CNRS Nantes University UFIP UFIP
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***  6n0t  ***

elNémo ID: 20020118471865398

Job options:

ID        	=	 20020118471865398
JOBID     	=	 6n0t
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6n0t

HEADER    LIGASE                                  07-NOV-18   6N0T              
TITLE     TRNA LIGASE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA LIGASE;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS  
SOURCE   3 144.50 / IMI 039719);                                                
SOURCE   4 ORGANISM_TAXID: 759272;                                              
SOURCE   5 STRAIN: DSM 1495 / CBS 144.50 / IMI 039719;                          
SOURCE   6 GENE: CTHT_0034810;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    TRNA, RNA LIGASE, NUCLEOTIDYLTRANSFERASE, N6-AMP-LYSINE INTERMEDIATE, 
KEYWDS   2 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.BANERJEE,Y.GOLDGUR,S.SHUMAN                                         
REVDAT   3   04-DEC-19 6N0T    1       REMARK                                   
REVDAT   2   03-JUL-19 6N0T    1       JRNL                                     
REVDAT   1   09-JAN-19 6N0T    0                                                
JRNL        AUTH   A.BANERJEE,S.GHOSH,Y.GOLDGUR,S.SHUMAN                        
JRNL        TITL   STRUCTURE AND TWO-METAL MECHANISM OF FUNGAL TRNA LIGASE.     
JRNL        REF    NUCLEIC ACIDS RES.            V.  47  1428 2019              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   30590734                                                     
JRNL        DOI    10.1093/NAR/GKY1275                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829)                                   
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) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17096                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1711                            
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 47.4239 -  5.7449    1.00     1409   157  0.1948 0.2363        
REMARK   3     2  5.7449 -  4.5611    1.00     1330   148  0.1546 0.2126        
REMARK   3     3  4.5611 -  3.9849    1.00     1306   146  0.1448 0.2217        
REMARK   3     4  3.9849 -  3.6207    1.00     1296   144  0.1548 0.2400        
REMARK   3     5  3.6207 -  3.3612    1.00     1281   142  0.1737 0.2351        
REMARK   3     6  3.3612 -  3.1631    1.00     1276   142  0.1774 0.2464        
REMARK   3     7  3.1631 -  3.0047    1.00     1272   141  0.1938 0.2525        
REMARK   3     8  3.0047 -  2.8740    1.00     1283   143  0.1979 0.3138        
REMARK   3     9  2.8740 -  2.7633    1.00     1261   140  0.2250 0.2862        
REMARK   3    10  2.7633 -  2.6680    1.00     1291   144  0.2121 0.2933        
REMARK   3    11  2.6680 -  2.5846    1.00     1218   135  0.2185 0.3100        
REMARK   3    12  2.5846 -  2.5107    0.90     1162   129  0.2386 0.3377        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3179                                  
REMARK   3   ANGLE     :  1.008           4299                                  
REMARK   3   CHIRALITY :  0.054            455                                  
REMARK   3   PLANARITY :  0.005            548                                  
REMARK   3   DIHEDRAL  :  6.798           1900                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND ( RESID 14:406 OR RESID 501:502 ) )      
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8984  62.3912  23.6597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2378 T22:   0.2198                                     
REMARK   3      T33:   0.2710 T12:   0.0373                                     
REMARK   3      T13:  -0.0127 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5689 L22:   0.5548                                     
REMARK   3      L33:   2.3045 L12:   0.2443                                     
REMARK   3      L13:  -0.3819 L23:  -0.6397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0012 S12:   0.0443 S13:  -0.0916                       
REMARK   3      S21:   0.0212 S22:  -0.0403 S23:  -0.0286                       
REMARK   3      S31:   0.2053 S32:   0.2318 S33:   0.0328                       
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 6N0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237980.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17102                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELXCD                                               
REMARK 200 STARTING MODEL: 6NOV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.6 AND 2.5 M AMMONIUM     
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.65500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       86.35900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.34400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       86.35900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.65500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.34400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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   -33                                                      
REMARK 465     GLY A   -32                                                      
REMARK 465     SER A   -31                                                      
REMARK 465     SER A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     SER A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     VAL A   -19                                                      
REMARK 465     PRO A   -18                                                      
REMARK 465     ARG A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     MET A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     LYS A    56                                                      
REMARK 465     LYS A    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     ARG A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     VAL A   178                                                      
REMARK 465     ALA A   179                                                      
REMARK 465     GLU A   407                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   607     O    HOH A   713     3555     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  23      -14.55    -48.99                                   
REMARK 500    ASP A  93       62.73     60.67                                   
REMARK 500    HIS A 170       16.43   -143.90                                   
REMARK 500    THR A 172       -6.44   -153.29                                   
REMARK 500    HIS A 227     -119.18   -110.06                                   
REMARK 500    LYS A 235      -24.29     72.51                                   
REMARK 500    CYS A 306     -169.49   -163.15                                   
REMARK 500    PRO A 312     -177.73    -64.21                                   
REMARK 500    VAL A 314     -149.17   -118.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 737        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 738        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A 739        DISTANCE =  9.34 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 503  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 502   O2G                                                    
REMARK 620 2 ATP A 502   O1B  90.7                                              
REMARK 620 3 HOH A 700   O    78.6 100.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 504  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 502   O2A                                                    
REMARK 620 2 HOH A 603   O    96.8                                              
REMARK 620 3 HOH A 605   O    90.7 172.0                                        
REMARK 620 4 HOH A 624   O    75.7  89.8  89.6                                  
REMARK 620 5 HOH A 652   O   111.0  79.5 100.3 167.8                            
REMARK 620 6 HOH A 601   O   151.7  99.7  72.3  81.6  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 504                  
DBREF  6N0T A    1   407  UNP    G0S6G2   G0S6G2_CHATD     1    407             
SEQADV 6N0T MET A  -33  UNP  G0S6G2              INITIATING METHIONINE          
SEQADV 6N0T GLY A  -32  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -31  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -30  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -29  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -28  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -27  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -26  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -25  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -24  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -23  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -22  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A  -21  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T LEU A  -20  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T VAL A  -19  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T PRO A  -18  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T ARG A  -17  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A  -16  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -15  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T HIS A  -14  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T MET A  -13  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T ALA A  -12  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A  -11  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T MET A  -10  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T THR A   -9  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A   -8  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A   -7  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLN A   -6  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLN A   -5  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T MET A   -4  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A   -3  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T ARG A   -2  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T GLY A   -1  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T SER A    0  UNP  G0S6G2              EXPRESSION TAG                 
SEQADV 6N0T MET A  148  UNP  G0S6G2    LYS   148 CONFLICT                       
SEQRES   1 A  441  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  441  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 A  441  GLY GLN GLN MET GLY ARG GLY SER MET ASP GLY THR ALA          
SEQRES   4 A  441  GLU LYS GLN ARG ASP SER LEU ALA SER ARG TYR LYS ALA          
SEQRES   5 A  441  SER THR ASP TYR ALA LYS ASP ALA GLU GLY LEU THR ALA          
SEQRES   6 A  441  PRO TYR VAL SER GLN ASP PRO GLN GLU THR ALA ALA LEU          
SEQRES   7 A  441  VAL ARG ALA LEU ASP ASP ALA ALA LYS LYS GLY LYS LYS          
SEQRES   8 A  441  SER GLY GLY PHE SER VAL LYS LYS THR ARG TYR ALA VAL          
SEQRES   9 A  441  ALA SER SER PRO THR GLY ALA GLU VAL ASP SER TRP ARG          
SEQRES  10 A  441  PHE ASN ASP TRP ASP TYR LYS LYS PRO ASP LEU PRO THR          
SEQRES  11 A  441  TYR ALA ARG GLY LEU PHE THR THR ARG THR GLN HIS GLY          
SEQRES  12 A  441  VAL PRO GLU ILE ALA VAL ARG GLY TYR ASP LYS PHE PHE          
SEQRES  13 A  441  ASN ILE ASP GLU THR ARG ASP THR ALA TRP SER ALA ILE          
SEQRES  14 A  441  ARG GLU ARG THR LYS GLY PRO TYR GLU LEU THR LEU MET          
SEQRES  15 A  441  GLU ASN GLY CYS ILE ILE PHE ILE SER GLY LEU GLU ASP          
SEQRES  16 A  441  GLY THR LEU LEU VAL CYS SER LYS HIS SER THR GLY ASP          
SEQRES  17 A  441  ARG SER ASP VAL ALA LEU SER HIS SER SER ALA GLY GLU          
SEQRES  18 A  441  LYS HIS LEU GLU ALA GLN LEU GLU ARG ILE GLY LYS THR          
SEQRES  19 A  441  LYS GLU GLU LEU ALA ARG GLU LEU ARG LYS ARG ASN ALA          
SEQRES  20 A  441  THR ALA VAL ALA GLU LEU CYS ASP ASP SER PHE GLU GLU          
SEQRES  21 A  441  HIS ILE LEU ALA TYR GLY PRO ASP LYS ALA GLY LEU TYR          
SEQRES  22 A  441  LEU HIS GLY ILE ASN LEU ASN ILE PRO GLU PHE ILE THR          
SEQRES  23 A  441  TYR PRO SER PRO LEU VAL GLN LYS PHE ALA GLU ASP TRP          
SEQRES  24 A  441  GLY PHE ARG LYS THR GLY LEU ILE ILE ILE ASP ASN ILE          
SEQRES  25 A  441  ASP ASP VAL LYS ALA PHE LEU GLU GLU VAL ALA GLU THR          
SEQRES  26 A  441  GLY ALA HIS ASP GLY ARG ASP VAL GLU GLY PHE VAL ILE          
SEQRES  27 A  441  ARG CYS LYS LYS SER THR ASN PRO GLY VAL GLY PRO TYR          
SEQRES  28 A  441  HIS ASP TRP PHE PHE LYS TYR LYS PHE GLU GLU PRO TYR          
SEQRES  29 A  441  LEU MET TYR ARG GLN TRP ARG GLU CYS THR LYS ALA LEU          
SEQRES  30 A  441  ILE SER GLY LYS GLN PRO LYS ILE LYS LYS HIS VAL LYS          
SEQRES  31 A  441  ILE THR GLU GLU TYR LEU LEU TYR ALA ARG LYS ARG LEU          
SEQRES  32 A  441  ALA ALA ASP PRO LYS LEU ALA LYS LEU TYR ASN GLN ASN          
SEQRES  33 A  441  HIS GLY ILE ILE LYS LEU ARG ASN ASP PHE LEU GLU TYR          
SEQRES  34 A  441  LYS ASN MET LYS GLY THR ASP ALA ALA ASN LEU GLU              
HET    SO4  A 501       5                                                       
HET    ATP  A 502      31                                                       
HET     MN  A 503       1                                                       
HET     MN  A 504       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4   MN    2(MN 2+)                                                     
FORMUL   6  HOH   *139(H2 O)                                                    
HELIX    1 AA1 ASP A   21  GLY A   28  5                                   8    
HELIX    2 AA2 ASP A   37  LYS A   53  1                                  17    
HELIX    3 AA3 TRP A   87  LYS A   91  5                                   5    
HELIX    4 AA4 ALA A  131  ARG A  138  1                                   8    
HELIX    5 AA5 SER A  181  GLY A  198  1                                  18    
HELIX    6 AA6 THR A  200  ARG A  211  1                                  12    
HELIX    7 AA7 PRO A  254  GLY A  266  1                                  13    
HELIX    8 AA8 ASN A  277  GLY A  292  1                                  16    
HELIX    9 AA9 PRO A  329  SER A  345  1                                  17    
HELIX   10 AB1 HIS A  354  ASP A  372  1                                  19    
HELIX   11 AB2 LYS A  374  GLN A  381  1                                   8    
HELIX   12 AB3 GLY A  384  LYS A  396  1                                  13    
HELIX   13 AB4 LYS A  399  LEU A  406  1                                   8    
SHEET    1 AA1 4 VAL A  63  ALA A  69  0                                        
SHEET    2 AA1 4 GLU A  78  PHE A  84 -1  O  SER A  81   N  THR A  66           
SHEET    3 AA1 4 LEU A 101  ARG A 105 -1  O  THR A 103   N  ASP A  80           
SHEET    4 AA1 4 PRO A 111  ARG A 116 -1  O  ALA A 114   N  PHE A 102           
SHEET    1 AA2 4 LEU A 272  ILE A 275  0                                        
SHEET    2 AA2 4 THR A 139  LEU A 147 -1  N  LEU A 145   O  ILE A 273           
SHEET    3 AA2 4 GLY A 301  LYS A 308 -1  O  ARG A 305   N  GLU A 144           
SHEET    4 AA2 4 HIS A 318  LYS A 325 -1  O  PHE A 322   N  ILE A 304           
SHEET    1 AA3 5 LEU A 164  CYS A 167  0                                        
SHEET    2 AA3 5 CYS A 152  GLY A 158 -1  N  PHE A 155   O  CYS A 167           
SHEET    3 AA3 5 ALA A 213  CYS A 220 -1  O  ALA A 215   N  ILE A 156           
SHEET    4 AA3 5 GLY A 237  LEU A 245 -1  O  TYR A 239   N  GLU A 218           
SHEET    5 AA3 5 ARG A 268  LYS A 269  1  O  ARG A 268   N  LEU A 238           
SHEET    1 AA4 2 ALA A 293  HIS A 294  0                                        
SHEET    2 AA4 2 ARG A 297  ASP A 298 -1  O  ARG A 297   N  HIS A 294           
LINK         O2G ATP A 502                MN    MN A 503     1555   1555  2.37  
LINK         O1B ATP A 502                MN    MN A 503     1555   1555  2.28  
LINK         O2A ATP A 502                MN    MN A 504     1555   1555  2.20  
LINK        MN    MN A 503                 O   HOH A 700     1555   1555  2.61  
LINK        MN    MN A 504                 O   HOH A 603     1555   1555  2.62  
LINK        MN    MN A 504                 O   HOH A 605     1555   1555  2.42  
LINK        MN    MN A 504                 O   HOH A 624     1555   1555  2.20  
LINK        MN    MN A 504                 O   HOH A 652     1555   1555  2.17  
LINK        MN    MN A 504                 O   HOH A 601     1555   1555  2.44  
CISPEP   1 GLY A  141    PRO A  142          0        -1.79                     
CISPEP   2 GLU A  328    PRO A  329          0         0.35                     
SITE     1 AC1  7 ASN A 150  HIS A 227  ILE A 228  ARG A 334                    
SITE     2 AC1  7 ARG A 337  HOH A 601  HOH A 605                               
SITE     1 AC2 23 ARG A  99  TYR A 118  LYS A 120  PHE A 121                    
SITE     2 AC2 23 THR A 146  LEU A 147  MET A 148  GLU A 149                    
SITE     3 AC2 23 ILE A 153  LYS A 169  GLU A 218  HIS A 241                    
SITE     4 AC2 23 VAL A 303  ARG A 305  LYS A 323  LYS A 325                    
SITE     5 AC2 23  MN A 503   MN A 504  HOH A 603  HOH A 624                    
SITE     6 AC2 23 HOH A 630  HOH A 682  HOH A 692                               
SITE     1 AC3  5 ASP A  86  ATP A 502  HOH A 630  HOH A 700                    
SITE     2 AC3  5 HOH A 724                                                     
SITE     1 AC4  6 ATP A 502  HOH A 601  HOH A 603  HOH A 605                    
SITE     2 AC4  6 HOH A 624  HOH A 652                                          
CRYST1   49.310   56.688  172.718  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020280  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017640  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005790        0.00000                         
ATOM      1  N   SER A  14      30.661  59.017  34.331  1.00 82.77           N  
ANISOU    1  N   SER A  14     8594  13215   9641   1194   -486   1278       N  
ATOM      2  CA  SER A  14      32.073  58.763  34.057  1.00 96.64           C  
ANISOU    2  CA  SER A  14    10148  15263  11308   1304   -471   1418       C  
ATOM      3  C   SER A  14      32.854  60.072  33.956  1.00101.46           C  
ANISOU    3  C   SER A  14    10629  16090  11831   1049   -527   1438       C  
ATOM      4  O   SER A  14      32.561  61.052  34.643  1.00 94.39           O  
ANISOU    4  O   SER A  14     9740  15222  10901    804   -612   1409       O  
ATOM      5  CB  SER A  14      32.228  57.950  32.761  1.00 92.36           C  
ANISOU    5  CB  SER A  14     9641  14637  10815   1538   -363   1400       C  
ATOM      6  OG  SER A  14      33.562  57.489  32.583  1.00 89.95           O  
ANISOU    6  OG  SER A  14     9222  14526  10430   1644   -305   1509       O  
ATOM      7  N   ARG A  15      33.862  60.078  33.090  1.00105.73           N  
ANISOU    7  N   ARG A  15    11068  16776  12328   1101   -472   1487       N  
ATOM      8  CA  ARG A  15      34.514  61.311  32.681  1.00105.16           C  
ANISOU    8  CA  ARG A  15    10897  16873  12185    874   -508   1491       C  
ATOM      9  C   ARG A  15      33.710  62.067  31.628  1.00104.51           C  
ANISOU    9  C   ARG A  15    10883  16654  12173    788   -516   1370       C  
ATOM     10  O   ARG A  15      34.265  62.927  30.931  1.00109.17           O  
ANISOU   10  O   ARG A  15    11406  17358  12716    652   -520   1369       O  
ATOM     11  CB  ARG A  15      35.923  61.013  32.161  1.00105.48           C  
ANISOU   11  CB  ARG A  15    10797  17138  12141    967   -444   1602       C  
ATOM     12  CG  ARG A  15      36.812  60.292  33.168  1.00108.77           C  
ANISOU   12  CG  ARG A  15    11129  17721  12478   1053   -430   1736       C  
ATOM     13  CD  ARG A  15      36.961  58.807  32.844  1.00107.97           C  
ANISOU   13  CD  ARG A  15    11062  17550  12412   1385   -330   1779       C  
ATOM     14  NE  ARG A  15      37.164  57.997  34.045  1.00108.21           N  
ANISOU   14  NE  ARG A  15    11087  17616  12413   1479   -330   1865       N  
ATOM     15  CZ  ARG A  15      38.290  57.966  34.756  1.00109.46           C  
ANISOU   15  CZ  ARG A  15    11104  18027  12458   1447   -335   1998       C  
ATOM     16  NH1 ARG A  15      39.333  58.698  34.395  1.00116.04           N  
ANISOU   16  NH1 ARG A  15    11792  19106  13193   1320   -339   2064       N  
ATOM     17  NH2 ARG A  15      38.379  57.198  35.831  1.00105.62           N  
ANISOU   17  NH2 ARG A  15    10623  17556  11953   1540   -334   2071       N  
ATOM     18  N   TYR A  16      32.421  61.757  31.497  1.00 90.05           N  
ANISOU   18  N   TYR A  16     9184  14584  10446    864   -517   1273       N  
ATOM     19  CA  TYR A  16      31.539  62.384  30.527  1.00 77.08           C  
ANISOU   19  CA  TYR A  16     7676  12725   8885    776   -492   1130       C  
ATOM     20  C   TYR A  16      30.459  63.197  31.237  1.00 72.67           C  
ANISOU   20  C   TYR A  16     7287  11960   8366    553   -536   1019       C  
ATOM     21  O   TYR A  16      30.024  62.862  32.343  1.00 83.13           O  
ANISOU   21  O   TYR A  16     8684  13204   9698    545   -558   1019       O  
ATOM     22  CB  TYR A  16      30.898  61.336  29.615  1.00 75.30           C  
ANISOU   22  CB  TYR A  16     7569  12281   8761   1018   -399   1064       C  
ATOM     23  CG  TYR A  16      31.819  60.793  28.535  1.00 79.83           C  
ANISOU   23  CG  TYR A  16     8013  13016   9305   1217   -337   1136       C  
ATOM     24  CD1 TYR A  16      32.236  59.463  28.550  1.00 72.97           C  
ANISOU   24  CD1 TYR A  16     7146  12148   8433   1484   -264   1204       C  
ATOM     25  CD2 TYR A  16      32.259  61.604  27.491  1.00 85.34           C  
ANISOU   25  CD2 TYR A  16     8624  13827   9974   1128   -335   1126       C  
ATOM     26  CE1 TYR A  16      33.070  58.956  27.562  1.00 71.45           C  
ANISOU   26  CE1 TYR A  16     6913  12027   8208   1634   -178   1242       C  
ATOM     27  CE2 TYR A  16      33.095  61.104  26.495  1.00 84.75           C  
ANISOU   27  CE2 TYR A  16     8493  13838   9870   1282   -254   1169       C  
ATOM     28  CZ  TYR A  16      33.498  59.778  26.540  1.00 74.84           C  
ANISOU   28  CZ  TYR A  16     7265  12560   8609   1535   -175   1225       C  
ATOM     29  OH  TYR A  16      34.325  59.271  25.560  1.00 70.83           O  
ANISOU   29  OH  TYR A  16     6720  12129   8061   1686    -90   1266       O  
ATOM     30  N   LYS A  17      30.030  64.269  30.577  1.00 64.72           N  
ANISOU   30  N   LYS A  17     6345  10866   7380    381   -543    928       N  
ATOM     31  CA  LYS A  17      29.175  65.297  31.164  1.00 72.35           C  
ANISOU   31  CA  LYS A  17     7455  11675   8359    150   -582    835       C  
ATOM     32  C   LYS A  17      28.105  65.698  30.156  1.00 70.52           C  
ANISOU   32  C   LYS A  17     7371  11196   8226    135   -537    705       C  
ATOM     33  O   LYS A  17      28.424  66.047  29.015  1.00 76.20           O  
ANISOU   33  O   LYS A  17     8038  11968   8944    137   -516    697       O  
ATOM     34  CB  LYS A  17      30.012  66.521  31.567  1.00 85.85           C  
ANISOU   34  CB  LYS A  17     9071  13600   9946   -108   -654    887       C  
ATOM     35  CG  LYS A  17      30.753  67.196  30.384  1.00 98.20           C  
ANISOU   35  CG  LYS A  17    10526  15317  11468   -171   -651    910       C  
ATOM     36  CD  LYS A  17      30.845  68.719  30.505  1.00102.74           C  
ANISOU   36  CD  LYS A  17    11145  15922  11971   -477   -702    878       C  
ATOM     37  CE  LYS A  17      29.503  69.349  30.870  1.00101.66           C  
ANISOU   37  CE  LYS A  17    11245  15479  11902   -588   -692    746       C  
ATOM     38  NZ  LYS A  17      29.562  70.841  30.935  1.00 98.77           N  
ANISOU   38  NZ  LYS A  17    10954  15113  11463   -873   -729    711       N  
ATOM     39  N   ALA A  18      26.837  65.630  30.548  1.00 60.43           N  
ANISOU   39  N   ALA A  18     6269   9662   7029    126   -521    610       N  
ATOM     40  CA  ALA A  18      25.812  66.247  29.718  1.00 55.54           C  
ANISOU   40  CA  ALA A  18     5782   8836   6486     71   -489    497       C  
ATOM     41  C   ALA A  18      26.047  67.747  29.709  1.00 53.97           C  
ANISOU   41  C   ALA A  18     5590   8694   6223   -171   -528    483       C  
ATOM     42  O   ALA A  18      26.340  68.352  30.747  1.00 52.94           O  
ANISOU   42  O   ALA A  18     5462   8635   6016   -332   -578    510       O  
ATOM     43  CB  ALA A  18      24.411  65.924  30.226  1.00 52.75           C  
ANISOU   43  CB  ALA A  18     5601   8222   6220     98   -466    412       C  
ATOM     44  N   SER A  19      25.977  68.344  28.535  1.00 44.85           N  
ANISOU   44  N   SER A  19     4441   7513   5087   -203   -506    444       N  
ATOM     45  CA  SER A  19      26.337  69.741  28.426  1.00 45.76           C  
ANISOU   45  CA  SER A  19     4561   7694   5130   -428   -539    441       C  
ATOM     46  C   SER A  19      25.313  70.477  27.577  1.00 46.21           C  
ANISOU   46  C   SER A  19     4759   7543   5258   -471   -502    344       C  
ATOM     47  O   SER A  19      24.666  69.896  26.702  1.00 43.28           O  
ANISOU   47  O   SER A  19     4418   7052   4974   -322   -456    298       O  
ATOM     48  CB  SER A  19      27.731  69.904  27.847  1.00 47.70           C  
ANISOU   48  CB  SER A  19     4622   8216   5287   -458   -562    534       C  
ATOM     49  OG  SER A  19      27.922  71.226  27.394  1.00 54.95           O  
ANISOU   49  OG  SER A  19     5569   9156   6151   -663   -579    515       O  
ATOM     50  N   THR A  20      25.157  71.764  27.875  1.00 47.45           N  
ANISOU   50  N   THR A  20     5009   7653   5366   -678   -522    315       N  
ATOM     51  CA  THR A  20      24.297  72.643  27.098  1.00 45.29           C  
ANISOU   51  CA  THR A  20     4866   7202   5140   -733   -488    238       C  
ATOM     52  C   THR A  20      25.055  73.855  26.572  1.00 45.77           C  
ANISOU   52  C   THR A  20     4907   7371   5114   -919   -509    262       C  
ATOM     53  O   THR A  20      24.437  74.873  26.268  1.00 47.20           O  
ANISOU   53  O   THR A  20     5224   7407   5302  -1020   -489    209       O  
ATOM     54  CB  THR A  20      23.095  73.093  27.928  1.00 44.00           C  
ANISOU   54  CB  THR A  20     4887   6817   5014   -785   -471    168       C  
ATOM     55  OG1 THR A  20      23.542  73.492  29.230  1.00 60.74           O  
ANISOU   55  OG1 THR A  20     7032   9003   7044   -934   -513    196       O  
ATOM     56  CG2 THR A  20      22.099  71.953  28.064  1.00 30.66           C  
ANISOU   56  CG2 THR A  20     3232   4989   3430   -595   -438    131       C  
ATOM     57  N   ASP A  21      26.383  73.780  26.465  1.00 52.80           N  
ANISOU   57  N   ASP A  21     5631   8517   5915   -968   -547    348       N  
ATOM     58  CA  ASP A  21      27.159  74.888  25.926  1.00 66.17           C  
ANISOU   58  CA  ASP A  21     7295  10331   7516  -1157   -568    378       C  
ATOM     59  C   ASP A  21      27.599  74.635  24.489  1.00 66.46           C  
ANISOU   59  C   ASP A  21     7213  10465   7575  -1056   -543    402       C  
ATOM     60  O   ASP A  21      28.483  75.333  23.982  1.00 72.48           O  
ANISOU   60  O   ASP A  21     7898  11389   8251  -1192   -564    450       O  
ATOM     61  CB  ASP A  21      28.369  75.203  26.814  1.00 77.59           C  
ANISOU   61  CB  ASP A  21     8639  12020   8822  -1335   -634    465       C  
ATOM     62  CG  ASP A  21      29.068  73.957  27.340  1.00 98.00           C  
ANISOU   62  CG  ASP A  21    11044  14799  11394  -1188   -657    547       C  
ATOM     63  OD1 ASP A  21      29.187  73.824  28.581  1.00103.73           O  
ANISOU   63  OD1 ASP A  21    11780  15564  12071  -1250   -695    573       O  
ATOM     64  OD2 ASP A  21      29.504  73.117  26.517  1.00106.05           O  
ANISOU   64  OD2 ASP A  21    11918  15929  12445  -1006   -632    590       O  
ATOM     65  N   TYR A  22      26.977  73.667  23.816  1.00 64.69           N  
ANISOU   65  N   TYR A  22     6982  10142   7457   -831   -496    366       N  
ATOM     66  CA  TYR A  22      27.375  73.333  22.453  1.00 67.76           C  
ANISOU   66  CA  TYR A  22     7266  10617   7863   -721   -465    384       C  
ATOM     67  C   TYR A  22      27.018  74.429  21.461  1.00 77.55           C  
ANISOU   67  C   TYR A  22     8593  11767   9107   -831   -448    341       C  
ATOM     68  O   TYR A  22      27.746  74.630  20.483  1.00 76.54           O  
ANISOU   68  O   TYR A  22     8362  11780   8937   -845   -443    380       O  
ATOM     69  CB  TYR A  22      26.709  72.033  22.026  1.00 55.53           C  
ANISOU   69  CB  TYR A  22     5722   8959   6418   -471   -418    347       C  
ATOM     70  CG  TYR A  22      27.273  70.810  22.678  1.00 48.14           C  
ANISOU   70  CG  TYR A  22     4677   8142   5472   -322   -422    407       C  
ATOM     71  CD1 TYR A  22      26.724  70.317  23.856  1.00 44.83           C  
ANISOU   71  CD1 TYR A  22     4328   7621   5083   -290   -434    391       C  
ATOM     72  CD2 TYR A  22      28.347  70.131  22.112  1.00 53.32           C  
ANISOU   72  CD2 TYR A  22     5162   9014   6085   -202   -408    484       C  
ATOM     73  CE1 TYR A  22      27.235  69.179  24.452  1.00 48.05           C  
ANISOU   73  CE1 TYR A  22     4644   8133   5480   -145   -435    452       C  
ATOM     74  CE2 TYR A  22      28.863  68.989  22.706  1.00 58.13           C  
ANISOU   74  CE2 TYR A  22     5677   9728   6682    -44   -403    548       C  
ATOM     75  CZ  TYR A  22      28.301  68.519  23.872  1.00 57.11           C  
ANISOU   75  CZ  TYR A  22     5626   9487   6584    -18   -418    532       C  
ATOM     76  OH  TYR A  22      28.816  67.388  24.463  1.00 71.60           O  
ANISOU   76  OH  TYR A  22     7376  11423   8405    145   -412    602       O  
ATOM     77  N   ALA A  23      25.923  75.155  21.714  1.00 83.64           N  
ANISOU   77  N   ALA A  23     9550  12309   9922   -904   -436    269       N  
ATOM     78  CA  ALA A  23      25.307  76.039  20.727  1.00 84.94           C  
ANISOU   78  CA  ALA A  23     9820  12342  10114   -953   -406    223       C  
ATOM     79  C   ALA A  23      26.293  76.970  20.040  1.00 90.61           C  
ANISOU   79  C   ALA A  23    10478  13215  10737  -1113   -424    272       C  
ATOM     80  O   ALA A  23      25.958  77.554  19.000  1.00 98.04           O  
ANISOU   80  O   ALA A  23    11471  14082  11696  -1128   -397    248       O  
ATOM     81  CB  ALA A  23      24.212  76.871  21.387  1.00 90.60           C  
ANISOU   81  CB  ALA A  23    10741  12828  10856  -1040   -394    162       C  
ATOM     82  N   LYS A  24      27.504  77.116  20.574  1.00 86.33           N  
ANISOU   82  N   LYS A  24     9820  12894  10087  -1237   -469    346       N  
ATOM     83  CA  LYS A  24      28.461  78.037  19.992  1.00 88.41           C  
ANISOU   83  CA  LYS A  24    10025  13318  10247  -1417   -490    399       C  
ATOM     84  C   LYS A  24      29.466  77.355  19.055  1.00 82.25           C  
ANISOU   84  C   LYS A  24     9027  12784   9442  -1313   -485    468       C  
ATOM     85  O   LYS A  24      30.070  78.038  18.221  1.00 81.42           O  
ANISOU   85  O   LYS A  24     8875  12787   9274  -1422   -486    502       O  
ATOM     86  CB  LYS A  24      29.154  78.818  21.123  1.00 94.66           C  
ANISOU   86  CB  LYS A  24    10840  14211  10916  -1664   -545    440       C  
ATOM     87  CG  LYS A  24      30.477  79.500  20.802  1.00102.63           C  
ANISOU   87  CG  LYS A  24    11729  15477  11787  -1867   -585    525       C  
ATOM     88  CD  LYS A  24      31.503  79.245  21.885  1.00103.34           C  
ANISOU   88  CD  LYS A  24    11685  15811  11770  -1971   -646    607       C  
ATOM     89  CE  LYS A  24      32.893  79.669  21.451  1.00102.65           C  
ANISOU   89  CE  LYS A  24    11458  15990  11553  -2100   -662    707       C  
ATOM     90  NZ  LYS A  24      33.902  78.926  22.248  1.00100.39           N  
ANISOU   90  NZ  LYS A  24    11020  15923  11200  -2039   -677    802       N  
ATOM     91  N   ASP A  25      29.621  76.027  19.119  1.00 80.17           N  
ANISOU   91  N   ASP A  25     8640  12596   9224  -1095   -470    489       N  
ATOM     92  CA  ASP A  25      30.291  75.306  18.036  1.00 80.38           C  
ANISOU   92  CA  ASP A  25     8501  12791   9250   -942   -439    534       C  
ATOM     93  C   ASP A  25      29.386  75.109  16.829  1.00 76.79           C  
ANISOU   93  C   ASP A  25     8130  12155   8889   -808   -384    459       C  
ATOM     94  O   ASP A  25      29.876  74.792  15.737  1.00 76.16           O  
ANISOU   94  O   ASP A  25     7946  12192   8798   -718   -353    485       O  
ATOM     95  CB  ASP A  25      30.774  73.941  18.510  1.00 84.13           C  
ANISOU   95  CB  ASP A  25     8837  13396   9733   -742   -432    585       C  
ATOM     96  CG  ASP A  25      31.314  73.985  19.904  1.00 93.79           C  
ANISOU   96  CG  ASP A  25    10011  14739  10885   -847   -488    644       C  
ATOM     97  OD1 ASP A  25      31.042  73.043  20.682  1.00 92.06           O  
ANISOU   97  OD1 ASP A  25     9793  14475  10710   -707   -485    642       O  
ATOM     98  OD2 ASP A  25      31.981  74.990  20.224  1.00 99.48           O  
ANISOU   98  OD2 ASP A  25    10703  15593  11501  -1084   -536    690       O  
ATOM     99  N   ALA A  26      28.080  75.304  17.011  1.00 64.56           N  
ANISOU   99  N   ALA A  26     6765  10339   7428   -795   -370    372       N  
ATOM    100  CA  ALA A  26      27.114  75.222  15.933  1.00 56.48           C  
ANISOU  100  CA  ALA A  26     5830   9143   6487   -693   -325    304       C  
ATOM    101  C   ALA A  26      27.336  76.261  14.839  1.00 59.82           C  
ANISOU  101  C   ALA A  26     6264   9597   6868   -813   -318    313       C  
ATOM    102  O   ALA A  26      26.729  76.139  13.769  1.00 58.32           O  
ANISOU  102  O   ALA A  26     6113   9315   6731   -723   -282    273       O  
ATOM    103  CB  ALA A  26      25.707  75.364  16.514  1.00 52.12           C  
ANISOU  103  CB  ALA A  26     5459   8325   6019   -683   -318    227       C  
ATOM    104  N   GLU A  27      28.166  77.282  15.066  1.00 67.08           N  
ANISOU  104  N   GLU A  27     7157  10641   7687  -1022   -352    366       N  
ATOM    105  CA  GLU A  27      28.382  78.263  14.005  1.00 76.31           C  
ANISOU  105  CA  GLU A  27     8346  11836   8813  -1139   -343    378       C  
ATOM    106  C   GLU A  27      29.246  77.705  12.882  1.00 74.68           C  
ANISOU  106  C   GLU A  27     7963  11837   8574  -1043   -321    427       C  
ATOM    107  O   GLU A  27      29.181  78.212  11.756  1.00 78.33           O  
ANISOU  107  O   GLU A  27     8443  12288   9029  -1070   -299    421       O  
ATOM    108  CB  GLU A  27      28.998  79.546  14.565  1.00 81.93           C  
ANISOU  108  CB  GLU A  27     9104  12609   9416  -1412   -384    419       C  
ATOM    109  CG  GLU A  27      30.233  79.351  15.419  1.00 95.70           C  
ANISOU  109  CG  GLU A  27    10696  14606  11059  -1507   -432    500       C  
ATOM    110  CD  GLU A  27      30.619  80.616  16.171  1.00108.61           C  
ANISOU  110  CD  GLU A  27    12425  16254  12587  -1799   -476    523       C  
ATOM    111  OE1 GLU A  27      31.663  80.611  16.861  1.00113.28           O  
ANISOU  111  OE1 GLU A  27    12894  17071  13076  -1920   -523    597       O  
ATOM    112  OE2 GLU A  27      29.879  81.618  16.067  1.00111.67           O  
ANISOU  112  OE2 GLU A  27    13016  16429  12986  -1908   -461    472       O  
ATOM    113  N   GLY A  28      30.036  76.665  13.160  1.00 72.45           N  
ANISOU  113  N   GLY A  28     7516  11741   8271   -920   -321    476       N  
ATOM    114  CA  GLY A  28      30.764  75.996  12.097  1.00 75.70           C  
ANISOU  114  CA  GLY A  28     7772  12333   8659   -785   -284    517       C  
ATOM    115  C   GLY A  28      29.879  75.118  11.236  1.00 78.65           C  
ANISOU  115  C   GLY A  28     8206  12549   9129   -568   -228    445       C  
ATOM    116  O   GLY A  28      30.180  74.902  10.054  1.00 81.28           O  
ANISOU  116  O   GLY A  28     8475  12961   9447   -491   -190    453       O  
ATOM    117  N   LEU A  29      28.768  74.629  11.800  1.00 69.93           N  
ANISOU  117  N   LEU A  29     7229  11223   8117   -481   -224    373       N  
ATOM    118  CA  LEU A  29      27.850  73.708  11.139  1.00 53.87           C  
ANISOU  118  CA  LEU A  29     5265   9033   6170   -291   -178    303       C  
ATOM    119  C   LEU A  29      26.747  74.442  10.378  1.00 45.70           C  
ANISOU  119  C   LEU A  29     4372   7807   5184   -349   -170    239       C  
ATOM    120  O   LEU A  29      26.471  75.624  10.603  1.00 47.12           O  
ANISOU  120  O   LEU A  29     4634   7918   5350   -517   -197    238       O  
ATOM    121  CB  LEU A  29      27.206  72.764  12.153  1.00 46.94           C  
ANISOU  121  CB  LEU A  29     4447   8029   5360   -175   -179    266       C  
ATOM    122  CG  LEU A  29      28.134  71.996  13.090  1.00 48.47           C  
ANISOU  122  CG  LEU A  29     4519   8383   5513   -104   -189    331       C  
ATOM    123  CD1 LEU A  29      27.329  71.396  14.219  1.00 45.36           C  
ANISOU  123  CD1 LEU A  29     4220   7828   5185    -47   -201    291       C  
ATOM    124  CD2 LEU A  29      28.895  70.920  12.323  1.00 49.15           C  
ANISOU  124  CD2 LEU A  29     4486   8617   5573     90   -136    367       C  
ATOM    125  N   THR A  30      26.084  73.700   9.492  1.00 38.10           N  
ANISOU  125  N   THR A  30     3449   6753   4275   -203   -131    186       N  
ATOM    126  CA  THR A  30      25.031  74.239   8.646  1.00 33.43           C  
ANISOU  126  CA  THR A  30     2972   6005   3726   -232   -121    135       C  
ATOM    127  C   THR A  30      23.794  73.363   8.770  1.00 31.88           C  
ANISOU  127  C   THR A  30     2876   5622   3617   -107   -106     64       C  
ATOM    128  O   THR A  30      23.876  72.136   8.628  1.00 31.16           O  
ANISOU  128  O   THR A  30     2755   5545   3539     44    -77     45       O  
ATOM    129  CB  THR A  30      25.498  74.313   7.184  1.00 41.63           C  
ANISOU  129  CB  THR A  30     3948   7150   4720   -209    -90    149       C  
ATOM    130  OG1 THR A  30      26.574  75.248   7.078  1.00 48.65           O  
ANISOU  130  OG1 THR A  30     4749   8210   5524   -352   -108    218       O  
ATOM    131  CG2 THR A  30      24.379  74.764   6.287  1.00 39.75           C  
ANISOU  131  CG2 THR A  30     3821   6759   4523   -225    -82    101       C  
ATOM    132  N   ALA A  31      22.653  73.990   9.033  1.00 33.04           N  
ANISOU  132  N   ALA A  31     3144   5595   3814   -170   -121     29       N  
ATOM    133  CA  ALA A  31      21.419  73.234   9.178  1.00 41.77           C  
ANISOU  133  CA  ALA A  31     4337   6537   4996    -73   -111    -30       C  
ATOM    134  C   ALA A  31      21.076  72.526   7.869  1.00 47.99           C  
ANISOU  134  C   ALA A  31     5126   7317   5790     28    -79    -65       C  
ATOM    135  O   ALA A  31      21.187  73.122   6.787  1.00 47.27           O  
ANISOU  135  O   ALA A  31     5022   7270   5668    -14    -70    -54       O  
ATOM    136  CB  ALA A  31      20.270  74.157   9.579  1.00 42.97           C  
ANISOU  136  CB  ALA A  31     4606   6528   5192   -156   -126    -48       C  
ATOM    137  N   PRO A  32      20.651  71.267   7.924  1.00 44.97           N  
ANISOU  137  N   PRO A  32     4770   6875   5440    151    -59   -107       N  
ATOM    138  CA  PRO A  32      20.169  70.609   6.707  1.00 46.19           C  
ANISOU  138  CA  PRO A  32     4956   7000   5595    227    -30   -149       C  
ATOM    139  C   PRO A  32      18.893  71.267   6.221  1.00 41.68           C  
ANISOU  139  C   PRO A  32     4465   6314   5059    162    -46   -173       C  
ATOM    140  O   PRO A  32      18.078  71.759   7.007  1.00 44.24           O  
ANISOU  140  O   PRO A  32     4846   6536   5429    111    -69   -174       O  
ATOM    141  CB  PRO A  32      19.913  69.166   7.156  1.00 43.11           C  
ANISOU  141  CB  PRO A  32     4606   6544   5230    351     -9   -189       C  
ATOM    142  CG  PRO A  32      19.611  69.285   8.624  1.00 29.04           C  
ANISOU  142  CG  PRO A  32     2848   4694   3492    318    -39   -179       C  
ATOM    143  CD  PRO A  32      20.493  70.416   9.117  1.00 34.89           C  
ANISOU  143  CD  PRO A  32     3516   5541   4199    215    -64   -120       C  
ATOM    144  N   TYR A  33      18.721  71.270   4.906  1.00 37.07           N  
ANISOU  144  N   TYR A  33     3884   5754   4447    171    -30   -186       N  
ATOM    145  CA  TYR A  33      17.478  71.742   4.322  1.00 29.50           C  
ANISOU  145  CA  TYR A  33     2990   4704   3514    127    -44   -201       C  
ATOM    146  C   TYR A  33      17.158  70.905   3.091  1.00 39.18           C  
ANISOU  146  C   TYR A  33     4237   5938   4712    184    -22   -243       C  
ATOM    147  O   TYR A  33      18.031  70.671   2.245  1.00 34.19           O  
ANISOU  147  O   TYR A  33     3559   5408   4024    217      6   -241       O  
ATOM    148  CB  TYR A  33      17.547  73.233   3.957  1.00 22.57           C  
ANISOU  148  CB  TYR A  33     2104   3854   2619     23    -58   -153       C  
ATOM    149  CG  TYR A  33      16.270  73.686   3.309  1.00 33.70           C  
ANISOU  149  CG  TYR A  33     3572   5183   4049     -1    -67   -156       C  
ATOM    150  CD1 TYR A  33      16.172  73.793   1.921  1.00 31.84           C  
ANISOU  150  CD1 TYR A  33     3325   4999   3773     -5    -59   -154       C  
ATOM    151  CD2 TYR A  33      15.132  73.929   4.069  1.00 29.75           C  
ANISOU  151  CD2 TYR A  33     3133   4567   3605    -11    -83   -156       C  
ATOM    152  CE1 TYR A  33      14.982  74.159   1.317  1.00 33.42           C  
ANISOU  152  CE1 TYR A  33     3568   5144   3987    -23    -71   -147       C  
ATOM    153  CE2 TYR A  33      13.932  74.304   3.462  1.00 39.47           C  
ANISOU  153  CE2 TYR A  33     4401   5747   4850    -20    -90   -146       C  
ATOM    154  CZ  TYR A  33      13.872  74.420   2.086  1.00 41.56           C  
ANISOU  154  CZ  TYR A  33     4648   6071   5072    -28    -87   -139       C  
ATOM    155  OH  TYR A  33      12.694  74.783   1.465  1.00 45.91           O  
ANISOU  155  OH  TYR A  33     5224   6591   5629    -36    -97   -118       O  
ATOM    156  N   VAL A  34      15.906  70.449   3.012  1.00 44.99           N  
ANISOU  156  N   VAL A  34     5042   6573   5480    190    -32   -278       N  
ATOM    157  CA  VAL A  34      15.346  69.748   1.861  1.00 37.33           C  
ANISOU  157  CA  VAL A  34     4112   5595   4478    212    -21   -319       C  
ATOM    158  C   VAL A  34      13.907  70.216   1.702  1.00 35.98           C  
ANISOU  158  C   VAL A  34     3980   5355   4336    152    -53   -311       C  
ATOM    159  O   VAL A  34      13.116  70.143   2.646  1.00 32.42           O  
ANISOU  159  O   VAL A  34     3559   4822   3937    145    -71   -312       O  
ATOM    160  CB  VAL A  34      15.384  68.213   2.022  1.00 40.89           C  
ANISOU  160  CB  VAL A  34     4617   6001   4919    296      6   -377       C  
ATOM    161  CG1 VAL A  34      14.588  67.552   0.917  1.00 31.76           C  
ANISOU  161  CG1 VAL A  34     3528   4816   3724    287     12   -423       C  
ATOM    162  CG2 VAL A  34      16.828  67.682   2.039  1.00 36.51           C  
ANISOU  162  CG2 VAL A  34     4019   5530   4324    384     50   -374       C  
ATOM    163  N   SER A  35      13.559  70.680   0.512  1.00 45.27           N  
ANISOU  163  N   SER A  35     5150   6575   5475    113    -59   -298       N  
ATOM    164  CA  SER A  35      12.201  71.153   0.300  1.00 41.77           C  
ANISOU  164  CA  SER A  35     4728   6090   5052     66    -88   -276       C  
ATOM    165  C   SER A  35      11.251  69.987   0.047  1.00 41.57           C  
ANISOU  165  C   SER A  35     4755   6025   5016     69    -97   -325       C  
ATOM    166  O   SER A  35      11.652  68.830  -0.133  1.00 36.57           O  
ANISOU  166  O   SER A  35     4161   5383   4352    107    -75   -382       O  
ATOM    167  CB  SER A  35      12.149  72.117  -0.869  1.00 39.32           C  
ANISOU  167  CB  SER A  35     4390   5848   4700     22    -94   -233       C  
ATOM    168  OG  SER A  35      13.029  71.651  -1.858  1.00 51.27           O  
ANISOU  168  OG  SER A  35     5891   7440   6151     38    -70   -261       O  
ATOM    169  N   GLN A  36       9.970  70.315   0.007  1.00 34.49           N  
ANISOU  169  N   GLN A  36     3862   5106   4137     28   -126   -297       N  
ATOM    170  CA  GLN A  36       8.929  69.315  -0.133  1.00 28.46           C  
ANISOU  170  CA  GLN A  36     3142   4313   3358      3   -143   -332       C  
ATOM    171  C   GLN A  36       8.631  69.091  -1.602  1.00 36.41           C  
ANISOU  171  C   GLN A  36     4157   5389   4288    -41   -152   -343       C  
ATOM    172  O   GLN A  36       8.564  70.043  -2.388  1.00 45.04           O  
ANISOU  172  O   GLN A  36     5205   6549   5359    -64   -162   -293       O  
ATOM    173  CB  GLN A  36       7.666  69.760   0.608  1.00 22.83           C  
ANISOU  173  CB  GLN A  36     2414   3566   2696    -20   -171   -285       C  
ATOM    174  CG  GLN A  36       7.555  69.140   1.965  1.00 30.81           C  
ANISOU  174  CG  GLN A  36     3455   4492   3759      6   -166   -310       C  
ATOM    175  CD  GLN A  36       6.339  69.547   2.696  1.00 36.21           C  
ANISOU  175  CD  GLN A  36     4121   5151   4487    -11   -185   -263       C  
ATOM    176  OE1 GLN A  36       6.365  70.272   3.695  1.00 50.58           O  
ANISOU  176  OE1 GLN A  36     5928   6929   6359     17   -176   -229       O  
ATOM    177  NE2 GLN A  36       5.232  69.082   2.197  1.00 39.79           N  
ANISOU  177  NE2 GLN A  36     4573   5636   4910    -61   -210   -258       N  
ATOM    178  N   ASP A  37       8.484  67.829  -1.980  1.00 37.11           N  
ANISOU  178  N   ASP A  37     4314   5457   4328    -55   -145   -410       N  
ATOM    179  CA  ASP A  37       8.095  67.509  -3.342  1.00 37.21           C  
ANISOU  179  CA  ASP A  37     4352   5532   4256   -115   -156   -428       C  
ATOM    180  C   ASP A  37       6.601  67.256  -3.361  1.00 38.54           C  
ANISOU  180  C   ASP A  37     4525   5706   4413   -197   -202   -410       C  
ATOM    181  O   ASP A  37       6.153  66.225  -2.829  1.00 42.70           O  
ANISOU  181  O   ASP A  37     5118   6167   4939   -220   -204   -455       O  
ATOM    182  CB  ASP A  37       8.850  66.288  -3.859  1.00 50.21           C  
ANISOU  182  CB  ASP A  37     6090   7152   5836    -89   -114   -514       C  
ATOM    183  CG  ASP A  37       8.737  66.129  -5.370  1.00 56.35           C  
ANISOU  183  CG  ASP A  37     6896   8002   6513   -145   -115   -534       C  
ATOM    184  OD1 ASP A  37       9.657  66.572  -6.084  1.00 59.65           O  
ANISOU  184  OD1 ASP A  37     7285   8481   6899   -109    -88   -528       O  
ATOM    185  OD2 ASP A  37       7.719  65.576  -5.841  1.00 54.44           O  
ANISOU  185  OD2 ASP A  37     6703   7764   6218   -235   -146   -553       O  
ATOM    186  N   PRO A  38       5.792  68.158  -3.927  1.00 41.49           N  
ANISOU  186  N   PRO A  38     4829   6162   4775   -243   -237   -337       N  
ATOM    187  CA  PRO A  38       4.331  67.941  -3.908  1.00 45.96           C  
ANISOU  187  CA  PRO A  38     5377   6761   5325   -321   -283   -303       C  
ATOM    188  C   PRO A  38       3.928  66.570  -4.408  1.00 45.75           C  
ANISOU  188  C   PRO A  38     5440   6727   5217   -407   -294   -376       C  
ATOM    189  O   PRO A  38       3.085  65.906  -3.791  1.00 50.46           O  
ANISOU  189  O   PRO A  38     6061   7292   5819   -459   -315   -385       O  
ATOM    190  CB  PRO A  38       3.789  69.075  -4.798  1.00 43.38           C  
ANISOU  190  CB  PRO A  38     4964   6547   4971   -343   -310   -212       C  
ATOM    191  CG  PRO A  38       5.002  69.799  -5.345  1.00 44.26           C  
ANISOU  191  CG  PRO A  38     5067   6672   5079   -290   -278   -211       C  
ATOM    192  CD  PRO A  38       6.139  69.500  -4.419  1.00 36.79           C  
ANISOU  192  CD  PRO A  38     4161   5629   4187   -218   -236   -266       C  
ATOM    193  N   GLN A  39       4.561  66.105  -5.482  1.00 48.22           N  
ANISOU  193  N   GLN A  39     5814   7058   5448   -427   -275   -433       N  
ATOM    194  CA  GLN A  39       4.291  64.768  -5.993  1.00 50.03           C  
ANISOU  194  CA  GLN A  39     6165   7259   5586   -512   -275   -514       C  
ATOM    195  C   GLN A  39       4.585  63.711  -4.938  1.00 50.27           C  
ANISOU  195  C   GLN A  39     6295   7155   5652   -475   -242   -582       C  
ATOM    196  O   GLN A  39       3.732  62.866  -4.633  1.00 50.42           O  
ANISOU  196  O   GLN A  39     6377   7137   5643   -561   -265   -607       O  
ATOM    197  CB  GLN A  39       5.113  64.534  -7.258  1.00 60.13           C  
ANISOU  197  CB  GLN A  39     7504   8569   6774   -511   -243   -566       C  
ATOM    198  CG  GLN A  39       4.337  63.878  -8.348  1.00 70.41           C  
ANISOU  198  CG  GLN A  39     8873   9926   7952   -650   -274   -596       C  
ATOM    199  CD  GLN A  39       3.900  62.508  -7.928  1.00 76.66           C  
ANISOU  199  CD  GLN A  39     9804  10619   8704   -720   -269   -672       C  
ATOM    200  OE1 GLN A  39       4.736  61.658  -7.630  1.00 82.28           O  
ANISOU  200  OE1 GLN A  39    10637  11214   9413   -652   -209   -753       O  
ATOM    201  NE2 GLN A  39       2.586  62.286  -7.861  1.00 72.95           N  
ANISOU  201  NE2 GLN A  39     9317  10200   8202   -854   -330   -641       N  
ATOM    202  N   GLU A  40       5.782  63.757  -4.352  1.00 50.15           N  
ANISOU  202  N   GLU A  40     6290   7072   5693   -351   -191   -606       N  
ATOM    203  CA  GLU A  40       6.125  62.810  -3.299  1.00 52.25           C  
ANISOU  203  CA  GLU A  40     6644   7215   5995   -298   -158   -659       C  
ATOM    204  C   GLU A  40       5.093  62.837  -2.179  1.00 45.03           C  
ANISOU  204  C   GLU A  40     5694   6270   5144   -340   -197   -620       C  
ATOM    205  O   GLU A  40       4.647  61.790  -1.698  1.00 44.86           O  
ANISOU  205  O   GLU A  40     5769   6169   5106   -385   -196   -664       O  
ATOM    206  CB  GLU A  40       7.513  63.125  -2.753  1.00 62.75           C  
ANISOU  206  CB  GLU A  40     7945   8516   7383   -157   -108   -660       C  
ATOM    207  CG  GLU A  40       8.635  62.656  -3.637  1.00 76.15           C  
ANISOU  207  CG  GLU A  40     9707  10218   9010    -96    -51   -714       C  
ATOM    208  CD  GLU A  40       9.808  62.132  -2.835  1.00 89.94           C  
ANISOU  208  CD  GLU A  40    11487  11895  10790     37      9   -740       C  
ATOM    209  OE1 GLU A  40       9.847  62.374  -1.602  1.00 82.10           O  
ANISOU  209  OE1 GLU A  40    10445  10866   9882     77     -2   -708       O  
ATOM    210  OE2 GLU A  40      10.686  61.472  -3.442  1.00 98.17           O  
ANISOU  210  OE2 GLU A  40    12606  12926  11769    106     69   -790       O  
ATOM    211  N   THR A  41       4.690  64.035  -1.761  1.00 38.17           N  
ANISOU  211  N   THR A  41     4695   5463   4344   -326   -227   -536       N  
ATOM    212  CA  THR A  41       3.761  64.151  -0.644  1.00 43.27           C  
ANISOU  212  CA  THR A  41     5301   6087   5053   -346   -254   -492       C  
ATOM    213  C   THR A  41       2.395  63.572  -0.993  1.00 44.40           C  
ANISOU  213  C   THR A  41     5460   6276   5133   -481   -299   -484       C  
ATOM    214  O   THR A  41       1.757  62.914  -0.162  1.00 39.07           O  
ANISOU  214  O   THR A  41     4820   5551   4474   -523   -310   -493       O  
ATOM    215  CB  THR A  41       3.630  65.618  -0.243  1.00 44.97           C  
ANISOU  215  CB  THR A  41     5389   6356   5340   -294   -265   -402       C  
ATOM    216  OG1 THR A  41       4.933  66.182  -0.030  1.00 55.43           O  
ANISOU  216  OG1 THR A  41     6702   7653   6705   -196   -228   -409       O  
ATOM    217  CG2 THR A  41       2.763  65.781   0.991  1.00 30.87           C  
ANISOU  217  CG2 THR A  41     3565   4543   3620   -294   -280   -358       C  
ATOM    218  N   ALA A  42       1.922  63.809  -2.216  1.00 32.63           N  
ANISOU  218  N   ALA A  42     3940   4892   3565   -561   -329   -463       N  
ATOM    219  CA  ALA A  42       0.590  63.340  -2.572  1.00 32.60           C  
ANISOU  219  CA  ALA A  42     3932   4963   3491   -705   -381   -441       C  
ATOM    220  C   ALA A  42       0.551  61.823  -2.676  1.00 34.78           C  
ANISOU  220  C   ALA A  42     4372   5152   3690   -798   -372   -537       C  
ATOM    221  O   ALA A  42      -0.458  61.199  -2.327  1.00 40.71           O  
ANISOU  221  O   ALA A  42     5145   5913   4412   -911   -405   -531       O  
ATOM    222  CB  ALA A  42       0.135  63.989  -3.878  1.00 34.52           C  
ANISOU  222  CB  ALA A  42     4100   5355   3663   -769   -418   -387       C  
ATOM    223  N   ALA A  43       1.633  61.207  -3.161  1.00 36.25           N  
ANISOU  223  N   ALA A  43     4682   5254   3837   -753   -323   -624       N  
ATOM    224  CA  ALA A  43       1.682  59.750  -3.168  1.00 39.01           C  
ANISOU  224  CA  ALA A  43     5218   5490   4114   -820   -299   -719       C  
ATOM    225  C   ALA A  43       1.703  59.191  -1.752  1.00 43.67           C  
ANISOU  225  C   ALA A  43     5856   5959   4779   -772   -279   -734       C  
ATOM    226  O   ALA A  43       1.095  58.144  -1.488  1.00 47.13           O  
ANISOU  226  O   ALA A  43     6410   6331   5167   -877   -287   -773       O  
ATOM    227  CB  ALA A  43       2.899  59.261  -3.939  1.00 29.13           C  
ANISOU  227  CB  ALA A  43     4090   4171   2807   -748   -236   -802       C  
ATOM    228  N   LEU A  44       2.404  59.862  -0.834  1.00 40.89           N  
