137   2696   -562     46   -798       O  
ATOM   2479  CB  SER A 294       8.283  22.861  -6.892  1.00 24.82           C  
ANISOU 2479  CB  SER A 294     2587   4247   2596   -727    105   -998       C  
ATOM   2480  OG  SER A 294       7.315  21.825  -6.849  1.00 23.24           O  
ANISOU 2480  OG  SER A 294     2395   4031   2405   -643     71   -929       O  
ATOM   2481  N   PRO A 295      10.736  21.264  -8.049  1.00 25.92           N  
ANISOU 2481  N   PRO A 295     2602   4548   2700   -680     32   -862       N  
ATOM   2482  CA  PRO A 295      11.324  19.941  -8.305  1.00 26.08           C  
ANISOU 2482  CA  PRO A 295     2570   4633   2705   -596     -3   -742       C  
ATOM   2483  C   PRO A 295      10.356  18.829  -7.955  1.00 22.83           C  
ANISOU 2483  C   PRO A 295     2172   4210   2291   -503    -25   -660       C  
ATOM   2484  O   PRO A 295      10.317  17.803  -8.636  1.00 19.64           O  
ANISOU 2484  O   PRO A 295     1787   3756   1920   -417    -35   -564       O  
ATOM   2485  CB  PRO A 295      12.531  19.892  -7.363  1.00 28.48           C  
ANISOU 2485  CB  PRO A 295     2756   5153   2913   -651    -26   -750       C  
ATOM   2486  CG  PRO A 295      12.888  21.308  -7.133  1.00 30.10           C  
ANISOU 2486  CG  PRO A 295     2985   5333   3120   -752     20   -855       C  
ATOM   2487  CD  PRO A 295      11.603  22.092  -7.187  1.00 27.94           C  
ANISOU 2487  CD  PRO A 295     2807   4910   2898   -769     55   -925       C  
ATOM   2488  N   GLU A 296       9.592  19.036  -6.884  1.00 22.49           N  
ANISOU 2488  N   GLU A 296     2123   4212   2209   -526    -27   -701       N  
ATOM   2489  CA  GLU A 296       8.629  18.039  -6.445  1.00 20.61           C  
ANISOU 2489  CA  GLU A 296     1895   3967   1968   -446    -42   -629       C  
ATOM   2490  C   GLU A 296       7.556  17.846  -7.503  1.00 21.93           C  
ANISOU 2490  C   GLU A 296     2158   3943   2233   -389    -31   -600       C  
ATOM   2491  O   GLU A 296       7.177  16.714  -7.807  1.00 21.15           O  
ANISOU 2491  O   GLU A 296     2072   3809   2155   -308    -44   -509       O  
ATOM   2492  CB  GLU A 296       7.990  18.432  -5.111  1.00 21.94           C  
ANISOU 2492  CB  GLU A 296     2046   4212   2079   -487    -38   -686       C  
ATOM   2493  CG  GLU A 296       8.933  18.344  -3.917  1.00 25.14           C  
ANISOU 2493  CG  GLU A 296     2351   4831   2370   -530    -60   -694       C  
ATOM   2494  CD  GLU A 296       9.857  19.537  -3.816  1.00 30.82           C  
ANISOU 2494  CD  GLU A 296     3062   5567   3081   -624    -27   -773       C  
ATOM   2495  OE1 GLU A 296       9.586  20.555  -4.492  1.00 28.89           O  
ANISOU 2495  OE1 GLU A 296     2884   5193   2900   -673      6   -850       O  
ATOM   2496  OE2 GLU A 296      10.857  19.455  -3.065  1.00 34.00           O  
ANISOU 2496  OE2 GLU A 296     3394   6112   3413   -646    -31   -755       O  
ATOM   2497  N   ALA A 297       7.068  18.952  -8.062  1.00 20.49           N  
ANISOU 2497  N   ALA A 297     2040   3639   2107   -432     -4   -677       N  
ATOM   2498  CA  ALA A 297       6.038  18.892  -9.098  1.00 18.49           C  
ANISOU 2498  CA  ALA A 297     1872   3214   1941   -383      3   -653       C  
ATOM   2499  C   ALA A 297       6.524  18.129 -10.323  1.00 18.26           C  
ANISOU 2499  C   ALA A 297     1868   3121   1949   -328    -10   -578       C  
ATOM   2500  O   ALA A 297       5.816  17.273 -10.854  1.00 16.26           O  
ANISOU 2500  O   ALA A 297     1653   2790   1732   -263    -25   -511       O  
ATOM   2501  CB  ALA A 297       5.606  20.286  -9.496  1.00 18.31           C  
ANISOU 2501  CB  ALA A 297     1908   3083   1966   -436     42   -743       C  
ATOM   2502  N   LEU A 298       7.736  18.441 -10.772  1.00 18.60           N  
ANISOU 2502  N   LEU A 298     1891   3196   1981   -359     -2   -591       N  
ATOM   2503  CA  LEU A 298       8.265  17.825 -11.980  1.00 20.52           C  
ANISOU 2503  CA  LEU A 298     2166   3372   2260   -309     -4   -525       C  
ATOM   2504  C   LEU A 298       8.551  16.347 -11.774  1.00 22.49           C  
ANISOU 2504  C   LEU A 298     2378   3688   2478   -237    -24   -421       C  
ATOM   2505  O   LEU A 298       8.336  15.543 -12.681  1.00 20.56           O  
ANISOU 2505  O   LEU A 298     2187   3352   2271   -177    -25   -355       O  
ATOM   2506  CB  LEU A 298       9.529  18.546 -12.452  1.00 21.10           C  
ANISOU 2506  CB  LEU A 298     2220   3468   2330   -361     17   -563       C  
ATOM   2507  CG  LEU A 298       9.304  19.991 -12.902  1.00 21.33           C  
ANISOU 2507  CG  LEU A 298     2303   3399   2401   -425     52   -659       C  
ATOM   2508  CD1 LEU A 298      10.574  20.576 -13.497  1.00 20.42           C  
ANISOU 2508  CD1 LEU A 298     2173   3294   2290   -471     78   -687       C  
ATOM   2509  CD2 LEU A 298       8.163  20.065 -13.902  1.00 22.71           C  
ANISOU 2509  CD2 LEU A 298     2577   3404   2647   -378     56   -644       C  
ATOM   2510  N   ASP A 299       9.025  15.981 -10.586  1.00 20.38           N  
ANISOU 2510  N   ASP A 299     2023   3580   2139   -243    -35   -404       N  
ATOM   2511  CA  ASP A 299       9.309  14.576 -10.322  1.00 20.29           C  
ANISOU 2511  CA  ASP A 299     1977   3636   2097   -166    -43   -297       C  
ATOM   2512  C   ASP A 299       8.024  13.763 -10.216  1.00 20.23           C  
ANISOU 2512  C   ASP A 299     2018   3554   2116   -112    -48   -253       C  
ATOM   2513  O   ASP A 299       7.959  12.630 -10.695  1.00 19.19           O  
ANISOU 2513  O   ASP A 299     1914   3375   2001    -43    -41   -167       O  
ATOM   2514  CB  ASP A 299      10.131  14.402  -9.049  1.00 24.20           C  
ANISOU 2514  CB  ASP A 299     2362   4332   2503   -180    -55   -282       C  
ATOM   2515  CG  ASP A 299      10.398  12.947  -8.740  1.00 24.94           C  
ANISOU 2515  CG  ASP A 299     2419   4493   2564    -89    -53   -161       C  
ATOM   2516  OD1 ASP A 299      11.084  12.284  -9.546  1.00 25.26           O  
ANISOU 2516  OD1 ASP A 299     2468   4503   2625    -37    -36    -89       O  
ATOM   2517  OD2 ASP A 299       9.919  12.460  -7.700  1.00 23.14           O  
ANISOU 2517  OD2 ASP A 299     2158   4344   2291    -67    -61   -134       O  
ATOM   2518  N   PHE A 300       7.011  14.344  -9.581  1.00 17.19           N  
ANISOU 2518  N   PHE A 300     1643   3155   1734   -145    -54   -312       N  
ATOM   2519  CA  PHE A 300       5.707  13.697  -9.486  1.00 15.70           C  
ANISOU 2519  CA  PHE A 300     1496   2893   1578   -103    -57   -278       C  
ATOM   2520  C   PHE A 300       5.117  13.506 -10.884  1.00 15.41           C  
ANISOU 2520  C   PHE A 300     1549   2689   1619    -79    -58   -261       C  
ATOM   2521  O   PHE A 300       4.638  12.421 -11.231  1.00 14.56           O  
ANISOU 2521  O   PHE A 300     1474   2527   1533    -26    -58   -192       O  
ATOM   2522  CB  PHE A 300       4.766  14.520  -8.605  1.00 17.76           C  
ANISOU 2522  CB  PHE A 300     1750   3166   1833   -147    -56   -350       C  
ATOM   2523  CG  PHE A 300       3.374  13.960  -8.514  1.00 20.34           C  
ANISOU 2523  CG  PHE A 300     2113   3417   2200   -110    -58   -319       C  
ATOM   2524  CD1 PHE A 300       3.171  12.617  -8.243  1.00 20.78           C  
ANISOU 2524  CD1 PHE A 300     2157   3494   2243    -49    -58   -231       C  
ATOM   2525  CD2 PHE A 300       2.274  14.782  -8.673  1.00 21.01           C  
ANISOU 2525  CD2 PHE A 300     2238   3411   2334   -135    -53   -375       C  
ATOM   2526  CE1 PHE A 300       1.887  12.102  -8.155  1.00 21.37           C  
ANISOU 2526  CE1 PHE A 300     2261   3500   2358    -24    -57   -206       C  
ATOM   2527  CE2 PHE A 300       0.991  14.273  -8.587  1.00 20.40           C  
ANISOU 2527  CE2 PHE A 300     2182   3273   2296   -104    -56   -344       C  
ATOM   2528  CZ  PHE A 300       0.797  12.934  -8.327  1.00 22.37           C  
ANISOU 2528  CZ  PHE A 300     2420   3545   2535    -53    -59   -263       C  
ATOM   2529  N   LEU A 301       5.162  14.560 -11.688  1.00 13.02           N  
ANISOU 2529  N   LEU A 301     1287   2306   1354   -119    -54   -323       N  
ATOM   2530  CA  LEU A 301       4.640  14.484 -13.049  1.00 16.06           C  
ANISOU 2530  CA  LEU A 301     1757   2543   1804    -98    -58   -309       C  
ATOM   2531  C   LEU A 301       5.390  13.421 -13.838  1.00 16.97           C  
ANISOU 2531  C   LEU A 301     1896   2637   1917    -50    -53   -234       C  
ATOM   2532  O   LEU A 301       4.790  12.625 -14.567  1.00 14.45           O  
ANISOU 2532  O   LEU A 301     1636   2226   1630    -15    -58   -188       O  
ATOM   2533  CB  LEU A 301       4.745  15.836 -13.756  1.00 14.39           C  
ANISOU 2533  CB  LEU A 301     1582   2260   1625   -144    -47   -383       C  
ATOM   2534  CG  LEU A 301       4.310  15.840 -15.227  1.00 16.99           C  
ANISOU 2534  CG  LEU A 301     1999   2445   2012   -121    -53   -367       C  
ATOM   2535  CD1 LEU A 301       2.817  15.563 -15.369  1.00 14.92           C  
ANISOU 2535  CD1 LEU A 301     1772   2110   1787   -100    -75   -352       C  
ATOM   2536  CD2 LEU A 301       4.679  17.163 -15.904  1.00 19.04           C  
ANISOU 2536  CD2 LEU A 301     2291   2647   2297   -160    -31   -431       C  
ATOM   2537  N   ASP A 302       6.707  13.403 -13.666  1.00 15.10           N  
ANISOU 2537  N   ASP A 302     1609   2488   1641    -53    -39   -220       N  
ATOM   2538  CA  ASP A 302       7.570  12.469 -14.374  1.00 17.90           C  