ANISOU  228  N   LEU A  44     5422   5575   4538   -625   -254   -702       N  
ATOM    229  CA  LEU A  44       2.425  59.393   0.547  1.00 40.01           C  
ANISOU  229  CA  LEU A  44     5347   5359   4497   -578   -238   -709       C  
ATOM    230  C   LEU A  44       1.025  59.439   1.143  1.00 37.63           C  
ANISOU  230  C   LEU A  44     4982   5107   4207   -690   -291   -653       C  
ATOM    231  O   LEU A  44       0.596  58.494   1.810  1.00 38.18           O  
ANISOU  231  O   LEU A  44     5146   5096   4266   -749   -291   -682       O  
ATOM    232  CB  LEU A  44       3.403  60.226   1.384  1.00 31.02           C  
ANISOU  232  CB  LEU A  44     4120   4201   3465   -416   -208   -676       C  
ATOM    233  CG  LEU A  44       3.201  60.197   2.908  1.00 42.13           C  
ANISOU  233  CG  LEU A  44     5504   5545   4959   -375   -208   -650       C  
ATOM    234  CD1 LEU A  44       3.545  58.797   3.438  1.00 33.94           C  
ANISOU  234  CD1 LEU A  44     4631   4368   3898   -362   -171   -721       C  
ATOM    235  CD2 LEU A  44       4.053  61.248   3.644  1.00 23.86           C  
ANISOU  235  CD2 LEU A  44     3087   3240   2738   -244   -190   -607       C  
ATOM    236  N   VAL A  45       0.278  60.511   0.862  1.00 41.99           N  
ANISOU  236  N   VAL A  45     5380   5799   4776   -721   -335   -568       N  
ATOM    237  CA  VAL A  45      -1.081  60.640   1.379  1.00 45.85           C  
ANISOU  237  CA  VAL A  45     5785   6363   5271   -814   -382   -499       C  
ATOM    238  C   VAL A  45      -1.992  59.594   0.743  1.00 48.60           C  
ANISOU  238  C   VAL A  45     6219   6745   5502  -1003   -418   -528       C  
ATOM    239  O   VAL A  45      -2.823  58.982   1.423  1.00 44.00           O  
ANISOU  239  O   VAL A  45     5658   6151   4909  -1095   -439   -518       O  
ATOM    240  CB  VAL A  45      -1.586  62.084   1.167  1.00 36.49           C  
ANISOU  240  CB  VAL A  45     4418   5322   4125   -775   -408   -392       C  
ATOM    241  CG1 VAL A  45      -3.103  62.137   1.175  1.00 30.25           C  
ANISOU  241  CG1 VAL A  45     3533   4663   3296   -895   -461   -312       C  
ATOM    242  CG2 VAL A  45      -1.010  63.006   2.273  1.00 30.75           C  
ANISOU  242  CG2 VAL A  45     3625   4542   3518   -620   -374   -356       C  
ATOM    243  N   ARG A  46      -1.841  59.363  -0.563  1.00 47.29           N  
ANISOU  243  N   ARG A  46     6109   6620   5237  -1075   -427   -565       N  
ATOM    244  CA  ARG A  46      -2.572  58.286  -1.212  1.00 44.85           C  
ANISOU  244  CA  ARG A  46     5916   6325   4799  -1270   -458   -608       C  
ATOM    245  C   ARG A  46      -2.397  56.988  -0.444  1.00 49.68           C  
ANISOU  245  C   ARG A  46     6713   6765   5399  -1302   -425   -689       C  
ATOM    246  O   ARG A  46      -3.379  56.344  -0.053  1.00 52.80           O  
ANISOU  246  O   ARG A  46     7139   7172   5750  -1448   -459   -678       O  
ATOM    247  CB  ARG A  46      -2.102  58.127  -2.662  1.00 44.90           C  
ANISOU  247  CB  ARG A  46     6001   6356   4702  -1314   -452   -662       C  
ATOM    248  CG  ARG A  46      -3.095  57.400  -3.563  1.00 62.36           C  
ANISOU  248  CG  ARG A  46     8281   8650   6762  -1547   -504   -676       C  
ATOM    249  CD  ARG A  46      -2.866  57.698  -5.049  1.00 77.24           C  
ANISOU  249  CD  ARG A  46    10168  10628   8551  -1591   -515   -689       C  
ATOM    250  NE  ARG A  46      -1.576  57.202  -5.530  1.00 86.27           N  
ANISOU  250  NE  ARG A  46    11480  11628   9669  -1497   -442   -795       N  
ATOM    251  CZ  ARG A  46      -0.598  57.971  -6.009  1.00 85.28           C  
ANISOU  251  CZ  ARG A  46    11299  11518   9585  -1349   -407   -792       C  
ATOM    252  NH1 ARG A  46      -0.746  59.291  -6.092  1.00 76.09           N  
ANISOU  252  NH1 ARG A  46     9930  10490   8489  -1282   -438   -692       N  
ATOM    253  NH2 ARG A  46       0.537  57.414  -6.412  1.00 87.31           N  
ANISOU  253  NH2 ARG A  46    11709  11654   9809  -1265   -335   -886       N  
ATOM    254  N   ALA A  47      -1.144  56.607  -0.186  1.00 50.64           N  
ANISOU  254  N   ALA A  47     6953   6730   5557  -1161   -357   -762       N  
ATOM    255  CA  ALA A  47      -0.887  55.321   0.455  1.00 44.75           C  
ANISOU  255  CA  ALA A  47     6405   5808   4790  -1173   -316   -839       C  
ATOM    256  C   ALA A  47      -1.428  55.312   1.875  1.00 44.88           C  
ANISOU  256  C   ALA A  47     6362   5799   4891  -1164   -330   -790       C  
ATOM    257  O   ALA A  47      -1.961  54.297   2.342  1.00 49.25           O  
ANISOU  257  O   ALA A  47     7042   6272   5400  -1275   -333   -820       O  
ATOM    258  CB  ALA A  47       0.609  55.014   0.441  1.00 45.60           C  
ANISOU  258  CB  ALA A  47     6626   5777   4921   -995   -235   -908       C  
ATOM    259  N   LEU A  48      -1.335  56.454   2.560  1.00 39.96           N  
ANISOU  259  N   LEU A  48     5556   5245   4384  -1043   -337   -715       N  
ATOM    260  CA  LEU A  48      -1.892  56.567   3.898  1.00 39.60           C  
ANISOU  260  CA  LEU A  48     5441   5189   4415  -1031   -348   -663       C  
ATOM    261  C   LEU A  48      -3.407  56.390   3.884  1.00 39.05           C  
ANISOU  261  C   LEU A  48     5314   5236   4288  -1220   -409   -608       C  
ATOM    262  O   LEU A  48      -3.958  55.665   4.719  1.00 52.79           O  
ANISOU  262  O   LEU A  48     7112   6922   6023  -1295   -414   -610       O  
ATOM    263  CB  LEU A  48      -1.491  57.911   4.504  1.00 47.68           C  
ANISOU  263  CB  LEU A  48     6293   6267   5558   -871   -340   -595       C  
ATOM    264  CG  LEU A  48      -0.007  57.995   4.885  1.00 47.60           C  
ANISOU  264  CG  LEU A  48     6331   6143   5610   -694   -283   -639       C  
ATOM    265  CD1 LEU A  48       0.351  59.381   5.444  1.00 45.82           C  
ANISOU  265  CD1 LEU A  48     5946   5976   5487   -566   -279   -572       C  
ATOM    266  CD2 LEU A  48       0.360  56.888   5.877  1.00 46.27           C  
ANISOU  266  CD2 LEU A  48     6306   5819   5456   -665   -247   -690       C  
ATOM    267  N   ASP A  49      -4.098  57.010   2.927  1.00 40.77           N  
ANISOU  267  N   ASP A  49     5416   5623   4453  -1304   -456   -554       N  
ATOM    268  CA  ASP A  49      -5.550  56.856   2.883  1.00 55.74           C  
ANISOU  268  CA  ASP A  49     7235   7660   6283  -1486   -517   -488       C  
ATOM    269  C   ASP A  49      -5.967  55.444   2.493  1.00 59.81           C  
ANISOU  269  C   ASP A  49     7939   8117   6669  -1693   -533   -558       C  
ATOM    270  O   ASP A  49      -7.020  54.972   2.936  1.00 65.45           O  
ANISOU  270  O   ASP A  49     8638   8890   7342  -1845   -570   -521       O  
ATOM    271  CB  ASP A  49      -6.178  57.870   1.929  1.00 51.01           C  
ANISOU  271  CB  ASP A  49     6459   7272   5651  -1519   -564   -400       C  
ATOM    272  CG  ASP A  49      -6.742  59.069   2.659  1.00 61.58           C  
ANISOU  272  CG  ASP A  49     7585   8727   7085  -1415   -572   -281       C  
ATOM    273  OD1 ASP A  49      -7.558  58.878   3.592  1.00 66.14           O  
ANISOU  273  OD1 ASP A  49     8112   9337   7682  -1459   -584   -233       O  
ATOM    274  OD2 ASP A  49      -6.351  60.204   2.315  1.00 68.94           O  
ANISOU  274  OD2 ASP A  49     8412   9713   8069  -1284   -561   -237       O  
ATOM    275  N   ASP A  50      -5.177  54.752   1.671  1.00 58.65           N  
ANISOU  275  N   ASP A  50     7978   7856   6452  -1708   -502   -659       N  
ATOM    276  CA  ASP A  50      -5.501  53.357   1.394  1.00 67.61           C  
ANISOU  276  CA  ASP A  50     9334   8896   7459  -1899   -505   -736       C  
ATOM    277  C   ASP A  50      -5.380  52.520   2.654  1.00 72.93           C  
ANISOU  277  C   ASP A  50    10132   9400   8176  -1876   -469   -769       C  
ATOM    278  O   ASP A  50      -6.184  51.611   2.883  1.00 82.45           O  
ANISOU  278  O   ASP A  50    11441  10585   9301  -2066   -493   -779       O  
ATOM    279  CB  ASP A  50      -4.600  52.805   0.295  1.00 70.27           C  
ANISOU  279  CB  ASP A  50     9863   9126   7710  -1891   -463   -840       C  
ATOM    280  CG  ASP A  50      -4.839  53.483  -1.030  1.00 76.89           C  
ANISOU  280  CG  ASP A  50    10600  10136   8479  -1956   -505   -811       C  
ATOM    281  OD1 ASP A  50      -3.856  53.790  -1.742  1.00 83.32           O  
ANISOU  281  OD1 ASP A  50    11445  10915   9297  -1833   -465   -854       O  
ATOM    282  OD2 ASP A  50      -6.019  53.720  -1.355  1.00 77.60           O  
ANISOU  282  OD2 ASP A  50    10568  10410   8505  -2128   -579   -738       O  
ATOM    283  N   ALA A  51      -4.395  52.833   3.492  1.00 67.41           N  
ANISOU  283  N   ALA A  51     9422   8591   7601  -1654   -414   -778       N  
ATOM    284  CA  ALA A  51      -4.242  52.131   4.756  1.00 62.94           C  
ANISOU  284  CA  ALA A  51     8956   7875   7085  -1612   -380   -797       C  
ATOM    285  C   ALA A  51      -5.349  52.493   5.740  1.00 76.52           C  
ANISOU  285  C   ALA A  51    10516   9705   8852  -1680   -425   -705       C  
ATOM    286  O   ALA A  51      -5.700  51.679   6.604  1.00 88.36           O  
ANISOU  286  O   ALA A  51    12113  11115  10343  -1749   -419   -714       O  
ATOM    287  CB  ALA A  51      -2.870  52.442   5.350  1.00 59.40           C  
ANISOU  287  CB  ALA A  51     8515   7306   6747  -1358   -314   -822       C  
ATOM    288  N   ALA A  52      -5.895  53.705   5.653  1.00 72.20           N  
ANISOU  288  N   ALA A  52     9730   9349   8354  -1651   -465   -610       N  
ATOM    289  CA  ALA A  52      -7.029  54.032   6.508  1.00 63.55           C  
ANISOU  289  CA  ALA A  52     8482   8376   7288  -1715   -502   -516       C  
ATOM    290  C   ALA A  52      -8.279  53.297   6.039  1.00 66.19           C  
ANISOU  290  C   ALA A  52     8843   8817   7490  -1984   -559   -495       C  
ATOM    291  O   ALA A  52      -9.124  52.920   6.855  1.00 67.45           O  
ANISOU  291  O   ALA A  52     8977   9009   7639  -2086   -578   -452       O  
ATOM    292  CB  ALA A  52      -7.252  55.547   6.547  1.00 48.27           C  
ANISOU  292  CB  ALA A  52     6297   6605   5436  -1590   -516   -416       C  
ATOM    293  N   LYS A  53      -8.401  53.068   4.730  1.00 68.98           N  
ANISOU  293  N   LYS A  53     9251   9229   7730  -2113   -588   -526       N  
ATOM    294  CA  LYS A  53      -9.491  52.273   4.160  1.00 80.22           C  
ANISOU  294  CA  LYS A  53    10730  10750   9002  -2397   -646   -518       C  
ATOM    295  C   LYS A  53      -9.192  50.793   4.406  1.00 88.91           C  
ANISOU  295  C   LYS A  53    12127  11626  10029  -2508   -613   -626       C  
ATOM    296  O   LYS A  53      -8.808  50.036   3.511  1.00 81.00           O  
ANISOU  296  O   LYS A  53    11333  10523   8921  -2600   -600   -718       O  
ATOM    297  CB  LYS A  53      -9.655  52.572   2.669  1.00 78.28           C  
ANISOU  297  CB  LYS A  53    10449  10640   8654  -2493   -687   -516       C  
ATOM    298  CG  LYS A  53     -10.492  53.810   2.327  1.00 71.66           C  
ANISOU  298  CG  LYS A  53     9316  10079   7833  -2483   -742   -380       C  
ATOM    299  CD  LYS A  53     -11.901  53.751   2.925  1.00 76.56           C  
ANISOU  299  CD  LYS A  53     9788  10883   8417  -2639   -796   -271       C  
ATOM    300  CE  LYS A  53     -12.677  52.474   2.547  1.00 78.53           C  
ANISOU  300  CE  LYS A  53    10189  11147   8502  -2941   -836   -302       C  
ATOM    301  NZ  LYS A  53     -13.261  52.463   1.164  1.00 74.55           N  
ANISOU  301  NZ  LYS A  53     9652  10799   7873  -3063   -865   -257       N  
ATOM    302  N   LYS A  54      -9.380  50.371   5.654  1.00104.64           N  
ANISOU  302  N   LYS A  54    14150  13534  12074  -2497   -595   -614       N  
ATOM    303  CA  LYS A  54      -9.007  49.028   6.081  1.00117.91           C  
ANISOU  303  CA  LYS A  54    16117  14978  13707  -2560   -552   -707       C  
ATOM    304  C   LYS A  54     -10.150  48.053   5.822  1.00129.76           C  
ANISOU  304  C   LYS A  54    17716  16531  15057  -2863   -596   -696       C  
ATOM    305  O   LYS A  54     -11.282  48.280   6.262  1.00136.62           O  
ANISOU  305  O   LYS A  54    18411  17581  15919  -2971   -643   -593       O  
ATOM    306  CB  LYS A  54      -8.627  49.021   7.565  1.00112.07           C  
ANISOU  306  CB  LYS A  54    15369  14120  13094  -2396   -508   -691       C  
ATOM    307  CG  LYS A  54      -7.626  47.934   7.963  1.00105.91           C  
ANISOU  307  CG  LYS A  54    14875  13055  12311  -2318   -434   -794       C  
ATOM    308  CD  LYS A  54      -8.324  46.626   8.283  1.00104.14           C  
ANISOU  308  CD  LYS A  54    14862  12733  11975  -2551   -442   -823       C  
ATOM    309  CE  LYS A  54      -7.338  45.481   8.408  1.00103.15           C  
ANISOU  309  CE  LYS A  54    15047  12322  11824  -2466   -359   -920       C  
ATOM    310  NZ  LYS A  54      -8.019  44.167   8.218  1.00102.50           N  
ANISOU  310  NZ  LYS A  54    15146  12178  11623  -2637   -341   -912       N  
ATOM    311  N   GLY A  55      -9.843  46.968   5.117  1.00127.28           N  
ANISOU  311  N   GLY A  55    17653  16064  14644  -2920   -550   -768       N  
ATOM    312  CA  GLY A  55     -10.819  45.939   4.814  1.00120.84           C  
ANISOU  312  CA  GLY A  55    16941  15275  13698  -3137   -556   -735       C  
ATOM    313  C   GLY A  55     -10.419  45.123   3.602  1.00117.17           C  
ANISOU  313  C   GLY A  55    16704  14697  13116  -3194   -514   -809       C  
ATOM    314  O   GLY A  55     -10.845  43.982   3.442  1.00117.41           O  
ANISOU  314  O   GLY A  55    16923  14648  13038  -3341   -489   -816       O  
ATOM    315  N   PHE A  61      -0.039  46.766   6.659  1.00115.84           N  
ANISOU  315  N   PHE A  61    16839  13474  13699  -1171     -8  -1157       N  
ATOM    316  CA  PHE A  61      -0.048  47.741   7.742  1.00110.51           C  
ANISOU  316  CA  PHE A  61    15918  12906  13166  -1066    -42  -1072       C  
ATOM    317  C   PHE A  61      -1.348  48.539   7.755  1.00104.29           C  
ANISOU  317  C   PHE A  61    14922  12312  12391  -1241   -133  -1004       C  
ATOM    318  O   PHE A  61      -1.992  48.713   6.723  1.00101.17           O  
ANISOU  318  O   PHE A  61    14501  12023  11917  -1394   -175  -1010       O  
ATOM    319  CB  PHE A  61       1.153  48.686   7.631  1.00112.22           C  
ANISOU  319  CB  PHE A  61    15985  13181  13472   -831    -12  -1054       C  
ATOM    320  CG  PHE A  61       1.069  49.658   6.478  1.00112.15           C  
ANISOU  320  CG  PHE A  61    15827  13335  13448   -862    -48  -1044       C  
ATOM    321  CD1 PHE A  61       0.623  50.959   6.676  1.00107.18           C  
ANISOU  321  CD1 PHE A  61    14937  12885  12901   -865   -108   -967       C  
ATOM    322  CD2 PHE A  61       1.456  49.275   5.201  1.00113.09           C  
ANISOU  322  CD2 PHE A  61    16077  13423  13468   -881    -15  -1111       C  
ATOM    323  CE1 PHE A  61       0.553  51.854   5.624  1.00103.47           C  
ANISOU  323  CE1 PHE A  61    14339  12559  12416   -887   -139   -951       C  
ATOM    324  CE2 PHE A  61       1.390  50.167   4.144  1.00110.82           C  
ANISOU  324  CE2 PHE A  61    15654  13287  13164   -910    -49  -1098       C  
ATOM    325  CZ  PHE A  61       0.933  51.456   4.357  1.00106.73           C  
ANISOU  325  CZ  PHE A  61    14874  12947  12731   -914   -112  -1015       C  
ATOM    326  N   SER A  62      -1.724  49.030   8.934  1.00101.34           N  
ANISOU  326  N   SER A  62    14398  11993  12113  -1210   -160   -934       N  
ATOM    327  CA  SER A  62      -2.978  49.746   9.116  1.00 95.98           C  
ANISOU  327  CA  SER A  62    13523  11497  11450  -1350   -234   -858       C  
ATOM    328  C   SER A  62      -2.726  51.039   9.875  1.00 92.54           C  
ANISOU  328  C   SER A  62    12847  11165  11148  -1188   -243   -784       C  
ATOM    329  O   SER A  62      -2.080  51.029  10.929  1.00 98.29           O  
ANISOU  329  O   SER A  62    13581  11807  11956  -1045   -209   -777       O  
ATOM    330  CB  SER A  62      -3.997  48.885   9.867  1.00 95.48           C  
ANISOU  330  CB  SER A  62    13545  11392  11340  -1527   -256   -843       C  
ATOM    331  OG  SER A  62      -5.291  49.446   9.766  1.00 99.27           O  
ANISOU  331  OG  SER A  62    13847  12070  11801  -1691   -327   -770       O  
ATOM    332  N   VAL A  63      -3.245  52.145   9.348  1.00 79.87           N  
ANISOU  332  N   VAL A  63    11043   9743   9562  -1214   -288   -728       N  
ATOM    333  CA  VAL A  63      -3.119  53.447   9.987  1.00 69.50           C  
ANISOU  333  CA  VAL A  63     9517   8529   8363  -1078   -295   -656       C  
ATOM    334  C   VAL A  63      -4.512  53.958  10.337  1.00 66.72           C  
ANISOU  334  C   VAL A  63     9005   8334   8013  -1195   -346   -570       C  
ATOM    335  O   VAL A  63      -5.522  53.501   9.799  1.00 70.61           O  
ANISOU  335  O   VAL A  63     9511   8903   8414  -1384   -386   -558       O  
ATOM    336  CB  VAL A  63      -2.374  54.459   9.089  1.00 66.16           C  
ANISOU  336  CB  VAL A  63     8995   8177   7966   -964   -289   -655       C  
ATOM    337  CG1 VAL A  63      -3.308  55.025   8.019  1.00 63.84           C  
ANISOU  337  CG1 VAL A  63     8588   8055   7613  -1090   -341   -613       C  
ATOM    338  CG2 VAL A  63      -1.743  55.582   9.930  1.00 57.61           C  
ANISOU  338  CG2 VAL A  63     7771   7116   7001   -786   -271   -608       C  
ATOM    339  N   LYS A  64      -4.560  54.917  11.259  1.00 64.96           N  
ANISOU  339  N   LYS A  64     8629   8165   7888  -1083   -342   -506       N  
ATOM    340  CA  LYS A  64      -5.789  55.632  11.571  1.00 63.78           C  
ANISOU  340  CA  LYS A  64     8303   8181   7750  -1145   -377   -411       C  
ATOM    341  C   LYS A  64      -5.562  57.127  11.368  1.00 56.53           C  
ANISOU  341  C   LYS A  64     7213   7366   6901  -1008   -373   -355       C  
ATOM    342  O   LYS A  64      -4.540  57.677  11.791  1.00 55.14           O  
ANISOU  342  O   LYS A  64     7035   7115   6801   -849   -338   -372       O  
ATOM    343  CB  LYS A  64      -6.268  55.337  13.001  1.00 63.71           C  
ANISOU  343  CB  LYS A  64     8289   8137   7782  -1151   -367   -378       C  
ATOM    344  CG  LYS A  64      -7.563  56.061  13.397  1.00 82.73           C  
ANISOU  344  CG  LYS A  64    10509  10725  10200  -1201   -392   -272       C  
ATOM    345  CD  LYS A  64      -7.337  57.429  14.089  1.00 92.16           C  
ANISOU  345  CD  LYS A  64    11558  11962  11497  -1019   -364   -214       C  
ATOM    346  CE  LYS A  64      -6.847  57.290  15.536  1.00 88.92           C  
ANISOU  346  CE  LYS A  64    11199  11428  11158   -923   -326   -229       C  
ATOM    347  NZ  LYS A  64      -7.985  57.178  16.492  1.00 83.66           N  
ANISOU  347  NZ  LYS A  64    10463  10836  10489   -990   -329   -161       N  
ATOM    348  N   LYS A  65      -6.528  57.775  10.739  1.00 50.65           N  
ANISOU  348  N   LYS A  65     6326   6795   6123  -1074   -408   -281       N  
ATOM    349  CA  LYS A  65      -6.438  59.166  10.339  1.00 48.45           C  
ANISOU  349  CA  LYS A  65     5900   6619   5890   -961   -405   -222       C  
ATOM    350  C   LYS A  65      -7.389  60.001  11.186  1.00 52.53           C  
ANISOU  350  C   LYS A  65     6261   7246   6452   -920   -401   -118       C  
ATOM    351  O   LYS A  65      -8.517  59.580  11.459  1.00 59.04           O  
ANISOU  351  O   LYS A  65     7037   8165   7233  -1036   -425    -67       O  
ATOM    352  CB  LYS A  65      -6.792  59.300   8.856  1.00 44.28           C  
ANISOU  352  CB  LYS A  65     5333   6214   5280  -1052   -444   -208       C  
ATOM    353  CG  LYS A  65      -6.885  60.697   8.333  1.00 50.29           C  
ANISOU  353  CG  LYS A  65     5941   7097   6072   -954   -444   -132       C  
ATOM    354  CD  LYS A  65      -7.616  60.626   6.994  1.00 65.68           C  
ANISOU  354  CD  LYS A  65     7837   9202   7919  -1089   -495    -98       C  
ATOM    355  CE  LYS A  65      -7.146  61.686   6.014  1.00 71.20           C  
ANISOU  355  CE  LYS A  65     8466   9960   8626   -998   -493    -73       C  
ATOM    356  NZ  LYS A  65      -8.149  61.911   4.936  1.00 74.73           N  
ANISOU  356  NZ  LYS A  65     8803  10607   8983  -1109   -544      4       N  
ATOM    357  N   THR A  66      -6.935  61.174  11.622  1.00 46.08           N  
ANISOU  357  N   THR A  66     5373   6419   5717   -757   -366    -85       N  
ATOM    358  CA  THR A  66      -7.820  62.092  12.330  1.00 41.16           C  
ANISOU  358  CA  THR A  66     4611   5897   5130   -695   -350     16       C  
ATOM    359  C   THR A  66      -7.598  63.497  11.793  1.00 46.11           C  
ANISOU  359  C   THR A  66     5147   6583   5789   -571   -332     69       C  
ATOM    360  O   THR A  66      -6.456  63.932  11.614  1.00 56.58           O  
ANISOU  360  O   THR A  66     6532   7812   7155   -481   -311     18       O  
ATOM    361  CB  THR A  66      -7.611  62.038  13.861  1.00 40.50           C  
ANISOU  361  CB  THR A  66     4565   5709   5114   -622   -310      6       C  
ATOM    362  OG1 THR A  66      -7.476  60.677  14.293  1.00 46.59           O  
ANISOU  362  OG1 THR A  66     5459   6383   5858   -722   -322    -61       O  
ATOM    363  CG2 THR A  66      -8.787  62.667  14.618  1.00 28.60           C  
ANISOU  363  CG2 THR A  66     2927   4319   3620   -593   -292    111       C  
ATOM    364  N   ARG A  67      -8.696  64.176  11.494  1.00 42.10           N  
ANISOU  364  N   ARG A  67     4498   6242   5257   -570   -339    176       N  
ATOM    365  CA  ARG A  67      -8.675  65.518  10.939  1.00 40.21           C  
ANISOU  365  CA  ARG A  67     4173   6070   5037   -453   -320    244       C  
ATOM    366  C   ARG A  67      -8.986  66.522  12.043  1.00 43.28           C  
ANISOU  366  C   ARG A  67     4508   6448   5489   -311   -261    313       C  
ATOM    367  O   ARG A  67      -9.829  66.275  12.912  1.00 38.11           O  
ANISOU  367  O   ARG A  67     3806   5841   4834   -325   -248    359       O  
ATOM    368  CB  ARG A  67      -9.687  65.630   9.794  1.00 30.67           C  
ANISOU  368  CB  ARG A  67     2843   5061   3748   -534   -363    329       C  
ATOM    369  CG  ARG A  67      -9.728  66.966   9.081  1.00 37.31           C  
ANISOU  369  CG  ARG A  67     3598   5983   4598   -417   -346    410       C  
ATOM    370  CD  ARG A  67     -10.506  66.837   7.773  1.00 54.51           C  
ANISOU  370  CD  ARG A  67     5677   8352   6682   -523   -402    474       C  
ATOM    371  NE  ARG A  67      -9.643  66.456   6.655  1.00 59.91           N  
ANISOU  371  NE  ARG A  67     6448   8986   7329   -593   -436    389       N  
ATOM    372  CZ  ARG A  67     -10.056  65.839   5.549  1.00 61.25           C  
ANISOU  372  CZ  ARG A  67     6597   9274   7402   -742   -495    390       C  
ATOM    373  NH1 ARG A  67     -11.334  65.518   5.389  1.00 66.45           N  
ANISOU  373  NH1 ARG A  67     7141  10120   7988   -853   -535    478       N  
ATOM    374  NH2 ARG A  67      -9.185  65.546   4.591  1.00 57.27           N  
ANISOU  374  NH2 ARG A  67     6186   8707   6866   -787   -513    306       N  
ATOM    375  N   TYR A  68      -8.278  67.642  12.025  1.00 42.89           N  
ANISOU  375  N   TYR A  68     4478   6332   5487   -178   -221    317       N  
ATOM    376  CA  TYR A  68      -8.481  68.688  13.007  1.00 38.18           C  
ANISOU  376  CA  TYR A  68     3861   5703   4941    -38   -157    375       C  
ATOM    377  C   TYR A  68      -8.514  70.026  12.298  1.00 35.63           C  
ANISOU  377  C   TYR A  68     3490   5428   4619     71   -129    449       C  
ATOM    378  O   TYR A  68      -7.836  70.222  11.288  1.00 42.18           O  
ANISOU  378  O   TYR A  68     4345   6246   5435     57   -152    419       O  
ATOM    379  CB  TYR A  68      -7.361  68.720  14.055  1.00 31.82           C  
ANISOU  379  CB  TYR A  68     3180   4713   4197     15   -123    289       C  
ATOM    380  CG  TYR A  68      -7.152  67.440  14.816  1.00 32.29           C  
ANISOU  380  CG  TYR A  68     3307   4701   4261    -73   -144    214       C  
ATOM    381  CD1 TYR A  68      -7.762  67.241  16.057  1.00 34.85           C  
ANISOU  381  CD1 TYR A  68     3622   5018   4603    -61   -116    239       C  
ATOM    382  CD2 TYR A  68      -6.322  66.440  14.323  1.00 30.60           C  
ANISOU  382  CD2 TYR A  68     3175   4422   4031   -159   -184    121       C  
ATOM    383  CE1 TYR A  68      -7.555  66.077  16.777  1.00 42.83           C  
ANISOU  383  CE1 TYR A  68     4702   5955   5615   -139   -133    175       C  
ATOM    384  CE2 TYR A  68      -6.115  65.259  15.033  1.00 34.50           C  
ANISOU  384  CE2 TYR A  68     3747   4837   4525   -227   -196     57       C  
ATOM    385  CZ  TYR A  68      -6.733  65.090  16.267  1.00 44.41           C  
ANISOU  385  CZ  TYR A  68     4990   6084   5799   -220   -173     86       C  
ATOM    386  OH  TYR A  68      -6.549  63.934  17.002  1.00 49.97           O  
ANISOU  386  OH  TYR A  68     5777   6708   6503   -286   -183     30       O  
ATOM    387  N   ALA A  69      -9.289  70.954  12.845  1.00 41.94           N  
ANISOU  387  N   ALA A  69     4228   6275   5431    188    -73    547       N  
ATOM    388  CA  ALA A  69      -9.147  72.333  12.406  1.00 50.02           C  
ANISOU  388  CA  ALA A  69     5250   7292   6464    318    -28    610       C  
ATOM    389  C   ALA A  69      -7.965  72.979  13.118  1.00 45.12           C  
ANISOU  389  C   ALA A  69     4771   6476   5898    389     19    537       C  
ATOM    390  O   ALA A  69      -7.510  72.517  14.160  1.00 51.49           O  
ANISOU  390  O   ALA A  69     5651   7176   6736    369     30    467       O  
ATOM    391  CB  ALA A  69     -10.420  73.134  12.669  1.00 44.06           C  
ANISOU  391  CB  ALA A  69     4389   6659   5694    435     26    751       C  
ATOM    392  N   VAL A  70      -7.440  74.030  12.519  1.00 48.48           N  
ANISOU  392  N   VAL A  70     5235   6860   6326    461     44    557       N  
ATOM    393  CA  VAL A  70      -6.408  74.848  13.137  1.00 44.01           C  
ANISOU  393  CA  VAL A  70     4800   6126   5797    523     92    508       C  
ATOM    394  C   VAL A  70      -7.103  76.146  13.513  1.00 48.69           C  
ANISOU  394  C   VAL A  70     5399   6712   6388    673    176    610       C  
ATOM    395  O   VAL A  70      -7.371  76.987  12.648  1.00 42.55           O  
ANISOU  395  O   VAL A  70     4594   5986   5588    740    193    688       O  
ATOM    396  CB  VAL A  70      -5.214  75.084  12.206  1.00 47.24           C  
ANISOU  396  CB  VAL A  70     5267   6483   6201    482     63    451       C  
ATOM    397  CG1 VAL A  70      -4.108  75.817  12.943  1.00 52.23           C  
ANISOU  397  CG1 VAL A  70     6032   6953   6861    516    105    397       C  
ATOM    398  CG2 VAL A  70      -4.701  73.751  11.634  1.00 35.55           C  
ANISOU  398  CG2 VAL A  70     3767   5032   4706    351    -13    365       C  
ATOM    399  N   ALA A  71      -7.413  76.300  14.807  1.00 57.17           N  
ANISOU  399  N   ALA A  71     6517   7721   7483    731    233    614       N  
ATOM    400  CA  ALA A  71      -8.349  77.337  15.234  1.00 55.92           C  
ANISOU  400  CA  ALA A  71     6352   7580   7316    885    321    723       C  
ATOM    401  C   ALA A  71      -7.863  78.737  14.879  1.00 53.86           C  
ANISOU  401  C   ALA A  71     6198   7217   7048    983    381    753       C  
ATOM    402  O   ALA A  71      -8.678  79.634  14.634  1.00 64.40           O  
ANISOU  402  O   ALA A  71     7507   8601   8361   1118    444    867       O  
ATOM    403  CB  ALA A  71      -8.596  77.233  16.739  1.00 50.31           C  
ANISOU  403  CB  ALA A  71     5695   6795   6624    922    376    703       C  
ATOM    404  N   SER A  72      -6.552  78.955  14.853  1.00 44.62           N  
ANISOU  404  N   SER A  72     5152   5911   5892    920    365    660       N  
ATOM    405  CA  SER A  72      -6.019  80.286  14.613  1.00 55.97           C  
ANISOU  405  CA  SER A  72     6715   7236   7316    991    422    682       C  
ATOM    406  C   SER A  72      -5.530  80.472  13.172  1.00 59.86           C  
ANISOU  406  C   SER A  72     7175   7778   7790    947    372    692       C  
ATOM    407  O   SER A  72      -4.784  81.419  12.887  1.00 56.79           O  
ANISOU  407  O   SER A  72     6901   7286   7389    961    401    686       O  
ATOM    408  CB  SER A  72      -4.908  80.579  15.623  1.00 51.56           C  
ANISOU  408  CB  SER A  72     6323   6498   6771    946    447    585       C  
ATOM    409  OG  SER A  72      -4.196  79.394  15.923  1.00 55.28           O  
ANISOU  409  OG  SER A  72     6765   6974   7264    815    372    484       O  
ATOM    410  N   SER A  73      -5.951  79.601  12.252  1.00 55.10           N  
ANISOU  410  N   SER A  73     6426   7333   7177    886    299    709       N  
ATOM    411  CA  SER A  73      -5.522  79.697  10.863  1.00 61.24           C  
ANISOU  411  CA  SER A  73     7169   8170   7930    838    250    716       C  
ATOM    412  C   SER A  73      -6.453  80.629  10.100  1.00 60.98           C  
ANISOU  412  C   SER A  73     7081   8225   7864    960    290    855       C  
ATOM    413  O   SER A  73      -7.639  80.302   9.928  1.00 64.59           O  
ANISOU  413  O   SER A  73     7402   8835   8303   1002    283    942       O  
ATOM    414  CB  SER A  73      -5.497  78.322  10.213  1.00 61.80           C  
ANISOU  414  CB  SER A  73     7130   8360   7993    708    156    663       C  
ATOM    415  OG  SER A  73      -5.467  78.438   8.800  1.00 64.01           O  
ANISOU  415  OG  SER A  73     7350   8736   8236    680    115    700       O  
ATOM    416  N   PRO A  74      -5.976  81.776   9.611  1.00 57.86           N  
ANISOU  416  N   PRO A  74     6783   7748   7455   1018    331    888       N  
ATOM    417  CA  PRO A  74      -6.881  82.705   8.905  1.00 58.25           C  
ANISOU  417  CA  PRO A  74     6788   7876   7469   1154    377   1034       C  
ATOM    418  C   PRO A  74      -7.444  82.161   7.586  1.00 61.75           C  
ANISOU  418  C   PRO A  74     7060   8526   7876   1110    302   1095       C  
ATOM    419  O   PRO A  74      -8.423  82.718   7.079  1.00 68.95           O  
ANISOU  419  O   PRO A  74     7891   9552   8755   1225    331   1232       O  
ATOM    420  CB  PRO A  74      -6.010  83.957   8.683  1.00 43.18           C  
ANISOU  420  CB  PRO A  74     5050   5805   5549   1193    430   1032       C  
ATOM    421  CG  PRO A  74      -4.589  83.497   8.808  1.00 36.57           C  
ANISOU  421  CG  PRO A  74     4294   4871   4732   1036    378    889       C  
ATOM    422  CD  PRO A  74      -4.599  82.294   9.733  1.00 45.00           C  
ANISOU  422  CD  PRO A  74     5310   5954   5833    960    340    802       C  
ATOM    423  N   THR A  75      -6.875  81.098   7.016  1.00 59.61           N  
ANISOU  423  N   THR A  75     6735   8312   7603    951    209   1003       N  
ATOM    424  CA  THR A  75      -7.457  80.433   5.853  1.00 49.63           C  
ANISOU  424  CA  THR A  75     5317   7247   6294    885    134   1048       C  
ATOM    425  C   THR A  75      -8.258  79.177   6.221  1.00 52.34           C  
ANISOU  425  C   THR A  75     5538   7717   6632    807     85   1035       C  
ATOM    426  O   THR A  75      -8.661  78.423   5.324  1.00 42.21           O  
ANISOU  426  O   THR A  75     4142   6593   5304    710     12   1050       O  
ATOM    427  CB  THR A  75      -6.366  80.067   4.842  1.00 40.96           C  
ANISOU  427  CB  THR A  75     4248   6136   5179    757     69    961       C  
ATOM    428  OG1 THR A  75      -5.588  78.968   5.339  1.00 52.10           O  
ANISOU  428  OG1 THR A  75     5696   7482   6618    633     26    820       O  
ATOM    429  CG2 THR A  75      -5.449  81.245   4.582  1.00 36.74           C  
ANISOU  429  CG2 THR A  75     3844   5466   4649    807    115    961       C  
ATOM    430  N   GLY A  76      -8.501  78.935   7.507  1.00 47.95           N  
ANISOU  430  N   GLY A  76     5010   7096   6113    836    123   1009       N  
ATOM    431  CA  GLY A  76      -9.209  77.727   7.898  1.00 41.88           C  
ANISOU  431  CA  GLY A  76     4138   6437   5337    749     77    993       C  
ATOM    432  C   GLY A  76      -8.509  76.441   7.512  1.00 39.03           C  
ANISOU  432  C   GLY A  76     3786   6073   4969    569     -9    867       C  
ATOM    433  O   GLY A  76      -9.170  75.466   7.129  1.00 38.84           O  
ANISOU  433  O   GLY A  76     3661   6192   4906    465    -69    876       O  
ATOM    434  N   ALA A  77      -7.180  76.418   7.594  1.00 36.04           N  
ANISOU  434  N   ALA A  77     3533   5537   4621    528    -12    753       N  
ATOM    435  CA  ALA A  77      -6.436  75.192   7.336  1.00 36.85           C  
ANISOU  435  CA  ALA A  77     3662   5619   4719    382    -78    632       C  
ATOM    436  C   ALA A  77      -6.894  74.084   8.270  1.00 42.90           C  
ANISOU  436  C   ALA A  77     4409   6393   5498    318    -94    590       C  
ATOM    437  O   ALA A  77      -7.173  74.321   9.450  1.00 46.14           O  
ANISOU  437  O   ALA A  77     4843   6741   5945    386    -45    604       O  
ATOM    438  CB  ALA A  77      -4.930  75.420   7.524  1.00 37.87           C  
ANISOU  438  CB  ALA A  77     3921   5583   4883    373    -65    529       C  
ATOM    439  N   GLU A  78      -6.984  72.873   7.725  1.00 44.93           N  
ANISOU  439  N   GLU A  78     4633   6720   5717    183   -161    540       N  
ATOM    440  CA  GLU A  78      -7.139  71.660   8.506  1.00 44.05           C  
ANISOU  440  CA  GLU A  78     4540   6585   5613     96   -183    474       C  
ATOM    441  C   GLU A  78      -5.877  70.818   8.356  1.00 43.57           C  
ANISOU  441  C   GLU A  78     4588   6408   5560     17   -210    341       C  
ATOM    442  O   GLU A  78      -5.107  70.976   7.400  1.00 41.74           O  
ANISOU  442  O   GLU A  78     4386   6165   5309      1   -226    307       O  
ATOM    443  CB  GLU A  78      -8.370  70.863   8.062  1.00 53.39           C  
ANISOU  443  CB  GLU A  78     5612   7944   6732     -7   -232    531       C  
ATOM    444  CG  GLU A  78      -9.703  71.586   8.229  1.00 63.61           C  
ANISOU  444  CG  GLU A  78     6772   9388   8008     75   -205    678       C  
ATOM    445  CD  GLU A  78     -10.797  71.022   7.331  1.00 73.04           C  
ANISOU  445  CD  GLU A  78     7834  10802   9117    -38   -267    753       C  
ATOM    446  OE1 GLU A  78     -10.499  70.633   6.180  1.00 80.51           O  
ANISOU  446  OE1 GLU A  78     8786  11794  10010   -139   -322    719       O  
ATOM    447  OE2 GLU A  78     -11.958  70.960   7.778  1.00 75.16           O  
ANISOU  447  OE2 GLU A  78     7990  11205   9363    -32   -261    849       O  
ATOM    448  N   VAL A  79      -5.650  69.929   9.322  1.00 34.76           N  
ANISOU  448  N   VAL A  79     3531   5208   4470    -24   -210    270       N  
ATOM    449  CA  VAL A  79      -4.531  69.000   9.256  1.00 34.46           C  
ANISOU  449  CA  VAL A  79     3593   5066   4433    -86   -231    153       C  
ATOM    450  C   VAL A  79      -5.019  67.600   9.593  1.00 37.22           C  
ANISOU  450  C   VAL A  79     3962   5424   4756   -195   -262    112       C  
ATOM    451  O   VAL A  79      -5.960  67.410  10.372  1.00 42.58           O  
ANISOU  451  O   VAL A  79     4596   6143   5439   -207   -256    158       O  
ATOM    452  CB  VAL A  79      -3.349  69.399  10.176  1.00 39.76           C  
ANISOU  452  CB  VAL A  79     4352   5589   5166     -9   -191     98       C  
ATOM    453  CG1 VAL A  79      -2.900  70.822   9.884  1.00 31.64           C  
ANISOU  453  CG1 VAL A  79     3321   4546   4155     81   -158    141       C  
ATOM    454  CG2 VAL A  79      -3.714  69.239  11.662  1.00 39.37           C  
ANISOU  454  CG2 VAL A  79     4319   5481   5157     20   -163    102       C  
ATOM    455  N   ASP A  80      -4.366  66.613   8.989  1.00 36.66           N  
ANISOU  455  N   ASP A  80     3967   5312   4650   -275   -290     26       N  
ATOM    456  CA  ASP A  80      -4.700  65.210   9.175  1.00 41.43           C  
ANISOU  456  CA  ASP A  80     4627   5899   5216   -391   -318    -24       C  
ATOM    457  C   ASP A  80      -3.552  64.533   9.895  1.00 43.23           C  
ANISOU  457  C   ASP A  80     4977   5969   5481   -361   -296   -119       C  
ATOM    458  O   ASP A  80      -2.411  64.565   9.422  1.00 43.42           O  
ANISOU  458  O   ASP A  80     5058   5931   5508   -321   -286   -175       O  
ATOM    459  CB  ASP A  80      -4.985  64.531   7.840  1.00 40.66           C  
ANISOU  459  CB  ASP A  80     4537   5881   5029   -514   -363    -44       C  
ATOM    460  CG  ASP A  80      -6.275  64.997   7.239  1.00 50.03           C  
ANISOU  460  CG  ASP A  80     5592   7250   6168   -565   -393     60       C  
ATOM    461  OD1 ASP A  80      -7.031  65.698   7.931  1.00 59.48           O  
ANISOU  461  OD1 ASP A  80     6694   8509   7399   -502   -374    148       O  
ATOM    462  OD2 ASP A  80      -6.528  64.705   6.065  1.00 59.63           O  
ANISOU  462  OD2 ASP A  80     6795   8555   7305   -661   -432     61       O  
ATOM    463  N   SER A  81      -3.859  63.948  11.046  1.00 36.98           N  
ANISOU  463  N   SER A  81     4216   5122   4712   -374   -287   -127       N  
ATOM    464  CA  SER A  81      -2.897  63.222  11.851  1.00 31.14           C  
ANISOU  464  CA  SER A  81     3587   4241   4003   -345   -267   -202       C  
ATOM    465  C   SER A  81      -3.006  61.742  11.541  1.00 33.68           C  
ANISOU  465  C   SER A  81     4009   4521   4264   -457   -289   -264       C  
ATOM    466  O   SER A  81      -4.110  61.185  11.506  1.00 30.18           O  
ANISOU  466  O   SER A  81     3550   4141   3777   -569   -314   -237       O  
ATOM    467  CB  SER A  81      -3.149  63.458  13.338  1.00 33.90           C  
ANISOU  467  CB  SER A  81     3923   4547   4409   -294   -241   -174       C  
ATOM    468  OG  SER A  81      -2.501  62.466  14.108  1.00 44.66           O  
ANISOU  468  OG  SER A  81     5392   5794   5784   -296   -233   -238       O  
ATOM    469  N   TRP A  82      -1.864  61.107  11.343  1.00 32.56           N  
ANISOU  469  N   TRP A  82     3977   4277   4117   -426   -274   -341       N  
ATOM    470  CA  TRP A  82      -1.797  59.681  11.065  1.00 34.36           C  
ANISOU  470  CA  TRP A  82     4339   4432   4284   -512   -279   -408       C  
ATOM    471  C   TRP A  82      -1.161  58.969  12.256  1.00 38.61           C  
ANISOU  471  C   TRP A  82     4974   4838   4860   -455   -251   -445       C  
ATOM    472  O   TRP A  82      -0.029  59.279  12.641  1.00 38.79           O  
ANISOU  472  O   TRP A  82     5007   4803   4929   -337   -223   -463       O  
ATOM    473  CB  TRP A  82      -1.011  59.445   9.779  1.00 32.45           C  
ANISOU  473  CB  TRP A  82     4160   4179   3991   -509   -276   -463       C  
ATOM    474  CG  TRP A  82      -1.570  60.230   8.623  1.00 40.79           C  
ANISOU  474  CG  TRP A  82     5116   5372   5011   -557   -305   -420       C  
ATOM    475  CD1 TRP A  82      -1.207  61.494   8.229  1.00 47.45           C  
ANISOU  475  CD1 TRP A  82     5857   6282   5890   -474   -301   -379       C  
ATOM    476  CD2 TRP A  82      -2.594  59.808   7.712  1.00 38.75           C  
ANISOU  476  CD2 TRP A  82     4852   5204   4665   -706   -345   -408       C  
ATOM    477  NE1 TRP A  82      -1.937  61.878   7.123  1.00 39.76           N  
ANISOU  477  NE1 TRP A  82     4814   5433   4861   -547   -333   -339       N  
ATOM    478  CE2 TRP A  82      -2.792  60.860   6.783  1.00 38.85           C  
ANISOU  478  CE2 TRP A  82     4749   5343   4668   -693   -363   -355       C  
ATOM    479  CE3 TRP A  82      -3.359  58.639   7.582  1.00 40.97           C  
ANISOU  479  CE3 TRP A  82     5223   5475   4869   -860   -369   -435       C  
ATOM    480  CZ2 TRP A  82      -3.728  60.780   5.746  1.00 32.32           C  
ANISOU  480  CZ2 TRP A  82     3879   4645   3756   -822   -407   -323       C  
ATOM    481  CZ3 TRP A  82      -4.285  58.560   6.545  1.00 47.33           C  
ANISOU  481  CZ3 TRP A  82     5989   6409   5585  -1005   -414   -408       C  
ATOM    482  CH2 TRP A  82      -4.464  59.628   5.644  1.00 39.29           C  
ANISOU  482  CH2 TRP A  82     4840   5528   4559   -981   -434   -350       C  
ATOM    483  N   ARG A  83      -1.903  58.049  12.866  1.00 44.67           N  
ANISOU  483  N   ARG A  83     5802   5567   5604   -545   -259   -448       N  
ATOM    484  CA  ARG A  83      -1.410  57.272  13.996  1.00 53.36           C  
ANISOU  484  CA  ARG A  83     7003   6541   6731   -501   -233   -477       C  
ATOM    485  C   ARG A  83      -1.287  55.818  13.557  1.00 64.02           C  
ANISOU  485  C   ARG A  83     8530   7788   8006   -578   -226   -544       C  
ATOM    486  O   ARG A  83      -2.277  55.198  13.150  1.00 71.01           O  
ANISOU  486  O   ARG A  83     9455   8700   8823   -730   -252   -545       O  
ATOM    487  CB  ARG A  83      -2.326  57.402  15.216  1.00 54.40           C  
ANISOU  487  CB  ARG A  83     7076   6696   6896   -533   -239   -423       C  
ATOM    488  CG  ARG A  83      -1.783  56.689  16.456  1.00 68.24           C  
ANISOU  488  CG  ARG A  83     8924   8323   8679   -480   -213   -445       C  
ATOM    489  CD  ARG A  83      -2.876  56.337  17.474  1.00 78.18           C  
ANISOU  489  CD  ARG A  83    10173   9595   9939   -563   -222   -404       C  
ATOM    490  NE  ARG A  83      -3.359  57.505  18.208  1.00 85.99           N  
ANISOU  490  NE  ARG A  83    11017  10671  10984   -513   -219   -337       N  
ATOM    491  CZ  ARG A  83      -3.078  57.761  19.484  1.00 87.07           C  
ANISOU  491  CZ  ARG A  83    11146  10763  11173   -437   -197   -321       C  
ATOM    492  NH1 ARG A  83      -2.314  56.925  20.183  1.00 85.11           N  
ANISOU  492  NH1 ARG A  83    11012  10395  10932   -400   -181   -359       N  
ATOM    493  NH2 ARG A  83      -3.559  58.861  20.061  1.00 86.43           N  
ANISOU  493  NH2 ARG A  83    10949  10758  11132   -392   -186   -263       N  
ATOM    494  N   PHE A  84      -0.070  55.301  13.580  1.00 61.29           N  
ANISOU  494  N   PHE A  84     8291   7331   7664   -475   -188   -595       N  
ATOM    495  CA  PHE A  84       0.157  53.878  13.418  1.00 60.25           C  
ANISOU  495  CA  PHE A  84     8357   7067   7467   -513   -164   -656       C  
ATOM    496  C   PHE A  84       0.182  53.237  14.800  1.00 68.25           C  
ANISOU  496  C   PHE A  84     9439   7981   8511   -485   -147   -647       C  
ATOM    497  O   PHE A  84       0.391  53.907  15.813  1.00 71.90           O  
ANISOU  497  O   PHE A  84     9801   8469   9048   -402   -146   -604       O  
ATOM    498  CB  PHE A  84       1.475  53.620  12.694  1.00 61.36           C  
ANISOU  498  CB  PHE A  84     8582   7146   7588   -394   -122   -709       C  
ATOM    499  CG  PHE A  84       1.531  54.175  11.298  1.00 70.22           C  
ANISOU  499  CG  PHE A  84     9652   8358   8671   -420   -134   -723       C  
ATOM    500  CD1 PHE A  84       1.309  53.352  10.203  1.00 82.02           C  
ANISOU  500  CD1 PHE A  84    11283   9815  10067   -518   -129   -779       C  
ATOM    501  CD2 PHE A  84       1.832  55.510  11.074  1.00 61.94           C  
ANISOU  501  CD2 PHE A  84     8434   7425   7677   -352   -149   -682       C  
ATOM    502  CE1 PHE A  84       1.374  53.852   8.910  1.00 82.08           C  
ANISOU  502  CE1 PHE A  84    11244   9909  10032   -544   -141   -791       C  
ATOM    503  CE2 PHE A  84       1.897  56.015   9.788  1.00 66.54           C  
ANISOU  503  CE2 PHE A  84     8971   8090   8221   -375   -160   -691       C  
ATOM    504  CZ  PHE A  84       1.668  55.188   8.703  1.00 74.02           C  
ANISOU  504  CZ  PHE A  84    10043   9011   9072   -470   -157   -744       C  
ATOM    505  N   ASN A  85      -0.054  51.938  14.851  1.00 82.38           N  
ANISOU  505  N   ASN A  85    11410   9654  10238   -562   -132   -685       N  
ATOM    506  CA  ASN A  85       0.196  51.296  16.130  1.00100.39           C  
ANISOU  506  CA  ASN A  85    13770  11826  12548   -508   -108   -676       C  
ATOM    507  C   ASN A  85       1.620  50.759  16.142  1.00103.91           C  
ANISOU  507  C   ASN A  85    14330  12156  12994   -339    -52   -712       C  
ATOM    508  O   ASN A  85       2.211  50.466  15.099  1.00107.93           O  
ANISOU  508  O   ASN A  85    14919  12634  13455   -303    -25   -759       O  
ATOM    509  CB  ASN A  85      -0.833  50.199  16.445  1.00110.90           C  
ANISOU  509  CB  ASN A  85    15237  13085  13815   -676   -118   -684       C  
ATOM    510  CG  ASN A  85      -0.982  49.182  15.336  1.00121.92           C  
ANISOU  510  CG  ASN A  85    16824  14398  15103   -787   -106   -749       C  
ATOM    511  OD1 ASN A  85      -0.083  48.980  14.522  1.00123.69           O  
ANISOU  511  OD1 ASN A  85    17132  14567  15299   -698    -70   -798       O  
ATOM    512  ND2 ASN A  85      -2.139  48.535  15.295  1.00126.46           N  
ANISOU  512  ND2 ASN A  85    17471  14970  15606   -991   -134   -749       N  
ATOM    513  N   ASP A  86       2.175  50.651  17.351  1.00 95.74           N  
ANISOU  513  N   ASP A  86    13295  11071  12012   -230    -33   -683       N  
ATOM    514  CA  ASP A  86       3.602  50.372  17.505  1.00 93.50           C  
ANISOU  514  CA  ASP A  86    13064  10721  11740    -42     17   -692       C  
ATOM    515  C   ASP A  86       4.044  49.128  16.736  1.00 99.19           C  
ANISOU  515  C   ASP A  86    14006  11305  12378    -16     70   -750       C  
ATOM    516  O   ASP A  86       5.231  48.989  16.425  1.00 95.62           O  
ANISOU  516  O   ASP A  86    13584  10827  11919    144    118   -761       O  
ATOM    517  CB  ASP A  86       3.937  50.223  18.987  1.00 94.43           C  
ANISOU  517  CB  ASP A  86    13172  10799  11907     40     25   -648       C  
ATOM    518  CG  ASP A  86       3.358  51.349  19.822  1.00102.56           C  
ANISOU  518  CG  ASP A  86    14018  11944  13005     -3    -20   -596       C  
ATOM    519  OD1 ASP A  86       2.178  51.701  19.591  1.00105.61           O  
ANISOU  519  OD1 ASP A  86    14349  12392  13386   -145    -56   -590       O  
ATOM    520  OD2 ASP A  86       4.067  51.866  20.707  1.00101.46           O  
ANISOU  520  OD2 ASP A  86    13795  11837  12918    105    -17   -559       O  
ATOM    521  N   TRP A  87       3.114  48.225  16.414  1.00107.07           N  
ANISOU  521  N   TRP A  87    15163  12216  13304   -173     68   -786       N  
ATOM    522  CA  TRP A  87       3.478  47.002  15.706  1.00109.30           C  
ANISOU  522  CA  TRP A  87    15692  12343  13495   -159    126   -847       C  
ATOM    523  C   TRP A  87       4.018  47.313  14.319  1.00106.06           C  
ANISOU  523  C   TRP A  87    15273  11980  13046   -118    145   -890       C  
ATOM    524  O   TRP A  87       5.048  46.765  13.905  1.00100.89           O  
ANISOU  524  O   TRP A  87    14739  11241  12356     30    213   -919       O  
ATOM    525  CB  TRP A  87       2.264  46.068  15.606  1.00114.14           C  
ANISOU  525  CB  TRP A  87    16476  12865  14026   -377    111   -878       C  
ATOM    526  CG  TRP A  87       1.318  46.076  16.766  1.00118.08           C  
ANISOU  526  CG  TRP A  87    16920  13384  14560   -488     68   -829       C  
ATOM    527  CD1 TRP A  87       1.570  46.483  18.048  1.00114.75           C  
ANISOU  527  CD1 TRP A  87    16384  12992  14225   -389     61   -770       C  
ATOM    528  CD2 TRP A  87      -0.069  45.723  16.727  1.00125.02           C  
ANISOU  528  CD2 TRP A  87    17841  14278  15384   -730     24   -830       C  
ATOM    529  NE1 TRP A  87       0.444  46.369  18.812  1.00121.31           N  
ANISOU  529  NE1 TRP A  87    17193  13842  15057   -543     22   -738       N  
ATOM    530  CE2 TRP A  87      -0.580  45.907  18.029  1.00127.13           C  
ANISOU  530  CE2 TRP A  87    18017  14577  15709   -753     -2   -770       C  
ATOM    531  CE3 TRP A  87      -0.926  45.250  15.723  1.00124.60           C  
ANISOU  531  CE3 TRP A  87    17892  14222  15227   -938      3   -872       C  
ATOM    532  CZ2 TRP A  87      -1.909  45.632  18.358  1.00131.03           C  
ANISOU  532  CZ2 TRP A  87    18514  15107  16165   -969    -44   -747       C  
ATOM    533  CZ3 TRP A  87      -2.249  44.978  16.051  1.00127.87           C  
ANISOU  533  CZ3 TRP A  87    18306  14678  15599  -1164    -46   -847       C  
ATOM    534  CH2 TRP A  87      -2.727  45.170  17.357  1.00133.57           C  
ANISOU  534  CH2 TRP A  87    18928  15438  16386  -1174    -67   -784       C  
ATOM    535  N   ASP A  88       3.321  48.181  13.587  1.00112.43           N  
ANISOU  535  N   ASP A  88    15939  12926  13853   -242     89   -889       N  
ATOM    536  CA  ASP A  88       3.592  48.353  12.162  1.00114.54           C  
ANISOU  536  CA  ASP A  88    16225  13233  14063   -250    101   -934       C  
ATOM    537  C   ASP A  88       4.998  48.882  11.898  1.00 85.36           C  
ANISOU  537  C   ASP A  88    12447   9580  10406    -35    144   -927       C  
ATOM    538  O   ASP A  88       5.556  48.656  10.813  1.00 78.42           O  
ANISOU  538  O   ASP A  88    11648   8683   9466     11    185   -972       O  
ATOM    539  CB  ASP A  88       2.550  49.289  11.537  1.00136.24           C  
ANISOU  539  CB  ASP A  88    18811  16143  16812   -416     27   -916       C  
ATOM    540  CG  ASP A  88       1.123  48.796  11.732  1.00151.55           C  
ANISOU  540  CG  ASP A  88    20805  18075  18702   -641    -18   -913       C  
ATOM    541  OD1 ASP A  88       0.904  47.566  11.655  1.00157.35           O  
ANISOU  541  OD1 ASP A  88    21770  18663  19352   -723     10   -960       O  
ATOM    542  OD2 ASP A  88       0.231  49.636  11.967  1.00155.18           O  
ANISOU  542  OD2 ASP A  88    21083  18676  19201   -733    -79   -859       O  
ATOM    543  N   TYR A  89       5.590  49.576  12.871  1.00 62.62           N  
ANISOU  543  N   TYR A  89     9412   6764   7618     90    136   -868       N  
ATOM    544  CA  TYR A  89       6.916  50.144  12.685  1.00 53.07           C  
ANISOU  544  CA  TYR A  89     8102   5621   6440    275    168   -849       C  
ATOM    545  C   TYR A  89       8.013  49.093  12.620  1.00 54.23           C  
ANISOU  545  C   TYR A  89     8416   5648   6539    446    254   -870       C  
ATOM    546  O   TYR A  89       9.132  49.424  12.210  1.00 54.37           O  
ANISOU  546  O   TYR A  89     8369   5731   6560    596    291   -859       O  
ATOM    547  CB  TYR A  89       7.239  51.127  13.803  1.00 52.13           C  
ANISOU  547  CB  TYR A  89     7787   5602   6419    342    134   -779       C  
ATOM    548  CG  TYR A  89       6.447  52.413  13.767  1.00 54.42           C  
ANISOU  548  CG  TYR A  89     7891   6027   6759    229     66   -749       C  
ATOM    549  CD1 TYR A  89       6.665  53.371  12.781  1.00 46.63           C  
ANISOU  549  CD1 TYR A  89     6788   5155   5772    226     51   -749       C  
ATOM    550  CD2 TYR A  89       5.515  52.694  14.753  1.00 52.05           C  
ANISOU  550  CD2 TYR A  89     7533   5740   6504    139     23   -714       C  
ATOM    551  CE1 TYR A  89       5.948  54.561  12.773  1.00 46.33           C  
ANISOU  551  CE1 TYR A  89     6593   5233   5779    139     -4   -714       C  
ATOM    552  CE2 TYR A  89       4.798  53.876  14.746  1.00 47.87           C  
ANISOU  552  CE2 TYR A  89     6842   5330   6017     59    -28   -680       C  
ATOM    553  CZ  TYR A  89       5.015  54.805  13.763  1.00 42.32           C  
ANISOU  553  CZ  TYR A  89     6036   4731   5314     63    -40   -679       C  
ATOM    554  OH  TYR A  89       4.291  55.979  13.787  1.00 39.07           O  
ANISOU  554  OH  TYR A  89     5476   4427   4941     -3    -83   -638       O  
ATOM    555  N   LYS A  90       7.736  47.852  13.025  1.00 57.10           N  
ANISOU  555  N   LYS A  90     8995   5846   6857    432    291   -894       N  
ATOM    556  CA  LYS A  90       8.702  46.769  12.907  1.00 63.89           C  
ANISOU  556  CA  LYS A  90    10045   6571   7659    603    386   -913       C  
ATOM    557  C   LYS A  90       8.600  46.033  11.579  1.00 71.20           C  
ANISOU  557  C   LYS A  90    11177   7402   8476    558    437   -993       C  
ATOM    558  O   LYS A  90       9.460  45.197  11.285  1.00 77.56           O  
ANISOU  558  O   LYS A  90    12148   8099   9223    718    529  -1013       O  
ATOM    559  CB  LYS A  90       8.531  45.790  14.072  1.00 67.43           C  
ANISOU  559  CB  LYS A  90    10640   6871   8107    627    409   -893       C  
ATOM    560  CG  LYS A  90       8.713  46.454  15.439  1.00 60.07           C  
ANISOU  560  CG  LYS A  90     9519   6031   7275    681    364   -813       C  
ATOM    561  CD  LYS A  90       8.681  45.451  16.576  1.00 68.41           C  
ANISOU  561  CD  LYS A  90    10724   6944   8326    728    394   -787       C  
ATOM    562  CE  LYS A  90       8.065  46.046  17.838  1.00 75.58           C  
ANISOU  562  CE  LYS A  90    11484   7921   9313    644    323   -733       C  
ATOM    563  NZ  LYS A  90       8.352  45.236  19.062  1.00 79.05           N  
ANISOU  563  NZ  LYS A  90    12022   8254   9758    738    353   -689       N  
ATOM    564  N   LYS A  91       7.570  46.335  10.771  1.00 72.07           N  
ANISOU  564  N   LYS A  91    11279   7554   8550    348    383  -1035       N  
ATOM    565  CA  LYS A  91       7.400  45.818   9.424  1.00 74.57           C  
ANISOU  565  CA  LYS A  91    11767   7810   8757    272    418  -1112       C  
ATOM    566  C   LYS A  91       8.289  46.573   8.443  1.00 71.77           C  
ANISOU  566  C   LYS A  91    11286   7581   8401    387    439  -1115       C  
ATOM    567  O   LYS A  91       8.529  47.772   8.607  1.00 66.42           O  