ANISOU 2538  CA  ASP A 302     1981   2829   1993     -3    -21   -145       C  
ATOM   2539  C   ASP A 302       7.215  11.017 -14.050  1.00 19.17           C  
ANISOU 2539  C   ASP A 302     2145   2998   2141     60    -14    -59       C  
ATOM   2540  O   ASP A 302       7.403  10.122 -14.875  1.00 16.86           O  
ANISOU 2540  O   ASP A 302     1908   2634   1866    105      6      2       O  
ATOM   2541  CB  ASP A 302       9.033  12.754 -14.018  1.00 17.99           C  
ANISOU 2541  CB  ASP A 302     1914   2962   1960    -18     -7   -143       C  
ATOM   2542  CG  ASP A 302      10.013  11.964 -14.870  1.00 24.34           C  
ANISOU 2542  CG  ASP A 302     2737   3743   2769     34     22    -68       C  
ATOM   2543  OD1 ASP A 302       9.917  12.005 -16.119  1.00 22.91           O  
ANISOU 2543  OD1 ASP A 302     2642   3432   2632     43     33    -69       O  
ATOM   2544  OD2 ASP A 302      10.880  11.284 -14.282  1.00 26.58           O  
ANISOU 2544  OD2 ASP A 302     2949   4143   3008     71     36     -3       O  
ATOM   2545  N   LYS A 303       6.696  10.791 -12.845  1.00 13.71           N  
ANISOU 2545  N   LYS A 303     1401   2390   1419     61    -23    -54       N  
ATOM   2546  CA  LYS A 303       6.422   9.440 -12.375  1.00 14.84           C  
ANISOU 2546  CA  LYS A 303     1540   2554   1546    121     -6     30       C  
ATOM   2547  C   LYS A 303       5.003   9.007 -12.713  1.00 15.60           C  
ANISOU 2547  C   LYS A 303     1705   2532   1690    125    -15     31       C  
ATOM   2548  O   LYS A 303       4.655   7.839 -12.572  1.00 19.28           O  
ANISOU 2548  O   LYS A 303     2190   2978   2156    169      6     97       O  
ATOM   2549  CB  LYS A 303       6.665   9.340 -10.871  1.00 12.64           C  
ANISOU 2549  CB  LYS A 303     1166   2436   1202    127     -8     45       C  
ATOM   2550  CG  LYS A 303       8.149   9.329 -10.497  1.00 16.54           C  
ANISOU 2550  CG  LYS A 303     1579   3067   1638    141      2     78       C  
ATOM   2551  CD  LYS A 303       8.335   9.550  -9.004  1.00 24.53           C  
ANISOU 2551  CD  LYS A 303     2494   4252   2576    126    -12     69       C  
ATOM   2552  CE  LYS A 303       9.733   9.130  -8.565  1.00 28.78           C  
ANISOU 2552  CE  LYS A 303     2943   4943   3049    161     -1    137       C  
ATOM   2553  NZ  LYS A 303      10.784   9.626  -9.502  1.00 32.56           N  
ANISOU 2553  NZ  LYS A 303     3420   5405   3547    140      4    122       N  
ATOM   2554  N   LEU A 304       4.190   9.957 -13.163  1.00 15.05           N  
ANISOU 2554  N   LEU A 304     1671   2387   1661     78    -41    -41       N  
ATOM   2555  CA  LEU A 304       2.859   9.648 -13.670  1.00 12.48           C  
ANISOU 2555  CA  LEU A 304     1407   1950   1385     75    -56    -42       C  
ATOM   2556  C   LEU A 304       2.920   9.343 -15.162  1.00 14.85           C  
ANISOU 2556  C   LEU A 304     1795   2127   1720     82    -56    -28       C  
ATOM   2557  O   LEU A 304       2.349   8.355 -15.636  1.00 14.64           O  
ANISOU 2557  O   LEU A 304     1822   2027   1712    100    -51     14       O  
ATOM   2558  CB  LEU A 304       1.903  10.812 -13.420  1.00 12.21           C  
ANISOU 2558  CB  LEU A 304     1363   1900   1377     30    -81   -116       C  
ATOM   2559  CG  LEU A 304       1.537  11.118 -11.964  1.00 15.53           C  
ANISOU 2559  CG  LEU A 304     1712   2422   1767     19    -78   -138       C  
ATOM   2560  CD1 LEU A 304       0.687  12.375 -11.886  1.00 15.74           C  
ANISOU 2560  CD1 LEU A 304     1741   2414   1825    -23    -90   -212       C  
ATOM   2561  CD2 LEU A 304       0.804   9.943 -11.336  1.00 15.80           C  
ANISOU 2561  CD2 LEU A 304     1736   2467   1798     52    -69    -78       C  
ATOM   2562  N   LEU A 305       3.615  10.203 -15.901  1.00 13.03           N  
ANISOU 2562  N   LEU A 305     1583   1872   1495     63    -59    -64       N  
ATOM   2563  CA  LEU A 305       3.639  10.109 -17.356  1.00 11.40           C  
ANISOU 2563  CA  LEU A 305     1466   1549   1317     66    -61    -60       C  
ATOM   2564  C   LEU A 305       4.736   9.164 -17.842  1.00 13.79           C  
ANISOU 2564  C   LEU A 305     1796   1845   1600    108    -21      3       C  
ATOM   2565  O   LEU A 305       5.800   9.601 -18.291  1.00 15.62           O  
ANISOU 2565  O   LEU A 305     2026   2086   1822    110     -4     -2       O  
ATOM   2566  CB  LEU A 305       3.818  11.502 -17.972  1.00 13.33           C  
ANISOU 2566  CB  LEU A 305     1724   1759   1581     31    -73   -125       C  
ATOM   2567  CG  LEU A 305       2.633  12.455 -17.787  1.00 15.47           C  
ANISOU 2567  CG  LEU A 305     1991   2006   1883     -2   -102   -181       C  
ATOM   2568  CD1 LEU A 305       2.899  13.784 -18.484  1.00 12.65           C  
ANISOU 2568  CD1 LEU A 305     1659   1602   1545    -27    -99   -236       C  
ATOM   2569  CD2 LEU A 305       1.339  11.820 -18.319  1.00 15.61           C  
ANISOU 2569  CD2 LEU A 305     2059   1942   1930      4   -130   -158       C  
ATOM   2570  N   ARG A 306       4.455   7.869 -17.730  1.00 15.86           N  
ANISOU 2570  N   ARG A 306     2083   2086   1856    141      0     64       N  
ATOM   2571  CA  ARG A 306       5.334   6.801 -18.192  1.00 19.88           C  
ANISOU 2571  CA  ARG A 306     2631   2571   2350    189     50    133       C  
ATOM   2572  C   ARG A 306       4.624   6.019 -19.293  1.00 17.77           C  
ANISOU 2572  C   ARG A 306     2476   2167   2108    185     55    146       C  
ATOM   2573  O   ARG A 306       3.442   5.725 -19.150  1.00 15.92           O  
ANISOU 2573  O   ARG A 306     2259   1897   1892    162     31    134       O  
ATOM   2574  CB  ARG A 306       5.690   5.866 -17.032  1.00 23.06           C  
ANISOU 2574  CB  ARG A 306     2971   3069   2721    237     87    202       C  
ATOM   2575  CG  ARG A 306       6.483   6.527 -15.924  1.00 28.44           C  
ANISOU 2575  CG  ARG A 306     3538   3903   3363    239     80    195       C  
ATOM   2576  CD  ARG A 306       7.932   6.574 -16.331  1.00 32.65           C  
ANISOU 2576  CD  ARG A 306     4054   4474   3877    267    112    227       C  
ATOM   2577  NE  ARG A 306       8.589   7.808 -15.946  1.00 39.47           N  
ANISOU 2577  NE  ARG A 306     4841   5433   4723    227     87    171       N  
ATOM   2578  CZ  ARG A 306       9.861   8.072 -16.212  1.00 40.35           C  
ANISOU 2578  CZ  ARG A 306     4917   5594   4819    237    108    188       C  
ATOM   2579  NH1 ARG A 306      10.599   7.187 -16.870  1.00 40.76           N  
ANISOU 2579  NH1 ARG A 306     5006   5608   4873    295    158    263       N  
ATOM   2580  NH2 ARG A 306      10.391   9.220 -15.830  1.00 43.38           N  
ANISOU 2580  NH2 ARG A 306     5231   6064   5187    187     85    127       N  
ATOM   2581  N   TYR A 307       5.326   5.680 -20.376  1.00 16.77           N  
ANISOU 2581  N   TYR A 307     2425   1967   1980    204     88    169       N  
ATOM   2582  CA  TYR A 307       4.739   4.816 -21.405  1.00 15.23           C  
ANISOU 2582  CA  TYR A 307     2344   1645   1797    197    101    181       C  
ATOM   2583  C   TYR A 307       4.215   3.521 -20.794  1.00 16.61           C  
ANISOU 2583  C   TYR A 307     2529   1813   1970    215    135    231       C  
ATOM   2584  O   TYR A 307       3.064   3.137 -21.014  1.00 17.96           O  
ANISOU 2584  O   TYR A 307     2744   1921   2158    177    111    212       O  
ATOM   2585  CB  TYR A 307       5.750   4.451 -22.489  1.00 16.94           C  
ANISOU 2585  CB  TYR A 307     2641   1792   2003    226    152    211       C  
ATOM   2586  CG  TYR A 307       6.078   5.522 -23.500  1.00 14.84           C  
ANISOU 2586  CG  TYR A 307     2410   1485   1744    203    127    163       C  
ATOM   2587  CD1 TYR A 307       5.104   6.047 -24.344  1.00 14.25           C  
ANISOU 2587  CD1 TYR A 307     2396   1334   1683    155     73    110       C  
ATOM   2588  CD2 TYR A 307       7.384   5.964 -23.647  1.00 15.00           C  
ANISOU 2588  CD2 TYR A 307     2402   1542   1755    232    162    179       C  
ATOM   2589  CE1 TYR A 307       5.420   7.020 -25.282  1.00 13.30           C  
ANISOU 2589  CE1 TYR A 307     2312   1174   1567    142     56     73       C  
ATOM   2590  CE2 TYR A 307       7.712   6.918 -24.580  1.00 14.48           C  
ANISOU 2590  CE2 TYR A 307     2373   1433   1698    213    148    139       C  
ATOM   2591  CZ  TYR A 307       6.734   7.440 -25.396  1.00 15.81           C  
ANISOU 2591  CZ  TYR A 307     2607   1521   1878    171     98     87       C  
ATOM   2592  OH  TYR A 307       7.092   8.391 -26.319  1.00 15.50           O  
ANISOU 2592  OH  TYR A 307     2606   1438   1845    159     92     54       O  
ATOM   2593  N   ASP A 308       5.084   2.844 -20.045  1.00 14.04           N  
ANISOU 2593  N   ASP A 308     2160   1553   1622    274    195    299       N  
ATOM   2594  CA  ASP A 308       4.744   1.574 -19.414  1.00 13.97           C  
ANISOU 2594  CA  ASP A 308     2160   1538   1609    304    245    358       C  
ATOM   2595  C   ASP A 308       3.745   1.779 -18.274  1.00 14.53           C  
ANISOU 2595  C   ASP A 308     2156   1679   1687    280    204    338       C  
ATOM   2596  O   ASP A 308       4.087   2.338 -17.231  1.00 15.39           O  
ANISOU 2596  O   ASP A 308     2162   1909   1776    296    189    339       O  
ATOM   2597  CB  ASP A 308       6.006   0.878 -18.892  1.00 13.39           C  
ANISOU 2597  CB  ASP A 308     2051   1529   1507    387    323    447       C  
ATOM   2598  CG  ASP A 308       5.768  -0.579 -18.543  1.00 22.37           C  
ANISOU 2598  CG  ASP A 308     3231   2623   2643    429    400    521       C  
ATOM   2599  OD1 ASP A 308       4.590  -0.985 -18.425  1.00 22.33           O  
ANISOU 2599  OD1 ASP A 308     3261   2564   2658    388    386    498       O  
ATOM   2600  OD2 ASP A 308       6.761  -1.320 -18.377  1.00 24.23           O  
ANISOU 2600  OD2 ASP A 308     3466   2881   2860    505    480    605       O  
ATOM   2601  N   HIS A 309       2.517   1.311 -18.477  1.00 16.10           N  
ANISOU 2601  N   HIS A 309     2405   1801   1912    238    189    317       N  
ATOM   2602  CA  HIS A 309       1.458   1.474 -17.482  1.00 15.29           C  
ANISOU 2602  CA  HIS A 309     2236   1750   1822    213    155    298       C  
ATOM   2603  C   HIS A 309       1.840   0.814 -16.158  1.00 15.64           C  
ANISOU 2603  C   HIS A 309     2213   1888   1841    271    207    366       C  
ATOM   2604  O   HIS A 309       1.415   1.259 -15.093  1.00 19.17           O  
ANISOU 2604  O   HIS A 309     2577   2424   2282    267    180    353       O  
ATOM   2605  CB  HIS A 309       0.127   0.903 -18.011  1.00 14.02           C  
ANISOU 2605  CB  HIS A 309     2143   1488   1694    157    139    276       C  
ATOM   2606  CG  HIS A 309       0.238  -0.490 -18.548  1.00 15.86           C  
ANISOU 2606  CG  HIS A 309     2476   1624   1928    169    213    323       C  
ATOM   2607  ND1 HIS A 309       0.703  -0.766 -19.818  1.00 16.08           N  
ANISOU 2607  ND1 HIS A 309     2606   1555   1950    160    234    318       N  
ATOM   2608  CD2 HIS A 309      -0.037  -1.693 -17.985  1.00 14.24           C  
ANISOU 2608  CD2 HIS A 309     2289   1395   1726    188    280    376       C  
ATOM   2609  CE1 HIS A 309       0.711  -2.070 -20.013  1.00 14.93           C  
ANISOU 2609  CE1 HIS A 309     2541   1330   1804    172    312    362       C  
ATOM   2610  NE2 HIS A 309       0.259  -2.657 -18.913  1.00 15.02           N  
ANISOU 2610  NE2 HIS A 309     2503   1381   1822    189    343    399       N  
ATOM   2611  N   GLN A 310       2.666  -0.228 -16.223  1.00 15.84           N  
ANISOU 2611  N   GLN A 310     2276   1895   1849    331    287    442       N  
ATOM   2612  CA  GLN A 310       3.124  -0.917 -15.017  1.00 20.10           C  
ANISOU 2612  CA  GLN A 310     2752   2525   2358    401    344    522       C  
ATOM   2613  C   GLN A 310       4.139  -0.094 -14.215  1.00 21.46           C  
ANISOU 2613  C   GLN A 310     2813   2853   2488    436    322    531       C  
ATOM   2614  O   GLN A 310       4.412  -0.400 -13.054  1.00 22.98           O  
ANISOU 2614  O   GLN A 310     2931   3154   2646    485    347    586       O  
ATOM   2615  CB  GLN A 310       3.735  -2.277 -15.378  1.00 21.03           C  
ANISOU 2615  CB  GLN A 310     2948   2573   2472    463    447    608       C  
ATOM   2616  CG  GLN A 310       2.711  -3.338 -15.763  1.00 22.23           C  
ANISOU 2616  CG  GLN A 310     3199   2591   2658    431    490    612       C  
ATOM   2617  CD  GLN A 310       3.356  -4.668 -16.129  1.00 27.32           C  
ANISOU 2617  CD  GLN A 310     3931   3153   3298    493    607    696       C  
ATOM   2618  OE1 GLN A 310       4.532  -4.898 -15.849  1.00 25.22           O  
ANISOU 2618  OE1 GLN A 310     3632   2949   3002    577    662    771       O  
ATOM   2619  NE2 GLN A 310       2.588  -5.545 -16.771  1.00 27.32           N  
ANISOU 2619  NE2 GLN A 310     4041   3012   3326    449    650    684       N  
ATOM   2620  N   SER A 311       4.689   0.948 -14.832  1.00 16.33           N  
ANISOU 2620  N   SER A 311     2153   2216   1837    408    276    478       N  
ATOM   2621  CA  SER A 311       5.737   1.748 -14.202  1.00 18.02           C  
ANISOU 2621  CA  SER A 311     2265   2571   2009    428    257    480       C  
ATOM   2622  C   SER A 311       5.231   3.032 -13.553  1.00 16.16           C  
ANISOU 2622  C   SER A 311     1957   2414   1769    369    183    396       C  
ATOM   2623  O   SER A 311       5.973   3.699 -12.833  1.00 20.10           O  
ANISOU 2623  O   SER A 311     2367   3044   2228    372    166    389       O  
ATOM   2624  CB  SER A 311       6.813   2.098 -15.228  1.00 22.07           C  
ANISOU 2624  CB  SER A 311     2806   3055   2523    435    267    478       C  
ATOM   2625  OG  SER A 311       7.482   0.928 -15.664  1.00 25.70           O  
ANISOU 2625  OG  SER A 311     3321   3464   2981    503    349    567       O  
ATOM   2626  N   ARG A 312       3.975   3.381 -13.812  1.00 15.10           N  
ANISOU 2626  N   ARG A 312     1860   2202   1673    313    143    334       N  
ATOM   2627  CA  ARG A 312       3.388   4.590 -13.249  1.00 14.56           C  
ANISOU 2627  CA  ARG A 312     1736   2190   1608    261     85    257       C  
ATOM   2628  C   ARG A 312       3.121   4.441 -11.755  1.00 14.72           C  
ANISOU 2628  C   ARG A 312     1674   2325   1592    278     91    278       C  
ATOM   2629  O   ARG A 312       2.882   3.334 -11.274  1.00 17.53           O  
ANISOU 2629  O   ARG A 312     2037   2682   1941    321    133    345       O  
ATOM   2630  CB  ARG A 312       2.084   4.936 -13.977  1.00 14.75           C  
ANISOU 2630  CB  ARG A 312     1819   2099   1685    206     46    199       C  
ATOM   2631  CG  ARG A 312       2.265   5.156 -15.477  1.00 12.43           C  
ANISOU 2631  CG  ARG A 312     1610   1695   1419    186     34    174       C  
ATOM   2632  CD  ARG A 312       0.922   5.280 -16.196  1.00 12.13           C  
ANISOU 2632  CD  ARG A 312     1628   1554   1427    138     -5    133       C  
ATOM   2633  NE  ARG A 312       1.094   5.027 -17.622  1.00 13.54           N  
ANISOU 2633  NE  ARG A 312     1902   1624   1619    129     -3    132       N  
ATOM   2634  CZ  ARG A 312       0.150   4.552 -18.428  1.00 14.67           C  
ANISOU 2634  CZ  ARG A 312     2116   1668   1788     97    -20    124       C  
ATOM   2635  NH1 ARG A 312      -1.067   4.278 -17.958  1.00 12.88           N  
ANISOU 2635  NH1 ARG A 312     1870   1437   1585     71    -39    118       N  
ATOM   2636  NH2 ARG A 312       0.432   4.348 -19.707  1.00 15.04           N  
ANISOU 2636  NH2 ARG A 312     2253   1625   1836     88    -16    121       N  
ATOM   2637  N   LEU A 313       3.175   5.552 -11.022  1.00 15.78           N  
ANISOU 2637  N   LEU A 313     1739   2554   1701    245     55    219       N  
ATOM   2638  CA  LEU A 313       2.733   5.567  -9.628  1.00 14.70           C  
ANISOU 2638  CA  LEU A 313     1535   2520   1530    250     55    223       C  
ATOM   2639  C   LEU A 313       1.297   5.070  -9.520  1.00 17.46           C  
ANISOU 2639  C   LEU A 313     1921   2789   1924    241     58    225       C  
ATOM   2640  O   LEU A 313       0.466   5.393 -10.374  1.00 17.01           O  
ANISOU 2640  O   LEU A 313     1916   2622   1923    201     33    181       O  
ATOM   2641  CB  LEU A 313       2.824   6.980  -9.038  1.00 16.36           C  
ANISOU 2641  CB  LEU A 313     1686   2814   1715    197     17    139       C  
ATOM   2642  CG  LEU A 313       4.207   7.583  -8.783  1.00 20.22           C  
ANISOU 2642  CG  LEU A 313     2114   3422   2148    191     10    126       C  
ATOM   2643  CD1 LEU A 313       4.065   9.034  -8.352  1.00 23.33           C  
ANISOU 2643  CD1 LEU A 313     2474   3862   2530    121    -21     25       C  
ATOM   2644  CD2 LEU A 313       4.948   6.784  -7.723  1.00 20.29           C  
ANISOU 2644  CD2 LEU A 313     2052   3572   2085    247     36    206       C  
ATOM   2645  N   THR A 314       0.999   4.284  -8.486  1.00 17.11           N  
ANISOU 2645  N   THR A 314     1845   2801   1855    278     91    280       N  
ATOM   2646  CA  THR A 314      -0.396   3.978  -8.173  1.00 15.44           C  
ANISOU 2646  CA  THR A 314     1649   2532   1683    261     94    274       C  
ATOM   2647  C   THR A 314      -0.971   5.183  -7.450  1.00 16.89           C  
ANISOU 2647  C   THR A 314     1783   2774   1861    218     58    200       C  
ATOM   2648  O   THR A 314      -0.220   6.064  -7.028  1.00 17.64           O  
ANISOU 2648  O   THR A 314     1831   2963   1910    206     40    161       O  
ATOM   2649  CB  THR A 314      -0.554   2.719  -7.294  1.00 18.45           C  
ANISOU 2649  CB  THR A 314     2019   2947   2042    317    152    360       C  
ATOM   2650  OG1 THR A 314       0.055   2.944  -6.017  1.00 21.81           O  
ANISOU 2650  OG1 THR A 314     2365   3528   2394    349    159    380       O  
ATOM   2651  CG2 THR A 314       0.077   1.507  -7.956  1.00 15.66           C  
ANISOU 2651  CG2 THR A 314     1723   2534   1695    366    204    439       C  
ATOM   2652  N   ALA A 315      -2.294   5.231  -7.303  1.00 15.82           N  
ANISOU 2652  N   ALA A 315     1656   2583   1772    194     52    178       N  
ATOM   2653  CA  ALA A 315      -2.913   6.359  -6.622  1.00 15.33           C  
ANISOU 2653  CA  ALA A 315     1552   2563   1708    159     31    112       C  
ATOM   2654  C   ALA A 315      -2.349   6.515  -5.214  1.00 18.37           C  
ANISOU 2654  C   ALA A 315     1871   3094   2013    180     49    120       C  
ATOM   2655  O   ALA A 315      -2.026   7.619  -4.792  1.00 19.98           O  
ANISOU 2655  O   ALA A 315     2042   3365   2183    149     31     57       O  
ATOM   2656  CB  ALA A 315      -4.430   6.203  -6.570  1.00 12.44           C  
ANISOU 2656  CB  ALA A 315     1197   2125   1405    141     32    107       C  
ATOM   2657  N   ARG A 316      -2.231   5.403  -4.495  1.00 20.74           N  
ANISOU 2657  N   ARG A 316     2155   3443   2280    231     89    198       N  
ATOM   2658  CA  ARG A 316      -1.722   5.430  -3.132  1.00 23.29           C  