ANISOU  567  O   LYS A  91    10355   7073   7807    419    389  -1062       O  
ATOM    568  CB  LYS A  91       5.949  45.959   8.973  1.00 81.53           C  
ANISOU  568  CB  LYS A  91    12652   8728   9598     -7    339  -1140       C  
ATOM    569  CG  LYS A  91       5.057  44.789   9.330  1.00 96.03           C  
ANISOU  569  CG  LYS A  91    14727  10399  11363   -164    344  -1175       C  
ATOM    570  CD  LYS A  91       3.646  45.001   8.801  1.00105.59           C  
ANISOU  570  CD  LYS A  91    15909  11687  12524   -449    261  -1191       C  
ATOM    571  CE  LYS A  91       2.606  44.541   9.813  1.00113.04           C  
ANISOU  571  CE  LYS A  91    16897  12581  13474   -606    218  -1165       C  
ATOM    572  NZ  LYS A  91       2.773  45.211  11.135  1.00114.56           N  
ANISOU  572  NZ  LYS A  91    16886  12845  13798   -496    190  -1085       N  
ATOM    573  N   PRO A  92       8.791  45.900   7.417  1.00 75.99           N  
ANISOU  573  N   PRO A  92    12003   8032   8837    447    517  -1176       N  
ATOM    574  CA  PRO A  92       9.363  46.615   6.277  1.00 79.22           C  
ANISOU  574  CA  PRO A  92    12305   8569   9227    497    528  -1188       C  
ATOM    575  C   PRO A  92       8.244  47.126   5.377  1.00 86.05           C  
ANISOU  575  C   PRO A  92    13126   9516  10053    255    450  -1222       C  
ATOM    576  O   PRO A  92       7.078  46.746   5.505  1.00 89.11           O  
ANISOU  576  O   PRO A  92    13600   9850  10407     52    401  -1244       O  
ATOM    577  CB  PRO A  92      10.210  45.547   5.574  1.00 79.34           C  
ANISOU  577  CB  PRO A  92    12567   8441   9136    647    650  -1244       C  
ATOM    578  CG  PRO A  92       9.477  44.270   5.856  1.00 77.71           C  
ANISOU  578  CG  PRO A  92    12650   8021   8856    540    677  -1294       C  
ATOM    579  CD  PRO A  92       8.881  44.436   7.251  1.00 77.33           C  
ANISOU  579  CD  PRO A  92    12504   7977   8902    478    608  -1236       C  
ATOM    580  N   ASP A  93       8.621  48.013   4.461  1.00 87.32           N  
ANISOU  580  N   ASP A  93    13141   9823  10215    276    438  -1217       N  
ATOM    581  CA  ASP A  93       7.712  48.504   3.428  1.00 95.91           C  
ANISOU  581  CA  ASP A  93    14187  11003  11252     73    374  -1245       C  
ATOM    582  C   ASP A  93       6.501  49.215   4.043  1.00 92.51           C  
ANISOU  582  C   ASP A  93    13592  10668  10889   -104    265  -1194       C  
ATOM    583  O   ASP A  93       5.350  48.792   3.912  1.00 93.70           O  
ANISOU  583  O   ASP A  93    13832  10787  10984   -308    221  -1217       O  
ATOM    584  CB  ASP A  93       7.287  47.362   2.494  1.00104.58           C  
ANISOU  584  CB  ASP A  93    15573  11959  12202    -46    418  -1337       C  
ATOM    585  CG  ASP A  93       8.477  46.684   1.821  1.00111.76           C  
ANISOU  585  CG  ASP A  93    16656  12773  13035    145    538  -1387       C  
ATOM    586  OD1 ASP A  93       8.727  45.488   2.095  1.00114.80           O  
ANISOU  586  OD1 ASP A  93    17295  12964  13360    213    619  -1428       O  
ATOM    587  OD2 ASP A  93       9.168  47.350   1.020  1.00112.04           O  
ANISOU  587  OD2 ASP A  93    16576  12926  13067    233    556  -1381       O  
ATOM    588  N   LEU A  94       6.796  50.302   4.744  1.00 85.63           N  
ANISOU  588  N   LEU A  94    12482   9919  10135    -22    227  -1120       N  
ATOM    589  CA  LEU A  94       5.836  51.315   5.137  1.00 69.80           C  
ANISOU  589  CA  LEU A  94    10278   8044   8200   -146    135  -1061       C  
ATOM    590  C   LEU A  94       6.135  52.591   4.365  1.00 64.21           C  
ANISOU  590  C   LEU A  94     9376   7503   7519   -123    106  -1029       C  
ATOM    591  O   LEU A  94       7.289  52.829   3.990  1.00 64.80           O  
ANISOU  591  O   LEU A  94     9421   7603   7597     27    155  -1032       O  
ATOM    592  CB  LEU A  94       5.895  51.612   6.637  1.00 61.55           C  
ANISOU  592  CB  LEU A  94     9129   6995   7263    -76    117  -1001       C  
ATOM    593  CG  LEU A  94       4.876  50.974   7.565  1.00 57.72           C  
ANISOU  593  CG  LEU A  94     8720   6429   6783   -195     88   -994       C  
ATOM    594  CD1 LEU A  94       5.029  49.471   7.519  1.00 63.79           C  
ANISOU  594  CD1 LEU A  94     9764   7009   7464   -193    151  -1059       C  
ATOM    595  CD2 LEU A  94       5.104  51.517   8.984  1.00 48.74           C  
ANISOU  595  CD2 LEU A  94     7445   5316   5757   -101     72   -929       C  
ATOM    596  N   PRO A  95       5.126  53.425   4.091  1.00 60.42           N  
ANISOU  596  N   PRO A  95     8760   7144   7052   -264     31   -992       N  
ATOM    597  CA  PRO A  95       5.392  54.618   3.268  1.00 57.34           C  
ANISOU  597  CA  PRO A  95     8206   6903   6678   -245      8   -960       C  
ATOM    598  C   PRO A  95       6.228  55.649   3.997  1.00 58.70           C  
ANISOU  598  C   PRO A  95     8207   7140   6956    -99     11   -899       C  
ATOM    599  O   PRO A  95       7.054  56.340   3.387  1.00 58.68           O  
ANISOU  599  O   PRO A  95     8122   7215   6958    -19     28   -888       O  
ATOM    600  CB  PRO A  95       3.985  55.133   2.946  1.00 62.64           C  
ANISOU  600  CB  PRO A  95     8789   7677   7333   -429    -71   -924       C  
ATOM    601  CG  PRO A  95       3.150  54.662   4.097  1.00 58.72           C  
ANISOU  601  CG  PRO A  95     8319   7121   6869   -498    -96   -905       C  
ATOM    602  CD  PRO A  95       3.721  53.344   4.522  1.00 56.32           C  
ANISOU  602  CD  PRO A  95     8224   6643   6532   -440    -33   -968       C  
ATOM    603  N   THR A  96       6.030  55.772   5.301  1.00 57.41           N  
ANISOU  603  N   THR A  96     7993   6949   6872    -75     -6   -860       N  
ATOM    604  CA  THR A  96       6.910  56.565   6.131  1.00 49.45           C  
ANISOU  604  CA  THR A  96     6857   5980   5950     57      3   -811       C  
ATOM    605  C   THR A  96       6.995  55.888   7.485  1.00 59.62           C  
ANISOU  605  C   THR A  96     8205   7167   7281    108     19   -805       C  
ATOM    606  O   THR A  96       6.174  55.033   7.831  1.00 66.06           O  
ANISOU  606  O   THR A  96     9133   7897   8072     23     11   -828       O  
ATOM    607  CB  THR A  96       6.422  58.007   6.273  1.00 44.91           C  
ANISOU  607  CB  THR A  96     6098   5527   5439     14    -51   -745       C  
ATOM    608  OG1 THR A  96       7.461  58.816   6.848  1.00 48.59           O  
ANISOU  608  OG1 THR A  96     6459   6035   5967    131    -37   -706       O  
ATOM    609  CG2 THR A  96       5.160  58.061   7.139  1.00 31.01           C  
ANISOU  609  CG2 THR A  96     4311   3756   3714    -84    -95   -713       C  
ATOM    610  N   TYR A  97       8.023  56.262   8.236  1.00 54.79           N  
ANISOU  610  N   TYR A  97     7521   6572   6725    242     41   -772       N  
ATOM    611  CA  TYR A  97       8.244  55.712   9.560  1.00 42.04           C  
ANISOU  611  CA  TYR A  97     5946   4878   5150    306     55   -757       C  
ATOM    612  C   TYR A  97       8.119  56.776  10.638  1.00 46.37           C  
ANISOU  612  C   TYR A  97     6343   5491   5783    305     14   -695       C  
ATOM    613  O   TYR A  97       8.503  56.531  11.786  1.00 44.41           O  
ANISOU  613  O   TYR A  97     6098   5203   5572    371     24   -672       O  
ATOM    614  CB  TYR A  97       9.601  55.012   9.608  1.00 32.27           C  
ANISOU  614  CB  TYR A  97     4777   3598   3888    472    123   -768       C  
ATOM    615  CG  TYR A  97       9.479  53.628   9.022  1.00 46.74           C  
ANISOU  615  CG  TYR A  97     6822   5300   5637    472    173   -833       C  
ATOM    616  CD1 TYR A  97       9.592  53.418   7.644  1.00 46.55           C  
ANISOU  616  CD1 TYR A  97     6868   5284   5536    455    201   -882       C  
ATOM    617  CD2 TYR A  97       9.172  52.543   9.831  1.00 45.97           C  
ANISOU  617  CD2 TYR A  97     6871   5066   5530    475    193   -847       C  
ATOM    618  CE1 TYR A  97       9.446  52.169   7.102  1.00 42.59           C  
ANISOU  618  CE1 TYR A  97     6584   4651   4947    443    251   -946       C  
ATOM    619  CE2 TYR A  97       9.016  51.289   9.299  1.00 52.24           C  
ANISOU  619  CE2 TYR A  97     7885   5723   6239    463    243   -908       C  
ATOM    620  CZ  TYR A  97       9.158  51.100   7.932  1.00 52.11           C  
ANISOU  620  CZ  TYR A  97     7945   5710   6143    446    274   -960       C  
ATOM    621  OH  TYR A  97       9.002  49.833   7.404  1.00 46.42           O  
ANISOU  621  OH  TYR A  97     7472   4839   5325    425    330  -1027       O  
ATOM    622  N   ALA A  98       7.551  57.932  10.297  1.00 45.86           N  
ANISOU  622  N   ALA A  98     6158   5522   5743    230    -28   -665       N  
ATOM    623  CA  ALA A  98       7.373  59.012  11.253  1.00 39.21           C  
ANISOU  623  CA  ALA A  98     5194   4732   4973    225    -58   -610       C  
ATOM    624  C   ALA A  98       6.430  58.599  12.375  1.00 37.11           C  
ANISOU  624  C   ALA A  98     4963   4402   4736    171    -76   -598       C  
ATOM    625  O   ALA A  98       5.386  57.983  12.139  1.00 42.58           O  
ANISOU  625  O   ALA A  98     5721   5059   5398     75    -90   -617       O  
ATOM    626  CB  ALA A  98       6.833  60.252  10.536  1.00 31.76           C  
ANISOU  626  CB  ALA A  98     4142   3886   4037    160    -90   -580       C  
ATOM    627  N   ARG A  99       6.817  58.924  13.606  1.00 38.17           N  
ANISOU  627  N   ARG A  99     5054   4529   4922    225    -75   -565       N  
ATOM    628  CA  ARG A  99       5.956  58.786  14.776  1.00 39.82           C  
ANISOU  628  CA  ARG A  99     5271   4695   5165    178    -92   -544       C  
ATOM    629  C   ARG A  99       5.470  60.194  15.091  1.00 33.75           C  
ANISOU  629  C   ARG A  99     4380   4002   4440    147   -117   -496       C  
ATOM    630  O   ARG A  99       6.194  60.998  15.687  1.00 38.44           O  
ANISOU  630  O   ARG A  99     4913   4626   5066    201   -114   -470       O  
ATOM    631  CB  ARG A  99       6.703  58.145  15.948  1.00 37.91           C  
ANISOU  631  CB  ARG A  99     5077   4388   4939    261    -71   -538       C  
ATOM    632  CG  ARG A  99       5.883  57.950  17.234  1.00 34.95           C  
ANISOU  632  CG  ARG A  99     4718   3967   4596    216    -85   -516       C  
ATOM    633  CD  ARG A  99       4.976  56.733  17.157  1.00 53.23           C  
ANISOU  633  CD  ARG A  99     7153   6196   6875    141    -82   -545       C  
ATOM    634  NE  ARG A  99       4.114  56.578  18.334  1.00 61.94           N  
ANISOU  634  NE  ARG A  99     8262   7269   8004     87    -96   -518       N  
ATOM    635  CZ  ARG A  99       3.271  55.565  18.517  1.00 61.75           C  
ANISOU  635  CZ  ARG A  99     8337   7174   7949      5    -97   -533       C  
ATOM    636  NH1 ARG A  99       3.175  54.609  17.599  1.00 55.37           N  
ANISOU  636  NH1 ARG A  99     7647   6309   7081    -38    -85   -578       N  
ATOM    637  NH2 ARG A  99       2.519  55.509  19.614  1.00 66.12           N  
ANISOU  637  NH2 ARG A  99     8882   7716   8527    -42   -107   -503       N  
ATOM    638  N   GLY A 100       4.240  60.489  14.688  1.00 27.50           N  
ANISOU  638  N   GLY A 100     3560   3245   3643     58   -138   -482       N  
ATOM    639  CA  GLY A 100       3.764  61.857  14.674  1.00 29.21           C  
ANISOU  639  CA  GLY A 100     3671   3537   3889     44   -151   -434       C  
ATOM    640  C   GLY A 100       3.869  62.387  13.259  1.00 39.85           C  
ANISOU  640  C   GLY A 100     4980   4955   5207     30   -159   -436       C  
ATOM    641  O   GLY A 100       4.959  62.743  12.796  1.00 30.91           O  
ANISOU  641  O   GLY A 100     3833   3842   4068     85   -147   -447       O  
ATOM    642  N   LEU A 101       2.758  62.400  12.535  1.00 38.97           N  
ANISOU  642  N   LEU A 101     4847   4892   5068    -49   -179   -422       N  
ATOM    643  CA  LEU A 101       2.783  62.917  11.180  1.00 38.93           C  
ANISOU  643  CA  LEU A 101     4802   4961   5028    -67   -189   -417       C  
ATOM    644  C   LEU A 101       1.473  63.631  10.903  1.00 39.09           C  
ANISOU  644  C   LEU A 101     4740   5065   5046   -125   -211   -357       C  
ATOM    645  O   LEU A 101       0.396  63.059  11.119  1.00 28.64           O  
ANISOU  645  O   LEU A 101     3423   3756   3706   -198   -228   -344       O  
ATOM    646  CB  LEU A 101       3.020  61.798  10.172  1.00 35.60           C  
ANISOU  646  CB  LEU A 101     4468   4519   4541   -105   -188   -476       C  
ATOM    647  CG  LEU A 101       2.802  62.183   8.711  1.00 33.17           C  
ANISOU  647  CG  LEU A 101     4125   4295   4182   -151   -204   -473       C  
ATOM    648  CD1 LEU A 101       4.078  62.759   8.095  1.00 23.96           C  
ANISOU  648  CD1 LEU A 101     2939   3151   3015    -72   -183   -484       C  
ATOM    649  CD2 LEU A 101       2.293  60.968   7.937  1.00 34.18           C  
ANISOU  649  CD2 LEU A 101     4350   4406   4232   -247   -215   -521       C  
ATOM    650  N   PHE A 102       1.572  64.886  10.449  1.00 38.76           N  
ANISOU  650  N   PHE A 102     4624   5085   5018    -90   -209   -313       N  
ATOM    651  CA  PHE A 102       0.410  65.704  10.124  1.00 44.87           C  
ANISOU  651  CA  PHE A 102     5313   5948   5788   -116   -223   -241       C  
ATOM    652  C   PHE A 102       0.481  66.212   8.685  1.00 41.00           C  
ANISOU  652  C   PHE A 102     4784   5539   5255   -133   -236   -225       C  
ATOM    653  O   PHE A 102       1.497  66.760   8.243  1.00 36.73           O  
ANISOU  653  O   PHE A 102     4248   4990   4718    -86   -223   -239       O  
ATOM    654  CB  PHE A 102       0.276  66.893  11.078  1.00 44.77           C  
ANISOU  654  CB  PHE A 102     5256   5925   5831    -46   -197   -184       C  
ATOM    655  CG  PHE A 102      -0.147  66.522  12.465  1.00 36.66           C  
ANISOU  655  CG  PHE A 102     4249   4844   4838    -40   -185   -181       C  
ATOM    656  CD1 PHE A 102       0.684  65.775  13.285  1.00 37.32           C  
ANISOU  656  CD1 PHE A 102     4403   4837   4939    -25   -177   -237       C  
ATOM    657  CD2 PHE A 102      -1.368  66.940  12.963  1.00 40.68           C  
ANISOU  657  CD2 PHE A 102     4700   5399   5357    -40   -178   -115       C  
ATOM    658  CE1 PHE A 102       0.300  65.444  14.582  1.00 38.93           C  
ANISOU  658  CE1 PHE A 102     4628   4993   5172    -21   -166   -232       C  
ATOM    659  CE2 PHE A 102      -1.757  66.608  14.266  1.00 39.03           C  
ANISOU  659  CE2 PHE A 102     4509   5144   5175    -35   -163   -111       C  
ATOM    660  CZ  PHE A 102      -0.923  65.860  15.069  1.00 35.41           C  
ANISOU  660  CZ  PHE A 102     4128   4590   4735    -30   -159   -171       C  
ATOM    661  N   THR A 103      -0.636  66.088   7.993  1.00 40.29           N  
ANISOU  661  N   THR A 103     4647   5541   5121   -204   -264   -187       N  
ATOM    662  CA  THR A 103      -0.768  66.342   6.569  1.00 37.01           C  
ANISOU  662  CA  THR A 103     4197   5217   4648   -243   -286   -171       C  
ATOM    663  C   THR A 103      -1.760  67.474   6.345  1.00 39.26           C  
ANISOU  663  C   THR A 103     4372   5607   4936   -223   -292    -66       C  
ATOM    664  O   THR A 103      -2.621  67.724   7.188  1.00 41.79           O  
ANISOU  664  O   THR A 103     4647   5947   5285   -204   -284    -10       O  
ATOM    665  CB  THR A 103      -1.224  65.042   5.908  1.00 34.96           C  
ANISOU  665  CB  THR A 103     3989   4980   4313   -361   -318   -217       C  
ATOM    666  OG1 THR A 103      -0.072  64.224   5.710  1.00 40.28           O  
ANISOU  666  OG1 THR A 103     4772   5560   4972   -350   -300   -309       O  
ATOM    667  CG2 THR A 103      -2.065  65.241   4.630  1.00 55.02           C  
ANISOU  667  CG2 THR A 103     6465   7660   6780   -443   -356   -170       C  
ATOM    668  N   THR A 104      -1.642  68.163   5.213  1.00 33.84           N  
ANISOU  668  N   THR A 104     3647   4994   4217   -216   -301    -34       N  
ATOM    669  CA  THR A 104      -2.556  69.267   4.953  1.00 30.60           C  
ANISOU  669  CA  THR A 104     3137   4684   3805   -179   -301     76       C  
ATOM    670  C   THR A 104      -2.623  69.560   3.455  1.00 29.44           C  
ANISOU  670  C   THR A 104     2950   4643   3593   -217   -328    104       C  
ATOM    671  O   THR A 104      -1.856  69.023   2.650  1.00 33.20           O  
ANISOU  671  O   THR A 104     3482   5104   4029   -264   -340     34       O  
ATOM    672  CB  THR A 104      -2.131  70.509   5.771  1.00 34.21           C  
ANISOU  672  CB  THR A 104     3599   5070   4332    -59   -252    114       C  
ATOM    673  OG1 THR A 104      -3.170  71.500   5.746  1.00 39.55           O  
ANISOU  673  OG1 THR A 104     4192   5827   5008     -3   -238    227       O  
ATOM    674  CG2 THR A 104      -0.848  71.114   5.247  1.00 26.93           C  
ANISOU  674  CG2 THR A 104     2722   4096   3415    -24   -236     80       C  
ATOM    675  N   ARG A 105      -3.588  70.398   3.091  1.00 36.41           N  
ANISOU  675  N   ARG A 105     3736   5640   4459   -190   -334    214       N  
ATOM    676  CA  ARG A 105      -3.595  71.121   1.826  1.00 34.91           C  
ANISOU  676  CA  ARG A 105     3499   5543   4221   -185   -347    269       C  
ATOM    677  C   ARG A 105      -3.470  72.605   2.142  1.00 35.70           C  
ANISOU  677  C   ARG A 105     3582   5612   4372    -54   -300    348       C  
ATOM    678  O   ARG A 105      -4.178  73.120   3.013  1.00 43.32           O  
ANISOU  678  O   ARG A 105     4511   6574   5375     19   -271    416       O  
ATOM    679  CB  ARG A 105      -4.879  70.857   1.026  1.00 36.24           C  
ANISOU  679  CB  ARG A 105     3567   5892   4312   -266   -396    347       C  
ATOM    680  CG  ARG A 105      -5.011  69.451   0.428  1.00 37.86           C  
ANISOU  680  CG  ARG A 105     3808   6137   4439   -425   -447    270       C  
ATOM    681  CD  ARG A 105      -4.110  69.276  -0.792  1.00 40.79           C  
ANISOU  681  CD  ARG A 105     4239   6501   4756   -469   -460    206       C  
ATOM    682  NE  ARG A 105      -4.211  67.936  -1.365  1.00 39.17           N  
ANISOU  682  NE  ARG A 105     4098   6317   4468   -619   -498    126       N  
ATOM    683  CZ  ARG A 105      -3.942  67.635  -2.637  1.00 42.23           C  
ANISOU  683  CZ  ARG A 105     4517   6759   4769   -698   -523     92       C  
ATOM    684  NH1 ARG A 105      -3.543  68.573  -3.489  1.00 40.51           N  
ANISOU  684  NH1 ARG A 105     4261   6592   4541   -643   -518    135       N  
ATOM    685  NH2 ARG A 105      -4.069  66.386  -3.059  1.00 40.62           N  
ANISOU  685  NH2 ARG A 105     4396   6555   4482   -838   -551     14       N  
ATOM    686  N   THR A 106      -2.560  73.288   1.461  1.00 42.95           N  
ANISOU  686  N   THR A 106     4535   6499   5286    -24   -287    338       N  
ATOM    687  CA  THR A 106      -2.477  74.730   1.621  1.00 45.81           C  
ANISOU  687  CA  THR A 106     4898   6826   5680     86   -241    418       C  
ATOM    688  C   THR A 106      -3.711  75.384   1.005  1.00 47.39           C  
ANISOU  688  C   THR A 106     4998   7168   5841    125   -249    552       C  
ATOM    689  O   THR A 106      -4.552  74.731   0.374  1.00 42.32           O  
ANISOU  689  O   THR A 106     4274   6664   5140     52   -297    582       O  
ATOM    690  CB  THR A 106      -1.209  75.282   0.972  1.00 43.11           C  
ANISOU  690  CB  THR A 106     4618   6429   5332     90   -229    381       C  
ATOM    691  OG1 THR A 106      -1.277  75.111  -0.452  1.00 40.37           O  
ANISOU  691  OG1 THR A 106     4230   6196   4913     30   -268    395       O  
ATOM    692  CG2 THR A 106       0.038  74.572   1.540  1.00 30.58           C  
ANISOU  692  CG2 THR A 106     3112   4732   3775     55   -223    259       C  
ATOM    693  N   GLN A 107      -3.815  76.702   1.188  1.00 45.41           N  
ANISOU  693  N   GLN A 107     4758   6882   5614    241   -198    639       N  
ATOM    694  CA  GLN A 107      -4.939  77.437   0.629  1.00 48.67           C  
ANISOU  694  CA  GLN A 107     5077   7425   5990    310   -194    782       C  
ATOM    695  C   GLN A 107      -4.969  77.360  -0.895  1.00 49.66           C  
ANISOU  695  C   GLN A 107     5146   7683   6039    243   -245    812       C  
ATOM    696  O   GLN A 107      -6.044  77.489  -1.484  1.00 50.68           O  
ANISOU  696  O   GLN A 107     5164   7974   6116    253   -268    921       O  
ATOM    697  CB  GLN A 107      -4.884  78.888   1.099  1.00 51.78           C  
ANISOU  697  CB  GLN A 107     5531   7724   6420    456   -118    861       C  
ATOM    698  CG  GLN A 107      -3.642  79.635   0.627  1.00 63.44           C  
ANISOU  698  CG  GLN A 107     7112   9094   7900    456    -98    823       C  
ATOM    699  CD  GLN A 107      -3.436  80.944   1.369  1.00 72.70           C  
ANISOU  699  CD  GLN A 107     8389  10125   9110    575    -17    871       C  
ATOM    700  OE1 GLN A 107      -4.315  81.810   1.380  1.00 65.06           O  
ANISOU  700  OE1 GLN A 107     7401   9187   8133    694     28    993       O  
ATOM    701  NE2 GLN A 107      -2.273  81.092   2.000  1.00 79.05           N  
ANISOU  701  NE2 GLN A 107     9310  10778   9949    544      6    777       N  
ATOM    702  N   HIS A 108      -3.822  77.113  -1.536  1.00 41.74           N  
ANISOU  702  N   HIS A 108     4210   6628   5021    172   -262    719       N  
ATOM    703  CA  HIS A 108      -3.707  76.961  -2.985  1.00 44.40           C  
ANISOU  703  CA  HIS A 108     4511   7079   5281     98   -308    728       C  
ATOM    704  C   HIS A 108      -3.865  75.516  -3.459  1.00 50.90           C  
ANISOU  704  C   HIS A 108     5309   7983   6048    -47   -371    647       C  
ATOM    705  O   HIS A 108      -3.728  75.248  -4.662  1.00 54.68           O  
ANISOU  705  O   HIS A 108     5772   8553   6452   -125   -410    638       O  
ATOM    706  CB  HIS A 108      -2.354  77.520  -3.463  1.00 28.88           C  
ANISOU  706  CB  HIS A 108     2634   5018   3320    102   -286    676       C  
ATOM    707  CG  HIS A 108      -2.070  78.894  -2.945  1.00 40.52           C  
ANISOU  707  CG  HIS A 108     4168   6386   4843    220   -222    739       C  
ATOM    708  ND1 HIS A 108      -2.764  80.004  -3.376  1.00 42.04           N  
ANISOU  708  ND1 HIS A 108     4326   6633   5014    312   -199    877       N  
ATOM    709  CD2 HIS A 108      -1.229  79.324  -1.970  1.00 43.78           C  
ANISOU  709  CD2 HIS A 108     4680   6638   5318    258   -174    688       C  
ATOM    710  CE1 HIS A 108      -2.331  81.067  -2.720  1.00 46.82           C  
ANISOU  710  CE1 HIS A 108     5026   7099   5665    401   -135    900       C  
ATOM    711  NE2 HIS A 108      -1.405  80.680  -1.857  1.00 43.24           N  
ANISOU  711  NE2 HIS A 108     4652   6517   5259    361   -122    786       N  
ATOM    712  N   GLY A 109      -4.156  74.587  -2.557  1.00 43.05           N  
ANISOU  712  N   GLY A 109     4323   6954   5080    -88   -378    589       N  
ATOM    713  CA  GLY A 109      -4.380  73.208  -2.927  1.00 41.93           C  
ANISOU  713  CA  GLY A 109     4181   6872   4878   -230   -431    515       C  
ATOM    714  C   GLY A 109      -3.159  72.312  -2.931  1.00 34.94           C  
ANISOU  714  C   GLY A 109     3412   5866   3998   -290   -428    365       C  
ATOM    715  O   GLY A 109      -3.273  71.142  -3.326  1.00 31.53           O  
ANISOU  715  O   GLY A 109     3009   5466   3506   -408   -464    296       O  
ATOM    716  N   VAL A 110      -2.002  72.810  -2.519  1.00 25.56           N  
ANISOU  716  N   VAL A 110     2295   4546   2870   -214   -383    318       N  
ATOM    717  CA  VAL A 110      -0.782  72.005  -2.558  1.00 36.45           C  
ANISOU  717  CA  VAL A 110     3770   5829   4249   -251   -373    190       C  
ATOM    718  C   VAL A 110      -0.789  71.057  -1.352  1.00 40.45           C  
ANISOU  718  C   VAL A 110     4325   6241   4801   -263   -365    120       C  
ATOM    719  O   VAL A 110      -1.120  71.494  -0.246  1.00 40.68           O  
ANISOU  719  O   VAL A 110     4338   6221   4897   -198   -342    158       O  
ATOM    720  CB  VAL A 110       0.460  72.897  -2.551  1.00 38.89           C  
ANISOU  720  CB  VAL A 110     4121   6058   4596   -177   -332    178       C  
ATOM    721  CG1 VAL A 110       1.713  72.101  -2.944  1.00 35.55           C  
ANISOU  721  CG1 VAL A 110     3773   5586   4149   -213   -324     65       C  
ATOM    722  CG2 VAL A 110       0.266  74.077  -3.510  1.00 28.71           C  
ANISOU  722  CG2 VAL A 110     2782   4852   3275   -147   -333    276       C  
ATOM    723  N   PRO A 111      -0.487  69.776  -1.535  1.00 46.18           N  
ANISOU  723  N   PRO A 111     5119   6939   5487   -342   -379     23       N  
ATOM    724  CA  PRO A 111      -0.427  68.874  -0.380  1.00 39.61           C  
ANISOU  724  CA  PRO A 111     4345   6007   4697   -347   -368    -41       C  
ATOM    725  C   PRO A 111       0.926  68.970   0.294  1.00 39.86           C  
ANISOU  725  C   PRO A 111     4442   5913   4790   -267   -324   -103       C  
ATOM    726  O   PRO A 111       1.966  69.067  -0.367  1.00 42.88           O  
ANISOU  726  O   PRO A 111     4857   6284   5151   -249   -308   -142       O  
ATOM    727  CB  PRO A 111      -0.642  67.491  -1.003  1.00 40.52           C  
ANISOU  727  CB  PRO A 111     4526   6141   4730   -467   -396   -114       C  
ATOM    728  CG  PRO A 111      -0.050  67.622  -2.363  1.00 38.24           C  
ANISOU  728  CG  PRO A 111     4254   5903   4373   -491   -400   -135       C  
ATOM    729  CD  PRO A 111      -0.285  69.056  -2.805  1.00 43.61           C  
ANISOU  729  CD  PRO A 111     4831   6670   5067   -434   -404    -29       C  
ATOM    730  N   GLU A 112       0.912  68.946   1.629  1.00 40.19           N  
ANISOU  730  N   GLU A 112     4497   5873   4902   -220   -304   -106       N  
ATOM    731  CA  GLU A 112       2.148  69.170   2.368  1.00 39.61           C  
ANISOU  731  CA  GLU A 112     4469   5699   4883   -146   -267   -148       C  
ATOM    732  C   GLU A 112       2.161  68.387   3.665  1.00 42.94           C  
ANISOU  732  C   GLU A 112     4937   6029   5349   -135   -257   -191       C  
ATOM    733  O   GLU A 112       1.118  68.149   4.282  1.00 43.00           O  
ANISOU  733  O   GLU A 112     4924   6044   5371   -160   -269   -162       O  
ATOM    734  CB  GLU A 112       2.350  70.646   2.714  1.00 39.42           C  
ANISOU  734  CB  GLU A 112     4406   5667   4906    -75   -244    -79       C  
ATOM    735  CG  GLU A 112       2.756  71.530   1.562  1.00 43.46           C  
ANISOU  735  CG  GLU A 112     4891   6240   5382    -70   -243    -43       C  
ATOM    736  CD  GLU A 112       3.102  72.919   2.028  1.00 52.67           C  
ANISOU  736  CD  GLU A 112     6054   7369   6591     -7   -213     15       C  
ATOM    737  OE1 GLU A 112       2.685  73.289   3.147  1.00 56.52           O  
ANISOU  737  OE1 GLU A 112     6548   7799   7129     33   -195     43       O  
ATOM    738  OE2 GLU A 112       3.782  73.641   1.274  1.00 56.94           O  
ANISOU  738  OE2 GLU A 112     6594   7932   7108     -2   -205     32       O  
ATOM    739  N   ILE A 113       3.366  68.038   4.099  1.00 37.62           N  
ANISOU  739  N   ILE A 113     4318   5281   4696    -94   -232   -251       N  
ATOM    740  CA  ILE A 113       3.567  67.572   5.461  1.00 34.08           C  
ANISOU  740  CA  ILE A 113     3907   4745   4299    -62   -217   -277       C  
ATOM    741  C   ILE A 113       3.656  68.808   6.355  1.00 36.51           C  
ANISOU  741  C   ILE A 113     4178   5030   4665     -7   -199   -222       C  
ATOM    742  O   ILE A 113       4.516  69.673   6.164  1.00 32.90           O  
ANISOU  742  O   ILE A 113     3710   4576   4213     25   -184   -209       O  
ATOM    743  CB  ILE A 113       4.821  66.695   5.571  1.00 33.47           C  
ANISOU  743  CB  ILE A 113     3897   4610   4211    -30   -195   -351       C  
ATOM    744  CG1 ILE A 113       4.572  65.315   4.915  1.00 27.55           C  
ANISOU  744  CG1 ILE A 113     3220   3847   3400    -83   -202   -412       C  
ATOM    745  CG2 ILE A 113       5.218  66.526   7.035  1.00 30.43           C  
ANISOU  745  CG2 ILE A 113     3534   4146   3882     17   -179   -360       C  
ATOM    746  CD1 ILE A 113       5.797  64.600   4.488  1.00 21.89           C  
ANISOU  746  CD1 ILE A 113     2568   3100   2648    -38   -172   -475       C  
ATOM    747  N   ALA A 114       2.723  68.925   7.293  1.00 32.84           N  
ANISOU  747  N   ALA A 114     3699   4544   4235     -4   -199   -187       N  
ATOM    748  CA  ALA A 114       2.737  70.052   8.217  1.00 31.78           C  
ANISOU  748  CA  ALA A 114     3553   4372   4148     49   -174   -139       C  
ATOM    749  C   ALA A 114       3.593  69.758   9.439  1.00 32.37           C  
ANISOU  749  C   ALA A 114     3677   4363   4259     75   -157   -182       C  
ATOM    750  O   ALA A 114       4.213  70.670   9.998  1.00 31.27           O  
ANISOU  750  O   ALA A 114     3549   4190   4142    106   -136   -165       O  
ATOM    751  CB  ALA A 114       1.308  70.393   8.655  1.00 20.86           C  
ANISOU  751  CB  ALA A 114     2129   3016   2780     54   -172    -73       C  
ATOM    752  N   VAL A 115       3.648  68.496   9.851  1.00 33.21           N  
ANISOU  752  N   VAL A 115     3818   4436   4365     58   -166   -233       N  
ATOM    753  CA  VAL A 115       4.325  68.083  11.075  1.00 30.31           C  
ANISOU  753  CA  VAL A 115     3493   3997   4028     86   -153   -264       C  
ATOM    754  C   VAL A 115       4.913  66.711  10.828  1.00 25.25           C  
ANISOU  754  C   VAL A 115     2899   3333   3360     81   -159   -327       C  
ATOM    755  O   VAL A 115       4.193  65.793  10.418  1.00 34.53           O  
ANISOU  755  O   VAL A 115     4100   4511   4510     38   -172   -348       O  
ATOM    756  CB  VAL A 115       3.354  68.037  12.280  1.00 29.31           C  
ANISOU  756  CB  VAL A 115     3370   3831   3935     86   -148   -239       C  
ATOM    757  CG1 VAL A 115       3.955  67.232  13.451  1.00 27.91           C  
ANISOU  757  CG1 VAL A 115     3242   3583   3777    102   -142   -279       C  
ATOM    758  CG2 VAL A 115       2.944  69.456  12.724  1.00 28.54           C  
ANISOU  758  CG2 VAL A 115     3248   3734   3862    115   -126   -178       C  
ATOM    759  N   ARG A 116       6.213  66.557  11.087  1.00 21.74           N  
ANISOU  759  N   ARG A 116     2472   2872   2917    125   -145   -354       N  
ATOM    760  CA  ARG A 116       6.855  65.246  11.025  1.00 33.86           C  
ANISOU  760  CA  ARG A 116     4063   4374   4427    150   -137   -406       C  
ATOM    761  C   ARG A 116       7.684  64.996  12.280  1.00 37.90           C  
ANISOU  761  C   ARG A 116     4590   4844   4965    201   -125   -410       C  
ATOM    762  O   ARG A 116       8.654  65.715  12.555  1.00 30.42           O  
ANISOU  762  O   ARG A 116     3604   3930   4023    228   -119   -391       O  
ATOM    763  CB  ARG A 116       7.735  65.106   9.786  1.00 33.95           C  
ANISOU  763  CB  ARG A 116     4072   4434   4392    170   -126   -431       C  
ATOM    764  CG  ARG A 116       8.092  63.664   9.548  1.00 31.23           C  
ANISOU  764  CG  ARG A 116     3808   4045   4011    199   -108   -485       C  
ATOM    765  CD  ARG A 116       9.562  63.454   9.326  1.00 30.11           C  
ANISOU  765  CD  ARG A 116     3663   3932   3847    280    -79   -498       C  
ATOM    766  NE  ARG A 116       9.789  62.202   8.600  1.00 36.66           N  
ANISOU  766  NE  ARG A 116     4582   4726   4622    311    -51   -551       N  
ATOM    767  CZ  ARG A 116      10.045  61.026   9.172  1.00 32.85           C  
ANISOU  767  CZ  ARG A 116     4186   4165   4131    365    -25   -579       C  
ATOM    768  NH1 ARG A 116      10.122  60.899  10.499  1.00 32.97           N  
ANISOU  768  NH1 ARG A 116     4198   4138   4189    393    -29   -558       N  
ATOM    769  NH2 ARG A 116      10.233  59.964   8.406  1.00 29.20           N  
ANISOU  769  NH2 ARG A 116     3825   3660   3609    394      9   -628       N  
ATOM    770  N   GLY A 117       7.316  63.965  13.028  1.00 41.81           N  
ANISOU  770  N   GLY A 117     5143   5274   5469    205   -123   -430       N  
ATOM    771  CA  GLY A 117       8.038  63.615  14.226  1.00 39.72           C  
ANISOU  771  CA  GLY A 117     4896   4972   5223    255   -113   -428       C  
ATOM    772  C   GLY A 117       9.255  62.784  13.884  1.00 43.85           C  
ANISOU  772  C   GLY A 117     5447   5502   5714    328    -91   -453       C  
ATOM    773  O   GLY A 117       9.634  62.614  12.721  1.00 36.29           O  
ANISOU  773  O   GLY A 117     4492   4578   4718    343    -79   -474       O  
ATOM    774  N   TYR A 118       9.884  62.257  14.933  1.00 34.92           N  
ANISOU  774  N   TYR A 118     4334   4342   4592    383    -82   -446       N  
ATOM    775  CA  TYR A 118      10.968  61.323  14.704  1.00 31.22           C  
ANISOU  775  CA  TYR A 118     3897   3876   4089    476    -52   -460       C  
ATOM    776  C   TYR A 118      10.414  60.027  14.135  1.00 37.71           C  
ANISOU  776  C   TYR A 118     4836   4613   4881    481    -32   -508       C  
ATOM    777  O   TYR A 118       9.223  59.720  14.267  1.00 37.88           O  
ANISOU  777  O   TYR A 118     4909   4572   4912    405    -47   -524       O  
ATOM    778  CB  TYR A 118      11.706  60.991  15.989  1.00 30.16           C  
ANISOU  778  CB  TYR A 118     3757   3736   3966    539    -47   -431       C  
ATOM    779  CG  TYR A 118      12.187  62.153  16.811  1.00 35.19           C  
ANISOU  779  CG  TYR A 118     4304   4444   4623    512    -71   -387       C  
ATOM    780  CD1 TYR A 118      13.010  63.129  16.265  1.00 23.03           C  
ANISOU  780  CD1 TYR A 118     2679   3007   3065    503    -75   -364       C  
ATOM    781  CD2 TYR A 118      11.869  62.232  18.173  1.00 34.51           C  
ANISOU  781  CD2 TYR A 118     4227   4321   4566    490    -86   -367       C  
ATOM    782  CE1 TYR A 118      13.478  64.183  17.043  1.00 36.15           C  
ANISOU  782  CE1 TYR A 118     4277   4727   4732    459    -96   -325       C  
ATOM    783  CE2 TYR A 118      12.336  63.267  18.955  1.00 36.66           C  
ANISOU  783  CE2 TYR A 118     4436   4650   4843    455   -105   -330       C  
ATOM    784  CZ  TYR A 118      13.132  64.249  18.390  1.00 37.95           C  
ANISOU  784  CZ  TYR A 118     4525   4909   4984    434   -111   -311       C  
ATOM    785  OH  TYR A 118      13.579  65.280  19.187  1.00 30.59           O  
ANISOU  785  OH  TYR A 118     3551   4027   4047    378   -130   -277       O  
ATOM    786  N   ASP A 119      11.292  59.249  13.504  1.00 26.83           N  
ANISOU  786  N   ASP A 119     3503   3234   3458    568      7   -528       N  
ATOM    787  CA  ASP A 119      10.914  57.881  13.199  1.00 38.96           C  
ANISOU  787  CA  ASP A 119     5184   4663   4957    585     37   -574       C  
ATOM    788  C   ASP A 119      10.744  57.144  14.516  1.00 34.87           C  
ANISOU  788  C   ASP A 119     4727   4059   4461    610     40   -561       C  
ATOM    789  O   ASP A 119      11.486  57.392  15.471  1.00 34.79           O  
ANISOU  789  O   ASP A 119     4655   4088   4476    675     38   -517       O  
ATOM    790  CB  ASP A 119      11.970  57.199  12.305  1.00 36.55           C  
ANISOU  790  CB  ASP A 119     4928   4365   4592    697     93   -595       C  
ATOM    791  CG  ASP A 119      11.884  57.628  10.833  1.00 38.10           C  
ANISOU  791  CG  ASP A 119     5107   4618   4750    653     95   -624       C  
ATOM    792  OD1 ASP A 119      12.562  56.997   9.992  1.00 40.19           O  
ANISOU  792  OD1 ASP A 119     5435   4878   4957    733    146   -651       O  
ATOM    793  OD2 ASP A 119      11.134  58.571  10.491  1.00 37.86           O  
ANISOU  793  OD2 ASP A 119     5008   4637   4741    545     51   -617       O  
ATOM    794  N   LYS A 120       9.744  56.271  14.588  1.00 35.99           N  
ANISOU  794  N   LYS A 120     4990   4094   4590    546     40   -594       N  
ATOM    795  CA  LYS A 120       9.612  55.435  15.774  1.00 44.61           C  
ANISOU  795  CA  LYS A 120     6161   5095   5695    573     49   -583       C  
ATOM    796  C   LYS A 120      10.956  54.787  16.083  1.00 47.83           C  
ANISOU  796  C   LYS A 120     6598   5493   6081    736     97   -563       C  
ATOM    797  O   LYS A 120      11.530  54.084  15.243  1.00 49.39           O  
ANISOU  797  O   LYS A 120     6878   5660   6227    817    146   -590       O  
ATOM    798  CB  LYS A 120       8.527  54.371  15.571  1.00 44.44           C  
ANISOU  798  CB  LYS A 120     6295   4952   5638    484     55   -627       C  
ATOM    799  CG  LYS A 120       8.275  53.483  16.788  1.00 54.28           C  
ANISOU  799  CG  LYS A 120     7636   6095   6895    496     63   -614       C  
ATOM    800  CD  LYS A 120       7.146  54.044  17.664  1.00 61.14           C  
ANISOU  800  CD  LYS A 120     8437   6983   7809    378     14   -588       C  
ATOM    801  CE  LYS A 120       7.010  53.300  18.987  1.00 57.03           C  
ANISOU  801  CE  LYS A 120     7990   6377   7303    395     21   -566       C  
ATOM    802  NZ  LYS A 120       8.335  53.190  19.657  1.00 54.91           N  
ANISOU  802  NZ  LYS A 120     7699   6119   7044    551     47   -531       N  
ATOM    803  N   PHE A 121      11.493  55.073  17.262  1.00 39.60           N  
ANISOU  803  N   PHE A 121     5482   4490   5073    790     85   -510       N  
ATOM    804  CA  PHE A 121      12.735  54.446  17.677  1.00 40.01           C  
ANISOU  804  CA  PHE A 121     5545   4553   5102    949    127   -474       C  
ATOM    805  C   PHE A 121      12.467  53.583  18.900  1.00 45.26           C  
ANISOU  805  C   PHE A 121     6302   5118   5778    973    132   -455       C  
ATOM    806  O   PHE A 121      11.398  53.645  19.514  1.00 36.45           O  
ANISOU  806  O   PHE A 121     5212   3945   4691    860     98   -464       O  
ATOM    807  CB  PHE A 121      13.848  55.484  17.920  1.00 41.88           C  
ANISOU  807  CB  PHE A 121     5608   4952   5352   1001    110   -417       C  
ATOM    808  CG  PHE A 121      13.531  56.534  18.967  1.00 48.02           C  
ANISOU  808  CG  PHE A 121     6279   5787   6178    909     53   -383       C  
ATOM    809  CD1 PHE A 121      12.939  57.737  18.604  1.00 40.07           C  
ANISOU  809  CD1 PHE A 121     5196   4830   5198    790     14   -396       C  
ATOM    810  CD2 PHE A 121      13.889  56.346  20.302  1.00 47.90           C  
ANISOU  810  CD2 PHE A 121     6246   5778   6175    949     43   -335       C  
ATOM    811  CE1 PHE A 121      12.665  58.716  19.550  1.00 34.39           C  
ANISOU  811  CE1 PHE A 121     4402   4151   4515    714    -26   -367       C  
ATOM    812  CE2 PHE A 121      13.618  57.333  21.255  1.00 38.83           C  
ANISOU  812  CE2 PHE A 121     5014   4678   5060    860     -4   -308       C  
ATOM    813  CZ  PHE A 121      12.998  58.516  20.875  1.00 29.50           C  
ANISOU  813  CZ  PHE A 121     3774   3532   3904    744    -35   -327       C  
ATOM    814  N   PHE A 122      13.431  52.728  19.220  1.00 53.44           N  
ANISOU  814  N   PHE A 122     7389   6133   6784   1129    180   -422       N  
ATOM    815  CA  PHE A 122      13.184  51.643  20.154  1.00 52.66           C  
ANISOU  815  CA  PHE A 122     7421   5909   6678   1169    200   -409       C  
ATOM    816  C   PHE A 122      14.288  51.563  21.194  1.00 51.40           C  
ANISOU  816  C   PHE A 122     7185   5825   6519   1306    208   -327       C  
ATOM    817  O   PHE A 122      15.411  52.044  20.995  1.00 46.26           O  
ANISOU  817  O   PHE A 122     6408   5314   5855   1400    216   -283       O  
ATOM    818  CB  PHE A 122      13.030  50.304  19.411  1.00 47.63           C  
ANISOU  818  CB  PHE A 122     6999   5116   5984   1224    267   -457       C  
ATOM    819  CG  PHE A 122      11.701  50.160  18.717  1.00 42.80           C  
ANISOU  819  CG  PHE A 122     6490   4410   5362   1052    249   -531       C  
ATOM    820  CD1 PHE A 122      11.584  50.376  17.354  1.00 43.86           C  
ANISOU  820  CD1 PHE A 122     6636   4564   5464   1011    260   -584       C  
ATOM    821  CD2 PHE A 122      10.558  49.859  19.438  1.00 40.83           C  
ANISOU  821  CD2 PHE A 122     6312   4072   5131    923    218   -542       C  
ATOM    822  CE1 PHE A 122      10.354  50.254  16.713  1.00 49.90           C  
ANISOU  822  CE1 PHE A 122     7484   5264   6211    842    237   -644       C  
ATOM    823  CE2 PHE A 122       9.324  49.746  18.808  1.00 49.59           C  
ANISOU  823  CE2 PHE A 122     7496   5123   6222    754    196   -599       C  
ATOM    824  CZ  PHE A 122       9.223  49.939  17.443  1.00 54.03           C  
ANISOU  824  CZ  PHE A 122     8071   5710   6749    712    204   -648       C  
ATOM    825  N   ASN A 123      13.940  50.948  22.320  1.00 49.19           N  
ANISOU  825  N   ASN A 123     6980   5461   6250   1307    204   -302       N  
ATOM    826  CA  ASN A 123      14.873  50.807  23.422  1.00 49.42           C  
ANISOU  826  CA  ASN A 123     6944   5560   6275   1426    205   -218       C  
ATOM    827  C   ASN A 123      15.822  49.633  23.169  1.00 48.31           C  
ANISOU  827  C   ASN A 123     6903   5372   6078   1634    285   -184       C  
ATOM    828  O   ASN A 123      15.538  48.739  22.370  1.00 49.15           O  
ANISOU  828  O   ASN A 123     7183   5340   6151   1670    342   -236       O  
ATOM    829  CB  ASN A 123      14.102  50.638  24.733  1.00 52.58           C  
ANISOU  829  CB  ASN A 123     7384   5891   6704   1343    170   -202       C  
ATOM    830  CG  ASN A 123      15.009  50.402  25.915  1.00 51.67           C  
ANISOU  830  CG  ASN A 123     7213   5843   6576   1461    170   -112       C  
ATOM    831  OD1 ASN A 123      15.539  51.341  26.510  1.00 48.96           O  
ANISOU  831  OD1 ASN A 123     6706   5653   6245   1439    124    -64       O  
ATOM    832  ND2 ASN A 123      15.214  49.138  26.246  1.00 54.67           N  
ANISOU  832  ND2 ASN A 123     7738   6110   6924   1584    221    -84       N  
ATOM    833  N   ILE A 124      16.983  49.671  23.834  1.00 54.72           N  
ANISOU  833  N   ILE A 124     7606   6312   6875   1773    291    -93       N  
ATOM    834  CA  ILE A 124      17.952  48.580  23.753  1.00 60.09           C  
ANISOU  834  CA  ILE A 124     8364   6967   7499   2001    371    -38       C  
ATOM    835  C   ILE A 124      17.257  47.254  24.023  1.00 61.98           C  
ANISOU  835  C   ILE A 124     8853   6974   7722   2030    420    -66       C  
ATOM    836  O   ILE A 124      16.480  47.130  24.977  1.00 61.34           O  
ANISOU  836  O   ILE A 124     8821   6817   7670   1927    381    -66       O  
ATOM    837  CB  ILE A 124      19.115  48.810  24.741  1.00 59.31           C  
ANISOU  837  CB  ILE A 124     8100   7049   7387   2121    354     81       C  
ATOM    838  CG1 ILE A 124      20.101  49.842  24.194  1.00 61.44           C  
ANISOU  838  CG1 ILE A 124     8152   7550   7643   2138    334    117       C  
ATOM    839  CG2 ILE A 124      19.871  47.507  25.010  1.00 52.15           C  
ANISOU  839  CG2 ILE A 124     7303   6085   6427   2361    437    153       C  
ATOM    840  CD1 ILE A 124      20.862  49.373  22.975  1.00 62.03           C  
ANISOU  840  CD1 ILE A 124     8254   7646   7668   2304    417    116       C  
ATOM    841  N   ASP A 125      17.529  46.263  23.166  1.00 61.42           N  
ANISOU  841  N   ASP A 125     8951   6787   7597   2165    509    -90       N  
ATOM    842  CA  ASP A 125      17.052  44.884  23.248  1.00 60.85           C  
ANISOU  842  CA  ASP A 125     9153   6479   7489   2217    576   -115       C  
ATOM    843  C   ASP A 125      15.554  44.753  23.008  1.00 62.24           C  
ANISOU  843  C   ASP A 125     9476   6492   7681   1988    544   -216       C  
ATOM    844  O   ASP A 125      15.004  43.652  23.161  1.00 68.74           O  
ANISOU  844  O   ASP A 125    10533   7113   8470   1982    587   -241       O  
ATOM    845  CB  ASP A 125      17.405  44.229  24.586  1.00 62.37           C  
ANISOU  845  CB  ASP A 125     9373   6650   7676   2324    584    -22       C  
ATOM    846  CG  ASP A 125      18.899  44.150  24.822  1.00 67.54           C  
ANISOU  846  CG  ASP A 125     9880   7487   8296   2526    616     92       C  
ATOM    847  OD1 ASP A 125      19.331  44.385  25.970  1.00 74.30           O  
ANISOU  847  OD1 ASP A 125    10614   8450   9166   2577    578    183       O  
ATOM    848  OD2 ASP A 125      19.645  43.846  23.866  1.00 69.94           O  
ANISOU  848  OD2 ASP A 125    10188   7835   8553   2628    678     96       O  
ATOM    849  N   GLU A 126      14.877  45.838  22.633  1.00 58.04           N  
ANISOU  849  N   GLU A 126     8813   6046   7194   1797    470   -268       N  
ATOM    850  CA  GLU A 126      13.452  45.775  22.346  1.00 58.45           C  
ANISOU  850  CA  GLU A 126     8975   5977   7255   1579    437   -352       C  
ATOM    851  C   GLU A 126      13.187  45.295  20.927  1.00 60.93           C  
ANISOU  851  C   GLU A 126     9445   6190   7514   1555    488   -435       C  
ATOM    852  O   GLU A 126      12.116  44.743  20.656  1.00 68.05           O  
ANISOU  852  O   GLU A 126    10517   6947   8391   1408    486   -499       O  
ATOM    853  CB  GLU A 126      12.814  47.151  22.588  1.00 59.56           C  
ANISOU  853  CB  GLU A 126     8910   6257   7462   1400    343   -360       C  
ATOM    854  CG  GLU A 126      11.356  47.277  22.171  1.00 67.12           C  
ANISOU  854  CG  GLU A 126     9933   7141   8428   1179    304   -435       C  
ATOM    855  CD  GLU A 126      10.749  48.628  22.527  1.00 72.02           C  
ANISOU  855  CD  GLU A 126    10356   7897   9113   1034    223   -429       C  
ATOM    856  OE1 GLU A 126      11.503  49.603  22.770  1.00 70.13           O  
ANISOU  856  OE1 GLU A 126     9933   7809   8905   1088    198   -386       O  
ATOM    857  OE2 GLU A 126       9.503  48.712  22.535  1.00 77.73           O  
ANISOU  857  OE2 GLU A 126    11112   8574   9846    863    189   -465       O  
ATOM    858  N   THR A 127      14.140  45.484  20.020  1.00 60.19           N  
ANISOU  858  N   THR A 127     9298   6178   7392   1688    532   -433       N  
ATOM    859  CA  THR A 127      14.030  44.976  18.663  1.00 57.74           C  
ANISOU  859  CA  THR A 127     9148   5773   7018   1688    591   -510       C  
ATOM    860  C   THR A 127      15.350  44.349  18.253  1.00 57.75           C  
ANISOU  860  C   THR A 127     9196   5782   6963   1941    689   -469       C  
ATOM    861  O   THR A 127      16.384  44.520  18.902  1.00 60.36           O  
ANISOU  861  O   THR A 127     9386   6239   7311   2102    698   -377       O  
ATOM    862  CB  THR A 127      13.674  46.064  17.648  1.00 57.26           C  
ANISOU  862  CB  THR A 127     8946   5834   6975   1549    539   -561       C  
ATOM    863  OG1 THR A 127      14.765  46.989  17.557  1.00 58.83           O  
ANISOU  863  OG1 THR A 127     8918   6235   7201   1662    530   -504       O  
ATOM    864  CG2 THR A 127      12.399  46.793  18.041  1.00 54.62           C  
ANISOU  864  CG2 THR A 127     8530   5526   6697   1310    443   -584       C  
ATOM    865  N   ARG A 128      15.290  43.622  17.143  1.00 59.42           N  
ANISOU  865  N   ARG A 128     9568   5903   7106   1925    747   -524       N  
ATOM    866  CA  ARG A 128      16.483  43.023  16.565  1.00 66.40           C  
ANISOU  866  CA  ARG A 128    10470   6827   7931   2115    832   -480       C  
ATOM    867  C   ARG A 128      17.554  44.073  16.277  1.00 66.34           C  
ANISOU  867  C   ARG A 128    10217   7042   7947   2245    828   -432       C  
ATOM    868  O   ARG A 128      18.750  43.817  16.461  1.00 63.93           O  
ANISOU  868  O   ARG A 128     9832   6840   7619   2431    875   -343       O  
ATOM    869  CB  ARG A 128      16.097  42.250  15.296  1.00 80.98           C  
ANISOU  869  CB  ARG A 128    12530   8541   9699   2046    887   -562       C  
ATOM    870  CG  ARG A 128      15.552  43.101  14.114  1.00 98.36           C  
ANISOU  870  CG  ARG A 128    14695  10783  11896   1914    856   -655       C  
ATOM    871  CD  ARG A 128      14.203  43.815  14.383  1.00102.49           C  
ANISOU  871  CD  ARG A 128    15200  11276  12467   1687    764   -718       C  
ATOM    872  NE  ARG A 128      13.179  42.914  14.919  1.00102.11           N  
ANISOU  872  NE  ARG A 128    15337  11058  12402   1538    749   -740       N  
ATOM    873  CZ  ARG A 128      11.960  43.298  15.286  1.00 90.39           C  
ANISOU  873  CZ  ARG A 128    13859   9537  10949   1334    674   -781       C  
ATOM    874  NH1 ARG A 128      11.606  44.570  15.162  1.00 96.45           N  
ANISOU  874  NH1 ARG A 128    14412  10458  11776   1229    593   -785       N  
ATOM    875  NH2 ARG A 128      11.093  42.412  15.762  1.00 73.52           N  
ANISOU  875  NH2 ARG A 128    11884   7262   8788   1201    665   -790       N  
ATOM    876  N   ASP A 129      17.145  45.274  15.851  1.00 69.87           N  
ANISOU  876  N   ASP A 129    10536   7578   8433   2146    771   -483       N  
ATOM    877  CA  ASP A 129      18.121  46.306  15.509  1.00 68.22           C  
ANISOU  877  CA  ASP A 129    10083   7596   8239   2235    760   -435       C  
ATOM    878  C   ASP A 129      18.735  46.950  16.746  1.00 63.27           C  
ANISOU  878  C   ASP A 129     9233   7138   7669   2282    703   -330       C  
ATOM    879  O   ASP A 129      19.852  47.475  16.679  1.00 67.27           O  
ANISOU  879  O   ASP A 129     9553   7838   8168   2404    713   -259       O  
ATOM    880  CB  ASP A 129      17.473  47.375  14.637  1.00 71.99           C  
ANISOU  880  CB  ASP A 129    10456   8156   8743   2031    690   -500       C  
ATOM    881  CG  ASP A 129      17.401  46.974  13.191  1.00 78.19           C  
ANISOU  881  CG  ASP A 129    11386   8868   9455   2037    755   -580       C  
ATOM    882  OD1 ASP A 129      18.019  45.955  12.833  1.00 84.81           O  
ANISOU  882  OD1 ASP A 129    12378   9620  10225   2204    854   -575       O  
ATOM    883  OD2 ASP A 129      16.727  47.677  12.411  1.00 82.23           O  
ANISOU  883  OD2 ASP A 129    11852   9417   9976   1863    702   -639       O  
ATOM    884  N   THR A 130      18.028  46.937  17.875  1.00 54.47           N  
ANISOU  884  N   THR A 130     8130   5964   6604   2176    643   -318       N  
ATOM    885  CA  THR A 130      18.526  47.567  19.085  1.00 59.03           C  
ANISOU  885  CA  THR A 130     8508   6693   7226   2196    584   -225       C  
ATOM    886  C   THR A 130      19.164  46.571  20.040  1.00 62.41           C  
ANISOU  886  C   THR A 130     9010   7074   7628   2389    638   -141       C  
ATOM    887  O   THR A 130      19.317  46.874  21.229  1.00 65.31           O  
ANISOU  887  O   THR A 130     9264   7522   8030   2378    585    -71       O  
ATOM    888  CB  THR A 130      17.409  48.333  19.786  1.00 55.21           C  
ANISOU  888  CB  THR A 130     7964   6202   6811   1963    483   -253       C  
ATOM    889  OG1 THR A 130      16.244  47.506  19.857  1.00 58.31           O  
ANISOU  889  OG1 THR A 130     8575   6381   7201   1864    492   -319       O  
ATOM    890  CG2 THR A 130      17.084  49.607  19.017  1.00 47.79           C  
ANISOU  890  CG2 THR A 130     6878   5377   5901   1806    424   -297       C  
ATOM    891  N   ALA A 131      19.518  45.386  19.556  1.00 61.20           N  
ANISOU  891  N   ALA A 131     9031   6810   7412   2512    729   -141       N  
ATOM    892  CA  ALA A 131      20.476  44.562  20.278  1.00 62.41           C  
ANISOU  892  CA  ALA A 131     9181   7003   7528   2676    773    -33       C  
ATOM    893  C   ALA A 131      21.856  45.195  20.166  1.00 59.24           C  
ANISOU  893  C   ALA A 131     8538   6861   7107   2813    779     62       C  
ATOM    894  O   ALA A 131      22.241  45.693  19.102  1.00 58.43           O  
ANISOU  894  O   ALA A 131     8362   6852   6987   2826    797     36       O  
ATOM    895  CB  ALA A 131      20.503  43.136  19.720  1.00 58.16           C  
ANISOU  895  CB  ALA A 131     8890   6291   6918   2741    866    -54       C  
ATOM    896  N   TRP A 132      22.605  45.180  21.268  1.00 54.40           N  
ANISOU  896  N   TRP A 132     7799   6377   6493   2904    761    176       N  
ATOM    897  CA  TRP A 132      23.918  45.814  21.264  1.00 60.08           C  
ANISOU  897  CA  TRP A 132     8272   7370   7187   3007    755    277       C  
ATOM    898  C   TRP A 132      24.759  45.341  20.081  1.00 69.14           C  
ANISOU  898  C   TRP A 132     9449   8558   8263   3132    843    287       C  
ATOM    899  O   TRP A 132      25.335  46.155  19.351  1.00 74.66           O  
ANISOU  899  O   TRP A 132     9985   9429   8952   3133    835    295       O  
ATOM    900  CB  TRP A 132      24.634  45.550  22.589  1.00 56.97           C  
ANISOU  900  CB  TRP A 132     7780   7089   6776   3098    738    404       C  
ATOM    901  CG  TRP A 132      24.313  46.573  23.639  1.00 54.04           C  
ANISOU  901  CG  TRP A 132     7248   6821   6464   2986    635    429       C  
ATOM    902  CD1 TRP A 132      23.747  46.342  24.856  1.00 60.50           C  
ANISOU  902  CD1 TRP A 132     8118   7555   7313   2944    593    449       C  
ATOM    903  CD2 TRP A 132      24.528  47.988  23.559  1.00 56.52           C  
ANISOU  903  CD2 TRP A 132     7329   7340   6805   2896    560    438       C  
ATOM    904  NE1 TRP A 132      23.602  47.520  25.545  1.00 66.36           N  
ANISOU  904  NE1 TRP A 132     8679   8437   8098   2841    498    470       N  
ATOM    905  CE2 TRP A 132      24.074  48.548  24.772  1.00 65.64           C  
ANISOU  905  CE2 TRP A 132     8412   8524   8005   2797    474    462       C  
ATOM    906  CE3 TRP A 132      25.064  48.837  22.582  1.00 52.99           C  