ANISOU 2658  CA  ARG A 316     2415   3916   2518    258    105    218       C  
ATOM   2659  C   ARG A 316      -0.269   5.883  -3.079  1.00 23.01           C  
ANISOU 2659  C   ARG A 316     2341   3988   2413    259     86    209       C  
ATOM   2660  O   ARG A 316       0.100   6.689  -2.225  1.00 23.57           O  
ANISOU 2660  O   ARG A 316     2360   4175   2419    235     71    164       O  
ATOM   2661  CB  ARG A 316      -1.856   4.058  -2.481  1.00 28.51           C  
ANISOU 2661  CB  ARG A 316     3073   4600   3160    323    158    318       C  
ATOM   2662  CG  ARG A 316      -1.340   4.018  -1.056  1.00 35.19           C  
ANISOU 2662  CG  ARG A 316     3852   5610   3908    359    175    349       C  
ATOM   2663  CD  ARG A 316      -2.176   4.901  -0.146  1.00 39.96           C  
ANISOU 2663  CD  ARG A 316     4430   6255   4498    319    166    281       C  
ATOM   2664  NE  ARG A 316      -3.373   4.209   0.309  1.00 40.38           N  
ANISOU 2664  NE  ARG A 316     4499   6252   4592    340    207    319       N  
ATOM   2665  CZ  ARG A 316      -3.556   3.779   1.554  1.00 41.55           C  
ANISOU 2665  CZ  ARG A 316     4615   6490   4682    379    245    364       C  
ATOM   2666  NH1 ARG A 316      -4.677   3.153   1.882  1.00 41.46           N  
ANISOU 2666  NH1 ARG A 316     4620   6415   4717    394    287    398       N  
ATOM   2667  NH2 ARG A 316      -2.621   3.981   2.470  1.00 41.22           N  
ANISOU 2667  NH2 ARG A 316     4521   6607   4533    401    240    376       N  
ATOM   2668  N   GLU A 317       0.554   5.358  -3.983  1.00 26.04           N  
ANISOU 2668  N   GLU A 317     2750   4336   2807    285     90    252       N  
ATOM   2669  CA  GLU A 317       1.956   5.769  -4.051  1.00 24.96           C  
ANISOU 2669  CA  GLU A 317     2571   4297   2613    285     73    248       C  
ATOM   2670  C   GLU A 317       2.048   7.264  -4.274  1.00 22.04           C  
ANISOU 2670  C   GLU A 317     2193   3934   2248    209     31    138       C  
ATOM   2671  O   GLU A 317       2.880   7.940  -3.675  1.00 23.46           O  
ANISOU 2671  O   GLU A 317     2314   4239   2360    184     15    104       O  
ATOM   2672  CB  GLU A 317       2.701   5.052  -5.174  1.00 23.99           C  
ANISOU 2672  CB  GLU A 317     2490   4106   2519    322     90    305       C  
ATOM   2673  CG  GLU A 317       3.072   3.620  -4.889  1.00 25.62           C  
ANISOU 2673  CG  GLU A 317     2696   4336   2702    407    145    424       C  
ATOM   2674  CD  GLU A 317       3.883   3.019  -6.016  1.00 25.71           C  
ANISOU 2674  CD  GLU A 317     2752   4276   2739    441    170    475       C  
ATOM   2675  OE1 GLU A 317       3.520   3.218  -7.198  1.00 20.77           O  
ANISOU 2675  OE1 GLU A 317     2199   3513   2179    404    157    432       O  
ATOM   2676  OE2 GLU A 317       4.906   2.377  -5.717  1.00 24.03           O  
ANISOU 2676  OE2 GLU A 317     2501   4151   2477    507    203    560       O  
ATOM   2677  N   ALA A 318       1.183   7.768  -5.150  1.00 19.33           N  
ANISOU 2677  N   ALA A 318     1908   3454   1983    170     16     83       N  
ATOM   2678  CA  ALA A 318       1.164   9.182  -5.494  1.00 15.84           C  
ANISOU 2678  CA  ALA A 318     1472   2990   1558    103    -12    -18       C  
ATOM   2679  C   ALA A 318       0.880  10.053  -4.271  1.00 20.76           C  
ANISOU 2679  C   ALA A 318     2048   3708   2132     65    -12    -80       C  
ATOM   2680  O   ALA A 318       1.455  11.136  -4.120  1.00 22.27           O  
ANISOU 2680  O   ALA A 318     2218   3952   2292     13    -24   -153       O  
ATOM   2681  CB  ALA A 318       0.125   9.444  -6.589  1.00 15.75           C  
ANISOU 2681  CB  ALA A 318     1529   2818   1638     82    -23    -48       C  
ATOM   2682  N   MET A 319       0.007   9.575  -3.389  1.00 18.74           N  
ANISOU 2682  N   MET A 319     1781   3472   1868     89      7    -52       N  
ATOM   2683  CA AMET A 319      -0.343  10.343  -2.200  0.39 19.83           C  
ANISOU 2683  CA AMET A 319     1884   3693   1957     56     15   -110       C  
ATOM   2684  CA BMET A 319      -0.358  10.317  -2.188  0.61 19.61           C  
ANISOU 2684  CA BMET A 319     1857   3666   1930     57     15   -108       C  
ATOM   2685  C   MET A 319       0.801  10.374  -1.193  1.00 21.58           C  
ANISOU 2685  C   MET A 319     2039   4092   2067     54     11   -104       C  
ATOM   2686  O   MET A 319       0.798  11.191  -0.277  1.00 23.95           O  
ANISOU 2686  O   MET A 319     2312   4477   2309     10     12   -169       O  
ATOM   2687  CB AMET A 319      -1.607   9.786  -1.542  0.39 19.73           C  
ANISOU 2687  CB AMET A 319     1878   3651   1968     85     41    -76       C  
ATOM   2688  CB BMET A 319      -1.603   9.695  -1.542  0.61 19.45           C  
ANISOU 2688  CB BMET A 319     1842   3615   1932     89     42    -70       C  
ATOM   2689  CG AMET A 319      -2.856   9.971  -2.383  0.39 19.39           C  
ANISOU 2689  CG AMET A 319     1885   3453   2029     73     41    -95       C  
ATOM   2690  CG BMET A 319      -2.806   9.664  -2.483  0.61 19.58           C  
ANISOU 2690  CG BMET A 319     1911   3472   2056     85     41    -74       C  
ATOM   2691  SD AMET A 319      -4.361   9.657  -1.449  0.39 23.08           S  
ANISOU 2691  SD AMET A 319     2345   3903   2523     91     76    -76       S  
ATOM   2692  SD BMET A 319      -4.257   8.799  -1.849  0.61 21.34           S  
ANISOU 2692  SD BMET A 319     2135   3653   2318    119     75    -21       S  
ATOM   2693  CE AMET A 319      -3.975   8.058  -0.745  0.39 19.93           C  
ANISOU 2693  CE AMET A 319     1922   3580   2071    159    103     34       C  
ATOM   2694  CE BMET A 319      -4.614   9.793  -0.400  0.61 23.78           C  
ANISOU 2694  CE BMET A 319     2408   4060   2568     93     98    -84       C  
ATOM   2695  N   GLU A 320       1.789   9.500  -1.376  1.00 23.01           N  
ANISOU 2695  N   GLU A 320     2194   4333   2214    101      8    -25       N  
ATOM   2696  CA  GLU A 320       2.973   9.504  -0.516  1.00 25.22           C  
ANISOU 2696  CA  GLU A 320     2399   4797   2386    103     -3     -9       C  
ATOM   2697  C   GLU A 320       4.049  10.475  -1.024  1.00 24.64           C  
ANISOU 2697  C   GLU A 320     2304   4762   2295     40    -31    -77       C  
ATOM   2698  O   GLU A 320       5.059  10.697  -0.348  1.00 24.00           O  
ANISOU 2698  O   GLU A 320     2154   4843   2124     21    -48    -82       O  
ATOM   2699  CB  GLU A 320       3.574   8.093  -0.403  1.00 24.39           C  
ANISOU 2699  CB  GLU A 320     2267   4750   2250    193     16    120       C  
ATOM   2700  CG  GLU A 320       2.623   6.992   0.070  1.00 26.74           C  
ANISOU 2700  CG  GLU A 320     2587   5006   2566    259     55    199       C  
ATOM   2701  CD  GLU A 320       2.447   6.941   1.580  1.00 26.02           C  
ANISOU 2701  CD  GLU A 320     2445   5059   2384    272     66    211       C  
ATOM   2702  OE1 GLU A 320       3.406   6.575   2.294  1.00 26.33           O  
ANISOU 2702  OE1 GLU A 320     2417   5258   2327    308     63    268       O  
ATOM   2703  OE2 GLU A 320       1.337   7.238   2.063  1.00 28.04           O  
ANISOU 2703  OE2 GLU A 320     2725   5268   2660    250     79    170       O  
ATOM   2704  N   HIS A 321       3.839  11.057  -2.205  1.00 21.71           N  
ANISOU 2704  N   HIS A 321     1991   4250   2009      7    -37   -127       N  
ATOM   2705  CA  HIS A 321       4.897  11.829  -2.876  1.00 22.04           C  
ANISOU 2705  CA  HIS A 321     2020   4306   2047    -42    -55   -177       C  
ATOM   2706  C   HIS A 321       5.167  13.170  -2.204  1.00 21.80           C  
ANISOU 2706  C   HIS A 321     1961   4359   1964   -135    -63   -290       C  
ATOM   2707  O   HIS A 321       4.236  13.844  -1.775  1.00 21.92           O  
ANISOU 2707  O   HIS A 321     2006   4330   1991   -171    -50   -357       O  
ATOM   2708  CB  HIS A 321       4.544  12.065  -4.351  1.00 22.24           C  
ANISOU 2708  CB  HIS A 321     2123   4151   2175    -47    -53   -195       C  
ATOM   2709  CG  HIS A 321       5.691  12.583  -5.165  1.00 22.84           C  
ANISOU 2709  CG  HIS A 321     2192   4232   2255    -78    -63   -220       C  
ATOM   2710  ND1 HIS A 321       6.028  13.916  -5.215  1.00 23.82           N  
ANISOU 2710  ND1 HIS A 321     2312   4365   2373   -161    -67   -323       N  
ATOM   2711  CD2 HIS A 321       6.600  11.936  -5.940  1.00 22.17           C  
ANISOU 2711  CD2 HIS A 321     2102   4142   2179    -37    -62   -153       C  
ATOM   2712  CE1 HIS A 321       7.083  14.076  -6.000  1.00 24.57           C  
ANISOU 2712  CE1 HIS A 321     2398   4462   2476   -173    -71   -320       C  
ATOM   2713  NE2 HIS A 321       7.449  12.890  -6.445  1.00 22.21           N  
ANISOU 2713  NE2 HIS A 321     2097   4157   2185    -96    -68   -216       N  
ATOM   2714  N   PRO A 322       6.452  13.571  -2.120  1.00 22.37           N  
ANISOU 2714  N   PRO A 322     1975   4548   1977   -176    -81   -312       N  
ATOM   2715  CA  PRO A 322       6.814  14.827  -1.449  1.00 24.74           C  
ANISOU 2715  CA  PRO A 322     2246   4936   2217   -278    -85   -426       C  
ATOM   2716  C   PRO A 322       6.090  16.074  -1.968  1.00 23.07           C  
ANISOU 2716  C   PRO A 322     2111   4580   2076   -345    -62   -536       C  
ATOM   2717  O   PRO A 322       6.005  17.063  -1.241  1.00 23.98           O  
ANISOU 2717  O   PRO A 322     2223   4741   2147   -424    -50   -633       O  