ANISOU  906  CE3 TRP A 132     6732   7057   6345   2877    556    429       C  
ATOM    907  CZ2 TRP A 132      24.135  49.918  25.034  1.00 64.14           C  
ANISOU  907  CZ2 TRP A 132     8021   8511   7838   2605    378    465       C  
ATOM    908  CZ3 TRP A 132      25.125  50.190  22.839  1.00 53.09           C  
ANISOU  908  CZ3 TRP A 132     6538   7249   6385   2735    466    442       C  
ATOM    909  CH2 TRP A 132      24.663  50.721  24.058  1.00 62.27           C  
ANISOU  909  CH2 TRP A 132     7649   8425   7585   2575    375    455       C  
ATOM    910  N   SER A 133      24.803  44.024  19.852  1.00 69.27           N  
ANISOU  910  N   SER A 133     9682   8411   8225   3231    929    284       N  
ATOM    911  CA  SER A 133      25.581  43.487  18.737  1.00 71.08           C  
ANISOU  911  CA  SER A 133     9964   8662   8379   3361   1021    294       C  
ATOM    912  C   SER A 133      25.108  44.043  17.394  1.00 67.27           C  
ANISOU  912  C   SER A 133     9508   8145   7905   3263   1023    184       C  
ATOM    913  O   SER A 133      25.925  44.326  16.511  1.00 60.21           O  
ANISOU  913  O   SER A 133     8518   7390   6970   3339   1060    208       O  
ATOM    914  CB  SER A 133      25.511  41.962  18.743  1.00 72.12           C  
ANISOU  914  CB  SER A 133    10361   8589   8450   3463   1112    297       C  
ATOM    915  OG  SER A 133      24.167  41.516  18.780  1.00 69.81           O  
ANISOU  915  OG  SER A 133    10293   8043   8189   3318   1097    189       O  
ATOM    916  N   ALA A 134      23.796  44.213  17.222  1.00 67.43           N  
ANISOU  916  N   ALA A 134     9655   7992   7975   3093    983     67       N  
ATOM    917  CA  ALA A 134      23.288  44.817  15.994  1.00 55.42           C  
ANISOU  917  CA  ALA A 134     8148   6449   6460   2988    977    -36       C  
ATOM    918  C   ALA A 134      23.788  46.247  15.832  1.00 54.35           C  
ANISOU  918  C   ALA A 134     7732   6560   6356   2960    918     -7       C  
ATOM    919  O   ALA A 134      24.188  46.653  14.733  1.00 59.22           O  
ANISOU  919  O   ALA A 134     8291   7266   6943   2976    945    -30       O  
ATOM    920  CB  ALA A 134      21.759  44.787  15.985  1.00 53.23           C  
ANISOU  920  CB  ALA A 134     8040   5961   6224   2797    935   -155       C  
ATOM    921  N   ILE A 135      23.781  47.023  16.918  1.00 48.01           N  
ANISOU  921  N   ILE A 135     6758   5874   5609   2912    838     45       N  
ATOM    922  CA  ILE A 135      24.186  48.424  16.843  1.00 54.28           C  
ANISOU  922  CA  ILE A 135     7292   6901   6431   2859    774     73       C  
ATOM    923  C   ILE A 135      25.669  48.542  16.517  1.00 63.86           C  
ANISOU  923  C   ILE A 135     8332   8349   7584   2990    811    179       C  
ATOM    924  O   ILE A 135      26.064  49.306  15.628  1.00 68.48           O  
ANISOU  924  O   ILE A 135     8793   9074   8153   2968    810    170       O  
ATOM    925  CB  ILE A 135      23.847  49.148  18.155  1.00 54.50           C  
ANISOU  925  CB  ILE A 135     7193   6993   6522   2774    682    110       C  
ATOM    926  CG1 ILE A 135      22.337  49.201  18.358  1.00 48.39           C  
ANISOU  926  CG1 ILE A 135     6568   6011   5806   2569    627      4       C  
ATOM    927  CG2 ILE A 135      24.460  50.537  18.162  1.00 53.47           C  
ANISOU  927  CG2 ILE A 135     6788   7126   6403   2684    609    160       C  
ATOM    928  CD1 ILE A 135      21.968  49.803  19.656  1.00 50.49           C  
ANISOU  928  CD1 ILE A 135     6734   6322   6127   2434    532     40       C  
ATOM    929  N   ARG A 136      26.515  47.809  17.251  1.00 64.88           N  
ANISOU  929  N   ARG A 136     8445   8534   7672   3124    843    287       N  
ATOM    930  CA  ARG A 136      27.941  47.786  16.939  1.00 67.46           C  
ANISOU  930  CA  ARG A 136     8624   9081   7928   3259    886    395       C  
ATOM    931  C   ARG A 136      28.162  47.540  15.459  1.00 62.17           C  
ANISOU  931  C   ARG A 136     8035   8379   7208   3313    963    343       C  
ATOM    932  O   ARG A 136      28.985  48.206  14.821  1.00 66.93           O  
ANISOU  932  O   ARG A 136     8467   9188   7778   3330    965    385       O  
ATOM    933  CB  ARG A 136      28.649  46.698  17.754  1.00 79.84           C  
ANISOU  933  CB  ARG A 136    10243  10649   9444   3419    937    500       C  
ATOM    934  CG  ARG A 136      29.424  47.186  18.967  1.00 89.71           C  
ANISOU  934  CG  ARG A 136    11270  12128  10689   3428    876    628       C  
ATOM    935  CD  ARG A 136      30.169  46.036  19.643  1.00 98.27           C  
ANISOU  935  CD  ARG A 136    12414  13216  11709   3607    940    735       C  
ATOM    936  NE  ARG A 136      29.705  45.815  21.012  1.00105.31           N  
ANISOU  936  NE  ARG A 136    13332  14043  12639   3571    890    761       N  
ATOM    937  CZ  ARG A 136      28.894  44.828  21.381  1.00109.57           C  
ANISOU  937  CZ  ARG A 136    14107  14327  13197   3591    922    712       C  
ATOM    938  NH1 ARG A 136      28.458  43.955  20.482  1.00111.13           N  
ANISOU  938  NH1 ARG A 136    14541  14310  13374   3638   1003    632       N  
ATOM    939  NH2 ARG A 136      28.520  44.709  22.651  1.00110.52           N  
ANISOU  939  NH2 ARG A 136    14232  14411  13350   3554    873    744       N  
ATOM    940  N   GLU A 137      27.399  46.610  14.889  1.00 64.19           N  
ANISOU  940  N   GLU A 137     8555   8379   7455   3323   1022    249       N  
ATOM    941  CA  GLU A 137      27.653  46.168  13.526  1.00 81.30           C  
ANISOU  941  CA  GLU A 137    10832  10498   9561   3391   1106    205       C  
ATOM    942  C   GLU A 137      27.197  47.206  12.504  1.00 89.13           C  
ANISOU  942  C   GLU A 137    11755  11533  10577   3259   1072    115       C  
ATOM    943  O   GLU A 137      27.940  47.532  11.573  1.00 93.11           O  
ANISOU  943  O   GLU A 137    12166  12176  11035   3311   1107    136       O  
ATOM    944  CB  GLU A 137      26.967  44.820  13.286  1.00 86.63           C  
ANISOU  944  CB  GLU A 137    11824  10883  10208   3423   1177    135       C  
ATOM    945  CG  GLU A 137      27.109  44.288  11.865  1.00 97.18           C  
ANISOU  945  CG  GLU A 137    13310  12139  11475   3479   1266     78       C  
ATOM    946  CD  GLU A 137      27.521  42.819  11.803  1.00104.46           C  
ANISOU  946  CD  GLU A 137    14448  12924  12319   3644   1371    116       C  
ATOM    947  OE1 GLU A 137      28.683  42.534  11.435  1.00107.29           O  
ANISOU  947  OE1 GLU A 137    14745  13412  12607   3818   1441    204       O  
ATOM    948  OE2 GLU A 137      26.681  41.947  12.112  1.00105.72           O  
ANISOU  948  OE2 GLU A 137    14842  12849  12480   3598   1387     61       O  
ATOM    949  N   ARG A 138      25.994  47.761  12.673  1.00 86.09           N  
ANISOU  949  N   ARG A 138    11409  11040  10261   3091   1005     20       N  
ATOM    950  CA  ARG A 138      25.330  48.493  11.599  1.00 76.55           C  
ANISOU  950  CA  ARG A 138    10209   9812   9064   2968    988    -86       C  
ATOM    951  C   ARG A 138      25.309  50.008  11.768  1.00 64.72           C  
ANISOU  951  C   ARG A 138     8465   8510   7616   2856    901    -75       C  
ATOM    952  O   ARG A 138      24.765  50.690  10.899  1.00 60.62           O  
ANISOU  952  O   ARG A 138     7939   7989   7103   2756    885   -157       O  
ATOM    953  CB  ARG A 138      23.888  48.000  11.436  1.00 80.51           C  
ANISOU  953  CB  ARG A 138    10960  10042   9587   2846    983   -213       C  
ATOM    954  CG  ARG A 138      23.750  46.677  10.716  1.00 87.96           C  
ANISOU  954  CG  ARG A 138    12171  10787  10464   2904   1073   -262       C  
ATOM    955  CD  ARG A 138      22.354  46.106  10.895  1.00 95.13           C  
ANISOU  955  CD  ARG A 138    13315  11440  11391   2761   1053   -363       C  
ATOM    956  NE  ARG A 138      22.389  44.659  11.092  1.00104.60           N  
ANISOU  956  NE  ARG A 138    14742  12461  12541   2839   1122   -350       N  
ATOM    957  CZ  ARG A 138      22.262  43.767  10.113  1.00107.98           C  
ANISOU  957  CZ  ARG A 138    15386  12746  12896   2851   1197   -407       C  
ATOM    958  NH1 ARG A 138      22.094  44.175   8.862  1.00108.55           N  
ANISOU  958  NH1 ARG A 138    15472  12836  12936   2790   1211   -483       N  
ATOM    959  NH2 ARG A 138      22.309  42.468  10.382  1.00108.00           N  
ANISOU  959  NH2 ARG A 138    15595  12590  12850   2924   1260   -388       N  
ATOM    960  N   THR A 139      25.855  50.563  12.846  1.00 61.98           N  
ANISOU  960  N   THR A 139     7921   8331   7298   2859    842     24       N  
ATOM    961  CA  THR A 139      25.860  52.015  12.993  1.00 56.97           C  
ANISOU  961  CA  THR A 139     7060   7882   6703   2723    754     38       C  
ATOM    962  C   THR A 139      27.278  52.566  12.892  1.00 54.96           C  
ANISOU  962  C   THR A 139     6566   7916   6400   2789    757    155       C  
ATOM    963  O   THR A 139      28.268  51.843  12.997  1.00 55.99           O  
ANISOU  963  O   THR A 139     6688   8112   6474   2928    810    242       O  
ATOM    964  CB  THR A 139      25.228  52.461  14.323  1.00 51.64           C  
ANISOU  964  CB  THR A 139     6346   7175   6100   2567    651     51       C  
ATOM    965  OG1 THR A 139      26.030  52.019  15.420  1.00 52.16           O  
ANISOU  965  OG1 THR A 139     6334   7337   6149   2714    663    163       O  
ATOM    966  CG2 THR A 139      23.820  51.919  14.473  1.00 47.18           C  
ANISOU  966  CG2 THR A 139     6010   6338   5580   2460    636    -53       C  
ATOM    967  N   LYS A 140      27.366  53.873  12.685  1.00 51.72           N  
ANISOU  967  N   LYS A 140     5972   7673   6007   2643    688    161       N  
ATOM    968  CA  LYS A 140      28.629  54.586  12.768  1.00 60.42           C  
ANISOU  968  CA  LYS A 140     6825   9068   7064   2657    668    276       C  
ATOM    969  C   LYS A 140      28.450  55.803  13.664  1.00 64.66           C  
ANISOU  969  C   LYS A 140     7208   9713   7647   2445    549    304       C  
ATOM    970  O   LYS A 140      27.339  56.320  13.827  1.00 60.72           O  
ANISOU  970  O   LYS A 140     6794   9064   7212   2251    482    219       O  
ATOM    971  CB  LYS A 140      29.134  55.012  11.380  1.00 72.87           C  
ANISOU  971  CB  LYS A 140     8341  10756   8589   2655    708    263       C  
ATOM    972  CG  LYS A 140      28.532  56.311  10.848  1.00 78.06           C  
ANISOU  972  CG  LYS A 140     8933  11444   9283   2428    634    199       C  
ATOM    973  CD  LYS A 140      28.995  56.603   9.423  1.00 79.50           C  
ANISOU  973  CD  LYS A 140     9071  11727   9409   2454    687    183       C  
ATOM    974  CE  LYS A 140      30.272  57.432   9.385  1.00 85.79           C  
ANISOU  974  CE  LYS A 140     9612  12834  10151   2438    668    300       C  
ATOM    975  NZ  LYS A 140      30.644  57.793   7.974  1.00 86.77           N  
ANISOU  975  NZ  LYS A 140     9702  13045  10223   2432    712    280       N  
ATOM    976  N   GLY A 141      29.557  56.247  14.252  1.00 72.99           N  
ANISOU  976  N   GLY A 141     8047  11026   8658   2468    523    427       N  
ATOM    977  CA  GLY A 141      29.564  57.432  15.072  1.00 68.83           C  
ANISOU  977  CA  GLY A 141     7380  10618   8153   2250    412    461       C  
ATOM    978  C   GLY A 141      29.785  58.697  14.264  1.00 61.89           C  
ANISOU  978  C   GLY A 141     6382   9876   7257   2077    372    451       C  
ATOM    979  O   GLY A 141      29.866  58.667  13.032  1.00 52.49           O  
ANISOU  979  O   GLY A 141     5216   8686   6044   2122    426    412       O  
ATOM    980  N   PRO A 142      29.896  59.847  14.950  1.00 58.94           N  
ANISOU  980  N   PRO A 142     5889   9617   6887   1870    277    485       N  
ATOM    981  CA  PRO A 142      29.784  59.982  16.408  1.00 60.40           C  
ANISOU  981  CA  PRO A 142     6051   9807   7092   1794    209    527       C  
ATOM    982  C   PRO A 142      28.377  59.714  16.954  1.00 61.23           C  
ANISOU  982  C   PRO A 142     6356   9623   7283   1727    184    425       C  
ATOM    983  O   PRO A 142      27.403  59.723  16.198  1.00 61.14           O  
ANISOU  983  O   PRO A 142     6487   9424   7321   1680    198    319       O  
ATOM    984  CB  PRO A 142      30.191  61.440  16.649  1.00 59.91           C  
ANISOU  984  CB  PRO A 142     5840   9924   7000   1558    124    566       C  
ATOM    985  CG  PRO A 142      31.034  61.795  15.477  1.00 54.68           C  
ANISOU  985  CG  PRO A 142     5056   9445   6276   1584    161    602       C  
ATOM    986  CD  PRO A 142      30.395  61.083  14.330  1.00 52.77           C  
ANISOU  986  CD  PRO A 142     4968   9015   6068   1710    239    508       C  
ATOM    987  N   TYR A 143      28.284  59.458  18.257  1.00 55.59           N  
ANISOU  987  N   TYR A 143     5649   8891   6583   1722    146    463       N  
ATOM    988  CA  TYR A 143      27.028  59.101  18.898  1.00 50.07           C  
ANISOU  988  CA  TYR A 143     5127   7939   5957   1674    127    382       C  
ATOM    989  C   TYR A 143      26.577  60.263  19.768  1.00 49.17           C  
ANISOU  989  C   TYR A 143     4984   7829   5868   1440     35    370       C  
ATOM    990  O   TYR A 143      27.271  60.645  20.715  1.00 62.55           O  
ANISOU  990  O   TYR A 143     6559   9685   7521   1388    -12    453       O  
ATOM    991  CB  TYR A 143      27.170  57.808  19.705  1.00 49.27           C  
ANISOU  991  CB  TYR A 143     5085   7783   5851   1862    167    429       C  
ATOM    992  CG  TYR A 143      27.422  56.634  18.803  1.00 53.57           C  
ANISOU  992  CG  TYR A 143     5714   8267   6373   2093    271    421       C  
ATOM    993  CD1 TYR A 143      26.369  55.883  18.303  1.00 53.74           C  
ANISOU  993  CD1 TYR A 143     5951   8027   6439   2128    315    316       C  
ATOM    994  CD2 TYR A 143      28.713  56.302  18.408  1.00 58.46           C  
ANISOU  994  CD2 TYR A 143     6199   9096   6918   2271    327    521       C  
ATOM    995  CE1 TYR A 143      26.597  54.817  17.446  1.00 52.65           C  
ANISOU  995  CE1 TYR A 143     5917   7819   6269   2330    416    302       C  
ATOM    996  CE2 TYR A 143      28.950  55.234  17.555  1.00 56.96           C  
ANISOU  996  CE2 TYR A 143     6103   8840   6698   2495    435    512       C  
ATOM    997  CZ  TYR A 143      27.892  54.505  17.071  1.00 51.18           C  
ANISOU  997  CZ  TYR A 143     5608   7829   6009   2519    480    398       C  
ATOM    998  OH  TYR A 143      28.124  53.463  16.213  1.00 44.02           O  
ANISOU  998  OH  TYR A 143     4829   6834   5063   2704    585    380       O  
ATOM    999  N   GLU A 144      25.436  60.843  19.416  1.00 40.29           N  
ANISOU  999  N   GLU A 144     3971   6533   4803   1300     13    270       N  
ATOM   1000  CA  GLU A 144      24.835  61.921  20.190  1.00 44.43           C  
ANISOU 1000  CA  GLU A 144     4507   7020   5355   1092    -59    246       C  
ATOM   1001  C   GLU A 144      24.037  61.310  21.331  1.00 41.53           C  
ANISOU 1001  C   GLU A 144     4249   6498   5032   1105    -72    226       C  
ATOM   1002  O   GLU A 144      23.056  60.593  21.104  1.00 38.16           O  
ANISOU 1002  O   GLU A 144     3966   5877   4658   1157    -41    156       O  
ATOM   1003  CB  GLU A 144      23.945  62.792  19.309  1.00 43.66           C  
ANISOU 1003  CB  GLU A 144     4479   6813   5298    959    -68    160       C  
ATOM   1004  CG  GLU A 144      24.683  63.559  18.229  1.00 36.33           C  
ANISOU 1004  CG  GLU A 144     3446   6034   4323    916    -63    181       C  
ATOM   1005  CD  GLU A 144      23.918  64.791  17.759  1.00 38.36           C  
ANISOU 1005  CD  GLU A 144     3751   6216   4610    737    -95    122       C  
ATOM   1006  OE1 GLU A 144      24.561  65.800  17.405  1.00 48.22           O  
ANISOU 1006  OE1 GLU A 144     4908   7601   5813    630   -117    156       O  
ATOM   1007  OE2 GLU A 144      22.670  64.758  17.757  1.00 47.10           O  
ANISOU 1007  OE2 GLU A 144     4986   7130   5779    703    -96     48       O  
ATOM   1008  N   LEU A 145      24.478  61.569  22.554  1.00 47.33           N  
ANISOU 1008  N   LEU A 145     4917   7330   5738   1051   -118    289       N  
ATOM   1009  CA  LEU A 145      23.775  61.134  23.751  1.00 40.30           C  
ANISOU 1009  CA  LEU A 145     4119   6313   4882   1041   -137    277       C  
ATOM   1010  C   LEU A 145      22.967  62.333  24.210  1.00 42.51           C  
ANISOU 1010  C   LEU A 145     4444   6520   5189    831   -188    225       C  
ATOM   1011  O   LEU A 145      23.535  63.308  24.712  1.00 52.42           O  
ANISOU 1011  O   LEU A 145     5613   7908   6396    700   -235    266       O  
ATOM   1012  CB  LEU A 145      24.746  60.663  24.833  1.00 42.61           C  
ANISOU 1012  CB  LEU A 145     4313   6759   5117   1114   -154    384       C  
ATOM   1013  CG  LEU A 145      25.361  59.254  24.775  1.00 47.29           C  
ANISOU 1013  CG  LEU A 145     4898   7382   5687   1356    -94    446       C  
ATOM   1014  CD1 LEU A 145      24.298  58.228  24.997  1.00 54.67           C  
ANISOU 1014  CD1 LEU A 145     6016   8073   6683   1436    -59    383       C  
ATOM   1015  CD2 LEU A 145      26.105  58.963  23.469  1.00 51.46           C  
ANISOU 1015  CD2 LEU A 145     5363   8004   6184   1489    -35    465       C  
ATOM   1016  N   THR A 146      21.655  62.290  23.986  1.00 39.85           N  
ANISOU 1016  N   THR A 146     4242   5978   4920    797   -175    138       N  
ATOM   1017  CA  THR A 146      20.765  63.373  24.385  1.00 40.20           C  
ANISOU 1017  CA  THR A 146     4345   5936   4994    626   -210     89       C  
ATOM   1018  C   THR A 146      19.934  62.902  25.567  1.00 38.56           C  
ANISOU 1018  C   THR A 146     4230   5601   4820    621   -218     73       C  
ATOM   1019  O   THR A 146      19.253  61.873  25.478  1.00 41.64           O  
ANISOU 1019  O   THR A 146     4708   5863   5251    716   -187     42       O  
ATOM   1020  CB  THR A 146      19.872  63.841  23.227  1.00 38.64           C  
ANISOU 1020  CB  THR A 146     4211   5628   4841    583   -190     14       C  
ATOM   1021  OG1 THR A 146      18.915  62.828  22.884  1.00 38.54           O  
ANISOU 1021  OG1 THR A 146     4305   5458   4881    670   -155    -38       O  
ATOM   1022  CG2 THR A 146      20.721  64.157  22.026  1.00 32.92           C  
ANISOU 1022  CG2 THR A 146     3399   5029   4081    603   -176     32       C  
ATOM   1023  N   LEU A 147      20.038  63.639  26.680  1.00 39.75           N  
ANISOU 1023  N   LEU A 147     4366   5795   4943    505   -259     97       N  
ATOM   1024  CA  LEU A 147      19.221  63.423  27.862  1.00 34.90           C  
ANISOU 1024  CA  LEU A 147     3838   5068   4353    473   -270     81       C  
ATOM   1025  C   LEU A 147      17.764  63.207  27.480  1.00 35.02           C  
ANISOU 1025  C   LEU A 147     3973   4889   4442    476   -241      3       C  
ATOM   1026  O   LEU A 147      17.232  63.908  26.622  1.00 35.71           O  
ANISOU 1026  O   LEU A 147     4082   4931   4555    421   -231    -42       O  
ATOM   1027  CB  LEU A 147      19.340  64.638  28.787  1.00 46.52           C  
ANISOU 1027  CB  LEU A 147     5302   6589   5783    307   -311     92       C  
ATOM   1028  CG  LEU A 147      20.615  64.807  29.624  1.00 45.89           C  
ANISOU 1028  CG  LEU A 147     5118   6701   5617    267   -353    175       C  
ATOM   1029  CD1 LEU A 147      20.684  66.194  30.271  1.00 41.29           C  
ANISOU 1029  CD1 LEU A 147     4553   6152   4982     69   -390    170       C  
ATOM   1030  CD2 LEU A 147      20.730  63.704  30.680  1.00 33.24           C  
ANISOU 1030  CD2 LEU A 147     3519   5104   4008    362   -358    222       C  
ATOM   1031  N   MET A 148      17.107  62.234  28.122  1.00 35.71           N  
ANISOU 1031  N   MET A 148     4138   4871   4561    537   -227     -6       N  
ATOM   1032  CA  MET A 148      15.699  61.940  27.849  1.00 38.68           C  
ANISOU 1032  CA  MET A 148     4619   5080   4997    529   -203    -70       C  
ATOM   1033  C   MET A 148      14.867  62.628  28.934  1.00 32.62           C  
ANISOU 1033  C   MET A 148     3902   4250   4241    422   -219    -84       C  
ATOM   1034  O   MET A 148      14.749  62.132  30.058  1.00 39.30           O  
ANISOU 1034  O   MET A 148     4779   5072   5080    431   -226    -63       O  
ATOM   1035  CB  MET A 148      15.467  60.426  27.767  1.00 38.96           C  
ANISOU 1035  CB  MET A 148     4721   5033   5051    652   -174    -72       C  
ATOM   1036  CG  MET A 148      14.014  59.964  27.932  1.00 50.79           C  
ANISOU 1036  CG  MET A 148     6330   6371   6597    622   -158   -121       C  
ATOM   1037  SD  MET A 148      13.641  58.285  27.360  1.00 50.48           S  
ANISOU 1037  SD  MET A 148     6398   6214   6570    735   -117   -142       S  
ATOM   1038  CE  MET A 148      14.613  57.337  28.543  1.00 67.59           C  
ANISOU 1038  CE  MET A 148     8563   8418   8699    845   -116    -68       C  
ATOM   1039  N   GLU A 149      14.300  63.788  28.606  1.00 37.83           N  
ANISOU 1039  N   GLU A 149     4574   4885   4914    327   -218   -118       N  
ATOM   1040  CA  GLU A 149      13.427  64.475  29.555  1.00 36.08           C  
ANISOU 1040  CA  GLU A 149     4415   4594   4702    241   -218   -134       C  
ATOM   1041  C   GLU A 149      12.081  63.762  29.639  1.00 37.57           C  
ANISOU 1041  C   GLU A 149     4676   4655   4942    270   -193   -166       C  
ATOM   1042  O   GLU A 149      11.585  63.205  28.655  1.00 37.84           O  
ANISOU 1042  O   GLU A 149     4724   4645   5009    315   -176   -191       O  
ATOM   1043  CB  GLU A 149      13.213  65.948  29.174  1.00 29.08           C  
ANISOU 1043  CB  GLU A 149     3535   3708   3807    145   -215   -155       C  
ATOM   1044  CG  GLU A 149      14.484  66.727  28.855  1.00 33.78           C  
ANISOU 1044  CG  GLU A 149     4060   4428   4345     92   -239   -127       C  
ATOM   1045  CD  GLU A 149      15.399  66.902  30.058  1.00 45.86           C  
ANISOU 1045  CD  GLU A 149     5566   6049   5809     35   -272    -84       C  
ATOM   1046  OE1 GLU A 149      14.900  66.997  31.205  1.00 51.45           O  
ANISOU 1046  OE1 GLU A 149     6337   6701   6510     -6   -272    -88       O  
ATOM   1047  OE2 GLU A 149      16.633  66.933  29.848  1.00 53.99           O  
ANISOU 1047  OE2 GLU A 149     6507   7219   6788     29   -298    -41       O  
ATOM   1048  N   ASN A 150      11.470  63.815  30.819  1.00 41.46           N  
ANISOU 1048  N   ASN A 150     5220   5097   5435    233   -191   -163       N  
ATOM   1049  CA  ASN A 150      10.310  62.980  31.156  1.00 40.74           C  
ANISOU 1049  CA  ASN A 150     5191   4907   5381    255   -172   -179       C  
ATOM   1050  C   ASN A 150       9.062  63.860  31.220  1.00 39.79           C  
ANISOU 1050  C   ASN A 150     5107   4726   5285    195   -147   -204       C  
ATOM   1051  O   ASN A 150       8.755  64.454  32.252  1.00 53.73           O  
ANISOU 1051  O   ASN A 150     6906   6476   7034    147   -140   -199       O  
ATOM   1052  CB  ASN A 150      10.584  62.247  32.483  1.00 43.69           C  
ANISOU 1052  CB  ASN A 150     5590   5279   5732    272   -183   -146       C  
ATOM   1053  CG  ASN A 150       9.391  61.483  33.000  1.00 50.59           C  
ANISOU 1053  CG  ASN A 150     6532   6055   6635    275   -164   -157       C  
ATOM   1054  OD1 ASN A 150       8.984  61.666  34.152  1.00 42.54           O  
ANISOU 1054  OD1 ASN A 150     5545   5014   5603    235   -161   -147       O  
ATOM   1055  ND2 ASN A 150       8.828  60.611  32.164  1.00 52.61           N  
ANISOU 1055  ND2 ASN A 150     6815   6253   6922    314   -149   -177       N  
ATOM   1056  N   GLY A 151       8.349  63.949  30.103  1.00 39.28           N  
ANISOU 1056  N   GLY A 151     5037   4636   5253    202   -132   -227       N  
ATOM   1057  CA  GLY A 151       7.135  64.742  30.020  1.00 35.45           C  
ANISOU 1057  CA  GLY A 151     4571   4109   4789    166   -104   -239       C  
ATOM   1058  C   GLY A 151       6.260  64.226  28.897  1.00 39.94           C  
ANISOU 1058  C   GLY A 151     5129   4655   5389    183    -95   -253       C  
ATOM   1059  O   GLY A 151       6.057  63.010  28.808  1.00 30.66           O  
ANISOU 1059  O   GLY A 151     3974   3454   4223    205   -101   -258       O  
ATOM   1060  N   CYS A 152       5.759  65.108  28.017  1.00 37.03           N  
ANISOU 1060  N   CYS A 152     4738   4299   5032    170    -81   -258       N  
ATOM   1061  CA  CYS A 152       5.077  64.672  26.798  1.00 42.14           C  
ANISOU 1061  CA  CYS A 152     5363   4949   5698    177    -81   -268       C  
ATOM   1062  C   CYS A 152       5.605  65.428  25.577  1.00 41.24           C  
ANISOU 1062  C   CYS A 152     5211   4881   5579    181    -86   -274       C  
ATOM   1063  O   CYS A 152       6.015  66.595  25.657  1.00 38.30           O  
ANISOU 1063  O   CYS A 152     4832   4525   5194    167    -79   -265       O  
ATOM   1064  CB  CYS A 152       3.548  64.837  26.904  1.00 35.48           C  
ANISOU 1064  CB  CYS A 152     4519   4089   4871    156    -58   -253       C  
ATOM   1065  SG  CYS A 152       2.952  66.549  26.855  1.00 47.11           S  
ANISOU 1065  SG  CYS A 152     5978   5576   6347    156    -21   -229       S  
ATOM   1066  N   ILE A 153       5.584  64.752  24.432  1.00 36.34           N  
ANISOU 1066  N   ILE A 153     4574   4273   4960    193    -97   -290       N  
ATOM   1067  CA  ILE A 153       6.175  65.336  23.232  1.00 39.08           C  
ANISOU 1067  CA  ILE A 153     4884   4669   5297    199   -103   -296       C  
ATOM   1068  C   ILE A 153       5.292  66.472  22.731  1.00 34.19           C  
ANISOU 1068  C   ILE A 153     4243   4060   4687    177    -86   -278       C  
ATOM   1069  O   ILE A 153       4.063  66.467  22.908  1.00 30.60           O  
ANISOU 1069  O   ILE A 153     3789   3591   4246    167    -72   -262       O  
ATOM   1070  CB  ILE A 153       6.406  64.265  22.143  1.00 28.92           C  
ANISOU 1070  CB  ILE A 153     3599   3389   4000    221   -113   -321       C  
ATOM   1071  CG1 ILE A 153       7.577  64.656  21.242  1.00 33.39           C  
ANISOU 1071  CG1 ILE A 153     4127   4014   4545    244   -118   -327       C  
ATOM   1072  CG2 ILE A 153       5.147  64.006  21.328  1.00 24.73           C  
ANISOU 1072  CG2 ILE A 153     3068   2854   3475    187   -112   -327       C  
ATOM   1073  CD1 ILE A 153       8.143  63.492  20.431  1.00 29.95           C  
ANISOU 1073  CD1 ILE A 153     3710   3581   4090    288   -119   -352       C  
ATOM   1074  N   ILE A 154       5.928  67.493  22.159  1.00 26.64           N  
ANISOU 1074  N   ILE A 154     3267   3138   3718    173    -84   -271       N  
ATOM   1075  CA  ILE A 154       5.219  68.615  21.554  1.00 32.53           C  
ANISOU 1075  CA  ILE A 154     4001   3892   4468    166    -65   -247       C  
ATOM   1076  C   ILE A 154       5.885  68.946  20.218  1.00 35.29           C  
ANISOU 1076  C   ILE A 154     4316   4292   4801    165    -77   -252       C  
ATOM   1077  O   ILE A 154       7.108  69.143  20.159  1.00 34.43           O  
ANISOU 1077  O   ILE A 154     4201   4210   4671    157    -88   -261       O  
ATOM   1078  CB  ILE A 154       5.197  69.847  22.482  1.00 34.73           C  
ANISOU 1078  CB  ILE A 154     4322   4135   4739    156    -36   -227       C  
ATOM   1079  CG1 ILE A 154       4.299  69.598  23.701  1.00 37.73           C  
ANISOU 1079  CG1 ILE A 154     4733   4469   5132    164    -14   -217       C  
ATOM   1080  CG2 ILE A 154       4.743  71.096  21.709  1.00 38.44           C  
ANISOU 1080  CG2 ILE A 154     4793   4609   5205    163    -10   -198       C  
ATOM   1081  CD1 ILE A 154       2.775  69.702  23.448  1.00 32.01           C  
ANISOU 1081  CD1 ILE A 154     3987   3750   4426    188     12   -186       C  
ATOM   1082  N   PHE A 155       5.079  69.001  19.153  1.00 27.49           N  
ANISOU 1082  N   PHE A 155     3300   3330   3817    167    -76   -241       N  
ATOM   1083  CA  PHE A 155       5.512  69.379  17.810  1.00 26.21           C  
ANISOU 1083  CA  PHE A 155     3105   3217   3635    163    -85   -241       C  
ATOM   1084  C   PHE A 155       5.115  70.816  17.510  1.00 28.26           C  
ANISOU 1084  C   PHE A 155     3367   3478   3892    163    -61   -200       C  
ATOM   1085  O   PHE A 155       3.974  71.215  17.761  1.00 32.60           O  
ANISOU 1085  O   PHE A 155     3920   4013   4456    180    -39   -166       O  
ATOM   1086  CB  PHE A 155       4.867  68.481  16.758  1.00 25.71           C  
ANISOU 1086  CB  PHE A 155     3016   3187   3566    158   -101   -253       C  
ATOM   1087  CG  PHE A 155       5.153  67.029  16.938  1.00 20.61           C  
ANISOU 1087  CG  PHE A 155     2395   2522   2916    159   -116   -294       C  
ATOM   1088  CD1 PHE A 155       4.119  66.106  16.925  1.00 24.18           C  
ANISOU 1088  CD1 PHE A 155     2860   2960   3368    135   -123   -300       C  
ATOM   1089  CD2 PHE A 155       6.450  66.576  17.101  1.00 18.41           C  
ANISOU 1089  CD2 PHE A 155     2129   2242   2625    185   -119   -319       C  
ATOM   1090  CE1 PHE A 155       4.368  64.756  17.077  1.00 25.66           C  
ANISOU 1090  CE1 PHE A 155     3095   3110   3543    134   -130   -338       C  
ATOM   1091  CE2 PHE A 155       6.709  65.212  17.256  1.00 24.35           C  
ANISOU 1091  CE2 PHE A 155     2919   2965   3368    205   -123   -352       C  
ATOM   1092  CZ  PHE A 155       5.670  64.312  17.248  1.00 28.87           C  
ANISOU 1092  CZ  PHE A 155     3526   3501   3941    179   -127   -364       C  
ATOM   1093  N   ILE A 156       6.034  71.583  16.927  1.00 29.19           N  
ANISOU 1093  N   ILE A 156     3484   3619   3988    149    -62   -197       N  
ATOM   1094  CA  ILE A 156       5.740  72.950  16.506  1.00 31.82           C  
ANISOU 1094  CA  ILE A 156     3836   3944   4312    149    -37   -156       C  
ATOM   1095  C   ILE A 156       6.217  73.132  15.071  1.00 35.62           C  
ANISOU 1095  C   ILE A 156     4277   4487   4769    138    -52   -153       C  
ATOM   1096  O   ILE A 156       7.332  72.721  14.727  1.00 33.46           O  
ANISOU 1096  O   ILE A 156     3983   4253   4476    118    -73   -181       O  
ATOM   1097  CB  ILE A 156       6.418  73.984  17.426  1.00 38.27           C  
ANISOU 1097  CB  ILE A 156     4721   4708   5111    121    -15   -150       C  
ATOM   1098  CG1 ILE A 156       5.904  73.836  18.850  1.00 38.98           C  
ANISOU 1098  CG1 ILE A 156     4857   4736   5216    132      4   -153       C  
ATOM   1099  CG2 ILE A 156       6.140  75.384  16.962  1.00 35.20           C  
ANISOU 1099  CG2 ILE A 156     4378   4292   4705    123     19   -108       C  
ATOM   1100  CD1 ILE A 156       7.022  73.636  19.843  1.00 24.41           C  
ANISOU 1100  CD1 ILE A 156     3038   2883   3352     88    -12   -181       C  
ATOM   1101  N   SER A 157       5.387  73.762  14.237  1.00 29.10           N  
ANISOU 1101  N   SER A 157     3438   3679   3940    156    -40   -112       N  
ATOM   1102  CA  SER A 157       5.753  74.006  12.846  1.00 32.70           C  
ANISOU 1102  CA  SER A 157     3859   4196   4370    143    -53   -104       C  
ATOM   1103  C   SER A 157       5.040  75.254  12.346  1.00 35.22           C  
ANISOU 1103  C   SER A 157     4195   4507   4682    167    -25    -41       C  
ATOM   1104  O   SER A 157       4.271  75.890  13.072  1.00 36.85           O  
ANISOU 1104  O   SER A 157     4441   4658   4901    202     10     -4       O  
ATOM   1105  CB  SER A 157       5.423  72.808  11.957  1.00 23.16           C  
ANISOU 1105  CB  SER A 157     2596   3049   3156    142    -83   -129       C  
ATOM   1106  OG  SER A 157       4.035  72.589  11.920  1.00 30.00           O  
ANISOU 1106  OG  SER A 157     3437   3926   4033    158    -82    -99       O  
ATOM   1107  N   GLY A 158       5.297  75.587  11.082  1.00 27.89           N  
ANISOU 1107  N   GLY A 158     3238   3633   3726    155    -35    -24       N  
ATOM   1108  CA  GLY A 158       4.723  76.763  10.474  1.00 33.81           C  
ANISOU 1108  CA  GLY A 158     4005   4380   4462    182     -8     43       C  
ATOM   1109  C   GLY A 158       3.977  76.476   9.191  1.00 32.20           C  
ANISOU 1109  C   GLY A 158     3728   4264   4241    196    -29     74       C  
ATOM   1110  O   GLY A 158       4.576  76.060   8.194  1.00 35.66           O  
ANISOU 1110  O   GLY A 158     4130   4765   4654    160    -58     48       O  
ATOM   1111  N   LEU A 159       2.666  76.700   9.209  1.00 33.48           N  
ANISOU 1111  N   LEU A 159     3865   4443   4413    248    -13    134       N  
ATOM   1112  CA  LEU A 159       1.812  76.464   8.058  1.00 31.11           C  
ANISOU 1112  CA  LEU A 159     3486   4246   4089    255    -37    178       C  
ATOM   1113  C   LEU A 159       2.046  77.524   6.992  1.00 41.48           C  
ANISOU 1113  C   LEU A 159     4808   5583   5370    266    -26    231       C  
ATOM   1114  O   LEU A 159       2.671  78.567   7.232  1.00 39.25           O  
ANISOU 1114  O   LEU A 159     4603   5226   5084    277      9    245       O  
ATOM   1115  CB  LEU A 159       0.342  76.448   8.470  1.00 29.82           C  
ANISOU 1115  CB  LEU A 159     3279   4114   3938    309    -21    242       C  
ATOM   1116  CG  LEU A 159       0.040  75.341   9.471  1.00 36.06           C  
ANISOU 1116  CG  LEU A 159     4059   4889   4755    287    -35    193       C  
ATOM   1117  CD1 LEU A 159      -1.436  75.187   9.713  1.00 38.93           C  
ANISOU 1117  CD1 LEU A 159     4355   5317   5119    324    -27    261       C  
ATOM   1118  CD2 LEU A 159       0.644  74.050   8.969  1.00 41.05           C  
ANISOU 1118  CD2 LEU A 159     4672   5554   5372    208    -85    114       C  
ATOM   1119  N   GLU A 160       1.518  77.239   5.795  1.00 46.93           N  
ANISOU 1119  N   GLU A 160     5424   6379   6026    255    -57    262       N  
ATOM   1120  CA  GLU A 160       1.770  78.096   4.638  1.00 49.22           C  
ANISOU 1120  CA  GLU A 160     5714   6709   6280    258    -54    311       C  
ATOM   1121  C   GLU A 160       1.217  79.503   4.840  1.00 36.16           C  
ANISOU 1121  C   GLU A 160     4107   5005   4627    342      0    407       C  
ATOM   1122  O   GLU A 160       1.852  80.485   4.442  1.00 40.45           O  
ANISOU 1122  O   GLU A 160     4713   5504   5151    343     23    431       O  
ATOM   1123  CB  GLU A 160       1.175  77.467   3.380  1.00 50.74           C  
ANISOU 1123  CB  GLU A 160     5816   7034   6429    226    -99    330       C  
ATOM   1124  CG  GLU A 160       1.514  78.227   2.110  1.00 47.65           C  
ANISOU 1124  CG  GLU A 160     5421   6693   5993    220   -102    375       C  
ATOM   1125  CD  GLU A 160       0.482  79.285   1.755  1.00 45.10           C  
ANISOU 1125  CD  GLU A 160     5075   6406   5655    300    -77    499       C  
ATOM   1126  OE1 GLU A 160      -0.640  79.255   2.308  1.00 39.71           O  
ANISOU 1126  OE1 GLU A 160     4353   5746   4988    357    -64    554       O  
ATOM   1127  OE2 GLU A 160       0.799  80.147   0.911  1.00 49.85           O  
ANISOU 1127  OE2 GLU A 160     5698   7020   6225    310    -66    547       O  
ATOM   1128  N   ASP A 161       0.043  79.625   5.448  1.00 34.19           N  
ANISOU 1128  N   ASP A 161     3834   4760   4396    416     26    466       N  
ATOM   1129  CA  ASP A 161      -0.556  80.925   5.726  1.00 38.59           C  
ANISOU 1129  CA  ASP A 161     4448   5261   4952    521     91    562       C  
ATOM   1130  C   ASP A 161       0.022  81.611   6.983  1.00 45.97           C  
ANISOU 1130  C   ASP A 161     5520   6035   5913    540    148    530       C  
ATOM   1131  O   ASP A 161      -0.639  82.488   7.551  1.00 53.34           O  
ANISOU 1131  O   ASP A 161     6515   6903   6849    639    214    598       O  
ATOM   1132  CB  ASP A 161      -2.077  80.781   5.857  1.00 39.48           C  
ANISOU 1132  CB  ASP A 161     4470   5464   5066    605    103    650       C  
ATOM   1133  CG  ASP A 161      -2.497  79.946   7.063  1.00 44.96           C  
ANISOU 1133  CG  ASP A 161     5145   6140   5796    600    104    605       C  
ATOM   1134  OD1 ASP A 161      -1.604  79.450   7.785  1.00 44.61           O  
ANISOU 1134  OD1 ASP A 161     5160   6011   5778    535     93    506       O  
ATOM   1135  OD2 ASP A 161      -3.730  79.783   7.283  1.00 40.62           O  
ANISOU 1135  OD2 ASP A 161     4515   5674   5246    661    115    677       O  
ATOM   1136  N   GLY A 162       1.210  81.229   7.451  1.00 37.95           N  
ANISOU 1136  N   GLY A 162     4554   4959   4907    452    128    434       N  
ATOM   1137  CA  GLY A 162       1.826  81.908   8.576  1.00 33.67           C  
ANISOU 1137  CA  GLY A 162     4142   4276   4373    446    174    405       C  
ATOM   1138  C   GLY A 162       1.420  81.429   9.956  1.00 35.59           C  
ANISOU 1138  C   GLY A 162     4402   4469   4651    469    192    373       C  
ATOM   1139  O   GLY A 162       1.962  81.937  10.941  1.00 54.98           O  
ANISOU 1139  O   GLY A 162     6972   6812   7107    452    228    343       O  
ATOM   1140  N   THR A 163       0.505  80.461  10.069  1.00 29.16           N  
ANISOU 1140  N   THR A 163     3483   3738   3859    495    168    378       N  
ATOM   1141  CA  THR A 163      -0.019  80.052  11.368  1.00 35.04           C  
ANISOU 1141  CA  THR A 163     4239   4441   4633    525    191    361       C  
ATOM   1142  C   THR A 163       0.989  79.177  12.098  1.00 37.49           C  
ANISOU 1142  C   THR A 163     4569   4716   4961    434    153    259       C  
ATOM   1143  O   THR A 163       1.592  78.280  11.497  1.00 33.47           O  
ANISOU 1143  O   THR A 163     3999   4270   4450    366     96    208       O  
ATOM   1144  CB  THR A 163      -1.339  79.298  11.197  1.00 42.50           C  
ANISOU 1144  CB  THR A 163     5060   5500   5586    568    174    408       C  
ATOM   1145  OG1 THR A 163      -2.295  80.137  10.535  1.00 52.97           O  
ANISOU 1145  OG1 THR A 163     6354   6880   6891    664    210    519       O  
ATOM   1146  CG2 THR A 163      -1.901  78.884  12.534  1.00 42.25           C  
ANISOU 1146  CG2 THR A 163     5039   5434   5582    596    200    396       C  
ATOM   1147  N   LEU A 164       1.184  79.449  13.393  1.00 41.23           N  
ANISOU 1147  N   LEU A 164     5131   5089   5445    440    190    234       N  
ATOM   1148  CA  LEU A 164       2.010  78.595  14.247  1.00 31.35           C  
ANISOU 1148  CA  LEU A 164     3890   3813   4208    368    157    151       C  
ATOM   1149  C   LEU A 164       1.176  77.398  14.675  1.00 34.72           C  
ANISOU 1149  C   LEU A 164     4235   4295   4664    382    135    140       C  
ATOM   1150  O   LEU A 164       0.199  77.546  15.418  1.00 43.27           O  
ANISOU 1150  O   LEU A 164     5325   5358   5758    443    175    178       O  
ATOM   1151  CB  LEU A 164       2.532  79.345  15.473  1.00 32.64           C  
ANISOU 1151  CB  LEU A 164     4183   3857   4361    354    201    131       C  
ATOM   1152  CG  LEU A 164       3.662  78.559  16.177  1.00 38.75           C  
ANISOU 1152  CG  LEU A 164     4960   4625   5137    266    158     53       C  
ATOM   1153  CD1 LEU A 164       4.964  78.508  15.351  1.00 20.36           C  
ANISOU 1153  CD1 LEU A 164     2609   2343   2785    188    114     22       C  
ATOM   1154  CD2 LEU A 164       3.959  79.086  17.575  1.00 43.07           C  
ANISOU 1154  CD2 LEU A 164     5624   5071   5671    246    196     33       C  
ATOM   1155  N   LEU A 165       1.556  76.211  14.221  1.00 34.73           N  
ANISOU 1155  N   LEU A 165     4166   4361   4670    325     76     91       N  
ATOM   1156  CA  LEU A 165       0.852  74.993  14.587  1.00 34.50           C  
ANISOU 1156  CA  LEU A 165     4075   4373   4659    317     52     75       C  
ATOM   1157  C   LEU A 165       1.570  74.335  15.765  1.00 28.07           C  
ANISOU 1157  C   LEU A 165     3307   3498   3861    283     43     10       C  
ATOM   1158  O   LEU A 165       2.787  74.133  15.719  1.00 30.66           O  
ANISOU 1158  O   LEU A 165     3658   3810   4181    239     20    -39       O  
ATOM   1159  CB  LEU A 165       0.763  74.047  13.380  1.00 21.45           C  
ANISOU 1159  CB  LEU A 165     2343   2816   2992    274     -1     60       C  
ATOM   1160  CG  LEU A 165       0.121  72.663  13.602  1.00 35.92           C  
ANISOU 1160  CG  LEU A 165     4129   4690   4830    239    -33     35       C  
ATOM   1161  CD1 LEU A 165      -1.346  72.820  14.021  1.00 33.34           C  
ANISOU 1161  CD1 LEU A 165     3754   4404   4507    278     -9    105       C  
ATOM   1162  CD2 LEU A 165       0.240  71.722  12.366  1.00 35.10           C  
ANISOU 1162  CD2 LEU A 165     3981   4660   4697    179    -82      4       C  
ATOM   1163  N   VAL A 166       0.821  74.022  16.821  1.00 28.10           N  
ANISOU 1163  N   VAL A 166     3317   3477   3882    305     63     19       N  
ATOM   1164  CA  VAL A 166       1.329  73.261  17.964  1.00 25.91           C  
ANISOU 1164  CA  VAL A 166     3075   3153   3619    275     52    -34       C  
ATOM   1165  C   VAL A 166       0.469  72.006  18.135  1.00 28.13           C  
ANISOU 1165  C   VAL A 166     3299   3476   3911    261     29    -39       C  
ATOM   1166  O   VAL A 166      -0.764  72.086  18.188  1.00 33.00           O  
ANISOU 1166  O   VAL A 166     3874   4133   4530    290     48     13       O  
ATOM   1167  CB  VAL A 166       1.337  74.115  19.252  1.00 28.46           C  
ANISOU 1167  CB  VAL A 166     3482   3390   3942    301    102    -25       C  
ATOM   1168  CG1 VAL A 166       1.940  73.340  20.427  1.00 24.42           C  
ANISOU 1168  CG1 VAL A 166     3003   2839   3437    264     86    -76       C  
ATOM   1169  CG2 VAL A 166       2.139  75.404  19.042  1.00 22.61           C  
ANISOU 1169  CG2 VAL A 166     2816   2599   3176    296    127    -19       C  
ATOM   1170  N   CYS A 167       1.115  70.850  18.197  1.00 24.33           N  
ANISOU 1170  N   CYS A 167     2820   2993   3433    216    -11    -95       N  
ATOM   1171  CA  CYS A 167       0.430  69.581  18.332  1.00 23.53           C  
ANISOU 1171  CA  CYS A 167     2690   2916   3334    185    -34   -107       C  
ATOM   1172  C   CYS A 167       1.015  68.818  19.512  1.00 35.70           C  
ANISOU 1172  C   CYS A 167     4283   4394   4886    172    -39   -150       C  
ATOM   1173  O   CYS A 167       2.151  69.063  19.937  1.00 25.69           O  
ANISOU 1173  O   CYS A 167     3055   3085   3619    178    -38   -177       O  
ATOM   1174  CB  CYS A 167       0.568  68.725  17.075  1.00 28.66           C  
ANISOU 1174  CB  CYS A 167     3310   3617   3962    142    -74   -133       C  
ATOM   1175  SG  CYS A 167       0.108  69.545  15.532  1.00 36.80           S  
ANISOU 1175  SG  CYS A 167     4279   4734   4968    147    -79    -86       S  
ATOM   1176  N   SER A 168       0.207  67.909  20.056  1.00 32.36           N  
ANISOU 1176  N   SER A 168     3855   3973   4468    150    -44   -147       N  
ATOM   1177  CA  SER A 168       0.748  66.794  20.813  1.00 36.33           C  
ANISOU 1177  CA  SER A 168     4404   4425   4974    129    -60   -191       C  
ATOM   1178  C   SER A 168       1.061  65.671  19.821  1.00 37.52           C  
ANISOU 1178  C   SER A 168     4561   4590   5106     93    -94   -229       C  
ATOM   1179  O   SER A 168       1.020  65.869  18.605  1.00 32.01           O  
ANISOU 1179  O   SER A 168     3832   3941   4391     82   -106   -227       O  
ATOM   1180  CB  SER A 168      -0.215  66.358  21.918  1.00 31.09           C  
ANISOU 1180  CB  SER A 168     3747   3748   4319    116    -45   -170       C  
ATOM   1181  OG  SER A 168      -1.553  66.223  21.441  1.00 29.64           O  
ANISOU 1181  OG  SER A 168     3504   3633   4124     89    -45   -128       O  
ATOM   1182  N   LYS A 169       1.366  64.473  20.331  1.00 41.32           N  
ANISOU 1182  N   LYS A 169     5094   5023   5583     77   -106   -263       N  
ATOM   1183  CA  LYS A 169       1.845  63.399  19.468  1.00 43.17           C  
ANISOU 1183  CA  LYS A 169     5365   5246   5791     58   -126   -306       C  
ATOM   1184  C   LYS A 169       0.846  63.058  18.376  1.00 48.27           C  
ANISOU 1184  C   LYS A 169     5990   5944   6409     -7   -143   -300       C  
ATOM   1185  O   LYS A 169       1.246  62.616  17.291  1.00 44.62           O  
ANISOU 1185  O   LYS A 169     5547   5490   5915    -22   -155   -332       O  
ATOM   1186  CB  LYS A 169       2.155  62.147  20.288  1.00 49.93           C  
ANISOU 1186  CB  LYS A 169     6298   6030   6644     57   -127   -334       C  
ATOM   1187  CG  LYS A 169       3.028  61.131  19.562  1.00 56.52           C  
ANISOU 1187  CG  LYS A 169     7196   6830   7450     74   -131   -380       C  
ATOM   1188  CD  LYS A 169       3.012  59.775  20.262  1.00 60.91           C  
ANISOU 1188  CD  LYS A 169     7846   7304   7993     66   -127   -400       C  
ATOM   1189  CE  LYS A 169       4.099  59.668  21.328  1.00 66.35           C  
ANISOU 1189  CE  LYS A 169     8556   7956   8700    144   -116   -396       C  
ATOM   1190  NZ  LYS A 169       3.659  58.786  22.469  1.00 71.39           N  
ANISOU 1190  NZ  LYS A 169     9259   8526   9339    126   -112   -389       N  
ATOM   1191  N   HIS A 170      -0.454  63.256  18.629  1.00 41.26           N  
ANISOU 1191  N   HIS A 170     5055   5101   5520    -48   -142   -255       N  
ATOM   1192  CA  HIS A 170      -1.426  62.886  17.609  1.00 42.33           C  
ANISOU 1192  CA  HIS A 170     5160   5308   5617   -126   -165   -241       C  
ATOM   1193  C   HIS A 170      -2.618  63.835  17.534  1.00 45.51           C  
ANISOU 1193  C   HIS A 170     5460   5811   6022   -129   -158   -165       C  
ATOM   1194  O   HIS A 170      -3.631  63.481  16.919  1.00 38.87           O  
ANISOU 1194  O   HIS A 170     4574   5051   5141   -206   -180   -136       O  
ATOM   1195  CB  HIS A 170      -1.903  61.452  17.856  1.00 44.57           C  
ANISOU 1195  CB  HIS A 170     5513   5554   5869   -212   -180   -267       C  
ATOM   1196  CG  HIS A 170      -0.810  60.435  17.740  1.00 61.57           C  
ANISOU 1196  CG  HIS A 170     7778   7609   8007   -198   -180   -336       C  
ATOM   1197  ND1 HIS A 170      -0.092  60.244  16.575  1.00 61.60           N  
ANISOU 1197  ND1 HIS A 170     7813   7609   7981   -190   -185   -376       N  
ATOM   1198  CD2 HIS A 170      -0.288  59.576  18.650  1.00 64.21           C  
ANISOU 1198  CD2 HIS A 170     8201   7847   8350   -177   -168   -364       C  
ATOM   1199  CE1 HIS A 170       0.812  59.300  16.768  1.00 61.28           C  
ANISOU 1199  CE1 HIS A 170     7878   7476   7931   -156   -172   -426       C  
ATOM   1200  NE2 HIS A 170       0.713  58.875  18.018  1.00 62.98           N  
ANISOU 1200  NE2 HIS A 170     8129   7633   8169   -147   -163   -417       N  
ATOM   1201  N   SER A 171      -2.527  65.034  18.112  1.00 46.09           N  
ANISOU 1201  N   SER A 171     5499   5884   6131    -48   -126   -128       N  
ATOM   1202  CA  SER A 171      -3.708  65.882  18.213  1.00 37.87           C  
ANISOU 1202  CA  SER A 171     4371   4927   5090    -27   -105    -48       C  
ATOM   1203  C   SER A 171      -3.293  67.345  18.310  1.00 32.85           C  
ANISOU 1203  C   SER A 171     3726   4274   4479     70    -67    -20       C  
ATOM   1204  O   SER A 171      -2.125  67.659  18.537  1.00 36.36           O  
ANISOU 1204  O   SER A 171     4231   4642   4942    103    -60    -63       O  
ATOM   1205  CB  SER A 171      -4.554  65.470  19.412  1.00 26.13           C  
ANISOU 1205  CB  SER A 171     2878   3441   3609    -44    -88    -21       C  
ATOM   1206  OG  SER A 171      -5.674  66.323  19.507  1.00 44.92           O  
ANISOU 1206  OG  SER A 171     5168   5914   5986     -3    -59     65       O  
ATOM   1207  N   THR A 172      -4.278  68.247  18.164  1.00 32.42           N  
ANISOU 1207  N   THR A 172     3600   4297   4420    114    -40     59       N  
ATOM   1208  CA  THR A 172      -3.980  69.678  18.251  1.00 40.34           C  
ANISOU 1208  CA  THR A 172     4617   5269   5439    208      6     91       C  
ATOM   1209  C   THR A 172      -5.128  70.583  18.703  1.00 46.91           C  
ANISOU 1209  C   THR A 172     5400   6151   6271    288     61    181       C  
ATOM   1210  O   THR A 172      -4.915  71.786  18.897  1.00 56.50           O  
ANISOU 1210  O   THR A 172     6654   7318   7494    372    111    207       O  
ATOM   1211  CB  THR A 172      -3.484  70.225  16.909  1.00 44.77           C  
ANISOU 1211  CB  THR A 172     5164   5861   5986    214    -12     93       C  
ATOM   1212  OG1 THR A 172      -3.304  71.638  17.044  1.00 38.31           O  
ANISOU 1212  OG1 THR A 172     4373   5006   5178    300     38    132       O  
ATOM   1213  CG2 THR A 172      -4.517  69.984  15.798  1.00 43.64           C  
ANISOU 1213  CG2 THR A 172     4922   5853   5807    178    -40    150       C  
ATOM   1214  N   GLY A 173      -6.338  70.067  18.863  1.00 51.65           N  
ANISOU 1214  N   GLY A 173     5921   6850   6855    265     59    234       N  
ATOM   1215  CA  GLY A 173      -7.385  70.944  19.371  1.00 64.82           C  
ANISOU 1215  CA  GLY A 173     7539   8571   8520    362    122    327       C  
ATOM   1216  C   GLY A 173      -7.223  71.409  20.814  1.00 66.79           C  
ANISOU 1216  C   GLY A 173     7869   8716   8791    429    185    315       C  
ATOM   1217  O   GLY A 173      -6.123  71.369  21.374  1.00 55.33           O  
ANISOU 1217  O   GLY A 173     6521   7142   7359    411    181    237       O  
ATOM   1218  N   ASP A 174      -8.320  71.866  21.426  1.00 85.03           N  
ANISOU 1218  N   ASP A 174    10132  11085  11092    507    245    396       N  
ATOM   1219  CA  ASP A 174      -8.375  72.150  22.869  1.00 90.70           C  
ANISOU 1219  CA  ASP A 174    10922  11721  11820    562    308    388       C  
ATOM   1220  C   ASP A 174      -9.087  71.029  23.637  1.00 94.72           C  
ANISOU 1220  C   ASP A 174    11378  12290  12323    495    292    393       C  
ATOM   1221  O   ASP A 174     -10.261  70.743  23.395  1.00 98.05           O  
ANISOU 1221  O   ASP A 174    11678  12856  12720    489    292    473       O  
ATOM   1222  CB  ASP A 174      -9.081  73.483  23.143  1.00 90.24           C  
ANISOU 1222  CB  ASP A 174    10868  11670  11748    714    405    475       C  
ATOM   1223  CG  ASP A 174      -8.141  74.664  23.088  1.00 94.16           C  
ANISOU 1223  CG  ASP A 174    11498  12029  12251    777    445    444       C  
ATOM   1224  OD1 ASP A 174      -8.012  75.272  22.010  1.00 97.93           O  
ANISOU 1224  OD1 ASP A 174    11959  12529  12722    807    439    474       O  
ATOM   1225  OD2 ASP A 174      -7.524  74.981  24.126  1.00 96.71           O  
ANISOU 1225  OD2 ASP A 174    11945  12224  12578    785    482    390       O  
ATOM   1226  N   LEU A 180      -8.116  71.403  29.068  1.00 41.71           N  
ANISOU 1226  N   LEU A 180     5027   5204   5618    575    465    267       N  
ATOM   1227  CA  LEU A 180      -6.782  71.851  28.676  1.00 50.01           C  
ANISOU 1227  CA  LEU A 180     6171   6152   6680    554    436    200       C  
ATOM   1228  C   LEU A 180      -5.975  70.684  28.098  1.00 49.99           C  
ANISOU 1228  C   LEU A 180     6145   6153   6696    441    338    139       C  
ATOM   1229  O   LEU A 180      -5.423  69.861  28.825  1.00 53.08           O  
ANISOU 1229  O   LEU A 180     6578   6498   7091    378    305     89       O  
ATOM   1230  CB  LEU A 180      -6.058  72.481  29.862  1.00 37.91           C  
ANISOU 1230  CB  LEU A 180     4781   4491   5131    570    480    154       C  
ATOM   1231  CG  LEU A 180      -4.772  73.279  29.614  1.00 49.68           C  
ANISOU 1231  CG  LEU A 180     6379   5881   6615    554    471    100       C  
ATOM   1232  CD1 LEU A 180      -5.028  74.718  29.180  1.00 44.59           C  
ANISOU 1232  CD1 LEU A 180     5790   5202   5952    650    544    142       C  
ATOM   1233  CD2 LEU A 180      -3.938  73.268  30.886  1.00 64.73           C  
ANISOU 1233  CD2 LEU A 180     8401   7693   8500    506    475     42       C  
ATOM   1234  N   SER A 181      -5.953  70.617  26.772  1.00 43.38           N  
ANISOU 1234  N   SER A 181     5243   5373   5865    425    297    150       N  
ATOM   1235  CA  SER A 181      -5.167  69.627  26.054  1.00 38.41           C  
ANISOU 1235  CA  SER A 181     4604   4743   5247    335    216     94       C  
ATOM   1236  C   SER A 181      -3.678  69.834  26.308  1.00 34.02           C  
ANISOU 1236  C   SER A 181     4145   4084   4698    318    198     24       C  
ATOM   1237  O   SER A 181      -3.219  70.920  26.666  1.00 40.44           O  
ANISOU 1237  O   SER A 181     5028   4836   5503    362    239     20       O  
ATOM   1238  CB  SER A 181      -5.433  69.743  24.558  1.00 32.39           C  
ANISOU 1238  CB  SER A 181     3764   4063   4481    330    187    122       C  
ATOM   1239  OG  SER A 181      -5.079  71.057  24.136  1.00 34.19           O  
ANISOU 1239  OG  SER A 181     4026   4259   4707    403    224    139       O  
ATOM   1240  N   HIS A 182      -2.909  68.771  26.101  1.00 33.36           N  
ANISOU 1240  N   HIS A 182     4069   3987   4621    251    137    -28       N  
ATOM   1241  CA  HIS A 182      -1.463  68.937  26.097  1.00 39.34           C  
ANISOU 1241  CA  HIS A 182     4888   4681   5379    237    113    -82       C  
ATOM   1242  C   HIS A 182      -1.028  69.984  25.073  1.00 33.31           C  
ANISOU 1242  C   HIS A 182     4121   3925   4610    263    119    -75       C  
ATOM   1243  O   HIS A 182      -0.119  70.786  25.341  1.00 28.88           O  
ANISOU 1243  O   HIS A 182     3624   3312   4039    267    131    -94       O  
ATOM   1244  CB  HIS A 182      -0.784  67.596  25.821  1.00 42.12           C  
ANISOU 1244  CB  HIS A 182     5238   5031   5735    183     55   -127       C  
ATOM   1245  CG  HIS A 182      -1.034  66.577  26.882  1.00 59.89           C  
ANISOU 1245  CG  HIS A 182     7514   7257   7986    156     49   -135       C  
ATOM   1246  ND1 HIS A 182      -2.226  65.892  26.986  1.00 64.86           N  
ANISOU 1246  ND1 HIS A 182     8105   7926   8613    128     52   -106       N  
ATOM   1247  CD2 HIS A 182      -0.260  66.146  27.905  1.00 62.02           C  
ANISOU 1247  CD2 HIS A 182     7839   7474   8252    147     40   -162       C  
ATOM   1248  CE1 HIS A 182      -2.166  65.064  28.015  1.00 60.47           C  
ANISOU 1248  CE1 HIS A 182     7591   7331   8055    103     47   -119       C  
ATOM   1249  NE2 HIS A 182      -0.984  65.201  28.589  1.00 62.28           N  
ANISOU 1249  NE2 HIS A 182     7877   7504   8284    119     40   -151       N  
ATOM   1250  N   SER A 183      -1.660  70.004  23.894  1.00 25.27           N  
ANISOU 1250  N   SER A 183     3033   2976   3593    271    109    -44       N  
ATOM   1251  CA  SER A 183      -1.134  70.893  22.866  1.00 31.43           C  
ANISOU 1251  CA  SER A 183     3814   3762   4367    289    109    -39       C  
ATOM   1252  C   SER A 183      -1.336  72.351  23.265  1.00 34.38           C  
ANISOU 1252  C   SER A 183     4242   4091   4730    352    174     -2       C  
ATOM   1253  O   SER A 183      -0.444  73.178  23.050  1.00 41.40           O  
ANISOU 1253  O   SER A 183     5189   4933   5607    349    180    -19       O  
ATOM   1254  CB  SER A 183      -1.726  70.552  21.484  1.00 29.03           C  
ANISOU 1254  CB  SER A 183     3424   3547   4058    276     79    -13       C  
ATOM   1255  OG  SER A 183      -3.075  70.957  21.305  1.00 32.54           O  
ANISOU 1255  OG  SER A 183     3806   4061   4497    319    111     60       O  
ATOM   1256  N   SER A 184      -2.459  72.679  23.922  1.00 35.36           N  
ANISOU 1256  N   SER A 184     4361   4223   4853    408    228     47       N  
ATOM   1257  CA  SER A 184      -2.648  74.058  24.374  1.00 24.03           C  
ANISOU 1257  CA  SER A 184     3005   2726   3400    482    304     80       C  
ATOM   1258  C   SER A 184      -1.701  74.396  25.514  1.00 33.58           C  
ANISOU 1258  C   SER A 184     4334   3830   4593    450    319     28       C  
ATOM   1259  O   SER A 184      -1.177  75.516  25.579  1.00 36.75           O  
ANISOU 1259  O   SER A 184     4834   4159   4971    462    356     24       O  
ATOM   1260  CB  SER A 184      -4.083  74.310  24.826  1.00 24.80           C  
ANISOU 1260  CB  SER A 184     3066   2865   3493    566    368    152       C  
ATOM   1261  OG  SER A 184      -5.024  73.697  23.984  1.00 49.08           O  
ANISOU 1261  OG  SER A 184     6008   6064   6575    569    340    202       O  
ATOM   1262  N   ALA A 185      -1.484  73.452  26.436  1.00 31.65           N  
ANISOU 1262  N   ALA A 185     4092   3578   4355    402    292     -9       N  
ATOM   1263  CA  ALA A 185      -0.527  73.700  27.510  1.00 33.38           C  
ANISOU 1263  CA  ALA A 185     4415   3717   4551    359    296    -56       C  
ATOM   1264  C   ALA A 185       0.862  73.928  26.934  1.00 29.69           C  
ANISOU 1264  C   ALA A 185     3973   3237   4072    297    250    -94       C  
ATOM   1265  O   ALA A 185       1.584  74.842  27.361  1.00 30.58           O  
ANISOU 1265  O   ALA A 185     4184   3286   4149    268    271   -111       O  
ATOM   1266  CB  ALA A 185      -0.526  72.536  28.511  1.00 29.40           C  
ANISOU 1266  CB  ALA A 185     3896   3221   4056    321    268    -80       C  
ATOM   1267  N   GLY A 186       1.240  73.123  25.939  1.00 21.89           N  
ANISOU 1267  N   GLY A 186     2900   2313   3106    271    189   -107       N  
ATOM   1268  CA  GLY A 186       2.493  73.372  25.248  1.00 28.19           C  
ANISOU 1268  CA  GLY A 186     3704   3119   3890    224    151   -134       C  
ATOM   1269  C   GLY A 186       2.531  74.739  24.593  1.00 33.28           C  
ANISOU 1269  C   GLY A 186     4398   3735   4514    241    189   -109       C  
ATOM   1270  O   GLY A 186       3.570  75.406  24.589  1.00 34.14           O  
ANISOU 1270  O   GLY A 186     4566   3816   4590    188    182   -127       O  
ATOM   1271  N   GLU A 187       1.392  75.186  24.051  1.00 34.67           N  
ANISOU 1271  N   GLU A 187     4550   3921   4701    313    230    -60       N  
ATOM   1272  CA  GLU A 187       1.373  76.468  23.351  1.00 34.31           C  
ANISOU 1272  CA  GLU A 187     4556   3844   4634    343    270    -27       C  
ATOM   1273  C   GLU A 187       1.456  77.620  24.336  1.00 31.75           C  
ANISOU 1273  C   GLU A 187     4380   3412   4272    351    338    -26       C  
ATOM   1274  O   GLU A 187       2.201  78.587  24.119  1.00 35.46           O  
ANISOU 1274  O   GLU A 187     4941   3826   4705    312    352    -33       O  
ATOM   1275  CB  GLU A 187       0.120  76.595  22.484  1.00 34.17           C  
ANISOU 1275  CB  GLU A 187     4464   3885   4635    428    295     37       C  
ATOM   1276  CG  GLU A 187       0.017  77.928  21.746  1.00 31.31           C  
ANISOU 1276  CG  GLU A 187     4159   3488   4250    478    342     83       C  
ATOM   1277  CD  GLU A 187      -0.754  77.824  20.440  1.00 49.63           C  
ANISOU 1277  CD  GLU A 187     6368   5904   6584    528    329    140       C  
ATOM   1278  OE1 GLU A 187      -1.273  76.723  20.127  1.00 57.11           O  
ANISOU 1278  OE1 GLU A 187     7199   6947   7554    516    284    142       O  
ATOM   1279  OE2 GLU A 187      -0.838  78.845  19.722  1.00 57.64           O  
ANISOU 1279  OE2 GLU A 187     7421   6901   7580    573    363    186       O  
ATOM   1280  N   LYS A 188       0.688  77.542  25.423  1.00 30.50           N  
ANISOU 1280  N   LYS A 188     4257   3219   4113    396    384    -17       N  
ATOM   1281  CA  LYS A 188       0.804  78.547  26.476  1.00 30.19           C  
ANISOU 1281  CA  LYS A 188     4378   3067   4027    396    453    -26       C  
ATOM   1282  C   LYS A 188       2.261  78.711  26.911  1.00 26.81           C  
ANISOU 1282  C   LYS A 188     4028   2601   3559    270    411    -83       C  
ATOM   1283  O   LYS A 188       2.778  79.831  26.988  1.00 24.50           O  
ANISOU 1283  O   LYS A 188     3869   2226   3214    231    446    -89       O  
ATOM   1284  CB  LYS A 188      -0.084  78.163  27.655  1.00 33.03           C  
ANISOU 1284  CB  LYS A 188     4746   3413   4390    447    496    -18       C  
ATOM   1285  CG  LYS A 188      -1.570  78.020  27.320  1.00 24.60           C  
ANISOU 1285  CG  LYS A 188     3589   2406   3352    567    541     51       C  
ATOM   1286  CD  LYS A 188      -2.249  79.348  27.115  1.00 40.74           C  
ANISOU 1286  CD  LYS A 188     5723   4388   5368    678    639    109       C  
ATOM   1287  CE  LYS A 188      -3.755  79.147  26.962  1.00 36.55           C  
ANISOU 1287  CE  LYS A 188     5086   3944   4859    804    686    189       C  
ATOM   1288  NZ  LYS A 188      -4.112  77.894  27.659  1.00 30.41           N  
ANISOU 1288  NZ  LYS A 188     4212   3237   4105    765    646    172       N  
ATOM   1289  N   HIS A 189       2.953  77.591  27.137  1.00 34.12           N  
ANISOU 1289  N   HIS A 189     4870   3593   4501    202    335   -120       N  
ATOM   1290  CA  HIS A 189       4.359  77.635  27.535  1.00 35.79           C  
ANISOU 1290  CA  HIS A 189     5124   3804   4670     85    288   -161       C  
ATOM   1291  C   HIS A 189       5.225  78.278  26.463  1.00 35.90           C  
ANISOU 1291  C   HIS A 189     5142   3836   4663     32    265   -159       C  
ATOM   1292  O   HIS A 189       6.171  79.023  26.771  1.00 37.53           O  
ANISOU 1292  O   HIS A 189     5442   4008   4809    -65    262   -176       O  
ATOM   1293  CB  HIS A 189       4.857  76.224  27.829  1.00 34.42           C  
ANISOU 1293  CB  HIS A 189     4843   3713   4524     54    216   -185       C  
ATOM   1294  CG  HIS A 189       4.860  75.879  29.282  1.00 41.15           C  
ANISOU 1294  CG  HIS A 189     5745   4537   5354     27    223   -203       C  
ATOM   1295  ND1 HIS A 189       5.829  76.336  30.152  1.00 42.62           N  
ANISOU 1295  ND1 HIS A 189     6018   4699   5475    -70    212   -227       N  
ATOM   1296  CD2 HIS A 189       4.020  75.115  30.021  1.00 38.96           C  
ANISOU 1296  CD2 HIS A 189     5441   4258   5102     76    236   -199       C  
ATOM   1297  CE1 HIS A 189       5.588  75.864  31.362  1.00 41.35           C  
ANISOU 1297  CE1 HIS A 189     5885   4522   5305    -74    219   -237       C  
ATOM   1298  NE2 HIS A 189       4.497  75.121  31.310  1.00 41.13           N  
ANISOU 1298  NE2 HIS A 189     5790   4504   5333     16    235   -220       N  
ATOM   1299  N   LEU A 190       4.934  77.977  25.197  1.00 35.03           N  
ANISOU 1299  N   LEU A 190     4929   3786   4594     82    245   -137       N  
ATOM   1300  CA  LEU A 190       5.622  78.630  24.089  1.00 27.26           C  
ANISOU 1300  CA  LEU A 190     3947   2821   3590     43    230   -128       C  
ATOM   1301  C   LEU A 190       5.317  80.119  24.063  1.00 34.32           C  
ANISOU 1301  C   LEU A 190     4989   3608   4442     55    303   -102       C  
ATOM   1302  O   LEU A 190       6.201  80.933  23.771  1.00 36.08           O  
ANISOU 1302  O   LEU A 190     5286   3806   4615    -30    299   -107       O  
ATOM   1303  CB  LEU A 190       5.207  77.969  22.784  1.00 31.85           C  
ANISOU 1303  CB  LEU A 190     4395   3485   4220    102    199   -108       C  
ATOM   1304  CG  LEU A 190       5.950  78.290  21.498  1.00 39.67           C  
ANISOU 1304  CG  LEU A 190     5348   4526   5197     65    170   -101       C  
ATOM   1305  CD1 LEU A 190       7.430  77.932  21.641  1.00 31.44           C  
ANISOU 1305  CD1 LEU A 190     4280   3541   4125    -36    113   -135       C  
ATOM   1306  CD2 LEU A 190       5.304  77.497  20.350  1.00 44.31           C  
ANISOU 1306  CD2 LEU A 190     5811   5195   5830    129    144    -84       C  
ATOM   1307  N   GLU A 191       4.070  80.497  24.378  1.00 38.88           N  
ANISOU 1307  N   GLU A 191     5616   4122   5033    160    375    -70       N  
ATOM   1308  CA  GLU A 191       3.725  81.914  24.429  1.00 36.60           C  
ANISOU 1308  CA  GLU A 191     5491   3715   4699    194    460    -41       C  
ATOM   1309  C   GLU A 191       4.535  82.634  25.491  1.00 36.27           C  
ANISOU 1309  C   GLU A 191     5622   3575   4584     85    482    -81       C  
ATOM   1310  O   GLU A 191       5.007  83.755  25.272  1.00 49.06           O  
ANISOU 1310  O   GLU A 191     7382   5112   6145     29    515    -78       O  
ATOM   1311  CB  GLU A 191       2.222  82.086  24.675  1.00 38.15           C  
ANISOU 1311  CB  GLU A 191     5696   3878   4920    347    540      9       C  
ATOM   1312  CG  GLU A 191       1.378  81.598  23.476  1.00 39.76           C  
ANISOU 1312  CG  GLU A 191     5739   4187   5179    442    521     63       C  
ATOM   1313  CD  GLU A 191      -0.115  81.610  23.728  1.00 39.46           C  
ANISOU 1313  CD  GLU A 191     5670   4160   5162    588    589    124       C  
ATOM   1314  OE1 GLU A 191      -0.875  81.576  22.747  1.00 46.48           O  
ANISOU 1314  OE1 GLU A 191     6459   5125   6076    670    592    185       O  
ATOM   1315  OE2 GLU A 191      -0.540  81.648  24.900  1.00 47.51           O  
ANISOU 1315  OE2 GLU A 191     6759   5125   6169    619    641    115       O  
ATOM   1316  N   ALA A 192       4.734  81.998  26.641  1.00 38.93           N  
ANISOU 1316  N   ALA A 192     5956   3921   4913     40    461   -119       N  
ATOM   1317  CA  ALA A 192       5.476  82.661  27.703  1.00 32.62           C  
ANISOU 1317  CA  ALA A 192     5323   3038   4032    -78    479   -157       C  
ATOM   1318  C   ALA A 192       6.932  82.834  27.306  1.00 29.88           C  
ANISOU 1318  C   ALA A 192     4970   2744   3639   -236    409   -178       C  
ATOM   1319  O   ALA A 192       7.486  83.932  27.429  1.00 33.36           O  
ANISOU 1319  O   ALA A 192     5573   3101   4001   -334    437   -186       O  
ATOM   1320  CB  ALA A 192       5.353  81.883  29.016  1.00 32.48           C  
ANISOU 1320  CB  ALA A 192     5292   3035   4015    -90    468   -186       C  
ATOM   1321  N   GLN A 193       7.574  81.759  26.826  1.00 31.61           N  
ANISOU 1321  N   GLN A 193     5008   3104   3898   -265    320   -184       N  
ATOM   1322  CA  GLN A 193       8.991  81.852  26.479  1.00 32.68           C  
ANISOU 1322  CA  GLN A 193     5113   3317   3985   -408    254   -196       C  
ATOM   1323  C   GLN A 193       9.225  82.891  25.394  1.00 31.31           C  
ANISOU 1323  C   GLN A 193     5003   3109   3784   -437    275   -172       C  
ATOM   1324  O   GLN A 193      10.197  83.653  25.459  1.00 42.04           O  
ANISOU 1324  O   GLN A 193     6451   4457   5063   -582    263   -179       O  
ATOM   1325  CB  GLN A 193       9.549  80.484  26.060  1.00 33.75           C  
ANISOU 1325  CB  GLN A 193     5044   3609   4172   -397    169   -199       C  
ATOM   1326  CG  GLN A 193       9.036  79.909  24.753  1.00 36.77           C  
ANISOU 1326  CG  GLN A 193     5294   4049   4629   -289    157   -178       C  
ATOM   1327  CD  GLN A 193       9.697  78.568  24.391  1.00 43.48           C  
ANISOU 1327  CD  GLN A 193     5972   5035   5513   -284     83   -186       C  
ATOM   1328  OE1 GLN A 193       9.629  77.603  25.163  1.00 39.28           O  
ANISOU 1328  OE1 GLN A 193     5391   4531   5003   -261     61   -201       O  
ATOM   1329  NE2 GLN A 193      10.331  78.506  23.202  1.00 31.19           N  
ANISOU 1329  NE2 GLN A 193     4333   3560   3958   -300     50   -175       N  
ATOM   1330  N   LEU A 194       8.326  82.966  24.409  1.00 38.49           N  
ANISOU 1330  N   LEU A 194     5870   4003   4751   -310    308   -140       N  
ATOM   1331  CA  LEU A 194       8.472  83.957  23.345  1.00 37.79           C  
ANISOU 1331  CA  LEU A 194     5844   3878   4636   -325    332   -110       C  
ATOM   1332  C   LEU A 194       8.283  85.365  23.886  1.00 36.21           C  
ANISOU 1332  C   LEU A 194     5887   3509   4361   -360    417   -106       C  
ATOM   1333  O   LEU A 194       9.020  86.282  23.509  1.00 41.91           O  
ANISOU 1333  O   LEU A 194     6715   4192   5016   -472    421   -101       O  
ATOM   1334  CB  LEU A 194       7.481  83.675  22.210  1.00 33.88           C  
ANISOU 1334  CB  LEU A 194     5244   3416   4215   -175    347    -69       C  
ATOM   1335  CG  LEU A 194       7.762  82.446  21.336  1.00 33.01           C  
ANISOU 1335  CG  LEU A 194     4921   3460   4162   -156    268    -72       C  
ATOM   1336  CD1 LEU A 194       6.579  82.094  20.411  1.00 22.03           C  
ANISOU 1336  CD1 LEU A 194     3435   2100   2835    -14    284    -33       C  
ATOM   1337  CD2 LEU A 194       9.029  82.677  20.522  1.00 44.08           C  
ANISOU 1337  CD2 LEU A 194     6289   4936   5524   -270    219    -75       C  
ATOM   1338  N   GLU A 195       7.311  85.554  24.781  1.00 29.41           N  
ANISOU 1338  N   GLU A 195     5126   2544   3504   -269    489   -107       N  
ATOM   1339  CA  GLU A 195       7.162  86.849  25.445  1.00 41.68           C  
ANISOU 1339  CA  GLU A 195     6940   3922   4976   -301    579   -111       C  
ATOM   1340  C   GLU A 195       8.445  87.248  26.154  1.00 48.64           C  
ANISOU 1340  C   GLU A 195     7934   4788   5758   -518    543   -156       C  
ATOM   1341  O   GLU A 195       8.896  88.395  26.054  1.00 46.76           O  
ANISOU 1341  O   GLU A 195     7886   4446   5435   -621    580   -156       O  
ATOM   1342  CB  GLU A 195       6.006  86.815  26.448  1.00 48.52           C  
ANISOU 1342  CB  GLU A 195     7880   4700   5856   -171    660   -110       C  
ATOM   1343  CG  GLU A 195       4.648  87.183  25.863  1.00 60.10           C  
ANISOU 1343  CG  GLU A 195     9353   6114   7370     36    746    -48       C  
ATOM   1344  CD  GLU A 195       4.419  88.677  25.780  1.00 71.77           C  
ANISOU 1344  CD  GLU A 195    11083   7411   8775     64    854    -22       C  
ATOM   1345  OE1 GLU A 195       5.397  89.451  25.915  1.00 77.11           O  
ANISOU 1345  OE1 GLU A 195    11924   8008   9365    -99    851    -53       O  
ATOM   1346  OE2 GLU A 195       3.249  89.077  25.590  1.00 76.08           O  
ANISOU 1346  OE2 GLU A 195    11666   7897   9343    250    945     35       O  
ATOM   1347  N   ARG A 196       9.040  86.305  26.889  1.00 45.21           N  
ANISOU 1347  N   ARG A 196     7389   4463   5327   -596    469   -190       N  
ATOM   1348  CA  ARG A 196      10.273  86.571  27.622  1.00 40.55           C  
ANISOU 1348  CA  ARG A 196     6876   3896   4637   -810    423   -223       C  
ATOM   1349  C   ARG A 196      11.387  87.088  26.704  1.00 38.86           C  
ANISOU 1349  C   ARG A 196     6650   3743   4370   -956    375   -209       C  
ATOM   1350  O   ARG A 196      12.129  87.995  27.085  1.00 37.09           O  
ANISOU 1350  O   ARG A 196     6595   3462   4036  -1134    382   -223       O  
ATOM   1351  CB  ARG A 196      10.707  85.297  28.351  1.00 42.45           C  
ANISOU 1351  CB  ARG A 196     6947   4279   4905   -837    343   -244       C  
ATOM   1352  CG  ARG A 196      11.768  85.488  29.415  1.00 58.33           C  
ANISOU 1352  CG  ARG A 196     9036   6318   6807  -1039    302   -273       C  
ATOM   1353  CD  ARG A 196      12.241  84.146  29.965  1.00 77.45           C  
ANISOU 1353  CD  ARG A 196    11261   8903   9262  -1044    217   -277       C  
ATOM   1354  NE  ARG A 196      13.220  83.501  29.088  1.00 97.78           N  
ANISOU 1354  NE  ARG A 196    13635  11658  11859  -1083    130   -253       N  
ATOM   1355  CZ  ARG A 196      13.012  82.363  28.425  1.00106.36           C  
ANISOU 1355  CZ  ARG A 196    14520  12846  13045   -950     94   -237       C  
ATOM   1356  NH1 ARG A 196      11.854  81.721  28.533  1.00109.54           N  
ANISOU 1356  NH1 ARG A 196    14886  13198  13536   -785    129   -242       N  
ATOM   1357  NH2 ARG A 196      13.968  81.861  27.654  1.00104.23           N  
ANISOU 1357  NH2 ARG A 196    14089  12733  12780   -987     26   -215       N  
ATOM   1358  N   ILE A 197      11.518  86.544  25.486  1.00 33.36           N  
ANISOU 1358  N   ILE A 197     5767   3165   3744   -893    328   -180       N  
ATOM   1359  CA  ILE A 197      12.633  86.964  24.628  1.00 37.34           C  
ANISOU 1359  CA  ILE A 197     6243   3750   4196  -1035    280   -163       C  
ATOM   1360  C   ILE A 197      12.191  88.028  23.636  1.00 44.07           C  
ANISOU 1360  C   ILE A 197     7218   4486   5039   -993    345   -131       C  
ATOM   1361  O   ILE A 197      12.958  88.416  22.747  1.00 45.65           O  
ANISOU 1361  O   ILE A 197     7395   4745   5204  -1090    314   -110       O  
ATOM   1362  CB  ILE A 197      13.279  85.781  23.869  1.00 34.14           C  
ANISOU 1362  CB  ILE A 197     5568   3555   3850  -1015    189   -150       C  
ATOM   1363  CG1 ILE A 197      12.316  85.164  22.865  1.00 30.10           C  
ANISOU 1363  CG1 ILE A 197     4927   3059   3448   -818    203   -129       C  
ATOM   1364  CG2 ILE A 197      13.754  84.689  24.821  1.00 28.93           C  
ANISOU 1364  CG2 ILE A 197     4785   3012   3197  -1042    128   -172       C  
ATOM   1365  CD1 ILE A 197      12.974  84.067  22.074  1.00 36.74           C  
ANISOU 1365  CD1 ILE A 197     5538   4087   4335   -802    125   -122       C  
ATOM   1366  N   GLY A 198      10.962  88.510  23.776  1.00 47.81           N  
ANISOU 1366  N   GLY A 198     7821   4803   5541   -845    437   -120       N  
ATOM   1367  CA  GLY A 198      10.450  89.492  22.843  1.00 41.53           C  
ANISOU 1367  CA  GLY A 198     7141   3897   4740   -776    505    -78       C  
ATOM   1368  C   GLY A 198      10.443  88.980  21.417  1.00 48.92           C  
ANISOU 1368  C   GLY A 198     7875   4964   5749   -700    458    -40       C  
ATOM   1369  O   GLY A 198      11.037  89.602  20.534  1.00 45.22           O  
ANISOU 1369  O   GLY A 198     7438   4506   5240   -783    448    -16       O  
ATOM   1370  N   LYS A 199       9.805  87.831  21.189  1.00 50.37           N  
ANISOU 1370  N   LYS A 199     7857   5251   6032   -556    428    -36       N  
ATOM   1371  CA  LYS A 199       9.527  87.324  19.851  1.00 49.13           C  
ANISOU 1371  CA  LYS A 199     7525   5199   5944   -459    396      0       C  
ATOM   1372  C   LYS A 199       8.089  86.819  19.824  1.00 49.58           C  
ANISOU 1372  C   LYS A 199     7514   5242   6083   -257    436     24       C  
ATOM   1373  O   LYS A 199       7.485  86.567  20.873  1.00 43.96           O  
ANISOU 1373  O   LYS A 199     6841   4478   5385   -202    468      6       O  
ATOM   1374  CB  LYS A 199      10.510  86.210  19.434  1.00 42.86           C  
ANISOU 1374  CB  LYS A 199     6516   4596   5172   -531    295    -22       C  
ATOM   1375  CG  LYS A 199      11.968  86.677  19.367  1.00 44.24           C  
ANISOU 1375  CG  LYS A 199     6723   4825   5260   -732    252    -32       C  
ATOM   1376  CD  LYS A 199      12.900  85.597  18.858  1.00 43.22           C  
ANISOU 1376  CD  LYS A 199     6375   4895   5153   -771    164    -40       C  
ATOM   1377  CE  LYS A 199      14.240  86.187  18.411  1.00 48.99           C  
ANISOU 1377  CE  LYS A 199     7115   5703   5797   -952    129    -27       C  
ATOM   1378  NZ  LYS A 199      15.095  85.189  17.686  1.00 47.19           N  
ANISOU 1378  NZ  LYS A 199     6664   5676   5589   -959     58    -23       N  
ATOM   1379  N   THR A 200       7.533  86.689  18.618  1.00 37.98           N  
ANISOU 1379  N   THR A 200     5943   3828   4660   -154    434     70       N  
ATOM   1380  CA  THR A 200       6.137  86.312  18.453  1.00 41.37           C  
ANISOU 1380  CA  THR A 200     6301   4264   5155     27    470    108       C  
ATOM   1381  C   THR A 200       6.017  84.940  17.806  1.00 46.60           C  
ANISOU 1381  C   THR A 200     6730   5090   5885     63    393    100       C  
ATOM   1382  O   THR A 200       6.974  84.406  17.237  1.00 45.47           O  
ANISOU 1382  O   THR A 200     6487   5049   5740    -26    322     74       O  
ATOM   1383  CB  THR A 200       5.384  87.343  17.611  1.00 38.92           C  
ANISOU 1383  CB  THR A 200     6075   3881   4833    132    540    183       C  
ATOM   1384  OG1 THR A 200       5.861  87.288  16.267  1.00 45.26           O  
ANISOU 1384  OG1 THR A 200     6780   4778   5639     96    490    204       O  
ATOM   1385  CG2 THR A 200       5.604  88.738  18.160  1.00 37.65           C  
ANISOU 1385  CG2 THR A 200     6174   3538   4592     88    622    189       C  
ATOM   1386  N   LYS A 201       4.803  84.377  17.896  1.00 43.86           N  
ANISOU 1386  N   LYS A 201     6303   4770   5592    195    412    126       N  
ATOM   1387  CA  LYS A 201       4.519  83.102  17.242  1.00 36.29           C  
ANISOU 1387  CA  LYS A 201     5146   3954   4689    228    347    121       C  
ATOM   1388  C   LYS A 201       4.692  83.203  15.734  1.00 43.93           C  
ANISOU 1388  C   LYS A 201     6038   5000   5656    228    317    154       C  
ATOM   1389  O   LYS A 201       5.273  82.310  15.105  1.00 42.97           O  
ANISOU 1389  O   LYS A 201     5792   4985   5548    177    248    123       O  
ATOM   1390  CB  LYS A 201       3.103  82.644  17.575  1.00 45.26           C  
ANISOU 1390  CB  LYS A 201     6223   5106   5867    356    378    156       C  
ATOM   1391  CG  LYS A 201       2.945  82.126  18.991  1.00 47.63           C  
ANISOU 1391  CG  LYS A 201     6550   5369   6179    351    388    116       C  
ATOM   1392  CD  LYS A 201       1.664  82.615  19.612  1.00 39.15           C  
ANISOU 1392  CD  LYS A 201     5534   4232   5108    477    473    166       C  
ATOM   1393  CE  LYS A 201       0.610  81.565  19.556  1.00 31.31           C  
ANISOU 1393  CE  LYS A 201     4387   3345   4163    550    453    190       C  
ATOM   1394  NZ  LYS A 201      -0.680  82.163  19.973  1.00 31.36           N  
ANISOU 1394  NZ  LYS A 201     4433   3315   4166    688    542    260       N  
ATOM   1395  N   GLU A 202       4.203  84.295  15.142  1.00 45.20           N  
ANISOU 1395  N   GLU A 202     6278   5104   5793    289    372    218       N  
ATOM   1396  CA  GLU A 202       4.301  84.476  13.698  1.00 52.64           C  
ANISOU 1396  CA  GLU A 202     7154   6118   6728    293    348    258       C  
ATOM   1397  C   GLU A 202       5.750  84.483  13.229  1.00 44.94           C  
ANISOU 1397  C   GLU A 202     6176   5180   5720    153    296    215       C  
ATOM   1398  O   GLU A 202       6.073  83.886  12.195  1.00 39.19           O  
ANISOU 1398  O   GLU A 202     5325   4566   5000    131    242    210       O  
ATOM   1399  CB  GLU A 202       3.577  85.757  13.293  1.00 68.59           C  
ANISOU 1399  CB  GLU A 202     9286   8054   8722    388    425    342       C  
ATOM   1400  CG  GLU A 202       2.228  85.929  14.020  1.00 91.08           C  
ANISOU 1400  CG  GLU A 202    12163  10853  11590    534    496    391       C  
ATOM   1401  CD  GLU A 202       2.340  86.647  15.375  1.00104.59           C  
ANISOU 1401  CD  GLU A 202    14065  12403  13271    529    568    366       C  
ATOM   1402  OE1 GLU A 202       2.892  87.769  15.415  1.00109.69           O  
ANISOU 1402  OE1 GLU A 202    14890  12926  13863    484    614    372       O  
ATOM   1403  OE2 GLU A 202       1.889  86.086  16.401  1.00102.83           O  
ANISOU 1403  OE2 GLU A 202    13823  12176  13073    560    579    339       O  
ATOM   1404  N   GLU A 203       6.649  85.121  13.986  1.00 37.07           N  
ANISOU 1404  N   GLU A 203     5310   4098   4678     51    311    183       N  
ATOM   1405  CA  GLU A 203       8.058  85.037  13.613  1.00 31.44           C  
ANISOU 1405  CA  GLU A 203     4569   3450   3928    -90    257    148       C  
ATOM   1406  C   GLU A 203       8.575  83.618  13.741  1.00 36.61           C  
ANISOU 1406  C   GLU A 203     5065   4230   4616   -118    187     94       C  
ATOM   1407  O   GLU A 203       9.383  83.180  12.911  1.00 40.92           O  
ANISOU 1407  O   GLU A 203     5514   4884   5152   -170    139     82       O  
ATOM   1408  CB  GLU A 203       8.911  85.989  14.452  1.00 24.23           C  
ANISOU 1408  CB  GLU A 203     3824   2435   2947   -214    283    130       C  
ATOM   1409  CG  GLU A 203       8.351  87.387  14.522  1.00 33.14           C  
ANISOU 1409  CG  GLU A 203     5152   3404   4035   -179    367    178       C  
ATOM   1410  CD  GLU A 203       9.017  88.242  15.580  1.00 43.46           C  
ANISOU 1410  CD  GLU A 203     6656   4589   5270   -305    400    150       C  
ATOM   1411  OE1 GLU A 203       9.746  89.165  15.203  1.00 52.29           O  
ANISOU 1411  OE1 GLU A 203     7886   5662   6319   -418    410    164       O  
ATOM   1412  OE2 GLU A 203       8.851  87.973  16.789  1.00 55.64           O  
ANISOU 1412  OE2 GLU A 203     8241   6084   6815   -306    412    113       O  
ATOM   1413  N   LEU A 204       8.121  82.884  14.764  1.00 38.26           N  
ANISOU 1413  N   LEU A 204     5252   4424   4861    -77    185     64       N  
ATOM   1414  CA  LEU A 204       8.536  81.493  14.905  1.00 30.60           C  
ANISOU 1414  CA  LEU A 204     4145   3558   3921    -88    126     18       C  
ATOM   1415  C   LEU A 204       7.993  80.639  13.760  1.00 33.41           C  
ANISOU 1415  C   LEU A 204     4370   4010   4316    -17     98     27       C  
ATOM   1416  O   LEU A 204       8.716  79.802  13.205  1.00 36.16           O  
ANISOU 1416  O   LEU A 204     4620   4456   4664    -47     51     -1       O  
ATOM   1417  CB  LEU A 204       8.093  80.942  16.258  1.00 31.14           C  
ANISOU 1417  CB  LEU A 204     4234   3582   4017    -60    135    -10       C  
ATOM   1418  CG  LEU A 204       8.439  79.467  16.500  1.00 36.75           C  
ANISOU 1418  CG  LEU A 204     4822   4382   4758    -59     80    -54       C  
ATOM   1419  CD1 LEU A 204       9.949  79.254  16.414  1.00 28.50           C  
ANISOU 1419  CD1 LEU A 204     3737   3416   3675   -157     36    -78       C  
ATOM   1420  CD2 LEU A 204       7.875  78.956  17.851  1.00 37.06           C  
ANISOU 1420  CD2 LEU A 204     4888   4370   4824    -28     93    -74       C  
ATOM   1421  N   ALA A 205       6.729  80.863  13.374  1.00 34.12           N  
ANISOU 1421  N   ALA A 205     4458   4076   4429     77    128     72       N  
ATOM   1422  CA  ALA A 205       6.122  80.121  12.269  1.00 33.15           C  
ANISOU 1422  CA  ALA A 205     4217   4048   4329    128    100     87       C  
ATOM   1423  C   ALA A 205       6.848  80.375  10.952  1.00 37.47           C  
ANISOU 1423  C   ALA A 205     4730   4665   4844     84     76     97       C  
ATOM   1424  O   ALA A 205       7.063  79.446  10.157  1.00 39.57           O  
ANISOU 1424  O   ALA A 205     4896   5026   5113     77     35     73       O  
ATOM   1425  CB  ALA A 205       4.641  80.496  12.130  1.00 24.63           C  
ANISOU 1425  CB  ALA A 205     3141   2949   3268    230    139    151       C  
ATOM   1426  N   ARG A 206       7.207  81.629  10.688  1.00 32.42           N  
ANISOU 1426  N   ARG A 206     4181   3972   4166     53    107    133       N  
ATOM   1427  CA  ARG A 206       7.931  81.937   9.462  1.00 38.26           C  
ANISOU 1427  CA  ARG A 206     4891   4777   4869      3     87    147       C  
ATOM   1428  C   ARG A 206       9.291  81.249   9.454  1.00 44.73           C  
ANISOU 1428  C   ARG A 206     5651   5676   5670    -83     43     91       C  
ATOM   1429  O   ARG A 206       9.686  80.640   8.450  1.00 34.50           O  
ANISOU 1429  O   ARG A 206     4262   4482   4364    -91     12     79       O  
ATOM   1430  CB  ARG A 206       8.083  83.448   9.312  1.00 37.56           C  
ANISOU 1430  CB  ARG A 206     4933   4601   4737    -24    133    198       C  
ATOM   1431  CG  ARG A 206       8.379  83.922   7.897  1.00 60.96           C  
ANISOU 1431  CG  ARG A 206     7872   7623   7665    -45    125    238       C  
ATOM   1432  CD  ARG A 206       7.983  85.388   7.737  1.00 80.99           C  
ANISOU 1432  CD  ARG A 206    10552  10051  10169    -23    184    309       C  
ATOM   1433  NE  ARG A 206       7.802  86.030   9.040  1.00 92.71           N  
ANISOU 1433  NE  ARG A 206    12181  11395  11651    -21    235    304       N  
ATOM   1434  CZ  ARG A 206       6.968  87.037   9.285  1.00 86.69           C  
ANISOU 1434  CZ  ARG A 206    11550  10511  10879     59    305    362       C  
ATOM   1435  NH1 ARG A 206       6.220  87.545   8.306  1.00 77.84           N  
ANISOU 1435  NH1 ARG A 206    10424   9399   9753    149    330    440       N  
ATOM   1436  NH2 ARG A 206       6.891  87.534  10.519  1.00 79.67           N  
ANISOU 1436  NH2 ARG A 206    10801   9492   9979     53    353    346       N  
ATOM   1437  N   GLU A 207      10.008  81.311  10.585  1.00 36.28           N  
ANISOU 1437  N   GLU A 207     4629   4567   4589   -145     43     60       N  
ATOM   1438  CA  GLU A 207      11.326  80.685  10.669  1.00 41.69           C  
ANISOU 1438  CA  GLU A 207     5246   5344   5250   -218      4     22       C  
ATOM   1439  C   GLU A 207      11.236  79.180  10.431  1.00 43.91           C  
ANISOU 1439  C   GLU A 207     5409   5708   5567   -157    -28    -18       C  
ATOM   1440  O   GLU A 207      12.065  78.607   9.710  1.00 35.90           O  
ANISOU 1440  O   GLU A 207     4313   4795   4531   -173    -53    -33       O  
ATOM   1441  CB  GLU A 207      11.966  80.993  12.034  1.00 45.26           C  
ANISOU 1441  CB  GLU A 207     5768   5748   5680   -293      8      3       C  
ATOM   1442  CG  GLU A 207      13.363  80.394  12.294  1.00 44.42           C  
ANISOU 1442  CG  GLU A 207     5583   5754   5541   -368    -32    -22       C  
ATOM   1443  CD  GLU A 207      14.446  80.873  11.304  1.00 55.16           C  
ANISOU 1443  CD  GLU A 207     6904   7212   6843   -450    -46      1       C  
ATOM   1444  OE1 GLU A 207      15.573  80.320  11.351  1.00 52.91           O  
ANISOU 1444  OE1 GLU A 207     6529   7048   6528   -494    -76     -8       O  
ATOM   1445  OE2 GLU A 207      14.181  81.788  10.481  1.00 45.33           O  
ANISOU 1445  OE2 GLU A 207     5714   5931   5577   -467    -25     35       O  
ATOM   1446  N   LEU A 208      10.210  78.529  10.992  1.00 39.11           N  
ANISOU 1446  N   LEU A 208     4797   5055   5007    -86    -24    -31       N  
ATOM   1447  CA  LEU A 208      10.117  77.079  10.868  1.00 38.45           C  
ANISOU 1447  CA  LEU A 208     4629   5030   4951    -41    -52    -72       C  
ATOM   1448  C   LEU A 208       9.738  76.670   9.452  1.00 28.39           C  
ANISOU 1448  C   LEU A 208     3294   3822   3671    -10    -63    -67       C  
ATOM   1449  O   LEU A 208      10.311  75.721   8.899  1.00 24.00           O  
ANISOU 1449  O   LEU A 208     2678   3339   3103     -4    -83   -100       O  
ATOM   1450  CB  LEU A 208       9.126  76.524  11.899  1.00 39.19           C  
ANISOU 1450  CB  LEU A 208     4742   5058   5089      9    -44    -84       C  
ATOM   1451  CG  LEU A 208       9.667  76.556  13.344  1.00 37.63           C  
ANISOU 1451  CG  LEU A 208     4591   4814   4893    -24    -41   -103       C  
ATOM   1452  CD1 LEU A 208       8.562  76.349  14.396  1.00 34.88           C  
ANISOU 1452  CD1 LEU A 208     4282   4387   4583     21    -22   -104       C  
ATOM   1453  CD2 LEU A 208      10.790  75.551  13.541  1.00 30.77           C  
ANISOU 1453  CD2 LEU A 208     3660   4018   4012    -40    -72   -139       C  
ATOM   1454  N   ARG A 209       8.781  77.371   8.845  1.00 40.13           N  
ANISOU 1454  N   ARG A 209     4800   5288   5159     15    -47    -21       N  
ATOM   1455  CA  ARG A 209       8.462  77.116   7.440  1.00 42.40           C  
ANISOU 1455  CA  ARG A 209     5031   5649   5428     29    -62     -9       C  
ATOM   1456  C   ARG A 209       9.664  77.379   6.546  1.00 42.50           C  
ANISOU 1456  C   ARG A 209     5021   5732   5395    -20    -69    -13       C  
ATOM   1457  O   ARG A 209       9.967  76.583   5.645  1.00 39.74           O  
ANISOU 1457  O   ARG A 209     4614   5461   5024    -16    -87    -40       O  
ATOM   1458  CB  ARG A 209       7.292  77.982   6.993  1.00 39.07           C  
ANISOU 1458  CB  ARG A 209     4631   5205   5009     66    -42     57       C  
ATOM   1459  CG  ARG A 209       7.017  77.870   5.520  1.00 37.86           C  
ANISOU 1459  CG  ARG A 209     4421   5138   4825     68    -60     80       C  
ATOM   1460  CD  ARG A 209       5.556  77.612   5.275  1.00 39.03           C  
ANISOU 1460  CD  ARG A 209     4533   5310   4987    118    -65    118       C  
ATOM   1461  NE  ARG A 209       5.259  77.521   3.851  1.00 50.20           N  
ANISOU 1461  NE  ARG A 209     5894   6818   6362    109    -86    144       N  
ATOM   1462  CZ  ARG A 209       4.871  76.405   3.243  1.00 55.32           C  
ANISOU 1462  CZ  ARG A 209     6485   7540   6994     91   -120    112       C  
ATOM   1463  NH1 ARG A 209       4.741  75.281   3.943  1.00 46.62           N  
ANISOU 1463  NH1 ARG A 209     5379   6420   5916     85   -133     55       N  
ATOM   1464  NH2 ARG A 209       4.612  76.413   1.938  1.00 60.46           N  
ANISOU 1464  NH2 ARG A 209     7094   8278   7598     74   -139    138       N  
ATOM   1465  N   LYS A 210      10.351  78.506   6.780  1.00 40.56           N  
ANISOU 1465  N   LYS A 210     4828   5458   5124    -72    -53     15       N  
ATOM   1466  CA  LYS A 210      11.599  78.805   6.082  1.00 31.61           C  
ANISOU 1466  CA  LYS A 210     3668   4401   3940   -134    -59     17       C  
ATOM   1467  C   LYS A 210      12.550  77.615   6.097  1.00 36.35           C  
ANISOU 1467  C   LYS A 210     4192   5088   4531   -131    -79    -34       C  
ATOM   1468  O   LYS A 210      13.213  77.330   5.093  1.00 34.89           O  
ANISOU 1468  O   LYS A 210     3950   4996   4309   -139    -85    -40       O  
ATOM   1469  CB  LYS A 210      12.261  80.027   6.719  1.00 42.68           C  
ANISOU 1469  CB  LYS A 210     5150   5752   5314   -213    -42     45       C  
ATOM   1470  CG  LYS A 210      13.151  80.835   5.799  1.00 44.26           C  
ANISOU 1470  CG  LYS A 210     5351   6013   5454   -289    -40     77       C  
ATOM   1471  CD  LYS A 210      14.471  81.166   6.483  1.00 47.22           C  
ANISOU 1471  CD  LYS A 210     5734   6421   5786   -392    -47     72       C  
ATOM   1472  CE  LYS A 210      15.201  79.885   6.906  1.00 55.45           C  
ANISOU 1472  CE  LYS A 210     6675   7557   6837   -369    -71     26       C  
ATOM   1473  NZ  LYS A 210      16.509  80.109   7.607  1.00 61.38           N  
ANISOU 1473  NZ  LYS A 210     7408   8375   7540   -467    -84     31       N  
ATOM   1474  N   ARG A 211      12.627  76.905   7.222  1.00 35.10           N  
ANISOU 1474  N   ARG A 211     4033   4900   4403   -111    -85    -68       N  
ATOM   1475  CA  ARG A 211      13.487  75.735   7.344  1.00 28.33           C  
ANISOU 1475  CA  ARG A 211     3112   4115   3537    -87    -96   -108       C  
ATOM   1476  C   ARG A 211      12.820  74.450   6.867  1.00 34.03           C  
ANISOU 1476  C   ARG A 211     3810   4841   4280    -14   -101   -148       C  
ATOM   1477  O   ARG A 211      13.485  73.410   6.835  1.00 20.60           O  
ANISOU 1477  O   ARG A 211     2072   3188   2566     23   -101   -182       O  
ATOM   1478  CB  ARG A 211      13.964  75.582   8.809  1.00 27.05           C  
ANISOU 1478  CB  ARG A 211     2964   3925   3389   -102   -101   -118       C  
ATOM   1479  CG  ARG A 211      14.682  76.831   9.367  1.00 30.11           C  
ANISOU 1479  CG  ARG A 211     3390   4309   3741   -199    -99    -83       C  
ATOM   1480  CD  ARG A 211      15.104  76.689  10.839  1.00 36.25           C  
ANISOU 1480  CD  ARG A 211     4185   5065   4522   -227   -108    -92       C  
ATOM   1481  NE  ARG A 211      16.071  77.709  11.272  1.00 27.13           N  
ANISOU 1481  NE  ARG A 211     3054   3943   3311   -344   -113    -61       N  
ATOM   1482  CZ  ARG A 211      17.383  77.503  11.424  1.00 28.55           C  
ANISOU 1482  CZ  ARG A 211     3157   4249   3440   -393   -131    -49       C  
ATOM   1483  NH1 ARG A 211      17.929  76.314  11.166  1.00 28.97           N  
ANISOU 1483  NH1 ARG A 211     3107   4403   3496   -315   -139    -62       N  
ATOM   1484  NH2 ARG A 211      18.165  78.497  11.822  1.00 25.45           N  
ANISOU 1484  NH2 ARG A 211     2794   3887   2987   -523   -139    -18       N  
ATOM   1485  N   ASN A 212      11.542  74.505   6.474  1.00 36.08           N  
ANISOU 1485  N   ASN A 212     4094   5055   4561      4   -103   -140       N  
ATOM   1486  CA  ASN A 212      10.718  73.315   6.193  1.00 35.73           C  
ANISOU 1486  CA  ASN A 212     4043   5002   4531     47   -111   -176       C  
ATOM   1487  C   ASN A 212      10.773  72.310   7.333  1.00 34.54           C  
ANISOU 1487  C   ASN A 212     3907   4805   4410     79   -113   -214       C  
ATOM   1488  O   ASN A 212      10.992  71.106   7.130  1.00 26.93           O  
ANISOU 1488  O   ASN A 212     2940   3857   3437    112   -113   -258       O  
ATOM   1489  CB  ASN A 212      11.109  72.610   4.894  1.00 23.39           C  
ANISOU 1489  CB  ASN A 212     2449   3515   2922     58   -112   -204       C  
ATOM   1490  CG  ASN A 212      10.116  71.492   4.535  1.00 28.21           C  
ANISOU 1490  CG  ASN A 212     3078   4108   3534     76   -122   -240       C  
ATOM   1491  OD1 ASN A 212       8.950  71.567   4.912  1.00 35.09           O  
ANISOU 1491  OD1 ASN A 212     3964   4935   4435     69   -134   -222       O  
ATOM   1492  ND2 ASN A 212      10.587  70.437   3.856  1.00 33.37           N  
ANISOU 1492  ND2 ASN A 212     3735   4795   4148     97   -115   -288       N  
ATOM   1493  N   ALA A 213      10.560  72.796   8.548  1.00 35.37           N  
ANISOU 1493  N   ALA A 213     4041   4848   4549     70   -110   -198       N  
ATOM   1494  CA  ALA A 213      10.950  71.994   9.692  1.00 33.72           C  
ANISOU 1494  CA  ALA A 213     3842   4611   4361     92   -112   -226       C  
ATOM   1495  C   ALA A 213       9.870  71.932  10.764  1.00 39.31           C  
ANISOU 1495  C   ALA A 213     4590   5234   5113    100   -111   -223       C  
ATOM   1496  O   ALA A 213       9.045  72.846  10.919  1.00 36.28           O  
ANISOU 1496  O   ALA A 213     4231   4811   4745     88   -102   -188       O  
ATOM   1497  CB  ALA A 213      12.257  72.528  10.265  1.00 32.64           C  
ANISOU 1497  CB  ALA A 213     3688   4513   4202     63   -111   -212       C  
ATOM   1498  N   THR A 214       9.884  70.813  11.487  1.00 37.42           N  
ANISOU 1498  N   THR A 214     4359   4968   4890    130   -116   -255       N  
ATOM   1499  CA  THR A 214       9.153  70.647  12.733  1.00 27.56           C  
ANISOU 1499  CA  THR A 214     3146   3648   3678    135   -114   -254       C  
ATOM   1500  C   THR A 214      10.131  70.735  13.901  1.00 30.93           C  
ANISOU 1500  C   THR A 214     3581   4068   4104    130   -114   -255       C  
ATOM   1501  O   THR A 214      11.142  70.025  13.924  1.00 33.67           O  
ANISOU 1501  O   THR A 214     3902   4459   4431    153   -119   -271       O  
ATOM   1502  CB  THR A 214       8.415  69.302  12.789  1.00 29.75           C  
ANISOU 1502  CB  THR A 214     3438   3897   3970    159   -120   -286       C  
ATOM   1503  OG1 THR A 214       7.425  69.234  11.751  1.00 30.88           O  
ANISOU 1503  OG1 THR A 214     3570   4059   4103    145   -127   -281       O  
ATOM   1504  CG2 THR A 214       7.713  69.117  14.174  1.00 25.79           C  
ANISOU 1504  CG2 THR A 214     2968   3327   3503    162   -117   -281       C  
ATOM   1505  N   ALA A 215       9.824  71.598  14.867  1.00 25.59           N  
ANISOU 1505  N   ALA A 215     2941   3341   3441    102   -105   -232       N  
ATOM   1506  CA  ALA A 215      10.497  71.587  16.153  1.00 24.54           C  
ANISOU 1506  CA  ALA A 215     2826   3195   3303     86   -109   -234       C  
ATOM   1507  C   ALA A 215       9.804  70.594  17.073  1.00 33.02           C  
ANISOU 1507  C   ALA A 215     3923   4215   4410    121   -109   -252       C  
ATOM   1508  O   ALA A 215       8.565  70.519  17.112  1.00 32.16           O  
ANISOU 1508  O   ALA A 215     3834   4056   4328    133    -99   -249       O  
ATOM   1509  CB  ALA A 215      10.500  72.978  16.793  1.00 27.00           C  
ANISOU 1509  CB  ALA A 215     3191   3467   3602     29    -94   -207       C  
ATOM   1510  N   VAL A 216      10.618  69.846  17.821  1.00 30.50           N  
ANISOU 1510  N   VAL A 216     3593   3914   4083    136   -121   -262       N  
ATOM   1511  CA  VAL A 216      10.175  68.737  18.661  1.00 31.30           C  
ANISOU 1511  CA  VAL A 216     3718   3968   4207    171   -123   -279       C  
ATOM   1512  C   VAL A 216      10.671  68.998  20.073  1.00 41.01           C  
ANISOU 1512  C   VAL A 216     4966   5189   5428    147   -128   -265       C  
ATOM   1513  O   VAL A 216      11.886  69.094  20.303  1.00 44.26           O  
ANISOU 1513  O   VAL A 216     5344   5667   5805    135   -141   -252       O  
ATOM   1514  CB  VAL A 216      10.698  67.378  18.161  1.00 36.78           C  
ANISOU 1514  CB  VAL A 216     4394   4690   4892    230   -127   -301       C  
ATOM   1515  CG1 VAL A 216      10.066  66.236  18.969  1.00 25.81           C  
ANISOU 1515  CG1 VAL A 216     3049   3232   3524    259   -126   -316       C  
ATOM   1516  CG2 VAL A 216      10.440  67.206  16.652  1.00 32.29           C  
ANISOU 1516  CG2 VAL A 216     3811   4144   4314    241   -123   -318       C  
ATOM   1517  N   ALA A 217       9.742  69.107  21.016  1.00 36.27           N  
ANISOU 1517  N   ALA A 217     4414   4517   4851    137   -117   -264       N  
ATOM   1518  CA  ALA A 217      10.090  69.493  22.372  1.00 35.27           C  
ANISOU 1518  CA  ALA A 217     4319   4374   4709    103   -119   -252       C  
ATOM   1519  C   ALA A 217       9.403  68.570  23.363  1.00 34.82           C  
ANISOU 1519  C   ALA A 217     4291   4262   4676    131   -116   -260       C  
ATOM   1520  O   ALA A 217       8.417  67.891  23.043  1.00 30.70           O  
ANISOU 1520  O   ALA A 217     3776   3703   4185    161   -108   -271       O  
ATOM   1521  CB  ALA A 217       9.709  70.955  22.663  1.00 24.81           C  
ANISOU 1521  CB  ALA A 217     3047   3008   3371     48    -96   -239       C  
ATOM   1522  N   GLU A 218       9.943  68.545  24.576  1.00 32.07           N  
ANISOU 1522  N   GLU A 218     3961   3917   4307    110   -125   -251       N  
ATOM   1523  CA  GLU A 218       9.302  67.856  25.691  1.00 35.79           C  
ANISOU 1523  CA  GLU A 218     4469   4333   4795    126   -120   -253       C  
ATOM   1524  C   GLU A 218       8.718  68.907  26.615  1.00 35.85           C  
ANISOU 1524  C   GLU A 218     4537   4290   4793     78    -96   -247       C  
ATOM   1525  O   GLU A 218       9.438  69.792  27.095  1.00 31.87           O  
ANISOU 1525  O   GLU A 218     4055   3805   4248     21    -99   -239       O  
ATOM   1526  CB  GLU A 218      10.276  66.954  26.446  1.00 29.53           C  
ANISOU 1526  CB  GLU A 218     3659   3581   3981    147   -144   -241       C  
ATOM   1527  CG  GLU A 218       9.587  65.839  27.202  1.00 32.45           C  
ANISOU 1527  CG  GLU A 218     4063   3892   4373    183   -139   -245       C  
ATOM   1528  CD  GLU A 218       9.310  64.621  26.346  1.00 41.99           C  
ANISOU 1528  CD  GLU A 218     5269   5081   5604    243   -137   -261       C  
ATOM   1529  OE1 GLU A 218       8.900  63.583  26.917  1.00 40.83           O  
ANISOU 1529  OE1 GLU A 218     5161   4886   5469    268   -135   -262       O  
ATOM   1530  OE2 GLU A 218       9.498  64.704  25.110  1.00 46.14           O  
ANISOU 1530  OE2 GLU A 218     5766   5635   6131    257   -136   -273       O  
ATOM   1531  N   LEU A 219       7.415  68.822  26.837  1.00 40.35           N  
ANISOU 1531  N   LEU A 219     5137   4799   5394     98    -68   -248       N  
ATOM   1532  CA  LEU A 219       6.726  69.714  27.757  1.00 39.18           C  
ANISOU 1532  CA  LEU A 219     5053   4595   5236     75    -32   -240       C  
ATOM   1533  C   LEU A 219       6.800  69.123  29.163  1.00 38.22           C  
ANISOU 1533  C   LEU A 219     4964   4456   5103     64    -38   -240       C  
ATOM   1534  O   LEU A 219       6.227  68.057  29.419  1.00 43.50           O  
ANISOU 1534  O   LEU A 219     5619   5111   5797     96    -42   -240       O  
ATOM   1535  CB  LEU A 219       5.276  69.889  27.314  1.00 27.48           C  
ANISOU 1535  CB  LEU A 219     3571   3081   3788    112      4   -229       C  
ATOM   1536  CG  LEU A 219       4.375  70.570  28.327  1.00 28.19           C  
ANISOU 1536  CG  LEU A 219     3725   3115   3872    118     54   -216       C  
ATOM   1537  CD1 LEU A 219       4.850  72.011  28.524  1.00 30.71           C  
ANISOU 1537  CD1 LEU A 219     4119   3400   4150     85     82   -215       C  
ATOM   1538  CD2 LEU A 219       2.936  70.512  27.864  1.00 31.72           C  
ANISOU 1538  CD2 LEU A 219     4141   3561   4349    166     86   -191       C  
ATOM   1539  N   CYS A 220       7.504  69.799  30.073  1.00 33.89           N  
ANISOU 1539  N   CYS A 220     4461   3908   4507     10    -39   -239       N  
ATOM   1540  CA  CYS A 220       7.667  69.299  31.441  1.00 39.25           C  
ANISOU 1540  CA  CYS A 220     5171   4580   5164     -8    -48   -235       C  
ATOM   1541  C   CYS A 220       7.282  70.391  32.430  1.00 38.63           C  
ANISOU 1541  C   CYS A 220     5187   4444   5047    -55     -8   -239       C  
ATOM   1542  O   CYS A 220       7.942  71.436  32.500  1.00 40.20           O  
ANISOU 1542  O   CYS A 220     5433   4645   5196   -120     -5   -243       O  
ATOM   1543  CB  CYS A 220       9.096  68.812  31.690  1.00 36.89           C  
ANISOU 1543  CB  CYS A 220     4827   4361   4827    -32    -99   -224       C  
ATOM   1544  SG  CYS A 220       9.705  67.652  30.405  1.00 35.63           S  
ANISOU 1544  SG  CYS A 220     4572   4266   4701     39   -132   -219       S  
ATOM   1545  N   ASP A 221       6.222  70.140  33.201  1.00 37.51           N  
ANISOU 1545  N   ASP A 221     5082   4249   4920    -26     28   -237       N  
ATOM   1546  CA  ASP A 221       5.717  71.116  34.163  1.00 41.59           C  
ANISOU 1546  CA  ASP A 221     5702   4702   5398    -52     81   -241       C  
ATOM   1547  C   ASP A 221       4.888  70.380  35.213  1.00 39.43           C  
ANISOU 1547  C   ASP A 221     5442   4404   5134    -26    100   -234       C  
ATOM   1548  O   ASP A 221       3.762  69.964  34.924  1.00 37.72           O  
ANISOU 1548  O   ASP A 221     5193   4176   4964     33    127   -222       O  
ATOM   1549  CB  ASP A 221       4.892  72.186  33.448  1.00 36.67           C  
ANISOU 1549  CB  ASP A 221     5117   4029   4788    -16    139   -238       C  
ATOM   1550  CG  ASP A 221       4.430  73.292  34.385  1.00 49.29           C  
ANISOU 1550  CG  ASP A 221     6845   5547   6337    -30    208   -242       C  
ATOM   1551  OD1 ASP A 221       4.998  73.405  35.504  1.00 45.79           O  
ANISOU 1551  OD1 ASP A 221     6470   5092   5837    -98    201   -257       O  
ATOM   1552  OD2 ASP A 221       3.500  74.048  33.997  1.00 51.00           O  
ANISOU 1552  OD2 ASP A 221     7099   5715   6565     31    273   -228       O  
ATOM   1553  N   ASP A 222       5.431  70.230  36.427  1.00 39.89           N  
ANISOU 1553  N   ASP A 222     5545   4467   5145    -77     85   -237       N  
ATOM   1554  CA  ASP A 222       4.664  69.588  37.499  1.00 44.47           C  
ANISOU 1554  CA  ASP A 222     6146   5023   5726    -58    106   -229       C  
ATOM   1555  C   ASP A 222       3.342  70.312  37.747  1.00 39.63           C  
ANISOU 1555  C   ASP A 222     5593   4348   5117    -17    188   -226       C  
ATOM   1556  O   ASP A 222       2.318  69.677  38.033  1.00 29.18           O  
ANISOU 1556  O   ASP A 222     4243   3021   3823     28    213   -209       O  
ATOM   1557  CB  ASP A 222       5.476  69.545  38.796  1.00 49.53           C  
ANISOU 1557  CB  ASP A 222     6840   5679   6300   -128     82   -230       C  
ATOM   1558  CG  ASP A 222       6.571  68.480  38.789  1.00 52.94           C  
ANISOU 1558  CG  ASP A 222     7195   6188   6731   -139      6   -213       C  
ATOM   1559  OD1 ASP A 222       6.655  67.685  37.824  1.00 43.37           O  
ANISOU 1559  OD1 ASP A 222     5903   5003   5572    -86    -21   -205       O  
ATOM   1560  OD2 ASP A 222       7.353  68.451  39.775  1.00 62.61           O  
ANISOU 1560  OD2 ASP A 222     8445   7448   7894   -198    -23   -204       O  
ATOM   1561  N   SER A 223       3.350  71.646  37.652  1.00 35.62           N  
ANISOU 1561  N   SER A 223     5169   3793   4573    -29    235   -238       N  
ATOM   1562  CA  SER A 223       2.123  72.424  37.788  1.00 41.95           C  
ANISOU 1562  CA  SER A 223     6030   4535   5374     35    325   -227       C  
ATOM   1563  C   SER A 223       1.104  72.125  36.689  1.00 37.71           C  
ANISOU 1563  C   SER A 223     5395   4028   4905    121    341   -197       C  
ATOM   1564  O   SER A 223      -0.086  72.378  36.876  1.00 35.09           O  
ANISOU 1564  O   SER A 223     5070   3682   4581    190    410   -170       O  
ATOM   1565  CB  SER A 223       2.449  73.919  37.784  1.00 42.70           C  
ANISOU 1565  CB  SER A 223     6254   4560   5412      8    375   -244       C  
ATOM   1566  OG  SER A 223       2.852  74.349  39.058  1.00 42.91           O  
ANISOU 1566  OG  SER A 223     6402   4542   5359    -62    394   -268       O  
ATOM   1567  N   PHE A 224       1.527  71.633  35.534  1.00 32.25           N  
ANISOU 1567  N   PHE A 224     4612   3385   4255    118    283   -196       N  
ATOM   1568  CA  PHE A 224       0.479  71.200  34.621  1.00 40.50           C  
ANISOU 1568  CA  PHE A 224     5565   4470   5355    182    293   -166       C  
ATOM   1569  C   PHE A 224       0.105  69.741  34.878  1.00 39.54           C  
ANISOU 1569  C   PHE A 224     5370   4391   5263    174    255   -157       C  
ATOM   1570  O   PHE A 224      -1.072  69.431  35.089  1.00 37.40           O  
ANISOU 1570  O   PHE A 224     5065   4139   5005    209    290   -127       O  
ATOM   1571  CB  PHE A 224       0.908  71.429  33.163  1.00 28.31           C  
ANISOU 1571  CB  PHE A 224     3967   2955   3836    187    261   -167       C  
ATOM   1572  CG  PHE A 224       0.040  70.724  32.163  1.00 31.22           C  
ANISOU 1572  CG  PHE A 224     4229   3381   4252    225    247   -140       C  
ATOM   1573  CD1 PHE A 224       0.566  69.724  31.345  1.00 35.01           C  
ANISOU 1573  CD1 PHE A 224     4640   3905   4758    197    180   -155       C  
ATOM   1574  CD2 PHE A 224      -1.307  71.044  32.039  1.00 32.38           C  
ANISOU 1574  CD2 PHE A 224     4347   3547   4408    288    304    -96       C  
ATOM   1575  CE1 PHE A 224      -0.237  69.055  30.417  1.00 36.38           C  
ANISOU 1575  CE1 PHE A 224     4730   4130   4962    213    165   -135       C  
ATOM   1576  CE2 PHE A 224      -2.122  70.370  31.114  1.00 27.40           C  
ANISOU 1576  CE2 PHE A 224     3611   2990   3809    303    284    -66       C  
ATOM   1577  CZ  PHE A 224      -1.589  69.375  30.309  1.00 23.65           C  
ANISOU 1577  CZ  PHE A 224     3082   2548   3356    256    213    -89       C  
ATOM   1578  N   GLU A 225       1.106  68.857  34.911  1.00 34.61           N  
ANISOU 1578  N   GLU A 225     4726   3782   4641    128    187   -179       N  
ATOM   1579  CA  GLU A 225       0.919  67.414  35.015  1.00 35.60           C  
ANISOU 1579  CA  GLU A 225     4804   3933   4791    119    148   -173       C  
ATOM   1580  C   GLU A 225       2.223  66.798  35.501  1.00 37.07           C  
ANISOU 1580  C   GLU A 225     5008   4121   4957     84     94   -191       C  
ATOM   1581  O   GLU A 225       3.288  67.109  34.964  1.00 37.92           O  
ANISOU 1581  O   GLU A 225     5106   4246   5055     71     63   -205       O  
ATOM   1582  CB  GLU A 225       0.537  66.809  33.656  1.00 40.04           C  
ANISOU 1582  CB  GLU A 225     5288   4532   5394    134    123   -167       C  
ATOM   1583  CG  GLU A 225      -0.314  65.551  33.718  1.00 54.02           C  
ANISOU 1583  CG  GLU A 225     7024   6319   7182    121    112   -151       C  
ATOM   1584  CD  GLU A 225      -0.219  64.717  32.449  1.00 61.50           C  