ATOM   2718  CB  PRO A 322       8.322  14.928  -1.706  1.00 24.95           C  
ANISOU 2718  CB  PRO A 322     2205   5076   2200   -306   -107   -418       C  
ATOM   2719  CG  PRO A 322       8.766  13.506  -1.774  1.00 24.59           C  
ANISOU 2719  CG  PRO A 322     2119   5086   2139   -202   -114   -279       C  
ATOM   2720  CD  PRO A 322       7.644  12.772  -2.465  1.00 21.76           C  
ANISOU 2720  CD  PRO A 322     1844   4550   1873   -128    -92   -224       C  
ATOM   2721  N   TYR A 323       5.572  16.022  -3.191  1.00 22.41           N  
ANISOU 2721  N   TYR A 323     2095   4323   2095   -313    -53   -519       N  
ATOM   2722  CA  TYR A 323       4.782  17.111  -3.765  1.00 20.41           C  
ANISOU 2722  CA  TYR A 323     1917   3923   1916   -356    -27   -603       C  
ATOM   2723  C   TYR A 323       3.627  17.519  -2.849  1.00 20.29           C  
ANISOU 2723  C   TYR A 323     1921   3894   1893   -370     -3   -648       C  
ATOM   2724  O   TYR A 323       3.222  18.677  -2.826  1.00 23.15           O  
ANISOU 2724  O   TYR A 323     2324   4195   2278   -428     29   -739       O  
ATOM   2725  CB  TYR A 323       4.252  16.688  -5.142  1.00 20.95           C  
ANISOU 2725  CB  TYR A 323     2049   3825   2085   -299    -29   -550       C  
ATOM   2726  CG  TYR A 323       3.414  17.710  -5.894  1.00 20.86           C  
ANISOU 2726  CG  TYR A 323     2112   3659   2156   -325     -5   -615       C  
ATOM   2727  CD1 TYR A 323       3.935  18.948  -6.255  1.00 23.22           C  
ANISOU 2727  CD1 TYR A 323     2431   3928   2463   -395     17   -702       C  
ATOM   2728  CD2 TYR A 323       2.119  17.408  -6.296  1.00 20.34           C  
ANISOU 2728  CD2 TYR A 323     2094   3475   2159   -277     -2   -581       C  
ATOM   2729  CE1 TYR A 323       3.174  19.869  -6.968  1.00 19.82           C  
ANISOU 2729  CE1 TYR A 323     2070   3353   2108   -407     47   -749       C  
ATOM   2730  CE2 TYR A 323       1.355  18.319  -7.001  1.00 18.12           C  
ANISOU 2730  CE2 TYR A 323     1873   3062   1950   -291     19   -627       C  
ATOM   2731  CZ  TYR A 323       1.885  19.544  -7.338  1.00 20.83           C  
ANISOU 2731  CZ  TYR A 323     2239   3376   2300   -350     46   -707       C  
ATOM   2732  OH  TYR A 323       1.121  20.445  -8.047  1.00 22.68           O  
ANISOU 2732  OH  TYR A 323     2534   3476   2605   -353     75   -742       O  
ATOM   2733  N   PHE A 324       3.122  16.568  -2.073  1.00 20.62           N  
ANISOU 2733  N   PHE A 324     1938   3994   1903   -315     -9   -581       N  
ATOM   2734  CA  PHE A 324       1.961  16.822  -1.229  1.00 20.26           C  
ANISOU 2734  CA  PHE A 324     1913   3930   1856   -316     19   -610       C  
ATOM   2735  C   PHE A 324       2.338  17.105   0.227  1.00 19.18           C  
ANISOU 2735  C   PHE A 324     1727   3958   1604   -363     26   -655       C  
ATOM   2736  O   PHE A 324       1.469  17.207   1.085  1.00 20.66           O  
ANISOU 2736  O   PHE A 324     1926   4152   1773   -360     52   -673       O  
ATOM   2737  CB  PHE A 324       0.989  15.638  -1.307  1.00 19.70           C  
ANISOU 2737  CB  PHE A 324     1852   3801   1831   -230     17   -512       C  
ATOM   2738  CG  PHE A 324       0.448  15.398  -2.689  1.00 21.35           C  
ANISOU 2738  CG  PHE A 324     2115   3849   2148   -194     11   -477       C  
ATOM   2739  CD1 PHE A 324      -0.398  16.319  -3.280  1.00 20.75           C  
ANISOU 2739  CD1 PHE A 324     2092   3644   2148   -217     30   -532       C  
ATOM   2740  CD2 PHE A 324       0.805  14.265  -3.404  1.00 21.46           C  
ANISOU 2740  CD2 PHE A 324     2127   3842   2183   -138    -12   -388       C  
ATOM   2741  CE1 PHE A 324      -0.898  16.109  -4.555  1.00 20.98           C  
ANISOU 2741  CE1 PHE A 324     2167   3539   2267   -186     17   -498       C  
ATOM   2742  CE2 PHE A 324       0.317  14.051  -4.683  1.00 23.72           C  
ANISOU 2742  CE2 PHE A 324     2467   3986   2559   -114    -20   -362       C  
ATOM   2743  CZ  PHE A 324      -0.537  14.973  -5.258  1.00 21.30           C  
ANISOU 2743  CZ  PHE A 324     2209   3564   2322   -139    -10   -417       C  
ATOM   2744  N   TYR A 325       3.630  17.249   0.511  1.00 22.94           N  
ANISOU 2744  N   TYR A 325     2147   4572   1998   -409      1   -676       N  
ATOM   2745  CA  TYR A 325       4.052  17.517   1.882  1.00 23.26           C  
ANISOU 2745  CA  TYR A 325     2137   4784   1917   -461      0   -720       C  
ATOM   2746  C   TYR A 325       3.487  18.846   2.398  1.00 23.23           C  
ANISOU 2746  C   TYR A 325     2183   4717   1927   -540     50   -833       C  
ATOM   2747  O   TYR A 325       3.130  18.956   3.572  1.00 19.52           O  
ANISOU 2747  O   TYR A 325     1704   4308   1404   -554     69   -849       O  
ATOM   2748  CB  TYR A 325       5.580  17.522   1.994  1.00 25.51           C  
ANISOU 2748  CB  TYR A 325     2351   5178   2165   -490    -21   -697       C  
ATOM   2749  CG  TYR A 325       6.236  16.151   1.945  1.00 28.29           C  
ANISOU 2749  CG  TYR A 325     2638   5629   2480   -405    -56   -571       C  
ATOM   2750  CD1 TYR A 325       5.477  14.981   1.925  1.00 26.38           C  
ANISOU 2750  CD1 TYR A 325     2404   5381   2237   -310    -66   -481       C  
ATOM   2751  CD2 TYR A 325       7.623  16.031   1.935  1.00 30.51           C  
ANISOU 2751  CD2 TYR A 325     2854   6008   2728   -416    -68   -537       C  
ATOM   2752  CE1 TYR A 325       6.091  13.728   1.886  1.00 27.33           C  
ANISOU 2752  CE1 TYR A 325     2473   5579   2332   -225    -84   -357       C  
ATOM   2753  CE2 TYR A 325       8.240  14.794   1.893  1.00 31.58           C  
ANISOU 2753  CE2 TYR A 325     2935   6227   2835   -330    -87   -415       C  
ATOM   2754  CZ  TYR A 325       7.475  13.647   1.869  1.00 30.66           C  
ANISOU 2754  CZ  TYR A 325     2831   6092   2726   -233    -92   -324       C  
ATOM   2755  OH  TYR A 325       8.113  12.424   1.831  1.00 30.45           O  
ANISOU 2755  OH  TYR A 325     2756   6136   2677   -143    -96   -196       O  
ATOM   2756  N   THR A 326       3.382  19.843   1.519  1.00 23.64           N  
ANISOU 2756  N   THR A 326     2291   4637   2053   -586     77   -905       N  
ATOM   2757  CA  THR A 326       2.922  21.171   1.937  1.00 25.61           C  
ANISOU 2757  CA  THR A 326     2594   4811   2324   -658    136  -1005       C  
ATOM   2758  C   THR A 326       1.400  21.254   2.084  1.00 22.88           C  
ANISOU 2758  C   THR A 326     2309   4373   2011   -621    178  -1025       C  
ATOM   2759  O   THR A 326       0.884  22.176   2.722  1.00 23.72           O  
ANISOU 2759  O   THR A 326     2456   4435   2122   -666    232  -1091       O  
ATOM   2760  CB  THR A 326       3.387  22.276   0.956  1.00 30.71           C  
ANISOU 2760  CB  THR A 326     3283   5344   3043   -715    164  -1066       C  
ATOM   2761  OG1 THR A 326       3.146  23.566   1.533  1.00 35.28           O  
ANISOU 2761  OG1 THR A 326     3906   5869   3630   -789    226  -1153       O  
ATOM   2762  CG2 THR A 326       2.650  22.179  -0.360  1.00 27.95           C  
ANISOU 2762  CG2 THR A 326     2991   4848   2782   -664    167  -1055       C  
ATOM   2763  N   VAL A 327       0.684  20.290   1.513  1.00 21.00           N  
ANISOU 2763  N   VAL A 327     2075   4069   1836   -528    158   -931       N  
ATOM   2764  CA  VAL A 327      -0.779  20.255   1.616  1.00 19.35           C  
ANISOU 2764  CA  VAL A 327     1908   3750   1696   -476    197   -909       C  
ATOM   2765  C   VAL A 327      -1.242  19.946   3.036  1.00 24.60           C  
ANISOU 2765  C   VAL A 327     2552   4515   2280   -469    217   -906       C  
ATOM   2766  O   VAL A 327      -0.808  18.959   3.633  1.00 25.87           O  
ANISOU 2766  O   VAL A 327     2658   4804   2369   -437    180   -842       O  
ATOM   2767  CB  VAL A 327      -1.381  19.211   0.662  1.00 18.76           C  
ANISOU 2767  CB  VAL A 327     1834   3581   1713   -384    166   -798       C  
ATOM   2768  CG1 VAL A 327      -2.874  19.010   0.946  1.00 17.55           C  
ANISOU 2768  CG1 VAL A 327     1703   3347   1618   -331    200   -765       C  
ATOM   2769  CG2 VAL A 327      -1.162  19.628  -0.770  1.00 24.30           C  
ANISOU 2769  CG2 VAL A 327     2571   4161   2499   -387    156   -805       C  
ATOM   2770  N   VAL A 328      -2.108  20.801   3.577  1.00 18.59           N  
ANISOU 2770  N   VAL A 328     1838   3696   1530   -494    282   -973       N  
ATOM   2771  CA  VAL A 328      -2.638  20.624   4.925  1.00 30.99           C  
ANISOU 2771  CA  VAL A 328     3400   5347   3026   -489    314   -978       C  
ATOM   2772  C   VAL A 328      -3.545  19.411   5.012  1.00 30.55           C  
ANISOU 2772  C   VAL A 328     3323   5271   3014   -390    302   -862       C  
ATOM   2773  O   VAL A 328      -4.534  19.321   4.287  1.00 26.45           O  
ANISOU 2773  O   VAL A 328     2829   4614   2607   -340    317   -822       O  
ATOM   2774  CB  VAL A 328      -3.439  21.863   5.400  1.00 33.66           C  
ANISOU 2774  CB  VAL A 328     3804   5606   3379   -533    401  -1074       C  
ATOM   2775  CG1 VAL A 328      -4.144  21.564   6.712  1.00 33.60           C  
ANISOU 2775  CG1 VAL A 328     3794   5664   3308   -512    438  -1065       C  
ATOM   2776  CG2 VAL A 328      -2.530  23.071   5.557  1.00 34.13           C  
ANISOU 2776  CG2 VAL A 328     3890   5671   3409   -638    415  -1172       C  
ATOM   2777  N   LYS A 329      -3.209  18.485   5.906  1.00 39.11           N  
ANISOU 2777  N   LYS A 329     4358   6495   4007   -364    277   -808       N  
ATOM   2778  CA  LYS A 329      -4.022  17.294   6.113  1.00 48.68           C  
ANISOU 2778  CA  LYS A 329     5551   7694   5251   -274    276   -700       C  
ATOM   2779  C   LYS A 329      -5.119  17.593   7.124  1.00 55.40           C  
ANISOU 2779  C   LYS A 329     6427   8531   6092   -267    342   -722       C  
ATOM   2780  O   LYS A 329      -4.958  18.449   7.994  1.00 57.81           O  
ANISOU 2780  O   LYS A 329     6752   8897   6316   -328    379   -811       O  
ATOM   2781  CB  LYS A 329      -3.167  16.122   6.588  1.00 50.45           C  
ANISOU 2781  CB  LYS A 329     5714   8069   5387   -237    229   -618       C  
ATOM   2782  CG  LYS A 329      -2.060  15.722   5.620  1.00 50.03           C  
ANISOU 2782  CG  LYS A 329     5632   8034   5344   -234    171   -582       C  
ATOM   2783  CD  LYS A 329      -2.566  15.685   4.184  1.00 46.98           C  
ANISOU 2783  CD  LYS A 329     5282   7473   5096   -208    164   -558       C  
ATOM   2784  CE  LYS A 329      -1.514  15.118   3.240  1.00 44.77           C  
ANISOU 2784  CE  LYS A 329     4978   7206   4825   -193    113   -509       C  
ATOM   2785  NZ  LYS A 329      -0.258  15.916   3.216  1.00 43.30           N  
ANISOU 2785  NZ  LYS A 329     4772   7107   4573   -266     91   -583       N  
ATOM   2786  N   ASP A 330      -6.239  16.892   7.004  1.00 59.75           N  
ANISOU 2786  N   ASP A 330     6979   9000   6723   -195    361   -644       N  
ATOM   2787  CA  ASP A 330      -7.386  17.134   7.871  1.00 65.35           C  
ANISOU 2787  CA  ASP A 330     7709   9681   7440   -179    430   -655       C  
ATOM   2788  C   ASP A 330      -7.276  16.358   9.177  1.00 65.80           C  
ANISOU 2788  C   ASP A 330     7736   9876   7386   -152    439   -612       C  
ATOM   2789  O   ASP A 330      -6.436  15.471   9.318  1.00 65.73           O  
ANISOU 2789  O   ASP A 330     7686   9977   7312   -131    391   -554       O  
ATOM   2790  CB  ASP A 330      -8.682  16.771   7.143  1.00 69.16           C  
ANISOU 2790  CB  ASP A 330     8199  10016   8063   -119    448   -589       C  
ATOM   2791  CG  ASP A 330      -9.125  17.858   6.183  1.00 72.19           C  
ANISOU 2791  CG  ASP A 330     8621  10263   8545   -143    467   -644       C  
ATOM   2792  OD1 ASP A 330      -8.378  18.851   6.036  1.00 73.09           O  
ANISOU 2792  OD1 ASP A 330     8762  10385   8623   -206    471   -732       O  
ATOM   2793  OD2 ASP A 330     -10.197  17.713   5.559  1.00 73.25           O  
ANISOU 2793  OD2 ASP A 330     8755  10284   8792   -100    480   -596       O  
TER    2794      ASP A 330                                                      
HETATM 2795  S   SO4 A 401     -17.090   0.453 -23.369  1.00 51.95           S  
HETATM 2796  O1  SO4 A 401     -15.741   0.965 -23.577  1.00 52.51           O  
HETATM 2797  O2  SO4 A 401     -17.545  -0.217 -24.582  1.00 54.44           O  
HETATM 2798  O3  SO4 A 401     -17.078  -0.494 -22.260  1.00 52.55           O  
HETATM 2799  O4  SO4 A 401     -17.981   1.566 -23.057  1.00 51.42           O  
HETATM 2800  S   SO4 A 402       8.765   4.696 -19.614  1.00 30.95           S  
HETATM 2801  O1  SO4 A 402      10.030   4.673 -20.353  1.00 32.78           O  
HETATM 2802  O2  SO4 A 402       7.887   3.623 -20.089  1.00 23.58           O  
HETATM 2803  O3  SO4 A 402       9.059   4.458 -18.203  1.00 35.68           O  
HETATM 2804  O4  SO4 A 402       8.133   6.010 -19.801  1.00 22.33           O  
HETATM 2805  CAI V55 A 403     -22.769  15.639 -13.412  1.00 18.18           C  
HETATM 2806  CAG V55 A 403     -22.550  15.151 -14.699  1.00 15.23           C  
HETATM 2807  CAK V55 A 403     -22.393  13.784 -14.890  1.00 14.42           C  
HETATM 2808  CAJ V55 A 403     -22.456  12.923 -13.797  1.00 15.31           C  
HETATM 2809  CAF V55 A 403     -22.669  13.411 -12.516  1.00 16.01           C  
HETATM 2810  OAB V55 A 403     -22.680  17.905 -14.076  1.00 24.24           O  
HETATM 2811  CAE V55 A 403     -22.829  14.774 -12.326  1.00 17.07           C  
HETATM 2812  CAD V55 A 403     -22.943  17.126 -13.179  1.00 21.94           C  
HETATM 2813  CAA V55 A 403     -22.032  14.148 -17.237  1.00 18.56           C  
HETATM 2814  OAH V55 A 403     -22.172  13.232 -16.169  1.00 17.53           O  
HETATM 2815  OAC V55 A 403     -22.293  11.543 -13.996  1.00 16.37           O  
HETATM 2816  O   HOH A 501     -20.614  16.694 -18.782  1.00 42.19           O  
HETATM 2817  O   HOH A 502       9.405  -7.953 -28.445  1.00 42.09           O  
HETATM 2818  O   HOH A 503      -3.774 -10.913  -5.614  1.00 39.97           O  
HETATM 2819  O   HOH A 504      16.544   8.109 -26.828  1.00 37.75           O  
HETATM 2820  O   HOH A 505     -14.369  11.933 -22.781  1.00 30.29           O  
HETATM 2821  O   HOH A 506     -18.608  14.194 -18.886  1.00 25.47           O  
HETATM 2822  O   HOH A 507     -35.994   8.144 -25.776  1.00 46.58           O  
HETATM 2823  O   HOH A 508      -9.502  11.071 -31.327  1.00 34.40           O  
HETATM 2824  O   HOH A 509     -32.826  14.518 -22.148  1.00 37.44           O  
HETATM 2825  O   HOH A 510      -5.470  24.072   3.154  1.00 28.35           O  
HETATM 2826  O   HOH A 511      -1.570  31.061 -10.225  1.00 34.87           O  
HETATM 2827  O   HOH A 512      15.383  20.269 -25.408  1.00 35.49           O  
HETATM 2828  O   HOH A 513      -3.159  26.064 -14.011  1.00 37.33           O  
HETATM 2829  O   HOH A 514       7.301  -4.331 -31.037  1.00 32.23           O  
HETATM 2830  O   HOH A 515      -7.314  30.341  -5.995  1.00 45.68           O  
HETATM 2831  O   HOH A 516     -44.940  19.842 -11.542  1.00 30.47           O  
HETATM 2832  O   HOH A 517     -17.002  12.404 -20.785  1.00 41.35           O  
HETATM 2833  O   HOH A 518       4.910   2.454  -9.183  1.00 37.68           O  
HETATM 2834  O   HOH A 519     -11.216  20.254 -13.224  1.00 26.73           O  
HETATM 2835  O   HOH A 520     -17.351  -2.690 -24.674  1.00 46.09           O  
HETATM 2836  O   HOH A 521      17.042  16.460 -27.020  1.00 34.08           O  
HETATM 2837  O   HOH A 522     -42.970  14.526  -4.717  1.00 38.93           O  
HETATM 2838  O   HOH A 523      -0.674  11.143   2.097  1.00 45.95           O  
HETATM 2839  O   HOH A 524     -16.249 -12.846  -7.284  1.00 49.92           O  
HETATM 2840  O   HOH A 525     -13.790  17.703  -1.933  1.00 38.44           O  
HETATM 2841  O   HOH A 526       7.783  34.103 -21.245  1.00 38.13           O  
HETATM 2842  O   HOH A 527     -21.792   9.213 -13.172  1.00 17.22           O  
HETATM 2843  O   HOH A 528     -41.731   7.804 -15.076  1.00 27.60           O  
HETATM 2844  O   HOH A 529       9.117  -0.462 -18.700  1.00 32.59           O  
HETATM 2845  O   HOH A 530      -6.285  17.655  -0.398  1.00 27.31           O  
HETATM 2846  O   HOH A 531     -30.420   0.342  -8.387  1.00 34.05           O  
HETATM 2847  O   HOH A 532     -33.758   4.594  -6.154  1.00 43.90           O  
HETATM 2848  O   HOH A 533     -22.375  -8.535 -15.725  1.00 37.17           O  
HETATM 2849  O   HOH A 534     -18.828   2.852  -1.263  1.00 28.93           O  
HETATM 2850  O   HOH A 535      -3.150  28.853 -12.637  1.00 29.79           O  
HETATM 2851  O   HOH A 536     -19.718   2.426 -16.499  1.00 19.47           O  
HETATM 2852  O   HOH A 537       1.654  23.087  -8.378  1.00 22.35           O  
HETATM 2853  O   HOH A 538       9.925  12.119 -19.709  1.00 37.68           O  
HETATM 2854  O   HOH A 539       8.019  10.874 -17.879  1.00 20.28           O  
HETATM 2855  O   HOH A 540      -3.828 -13.228 -19.097  1.00 32.10           O  
HETATM 2856  O   HOH A 541      13.536  -4.761 -28.598  1.00 38.59           O  
HETATM 2857  O   HOH A 542       6.846  10.174   1.541  1.00 35.63           O  
HETATM 2858  O   HOH A 543     -12.473  -3.749  -2.229  1.00 43.24           O  
HETATM 2859  O   HOH A 544      13.322  -1.289 -28.240  1.00 31.88           O  
HETATM 2860  O   HOH A 545      11.609  16.203 -31.093  1.00 32.91           O  
HETATM 2861  O   HOH A 546     -25.437  -7.128  -9.436  1.00 37.12           O  
HETATM 2862  O   HOH A 547     -37.391  13.062 -15.185  1.00 36.48           O  
HETATM 2863  O   HOH A 548      -5.181  -7.678 -16.503  1.00 19.25           O  
HETATM 2864  O   HOH A 549      -8.826  -3.222 -29.702  1.00 32.51           O  
HETATM 2865  O   HOH A 550     -18.232  -2.605  -0.331  1.00 37.77           O  
HETATM 2866  O   HOH A 551     -22.863  20.262 -10.196  1.00 53.49           O  
HETATM 2867  O   HOH A 552     -37.845   9.354  -5.171  1.00 24.78           O  
HETATM 2868  O   HOH A 553      -8.322   5.022 -28.182  1.00 32.52           O  
HETATM 2869  O   HOH A 554       7.610  -1.610 -14.966  1.00 32.29           O  
HETATM 2870  O   HOH A 555      11.947  30.369 -15.910  1.00 50.62           O  
HETATM 2871  O   HOH A 556     -17.533  14.906 -21.582  1.00 38.37           O  
HETATM 2872  O   HOH A 557      -2.719  -5.005 -16.826  1.00 19.27           O  
HETATM 2873  O   HOH A 558     -44.359   9.792 -10.872  1.00 33.22           O  
HETATM 2874  O   HOH A 559      12.240   4.194 -18.979  1.00 30.90           O  
HETATM 2875  O   HOH A 560       1.143   9.410   3.562  1.00 30.36           O  
HETATM 2876  O   HOH A 561      -5.932  -7.672 -28.164  1.00 34.09           O  
HETATM 2877  O   HOH A 562       9.557   1.983 -17.386  1.00 29.75           O  
HETATM 2878  O   HOH A 563     -24.186   4.583 -18.631  1.00 28.61           O  
HETATM 2879  O   HOH A 564      11.532  -3.576 -23.861  1.00 24.24           O  
HETATM 2880  O   HOH A 565      -6.670   6.638  -0.251  1.00 34.04           O  
HETATM 2881  O   HOH A 566       2.669  26.984 -21.179  1.00 23.47           O  