ANISOU 1584  CD  GLU A 225     7925   7290   8152    110     69   -160       C  
ATOM   1585  OE1 GLU A 225      -0.140  63.469  32.550  1.00 62.96           O  
ANISOU 1585  OE1 GLU A 225     8121   7461   8340     86     39   -166       O  
ATOM   1586  OE2 GLU A 225      -0.209  65.314  31.352  1.00 61.00           O  
ANISOU 1586  OE2 GLU A 225     7826   7253   8100    126     68   -161       O  
ATOM   1587  N   GLU A 226       2.142  65.920  36.497  1.00 39.82           N  
ANISOU 1587  N   GLU A 226     5374   4460   5295     71     84   -182       N  
ATOM   1588  CA  GLU A 226       3.329  65.252  37.013  1.00 38.80           C  
ANISOU 1588  CA  GLU A 226     5255   4344   5144     51     35   -185       C  
ATOM   1589  C   GLU A 226       3.575  63.976  36.228  1.00 44.24           C  
ANISOU 1589  C   GLU A 226     5901   5043   5864     76     -5   -182       C  
ATOM   1590  O   GLU A 226       2.636  63.264  35.861  1.00 45.30           O  
ANISOU 1590  O   GLU A 226     6022   5162   6027     84      4   -177       O  
ATOM   1591  CB  GLU A 226       3.183  64.908  38.500  1.00 38.29           C  
ANISOU 1591  CB  GLU A 226     5240   4263   5046     29     44   -171       C  
ATOM   1592  CG  GLU A 226       3.569  65.991  39.493  1.00 39.53           C  
ANISOU 1592  CG  GLU A 226     5463   4413   5145    -11     65   -179       C  
ATOM   1593  CD  GLU A 226       3.175  65.629  40.924  1.00 41.73           C  
ANISOU 1593  CD  GLU A 226     5791   4674   5389    -31     83   -166       C  
ATOM   1594  OE1 GLU A 226       2.670  66.503  41.673  1.00 40.05           O  
ANISOU 1594  OE1 GLU A 226     5645   4433   5140    -48    136   -173       O  
ATOM   1595  OE2 GLU A 226       3.345  64.450  41.295  1.00 38.81           O  
ANISOU 1595  OE2 GLU A 226     5405   4314   5026    -26     49   -146       O  
ATOM   1596  N   HIS A 227       4.847  63.688  35.976  1.00 47.97           N  
ANISOU 1596  N   HIS A 227     6356   5546   6324     87    -46   -183       N  
ATOM   1597  CA  HIS A 227       5.209  62.375  35.465  1.00 46.71           C  
ANISOU 1597  CA  HIS A 227     6181   5384   6181    124    -75   -178       C  
ATOM   1598  C   HIS A 227       5.957  61.618  36.560  1.00 42.61           C  
ANISOU 1598  C   HIS A 227     5687   4871   5630    136    -98   -152       C  
ATOM   1599  O   HIS A 227       5.396  61.392  37.635  1.00 46.03           O  
ANISOU 1599  O   HIS A 227     6161   5278   6052    113    -85   -139       O  
ATOM   1600  CB  HIS A 227       5.987  62.526  34.155  1.00 42.64           C  
ANISOU 1600  CB  HIS A 227     5620   4905   5676    152    -94   -191       C  
ATOM   1601  CG  HIS A 227       5.101  62.879  33.002  1.00 35.75           C  
ANISOU 1601  CG  HIS A 227     4726   4021   4836    148    -75   -211       C  
ATOM   1602  ND1 HIS A 227       4.633  61.944  32.103  1.00 35.43           N  
ANISOU 1602  ND1 HIS A 227     4682   3959   4818    163    -78   -220       N  
ATOM   1603  CD2 HIS A 227       4.517  64.052  32.659  1.00 34.01           C  
ANISOU 1603  CD2 HIS A 227     4492   3807   4623    128    -49   -217       C  
ATOM   1604  CE1 HIS A 227       3.831  62.531  31.233  1.00 34.24           C  
ANISOU 1604  CE1 HIS A 227     4503   3819   4687    147    -63   -229       C  
ATOM   1605  NE2 HIS A 227       3.752  63.813  31.543  1.00 37.77           N  
ANISOU 1605  NE2 HIS A 227     4941   4282   5127    135    -43   -223       N  
ATOM   1606  N   ILE A 228       7.203  61.231  36.333  1.00 34.94           N  
ANISOU 1606  N   ILE A 228     4690   3946   4642    174   -130   -137       N  
ATOM   1607  CA  ILE A 228       7.977  60.484  37.315  1.00 30.81           C  
ANISOU 1607  CA  ILE A 228     4179   3444   4083    200   -153    -98       C  
ATOM   1608  C   ILE A 228       9.070  61.348  37.935  1.00 39.63           C  
ANISOU 1608  C   ILE A 228     5262   4650   5146    165   -180    -77       C  
ATOM   1609  O   ILE A 228       9.133  61.498  39.158  1.00 52.47           O  
ANISOU 1609  O   ILE A 228     6914   6289   6732    126   -186    -58       O  
ATOM   1610  CB  ILE A 228       8.559  59.194  36.702  1.00 34.61           C  
ANISOU 1610  CB  ILE A 228     4660   3915   4573    286   -164    -80       C  
ATOM   1611  CG1 ILE A 228       7.414  58.236  36.350  1.00 43.55           C  
ANISOU 1611  CG1 ILE A 228     5856   4949   5742    291   -139    -99       C  
ATOM   1612  CG2 ILE A 228       9.554  58.581  37.651  1.00 37.47           C  
ANISOU 1612  CG2 ILE A 228     5021   4324   4893    330   -187    -27       C  
ATOM   1613  CD1 ILE A 228       6.465  57.926  37.524  1.00 38.42           C  
ANISOU 1613  CD1 ILE A 228     5261   4248   5087    245   -126    -87       C  
ATOM   1614  N   LEU A 229       9.953  61.910  37.113  1.00 33.31           N  
ANISOU 1614  N   LEU A 229     4403   3919   4335    169   -197    -80       N  
ATOM   1615  CA  LEU A 229      10.929  62.838  37.660  1.00 37.18           C  
ANISOU 1615  CA  LEU A 229     4862   4502   4763    106   -224    -60       C  
ATOM   1616  C   LEU A 229      10.314  64.228  37.754  1.00 39.19           C  
ANISOU 1616  C   LEU A 229     5159   4722   5009     17   -199    -99       C  
ATOM   1617  O   LEU A 229       9.309  64.537  37.104  1.00 37.85           O  
ANISOU 1617  O   LEU A 229     5015   4481   4887     24   -163   -134       O  
ATOM   1618  CB  LEU A 229      12.203  62.864  36.819  1.00 48.52           C  
ANISOU 1618  CB  LEU A 229     6214   6043   6180    139   -253    -37       C  
ATOM   1619  CG  LEU A 229      12.937  61.528  36.684  1.00 51.56           C  
ANISOU 1619  CG  LEU A 229     6559   6468   6563    251   -267     10       C  
ATOM   1620  CD1 LEU A 229      12.485  60.789  35.432  1.00 53.96           C  
ANISOU 1620  CD1 LEU A 229     6876   6701   6927    334   -239    -19       C  
ATOM   1621  CD2 LEU A 229      14.424  61.753  36.659  1.00 43.64           C  
ANISOU 1621  CD2 LEU A 229     5460   5621   5500    257   -304     64       C  
ATOM   1622  N   ALA A 230      10.918  65.068  38.587  1.00 42.77           N  
ANISOU 1622  N   ALA A 230     5628   5228   5393    -68   -216    -89       N  
ATOM   1623  CA  ALA A 230      10.264  66.302  38.988  1.00 42.63           C  
ANISOU 1623  CA  ALA A 230     5690   5153   5354   -148   -180   -124       C  
ATOM   1624  C   ALA A 230      10.659  67.469  38.093  1.00 35.32           C  
ANISOU 1624  C   ALA A 230     4759   4246   4414   -198   -177   -145       C  
ATOM   1625  O   ALA A 230      11.760  67.521  37.542  1.00 43.74           O  
ANISOU 1625  O   ALA A 230     5756   5407   5456   -212   -216   -125       O  
ATOM   1626  CB  ALA A 230      10.587  66.628  40.443  1.00 21.58           C  
ANISOU 1626  CB  ALA A 230     3077   2513   2609   -230   -193   -110       C  
ATOM   1627  N   TYR A 231       9.744  68.422  37.969  1.00 36.96           N  
ANISOU 1627  N   TYR A 231     5043   4368   4633   -222   -126   -180       N  
ATOM   1628  CA  TYR A 231      10.008  69.640  37.200  1.00 43.32           C  
ANISOU 1628  CA  TYR A 231     5870   5169   5419   -273   -113   -199       C  
ATOM   1629  C   TYR A 231       9.282  70.788  37.917  1.00 38.92           C  
ANISOU 1629  C   TYR A 231     5444   4520   4824   -329    -55   -227       C  
ATOM   1630  O   TYR A 231       8.135  71.116  37.586  1.00 32.38           O  
ANISOU 1630  O   TYR A 231     4658   3607   4040   -273      3   -243       O  
ATOM   1631  CB  TYR A 231       9.549  69.488  35.755  1.00 34.67           C  
ANISOU 1631  CB  TYR A 231     4720   4054   4397   -197    -98   -209       C  
ATOM   1632  CG  TYR A 231      10.351  68.518  34.894  1.00 33.35           C  
ANISOU 1632  CG  TYR A 231     4444   3970   4257   -143   -144   -189       C  
ATOM   1633  CD1 TYR A 231       9.952  67.196  34.738  1.00 35.28           C  
ANISOU 1633  CD1 TYR A 231     4650   4202   4553    -55   -149   -181       C  
ATOM   1634  CD2 TYR A 231      11.486  68.946  34.189  1.00 36.29           C  
ANISOU 1634  CD2 TYR A 231     4762   4431   4597   -180   -176   -177       C  
ATOM   1635  CE1 TYR A 231      10.672  66.319  33.925  1.00 32.66           C  
ANISOU 1635  CE1 TYR A 231     4240   3931   4239      6   -178   -165       C  
ATOM   1636  CE2 TYR A 231      12.218  68.080  33.366  1.00 22.46           C  
ANISOU 1636  CE2 TYR A 231     2912   2757   2865   -115   -207   -156       C  
ATOM   1637  CZ  TYR A 231      11.798  66.773  33.238  1.00 35.18           C  
ANISOU 1637  CZ  TYR A 231     4499   4341   4526    -16   -204   -152       C  
ATOM   1638  OH  TYR A 231      12.514  65.911  32.434  1.00 35.42           O  
ANISOU 1638  OH  TYR A 231     4454   4435   4569     59   -223   -134       O  
ATOM   1639  N   GLY A 232       9.959  71.375  38.918  1.00 32.02           N  
ANISOU 1639  N   GLY A 232     4637   3669   3858   -437    -69   -227       N  
ATOM   1640  CA  GLY A 232       9.452  72.515  39.654  1.00 38.01           C  
ANISOU 1640  CA  GLY A 232     5546   4336   4559   -501    -11   -256       C  
ATOM   1641  C   GLY A 232       9.182  73.713  38.763  1.00 40.14           C  
ANISOU 1641  C   GLY A 232     5885   4535   4830   -510     36   -278       C  
ATOM   1642  O   GLY A 232       9.254  73.617  37.543  1.00 44.86           O  
ANISOU 1642  O   GLY A 232     6403   5157   5484   -461     24   -271       O  
ATOM   1643  N   PRO A 233       8.839  74.860  39.350  1.00 44.44           N  
ANISOU 1643  N   PRO A 233     6589   4985   5310   -568     96   -305       N  
ATOM   1644  CA  PRO A 233       8.473  76.017  38.509  1.00 39.12           C  
ANISOU 1644  CA  PRO A 233     6001   4225   4639   -558    154   -320       C  
ATOM   1645  C   PRO A 233       9.614  76.524  37.649  1.00 44.79           C  
ANISOU 1645  C   PRO A 233     6689   5006   5324   -649    105   -315       C  
ATOM   1646  O   PRO A 233       9.431  76.710  36.434  1.00 50.77           O  
ANISOU 1646  O   PRO A 233     7397   5756   6136   -591    114   -308       O  
ATOM   1647  CB  PRO A 233       7.997  77.062  39.526  1.00 53.03           C  
ANISOU 1647  CB  PRO A 233     7964   5866   6318   -607    233   -349       C  
ATOM   1648  CG  PRO A 233       8.370  76.530  40.864  1.00 59.39           C  
ANISOU 1648  CG  PRO A 233     8783   6716   7065   -678    199   -352       C  
ATOM   1649  CD  PRO A 233       8.459  75.051  40.758  1.00 50.26           C  
ANISOU 1649  CD  PRO A 233     7445   5666   5984   -607    134   -321       C  
ATOM   1650  N   ASP A 234      10.785  76.774  38.227  1.00 43.46           N  
ANISOU 1650  N   ASP A 234     6544   4909   5061   -798     52   -314       N  
ATOM   1651  CA  ASP A 234      11.962  76.748  37.374  1.00 45.76           C  
ANISOU 1651  CA  ASP A 234     6728   5320   5337   -865    -17   -291       C  
ATOM   1652  C   ASP A 234      12.147  75.320  36.892  1.00 53.48           C  
ANISOU 1652  C   ASP A 234     7511   6409   6399   -756    -72   -259       C  
ATOM   1653  O   ASP A 234      11.538  74.397  37.427  1.00 70.40           O  
ANISOU 1653  O   ASP A 234     9618   8540   8590   -669    -67   -255       O  
ATOM   1654  CB  ASP A 234      13.183  77.237  38.134  1.00 53.05           C  
ANISOU 1654  CB  ASP A 234     7697   6327   6133  -1055    -69   -285       C  
ATOM   1655  CG  ASP A 234      12.841  78.317  39.137  1.00 70.68           C  
ANISOU 1655  CG  ASP A 234    10153   8434   8270  -1160    -10   -323       C  
ATOM   1656  OD1 ASP A 234      13.135  78.131  40.340  1.00 67.82           O  
ANISOU 1656  OD1 ASP A 234     9829   8106   7833  -1243    -33   -324       O  
ATOM   1657  OD2 ASP A 234      12.268  79.351  38.717  1.00 82.13           O  
ANISOU 1657  OD2 ASP A 234    11746   9747   9714  -1154     63   -351       O  
ATOM   1658  N   LYS A 235      12.984  75.122  35.882  1.00 33.66           N  
ANISOU 1658  N   LYS A 235     4883   4003   3903   -761   -120   -236       N  
ATOM   1659  CA  LYS A 235      13.052  73.800  35.230  1.00 41.29           C  
ANISOU 1659  CA  LYS A 235     5688   5048   4953   -636   -154   -211       C  
ATOM   1660  C   LYS A 235      11.825  73.489  34.359  1.00 37.02           C  
ANISOU 1660  C   LYS A 235     5137   4415   4516   -498   -106   -228       C  
ATOM   1661  O   LYS A 235      11.926  72.676  33.435  1.00 37.86           O  
ANISOU 1661  O   LYS A 235     5130   4572   4681   -414   -128   -215       O  
ATOM   1662  CB  LYS A 235      13.252  72.641  36.245  1.00 29.69           C  
ANISOU 1662  CB  LYS A 235     4159   3641   3480   -604   -190   -187       C  
ATOM   1663  CG  LYS A 235      14.633  72.603  36.895  1.00 53.92           C  
ANISOU 1663  CG  LYS A 235     7174   6859   6453   -715   -256   -148       C  
ATOM   1664  CD  LYS A 235      14.594  72.079  38.338  1.00 77.16           C  
ANISOU 1664  CD  LYS A 235    10145   9816   9355   -736   -272   -134       C  
ATOM   1665  CE  LYS A 235      14.875  70.575  38.421  1.00 84.61           C  
ANISOU 1665  CE  LYS A 235    10959  10844  10345   -618   -309    -89       C  
ATOM   1666  NZ  LYS A 235      16.096  70.251  39.228  1.00 84.71           N  
ANISOU 1666  NZ  LYS A 235    10898  11021  10267   -688   -375    -30       N  
ATOM   1667  N   ALA A 236      10.671  74.107  34.626  1.00 32.59           N  
ANISOU 1667  N   ALA A 236     4688   3724   3969   -471    -39   -253       N  
ATOM   1668  CA  ALA A 236       9.456  73.817  33.861  1.00 38.40           C  
ANISOU 1668  CA  ALA A 236     5401   4396   4794   -347      4   -257       C  
ATOM   1669  C   ALA A 236       9.467  74.521  32.505  1.00 35.81           C  
ANISOU 1669  C   ALA A 236     5062   4059   4485   -336     18   -257       C  
ATOM   1670  O   ALA A 236       9.937  75.650  32.382  1.00 39.60           O  
ANISOU 1670  O   ALA A 236     5623   4516   4908   -420     31   -262       O  
ATOM   1671  CB  ALA A 236       8.216  74.249  34.644  1.00 29.31           C  
ANISOU 1671  CB  ALA A 236     4361   3131   3645   -311     77   -270       C  
ATOM   1672  N   GLY A 237       8.932  73.864  31.494  1.00 37.95           N  
ANISOU 1672  N   GLY A 237     5243   4345   4831   -240     16   -250       N  
ATOM   1673  CA  GLY A 237       8.826  74.483  30.183  1.00 38.06           C  
ANISOU 1673  CA  GLY A 237     5243   4354   4865   -220     30   -245       C  
ATOM   1674  C   GLY A 237       8.986  73.455  29.073  1.00 38.80           C  
ANISOU 1674  C   GLY A 237     5205   4524   5013   -157     -9   -238       C  
ATOM   1675  O   GLY A 237       8.805  72.246  29.290  1.00 31.82           O  
ANISOU 1675  O   GLY A 237     4259   3666   4164   -106    -30   -238       O  
ATOM   1676  N   LEU A 238       9.328  73.977  27.880  1.00 33.55           N  
ANISOU 1676  N   LEU A 238     4513   3886   4348   -165    -13   -233       N  
ATOM   1677  CA  LEU A 238       9.475  73.180  26.659  1.00 32.84           C  
ANISOU 1677  CA  LEU A 238     4316   3862   4300   -110    -41   -229       C  
ATOM   1678  C   LEU A 238      10.951  72.909  26.407  1.00 40.36           C  
ANISOU 1678  C   LEU A 238     5199   4921   5214   -157    -90   -222       C  
ATOM   1679  O   LEU A 238      11.716  73.837  26.119  1.00 38.07           O  
ANISOU 1679  O   LEU A 238     4927   4663   4875   -234    -96   -214       O  
ATOM   1680  CB  LEU A 238       8.870  73.886  25.452  1.00 25.85           C  
ANISOU 1680  CB  LEU A 238     3436   2951   3435    -81    -13   -222       C  
ATOM   1681  CG  LEU A 238       7.347  74.042  25.367  1.00 28.85           C  
ANISOU 1681  CG  LEU A 238     3845   3260   3856    -10     35   -212       C  
ATOM   1682  CD1 LEU A 238       6.972  74.975  24.206  1.00 34.87           C  
ANISOU 1682  CD1 LEU A 238     4619   4009   4621      9     62   -192       C  
ATOM   1683  CD2 LEU A 238       6.720  72.699  25.177  1.00 20.60           C  
ANISOU 1683  CD2 LEU A 238     2723   2243   2861     51     16   -217       C  
ATOM   1684  N   TYR A 239      11.340  71.635  26.501  1.00 33.92           N  
ANISOU 1684  N   TYR A 239     4308   4165   4416   -108   -122   -221       N  
ATOM   1685  CA  TYR A 239      12.713  71.201  26.273  1.00 34.17           C  
ANISOU 1685  CA  TYR A 239     4257   4315   4412   -121   -162   -202       C  
ATOM   1686  C   TYR A 239      12.864  70.817  24.810  1.00 39.61           C  
ANISOU 1686  C   TYR A 239     4876   5047   5126    -64   -164   -205       C  
ATOM   1687  O   TYR A 239      12.373  69.765  24.383  1.00 39.40           O  
ANISOU 1687  O   TYR A 239     4825   5002   5143     20   -160   -218       O  
ATOM   1688  CB  TYR A 239      13.059  70.020  27.175  1.00 37.18           C  
ANISOU 1688  CB  TYR A 239     4604   4730   4793    -79   -185   -191       C  
ATOM   1689  CG  TYR A 239      13.332  70.419  28.590  1.00 30.23           C  
ANISOU 1689  CG  TYR A 239     3773   3850   3864   -155   -195   -180       C  
ATOM   1690  CD1 TYR A 239      12.283  70.778  29.449  1.00 34.23           C  
ANISOU 1690  CD1 TYR A 239     4375   4247   4383   -171   -164   -199       C  
ATOM   1691  CD2 TYR A 239      14.622  70.457  29.076  1.00 25.89           C  
ANISOU 1691  CD2 TYR A 239     3171   3418   3247   -213   -234   -147       C  
ATOM   1692  CE1 TYR A 239      12.521  71.157  30.769  1.00 28.86           C  
ANISOU 1692  CE1 TYR A 239     3753   3562   3649   -247   -171   -193       C  
ATOM   1693  CE2 TYR A 239      14.878  70.838  30.409  1.00 28.25           C  
ANISOU 1693  CE2 TYR A 239     3520   3725   3490   -300   -248   -136       C  
ATOM   1694  CZ  TYR A 239      13.831  71.186  31.232  1.00 28.09           C  
ANISOU 1694  CZ  TYR A 239     3609   3582   3482   -317   -216   -163       C  
ATOM   1695  OH  TYR A 239      14.104  71.572  32.508  1.00 36.95           O  
ANISOU 1695  OH  TYR A 239     4789   4711   4539   -408   -227   -156       O  
ATOM   1696  N   LEU A 240      13.533  71.665  24.039  1.00 43.25           N  
ANISOU 1696  N   LEU A 240     5316   5565   5553   -118   -169   -194       N  
ATOM   1697  CA  LEU A 240      13.757  71.355  22.637  1.00 36.17           C  
ANISOU 1697  CA  LEU A 240     4354   4719   4671    -69   -169   -195       C  
ATOM   1698  C   LEU A 240      14.788  70.248  22.528  1.00 32.95           C  
ANISOU 1698  C   LEU A 240     3856   4417   4246    -11   -192   -180       C  
ATOM   1699  O   LEU A 240      15.941  70.427  22.932  1.00 37.85           O  
ANISOU 1699  O   LEU A 240     4426   5143   4812    -56   -215   -148       O  
ATOM   1700  CB  LEU A 240      14.228  72.594  21.882  1.00 36.53           C  
ANISOU 1700  CB  LEU A 240     4403   4799   4677   -148   -167   -182       C  
ATOM   1701  CG  LEU A 240      14.184  72.402  20.365  1.00 36.48           C  
ANISOU 1701  CG  LEU A 240     4345   4826   4689    -98   -160   -187       C  
ATOM   1702  CD1 LEU A 240      12.719  72.228  19.916  1.00 28.16           C  
ANISOU 1702  CD1 LEU A 240     3335   3670   3694    -38   -135   -209       C  
ATOM   1703  CD2 LEU A 240      14.902  73.537  19.633  1.00 39.59           C  
ANISOU 1703  CD2 LEU A 240     4730   5278   5034   -181   -163   -166       C  
ATOM   1704  N   HIS A 241      14.394  69.101  21.984  1.00 31.22           N  
ANISOU 1704  N   HIS A 241     3621   4176   4067     89   -182   -198       N  
ATOM   1705  CA  HIS A 241      15.385  68.069  21.717  1.00 30.14           C  
ANISOU 1705  CA  HIS A 241     3412   4131   3910    166   -188   -181       C  
ATOM   1706  C   HIS A 241      15.462  67.638  20.252  1.00 32.53           C  
ANISOU 1706  C   HIS A 241     3684   4458   4218    229   -171   -197       C  
ATOM   1707  O   HIS A 241      16.242  66.731  19.933  1.00 35.53           O  
ANISOU 1707  O   HIS A 241     4017   4905   4579    313   -164   -185       O  
ATOM   1708  CB  HIS A 241      15.168  66.842  22.628  1.00 22.34           C  
ANISOU 1708  CB  HIS A 241     2449   3099   2941    240   -188   -182       C  
ATOM   1709  CG  HIS A 241      13.753  66.352  22.697  1.00 31.02           C  
ANISOU 1709  CG  HIS A 241     3627   4065   4094    262   -171   -220       C  
ATOM   1710  ND1 HIS A 241      13.141  65.696  21.651  1.00 31.64           N  
ANISOU 1710  ND1 HIS A 241     3726   4099   4199    313   -153   -250       N  
ATOM   1711  CD2 HIS A 241      12.852  66.363  23.712  1.00 34.72           C  
ANISOU 1711  CD2 HIS A 241     4157   4449   4588    235   -169   -228       C  
ATOM   1712  CE1 HIS A 241      11.918  65.346  22.009  1.00 36.01           C  
ANISOU 1712  CE1 HIS A 241     4342   4553   4789    306   -145   -272       C  
ATOM   1713  NE2 HIS A 241      11.715  65.742  23.253  1.00 31.32           N  
ANISOU 1713  NE2 HIS A 241     3769   3934   4198    266   -152   -258       N  
ATOM   1714  N   GLY A 242      14.731  68.274  19.342  1.00 28.84           N  
ANISOU 1714  N   GLY A 242     3243   3946   3770    197   -161   -219       N  
ATOM   1715  CA  GLY A 242      14.812  67.864  17.953  1.00 30.80           C  
ANISOU 1715  CA  GLY A 242     3465   4223   4015    247   -146   -235       C  
ATOM   1716  C   GLY A 242      14.274  68.888  16.983  1.00 30.71           C  
ANISOU 1716  C   GLY A 242     3464   4198   4008    190   -142   -242       C  
ATOM   1717  O   GLY A 242      13.389  69.684  17.313  1.00 31.51           O  
ANISOU 1717  O   GLY A 242     3615   4227   4131    138   -141   -242       O  
ATOM   1718  N   ILE A 243      14.832  68.875  15.773  1.00 35.34           N  
ANISOU 1718  N   ILE A 243     4005   4856   4567    209   -134   -241       N  
ATOM   1719  CA  ILE A 243      14.255  69.572  14.627  1.00 33.86           C  
ANISOU 1719  CA  ILE A 243     3827   4656   4382    176   -128   -248       C  
ATOM   1720  C   ILE A 243      14.340  68.630  13.436  1.00 34.95           C  
ANISOU 1720  C   ILE A 243     3950   4822   4507    245   -113   -274       C  
ATOM   1721  O   ILE A 243      15.412  68.077  13.158  1.00 26.28           O  
ANISOU 1721  O   ILE A 243     2804   3806   3374    297   -103   -268       O  
ATOM   1722  CB  ILE A 243      14.960  70.909  14.314  1.00 34.23           C  
ANISOU 1722  CB  ILE A 243     3844   4772   4392     95   -134   -214       C  
ATOM   1723  CG1 ILE A 243      14.957  71.814  15.557  1.00 34.68           C  
ANISOU 1723  CG1 ILE A 243     3940   4791   4446     17   -145   -194       C  
ATOM   1724  CG2 ILE A 243      14.272  71.593  13.103  1.00 23.74           C  
ANISOU 1724  CG2 ILE A 243     2532   3422   3066     72   -125   -216       C  
ATOM   1725  CD1 ILE A 243      15.759  73.085  15.412  1.00 32.89           C  
ANISOU 1725  CD1 ILE A 243     3703   4624   4168    -83   -151   -161       C  
ATOM   1726  N   ASN A 244      13.203  68.415  12.758  1.00 37.34           N  
ANISOU 1726  N   ASN A 244     4294   5061   4831    246   -109   -300       N  
ATOM   1727  CA  ASN A 244      13.133  67.488  11.631  1.00 36.05           C  
ANISOU 1727  CA  ASN A 244     4142   4909   4647    294    -94   -333       C  
ATOM   1728  C   ASN A 244      12.667  68.194  10.366  1.00 42.84           C  
ANISOU 1728  C   ASN A 244     4991   5794   5492    251    -96   -330       C  
ATOM   1729  O   ASN A 244      11.941  69.199  10.415  1.00 37.73           O  
ANISOU 1729  O   ASN A 244     4347   5123   4864    197   -108   -306       O  
ATOM   1730  CB  ASN A 244      12.179  66.321  11.892  1.00 33.13           C  
ANISOU 1730  CB  ASN A 244     3841   4448   4299    322    -91   -370       C  
ATOM   1731  CG  ASN A 244      12.502  65.564  13.169  1.00 38.22           C  
ANISOU 1731  CG  ASN A 244     4508   5054   4959    366    -88   -370       C  
ATOM   1732  OD1 ASN A 244      13.673  65.398  13.552  1.00 35.65           O  
ANISOU 1732  OD1 ASN A 244     4145   4787   4614    414    -80   -351       O  
ATOM   1733  ND2 ASN A 244      11.455  65.086  13.831  1.00 27.95           N  
ANISOU 1733  ND2 ASN A 244     3264   3665   3690    351    -95   -384       N  
ATOM   1734  N   LEU A 245      13.080  67.634   9.227  1.00 30.33           N  
ANISOU 1734  N   LEU A 245     3400   4258   3868    285    -81   -352       N  
ATOM   1735  CA  LEU A 245      12.637  68.128   7.937  1.00 24.72           C  
ANISOU 1735  CA  LEU A 245     2682   3577   3134    248    -83   -352       C  
ATOM   1736  C   LEU A 245      11.260  67.555   7.639  1.00 32.17           C  
ANISOU 1736  C   LEU A 245     3680   4455   4090    228    -93   -378       C  
ATOM   1737  O   LEU A 245      11.022  66.355   7.820  1.00 25.02           O  
ANISOU 1737  O   LEU A 245     2829   3498   3180    258    -85   -418       O  
ATOM   1738  CB  LEU A 245      13.640  67.740   6.847  1.00 36.01           C  
ANISOU 1738  CB  LEU A 245     4086   5090   4507    289    -59   -366       C  
ATOM   1739  CG  LEU A 245      15.004  68.451   6.929  1.00 40.15           C  
ANISOU 1739  CG  LEU A 245     4533   5717   5007    291    -51   -326       C  
ATOM   1740  CD1 LEU A 245      15.825  68.259   5.661  1.00 46.16           C  
ANISOU 1740  CD1 LEU A 245     5259   6572   5706    324    -24   -332       C  
ATOM   1741  CD2 LEU A 245      14.847  69.942   7.249  1.00 39.83           C  
ANISOU 1741  CD2 LEU A 245     4469   5683   4983    204    -75   -280       C  
ATOM   1742  N   ASN A 246      10.344  68.405   7.185  1.00 40.45           N  
ANISOU 1742  N   ASN A 246     4715   5507   5145    174   -111   -351       N  
ATOM   1743  CA  ASN A 246       8.999  67.923   6.881  1.00 33.21           C  
ANISOU 1743  CA  ASN A 246     3831   4558   4231    143   -126   -362       C  
ATOM   1744  C   ASN A 246       9.034  67.248   5.513  1.00 36.38           C  
ANISOU 1744  C   ASN A 246     4252   4998   4572    134   -122   -397       C  
ATOM   1745  O   ASN A 246       8.641  67.819   4.492  1.00 41.06           O  
ANISOU 1745  O   ASN A 246     4819   5646   5137     96   -133   -376       O  
ATOM   1746  CB  ASN A 246       7.991  69.067   6.950  1.00 34.39           C  
ANISOU 1746  CB  ASN A 246     3951   4710   4405    105   -141   -307       C  
ATOM   1747  CG  ASN A 246       7.878  69.671   8.360  1.00 37.03           C  
ANISOU 1747  CG  ASN A 246     4289   4990   4790    116   -136   -279       C  
ATOM   1748  OD1 ASN A 246       8.168  69.012   9.350  1.00 29.45           O  
ANISOU 1748  OD1 ASN A 246     3355   3985   3852    137   -132   -303       O  
ATOM   1749  ND2 ASN A 246       7.419  70.911   8.442  1.00 41.88           N  
ANISOU 1749  ND2 ASN A 246     4890   5604   5420    103   -133   -226       N  
ATOM   1750  N   ILE A 247       9.553  66.017   5.503  1.00 42.00           N  
ANISOU 1750  N   ILE A 247     5019   5680   5258    174   -101   -450       N  
ATOM   1751  CA  ILE A 247       9.644  65.184   4.304  1.00 43.46           C  
ANISOU 1751  CA  ILE A 247     5255   5881   5376    171    -86   -497       C  
ATOM   1752  C   ILE A 247       9.378  63.735   4.699  1.00 40.41           C  
ANISOU 1752  C   ILE A 247     4972   5406   4976    186    -71   -551       C  
ATOM   1753  O   ILE A 247       9.507  63.373   5.874  1.00 46.65           O  
ANISOU 1753  O   ILE A 247     5780   6137   5808    223    -66   -549       O  
ATOM   1754  CB  ILE A 247      11.027  65.290   3.621  1.00 41.51           C  
ANISOU 1754  CB  ILE A 247     4983   5701   5090    232    -52   -503       C  
ATOM   1755  CG1 ILE A 247      12.152  65.047   4.626  1.00 38.01           C  
ANISOU 1755  CG1 ILE A 247     4522   5249   4670    315    -26   -497       C  
ATOM   1756  CG2 ILE A 247      11.204  66.611   2.898  1.00 35.29           C  
ANISOU 1756  CG2 ILE A 247     4114   5001   4294    195    -65   -456       C  
ATOM   1757  CD1 ILE A 247      13.534  65.168   3.995  1.00 41.98           C  
ANISOU 1757  CD1 ILE A 247     4979   5844   5129    378      9   -491       C  
ATOM   1758  N   PRO A 248       9.016  62.883   3.729  1.00 40.51           N  
ANISOU 1758  N   PRO A 248     5065   5404   4922    151    -63   -598       N  
ATOM   1759  CA  PRO A 248       8.728  61.477   4.093  1.00 34.78           C  
ANISOU 1759  CA  PRO A 248     4465   4576   4173    152    -45   -652       C  
ATOM   1760  C   PRO A 248       9.897  60.780   4.768  1.00 32.83           C  
ANISOU 1760  C   PRO A 248     4262   4277   3935    274      4   -671       C  
ATOM   1761  O   PRO A 248       9.700  60.035   5.740  1.00 39.49           O  
ANISOU 1761  O   PRO A 248     5170   5033   4802    293     10   -682       O  
ATOM   1762  CB  PRO A 248       8.376  60.828   2.744  1.00 31.36           C  
ANISOU 1762  CB  PRO A 248     4119   4147   3649     91    -38   -702       C  
ATOM   1763  CG  PRO A 248       7.956  61.949   1.876  1.00 30.90           C  
ANISOU 1763  CG  PRO A 248     3961   4197   3582     27    -74   -661       C  
ATOM   1764  CD  PRO A 248       8.827  63.107   2.284  1.00 33.08           C  
ANISOU 1764  CD  PRO A 248     4121   4531   3917     99    -69   -608       C  
ATOM   1765  N   GLU A 249      11.115  61.028   4.294  1.00 29.12           N  
ANISOU 1765  N   GLU A 249     3751   3870   3443    360     39   -665       N  
ATOM   1766  CA  GLU A 249      12.323  60.443   4.859  1.00 29.36           C  
ANISOU 1766  CA  GLU A 249     3798   3885   3473    492     89   -666       C  
ATOM   1767  C   GLU A 249      12.718  61.163   6.158  1.00 29.75           C  
ANISOU 1767  C   GLU A 249     3744   3964   3594    518     66   -608       C  
ATOM   1768  O   GLU A 249      12.262  62.271   6.443  1.00 32.28           O  
ANISOU 1768  O   GLU A 249     3980   4325   3959    446     22   -570       O  
ATOM   1769  CB  GLU A 249      13.445  60.517   3.822  1.00 36.82           C  
ANISOU 1769  CB  GLU A 249     4717   4915   4359    568    135   -670       C  
ATOM   1770  CG  GLU A 249      13.425  61.814   2.973  1.00 57.55           C  
ANISOU 1770  CG  GLU A 249     7231   7655   6981    497    104   -638       C  
ATOM   1771  CD  GLU A 249      12.525  61.754   1.727  1.00 73.40           C  
ANISOU 1771  CD  GLU A 249     9294   9660   8934    402     89   -674       C  
ATOM   1772  OE1 GLU A 249      11.604  60.911   1.691  1.00 80.16           O  
ANISOU 1772  OE1 GLU A 249    10261  10427   9769    347     81   -718       O  
ATOM   1773  OE2 GLU A 249      12.728  62.568   0.790  1.00 77.70           O  
ANISOU 1773  OE2 GLU A 249     9772  10299   9452    371     81   -655       O  
ATOM   1774  N   PHE A 250      13.577  60.524   6.958  1.00 29.29           N  
ANISOU 1774  N   PHE A 250     3702   3886   3542    626    100   -599       N  
ATOM   1775  CA  PHE A 250      13.957  61.068   8.264  1.00 31.99           C  
ANISOU 1775  CA  PHE A 250     3960   4254   3941    643     77   -547       C  
ATOM   1776  C   PHE A 250      15.304  61.773   8.171  1.00 36.28           C  
ANISOU 1776  C   PHE A 250     4384   4932   4470    701     90   -499       C  
ATOM   1777  O   PHE A 250      16.348  61.133   7.974  1.00 38.03           O  
ANISOU 1777  O   PHE A 250     4606   5195   4650    817    139   -493       O  
ATOM   1778  CB  PHE A 250      14.015  59.989   9.343  1.00 31.84           C  
ANISOU 1778  CB  PHE A 250     4019   4143   3935    713     97   -553       C  
ATOM   1779  CG  PHE A 250      14.317  60.531  10.722  1.00 32.80           C  
ANISOU 1779  CG  PHE A 250     4060   4293   4109    717     68   -500       C  
ATOM   1780  CD1 PHE A 250      13.706  61.698  11.173  1.00 39.31           C  
ANISOU 1780  CD1 PHE A 250     4816   5141   4980    613     19   -475       C  
ATOM   1781  CD2 PHE A 250      15.197  59.867  11.573  1.00 31.23           C  
ANISOU 1781  CD2 PHE A 250     3863   4097   3905    827     95   -473       C  
ATOM   1782  CE1 PHE A 250      13.965  62.207  12.456  1.00 28.13           C  
ANISOU 1782  CE1 PHE A 250     3344   3743   3601    606     -5   -432       C  
ATOM   1783  CE2 PHE A 250      15.466  60.357  12.853  1.00 34.69           C  
ANISOU 1783  CE2 PHE A 250     4230   4570   4382    818     65   -424       C  
ATOM   1784  CZ  PHE A 250      14.851  61.539  13.294  1.00 30.61           C  
ANISOU 1784  CZ  PHE A 250     3655   4070   3907    700     15   -408       C  
ATOM   1785  N   ILE A 251      15.278  63.088   8.348  1.00 28.92           N  
ANISOU 1785  N   ILE A 251     3353   4068   3566    621     50   -459       N  
ATOM   1786  CA  ILE A 251      16.481  63.902   8.411  1.00 31.51           C  
ANISOU 1786  CA  ILE A 251     3565   4529   3879    638     51   -406       C  
ATOM   1787  C   ILE A 251      16.291  64.840   9.592  1.00 28.52           C  
ANISOU 1787  C   ILE A 251     3138   4150   3549    563      6   -367       C  
ATOM   1788  O   ILE A 251      15.283  65.555   9.655  1.00 33.49           O  
ANISOU 1788  O   ILE A 251     3786   4727   4212    473    -25   -371       O  
ATOM   1789  CB  ILE A 251      16.719  64.680   7.103  1.00 30.76           C  
ANISOU 1789  CB  ILE A 251     3420   4521   3746    596     54   -402       C  
ATOM   1790  CG1 ILE A 251      16.915  63.698   5.924  1.00 35.97           C  
ANISOU 1790  CG1 ILE A 251     4143   5178   4347    671    104   -447       C  
ATOM   1791  CG2 ILE A 251      17.888  65.655   7.266  1.00 24.47           C  
ANISOU 1791  CG2 ILE A 251     2501   3865   2931    581     47   -340       C  
ATOM   1792  CD1 ILE A 251      17.249  64.332   4.529  1.00 24.45           C  
ANISOU 1792  CD1 ILE A 251     2638   3815   2838    642    115   -444       C  
ATOM   1793  N   THR A 252      17.225  64.808  10.546  1.00 30.70           N  
ANISOU 1793  N   THR A 252     3358   4486   3822    605      7   -325       N  
ATOM   1794  CA  THR A 252      17.111  65.579  11.783  1.00 31.78           C  
ANISOU 1794  CA  THR A 252     3465   4617   3992    533    -32   -292       C  
ATOM   1795  C   THR A 252      18.362  66.429  12.017  1.00 36.19           C  
ANISOU 1795  C   THR A 252     3914   5323   4515    504    -43   -233       C  
ATOM   1796  O   THR A 252      19.481  66.041  11.651  1.00 36.42           O  
ANISOU 1796  O   THR A 252     3875   5466   4496    578    -17   -206       O  
ATOM   1797  CB  THR A 252      16.842  64.642  12.998  1.00 35.20           C  
ANISOU 1797  CB  THR A 252     3953   4968   4455    586    -32   -298       C  
ATOM   1798  OG1 THR A 252      16.210  65.389  14.029  1.00 39.67           O  
ANISOU 1798  OG1 THR A 252     4528   5485   5060    498    -67   -286       O  
ATOM   1799  CG2 THR A 252      18.127  64.010  13.571  1.00 24.65           C  
ANISOU 1799  CG2 THR A 252     2558   3723   3084    687    -12   -255       C  
ATOM   1800  N   TYR A 253      18.166  67.600  12.632  1.00 30.87           N  
ANISOU 1800  N   TYR A 253     3227   4647   3856    390    -78   -210       N  
ATOM   1801  CA  TYR A 253      19.294  68.482  12.927  1.00 41.53           C  
ANISOU 1801  CA  TYR A 253     4487   6133   5162    326    -95   -154       C  
ATOM   1802  C   TYR A 253      20.270  67.813  13.899  1.00 43.83           C  
ANISOU 1802  C   TYR A 253     4716   6510   5427    390    -96   -113       C  
ATOM   1803  O   TYR A 253      19.842  67.140  14.843  1.00 42.18           O  
ANISOU 1803  O   TYR A 253     4555   6220   5250    432   -100   -125       O  
ATOM   1804  CB  TYR A 253      18.825  69.783  13.573  1.00 41.18           C  
ANISOU 1804  CB  TYR A 253     4475   6039   5131    191   -127   -143       C  
ATOM   1805  CG  TYR A 253      18.265  70.865  12.686  1.00 37.62           C  
ANISOU 1805  CG  TYR A 253     4058   5554   4683    110   -128   -151       C  
ATOM   1806  CD1 TYR A 253      17.526  70.565  11.541  1.00 36.56           C  
ANISOU 1806  CD1 TYR A 253     3954   5370   4566    152   -110   -185       C  
ATOM   1807  CD2 TYR A 253      18.429  72.203  13.040  1.00 34.65           C  
ANISOU 1807  CD2 TYR A 253     3694   5186   4284    -15   -146   -122       C  
ATOM   1808  CE1 TYR A 253      16.986  71.571  10.760  1.00 30.51           C  
ANISOU 1808  CE1 TYR A 253     3215   4578   3800     85   -112   -181       C  
ATOM   1809  CE2 TYR A 253      17.901  73.210  12.275  1.00 35.79           C  
ANISOU 1809  CE2 TYR A 253     3882   5287   4429    -79   -142   -121       C  
ATOM   1810  CZ  TYR A 253      17.176  72.891  11.134  1.00 34.27           C  
ANISOU 1810  CZ  TYR A 253     3704   5057   4259    -22   -125   -147       C  
ATOM   1811  OH  TYR A 253      16.649  73.908  10.379  1.00 35.44           O  
ANISOU 1811  OH  TYR A 253     3892   5171   4404    -79   -121   -137       O  
ATOM   1812  N   PRO A 254      21.577  68.012  13.731  1.00 50.30           N  
ANISOU 1812  N   PRO A 254     5422   7505   6184    393    -94    -57       N  
ATOM   1813  CA  PRO A 254      22.517  67.665  14.812  1.00 42.22           C  
ANISOU 1813  CA  PRO A 254     4322   6591   5127    423   -108      1       C  
ATOM   1814  C   PRO A 254      22.249  68.488  16.069  1.00 44.50           C  
ANISOU 1814  C   PRO A 254     4639   6843   5425    289   -154     14       C  
ATOM   1815  O   PRO A 254      21.831  69.647  16.006  1.00 46.14           O  
ANISOU 1815  O   PRO A 254     4890   7006   5636    154   -175      1       O  
ATOM   1816  CB  PRO A 254      23.893  67.977  14.206  1.00 34.31           C  
ANISOU 1816  CB  PRO A 254     3181   5807   4048    421   -100     66       C  
ATOM   1817  CG  PRO A 254      23.626  68.745  12.948  1.00 36.47           C  
ANISOU 1817  CG  PRO A 254     3471   6069   4318    354    -91     39       C  
ATOM   1818  CD  PRO A 254      22.265  68.369  12.479  1.00 42.02           C  
ANISOU 1818  CD  PRO A 254     4303   6575   5087    391    -75    -40       C  
ATOM   1819  N   SER A 255      22.487  67.871  17.227  1.00 42.60           N  
ANISOU 1819  N   SER A 255     4386   6616   5182    333   -166     40       N  
ATOM   1820  CA  SER A 255      22.038  68.486  18.478  1.00 39.13           C  
ANISOU 1820  CA  SER A 255     4002   6111   4756    219   -204     38       C  
ATOM   1821  C   SER A 255      22.670  69.841  18.788  1.00 40.90           C  
ANISOU 1821  C   SER A 255     4185   6437   4918     43   -242     77       C  
ATOM   1822  O   SER A 255      21.951  70.711  19.320  1.00 38.33           O  
ANISOU 1822  O   SER A 255     3955   5999   4609    -74   -258     49       O  
ATOM   1823  CB  SER A 255      22.249  67.520  19.646  1.00 36.79           C  
ANISOU 1823  CB  SER A 255     3694   5825   4460    301   -211     66       C  
ATOM   1824  OG  SER A 255      21.501  66.326  19.444  1.00 28.98           O  
ANISOU 1824  OG  SER A 255     2780   4705   3527    441   -175     22       O  
ATOM   1825  N   PRO A 256      23.942  70.120  18.480  1.00 40.05           N  
ANISOU 1825  N   PRO A 256     3951   6532   4734      8   -253    141       N  
ATOM   1826  CA  PRO A 256      24.421  71.509  18.637  1.00 47.53           C  
ANISOU 1826  CA  PRO A 256     4886   7556   5617   -192   -288    170       C  
ATOM   1827  C   PRO A 256      23.582  72.510  17.857  1.00 45.52           C  
ANISOU 1827  C   PRO A 256     4738   7164   5392   -278   -276    118       C  
ATOM   1828  O   PRO A 256      23.420  73.647  18.304  1.00 42.96           O  
ANISOU 1828  O   PRO A 256     4489   6794   5041   -437   -296    115       O  
ATOM   1829  CB  PRO A 256      25.867  71.447  18.122  1.00 37.57           C  
ANISOU 1829  CB  PRO A 256     3455   6548   4273   -188   -293    249       C  
ATOM   1830  CG  PRO A 256      26.267  70.027  18.294  1.00 30.91           C  
ANISOU 1830  CG  PRO A 256     2532   5774   3439     10   -269    279       C  
ATOM   1831  CD  PRO A 256      25.020  69.224  18.018  1.00 31.08           C  
ANISOU 1831  CD  PRO A 256     2679   5572   3557    142   -231    198       C  
ATOM   1832  N   LEU A 257      23.027  72.116  16.708  1.00 39.19           N  
ANISOU 1832  N   LEU A 257     3956   6293   4640   -175   -240     79       N  
ATOM   1833  CA  LEU A 257      22.144  73.026  15.997  1.00 32.97           C  
ANISOU 1833  CA  LEU A 257     3269   5377   3881   -243   -229     38       C  
ATOM   1834  C   LEU A 257      20.803  73.136  16.702  1.00 33.54           C  
ANISOU 1834  C   LEU A 257     3476   5248   4020   -244   -225    -12       C  
ATOM   1835  O   LEU A 257      20.182  74.207  16.690  1.00 30.66           O  
ANISOU 1835  O   LEU A 257     3207   4783   3660   -339   -223    -27       O  
ATOM   1836  CB  LEU A 257      21.962  72.565  14.550  1.00 33.13           C  
ANISOU 1836  CB  LEU A 257     3263   5401   3924   -141   -195     16       C  
ATOM   1837  CG  LEU A 257      23.181  72.844  13.676  1.00 33.57           C  
ANISOU 1837  CG  LEU A 257     3201   5647   3906   -170   -192     66       C  
ATOM   1838  CD1 LEU A 257      22.903  72.439  12.252  1.00 30.85           C  
ANISOU 1838  CD1 LEU A 257     2851   5290   3580    -76   -156     38       C  
ATOM   1839  CD2 LEU A 257      23.586  74.329  13.748  1.00 34.30           C  
ANISOU 1839  CD2 LEU A 257     3309   5783   3940   -366   -218     99       C  
ATOM   1840  N   VAL A 258      20.346  72.051  17.332  1.00 26.29           N  
ANISOU 1840  N   VAL A 258     2571   4270   3149   -136   -220    -33       N  
ATOM   1841  CA  VAL A 258      19.123  72.139  18.126  1.00 36.02           C  
ANISOU 1841  CA  VAL A 258     3918   5333   4436   -142   -216    -72       C  
ATOM   1842  C   VAL A 258      19.314  73.097  19.301  1.00 34.28           C  
ANISOU 1842  C   VAL A 258     3749   5102   4175   -278   -239    -54       C  
ATOM   1843  O   VAL A 258      18.449  73.936  19.584  1.00 32.29           O  
ANISOU 1843  O   VAL A 258     3608   4721   3941   -340   -228    -78       O  
ATOM   1844  CB  VAL A 258      18.695  70.743  18.609  1.00 37.45           C  
ANISOU 1844  CB  VAL A 258     4102   5463   4664    -12   -208    -92       C  
ATOM   1845  CG1 VAL A 258      17.399  70.854  19.418  1.00 29.80           C  
ANISOU 1845  CG1 VAL A 258     3243   4332   3748    -25   -203   -128       C  
ATOM   1846  CG2 VAL A 258      18.549  69.787  17.421  1.00 36.54           C  
ANISOU 1846  CG2 VAL A 258     3960   5349   4574    110   -181   -115       C  
ATOM   1847  N   GLN A 259      20.450  72.991  19.998  1.00 26.14           N  
ANISOU 1847  N   GLN A 259     2640   4211   3081   -326   -269     -8       N  
ATOM   1848  CA  GLN A 259      20.663  73.825  21.181  1.00 41.01           C  
ANISOU 1848  CA  GLN A 259     4579   6090   4912   -469   -294      6       C  
ATOM   1849  C   GLN A 259      20.737  75.293  20.797  1.00 46.88           C  
ANISOU 1849  C   GLN A 259     5395   6810   5608   -624   -292      8       C  
ATOM   1850  O   GLN A 259      20.260  76.162  21.544  1.00 34.15           O  
ANISOU 1850  O   GLN A 259     3909   5088   3979   -725   -288    -10       O  
ATOM   1851  CB  GLN A 259      21.936  73.392  21.928  1.00 31.82           C  
ANISOU 1851  CB  GLN A 259     3299   5115   3678   -497   -332     67       C  
ATOM   1852  CG  GLN A 259      21.795  72.044  22.671  1.00 24.33           C  
ANISOU 1852  CG  GLN A 259     2315   4161   2767   -357   -332     70       C  
ATOM   1853  CD  GLN A 259      22.898  71.804  23.682  1.00 32.57           C  
ANISOU 1853  CD  GLN A 259     3266   5375   3735   -402   -373    137       C  
ATOM   1854  OE1 GLN A 259      23.894  72.528  23.723  1.00 39.93           O  
ANISOU 1854  OE1 GLN A 259     4131   6462   4579   -534   -404    186       O  
ATOM   1855  NE2 GLN A 259      22.709  70.796  24.531  1.00 36.48           N  
ANISOU 1855  NE2 GLN A 259     3756   5849   4257   -301   -375    143       N  
ATOM   1856  N   LYS A 260      21.319  75.587  19.625  1.00 43.67           N  
ANISOU 1856  N   LYS A 260     4920   6496   5175   -640   -289     29       N  
ATOM   1857  CA  LYS A 260      21.333  76.960  19.130  1.00 40.23           C  
ANISOU 1857  CA  LYS A 260     4566   6024   4697   -781   -282     32       C  
ATOM   1858  C   LYS A 260      19.910  77.461  18.880  1.00 39.96           C  
ANISOU 1858  C   LYS A 260     4677   5776   4729   -742   -242    -16       C  
ATOM   1859  O   LYS A 260      19.530  78.542  19.346  1.00 42.60           O  
ANISOU 1859  O   LYS A 260     5149   6000   5037   -847   -229    -24       O  
ATOM   1860  CB  LYS A 260      22.189  77.058  17.864  1.00 38.69           C  
ANISOU 1860  CB  LYS A 260     4260   5976   4464   -790   -284     67       C  
ATOM   1861  CG  LYS A 260      22.248  78.450  17.226  1.00 48.15           C  
ANISOU 1861  CG  LYS A 260     5542   7139   5614   -935   -276     75       C  
ATOM   1862  CD  LYS A 260      21.575  78.470  15.854  1.00 70.68           C  
ANISOU 1862  CD  LYS A 260     8408   9925   8523   -842   -242     55       C  
ATOM   1863  CE  LYS A 260      22.591  78.490  14.716  1.00 73.66           C  
ANISOU 1863  CE  LYS A 260     8662  10478   8849   -864   -248     95       C  
ATOM   1864  NZ  LYS A 260      21.942  78.649  13.373  1.00 77.58           N  
ANISOU 1864  NZ  LYS A 260     9183  10908   9385   -796   -217     77       N  
ATOM   1865  N   PHE A 261      19.097  76.665  18.176  1.00 43.93           N  
ANISOU 1865  N   PHE A 261     5157   6222   5312   -589   -220    -43       N  
ATOM   1866  CA  PHE A 261      17.701  77.036  17.940  1.00 37.58           C  
ANISOU 1866  CA  PHE A 261     4467   5244   4570   -540   -184    -76       C  
ATOM   1867  C   PHE A 261      16.946  77.257  19.256  1.00 36.88           C  
ANISOU 1867  C   PHE A 261     4489   5027   4496   -557   -173    -96       C  
ATOM   1868  O   PHE A 261      16.106  78.159  19.350  1.00 39.83           O  
ANISOU 1868  O   PHE A 261     4988   5267   4878   -581   -140   -105       O  
ATOM   1869  CB  PHE A 261      17.006  75.961  17.087  1.00 23.68           C  
ANISOU 1869  CB  PHE A 261     2648   3468   2881   -388   -171    -99       C  
ATOM   1870  CG  PHE A 261      15.707  76.425  16.451  1.00 33.23           C  
ANISOU 1870  CG  PHE A 261     3937   4551   4138   -346   -140   -115       C  
ATOM   1871  CD1 PHE A 261      14.487  76.238  17.099  1.00 34.95           C  
ANISOU 1871  CD1 PHE A 261     4225   4646   4409   -289   -120   -136       C  
ATOM   1872  CD2 PHE A 261      15.710  77.077  15.215  1.00 31.23           C  
ANISOU 1872  CD2 PHE A 261     3682   4313   3870   -364   -128   -100       C  
ATOM   1873  CE1 PHE A 261      13.290  76.680  16.515  1.00 43.63           C  
ANISOU 1873  CE1 PHE A 261     5380   5652   5545   -244    -90   -135       C  
ATOM   1874  CE2 PHE A 261      14.521  77.516  14.628  1.00 33.80           C  
ANISOU 1874  CE2 PHE A 261     4072   4539   4234   -319   -100   -101       C  
ATOM   1875  CZ  PHE A 261      13.310  77.317  15.269  1.00 39.85           C  
ANISOU 1875  CZ  PHE A 261     4896   5195   5051   -256    -81   -116       C  
ATOM   1876  N   ALA A 262      17.231  76.444  20.281  1.00 28.08           N  
ANISOU 1876  N   ALA A 262     3336   3952   3383   -536   -195    -99       N  
ATOM   1877  CA  ALA A 262      16.616  76.650  21.594  1.00 37.84           C  
ANISOU 1877  CA  ALA A 262     4676   5080   4622   -562   -184   -116       C  
ATOM   1878  C   ALA A 262      16.962  78.022  22.161  1.00 35.71           C  
ANISOU 1878  C   ALA A 262     4523   4771   4273   -724   -180   -107       C  
ATOM   1879  O   ALA A 262      16.093  78.727  22.699  1.00 31.95           O  
ANISOU 1879  O   ALA A 262     4190   4147   3802   -740   -142   -127       O  
ATOM   1880  CB  ALA A 262      17.064  75.556  22.571  1.00 38.12           C  
ANISOU 1880  CB  ALA A 262     4639   5188   4657   -526   -215   -110       C  
ATOM   1881  N   GLU A 263      18.237  78.402  22.085  1.00 31.17           N  
ANISOU 1881  N   GLU A 263     3896   4330   3616   -848   -214    -75       N  
ATOM   1882  CA  GLU A 263      18.636  79.698  22.610  1.00 38.27           C  
ANISOU 1882  CA  GLU A 263     4921   5195   4424  -1029   -213    -68       C  
ATOM   1883  C   GLU A 263      17.934  80.815  21.853  1.00 41.86           C  
ANISOU 1883  C   GLU A 263     5511   5509   4886  -1046   -164    -78       C  
ATOM   1884  O   GLU A 263      17.291  81.678  22.456  1.00 41.00           O  
ANISOU 1884  O   GLU A 263     5576   5246   4757  -1091   -123    -97       O  
ATOM   1885  CB  GLU A 263      20.157  79.842  22.539  1.00 41.75           C  
ANISOU 1885  CB  GLU A 263     5258   5835   4769  -1169   -265    -22       C  
ATOM   1886  CG  GLU A 263      20.855  79.529  23.853  1.00 56.01           C  
ANISOU 1886  CG  GLU A 263     7034   7737   6511  -1255   -307     -5       C  
ATOM   1887  CD  GLU A 263      22.322  79.174  23.684  1.00 67.98           C  
ANISOU 1887  CD  GLU A 263     8372   9504   7953  -1325   -363     57       C  
ATOM   1888  OE1 GLU A 263      22.799  78.242  24.376  1.00 74.69           O  
ANISOU 1888  OE1 GLU A 263     9108  10473   8796  -1278   -397     83       O  
ATOM   1889  OE2 GLU A 263      22.997  79.823  22.857  1.00 67.16           O  
ANISOU 1889  OE2 GLU A 263     8237   9485   7794  -1423   -371     85       O  
ATOM   1890  N   ASP A 264      17.990  80.775  20.517  1.00 44.24           N  
ANISOU 1890  N   ASP A 264     5739   5856   5215   -992   -160    -64       N  
ATOM   1891  CA  ASP A 264      17.407  81.853  19.726  1.00 42.61           C  
ANISOU 1891  CA  ASP A 264     5652   5531   5008  -1007   -115    -61       C  
ATOM   1892  C   ASP A 264      15.905  81.987  19.930  1.00 34.78           C  
ANISOU 1892  C   ASP A 264     4771   4357   4085   -885    -59    -85       C  
ATOM   1893  O   ASP A 264      15.359  83.068  19.710  1.00 40.45           O  
ANISOU 1893  O   ASP A 264     5636   4946   4786   -906    -11    -79       O  
ATOM   1894  CB  ASP A 264      17.698  81.645  18.240  1.00 44.13           C  
ANISOU 1894  CB  ASP A 264     5729   5818   5219   -959   -124    -40       C  
ATOM   1895  CG  ASP A 264      19.173  81.763  17.917  1.00 48.86           C  
ANISOU 1895  CG  ASP A 264     6229   6599   5736  -1089   -167     -5       C  
ATOM   1896  OD1 ASP A 264      19.619  81.063  16.982  1.00 53.16           O  
ANISOU 1896  OD1 ASP A 264     6624   7274   6300  -1021   -184     10       O  
ATOM   1897  OD2 ASP A 264      19.885  82.537  18.598  1.00 44.47           O  
ANISOU 1897  OD2 ASP A 264     5744   6063   5090  -1261   -182      9       O  
ATOM   1898  N   TRP A 265      15.216  80.927  20.338  1.00 34.12           N  
ANISOU 1898  N   TRP A 265     4624   4265   4075   -756    -61   -106       N  
ATOM   1899  CA  TRP A 265      13.760  80.961  20.371  1.00 36.48           C  
ANISOU 1899  CA  TRP A 265     4994   4425   4441   -631    -10   -117       C  
ATOM   1900  C   TRP A 265      13.207  80.649  21.755  1.00 36.93           C  
ANISOU 1900  C   TRP A 265     5112   4409   4511   -607      4   -140       C  
ATOM   1901  O   TRP A 265      12.009  80.368  21.898  1.00 36.79           O  
ANISOU 1901  O   TRP A 265     5114   4311   4554   -490     40   -147       O  
ATOM   1902  CB  TRP A 265      13.193  80.020  19.304  1.00 28.91           C  
ANISOU 1902  CB  TRP A 265     3907   3518   3560   -495    -19   -115       C  
ATOM   1903  CG  TRP A 265      13.442  80.557  17.922  1.00 32.08           C  
ANISOU 1903  CG  TRP A 265     4285   3957   3947   -509    -16    -91       C  
ATOM   1904  CD1 TRP A 265      14.423  80.169  17.052  1.00 29.87           C  
ANISOU 1904  CD1 TRP A 265     3888   3814   3648   -538    -54    -81       C  
ATOM   1905  CD2 TRP A 265      12.720  81.615  17.263  1.00 40.05           C  
ANISOU 1905  CD2 TRP A 265     5395   4867   4954   -490     30    -66       C  
ATOM   1906  NE1 TRP A 265      14.340  80.900  15.883  1.00 34.62           N  
ANISOU 1906  NE1 TRP A 265     4509   4410   4236   -547    -38    -57       N  
ATOM   1907  CE2 TRP A 265      13.306  81.793  15.989  1.00 39.09           C  
ANISOU 1907  CE2 TRP A 265     5209   4831   4813   -518     13    -45       C  
ATOM   1908  CE3 TRP A 265      11.627  82.416  17.620  1.00 33.44           C  
ANISOU 1908  CE3 TRP A 265     4696   3883   4127   -440     91    -54       C  
ATOM   1909  CZ2 TRP A 265      12.837  82.743  15.076  1.00 33.77           C  
ANISOU 1909  CZ2 TRP A 265     4606   4096   4130   -505     48    -12       C  
ATOM   1910  CZ3 TRP A 265      11.161  83.360  16.707  1.00 33.84           C  
ANISOU 1910  CZ3 TRP A 265     4816   3874   4169   -414    130    -17       C  
ATOM   1911  CH2 TRP A 265      11.767  83.514  15.453  1.00 33.19           C  
ANISOU 1911  CH2 TRP A 265     4668   3876   4068   -450    106      4       C  
ATOM   1912  N   GLY A 266      14.056  80.717  22.779  1.00 38.61           N  
ANISOU 1912  N   GLY A 266     5351   4659   4660   -722    -23   -148       N  
ATOM   1913  CA  GLY A 266      13.588  80.641  24.146  1.00 36.27           C  
ANISOU 1913  CA  GLY A 266     5140   4283   4357   -723     -4   -169       C  
ATOM   1914  C   GLY A 266      13.202  79.269  24.651  1.00 34.43           C  
ANISOU 1914  C   GLY A 266     4800   4093   4190   -616    -26   -182       C  
ATOM   1915  O   GLY A 266      12.472  79.190  25.646  1.00 35.96           O  
ANISOU 1915  O   GLY A 266     5067   4201   4395   -584      3   -198       O  
ATOM   1916  N   PHE A 267      13.642  78.185  23.997  1.00 29.87           N  
ANISOU 1916  N   PHE A 267     4061   3637   3650   -558    -70   -174       N  
ATOM   1917  CA  PHE A 267      13.404  76.866  24.570  1.00 33.83           C  
ANISOU 1917  CA  PHE A 267     4481   4172   4200   -472    -91   -184       C  
ATOM   1918  C   PHE A 267      14.430  76.567  25.663  1.00 35.60           C  
ANISOU 1918  C   PHE A 267     4681   4482   4365   -557   -133   -176       C  
ATOM   1919  O   PHE A 267      15.504  77.162  25.726  1.00 44.08           O  
ANISOU 1919  O   PHE A 267     5753   5634   5361   -681   -160   -158       O  
ATOM   1920  CB  PHE A 267      13.490  75.761  23.521  1.00 32.74           C  
ANISOU 1920  CB  PHE A 267     4205   4118   4116   -372   -114   -181       C  
ATOM   1921  CG  PHE A 267      12.383  75.780  22.518  1.00 36.29           C  
ANISOU 1921  CG  PHE A 267     4659   4504   4626   -282    -82   -186       C  
ATOM   1922  CD1 PHE A 267      12.543  76.435  21.297  1.00 32.77           C  
ANISOU 1922  CD1 PHE A 267     4203   4077   4170   -297    -75   -173       C  
ATOM   1923  CD2 PHE A 267      11.196  75.117  22.774  1.00 29.91           C  