HETATM 2882  O   HOH A 567     -26.756  -5.757  -7.535  1.00 40.10           O  
HETATM 2883  O   HOH A 568     -14.656  22.361 -12.625  1.00 41.43           O  
HETATM 2884  O   HOH A 569     -30.956  12.863 -22.473  1.00 25.62           O  
HETATM 2885  O   HOH A 570     -41.763  10.261 -25.305  1.00 24.83           O  
HETATM 2886  O   HOH A 571     -27.282  18.219  -3.629  1.00 50.10           O  
HETATM 2887  O   HOH A 572     -21.442  22.783  -3.639  1.00 37.19           O  
HETATM 2888  O   HOH A 573       5.242  33.143 -12.474  1.00 38.07           O  
HETATM 2889  O   HOH A 574      14.834   7.360 -20.952  1.00 28.77           O  
HETATM 2890  O   HOH A 575      10.198  27.023  -9.261  1.00 52.17           O  
HETATM 2891  O   HOH A 576       9.342   2.169 -21.802  1.00 23.59           O  
HETATM 2892  O   HOH A 577       5.013   1.921 -37.334  1.00 33.53           O  
HETATM 2893  O   HOH A 578       7.631  21.890  -3.230  1.00 25.89           O  
HETATM 2894  O   HOH A 579       6.002  -3.038 -36.733  1.00 38.43           O  
HETATM 2895  O   HOH A 580       6.805   6.090 -11.922  1.00 14.08           O  
HETATM 2896  O   HOH A 581     -11.465  16.840 -24.015  1.00 45.46           O  
HETATM 2897  O   HOH A 582      -6.677  -6.097 -18.178  1.00 16.00           O  
HETATM 2898  O   HOH A 583      -1.474   1.249  -4.581  1.00 25.52           O  
HETATM 2899  O   HOH A 584     -14.849  20.693 -14.483  1.00 37.12           O  
HETATM 2900  O   HOH A 585      -2.730  23.271 -25.900  1.00 37.17           O  
HETATM 2901  O   HOH A 586      -0.688  -0.822 -32.572  1.00 40.60           O  
HETATM 2902  O   HOH A 587       1.235   1.069 -12.403  1.00 21.08           O  
HETATM 2903  O   HOH A 588     -38.636   2.595 -25.232  1.00 48.72           O  
HETATM 2904  O   HOH A 589     -16.976   2.694   1.955  1.00 51.03           O  
HETATM 2905  O   HOH A 590     -13.292   9.003 -26.776  1.00 36.55           O  
HETATM 2906  O   HOH A 591       5.289  20.203  -0.372  1.00 29.16           O  
HETATM 2907  O   HOH A 592      -9.962  19.385 -21.699  1.00 39.74           O  
HETATM 2908  O   HOH A 593     -33.765  18.303 -24.297  1.00 40.41           O  
HETATM 2909  O   HOH A 594     -10.735  11.650 -20.638  1.00 22.56           O  
HETATM 2910  O   HOH A 595      13.637  14.755 -34.288  1.00 45.69           O  
HETATM 2911  O   HOH A 596      -5.920  19.204 -19.063  1.00 26.69           O  
HETATM 2912  O   HOH A 597     -10.756  28.354  -2.047  1.00 44.09           O  
HETATM 2913  O   HOH A 598      13.786   5.981 -31.904  1.00 24.84           O  
HETATM 2914  O   HOH A 599     -26.409   6.679 -22.374  1.00 41.59           O  
HETATM 2915  O   HOH A 600      14.269   8.556 -27.403  1.00 19.55           O  
HETATM 2916  O   HOH A 601       5.603   8.148  -3.784  1.00 28.79           O  
HETATM 2917  O   HOH A 602     -12.277  -8.087  -2.381  1.00 41.74           O  
HETATM 2918  O   HOH A 603     -16.682  -5.954 -16.379  1.00 28.48           O  
HETATM 2919  O   HOH A 604       4.640  17.316 -28.249  1.00 21.00           O  
HETATM 2920  O   HOH A 605     -15.694  -3.855 -21.183  1.00 27.59           O  
HETATM 2921  O   HOH A 606       5.553  15.855 -36.564  1.00 46.40           O  
HETATM 2922  O   HOH A 607      -3.357   0.620 -17.810  1.00 15.22           O  
HETATM 2923  O   HOH A 608      -1.818 -11.370 -23.770  1.00 39.04           O  
HETATM 2924  O   HOH A 609     -29.340   4.206  -6.176  1.00 33.31           O  
HETATM 2925  O   HOH A 610       3.307  -8.209 -17.966  1.00 28.56           O  
HETATM 2926  O   HOH A 611     -13.828  16.849 -22.962  1.00 46.95           O  
HETATM 2927  O   HOH A 612      12.513  17.223 -10.200  1.00 31.87           O  
HETATM 2928  O   HOH A 613     -19.896  -1.112  -2.204  1.00 31.68           O  
HETATM 2929  O   HOH A 614       4.200  -8.366 -31.951  1.00 34.50           O  
HETATM 2930  O   HOH A 615      -6.106  -7.799  -4.942  1.00 37.51           O  
HETATM 2931  O   HOH A 616     -22.208  10.405 -19.591  1.00 38.99           O  
HETATM 2932  O   HOH A 617     -12.463   7.189 -28.446  1.00 39.86           O  
HETATM 2933  O   HOH A 618      16.263  15.392 -16.239  1.00 30.79           O  
HETATM 2934  O   HOH A 619     -23.303   0.894  -1.492  1.00 55.49           O  
HETATM 2935  O   HOH A 620     -33.065  19.620 -28.607  1.00 32.71           O  
HETATM 2936  O   HOH A 621      -9.591  -7.826 -30.053  1.00 49.19           O  
HETATM 2937  O   HOH A 622      12.372  11.171 -17.144  1.00 44.03           O  
HETATM 2938  O   HOH A 623       2.836  13.081   0.514  1.00 28.45           O  
HETATM 2939  O   HOH A 624      -0.415   5.659   3.555  1.00 29.45           O  
HETATM 2940  O   HOH A 625      -9.643   2.495  -0.081  1.00 48.58           O  
HETATM 2941  O   HOH A 626     -33.544  -3.514 -13.289  1.00 53.50           O  
HETATM 2942  O   HOH A 627      -2.577  11.684 -23.814  1.00 13.02           O  
HETATM 2943  O   HOH A 628      -3.694  18.052 -20.601  1.00 15.80           O  
HETATM 2944  O   HOH A 629      -5.543   2.869 -30.906  1.00 44.04           O  
HETATM 2945  O   HOH A 630       4.009  30.020  -5.952  1.00 30.91           O  
HETATM 2946  O   HOH A 631     -39.239   6.333 -11.692  1.00 25.50           O  
HETATM 2947  O   HOH A 632     -17.799  -7.086 -14.119  1.00 23.63           O  
HETATM 2948  O   HOH A 633      -0.188  -2.655 -14.345  1.00 22.14           O  
HETATM 2949  O   HOH A 634     -39.923  21.979 -14.761  1.00 35.24           O  
HETATM 2950  O   HOH A 635      -3.777  25.572 -16.807  1.00 38.04           O  
HETATM 2951  O   HOH A 636     -25.927  -2.047  -5.486  1.00 31.34           O  
HETATM 2952  O   HOH A 637     -16.375   6.816 -16.579  1.00 18.86           O  
HETATM 2953  O   HOH A 638      -9.153   7.324  -0.655  1.00 25.32           O  
HETATM 2954  O   HOH A 639     -42.172   7.989 -10.684  1.00 37.29           O  
HETATM 2955  O   HOH A 640      -4.203  -7.757 -24.964  1.00 35.32           O  
HETATM 2956  O   HOH A 641      16.508  16.267 -24.486  1.00 26.62           O  
HETATM 2957  O   HOH A 642     -29.873  23.555  -2.720  1.00 40.91           O  
HETATM 2958  O   HOH A 643      -2.978   2.069 -32.686  1.00 42.78           O  
HETATM 2959  O   HOH A 644       2.908  16.263 -34.098  1.00 46.12           O  
HETATM 2960  O   HOH A 645     -23.481   8.189 -19.097  1.00 21.39           O  
HETATM 2961  O   HOH A 646       4.190  -2.010 -38.124  1.00 39.24           O  
HETATM 2962  O   HOH A 647      -3.157   5.938 -31.974  1.00 26.60           O  
HETATM 2963  O   HOH A 648       4.914  23.174  -7.500  1.00 22.97           O  
HETATM 2964  O   HOH A 649      -9.310  -3.518  -1.710  1.00 37.00           O  
HETATM 2965  O   HOH A 650       2.142  14.487   2.746  1.00 32.35           O  
HETATM 2966  O   HOH A 651      -0.092  -1.461 -11.996  1.00 24.35           O  
HETATM 2967  O   HOH A 652     -10.182  -7.614  -9.522  1.00 23.91           O  
HETATM 2968  O   HOH A 653      -3.532   2.971  -5.357  1.00 18.17           O  
HETATM 2969  O   HOH A 654      -2.615  -0.719 -11.422  1.00 19.55           O  
HETATM 2970  O   HOH A 655     -45.031  15.294  -6.688  1.00 43.64           O  
HETATM 2971  O   HOH A 656      12.722   7.877 -25.150  1.00 17.63           O  
HETATM 2972  O   HOH A 657       0.783  19.361 -28.102  1.00 22.55           O  
HETATM 2973  O   HOH A 658     -14.254  -2.017 -22.187  1.00 22.43           O  
HETATM 2974  O   HOH A 659     -16.165 -10.040 -16.843  1.00 48.85           O  
HETATM 2975  O   HOH A 660      -0.605   3.134 -11.759  1.00 22.82           O  
HETATM 2976  O   HOH A 661     -36.146  -2.622 -12.133  1.00 43.30           O  
HETATM 2977  O   HOH A 662       0.615  29.876 -20.319  1.00 36.16           O  
HETATM 2978  O   HOH A 663       3.992  13.798 -37.517  1.00 27.51           O  
HETATM 2979  O   HOH A 664      -4.066   3.001  -8.124  1.00 17.25           O  
HETATM 2980  O   HOH A 665       7.153   0.875 -35.953  1.00 29.96           O  
HETATM 2981  O   HOH A 666      -2.933  16.299 -22.621  1.00 15.29           O  
HETATM 2982  O   HOH A 667     -19.517   8.858   3.380  1.00 44.25           O  
HETATM 2983  O   HOH A 668       0.292   8.197 -41.703  1.00 44.65           O  
HETATM 2984  O   HOH A 669     -11.811   8.671 -30.596  1.00 28.70           O  
HETATM 2985  O   HOH A 670     -22.688   7.480  -5.596  1.00 18.79           O  
HETATM 2986  O   HOH A 671     -12.367 -11.531 -11.300  1.00 39.54           O  
HETATM 2987  O   HOH A 672      -8.055   9.288 -34.688  1.00 39.74           O  
HETATM 2988  O   HOH A 673       2.910  18.653 -25.805  1.00 33.85           O  
HETATM 2989  O   HOH A 674      -4.441   1.841 -35.012  1.00 31.19           O  
HETATM 2990  O   HOH A 675       0.553  22.313 -28.708  1.00 39.26           O  
HETATM 2991  O   HOH A 676       1.361  13.395 -36.773  1.00 28.59           O  
HETATM 2992  O   HOH A 677     -22.038  12.205 -22.528  1.00 49.22           O  
HETATM 2993  O   HOH A 678      -8.904   8.039 -17.321  1.00 14.27           O  
HETATM 2994  O   HOH A 679      -6.175  17.849   2.388  1.00 33.26           O  
HETATM 2995  O   HOH A 680     -23.165  17.635  -9.554  1.00 29.17           O  
HETATM 2996  O   HOH A 681     -33.571  -5.434 -14.703  1.00 44.35           O  
HETATM 2997  O   HOH A 682       4.724  25.269 -21.397  1.00 26.36           O  
HETATM 2998  O   HOH A 683       7.611  13.187 -36.008  1.00 26.75           O  
HETATM 2999  O   HOH A 684       6.112  -1.239 -34.600  1.00 29.54           O  
HETATM 3000  O   HOH A 685       3.628  18.449 -33.009  1.00 31.32           O  
HETATM 3001  O   HOH A 686       8.897  27.093 -22.327  1.00 39.15           O  