ANISOU 1923  CD2 PHE A 267     3857   3630   3878   -190    -62   -199       C  
ATOM   1924  CE1 PHE A 267      11.511  76.453  20.367  1.00 33.02           C  
ANISOU 1924  CE1 PHE A 267     4232   4064   4250   -217    -49   -170       C  
ATOM   1925  CE2 PHE A 267      10.159  75.132  21.846  1.00 34.23           C  
ANISOU 1925  CE2 PHE A 267     4395   4141   4470   -117    -37   -195       C  
ATOM   1926  CZ  PHE A 267      10.313  75.798  20.644  1.00 28.06           C  
ANISOU 1926  CZ  PHE A 267     3604   3381   3678   -129    -32   -179       C  
ATOM   1927  N   ARG A 268      14.086  75.625  26.528  1.00 34.85           N  
ANISOU 1927  N   ARG A 268     4563   4378   4300   -495   -141   -184       N  
ATOM   1928  CA  ARG A 268      15.087  74.988  27.366  1.00 36.91           C  
ANISOU 1928  CA  ARG A 268     4755   4752   4516   -538   -188   -165       C  
ATOM   1929  C   ARG A 268      15.809  73.926  26.549  1.00 43.65           C  
ANISOU 1929  C   ARG A 268     5456   5736   5393   -459   -222   -143       C  
ATOM   1930  O   ARG A 268      15.200  73.228  25.730  1.00 46.03           O  
ANISOU 1930  O   ARG A 268     5718   6007   5764   -344   -206   -156       O  
ATOM   1931  CB  ARG A 268      14.439  74.374  28.608  1.00 36.80           C  
ANISOU 1931  CB  ARG A 268     4784   4676   4523   -497   -181   -178       C  
ATOM   1932  CG  ARG A 268      13.433  75.293  29.290  1.00 39.46           C  
ANISOU 1932  CG  ARG A 268     5277   4863   4851   -530   -128   -205       C  
ATOM   1933  CD  ARG A 268      12.971  74.726  30.606  1.00 50.12           C  
ANISOU 1933  CD  ARG A 268     6665   6175   6205   -509   -124   -213       C  
ATOM   1934  NE  ARG A 268      14.110  74.593  31.499  1.00 64.09           N  
ANISOU 1934  NE  ARG A 268     8406   8048   7896   -608   -174   -192       N  
ATOM   1935  CZ  ARG A 268      14.567  75.564  32.280  1.00 56.55           C  
ANISOU 1935  CZ  ARG A 268     7551   7085   6849   -752   -176   -195       C  
ATOM   1936  NH1 ARG A 268      13.962  76.750  32.311  1.00 43.86           N  
ANISOU 1936  NH1 ARG A 268     6098   5348   5217   -803   -121   -223       N  
ATOM   1937  NH2 ARG A 268      15.631  75.338  33.033  1.00 56.98           N  
ANISOU 1937  NH2 ARG A 268     7557   7264   6828   -845   -231   -167       N  
ATOM   1938  N   LYS A 269      17.118  73.829  26.754  1.00 39.69           N  
ANISOU 1938  N   LYS A 269     4870   5385   4825   -525   -265   -105       N  
ATOM   1939  CA  LYS A 269      17.964  72.949  25.965  1.00 34.13           C  
ANISOU 1939  CA  LYS A 269     4021   4820   4125   -448   -288    -74       C  
ATOM   1940  C   LYS A 269      18.047  71.557  26.576  1.00 37.93           C  
ANISOU 1940  C   LYS A 269     4440   5337   4634   -335   -300    -59       C  
ATOM   1941  O   LYS A 269      17.902  71.369  27.786  1.00 47.23           O  
ANISOU 1941  O   LYS A 269     5657   6491   5797   -357   -311    -56       O  
ATOM   1942  CB  LYS A 269      19.363  73.551  25.807  1.00 32.22           C  
ANISOU 1942  CB  LYS A 269     3703   4748   3791   -567   -324    -26       C  
ATOM   1943  CG  LYS A 269      19.336  75.044  25.516  1.00 42.18           C  
ANISOU 1943  CG  LYS A 269     5061   5960   5005   -716   -313    -38       C  
ATOM   1944  CD  LYS A 269      20.684  75.604  25.087  1.00 42.07           C  
ANISOU 1944  CD  LYS A 269     4962   6122   4900   -839   -348     11       C  
ATOM   1945  CE  LYS A 269      21.564  75.794  26.295  1.00 56.96           C  
ANISOU 1945  CE  LYS A 269     6830   8122   6689   -974   -393     49       C  
ATOM   1946  NZ  LYS A 269      21.546  77.172  26.848  1.00 66.52           N  
ANISOU 1946  NZ  LYS A 269     8192   9262   7820  -1174   -393     33       N  
ATOM   1947  N   THR A 270      18.262  70.573  25.710  1.00 37.50           N  
ANISOU 1947  N   THR A 270     4301   5333   4616   -209   -294    -51       N  
ATOM   1948  CA  THR A 270      18.396  69.182  26.114  1.00 34.76           C  
ANISOU 1948  CA  THR A 270     3906   5011   4291    -84   -297    -34       C  
ATOM   1949  C   THR A 270      19.879  68.845  26.160  1.00 42.41           C  
ANISOU 1949  C   THR A 270     4743   6178   5191    -72   -326     35       C  
ATOM   1950  O   THR A 270      20.614  69.107  25.195  1.00 32.86           O  
ANISOU 1950  O   THR A 270     3455   5076   3954    -76   -326     56       O  
ATOM   1951  CB  THR A 270      17.633  68.274  25.145  1.00 41.61           C  
ANISOU 1951  CB  THR A 270     4787   5791   5232     48   -263    -70       C  
ATOM   1952  OG1 THR A 270      16.238  68.613  25.198  1.00 34.83           O  
ANISOU 1952  OG1 THR A 270     4033   4773   4427     29   -240   -120       O  
ATOM   1953  CG2 THR A 270      17.805  66.799  25.490  1.00 37.16           C  
ANISOU 1953  CG2 THR A 270     4199   5237   4685    180   -258    -52       C  
ATOM   1954  N   GLY A 271      20.326  68.324  27.305  1.00 40.14           N  
ANISOU 1954  N   GLY A 271     4427   5954   4871    -63   -351     76       N  
ATOM   1955  CA  GLY A 271      21.747  68.095  27.501  1.00 32.54           C  
ANISOU 1955  CA  GLY A 271     3327   5205   3830    -60   -382    157       C  
ATOM   1956  C   GLY A 271      22.280  67.006  26.588  1.00 42.47           C  
ANISOU 1956  C   GLY A 271     4494   6539   5106    115   -356    187       C  
ATOM   1957  O   GLY A 271      21.583  66.049  26.250  1.00 44.37           O  
ANISOU 1957  O   GLY A 271     4790   6657   5413    250   -319    151       O  
ATOM   1958  N   LEU A 272      23.552  67.141  26.207  1.00 42.38           N  
ANISOU 1958  N   LEU A 272     4344   6736   5023    110   -371    256       N  
ATOM   1959  CA  LEU A 272      24.143  66.307  25.171  1.00 38.84           C  
ANISOU 1959  CA  LEU A 272     3808   6370   4578    272   -336    285       C  
ATOM   1960  C   LEU A 272      25.555  65.880  25.548  1.00 42.82           C  
ANISOU 1960  C   LEU A 272     4149   7122   4999    328   -355    396       C  
ATOM   1961  O   LEU A 272      26.339  66.666  26.097  1.00 42.87           O  
ANISOU 1961  O   LEU A 272     4071   7294   4924    184   -404    453       O  
ATOM   1962  CB  LEU A 272      24.184  67.047  23.828  1.00 35.25           C  
ANISOU 1962  CB  LEU A 272     3340   5929   4126    223   -319    254       C  
ATOM   1963  CG  LEU A 272      25.074  66.459  22.733  1.00 36.62           C  
ANISOU 1963  CG  LEU A 272     3399   6242   4273    357   -285    297       C  
ATOM   1964  CD1 LEU A 272      24.317  65.342  22.017  1.00 41.80           C  
ANISOU 1964  CD1 LEU A 272     4141   6739   5002    534   -228    239       C  
ATOM   1965  CD2 LEU A 272      25.516  67.533  21.737  1.00 29.45           C  
ANISOU 1965  CD2 LEU A 272     2436   5427   3327    242   -291    299       C  
ATOM   1966  N   ILE A 273      25.861  64.624  25.238  1.00 39.03           N  
ANISOU 1966  N   ILE A 273     3631   6665   4533    538   -312    428       N  
ATOM   1967  CA  ILE A 273      27.198  64.049  25.301  1.00 40.10           C  
ANISOU 1967  CA  ILE A 273     3601   7040   4593    652   -309    542       C  
ATOM   1968  C   ILE A 273      27.511  63.501  23.912  1.00 48.86           C  
ANISOU 1968  C   ILE A 273     4677   8174   5715    811   -245    538       C  
ATOM   1969  O   ILE A 273      26.633  62.942  23.240  1.00 43.86           O  
ANISOU 1969  O   ILE A 273     4170   7342   5153    903   -196    456       O  
ATOM   1970  CB  ILE A 273      27.279  62.931  26.368  1.00 42.74           C  
ANISOU 1970  CB  ILE A 273     3943   7369   4927    790   -305    595       C  
ATOM   1971  CG1 ILE A 273      27.044  63.502  27.763  1.00 48.76           C  
ANISOU 1971  CG1 ILE A 273     4733   8127   5665    624   -369    604       C  
ATOM   1972  CG2 ILE A 273      28.630  62.243  26.352  1.00 43.92           C  
ANISOU 1972  CG2 ILE A 273     3920   7766   5000    947   -289    723       C  
ATOM   1973  CD1 ILE A 273      26.522  62.498  28.780  1.00 46.27           C  
ANISOU 1973  CD1 ILE A 273     4502   7695   5385    729   -361    609       C  
ATOM   1974  N   ILE A 274      28.745  63.675  23.462  1.00 51.02           N  
ANISOU 1974  N   ILE A 274     4781   8696   5910    836   -243    626       N  
ATOM   1975  CA  ILE A 274      29.150  63.101  22.187  1.00 51.64           C  
ANISOU 1975  CA  ILE A 274     4818   8817   5985   1004   -174    633       C  
ATOM   1976  C   ILE A 274      30.280  62.124  22.453  1.00 51.82           C  
ANISOU 1976  C   ILE A 274     4705   9040   5945   1208   -142    755       C  
ATOM   1977  O   ILE A 274      31.316  62.496  23.020  1.00 60.09           O  
ANISOU 1977  O   ILE A 274     5581  10344   6907   1152   -185    865       O  
ATOM   1978  CB  ILE A 274      29.556  64.159  21.152  1.00 45.07           C  
ANISOU 1978  CB  ILE A 274     3910   8098   5118    877   -183    626       C  
ATOM   1979  CG1 ILE A 274      28.487  65.245  21.062  1.00 42.79           C  
ANISOU 1979  CG1 ILE A 274     3752   7625   4881    668   -219    523       C  
ATOM   1980  CG2 ILE A 274      29.675  63.491  19.781  1.00 37.27           C  
ANISOU 1980  CG2 ILE A 274     2927   7091   4142   1056   -102    604       C  
ATOM   1981  CD1 ILE A 274      28.583  66.136  19.810  1.00 44.09           C  
ANISOU 1981  CD1 ILE A 274     3894   7824   5033    574   -211    493       C  
ATOM   1982  N   ILE A 275      30.061  60.871  22.069  1.00 47.76           N  
ANISOU 1982  N   ILE A 275     4274   8407   5466   1442    -65    739       N  
ATOM   1983  CA  ILE A 275      31.002  59.790  22.296  1.00 45.68           C  
ANISOU 1983  CA  ILE A 275     3918   8288   5149   1680    -15    852       C  
ATOM   1984  C   ILE A 275      31.327  59.180  20.943  1.00 55.78           C  
ANISOU 1984  C   ILE A 275     5204   9572   6420   1872     80    842       C  
ATOM   1985  O   ILE A 275      30.422  58.740  20.224  1.00 57.63           O  
ANISOU 1985  O   ILE A 275     5615   9564   6717   1921    129    732       O  
ATOM   1986  CB  ILE A 275      30.434  58.747  23.264  1.00 43.61           C  
ANISOU 1986  CB  ILE A 275     3785   7857   4928   1799     -1    847       C  
ATOM   1987  CG1 ILE A 275      30.054  59.443  24.581  1.00 45.08           C  
ANISOU 1987  CG1 ILE A 275     3973   8036   5120   1592    -94    847       C  
ATOM   1988  CG2 ILE A 275      31.444  57.646  23.499  1.00 41.10           C  
ANISOU 1988  CG2 ILE A 275     3407   7662   4549   2032     61    964       C  
ATOM   1989  CD1 ILE A 275      29.708  58.499  25.732  1.00 34.78           C  
ANISOU 1989  CD1 ILE A 275     2754   6626   3836   1693    -92    873       C  
ATOM   1990  N   ASP A 276      32.615  59.181  20.583  1.00 61.01           N  
ANISOU 1990  N   ASP A 276     5746  10442   6991   1906    109    935       N  
ATOM   1991  CA  ASP A 276      33.003  58.720  19.256  1.00 66.48           C  
ANISOU 1991  CA  ASP A 276     6470  11127   7661   2043    199    920       C  
ATOM   1992  C   ASP A 276      32.807  57.222  19.116  1.00 66.13           C  
ANISOU 1992  C   ASP A 276     6588  10904   7634   2291    294    905       C  
ATOM   1993  O   ASP A 276      32.308  56.746  18.090  1.00 64.52           O  
ANISOU 1993  O   ASP A 276     6514  10542   7461   2387    361    821       O  
ATOM   1994  CB  ASP A 276      34.462  59.075  18.970  1.00 75.25           C  
ANISOU 1994  CB  ASP A 276     7414  12516   8661   2020    208   1034       C  
ATOM   1995  CG  ASP A 276      34.691  60.562  18.844  1.00 80.10           C  
ANISOU 1995  CG  ASP A 276     7898  13290   9246   1763    127   1040       C  
ATOM   1996  OD1 ASP A 276      33.737  61.294  18.505  1.00 78.25           O  
ANISOU 1996  OD1 ASP A 276     7710  12942   9079   1632     88    942       O  
ATOM   1997  OD2 ASP A 276      35.839  60.995  19.078  1.00 83.34           O  
ANISOU 1997  OD2 ASP A 276     8165  13942   9560   1687    107   1147       O  
ATOM   1998  N   ASN A 277      33.192  56.467  20.136  1.00 63.29           N  
ANISOU 1998  N   ASN A 277     6236  10564   7248   2387    301    983       N  
ATOM   1999  CA  ASN A 277      33.279  55.021  20.051  1.00 60.89           C  
ANISOU 1999  CA  ASN A 277     6078  10124   6934   2622    397    995       C  
ATOM   2000  C   ASN A 277      32.030  54.394  20.657  1.00 60.59           C  
ANISOU 2000  C   ASN A 277     6227   9814   6982   2654    394    913       C  
ATOM   2001  O   ASN A 277      31.522  54.858  21.681  1.00 70.44           O  
ANISOU 2001  O   ASN A 277     7444  11052   8268   2536    314    911       O  
ATOM   2002  CB  ASN A 277      34.545  54.539  20.762  1.00 62.67           C  
ANISOU 2002  CB  ASN A 277     6195  10552   7066   2719    416   1145       C  
ATOM   2003  CG  ASN A 277      34.647  53.036  20.829  1.00 67.64           C  
ANISOU 2003  CG  ASN A 277     6981  11041   7679   2960    513   1169       C  
ATOM   2004  OD1 ASN A 277      34.075  52.413  21.717  1.00 76.54           O  
ANISOU 2004  OD1 ASN A 277     8216  12022   8846   3002    508   1159       O  
ATOM   2005  ND2 ASN A 277      35.403  52.447  19.912  1.00 64.49           N  
ANISOU 2005  ND2 ASN A 277     6599  10690   7215   3116    604   1206       N  
ATOM   2006  N   ILE A 278      31.538  53.333  20.016  1.00 62.28           N  
ANISOU 2006  N   ILE A 278     6643   9802   7217   2804    481    846       N  
ATOM   2007  CA  ILE A 278      30.294  52.702  20.448  1.00 57.85           C  
ANISOU 2007  CA  ILE A 278     6286   8963   6730   2821    485    758       C  
ATOM   2008  C   ILE A 278      30.501  51.824  21.684  1.00 57.71           C  
ANISOU 2008  C   ILE A 278     6314   8916   6696   2916    491    837       C  
ATOM   2009  O   ILE A 278      29.573  51.646  22.481  1.00 64.25           O  
ANISOU 2009  O   ILE A 278     7244   9585   7584   2873    456    794       O  
ATOM   2010  CB  ILE A 278      29.689  51.910  19.277  1.00 55.96           C  
ANISOU 2010  CB  ILE A 278     6263   8492   6506   2915    574    653       C  
ATOM   2011  CG1 ILE A 278      28.303  51.368  19.643  1.00 61.10           C  
ANISOU 2011  CG1 ILE A 278     7133   8852   7230   2891    572    552       C  
ATOM   2012  CG2 ILE A 278      30.650  50.788  18.835  1.00 53.48           C  
ANISOU 2012  CG2 ILE A 278     6011   8197   6112   3116    677    721       C  
ATOM   2013  CD1 ILE A 278      27.322  52.433  20.085  1.00 62.20           C  
ANISOU 2013  CD1 ILE A 278     7221   8969   7444   2711    477    489       C  
ATOM   2014  N   ASP A 279      31.703  51.270  21.874  1.00 57.08           N  
ANISOU 2014  N   ASP A 279     6162   8993   6534   3046    537    955       N  
ATOM   2015  CA  ASP A 279      31.982  50.517  23.097  1.00 63.45           C  
ANISOU 2015  CA  ASP A 279     6988   9804   7317   3132    540   1043       C  
ATOM   2016  C   ASP A 279      32.000  51.430  24.314  1.00 63.25           C  
ANISOU 2016  C   ASP A 279     6798   9932   7302   2972    429   1095       C  
ATOM   2017  O   ASP A 279      31.650  50.999  25.423  1.00 57.83           O  
ANISOU 2017  O   ASP A 279     6167   9173   6635   2984    404   1120       O  
ATOM   2018  CB  ASP A 279      33.326  49.782  22.991  1.00 63.76           C  
ANISOU 2018  CB  ASP A 279     6970  10005   7253   3312    618   1168       C  
ATOM   2019  CG  ASP A 279      33.240  48.500  22.185  1.00 70.18           C  
ANISOU 2019  CG  ASP A 279     8002  10617   8046   3504    737   1132       C  
ATOM   2020  OD1 ASP A 279      32.119  48.110  21.798  1.00 72.15           O  
ANISOU 2020  OD1 ASP A 279     8459  10595   8360   3487    757   1010       O  
ATOM   2021  OD2 ASP A 279      34.299  47.877  21.946  1.00 79.23           O  
ANISOU 2021  OD2 ASP A 279     9118  11882   9106   3668    813   1230       O  
ATOM   2022  N   ASP A 280      32.439  52.679  24.132  1.00 67.38           N  
ANISOU 2022  N   ASP A 280     7126  10671   7805   2815    361   1116       N  
ATOM   2023  CA  ASP A 280      32.382  53.648  25.220  1.00 69.46           C  
ANISOU 2023  CA  ASP A 280     7250  11069   8073   2630    250   1152       C  
ATOM   2024  C   ASP A 280      30.940  53.993  25.557  1.00 62.10           C  
ANISOU 2024  C   ASP A 280     6431   9927   7239   2521    193   1041       C  
ATOM   2025  O   ASP A 280      30.588  54.140  26.733  1.00 56.13           O  
ANISOU 2025  O   ASP A 280     5663   9166   6497   2448    127   1065       O  
ATOM   2026  CB  ASP A 280      33.164  54.905  24.838  1.00 70.36           C  
ANISOU 2026  CB  ASP A 280     7158  11444   8133   2467    196   1191       C  
ATOM   2027  CG  ASP A 280      34.661  54.672  24.797  1.00 72.91           C  
ANISOU 2027  CG  ASP A 280     7339  12020   8343   2549    237   1326       C  
ATOM   2028  OD1 ASP A 280      35.151  53.794  25.540  1.00 75.40           O  
ANISOU 2028  OD1 ASP A 280     7665  12368   8617   2683    271   1414       O  
ATOM   2029  OD2 ASP A 280      35.351  55.370  24.024  1.00 75.71           O  
ANISOU 2029  OD2 ASP A 280     7573  12546   8647   2480    236   1348       O  
ATOM   2030  N   VAL A 281      30.092  54.110  24.530  1.00 53.25           N  
ANISOU 2030  N   VAL A 281     5420   8634   6178   2511    220    922       N  
ATOM   2031  CA  VAL A 281      28.676  54.402  24.740  1.00 54.59           C  
ANISOU 2031  CA  VAL A 281     5728   8578   6436   2384    177    804       C  
ATOM   2032  C   VAL A 281      28.047  53.348  25.644  1.00 57.70           C  
ANISOU 2032  C   VAL A 281     6288   8776   6860   2475    197    801       C  
ATOM   2033  O   VAL A 281      27.402  53.674  26.649  1.00 61.39           O  
ANISOU 2033  O   VAL A 281     6791   9176   7360   2324    129    778       O  
ATOM   2034  CB  VAL A 281      27.945  54.495  23.387  1.00 48.79           C  
ANISOU 2034  CB  VAL A 281     5121   7670   5746   2349    220    674       C  
ATOM   2035  CG1 VAL A 281      26.447  54.539  23.597  1.00 33.48           C  
ANISOU 2035  CG1 VAL A 281     3375   5458   3889   2198    191    548       C  
ATOM   2036  CG2 VAL A 281      28.456  55.689  22.562  1.00 45.66           C  
ANISOU 2036  CG2 VAL A 281     4566   7458   5324   2221    189    672       C  
ATOM   2037  N   LYS A 282      28.229  52.068  25.296  1.00 60.52           N  
ANISOU 2037  N   LYS A 282     6774   9022   7200   2693    294    816       N  
ATOM   2038  CA  LYS A 282      27.652  50.985  26.091  1.00 62.58           C  
ANISOU 2038  CA  LYS A 282     7215   9080   7482   2778    321    813       C  
ATOM   2039  C   LYS A 282      28.138  51.041  27.536  1.00 72.98           C  
ANISOU 2039  C   LYS A 282     8420  10542   8768   2761    262    926       C  
ATOM   2040  O   LYS A 282      27.341  50.927  28.478  1.00 78.21           O  
ANISOU 2040  O   LYS A 282     9161  11086   9470   2714    220    911       O  
ATOM   2041  CB  LYS A 282      27.993  49.633  25.461  1.00 58.45           C  
ANISOU 2041  CB  LYS A 282     6856   8431   6922   2962    437    816       C  
ATOM   2042  CG  LYS A 282      27.746  48.424  26.356  1.00 52.01           C  
ANISOU 2042  CG  LYS A 282     6204   7456   6101   3063    473    847       C  
ATOM   2043  CD  LYS A 282      27.101  47.270  25.583  1.00 57.25           C  
ANISOU 2043  CD  LYS A 282     7142   7839   6774   3147    567    758       C  
ATOM   2044  CE  LYS A 282      27.761  45.935  25.875  1.00 67.17           C  
ANISOU 2044  CE  LYS A 282     8503   9054   7964   3328    652    837       C  
ATOM   2045  NZ  LYS A 282      27.987  45.745  27.338  1.00 76.47           N  
ANISOU 2045  NZ  LYS A 282     9620  10302   9132   3346    611    936       N  
ATOM   2046  N   ALA A 283      29.448  51.213  27.731  1.00 71.86           N  
ANISOU 2046  N   ALA A 283     8095  10661   8546   2791    259   1043       N  
ATOM   2047  CA  ALA A 283      29.994  51.262  29.082  1.00 68.00           C  
ANISOU 2047  CA  ALA A 283     7493  10332   8014   2766    203   1155       C  
ATOM   2048  C   ALA A 283      29.446  52.461  29.838  1.00 68.72           C  
ANISOU 2048  C   ALA A 283     7485  10492   8133   2553     84   1137       C  
ATOM   2049  O   ALA A 283      29.006  52.337  30.990  1.00 58.99           O  
ANISOU 2049  O   ALA A 283     6286   9216   6912   2517     35   1161       O  
ATOM   2050  CB  ALA A 283      31.522  51.306  29.032  1.00 66.18           C  
ANISOU 2050  CB  ALA A 283     7078  10386   7683   2820    225   1282       C  
ATOM   2051  N   PHE A 284      29.449  53.633  29.191  1.00 65.91           N  
ANISOU 2051  N   PHE A 284     7017  10243   7784   2406     36   1094       N  
ATOM   2052  CA  PHE A 284      28.908  54.828  29.827  1.00 56.66           C  
ANISOU 2052  CA  PHE A 284     5815   9082   6631   2123    -64   1040       C  
ATOM   2053  C   PHE A 284      27.465  54.610  30.243  1.00 55.30           C  
ANISOU 2053  C   PHE A 284     5862   8607   6543   2031    -70    920       C  
ATOM   2054  O   PHE A 284      27.095  54.850  31.399  1.00 59.08           O  
ANISOU 2054  O   PHE A 284     6357   9068   7023   1913   -128    928       O  
ATOM   2055  CB  PHE A 284      29.004  56.031  28.889  1.00 54.20           C  
ANISOU 2055  CB  PHE A 284     5420   8853   6319   1954    -91    981       C  
ATOM   2056  CG  PHE A 284      28.260  57.234  29.393  1.00 53.95           C  
ANISOU 2056  CG  PHE A 284     5418   8765   6316   1668   -174    900       C  
ATOM   2057  CD1 PHE A 284      28.825  58.052  30.364  1.00 54.92           C  
ANISOU 2057  CD1 PHE A 284     5407   9087   6372   1508   -256    971       C  
ATOM   2058  CD2 PHE A 284      26.990  57.535  28.925  1.00 56.26           C  
ANISOU 2058  CD2 PHE A 284     5877   8807   6693   1560   -166    757       C  
ATOM   2059  CE1 PHE A 284      28.148  59.156  30.854  1.00 50.44           C  
ANISOU 2059  CE1 PHE A 284     4890   8454   5822   1253   -321    895       C  
ATOM   2060  CE2 PHE A 284      26.300  58.645  29.410  1.00 57.75           C  
ANISOU 2060  CE2 PHE A 284     6098   8940   6903   1319   -231    690       C  
ATOM   2061  CZ  PHE A 284      26.884  59.453  30.378  1.00 55.79           C  
ANISOU 2061  CZ  PHE A 284     5735   8875   6588   1169   -304    756       C  
ATOM   2062  N   LEU A 285      26.625  54.176  29.300  1.00 55.90           N  
ANISOU 2062  N   LEU A 285     6105   8453   6684   2075    -10    811       N  
ATOM   2063  CA  LEU A 285      25.210  54.020  29.611  1.00 54.94           C  
ANISOU 2063  CA  LEU A 285     6177   8062   6636   1971    -17    699       C  
ATOM   2064  C   LEU A 285      25.007  53.012  30.726  1.00 53.94           C  
ANISOU 2064  C   LEU A 285     6143   7846   6507   2069     -7    751       C  
ATOM   2065  O   LEU A 285      24.090  53.167  31.538  1.00 53.36           O  
ANISOU 2065  O   LEU A 285     6157   7647   6471   1937    -46    702       O  
ATOM   2066  CB  LEU A 285      24.433  53.603  28.366  1.00 46.72           C  
ANISOU 2066  CB  LEU A 285     5291   6812   5647   2010     47    588       C  
ATOM   2067  CG  LEU A 285      24.208  54.697  27.316  1.00 53.77           C  
ANISOU 2067  CG  LEU A 285     6135   7732   6562   1865     27    509       C  
ATOM   2068  CD1 LEU A 285      23.702  54.114  25.981  1.00 45.18           C  
ANISOU 2068  CD1 LEU A 285     5184   6481   5503   1944     99    422       C  
ATOM   2069  CD2 LEU A 285      23.243  55.760  27.834  1.00 50.09           C  
ANISOU 2069  CD2 LEU A 285     5690   7200   6140   1621    -44    437       C  
ATOM   2070  N   GLU A 286      25.870  51.996  30.797  1.00 57.70           N  
ANISOU 2070  N   GLU A 286     6598   8392   6935   2306     49    856       N  
ATOM   2071  CA  GLU A 286      25.745  50.976  31.834  1.00 57.35           C  
ANISOU 2071  CA  GLU A 286     6649   8262   6881   2420     65    917       C  
ATOM   2072  C   GLU A 286      26.170  51.513  33.196  1.00 55.15           C  
ANISOU 2072  C   GLU A 286     6230   8166   6558   2321    -19   1008       C  
ATOM   2073  O   GLU A 286      25.550  51.195  34.219  1.00 52.06           O  
ANISOU 2073  O   GLU A 286     5932   7665   6183   2273    -43   1005       O  
ATOM   2074  CB  GLU A 286      26.559  49.742  31.447  1.00 49.82           C  
ANISOU 2074  CB  GLU A 286     5724   7322   5881   2722    161   1008       C  
ATOM   2075  CG  GLU A 286      25.766  48.762  30.592  1.00 53.63           C  
ANISOU 2075  CG  GLU A 286     6455   7514   6406   2821    252    910       C  
ATOM   2076  CD  GLU A 286      26.645  47.781  29.851  1.00 65.48           C  
ANISOU 2076  CD  GLU A 286     8006   9022   7852   2996    355    947       C  
ATOM   2077  OE1 GLU A 286      26.092  46.889  29.169  1.00 67.26           O  
ANISOU 2077  OE1 GLU A 286     8450   9014   8093   3058    433    869       O  
ATOM   2078  OE2 GLU A 286      27.889  47.900  29.952  1.00 72.35           O  
ANISOU 2078  OE2 GLU A 286     8702  10133   8655   3060    360   1053       O  
ATOM   2079  N   GLU A 287      27.212  52.344  33.223  1.00 53.47           N  
ANISOU 2079  N   GLU A 287     5796   8238   6283   2273    -67   1088       N  
ATOM   2080  CA  GLU A 287      27.633  52.968  34.471  1.00 64.93           C  
ANISOU 2080  CA  GLU A 287     7113   9878   7678   2143   -155   1169       C  
ATOM   2081  C   GLU A 287      26.520  53.837  35.052  1.00 63.63           C  
ANISOU 2081  C   GLU A 287     7035   9579   7562   1878   -219   1057       C  
ATOM   2082  O   GLU A 287      26.159  53.702  36.231  1.00 52.09           O  
ANISOU 2082  O   GLU A 287     5619   8080   6093   1819   -256   1077       O  
ATOM   2083  CB  GLU A 287      28.902  53.785  34.230  1.00 77.27           C  
ANISOU 2083  CB  GLU A 287     8429  11771   9159   2105   -195   1264       C  
ATOM   2084  CG  GLU A 287      29.673  54.151  35.482  1.00 84.01           C  
ANISOU 2084  CG  GLU A 287     9120  12878   9923   2027   -275   1390       C  
ATOM   2085  CD  GLU A 287      30.972  54.861  35.161  1.00 92.31           C  
ANISOU 2085  CD  GLU A 287     9948  14239  10885   1964   -299   1475       C  
ATOM   2086  OE1 GLU A 287      31.367  54.880  33.970  1.00 95.02           O  
ANISOU 2086  OE1 GLU A 287    10265  14602  11236   2029   -240   1451       O  
ATOM   2087  OE2 GLU A 287      31.594  55.402  36.097  1.00 95.77           O  
ANISOU 2087  OE2 GLU A 287    10263  14881  11243   1821   -368   1552       O  
ATOM   2088  N   VAL A 288      25.947  54.725  34.233  1.00 56.85           N  
ANISOU 2088  N   VAL A 288     6206   8645   6751   1726   -227    941       N  
ATOM   2089  CA  VAL A 288      24.859  55.572  34.718  1.00 54.44           C  
ANISOU 2089  CA  VAL A 288     5988   8206   6489   1496   -275    837       C  
ATOM   2090  C   VAL A 288      23.700  54.715  35.210  1.00 57.18           C  
ANISOU 2090  C   VAL A 288     6529   8298   6897   1532   -245    780       C  
ATOM   2091  O   VAL A 288      23.023  55.059  36.187  1.00 61.41           O  
ANISOU 2091  O   VAL A 288     7121   8770   7443   1395   -285    751       O  
ATOM   2092  CB  VAL A 288      24.401  56.550  33.619  1.00 55.92           C  
ANISOU 2092  CB  VAL A 288     6188   8340   6720   1364   -274    729       C  
ATOM   2093  CG1 VAL A 288      23.322  57.470  34.160  1.00 60.39           C  
ANISOU 2093  CG1 VAL A 288     6840   8783   7323   1145   -316    635       C  
ATOM   2094  CG2 VAL A 288      25.576  57.349  33.078  1.00 51.51           C  
ANISOU 2094  CG2 VAL A 288     5443   8034   6096   1327   -300    789       C  
ATOM   2095  N   ALA A 289      23.460  53.581  34.548  1.00 53.09           N  
ANISOU 2095  N   ALA A 289     6126   7632   6415   1711   -171    764       N  
ATOM   2096  CA  ALA A 289      22.341  52.718  34.903  1.00 54.21           C  
ANISOU 2096  CA  ALA A 289     6464   7525   6609   1734   -139    708       C  
ATOM   2097  C   ALA A 289      22.460  52.128  36.311  1.00 63.70           C  
ANISOU 2097  C   ALA A 289     7682   8746   7776   1774   -160    794       C  
ATOM   2098  O   ALA A 289      21.444  51.702  36.870  1.00 68.76           O  
ANISOU 2098  O   ALA A 289     8470   9203   8455   1727   -154    747       O  
ATOM   2099  CB  ALA A 289      22.213  51.599  33.869  1.00 36.46           C  
ANISOU 2099  CB  ALA A 289     4342   5126   4385   1916    -52    682       C  
ATOM   2100  N   GLU A 290      23.666  52.077  36.896  1.00 64.19           N  
ANISOU 2100  N   GLU A 290     7594   9033   7761   1858   -184    926       N  
ATOM   2101  CA  GLU A 290      23.789  51.590  38.273  1.00 68.54           C  
ANISOU 2101  CA  GLU A 290     8151   9620   8272   1885   -212   1014       C  
ATOM   2102  C   GLU A 290      23.029  52.485  39.239  1.00 74.37           C  
ANISOU 2102  C   GLU A 290     8906  10332   9018   1645   -280    958       C  
ATOM   2103  O   GLU A 290      22.403  51.998  40.187  1.00 72.16           O  
ANISOU 2103  O   GLU A 290     8730   9941   8746   1628   -285    961       O  
ATOM   2104  CB  GLU A 290      25.254  51.511  38.707  1.00 59.91           C  
ANISOU 2104  CB  GLU A 290     6866   8814   7085   1999   -236   1175       C  
ATOM   2105  CG  GLU A 290      26.121  50.561  37.906  1.00 75.34           C  
ANISOU 2105  CG  GLU A 290     8791  10819   9015   2272   -159   1258       C  
ATOM   2106  CD  GLU A 290      27.606  50.874  38.054  1.00 88.64           C  
ANISOU 2106  CD  GLU A 290    10230  12847  10604   2343   -190   1408       C  
ATOM   2107  OE1 GLU A 290      27.942  51.752  38.882  1.00 91.01           O  
ANISOU 2107  OE1 GLU A 290    10395  13335  10849   2168   -278   1451       O  
ATOM   2108  OE2 GLU A 290      28.433  50.254  37.343  1.00 91.95           O  
ANISOU 2108  OE2 GLU A 290    10599  13343  10994   2552   -122   1477       O  
ATOM   2109  N   THR A 291      23.089  53.799  39.023  1.00 75.26           N  
ANISOU 2109  N   THR A 291     8926  10546   9123   1461   -329    909       N  
ATOM   2110  CA  THR A 291      22.405  54.763  39.871  1.00 69.10           C  
ANISOU 2110  CA  THR A 291     8172   9742   8343   1235   -384    851       C  
ATOM   2111  C   THR A 291      21.089  55.245  39.280  1.00 62.74           C  
ANISOU 2111  C   THR A 291     7493   8723   7621   1119   -362    707       C  
ATOM   2112  O   THR A 291      20.201  55.670  40.029  1.00 58.16           O  
ANISOU 2112  O   THR A 291     6991   8049   7057    982   -381    653       O  
ATOM   2113  CB  THR A 291      23.304  55.984  40.132  1.00 63.40           C  
ANISOU 2113  CB  THR A 291     7284   9263   7541   1087   -453    894       C  
ATOM   2114  OG1 THR A 291      24.010  56.337  38.937  1.00 70.64           O  
ANISOU 2114  OG1 THR A 291     8097  10289   8453   1127   -439    898       O  
ATOM   2115  CG2 THR A 291      24.310  55.678  41.211  1.00 52.50           C  
ANISOU 2115  CG2 THR A 291     5789   8095   6064   1128   -497   1035       C  
ATOM   2116  N   GLY A 292      20.938  55.181  37.960  1.00 58.34           N  
ANISOU 2116  N   GLY A 292     6957   8096   7113   1176   -319    649       N  
ATOM   2117  CA  GLY A 292      19.893  55.952  37.316  1.00 48.12           C  
ANISOU 2117  CA  GLY A 292     5734   6668   5882   1042   -312    527       C  
ATOM   2118  C   GLY A 292      20.072  57.449  37.435  1.00 53.61           C  
ANISOU 2118  C   GLY A 292     6347   7476   6548    856   -361    502       C  
ATOM   2119  O   GLY A 292      19.135  58.201  37.151  1.00 61.55           O  
ANISOU 2119  O   GLY A 292     7417   8370   7597    735   -357    410       O  
ATOM   2120  N   ALA A 293      21.250  57.907  37.849  1.00 50.95           N  
ANISOU 2120  N   ALA A 293     5870   7358   6128    826   -407    587       N  
ATOM   2121  CA  ALA A 293      21.541  59.322  38.003  1.00 51.79           C  
ANISOU 2121  CA  ALA A 293     5910   7579   6187    634   -455    570       C  
ATOM   2122  C   ALA A 293      22.872  59.647  37.335  1.00 62.31           C  
ANISOU 2122  C   ALA A 293     7080   9136   7459    659   -474    640       C  
ATOM   2123  O   ALA A 293      23.771  58.803  37.249  1.00 63.97           O  
ANISOU 2123  O   ALA A 293     7199   9471   7636    818   -465    736       O  
ATOM   2124  CB  ALA A 293      21.574  59.713  39.480  1.00 49.08           C  
ANISOU 2124  CB  ALA A 293     5573   7297   5780    508   -506    604       C  
ATOM   2125  N   HIS A 294      22.990  60.880  36.854  1.00 60.90           N  
ANISOU 2125  N   HIS A 294     6866   9010   7262    504   -497    597       N  
ATOM   2126  CA  HIS A 294      24.208  61.317  36.193  1.00 56.32           C  
ANISOU 2126  CA  HIS A 294     6129   8650   6619    496   -517    661       C  
ATOM   2127  C   HIS A 294      24.386  62.805  36.452  1.00 61.26           C  
ANISOU 2127  C   HIS A 294     6737   9356   7183    252   -568    636       C  
ATOM   2128  O   HIS A 294      23.420  63.570  36.373  1.00 56.83           O  
ANISOU 2128  O   HIS A 294     6299   8629   6665    134   -557    536       O  
ATOM   2129  CB  HIS A 294      24.154  61.018  34.686  1.00 62.89           C  
ANISOU 2129  CB  HIS A 294     6958   9425   7512    618   -462    622       C  
ATOM   2130  CG  HIS A 294      25.092  61.852  33.868  1.00 60.68           C  
ANISOU 2130  CG  HIS A 294     6546   9329   7179    550   -480    651       C  
ATOM   2131  ND1 HIS A 294      26.438  61.568  33.759  1.00 57.91           N  
ANISOU 2131  ND1 HIS A 294     6022   9232   6751    630   -494    769       N  
ATOM   2132  CD2 HIS A 294      24.878  62.968  33.130  1.00 55.40           C  
ANISOU 2132  CD2 HIS A 294     5894   8637   6520    408   -485    583       C  
ATOM   2133  CE1 HIS A 294      27.011  62.474  32.987  1.00 62.48           C  
ANISOU 2133  CE1 HIS A 294     6512   9937   7292    529   -509    770       C  
ATOM   2134  NE2 HIS A 294      26.088  63.335  32.593  1.00 61.47           N  
ANISOU 2134  NE2 HIS A 294     6503   9638   7216    392   -504    657       N  
ATOM   2135  N   ASP A 295      25.621  63.205  36.775  1.00 75.83           N  
ANISOU 2135  N   ASP A 295     8432  11459   8919    177   -620    732       N  
ATOM   2136  CA  ASP A 295      25.954  64.602  37.080  1.00 80.44           C  
ANISOU 2136  CA  ASP A 295     9002  12142   9420    -76   -673    721       C  
ATOM   2137  C   ASP A 295      25.077  65.157  38.201  1.00 70.44           C  
ANISOU 2137  C   ASP A 295     7887  10731   8145   -229   -690    656       C  
ATOM   2138  O   ASP A 295      24.606  66.294  38.142  1.00 64.94           O  
ANISOU 2138  O   ASP A 295     7289   9944   7441   -402   -691    577       O  
ATOM   2139  CB  ASP A 295      25.859  65.485  35.831  1.00 91.02           C  
ANISOU 2139  CB  ASP A 295    10354  13442  10787   -147   -652    655       C  
ATOM   2140  CG  ASP A 295      26.491  66.854  36.033  1.00 94.63           C  
ANISOU 2140  CG  ASP A 295    10778  14040  11137   -400   -706    666       C  
ATOM   2141  OD1 ASP A 295      27.737  66.942  36.051  1.00 94.71           O  
ANISOU 2141  OD1 ASP A 295    10620  14316  11047   -442   -750    770       O  
ATOM   2142  OD2 ASP A 295      25.737  67.843  36.176  1.00 95.47           O  
ANISOU 2142  OD2 ASP A 295    11031  13992  11253   -559   -702    576       O  
ATOM   2143  N   GLY A 296      24.843  64.344  39.231  1.00 69.49           N  
ANISOU 2143  N   GLY A 296     7796  10584   8025   -157   -696    690       N  
ATOM   2144  CA  GLY A 296      24.082  64.772  40.384  1.00 70.71           C  
ANISOU 2144  CA  GLY A 296     8084  10621   8160   -290   -709    639       C  
ATOM   2145  C   GLY A 296      22.577  64.799  40.212  1.00 68.69           C  
ANISOU 2145  C   GLY A 296     8006  10079   8015   -263   -650    520       C  
ATOM   2146  O   GLY A 296      21.858  64.856  41.216  1.00 64.85           O  
ANISOU 2146  O   GLY A 296     7629   9487   7525   -321   -648    488       O  
ATOM   2147  N   ARG A 297      22.067  64.760  38.987  1.00 71.28           N  
ANISOU 2147  N   ARG A 297     8362  10288   8435   -180   -602    459       N  
ATOM   2148  CA  ARG A 297      20.632  64.800  38.755  1.00 70.43           C  
ANISOU 2148  CA  ARG A 297     8403   9933   8425   -158   -548    357       C  
ATOM   2149  C   ARG A 297      20.109  63.417  38.381  1.00 68.61           C  
ANISOU 2149  C   ARG A 297     8189   9597   8284     46   -507    358       C  
ATOM   2150  O   ARG A 297      20.793  62.631  37.718  1.00 70.94           O  
ANISOU 2150  O   ARG A 297     8392   9974   8588    184   -500    411       O  
ATOM   2151  CB  ARG A 297      20.288  65.805  37.654  1.00 76.65           C  
ANISOU 2151  CB  ARG A 297     9228  10650   9246   -227   -523    285       C  
ATOM   2152  CG  ARG A 297      21.245  66.990  37.565  1.00 89.59           C  
ANISOU 2152  CG  ARG A 297    10811  12442  10788   -399   -565    308       C  
ATOM   2153  CD  ARG A 297      20.557  68.234  36.993  1.00102.87           C  
ANISOU 2153  CD  ARG A 297    12604  13993  12490   -515   -535    222       C  
ATOM   2154  NE  ARG A 297      19.659  68.874  37.959  1.00108.41           N  
ANISOU 2154  NE  ARG A 297    13460  14553  13178   -619   -518    166       N  
ATOM   2155  CZ  ARG A 297      19.896  70.043  38.549  1.00107.46           C  
ANISOU 2155  CZ  ARG A 297    13413  14453  12965   -810   -537    151       C  
ATOM   2156  NH1 ARG A 297      21.005  70.718  38.272  1.00108.23           N  
ANISOU 2156  NH1 ARG A 297    13438  14711  12972   -937   -579    191       N  
ATOM   2157  NH2 ARG A 297      19.020  70.540  39.414  1.00103.19           N  
ANISOU 2157  NH2 ARG A 297    13024  13769  12413   -879   -508     98       N  
ATOM   2158  N   ASP A 298      18.895  63.117  38.838  1.00 54.94           N  
ANISOU 2158  N   ASP A 298     6581   7683   6611     60   -475    302       N  
ATOM   2159  CA  ASP A 298      18.173  61.958  38.335  1.00 48.81           C  
ANISOU 2159  CA  ASP A 298     5853   6772   5922    217   -430    282       C  
ATOM   2160  C   ASP A 298      17.927  62.116  36.832  1.00 58.34           C  
ANISOU 2160  C   ASP A 298     7054   7923   7191    261   -397    229       C  
ATOM   2161  O   ASP A 298      17.785  63.229  36.318  1.00 60.53           O  
ANISOU 2161  O   ASP A 298     7337   8195   7466    158   -398    184       O  
ATOM   2162  CB  ASP A 298      16.843  61.806  39.068  1.00 53.35           C  
ANISOU 2162  CB  ASP A 298     6555   7174   6539    188   -405    229       C  
ATOM   2163  CG  ASP A 298      16.925  60.881  40.267  1.00 62.28           C  
ANISOU 2163  CG  ASP A 298     7705   8317   7643    237   -418    287       C  
ATOM   2164  OD1 ASP A 298      15.883  60.680  40.932  1.00 62.61           O  
ANISOU 2164  OD1 ASP A 298     7845   8231   7712    215   -397    252       O  
ATOM   2165  OD2 ASP A 298      18.018  60.350  40.543  1.00 69.30           O  
ANISOU 2165  OD2 ASP A 298     8504   9348   8478    302   -448    373       O  
ATOM   2166  N   VAL A 299      17.863  60.993  36.120  1.00 51.17           N  
ANISOU 2166  N   VAL A 299     6147   6964   6330    415   -366    236       N  
ATOM   2167  CA  VAL A 299      17.751  61.027  34.663  1.00 50.86           C  
ANISOU 2167  CA  VAL A 299     6098   6889   6337    464   -336    194       C  
ATOM   2168  C   VAL A 299      16.967  59.805  34.188  1.00 50.96           C  
ANISOU 2168  C   VAL A 299     6197   6751   6414    588   -291    164       C  
ATOM   2169  O   VAL A 299      17.296  58.664  34.542  1.00 44.32           O  
ANISOU 2169  O   VAL A 299     5367   5908   5563    706   -280    213       O  
ATOM   2170  CB  VAL A 299      19.143  61.104  34.000  1.00 55.97           C  
ANISOU 2170  CB  VAL A 299     6613   7720   6934    515   -350    255       C  
ATOM   2171  CG1 VAL A 299      20.070  59.989  34.533  1.00 57.62           C  
ANISOU 2171  CG1 VAL A 299     6759   8032   7100    655   -355    350       C  
ATOM   2172  CG2 VAL A 299      19.018  61.038  32.494  1.00 63.57           C  
ANISOU 2172  CG2 VAL A 299     7573   8640   7941    576   -314    211       C  
ATOM   2173  N   GLU A 300      15.926  60.049  33.380  1.00 48.64           N  
ANISOU 2173  N   GLU A 300     5969   6333   6179    555   -264     88       N  
ATOM   2174  CA  GLU A 300      15.064  58.955  32.936  1.00 50.46           C  
ANISOU 2174  CA  GLU A 300     6294   6418   6461    635   -226     53       C  
ATOM   2175  C   GLU A 300      15.798  58.033  31.968  1.00 52.88           C  
ANISOU 2175  C   GLU A 300     6583   6748   6761    777   -199     74       C  
ATOM   2176  O   GLU A 300      15.619  56.809  32.006  1.00 49.88           O  
ANISOU 2176  O   GLU A 300     6282   6281   6390    877   -169     83       O  
ATOM   2177  CB  GLU A 300      13.794  59.507  32.288  1.00 48.80           C  
ANISOU 2177  CB  GLU A 300     6141   6099   6303    554   -209    -23       C  
ATOM   2178  CG  GLU A 300      12.879  58.433  31.675  1.00 52.53           C  
ANISOU 2178  CG  GLU A 300     6707   6436   6817    608   -174    -61       C  
ATOM   2179  CD  GLU A 300      11.729  58.993  30.832  1.00 51.17           C  
ANISOU 2179  CD  GLU A 300     6562   6193   6687    533   -162   -124       C  
ATOM   2180  OE1 GLU A 300      11.822  60.167  30.392  1.00 48.53           O  
ANISOU 2180  OE1 GLU A 300     6171   5915   6352    472   -172   -139       O  
ATOM   2181  OE2 GLU A 300      10.741  58.258  30.604  1.00 43.50           O  
ANISOU 2181  OE2 GLU A 300     5670   5117   5742    531   -142   -153       O  
ATOM   2182  N   GLY A 301      16.640  58.593  31.105  1.00 50.71           N  
ANISOU 2182  N   GLY A 301     6216   6587   6465    788   -203     84       N  
ATOM   2183  CA  GLY A 301      17.411  57.777  30.183  1.00 49.61           C  
ANISOU 2183  CA  GLY A 301     6055   6483   6310    933   -169    108       C  
ATOM   2184  C   GLY A 301      18.113  58.655  29.168  1.00 49.79           C  
ANISOU 2184  C   GLY A 301     5975   6629   6315    908   -176    106       C  
ATOM   2185  O   GLY A 301      18.190  59.873  29.342  1.00 53.95           O  
ANISOU 2185  O   GLY A 301     6441   7227   6829    778   -211    101       O  
ATOM   2186  N   PHE A 302      18.647  58.017  28.122  1.00 44.82           N  
ANISOU 2186  N   PHE A 302     5335   6019   5676   1032   -136    112       N  
ATOM   2187  CA  PHE A 302      19.217  58.730  26.987  1.00 47.35           C  
ANISOU 2187  CA  PHE A 302     5569   6440   5980   1016   -133    104       C  
ATOM   2188  C   PHE A 302      18.564  58.271  25.697  1.00 45.61           C  
ANISOU 2188  C   PHE A 302     5437   6099   5793   1059    -88     33       C  
ATOM   2189  O   PHE A 302      18.071  57.151  25.581  1.00 46.75           O  
ANISOU 2189  O   PHE A 302     5698   6112   5954   1143    -50      9       O  
ATOM   2190  CB  PHE A 302      20.738  58.532  26.886  1.00 49.06           C  
ANISOU 2190  CB  PHE A 302     5656   6854   6132   1127   -127    194       C  
ATOM   2191  CG  PHE A 302      21.509  59.271  27.933  1.00 50.94           C  
ANISOU 2191  CG  PHE A 302     5775   7260   6319   1044   -182    267       C  
ATOM   2192  CD1 PHE A 302      21.776  58.682  29.156  1.00 47.00           C  
ANISOU 2192  CD1 PHE A 302     5273   6789   5795   1092   -197    331       C  
ATOM   2193  CD2 PHE A 302      21.964  60.565  27.696  1.00 49.69           C  
ANISOU 2193  CD2 PHE A 302     5517   7232   6130    907   -220    273       C  
ATOM   2194  CE1 PHE A 302      22.489  59.369  30.130  1.00 43.17           C  
ANISOU 2194  CE1 PHE A 302     4680   6471   5252   1000   -253    399       C  
ATOM   2195  CE2 PHE A 302      22.679  61.258  28.660  1.00 38.49           C  
ANISOU 2195  CE2 PHE A 302     4002   5971   4651    806   -274    338       C  
ATOM   2196  CZ  PHE A 302      22.942  60.661  29.876  1.00 40.63           C  
ANISOU 2196  CZ  PHE A 302     4265   6280   4894    850   -292    400       C  
ATOM   2197  N   VAL A 303      18.538  59.169  24.736  1.00 41.53           N  
ANISOU 2197  N   VAL A 303     4875   5625   5282    986    -95     -1       N  
ATOM   2198  CA  VAL A 303      18.209  58.834  23.360  1.00 40.57           C  
ANISOU 2198  CA  VAL A 303     4806   5437   5172   1028    -55    -55       C  
ATOM   2199  C   VAL A 303      19.479  59.029  22.539  1.00 35.70           C  
ANISOU 2199  C   VAL A 303     4077   4982   4506   1103    -37    -13       C  
ATOM   2200  O   VAL A 303      20.075  60.114  22.552  1.00 34.03           O  
ANISOU 2200  O   VAL A 303     3750   4910   4271   1019    -72     18       O  
ATOM   2201  CB  VAL A 303      17.046  59.698  22.845  1.00 47.11           C  
ANISOU 2201  CB  VAL A 303     5674   6183   6043    888    -74   -124       C  
ATOM   2202  CG1 VAL A 303      16.786  59.445  21.372  1.00 52.08           C  
ANISOU 2202  CG1 VAL A 303     6343   6771   6673    917    -40   -175       C  
ATOM   2203  CG2 VAL A 303      15.791  59.454  23.658  1.00 55.68           C  
ANISOU 2203  CG2 VAL A 303     6858   7128   7171    825    -85   -157       C  
ATOM   2204  N   ILE A 304      19.921  57.969  21.865  1.00 38.38           N  
ANISOU 2204  N   ILE A 304     4455   5306   4821   1259     20     -7       N  
ATOM   2205  CA  ILE A 304      21.217  57.946  21.179  1.00 47.76           C  
ANISOU 2205  CA  ILE A 304     5532   6659   5953   1367     50     48       C  
ATOM   2206  C   ILE A 304      20.995  58.125  19.674  1.00 53.41           C  
ANISOU 2206  C   ILE A 304     6277   7348   6669   1359     81    -14       C  
ATOM   2207  O   ILE A 304      20.138  57.457  19.080  1.00 54.94           O  
ANISOU 2207  O   ILE A 304     6611   7380   6884   1377    114    -84       O  
ATOM   2208  CB  ILE A 304      21.993  56.647  21.477  1.00 40.70           C  
ANISOU 2208  CB  ILE A 304     4660   5782   5020   1576    105    110       C  
ATOM   2209  CG1 ILE A 304      22.188  56.433  22.992  1.00 46.96           C  
ANISOU 2209  CG1 ILE A 304     5427   6606   5810   1585     71    177       C  
ATOM   2210  CG2 ILE A 304      23.326  56.689  20.821  1.00 34.18           C  
ANISOU 2210  CG2 ILE A 304     3702   5151   4133   1693    139    177       C  
ATOM   2211  CD1 ILE A 304      20.998  55.819  23.765  1.00 35.28           C  
ANISOU 2211  CD1 ILE A 304     4107   4919   4379   1547     65    128       C  
ATOM   2212  N   ARG A 305      21.761  59.033  19.060  1.00 45.51           N  
ANISOU 2212  N   ARG A 305     5144   6511   5636   1320     69     15       N  
ATOM   2213  CA  ARG A 305      21.534  59.493  17.694  1.00 43.04           C  
ANISOU 2213  CA  ARG A 305     4838   6193   5323   1276     85    -38       C  
ATOM   2214  C   ARG A 305      22.783  59.244  16.854  1.00 43.09           C  
ANISOU 2214  C   ARG A 305     4752   6355   5265   1408    135     10       C  
ATOM   2215  O   ARG A 305      23.888  59.651  17.237  1.00 42.48           O  
ANISOU 2215  O   ARG A 305     4524   6472   5144   1425    120     95       O  
ATOM   2216  CB  ARG A 305      21.188  60.975  17.685  1.00 42.92           C  
ANISOU 2216  CB  ARG A 305     4760   6220   5328   1086     24    -51       C  
ATOM   2217  CG  ARG A 305      20.242  61.387  18.793  1.00 46.02           C  
ANISOU 2217  CG  ARG A 305     5205   6510   5768    968    -24    -71       C  
ATOM   2218  CD  ARG A 305      19.674  62.756  18.543  1.00 33.80           C  
ANISOU 2218  CD  ARG A 305     3642   4958   4243    801    -63    -99       C  
ATOM   2219  NE  ARG A 305      18.589  63.029  19.461  1.00 32.53           N  
ANISOU 2219  NE  ARG A 305     3556   4675   4129    712    -93   -127       N  
ATOM   2220  CZ  ARG A 305      17.667  63.956  19.252  1.00 37.18           C  
ANISOU 2220  CZ  ARG A 305     4180   5196   4749    595   -112   -164       C  
ATOM   2221  NH1 ARG A 305      17.688  64.697  18.131  1.00 26.81           N  
ANISOU 2221  NH1 ARG A 305     2840   3921   3427    549   -109   -179       N  
ATOM   2222  NH2 ARG A 305      16.708  64.120  20.154  1.00 29.81           N  
ANISOU 2222  NH2 ARG A 305     3311   4160   3854    535   -130   -182       N  
ATOM   2223  N   CYS A 306      22.608  58.601  15.703  1.00 32.43           N  
ANISOU 2223  N   CYS A 306     3490   4931   3901   1493    195    -40       N  
ATOM   2224  CA  CYS A 306      23.764  58.189  14.912  1.00 46.33           C  
ANISOU 2224  CA  CYS A 306     5182   6826   5596   1649    260      5       C  
ATOM   2225  C   CYS A 306      23.290  57.874  13.502  1.00 37.90           C  
ANISOU 2225  C   CYS A 306     4224   5660   4517   1669    310    -76       C  
ATOM   2226  O   CYS A 306      22.149  58.171  13.140  1.00 44.26           O  
ANISOU 2226  O   CYS A 306     5123   6332   5364   1539    281   -155       O  
ATOM   2227  CB  CYS A 306      24.473  57.002  15.576  1.00 50.87           C  
ANISOU 2227  CB  CYS A 306     5772   7417   6138   1854    314     70       C  
ATOM   2228  SG  CYS A 306      23.388  55.600  15.911  1.00 52.88           S  
ANISOU 2228  SG  CYS A 306     6278   7388   6426   1928    355      0       S  
ATOM   2229  N   LYS A 307      24.165  57.277  12.698  1.00 46.12           N  
ANISOU 2229  N   LYS A 307     5250   6777   5495   1833    388    -52       N  
ATOM   2230  CA  LYS A 307      23.816  56.877  11.339  1.00 60.10           C  
ANISOU 2230  CA  LYS A 307     7137   8458   7239   1865    445   -129       C  
ATOM   2231  C   LYS A 307      23.762  55.359  11.247  1.00 57.57           C  
ANISOU 2231  C   LYS A 307     6998   7988   6889   2048    534   -155       C  
ATOM   2232  O   LYS A 307      24.592  54.669  11.849  1.00 60.07           O  
ANISOU 2232  O   LYS A 307     7289   8358   7176   2222    581    -83       O  
ATOM   2233  CB  LYS A 307      24.810  57.431  10.310  1.00 60.57           C  
ANISOU 2233  CB  LYS A 307     7061   8712   7240   1902    476    -92       C  
ATOM   2234  CG  LYS A 307      25.267  58.856  10.571  1.00 60.06           C  
ANISOU 2234  CG  LYS A 307     6798   8837   7185   1754    400    -33       C  
ATOM   2235  CD  LYS A 307      24.104  59.841  10.534  1.00 60.34           C  
ANISOU 2235  CD  LYS A 307     6872   8772   7280   1531    321    -97       C  
ATOM   2236  CE  LYS A 307      23.773  60.320   9.133  1.00 65.33           C  
ANISOU 2236  CE  LYS A 307     7529   9399   7896   1462    332   -153       C  
ATOM   2237  NZ  LYS A 307      23.213  61.712   9.160  1.00 58.43           N  
ANISOU 2237  NZ  LYS A 307     6599   8542   7061   1255    253   -161       N  
ATOM   2238  N   LYS A 308      22.785  54.838  10.497  1.00 46.72           N  
ANISOU 2238  N   LYS A 308     5813   6426   5515   2005    558   -255       N  
ATOM   2239  CA  LYS A 308      22.610  53.397  10.363  1.00 55.12           C  
ANISOU 2239  CA  LYS A 308     7089   7312   6541   2150    644   -294       C  
ATOM   2240  C   LYS A 308      22.637  52.972   8.899  1.00 66.43           C  
ANISOU 2240  C   LYS A 308     8637   8697   7905   2203    720   -361       C  
ATOM   2241  O   LYS A 308      22.134  53.680   8.015  1.00 65.75           O  
ANISOU 2241  O   LYS A 308     8532   8627   7822   2058    685   -414       O  
ATOM   2242  CB  LYS A 308      21.310  52.927  11.018  1.00 54.76           C  
ANISOU 2242  CB  LYS A 308     7210   7054   6544   2038    604   -356       C  
ATOM   2243  CG  LYS A 308      20.840  51.558  10.541  1.00 59.19           C  
ANISOU 2243  CG  LYS A 308     8034   7399   7056   2117    686   -427       C  
ATOM   2244  CD  LYS A 308      20.405  50.654  11.671  1.00 56.29           C  
ANISOU 2244  CD  LYS A 308     7800   6876   6711   2152    690   -419       C  
ATOM   2245  CE  LYS A 308      19.847  49.349  11.122  1.00 62.54           C  
ANISOU 2245  CE  LYS A 308     8880   7437   7444   2195    769   -499       C  
ATOM   2246  NZ  LYS A 308      18.706  49.586  10.192  1.00 71.92           N  
ANISOU 2246  NZ  LYS A 308    10162   8538   8627   1992    732   -600       N  
ATOM   2247  N   SER A 309      23.252  51.818   8.660  1.00 71.79           N  
ANISOU 2247  N   SER A 309     9440   9318   8519   2418    830   -352       N  
ATOM   2248  CA  SER A 309      23.275  51.144   7.374  1.00 78.73           C  
ANISOU 2248  CA  SER A 309    10484  10112   9319   2496    924   -421       C  
ATOM   2249  C   SER A 309      22.310  49.965   7.383  1.00 85.91           C  
ANISOU 2249  C   SER A 309    11688  10744  10209   2482    963   -509       C  
ATOM   2250  O   SER A 309      22.141  49.289   8.402  1.00 81.58           O  
ANISOU 2250  O   SER A 309    11224  10088   9684   2537    968   -486       O  
ATOM   2251  CB  SER A 309      24.687  50.641   7.061  1.00 80.92           C  
ANISOU 2251  CB  SER A 309    10709  10511   9525   2741   1028   -342       C  
ATOM   2252  OG  SER A 309      25.432  51.610   6.352  1.00 86.98           O  
ANISOU 2252  OG  SER A 309    11272  11508  10270   2742   1025   -305       O  
ATOM   2253  N   THR A 310      21.676  49.719   6.231  1.00 95.02           N  
ANISOU 2253  N   THR A 310    13003  11788  11312   2399    990   -608       N  
ATOM   2254  CA  THR A 310      20.934  48.473   6.048  1.00 97.52           C  
ANISOU 2254  CA  THR A 310    13628  11847  11579   2400   1048   -693       C  
ATOM   2255  C   THR A 310      21.827  47.275   6.341  1.00110.13           C  
ANISOU 2255  C   THR A 310    15313  13391  13141   2577   1130   -621       C  
ATOM   2256  O   THR A 310      21.474  46.398   7.140  1.00112.43           O  
ANISOU 2256  O   THR A 310    15744  13529  13445   2579   1133   -611       O  
ATOM   2257  CB  THR A 310      20.371  48.383   4.628  1.00 82.18           C  
ANISOU 2257  CB  THR A 310    11829   9832   9565   2292   1072   -797       C  
ATOM   2258  OG1 THR A 310      19.165  49.147   4.545  1.00 83.02           O  
ANISOU 2258  OG1 THR A 310    11886   9933   9723   2020    953   -843       O  
ATOM   2259  CG2 THR A 310      20.050  46.950   4.280  1.00 80.12           C  
ANISOU 2259  CG2 THR A 310    11860   9346   9236   2297   1141   -848       C  
ATOM   2260  N   ASN A 311      22.999  47.231   5.710  1.00116.18           N  
ANISOU 2260  N   ASN A 311    15995  14291  13859   2725   1195   -562       N  
ATOM   2261  CA  ASN A 311      24.017  46.262   6.062  1.00124.13           C  
ANISOU 2261  CA  ASN A 311    17036  15298  14831   2914   1267   -469       C  
ATOM   2262  C   ASN A 311      25.356  46.971   6.221  1.00132.46           C  