HETATM 3002  O   HOH A 687      12.694   8.952 -17.951  1.00 38.43           O  
HETATM 3003  O   HOH A 688     -21.512  15.011  -0.159  1.00 50.21           O  
HETATM 3004  O   HOH A 689     -38.175  -0.199  -7.790  1.00 41.70           O  
HETATM 3005  O   HOH A 690      -0.704   1.615 -33.203  1.00 43.43           O  
HETATM 3006  O   HOH A 691     -39.515  18.702 -14.601  1.00 34.22           O  
HETATM 3007  O   HOH A 692      11.164  17.130  -1.246  1.00 42.48           O  
HETATM 3008  O   HOH A 693     -17.611   9.084 -18.871  1.00 26.63           O  
HETATM 3009  O   HOH A 694      -2.458  21.541 -31.331  1.00 41.46           O  
HETATM 3010  O   HOH A 695     -41.183   4.257  -8.494  1.00 46.66           O  
HETATM 3011  O   HOH A 696     -12.137  18.307 -20.040  1.00 21.11           O  
HETATM 3012  O   HOH A 697       1.149  30.181  -6.309  1.00 28.67           O  
HETATM 3013  O   HOH A 698     -12.006  12.865 -27.732  1.00 37.11           O  
HETATM 3014  O   HOH A 699     -16.514 -10.598  -0.179  1.00 43.14           O  
HETATM 3015  O   HOH A 700      15.390  18.456 -23.135  1.00 35.31           O  
HETATM 3016  O   HOH A 701     -16.647  13.053  -0.072  1.00 32.45           O  
HETATM 3017  O   HOH A 702      21.526   7.871 -36.804  1.00 35.12           O  
HETATM 3018  O   HOH A 703      -3.567  -7.500  -5.414  1.00 39.13           O  
HETATM 3019  O   HOH A 704     -31.826  15.786  -2.536  1.00 54.40           O  
HETATM 3020  O   HOH A 705      -4.065  -6.109 -26.952  1.00 21.72           O  
HETATM 3021  O   HOH A 706     -36.698  16.169   3.024  1.00 41.57           O  
HETATM 3022  O   HOH A 707      10.351  32.750 -19.754  1.00 32.53           O  
HETATM 3023  O   HOH A 708       4.398 -12.941 -26.303  1.00 35.80           O  
HETATM 3024  O   HOH A 709     -33.783  21.316   3.100  1.00 42.06           O  
HETATM 3025  O   HOH A 710     -43.155   6.152  -8.724  1.00 40.10           O  
HETATM 3026  O   HOH A 711      -9.804  14.051 -35.761  1.00 41.09           O  
HETATM 3027  O   HOH A 712      -2.502  11.487 -38.552  1.00 42.41           O  
HETATM 3028  O   HOH A 713       0.996  16.162   5.980  1.00 39.89           O  
HETATM 3029  O   HOH A 714      -0.002  -5.170 -32.166  1.00 43.47           O  
HETATM 3030  O   HOH A 715      -3.563  33.767 -11.762  1.00 40.07           O  
HETATM 3031  O   HOH A 716       0.127  -3.172 -36.271  1.00 33.79           O  
HETATM 3032  O   HOH A 717     -23.114  -5.236  -4.160  1.00 30.43           O  
HETATM 3033  O   HOH A 718      11.295   8.671 -12.383  1.00 42.13           O  
HETATM 3034  O   HOH A 719     -10.764  -2.256 -28.390  1.00 30.56           O  
HETATM 3035  O   HOH A 720     -11.265 -10.863 -22.033  1.00 39.15           O  
HETATM 3036  O   HOH A 721     -14.451  -6.150 -21.216  1.00 38.06           O  
HETATM 3037  O   HOH A 722       8.353  -0.220 -11.351  1.00 46.45           O  
HETATM 3038  O   HOH A 723      10.848  36.088 -19.324  1.00 51.46           O  
HETATM 3039  O   HOH A 724      12.187  12.849 -36.804  1.00 35.86           O  
HETATM 3040  O   HOH A 725       5.730  37.005 -15.496  1.00 51.60           O  
HETATM 3041  O   HOH A 726      -4.071  27.061 -21.428  1.00 44.73           O  
HETATM 3042  O   HOH A 727       1.907  -8.430 -15.087  1.00 33.91           O  
HETATM 3043  O   HOH A 728     -18.654  11.951  -1.125  1.00 35.55           O  
HETATM 3044  O   HOH A 729      -4.202 -11.959 -25.145  1.00 49.31           O  
HETATM 3045  O   HOH A 730     -11.735  -0.458 -30.387  1.00 44.16           O  
HETATM 3046  O   HOH A 731      -7.017   0.853 -31.777  1.00 44.44           O  
HETATM 3047  O   HOH A 732      -2.625  14.651 -37.803  1.00 45.29           O  
HETATM 3048  O   HOH A 733       8.277 -10.013 -22.223  1.00 36.18           O  
HETATM 3049  O   HOH A 734      12.170   2.305 -20.841  1.00 41.92           O  
HETATM 3050  O   HOH A 735     -37.915  15.520 -13.990  1.00 46.84           O  
HETATM 3051  O   HOH A 736       9.165  23.433 -26.077  1.00 37.39           O  
HETATM 3052  O   HOH A 737       4.034  19.010 -30.422  1.00 29.89           O  
HETATM 3053  O   HOH A 738      -6.946   5.479   2.745  1.00 40.68           O  
HETATM 3054  O   HOH A 739       7.612  -8.628 -20.296  1.00 42.74           O  
HETATM 3055  O   HOH A 740      11.602  30.294 -20.385  1.00 41.08           O  
HETATM 3056  O   HOH A 741     -26.578   1.371 -27.997  1.00 50.68           O  
HETATM 3057  O   HOH A 742     -19.652   8.399 -20.588  1.00 35.46           O  
HETATM 3058  O   HOH A 743     -36.686  -2.087 -14.963  1.00 45.63           O  
HETATM 3059  O   HOH A 744      11.385  -2.155 -21.494  1.00 36.38           O  
HETATM 3060  O   HOH A 745      -1.794  -5.664 -28.492  1.00 38.63           O  
HETATM 3061  O   HOH A 746       9.101  -0.534 -21.219  1.00 29.28           O  
HETATM 3062  O   HOH A 747     -12.809  -3.715 -28.182  1.00 41.13           O  
HETATM 3063  O   HOH A 748     -20.285  30.954   2.920  1.00 40.54           O  
HETATM 3064  O   HOH A 749      -9.100   4.264 -30.394  1.00 47.35           O  
HETATM 3065  O   HOH A 750      -2.767   1.962 -10.488  1.00 19.13           O  
HETATM 3066  O   HOH A 751     -32.317  11.372 -23.888  1.00 39.62           O  
HETATM 3067  O   HOH A 752      11.353  -6.428 -23.763  1.00 44.73           O  
HETATM 3068  O   HOH A 753      13.862   6.866 -18.651  1.00 43.64           O  
HETATM 3069  O   HOH A 754     -19.868  -8.525 -15.864  1.00 51.43           O  
HETATM 3070  O   HOH A 755       3.585  11.030   3.137  1.00 41.55           O  
HETATM 3071  O   HOH A 756       8.561  23.090 -28.846  1.00 33.88           O  
HETATM 3072  O   HOH A 757     -41.706   6.006 -19.281  1.00 47.85           O  
HETATM 3073  O   HOH A 758      10.063  14.027 -37.358  1.00 45.72           O  
HETATM 3074  O   HOH A 759       1.105  35.145 -15.769  1.00 45.96           O  
HETATM 3075  O   HOH A 760       1.381  27.455 -23.709  1.00 31.43           O  
HETATM 3076  O   HOH A 761     -17.988  -4.453 -22.520  1.00 45.64           O  
HETATM 3077  O   HOH A 762     -24.498   6.148 -20.875  1.00 27.10           O  
HETATM 3078  O   HOH A 763     -42.298   6.257 -17.000  1.00 36.12           O  
HETATM 3079  O   HOH A 764       3.845  21.194 -28.939  1.00 37.57           O  
HETATM 3080  O   HOH A 765      -5.697   4.844 -32.432  1.00 38.37           O  
HETATM 3081  O   HOH A 766      12.743  -0.351 -20.201  1.00 49.20           O  
HETATM 3082  O   HOH A 767       9.572   9.744  -4.495  1.00 34.98           O  
HETATM 3083  O   HOH A 768     -41.878   6.267 -12.840  1.00 39.41           O  
HETATM 3084  O   HOH A 769      -4.482  27.054 -18.596  1.00 41.25           O  
HETATM 3085  O   HOH A 770       7.254  19.026 -27.915  1.00 42.55           O  
HETATM 3086  O   HOH A 771       4.253  20.769 -26.019  1.00 42.36           O  
HETATM 3087  O   HOH A 772     -14.227  18.841 -21.623  1.00 46.31           O  
HETATM 3088  O   HOH A 773       7.541   8.538  -5.705  1.00 31.08           O  
HETATM 3089  O   HOH A 774       8.062   5.680  -9.482  1.00 33.98           O  
HETATM 3090  O   HOH A 775      -8.430   9.740 -37.606  1.00 44.42           O  
HETATM 3091  O   HOH A 776      -0.362  12.969 -38.645  1.00 37.99           O  
HETATM 3092  O   HOH A 777      -9.837   1.783 -32.148  1.00 48.82           O  
HETATM 3093  O   HOH A 778       1.441  10.075 -43.561  1.00 52.09           O  
HETATM 3094  O   HOH A 779       5.099  24.881 -23.727  1.00 40.39           O  
HETATM 3095  O   HOH A 780      -9.332   9.116   1.655  1.00 31.52           O  
HETATM 3096  O   HOH A 781       8.317   6.050  -6.793  1.00 27.47           O  
HETATM 3097  O   HOH A 782      -1.360   9.928 -42.045  1.00 42.43           O  
CONECT 2795 2796 2797 2798 2799                                                 
CONECT 2796 2795                                                                
CONECT 2797 2795                                                                
CONECT 2798 2795                                                                
CONECT 2799 2795                                                                
CONECT 2800 2801 2802 2803 2804                                                 
CONECT 2801 2800                                                                
CONECT 2802 2800                                                                
CONECT 2803 2800                                                                
CONECT 2804 2800                                                                
CONECT 2805 2806 2811 2812                                                      
CONECT 2806 2805 2807                                                           
CONECT 2807 2806 2808 2814                                                      
CONECT 2808 2807 2809 2815                                                      
CONECT 2809 2808 2811                                                           
CONECT 2810 2812                                                                
CONECT 2811 2805 2809                                                           
CONECT 2812 2805 2810                                                           
CONECT 2813 2814                                                                
CONECT 2814 2807 2813                                                           
CONECT 2815 2808                                                                
MASTER      344    0    3   20    9    0    6    6 3076    1   21   26          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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