ANISOU 2262  C   ASN A 311    17814  16627  15889   3045   1269   -348       C  
ATOM   2263  O   ASN A 311      25.654  47.917   5.478  1.00129.75           O  
ANISOU 2263  O   ASN A 311    17315  16446  15537   3014   1255   -355       O  
ATOM   2264  CB  ASN A 311      24.120  45.148   5.012  1.00125.43           C  
ANISOU 2264  CB  ASN A 311    17442  15314  14903   2973   1367   -515       C  
ATOM   2265  CG  ASN A 311      23.228  43.960   5.341  1.00124.11           C  
ANISOU 2265  CG  ASN A 311    17560  14879  14719   2910   1384   -572       C  
ATOM   2266  OD1 ASN A 311      23.490  43.213   6.283  1.00129.03           O  
ANISOU 2266  OD1 ASN A 311    18234  15441  15348   3002   1402   -504       O  
ATOM   2267  ND2 ASN A 311      22.165  43.784   4.563  1.00119.18           N  
ANISOU 2267  ND2 ASN A 311    17119  14101  14063   2740   1375   -692       N  
ATOM   2268  N   PRO A 312      26.186  46.528   7.184  1.00141.55           N  
ANISOU 2268  N   PRO A 312    18896  17844  17044   3184   1283   -233       N  
ATOM   2269  CA  PRO A 312      27.395  47.286   7.548  1.00143.86           C  
ANISOU 2269  CA  PRO A 312    18902  18419  17340   3272   1262   -108       C  
ATOM   2270  C   PRO A 312      28.433  47.400   6.444  1.00142.03           C  
ANISOU 2270  C   PRO A 312    18590  18340  17035   3378   1328    -68       C  
ATOM   2271  O   PRO A 312      28.237  46.909   5.328  1.00146.71           O  
ANISOU 2271  O   PRO A 312    19350  18818  17574   3391   1395   -142       O  
ATOM   2272  CB  PRO A 312      27.951  46.483   8.731  1.00144.40           C  
ANISOU 2272  CB  PRO A 312    18981  18480  17404   3402   1279     -2       C  
ATOM   2273  CG  PRO A 312      27.426  45.101   8.510  1.00143.30           C  
ANISOU 2273  CG  PRO A 312    19153  18070  17224   3447   1353    -61       C  
ATOM   2274  CD  PRO A 312      26.031  45.326   8.021  1.00141.91           C  
ANISOU 2274  CD  PRO A 312    19121  17716  17082   3252   1314   -207       C  
ATOM   2275  N   GLY A 313      29.557  48.041   6.763  1.00134.19           N  
ANISOU 2275  N   GLY A 313    17341  17612  16033   3444   1308     52       N  
ATOM   2276  CA  GLY A 313      30.629  48.234   5.807  1.00129.65           C  
ANISOU 2276  CA  GLY A 313    16659  17216  15388   3540   1363    108       C  
ATOM   2277  C   GLY A 313      30.505  49.543   5.057  1.00122.37           C  
ANISOU 2277  C   GLY A 313    15571  16443  14482   3401   1311     67       C  
ATOM   2278  O   GLY A 313      31.056  50.566   5.475  1.00119.99           O  
ANISOU 2278  O   GLY A 313    15017  16375  14200   3346   1245    145       O  
ATOM   2279  N   VAL A 314      29.791  49.518   3.935  1.00121.49           N  
ANISOU 2279  N   VAL A 314    15604  16202  14353   3334   1342    -52       N  
ATOM   2280  CA  VAL A 314      29.443  50.736   3.214  1.00117.75           C  
ANISOU 2280  CA  VAL A 314    15007  15838  13895   3186   1292   -107       C  
ATOM   2281  C   VAL A 314      27.919  50.825   3.207  1.00116.73           C  
ANISOU 2281  C   VAL A 314    15040  15499  13814   3030   1250   -243       C  
ATOM   2282  O   VAL A 314      27.252  50.348   4.135  1.00106.65           O  
ANISOU 2282  O   VAL A 314    13870  14067  12583   3005   1222   -263       O  
ATOM   2283  CB  VAL A 314      30.043  50.750   1.789  1.00113.54           C  
ANISOU 2283  CB  VAL A 314    14476  15382  13281   3242   1365   -118       C  
ATOM   2284  CG1 VAL A 314      30.141  52.178   1.232  1.00109.76           C  
ANISOU 2284  CG1 VAL A 314    13780  15113  12809   3112   1308   -117       C  
ATOM   2285  CG2 VAL A 314      31.422  50.095   1.777  1.00115.89           C  
ANISOU 2285  CG2 VAL A 314    14722  15798  13513   3443   1438      4       C  
ATOM   2286  N   GLY A 315      27.356  51.417   2.161  1.00120.84           N  
ANISOU 2286  N   GLY A 315    15582  16017  14315   2920   1245   -334       N  
ATOM   2287  CA  GLY A 315      25.933  51.591   2.061  1.00118.72           C  
ANISOU 2287  CA  GLY A 315    15454  15579  14074   2764   1201   -458       C  
ATOM   2288  C   GLY A 315      25.541  53.001   2.426  1.00119.83           C  
ANISOU 2288  C   GLY A 315    15389  15855  14288   2578   1082   -444       C  
ATOM   2289  O   GLY A 315      26.265  53.715   3.126  1.00130.21           O  
ANISOU 2289  O   GLY A 315    16476  17362  15638   2590   1037   -343       O  
ATOM   2290  N   PRO A 316      24.387  53.438   1.935  1.00 93.55           N  
ANISOU 2290  N   PRO A 316    12136  12424  10986   2359   1010   -530       N  
ATOM   2291  CA  PRO A 316      23.850  54.741   2.352  1.00 86.90           C  
ANISOU 2291  CA  PRO A 316    11127  11662  10228   2138    878   -510       C  
ATOM   2292  C   PRO A 316      23.546  54.762   3.847  1.00 81.68           C  
ANISOU 2292  C   PRO A 316    10428  10956   9650   2104    812   -469       C  
ATOM   2293  O   PRO A 316      22.906  53.854   4.385  1.00 78.08           O  
ANISOU 2293  O   PRO A 316    10145  10313   9207   2125    825   -510       O  
ATOM   2294  CB  PRO A 316      22.579  54.880   1.508  1.00 78.93           C  
ANISOU 2294  CB  PRO A 316    10254  10520   9216   1949    836   -613       C  
ATOM   2295  CG  PRO A 316      22.238  53.453   1.100  1.00 73.25           C  
ANISOU 2295  CG  PRO A 316     9808   9598   8428   2044    928   -694       C  
ATOM   2296  CD  PRO A 316      23.545  52.769   0.931  1.00 75.24           C  
ANISOU 2296  CD  PRO A 316    10059   9919   8609   2304   1050   -646       C  
ATOM   2297  N   TYR A 317      24.023  55.806   4.522  1.00 79.49           N  
ANISOU 2297  N   TYR A 317     9931  10851   9420   2045    742   -387       N  
ATOM   2298  CA  TYR A 317      23.789  55.991   5.952  1.00 69.73           C  
ANISOU 2298  CA  TYR A 317     8640   9596   8258   1996    674   -343       C  
ATOM   2299  C   TYR A 317      22.656  56.988   6.155  1.00 61.36           C  
ANISOU 2299  C   TYR A 317     7558   8486   7269   1757    565   -381       C  
ATOM   2300  O   TYR A 317      22.658  58.070   5.564  1.00 61.54           O  
ANISOU 2300  O   TYR A 317     7473   8613   7295   1639    523   -375       O  
ATOM   2301  CB  TYR A 317      25.047  56.488   6.666  1.00 64.38           C  
ANISOU 2301  CB  TYR A 317     7743   9143   7576   2076    666   -225       C  
ATOM   2302  CG  TYR A 317      26.089  55.416   6.908  1.00 71.31           C  
ANISOU 2302  CG  TYR A 317     8631  10068   8396   2334    765   -163       C  
ATOM   2303  CD1 TYR A 317      25.938  54.463   7.924  1.00 78.04           C  
ANISOU 2303  CD1 TYR A 317     9587  10798   9268   2438    785   -149       C  
ATOM   2304  CD2 TYR A 317      27.219  55.336   6.098  1.00 70.04           C  
ANISOU 2304  CD2 TYR A 317     8380  10077   8156   2483    846   -113       C  
ATOM   2305  CE1 TYR A 317      26.908  53.475   8.133  1.00 82.88           C  
ANISOU 2305  CE1 TYR A 317    10213  11455   9824   2695    884    -81       C  
ATOM   2306  CE2 TYR A 317      28.182  54.353   6.292  1.00 73.78           C  
ANISOU 2306  CE2 TYR A 317     8864  10595   8574   2724    940    -44       C  
ATOM   2307  CZ  TYR A 317      28.023  53.430   7.301  1.00 79.46           C  
ANISOU 2307  CZ  TYR A 317     9695  11177   9317   2799    946    -23       C  
ATOM   2308  OH  TYR A 317      28.993  52.473   7.481  1.00 83.66           O  
ANISOU 2308  OH  TYR A 317    10258  11732   9799   2965   1010     61       O  
ATOM   2309  N   HIS A 318      21.692  56.625   6.986  1.00 60.37           N  
ANISOU 2309  N   HIS A 318     7538   8203   7198   1692    526   -414       N  
ATOM   2310  CA  HIS A 318      20.589  57.513   7.304  1.00 55.51           C  
ANISOU 2310  CA  HIS A 318     6901   7539   6649   1487    432   -439       C  
ATOM   2311  C   HIS A 318      20.546  57.748   8.811  1.00 51.42           C  
ANISOU 2311  C   HIS A 318     6319   7024   6193   1461    379   -388       C  
ATOM   2312  O   HIS A 318      21.179  57.031   9.592  1.00 52.75           O  
ANISOU 2312  O   HIS A 318     6491   7199   6352   1595    413   -344       O  
ATOM   2313  CB  HIS A 318      19.258  56.942   6.790  1.00 55.78           C  
ANISOU 2313  CB  HIS A 318     7122   7388   6684   1398    428   -532       C  
ATOM   2314  CG  HIS A 318      18.893  55.617   7.387  1.00 74.05           C  
ANISOU 2314  CG  HIS A 318     9610   9532   8991   1475    468   -563       C  
ATOM   2315  ND1 HIS A 318      19.246  54.418   6.806  1.00 80.25           N  
ANISOU 2315  ND1 HIS A 318    10553  10232   9705   1615    561   -598       N  
ATOM   2316  CD2 HIS A 318      18.203  55.301   8.510  1.00 77.32           C  
ANISOU 2316  CD2 HIS A 318    10080   9840   9458   1430    431   -562       C  
ATOM   2317  CE1 HIS A 318      18.794  53.421   7.547  1.00 83.09           C  
ANISOU 2317  CE1 HIS A 318    11064  10434  10073   1650    579   -617       C  
ATOM   2318  NE2 HIS A 318      18.155  53.929   8.586  1.00 78.70           N  
ANISOU 2318  NE2 HIS A 318    10443   9868   9592   1536    499   -595       N  
ATOM   2319  N   ASP A 319      19.802  58.775   9.210  1.00 40.44           N  
ANISOU 2319  N   ASP A 319     4872   5633   4860   1293    298   -389       N  
ATOM   2320  CA  ASP A 319      19.664  59.092  10.624  1.00 36.59           C  
ANISOU 2320  CA  ASP A 319     4334   5142   4426   1249    247   -348       C  
ATOM   2321  C   ASP A 319      18.886  58.004  11.359  1.00 44.26           C  
ANISOU 2321  C   ASP A 319     5455   5940   5421   1279    257   -382       C  
ATOM   2322  O   ASP A 319      17.908  57.460  10.838  1.00 44.90           O  
ANISOU 2322  O   ASP A 319     5675   5884   5500   1234    266   -451       O  
ATOM   2323  CB  ASP A 319      18.949  60.427  10.798  1.00 27.76           C  
ANISOU 2323  CB  ASP A 319     3149   4041   3356   1069    172   -349       C  
ATOM   2324  CG  ASP A 319      19.846  61.587  10.538  1.00 34.15           C  
ANISOU 2324  CG  ASP A 319     3805   5025   4145   1028    152   -295       C  
ATOM   2325  OD1 ASP A 319      19.353  62.624  10.029  1.00 38.47           O  
ANISOU 2325  OD1 ASP A 319     4325   5586   4707    903    116   -307       O  
ATOM   2326  OD2 ASP A 319      21.053  61.437  10.815  1.00 41.43           O  
ANISOU 2326  OD2 ASP A 319     4635   6076   5031   1122    175   -234       O  
ATOM   2327  N   TRP A 320      19.293  57.726  12.600  1.00 39.16           N  
ANISOU 2327  N   TRP A 320     4779   5307   4793   1338    249   -330       N  
ATOM   2328  CA  TRP A 320      18.774  56.568  13.315  1.00 44.28           C  
ANISOU 2328  CA  TRP A 320     5572   5800   5453   1394    271   -350       C  
ATOM   2329  C   TRP A 320      18.985  56.739  14.816  1.00 47.17           C  
ANISOU 2329  C   TRP A 320     5870   6199   5854   1392    231   -288       C  
ATOM   2330  O   TRP A 320      20.102  57.044  15.267  1.00 27.08           O  
ANISOU 2330  O   TRP A 320     3193   3807   3289   1461    230   -213       O  
ATOM   2331  CB  TRP A 320      19.451  55.282  12.816  1.00 39.65           C  
ANISOU 2331  CB  TRP A 320     5090   5170   4804   1583    363   -353       C  
ATOM   2332  CG  TRP A 320      18.807  54.062  13.342  1.00 38.69           C  
ANISOU 2332  CG  TRP A 320     5155   4861   4685   1625    392   -386       C  
ATOM   2333  CD1 TRP A 320      17.611  53.544  12.957  1.00 33.39           C  
ANISOU 2333  CD1 TRP A 320     4652   4019   4015   1530    391   -466       C  
ATOM   2334  CD2 TRP A 320      19.305  53.207  14.386  1.00 45.54           C  
ANISOU 2334  CD2 TRP A 320     6061   5694   5546   1762    423   -332       C  
ATOM   2335  NE1 TRP A 320      17.328  52.409  13.694  1.00 36.51           N  
ANISOU 2335  NE1 TRP A 320     5200   4266   4405   1591    421   -470       N  
ATOM   2336  CE2 TRP A 320      18.353  52.181  14.576  1.00 38.77           C  
ANISOU 2336  CE2 TRP A 320     5414   4627   4689   1741    443   -388       C  
ATOM   2337  CE3 TRP A 320      20.467  53.207  15.174  1.00 50.23           C  
ANISOU 2337  CE3 TRP A 320     6531   6424   6128   1897    434   -235       C  
ATOM   2338  CZ2 TRP A 320      18.527  51.158  15.521  1.00 38.03           C  
ANISOU 2338  CZ2 TRP A 320     5420   4440   4588   1857    479   -354       C  
ATOM   2339  CZ3 TRP A 320      20.641  52.185  16.118  1.00 44.32           C  
ANISOU 2339  CZ3 TRP A 320     5872   5595   5374   2021    468   -195       C  
ATOM   2340  CH2 TRP A 320      19.672  51.177  16.279  1.00 40.16           C  
ANISOU 2340  CH2 TRP A 320     5566   4842   4851   2004    492   -256       C  
ATOM   2341  N   PHE A 321      17.915  56.516  15.578  1.00 32.10           N  
ANISOU 2341  N   PHE A 321     4049   4157   3989   1310    200   -317       N  
ATOM   2342  CA  PHE A 321      17.901  56.680  17.022  1.00 34.07           C  
ANISOU 2342  CA  PHE A 321     4256   4417   4272   1287    160   -270       C  
ATOM   2343  C   PHE A 321      17.807  55.315  17.682  1.00 48.37           C  
ANISOU 2343  C   PHE A 321     6201   6105   6074   1395    199   -266       C  
ATOM   2344  O   PHE A 321      17.282  54.358  17.105  1.00 52.54           O  
ANISOU 2344  O   PHE A 321     6887   6492   6583   1428    243   -320       O  
ATOM   2345  CB  PHE A 321      16.701  57.518  17.507  1.00 27.45           C  
ANISOU 2345  CB  PHE A 321     3416   3524   3489   1110     96   -300       C  
ATOM   2346  CG  PHE A 321      16.777  58.995  17.199  1.00 39.83           C  
ANISOU 2346  CG  PHE A 321     4860   5205   5071    998     53   -289       C  
ATOM   2347  CD1 PHE A 321      15.885  59.872  17.807  1.00 35.05           C  
ANISOU 2347  CD1 PHE A 321     4240   4567   4509    864      4   -298       C  
ATOM   2348  CD2 PHE A 321      17.690  59.512  16.291  1.00 46.14           C  
ANISOU 2348  CD2 PHE A 321     5566   6133   5834   1027     66   -271       C  
ATOM   2349  CE1 PHE A 321      15.914  61.243  17.531  1.00 28.87           C  
ANISOU 2349  CE1 PHE A 321     3368   3866   3734    764    -28   -288       C  
ATOM   2350  CE2 PHE A 321      17.721  60.874  16.017  1.00 38.79           C  
ANISOU 2350  CE2 PHE A 321     4538   5289   4910    913     28   -260       C  
ATOM   2351  CZ  PHE A 321      16.833  61.742  16.656  1.00 29.81           C  
ANISOU 2351  CZ  PHE A 321     3405   4106   3817    783    -18   -269       C  
ATOM   2352  N   PHE A 322      18.296  55.241  18.919  1.00 46.57           N  
ANISOU 2352  N   PHE A 322     5917   5925   5853   1441    182   -199       N  
ATOM   2353  CA  PHE A 322      17.830  54.210  19.829  1.00 46.54           C  
ANISOU 2353  CA  PHE A 322     6041   5784   5858   1484    196   -197       C  
ATOM   2354  C   PHE A 322      17.762  54.782  21.235  1.00 46.51           C  
ANISOU 2354  C   PHE A 322     5953   5832   5886   1412    137   -148       C  
ATOM   2355  O   PHE A 322      18.413  55.783  21.568  1.00 46.88           O  
ANISOU 2355  O   PHE A 322     5846   6037   5930   1371     97   -100       O  
ATOM   2356  CB  PHE A 322      18.671  52.916  19.771  1.00 45.81           C  
ANISOU 2356  CB  PHE A 322     6032   5659   5714   1695    274   -160       C  
ATOM   2357  CG  PHE A 322      20.089  53.047  20.263  1.00 46.88           C  
ANISOU 2357  CG  PHE A 322     6016   5981   5816   1831    284    -56       C  
ATOM   2358  CD1 PHE A 322      20.420  52.723  21.576  1.00 46.64           C  
ANISOU 2358  CD1 PHE A 322     5959   5977   5786   1887    268     17       C  
ATOM   2359  CD2 PHE A 322      21.106  53.422  19.393  1.00 45.99           C  
ANISOU 2359  CD2 PHE A 322     5786   6025   5662   1909    311    -26       C  
ATOM   2360  CE1 PHE A 322      21.749  52.812  22.023  1.00 48.05           C  
ANISOU 2360  CE1 PHE A 322     5984   6350   5922   2012    273    125       C  
ATOM   2361  CE2 PHE A 322      22.427  53.514  19.831  1.00 45.71           C  
ANISOU 2361  CE2 PHE A 322     5596   6186   5586   2033    320     81       C  
ATOM   2362  CZ  PHE A 322      22.749  53.214  21.144  1.00 46.91           C  
ANISOU 2362  CZ  PHE A 322     5712   6375   5735   2083    299    159       C  
ATOM   2363  N   LYS A 323      16.915  54.143  22.035  1.00 40.20           N  
ANISOU 2363  N   LYS A 323     5270   4893   5110   1381    131   -164       N  
ATOM   2364  CA  LYS A 323      16.564  54.547  23.386  1.00 43.02           C  
ANISOU 2364  CA  LYS A 323     5588   5259   5497   1300     80   -134       C  
ATOM   2365  C   LYS A 323      17.402  53.754  24.377  1.00 50.73           C  
ANISOU 2365  C   LYS A 323     6565   6265   6445   1438     99    -55       C  
ATOM   2366  O   LYS A 323      17.773  52.606  24.115  1.00 55.26           O  
ANISOU 2366  O   LYS A 323     7238   6772   6987   1587    159    -42       O  
ATOM   2367  CB  LYS A 323      15.071  54.289  23.610  1.00 47.21           C  
ANISOU 2367  CB  LYS A 323     6244   5628   6065   1181     67   -195       C  
ATOM   2368  CG  LYS A 323      14.443  54.857  24.849  1.00 51.83           C  
ANISOU 2368  CG  LYS A 323     6797   6212   6685   1072     17   -180       C  
ATOM   2369  CD  LYS A 323      13.038  55.365  24.525  1.00 53.35           C  
ANISOU 2369  CD  LYS A 323     7025   6329   6915    920     -5   -243       C  
ATOM   2370  CE  LYS A 323      12.118  54.269  24.026  1.00 51.78           C  
ANISOU 2370  CE  LYS A 323     6984   5979   6711    907     25   -293       C  
ATOM   2371  NZ  LYS A 323      11.424  53.582  25.130  1.00 63.14           N  
ANISOU 2371  NZ  LYS A 323     8512   7318   8159    877     22   -283       N  
ATOM   2372  N   TYR A 324      17.732  54.382  25.509  1.00 53.43           N  
ANISOU 2372  N   TYR A 324     6800   6710   6789   1392     49      2       N  
ATOM   2373  CA  TYR A 324      18.356  53.684  26.649  1.00 47.37           C  
ANISOU 2373  CA  TYR A 324     6031   5974   5996   1498     54     83       C  
ATOM   2374  C   TYR A 324      17.632  54.152  27.904  1.00 39.89           C  
ANISOU 2374  C   TYR A 324     5082   4998   5076   1364      0     84       C  
ATOM   2375  O   TYR A 324      18.074  55.090  28.581  1.00 38.93           O  
ANISOU 2375  O   TYR A 324     4836   5012   4943   1290    -50    124       O  
ATOM   2376  CB  TYR A 324      19.847  53.930  26.740  1.00 48.05           C  
ANISOU 2376  CB  TYR A 324     5957   6271   6030   1604     53    177       C  
ATOM   2377  CG  TYR A 324      20.548  52.859  27.538  1.00 62.01           C  
ANISOU 2377  CG  TYR A 324     7747   8056   7759   1776     84    266       C  
ATOM   2378  CD1 TYR A 324      20.537  52.885  28.931  1.00 61.88           C  
ANISOU 2378  CD1 TYR A 324     7704   8070   7738   1739     41    322       C  
ATOM   2379  CD2 TYR A 324      21.194  51.803  26.907  1.00 68.76           C  
ANISOU 2379  CD2 TYR A 324     8659   8889   8577   1983    161    298       C  
ATOM   2380  CE1 TYR A 324      21.158  51.903  29.668  1.00 57.82           C  
ANISOU 2380  CE1 TYR A 324     7209   7574   7186   1901     68    412       C  
ATOM   2381  CE2 TYR A 324      21.823  50.811  27.642  1.00 65.38           C  
ANISOU 2381  CE2 TYR A 324     8260   8472   8112   2159    197    389       C  
ATOM   2382  CZ  TYR A 324      21.801  50.867  29.020  1.00 60.76           C  
ANISOU 2382  CZ  TYR A 324     7637   7924   7524   2116    147    448       C  
ATOM   2383  OH  TYR A 324      22.430  49.882  29.754  1.00 57.60           O  
ANISOU 2383  OH  TYR A 324     7262   7541   7083   2297    181    548       O  
ATOM   2384  N   LYS A 325      16.516  53.488  28.203  1.00 37.03           N  
ANISOU 2384  N   LYS A 325     4867   4460   4744   1324     11     38       N  
ATOM   2385  CA  LYS A 325      15.603  53.901  29.266  1.00 50.39           C  
ANISOU 2385  CA  LYS A 325     6576   6105   6465   1190    -31     26       C  
ATOM   2386  C   LYS A 325      15.991  53.164  30.551  1.00 49.51           C  
ANISOU 2386  C   LYS A 325     6489   5994   6329   1266    -32     99       C  
ATOM   2387  O   LYS A 325      15.852  51.940  30.633  1.00 55.28           O  
ANISOU 2387  O   LYS A 325     7347   6606   7049   1363     10    108       O  
ATOM   2388  CB  LYS A 325      14.160  53.616  28.838  1.00 44.98           C  
ANISOU 2388  CB  LYS A 325     6019   5254   5818   1096    -19    -55       C  
ATOM   2389  CG  LYS A 325      13.083  54.444  29.540  1.00 47.31           C  
ANISOU 2389  CG  LYS A 325     6299   5529   6149    936    -59    -83       C  
ATOM   2390  CD  LYS A 325      11.686  54.188  28.980  1.00 43.53           C  
ANISOU 2390  CD  LYS A 325     5920   4919   5699    845    -47   -151       C  
ATOM   2391  CE  LYS A 325      10.651  55.031  29.725  1.00 49.37           C  
ANISOU 2391  CE  LYS A 325     6632   5657   6470    709    -78   -165       C  
ATOM   2392  NZ  LYS A 325       9.233  54.837  29.267  1.00 47.74           N  
ANISOU 2392  NZ  LYS A 325     6498   5355   6286    612    -71   -216       N  
ATOM   2393  N   PHE A 326      16.505  53.902  31.541  1.00 47.46           N  
ANISOU 2393  N   PHE A 326     6115   5866   6050   1220    -79    154       N  
ATOM   2394  CA  PHE A 326      17.049  53.276  32.752  1.00 53.35           C  
ANISOU 2394  CA  PHE A 326     6860   6651   6761   1298    -86    238       C  
ATOM   2395  C   PHE A 326      15.951  52.592  33.558  1.00 44.06           C  
ANISOU 2395  C   PHE A 326     5824   5310   5609   1254    -80    216       C  
ATOM   2396  O   PHE A 326      14.964  53.228  33.945  1.00 51.44           O  
ANISOU 2396  O   PHE A 326     6774   6197   6575   1106   -106    167       O  
ATOM   2397  CB  PHE A 326      17.759  54.307  33.629  1.00 43.57           C  
ANISOU 2397  CB  PHE A 326     5471   5596   5487   1223   -145    295       C  
ATOM   2398  CG  PHE A 326      18.976  54.905  32.993  1.00 49.44           C  
ANISOU 2398  CG  PHE A 326     6066   6529   6191   1262   -155    338       C  
ATOM   2399  CD1 PHE A 326      19.114  56.282  32.892  1.00 54.11           C  
ANISOU 2399  CD1 PHE A 326     6555   7228   6774   1115   -199    317       C  
ATOM   2400  CD2 PHE A 326      19.978  54.093  32.480  1.00 53.40           C  
ANISOU 2400  CD2 PHE A 326     6534   7099   6658   1447   -115    401       C  
ATOM   2401  CE1 PHE A 326      20.231  56.839  32.295  1.00 54.84           C  
ANISOU 2401  CE1 PHE A 326     6510   7502   6825   1135   -210    359       C  
ATOM   2402  CE2 PHE A 326      21.101  54.639  31.885  1.00 52.35           C  
ANISOU 2402  CE2 PHE A 326     6249   7158   6483   1483   -122    448       C  
ATOM   2403  CZ  PHE A 326      21.226  56.014  31.789  1.00 56.03           C  
ANISOU 2403  CZ  PHE A 326     6609   7738   6941   1317   -173    427       C  
ATOM   2404  N   GLU A 327      16.143  51.301  33.837  1.00 41.17           N  
ANISOU 2404  N   GLU A 327     5560   4861   5222   1389    -41    260       N  
ATOM   2405  CA  GLU A 327      15.079  50.501  34.446  1.00 53.17           C  
ANISOU 2405  CA  GLU A 327     7235   6206   6760   1348    -26    237       C  
ATOM   2406  C   GLU A 327      14.727  50.994  35.855  1.00 52.07           C  
ANISOU 2406  C   GLU A 327     7056   6109   6619   1242    -75    265       C  
ATOM   2407  O   GLU A 327      13.556  51.236  36.169  1.00 53.56           O  
ANISOU 2407  O   GLU A 327     7301   6210   6839   1108    -86    210       O  
ATOM   2408  CB  GLU A 327      15.490  49.028  34.466  1.00 57.87           C  
ANISOU 2408  CB  GLU A 327     7961   6703   7324   1524     31    287       C  
ATOM   2409  CG  GLU A 327      14.376  48.072  34.060  1.00 74.74           C  
ANISOU 2409  CG  GLU A 327    10304   8617   9478   1490     74    221       C  
ATOM   2410  CD  GLU A 327      14.535  46.675  34.649  1.00 95.96           C  
ANISOU 2410  CD  GLU A 327    13149  11181  12130   1619    120    279       C  
ATOM   2411  OE1 GLU A 327      15.567  46.402  35.300  1.00105.06           O  
ANISOU 2411  OE1 GLU A 327    14244  12427  13246   1762    124    377       O  
ATOM   2412  OE2 GLU A 327      13.616  45.848  34.470  1.00102.77           O  
ANISOU 2412  OE2 GLU A 327    14196  11856  12996   1572    152    231       O  
ATOM   2413  N   GLU A 328      15.721  51.175  36.705  1.00 45.06           N  
ANISOU 2413  N   GLU A 328     6066   5365   5687   1295   -103    351       N  
ATOM   2414  CA  GLU A 328      15.447  51.491  38.090  1.00 48.66           C  
ANISOU 2414  CA  GLU A 328     6506   5855   6129   1205   -143    382       C  
ATOM   2415  C   GLU A 328      16.129  52.789  38.482  1.00 47.78           C  
ANISOU 2415  C   GLU A 328     6233   5935   5987   1120   -198    406       C  
ATOM   2416  O   GLU A 328      17.157  53.148  37.902  1.00 45.26           O  
ANISOU 2416  O   GLU A 328     5802   5754   5642   1176   -206    439       O  
ATOM   2417  CB  GLU A 328      15.938  50.364  39.010  1.00 51.30           C  
ANISOU 2417  CB  GLU A 328     6894   6177   6422   1334   -130    477       C  
ATOM   2418  CG  GLU A 328      15.307  49.014  38.718  1.00 55.86           C  
ANISOU 2418  CG  GLU A 328     7659   6548   7016   1414    -72    460       C  
ATOM   2419  CD  GLU A 328      13.798  48.980  38.965  1.00 65.23           C  
ANISOU 2419  CD  GLU A 328     8962   7580   8244   1260    -71    382       C  
ATOM   2420  OE1 GLU A 328      13.226  49.972  39.477  1.00 65.11           O  
ANISOU 2420  OE1 GLU A 328     8882   7614   8245   1110   -111    349       O  
ATOM   2421  OE2 GLU A 328      13.184  47.934  38.664  1.00 68.21           O  
ANISOU 2421  OE2 GLU A 328     9501   7786   8630   1289    -27    359       O  
ATOM   2422  N   PRO A 329      15.596  53.510  39.482  1.00 47.03           N  
ANISOU 2422  N   PRO A 329     6129   5855   5886    979   -234    393       N  
ATOM   2423  CA  PRO A 329      14.403  53.199  40.282  1.00 49.63           C  
ANISOU 2423  CA  PRO A 329     6571   6048   6238    903   -227    362       C  
ATOM   2424  C   PRO A 329      13.085  53.583  39.629  1.00 50.94           C  
ANISOU 2424  C   PRO A 329     6802   6089   6464    800   -206    262       C  
ATOM   2425  O   PRO A 329      12.057  53.587  40.309  1.00 56.11           O  
ANISOU 2425  O   PRO A 329     7523   6662   7134    714   -202    237       O  
ATOM   2426  CB  PRO A 329      14.611  54.044  41.539  1.00 52.70           C  
ANISOU 2426  CB  PRO A 329     6895   6548   6580    798   -274    394       C  
ATOM   2427  CG  PRO A 329      15.318  55.258  41.015  1.00 51.04           C  
ANISOU 2427  CG  PRO A 329     6564   6479   6351    738   -303    381       C  
ATOM   2428  CD  PRO A 329      16.286  54.712  39.983  1.00 45.79           C  
ANISOU 2428  CD  PRO A 329     5843   5872   5682    883   -286    418       C  
ATOM   2429  N   TYR A 330      13.117  53.897  38.335  1.00 44.68           N  
ANISOU 2429  N   TYR A 330     5984   5292   5701    811   -191    213       N  
ATOM   2430  CA  TYR A 330      11.956  54.496  37.683  1.00 45.15           C  
ANISOU 2430  CA  TYR A 330     6073   5273   5810    705   -179    129       C  
ATOM   2431  C   TYR A 330      10.848  53.480  37.431  1.00 38.56           C  
ANISOU 2431  C   TYR A 330     5368   4278   5006    704   -144     95       C  
ATOM   2432  O   TYR A 330       9.665  53.844  37.461  1.00 33.09           O  
ANISOU 2432  O   TYR A 330     4705   3526   4342    599   -139     48       O  
ATOM   2433  CB  TYR A 330      12.411  55.194  36.389  1.00 48.96           C  
ANISOU 2433  CB  TYR A 330     6480   5817   6305    713   -179     95       C  
ATOM   2434  CG  TYR A 330      13.570  56.091  36.712  1.00 44.93           C  
ANISOU 2434  CG  TYR A 330     5849   5472   5751    703   -215    139       C  
ATOM   2435  CD1 TYR A 330      13.405  57.146  37.598  1.00 49.00           C  
ANISOU 2435  CD1 TYR A 330     6331   6041   6247    585   -244    136       C  
ATOM   2436  CD2 TYR A 330      14.848  55.832  36.228  1.00 47.05           C  
ANISOU 2436  CD2 TYR A 330     6041   5848   5986    810   -217    190       C  
ATOM   2437  CE1 TYR A 330      14.463  57.952  37.958  1.00 51.70           C  
ANISOU 2437  CE1 TYR A 330     6574   6535   6533    550   -281    177       C  
ATOM   2438  CE2 TYR A 330      15.917  56.638  36.581  1.00 45.89           C  
ANISOU 2438  CE2 TYR A 330     5774   5874   5788    782   -256    240       C  
ATOM   2439  CZ  TYR A 330      15.716  57.695  37.458  1.00 46.62           C  
ANISOU 2439  CZ  TYR A 330     5844   6013   5858    641   -291    231       C  
ATOM   2440  OH  TYR A 330      16.758  58.511  37.847  1.00 45.23           O  
ANISOU 2440  OH  TYR A 330     5561   6008   5617    585   -333    279       O  
ATOM   2441  N   LEU A 331      11.197  52.213  37.188  1.00 32.72           N  
ANISOU 2441  N   LEU A 331     4710   3467   4254    816   -117    123       N  
ATOM   2442  CA  LEU A 331      10.165  51.184  37.116  1.00 39.79           C  
ANISOU 2442  CA  LEU A 331     5750   4204   5163    793    -87     96       C  
ATOM   2443  C   LEU A 331       9.429  51.083  38.447  1.00 44.12           C  
ANISOU 2443  C   LEU A 331     6337   4720   5705    715    -98    118       C  
ATOM   2444  O   LEU A 331       8.193  51.033  38.488  1.00 45.29           O  
ANISOU 2444  O   LEU A 331     6541   4792   5874    610    -89     78       O  
ATOM   2445  CB  LEU A 331      10.778  49.838  36.719  1.00 43.46           C  
ANISOU 2445  CB  LEU A 331     6322   4587   5603    937    -49    128       C  
ATOM   2446  CG  LEU A 331       9.924  48.559  36.740  1.00 54.58           C  
ANISOU 2446  CG  LEU A 331     7915   5817   7007    924    -12    113       C  
ATOM   2447  CD1 LEU A 331      10.535  47.531  35.812  1.00 41.72           C  
ANISOU 2447  CD1 LEU A 331     6393   4103   5354   1061     37    115       C  
ATOM   2448  CD2 LEU A 331       9.736  47.933  38.149  1.00 59.32           C  
ANISOU 2448  CD2 LEU A 331     8581   6374   7584    923    -16    173       C  
ATOM   2449  N   MET A 332      10.182  51.065  39.552  1.00 37.30           N  
ANISOU 2449  N   MET A 332     5437   3929   4807    762   -118    186       N  
ATOM   2450  CA  MET A 332       9.562  50.999  40.870  1.00 35.24           C  
ANISOU 2450  CA  MET A 332     5211   3647   4532    690   -128    210       C  
ATOM   2451  C   MET A 332       8.658  52.202  41.117  1.00 37.79           C  
ANISOU 2451  C   MET A 332     5477   4006   4877    548   -141    160       C  
ATOM   2452  O   MET A 332       7.543  52.055  41.642  1.00 35.04           O  
ANISOU 2452  O   MET A 332     5185   3592   4537    464   -129    145       O  
ATOM   2453  CB  MET A 332      10.630  50.913  41.952  1.00 37.49           C  
ANISOU 2453  CB  MET A 332     5448   4029   4766    760   -154    295       C  
ATOM   2454  CG  MET A 332      10.031  50.931  43.341  1.00 39.78           C  
ANISOU 2454  CG  MET A 332     5769   4310   5035    679   -166    319       C  
ATOM   2455  SD  MET A 332      11.263  50.846  44.631  1.00 44.83           S  
ANISOU 2455  SD  MET A 332     6350   5080   5604    747   -203    424       S  
ATOM   2456  CE  MET A 332      11.845  52.544  44.627  1.00 40.87           C  
ANISOU 2456  CE  MET A 332     5694   4752   5084    658   -246    401       C  
ATOM   2457  N   TYR A 333       9.125  53.402  40.754  1.00 34.70           N  
ANISOU 2457  N   TYR A 333     4978   3719   4488    524   -161    139       N  
ATOM   2458  CA  TYR A 333       8.279  54.582  40.874  1.00 33.14           C  
ANISOU 2458  CA  TYR A 333     4742   3541   4307    408   -162     92       C  
ATOM   2459  C   TYR A 333       7.031  54.427  40.025  1.00 34.52           C  
ANISOU 2459  C   TYR A 333     4961   3627   4527    358   -133     37       C  
ATOM   2460  O   TYR A 333       5.940  54.827  40.436  1.00 37.71           O  
ANISOU 2460  O   TYR A 333     5376   4011   4942    274   -120     18       O  
ATOM   2461  CB  TYR A 333       9.032  55.847  40.458  1.00 30.52           C  
ANISOU 2461  CB  TYR A 333     4311   3319   3968    392   -182     77       C  
ATOM   2462  CG  TYR A 333      10.254  56.196  41.287  1.00 44.09           C  
ANISOU 2462  CG  TYR A 333     5969   5156   5629    408   -218    132       C  
ATOM   2463  CD1 TYR A 333      11.164  57.164  40.839  1.00 40.45           C  
ANISOU 2463  CD1 TYR A 333     5417   4806   5147    395   -241    131       C  
ATOM   2464  CD2 TYR A 333      10.500  55.579  42.514  1.00 40.71           C  
ANISOU 2464  CD2 TYR A 333     5570   4739   5160    426   -231    190       C  
ATOM   2465  CE1 TYR A 333      12.282  57.499  41.583  1.00 41.98           C  
ANISOU 2465  CE1 TYR A 333     5547   5127   5276    388   -279    187       C  
ATOM   2466  CE2 TYR A 333      11.615  55.912  43.268  1.00 41.99           C  
ANISOU 2466  CE2 TYR A 333     5666   5029   5258    429   -269    248       C  
ATOM   2467  CZ  TYR A 333      12.506  56.870  42.801  1.00 48.41           C  
ANISOU 2467  CZ  TYR A 333     6386   5961   6047    406   -295    246       C  
ATOM   2468  OH  TYR A 333      13.628  57.192  43.539  1.00 39.19           O  
ANISOU 2468  OH  TYR A 333     5145   4941   4806    391   -338    310       O  
ATOM   2469  N   ARG A 334       7.168  53.851  38.833  1.00 46.38           N  
ANISOU 2469  N   ARG A 334     6487   5087   6049    408   -123     16       N  
ATOM   2470  CA  ARG A 334       6.005  53.722  37.965  1.00 45.22           C  
ANISOU 2470  CA  ARG A 334     6374   4873   5933    345   -103    -32       C  
ATOM   2471  C   ARG A 334       5.022  52.710  38.535  1.00 36.54           C  
ANISOU 2471  C   ARG A 334     5376   3679   4827    295    -86    -21       C  
ATOM   2472  O   ARG A 334       3.810  52.957  38.566  1.00 33.78           O  
ANISOU 2472  O   ARG A 334     5026   3319   4492    201    -76    -41       O  
ATOM   2473  CB  ARG A 334       6.438  53.350  36.542  1.00 45.63           C  
ANISOU 2473  CB  ARG A 334     6437   4903   5996    401    -96    -60       C  
ATOM   2474  CG  ARG A 334       6.776  54.571  35.686  1.00 50.04           C  
ANISOU 2474  CG  ARG A 334     6892   5549   6573    394   -106    -89       C  
ATOM   2475  CD  ARG A 334       7.300  54.230  34.298  1.00 56.21           C  
ANISOU 2475  CD  ARG A 334     7679   6320   7357    455    -98   -114       C  
ATOM   2476  NE  ARG A 334       7.782  55.430  33.614  1.00 61.61           N  
ANISOU 2476  NE  ARG A 334     8259   7098   8052    452   -111   -131       N  
ATOM   2477  CZ  ARG A 334       9.059  55.796  33.551  1.00 63.62           C  
ANISOU 2477  CZ  ARG A 334     8447   7439   8287    519   -124   -106       C  
ATOM   2478  NH1 ARG A 334       9.994  55.047  34.120  1.00 70.04           N  
ANISOU 2478  NH1 ARG A 334     9276   8267   9071    609   -125    -57       N  
ATOM   2479  NH2 ARG A 334       9.402  56.910  32.921  1.00 57.98           N  
ANISOU 2479  NH2 ARG A 334     7646   6804   7578    495   -135   -123       N  
ATOM   2480  N   GLN A 335       5.530  51.571  39.015  1.00 29.27           N  
ANISOU 2480  N   GLN A 335     4543   2698   3881    360    -82     18       N  
ATOM   2481  CA  GLN A 335       4.666  50.607  39.680  1.00 30.48           C  
ANISOU 2481  CA  GLN A 335     4803   2759   4019    306    -67     35       C  
ATOM   2482  C   GLN A 335       3.933  51.260  40.854  1.00 42.33           C  
ANISOU 2482  C   GLN A 335     6260   4307   5516    222    -71     50       C  
ATOM   2483  O   GLN A 335       2.704  51.137  40.987  1.00 35.27           O  
ANISOU 2483  O   GLN A 335     5391   3384   4627    123    -57     39       O  
ATOM   2484  CB  GLN A 335       5.494  49.407  40.133  1.00 39.40           C  
ANISOU 2484  CB  GLN A 335     6034   3821   5117    408    -58     86       C  
ATOM   2485  CG  GLN A 335       4.726  48.400  40.975  1.00 56.16           C  
ANISOU 2485  CG  GLN A 335     8278   5844   7216    354    -44    115       C  
ATOM   2486  CD  GLN A 335       5.547  47.166  41.299  1.00 65.06           C  
ANISOU 2486  CD  GLN A 335     9525   6886   8307    471    -27    169       C  
ATOM   2487  OE1 GLN A 335       5.662  46.249  40.486  1.00 73.62           O  
ANISOU 2487  OE1 GLN A 335    10726   7864   9382    517      0    155       O  
ATOM   2488  NE2 GLN A 335       6.132  47.141  42.491  1.00 62.26           N  
ANISOU 2488  NE2 GLN A 335     9150   6579   7929    524    -41    233       N  
ATOM   2489  N   TRP A 336       4.668  52.013  41.685  1.00 30.51           N  
ANISOU 2489  N   TRP A 336     4694   2895   4005    254    -89     76       N  
ATOM   2490  CA  TRP A 336       4.022  52.730  42.778  1.00 39.41           C  
ANISOU 2490  CA  TRP A 336     5788   4065   5119    179    -86     84       C  
ATOM   2491  C   TRP A 336       2.904  53.628  42.262  1.00 38.47           C  
ANISOU 2491  C   TRP A 336     5617   3970   5030     98    -67     39       C  
ATOM   2492  O   TRP A 336       1.798  53.627  42.815  1.00 39.90           O  
ANISOU 2492  O   TRP A 336     5812   4141   5207     25    -46     43       O  
ATOM   2493  CB  TRP A 336       5.055  53.535  43.575  1.00 35.43           C  
ANISOU 2493  CB  TRP A 336     5222   3655   4586    211   -110    109       C  
ATOM   2494  CG  TRP A 336       5.944  52.648  44.398  1.00 33.41           C  
ANISOU 2494  CG  TRP A 336     5009   3396   4290    280   -127    173       C  
ATOM   2495  CD1 TRP A 336       5.900  51.279  44.460  1.00 33.91           C  
ANISOU 2495  CD1 TRP A 336     5170   3367   4345    326   -116    206       C  
ATOM   2496  CD2 TRP A 336       7.021  53.053  45.253  1.00 29.09           C  
ANISOU 2496  CD2 TRP A 336     4412   2944   3696    312   -158    218       C  
ATOM   2497  NE1 TRP A 336       6.883  50.812  45.298  1.00 26.51           N  
ANISOU 2497  NE1 TRP A 336     4244   2464   3366    402   -135    274       N  
ATOM   2498  CE2 TRP A 336       7.578  51.880  45.806  1.00 28.08           C  
ANISOU 2498  CE2 TRP A 336     4343   2788   3538    390   -164    284       C  
ATOM   2499  CE3 TRP A 336       7.568  54.297  45.608  1.00 24.67           C  
ANISOU 2499  CE3 TRP A 336     3771   2493   3109    274   -180    211       C  
ATOM   2500  CZ2 TRP A 336       8.651  51.912  46.700  1.00 31.99           C  
ANISOU 2500  CZ2 TRP A 336     4799   3378   3978    436   -196    352       C  
ATOM   2501  CZ3 TRP A 336       8.633  54.325  46.483  1.00 34.27           C  
ANISOU 2501  CZ3 TRP A 336     4955   3801   4267    300   -215    270       C  
ATOM   2502  CH2 TRP A 336       9.159  53.139  47.033  1.00 33.75           C  
ANISOU 2502  CH2 TRP A 336     4930   3722   4172    383   -225    343       C  
ATOM   2503  N   ARG A 337       3.154  54.374  41.182  1.00 38.14           N  
ANISOU 2503  N   ARG A 337     5512   3966   5014    115    -72      2       N  
ATOM   2504  CA  ARG A 337       2.110  55.250  40.654  1.00 42.29           C  
ANISOU 2504  CA  ARG A 337     5984   4519   5564     54    -51    -30       C  
ATOM   2505  C   ARG A 337       0.861  54.454  40.307  1.00 39.99           C  
ANISOU 2505  C   ARG A 337     5733   4181   5282    -13    -34    -31       C  
ATOM   2506  O   ARG A 337      -0.246  54.778  40.759  1.00 41.16           O  
ANISOU 2506  O   ARG A 337     5859   4354   5427    -76    -11    -22       O  
ATOM   2507  CB  ARG A 337       2.612  56.013  39.429  1.00 48.03           C  
ANISOU 2507  CB  ARG A 337     6648   5284   6315     86    -60    -64       C  
ATOM   2508  CG  ARG A 337       1.592  57.022  38.872  1.00 45.77           C  
ANISOU 2508  CG  ARG A 337     6304   5036   6052     39    -37    -87       C  
ATOM   2509  CD  ARG A 337       2.179  57.773  37.704  1.00 46.28           C  
ANISOU 2509  CD  ARG A 337     6313   5135   6135     72    -47   -115       C  
ATOM   2510  NE  ARG A 337       2.609  56.860  36.650  1.00 49.26           N  
ANISOU 2510  NE  ARG A 337     6716   5479   6523    101    -64   -129       N  
ATOM   2511  CZ  ARG A 337       3.319  57.221  35.584  1.00 42.64           C  
ANISOU 2511  CZ  ARG A 337     5841   4666   5695    141    -76   -151       C  
ATOM   2512  NH1 ARG A 337       3.689  58.484  35.430  1.00 40.16           N  
ANISOU 2512  NH1 ARG A 337     5463   4410   5384    146    -77   -159       N  
ATOM   2513  NH2 ARG A 337       3.670  56.315  34.678  1.00 35.80           N  
ANISOU 2513  NH2 ARG A 337     5013   3761   4830    172    -83   -164       N  
ATOM   2514  N   GLU A 338       1.030  53.380  39.533  1.00 30.18           N  
ANISOU 2514  N   GLU A 338     4554   2872   4039     -2    -43    -39       N  
ATOM   2515  CA  GLU A 338      -0.124  52.612  39.089  1.00 33.97           C  
ANISOU 2515  CA  GLU A 338     5082   3310   4516    -90    -33    -43       C  
ATOM   2516  C   GLU A 338      -0.784  51.866  40.248  1.00 41.42           C  
ANISOU 2516  C   GLU A 338     6090   4216   5431   -149    -21     -5       C  
ATOM   2517  O   GLU A 338      -2.009  51.695  40.259  1.00 34.75           O  
ANISOU 2517  O   GLU A 338     5239   3387   4577   -248     -8      3       O  
ATOM   2518  CB  GLU A 338       0.299  51.656  37.973  1.00 27.26           C  
ANISOU 2518  CB  GLU A 338     4311   2384   3661    -69    -40    -67       C  
ATOM   2519  CG  GLU A 338       0.051  52.202  36.549  1.00 61.63           C  
ANISOU 2519  CG  GLU A 338     8603   6778   8034    -88    -45   -107       C  
ATOM   2520  CD  GLU A 338       0.682  53.590  36.284  1.00 70.56           C  
ANISOU 2520  CD  GLU A 338     9619   7996   9194    -24    -51   -120       C  
ATOM   2521  OE1 GLU A 338       1.927  53.671  36.101  1.00 75.01           O  
ANISOU 2521  OE1 GLU A 338    10182   8560   9760     67    -62   -125       O  
ATOM   2522  OE2 GLU A 338      -0.074  54.596  36.235  1.00 55.38           O  
ANISOU 2522  OE2 GLU A 338     7610   6147   7286    -65    -43   -121       O  
ATOM   2523  N   CYS A 339      -0.010  51.445  41.251  1.00 42.43           N  
ANISOU 2523  N   CYS A 339     6272   4310   5539    -94    -26     25       N  
ATOM   2524  CA  CYS A 339      -0.626  50.774  42.395  1.00 40.28           C  
ANISOU 2524  CA  CYS A 339     6062   4005   5236   -151    -14     64       C  
ATOM   2525  C   CYS A 339      -1.482  51.737  43.212  1.00 35.64           C  
ANISOU 2525  C   CYS A 339     5391   3504   4646   -205      5     76       C  
ATOM   2526  O   CYS A 339      -2.566  51.368  43.685  1.00 31.50           O  
ANISOU 2526  O   CYS A 339     4883   2982   4104   -292     24     98       O  
ATOM   2527  CB  CYS A 339       0.449  50.126  43.261  1.00 33.74           C  
ANISOU 2527  CB  CYS A 339     5307   3130   4384    -70    -25    102       C  
ATOM   2528  SG  CYS A 339       1.142  48.638  42.496  1.00 42.87           S  
ANISOU 2528  SG  CYS A 339     6607   4155   5527     -7    -26    106       S  
ATOM   2529  N   THR A 340      -1.033  52.985  43.355  1.00 30.57           N  
ANISOU 2529  N   THR A 340     4665   2933   4017   -156      6     61       N  
ATOM   2530  CA  THR A 340      -1.821  53.973  44.080  1.00 35.59           C  
ANISOU 2530  CA  THR A 340     5239   3640   4645   -190     37     68       C  
ATOM   2531  C   THR A 340      -3.135  54.250  43.364  1.00 43.39           C  
ANISOU 2531  C   THR A 340     6167   4671   5648   -254     62     62       C  
ATOM   2532  O   THR A 340      -4.203  54.259  43.988  1.00 34.85           O  
ANISOU 2532  O   THR A 340     5067   3626   4547   -312     93     90       O  
ATOM   2533  CB  THR A 340      -1.023  55.263  44.257  1.00 38.23           C  
ANISOU 2533  CB  THR A 340     5521   4024   4982   -132     36     48       C  
ATOM   2534  OG1 THR A 340       0.268  54.972  44.809  1.00 34.30           O  
ANISOU 2534  OG1 THR A 340     5062   3510   4462    -80      5     62       O  
ATOM   2535  CG2 THR A 340      -1.760  56.211  45.184  1.00 44.95           C  
ANISOU 2535  CG2 THR A 340     6342   4925   5810   -157     79     56       C  
ATOM   2536  N   LYS A 341      -3.078  54.464  42.044  1.00 49.17           N  
ANISOU 2536  N   LYS A 341     6861   5412   6410   -243     49     33       N  
ATOM   2537  CA  LYS A 341      -4.303  54.658  41.272  1.00 38.90           C  
ANISOU 2537  CA  LYS A 341     5496   4169   5117   -306     66     37       C  
ATOM   2538  C   LYS A 341      -5.253  53.486  41.451  1.00 37.74           C  
ANISOU 2538  C   LYS A 341     5394   4003   4941   -411     67     66       C  
ATOM   2539  O   LYS A 341      -6.469  53.676  41.587  1.00 42.97           O  
ANISOU 2539  O   LYS A 341     5994   4744   5589   -477     92     97       O  
ATOM   2540  CB  LYS A 341      -3.969  54.854  39.795  1.00 34.70           C  
ANISOU 2540  CB  LYS A 341     4933   3639   4612   -285     44      1       C  
ATOM   2541  CG  LYS A 341      -3.089  56.063  39.541  1.00 38.76           C  
ANISOU 2541  CG  LYS A 341     5399   4178   5149   -197     44    -25       C  
ATOM   2542  CD  LYS A 341      -3.594  56.919  38.407  1.00 33.55           C  
ANISOU 2542  CD  LYS A 341     4654   3582   4511   -194     53    -36       C  
ATOM   2543  CE  LYS A 341      -2.788  58.209  38.323  1.00 35.90           C  
ANISOU 2543  CE  LYS A 341     4918   3899   4825   -117     60    -58       C  
ATOM   2544  NZ  LYS A 341      -2.150  58.425  36.981  1.00 39.40           N  
ANISOU 2544  NZ  LYS A 341     5337   4343   5290    -87     35    -89       N  
ATOM   2545  N   ALA A 342      -4.713  52.265  41.474  1.00 28.72           N  
ANISOU 2545  N   ALA A 342     4367   2762   3785   -427     42     63       N  
ATOM   2546  CA  ALA A 342      -5.557  51.096  41.669  1.00 29.54           C  
ANISOU 2546  CA  ALA A 342     4541   2830   3851   -542     43     91       C  
ATOM   2547  C   ALA A 342      -6.126  51.070  43.078  1.00 50.55           C  
ANISOU 2547  C   ALA A 342     7200   5521   6485   -575     68    136       C  
ATOM   2548  O   ALA A 342      -7.252  50.611  43.285  1.00 64.54           O  
ANISOU 2548  O   ALA A 342     8966   7331   8227   -687     81    170       O  
ATOM   2549  CB  ALA A 342      -4.762  49.825  41.387  1.00 25.52           C  
ANISOU 2549  CB  ALA A 342     4180   2187   3328   -533     20     77       C  
ATOM   2550  N   LEU A 343      -5.347  51.536  44.060  1.00 47.53           N  
ANISOU 2550  N   LEU A 343     6824   5129   6106   -489     75    140       N  
ATOM   2551  CA  LEU A 343      -5.852  51.678  45.424  1.00 45.12           C  
ANISOU 2551  CA  LEU A 343     6512   4861   5771   -513    104    179       C  
ATOM   2552  C   LEU A 343      -6.983  52.695  45.474  1.00 45.58           C  
ANISOU 2552  C   LEU A 343     6450   5040   5829   -537    146    194       C  
ATOM   2553  O   LEU A 343      -8.030  52.458  46.091  1.00 45.13           O  
ANISOU 2553  O   LEU A 343     6372   5036   5740   -611    175    236       O  
ATOM   2554  CB  LEU A 343      -4.708  52.105  46.346  1.00 39.78           C  
ANISOU 2554  CB  LEU A 343     5862   4161   5090   -418     99    176       C  
ATOM   2555  CG  LEU A 343      -4.821  52.105  47.859  1.00 47.53           C  
ANISOU 2555  CG  LEU A 343     6871   5156   6031   -428    120    212       C  
ATOM   2556  CD1 LEU A 343      -5.001  50.677  48.400  1.00 57.43           C  
ANISOU 2556  CD1 LEU A 343     8232   6336   7253   -491    109    252       C  
ATOM   2557  CD2 LEU A 343      -3.575  52.772  48.448  1.00 43.10           C  
ANISOU 2557  CD2 LEU A 343     6316   4594   5464   -338    105    199       C  
ATOM   2558  N   ILE A 344      -6.782  53.840  44.819  1.00 45.77           N  
ANISOU 2558  N   ILE A 344     6395   5113   5885   -468    155    165       N  
ATOM   2559  CA  ILE A 344      -7.802  54.880  44.793  1.00 44.31           C  
ANISOU 2559  CA  ILE A 344     6100   5038   5698   -462    204    183       C  
ATOM   2560  C   ILE A 344      -9.050  54.391  44.071  1.00 52.65           C  
ANISOU 2560  C   ILE A 344     7094   6168   6744   -560    206    217       C  
ATOM   2561  O   ILE A 344     -10.162  54.461  44.608  1.00 68.48           O  
ANISOU 2561  O   ILE A 344     9039   8262   8718   -607    245    266       O  
ATOM   2562  CB  ILE A 344      -7.242  56.156  44.155  1.00 36.51           C  
ANISOU 2562  CB  ILE A 344     5061   4068   4744   -366    211    147       C  
ATOM   2563  CG1 ILE A 344      -6.144  56.729  45.041  1.00 35.58           C  
ANISOU 2563  CG1 ILE A 344     4999   3902   4617   -296    213    123       C  
ATOM   2564  CG2 ILE A 344      -8.332  57.179  44.006  1.00 37.26           C  
ANISOU 2564  CG2 ILE A 344     5052   4270   4835   -345    268    174       C  
ATOM   2565  CD1 ILE A 344      -5.273  57.724  44.350  1.00 34.72           C  
ANISOU 2565  CD1 ILE A 344     4872   3785   4536   -223    203     81       C  
ATOM   2566  N   SER A 345      -8.895  53.900  42.846  1.00 40.15           N  
ANISOU 2566  N   SER A 345     5520   4558   5177   -597    164    194       N  
ATOM   2567  CA  SER A 345      -9.977  53.157  42.213  1.00 37.82           C  
ANISOU 2567  CA  SER A 345     5195   4321   4855   -726    153    225       C  
ATOM   2568  C   SER A 345     -10.196  51.864  42.982  1.00 42.51           C  
ANISOU 2568  C   SER A 345     5892   4853   5406   -830    142    250       C  
ATOM   2569  O   SER A 345      -9.482  51.543  43.930  1.00 61.70           O  
ANISOU 2569  O   SER A 345     8413   7197   7834   -789    143    244       O  
ATOM   2570  CB  SER A 345      -9.642  52.861  40.756  1.00 43.86           C  
ANISOU 2570  CB  SER A 345     5975   5054   5636   -749    109    186       C  
ATOM   2571  OG  SER A 345      -8.561  51.941  40.663  1.00 53.97           O  
ANISOU 2571  OG  SER A 345     7398   6188   6921   -739     75    146       O  
ATOM   2572  N   GLY A 346     -11.177  51.089  42.598  1.00 37.08           N  
ANISOU 2572  N   GLY A 346     5197   4213   4680   -974    131    282       N  
ATOM   2573  CA  GLY A 346     -11.311  49.866  43.366  1.00 42.30           C  
ANISOU 2573  CA  GLY A 346     5978   4798   5297  -1075    124    305       C  
ATOM   2574  C   GLY A 346     -10.509  48.666  42.895  1.00 41.67           C  
ANISOU 2574  C   GLY A 346     6072   4551   5208  -1111     84    266       C  
ATOM   2575  O   GLY A 346     -10.744  47.562  43.385  1.00 46.07           O  
ANISOU 2575  O   GLY A 346     6744   5039   5721  -1214     79    289       O  
ATOM   2576  N   LYS A 347      -9.569  48.844  41.971  1.00 45.24           N  
ANISOU 2576  N   LYS A 347     6555   4935   5698  -1026     61    211       N  
ATOM   2577  CA  LYS A 347      -8.955  47.714  41.280  1.00 46.87           C  
ANISOU 2577  CA  LYS A 347     6924   4996   5889  -1061     33    175       C  
ATOM   2578  C   LYS A 347      -7.739  47.168  42.030  1.00 42.57           C  
ANISOU 2578  C   LYS A 347     6515   4306   5352   -955     34    165       C  
ATOM   2579  O   LYS A 347      -7.073  47.871  42.788  1.00 43.78           O  
ANISOU 2579  O   LYS A 347     6621   4476   5536   -832     44    169       O  
ATOM   2580  CB  LYS A 347      -8.542  48.121  39.867  1.00 48.11           C  
ANISOU 2580  CB  LYS A 347     7048   5159   6074  -1019     12    125       C  
ATOM   2581  CG  LYS A 347      -9.605  48.909  39.121  1.00 56.30           C  
ANISOU 2581  CG  LYS A 347     7922   6361   7109  -1086     11    141       C  
ATOM   2582  CD  LYS A 347      -8.968  49.781  38.051  1.00 67.66           C  
ANISOU 2582  CD  LYS A 347     9293   7821   8594   -981      0     97       C  
ATOM   2583  CE  LYS A 347      -9.999  50.552  37.244  1.00 71.20           C  
ANISOU 2583  CE  LYS A 347     9581   8434   9037  -1036     -1    121       C  
ATOM   2584  NZ  LYS A 347      -9.492  50.789  35.856  1.00 75.10           N  
ANISOU 2584  NZ  LYS A 347    10071   8915   9548  -1005    -26     73       N  
ATOM   2585  N   GLN A 348      -7.435  45.905  41.774  1.00 44.62           N  
ANISOU 2585  N   GLN A 348     6953   4424   5579  -1003     24    155       N  
ATOM   2586  CA  GLN A 348      -6.346  45.223  42.478  1.00 48.62           C  
ANISOU 2586  CA  GLN A 348     7600   4792   6083   -900     29    162       C  
ATOM   2587  C   GLN A 348      -4.989  45.785  42.071  1.00 50.51           C  
ANISOU 2587  C   GLN A 348     7813   5007   6369   -719     21    126       C  
ATOM   2588  O   GLN A 348      -4.630  45.708  40.890  1.00 46.76           O  
ANISOU 2588  O   GLN A 348     7363   4498   5904   -697     12     83       O  
ATOM   2589  CB  GLN A 348      -6.396  43.729  42.186  1.00 46.64           C  
ANISOU 2589  CB  GLN A 348     7562   4383   5777   -989     30    161       C  
ATOM   2590  CG  GLN A 348      -5.648  42.881  43.188  1.00 53.88           C  
ANISOU 2590  CG  GLN A 348     8630   5168   6674   -914     44    195       C  
ATOM   2591  CD  GLN A 348      -6.190  43.021  44.607  1.00 59.00           C  
ANISOU 2591  CD  GLN A 348     9230   5881   7307   -957     53    253       C  
ATOM   2592  OE1 GLN A 348      -5.699  43.837  45.391  1.00 55.15           O  
ANISOU 2592  OE1 GLN A 348     8638   5465   6851   -846     55    268       O  
ATOM   2593  NE2 GLN A 348      -7.203  42.211  44.946  1.00 59.01           N  
ANISOU 2593  NE2 GLN A 348     9312   5857   7251  -1128     61    286       N  
ATOM   2594  N   PRO A 349      -4.211  46.349  42.996  1.00 50.11           N  
ANISOU 2594  N   PRO A 349     7715   4983   6342   -598     24    145       N  
ATOM   2595  CA  PRO A 349      -2.843  46.779  42.663  1.00 45.34           C  
ANISOU 2595  CA  PRO A 349     7092   4365   5772   -437     13    122       C  
ATOM   2596  C   PRO A 349      -2.012  45.626  42.117  1.00 43.78           C  
ANISOU 2596  C   PRO A 349     7057   4023   5555   -376     15    114       C  
ATOM   2597  O   PRO A 349      -1.999  44.526  42.677  1.00 45.72           O  
ANISOU 2597  O   PRO A 349     7450   4160   5763   -393     27    147       O  
ATOM   2598  CB  PRO A 349      -2.299  47.275  44.010  1.00 33.21           C  
ANISOU 2598  CB  PRO A 349     5508   2873   4237   -360     14    160       C  
ATOM   2599  CG  PRO A 349      -3.507  47.701  44.732  1.00 34.25           C  
ANISOU 2599  CG  PRO A 349     5570   3087   4355   -467     29    181       C  
ATOM   2600  CD  PRO A 349      -4.561  46.695  44.381  1.00 43.30           C  
ANISOU 2600  CD  PRO A 349     6802   4181   5469   -610     36    190       C  
ATOM   2601  N   LYS A 350      -1.303  45.889  41.020  1.00 51.27           N  
ANISOU 2601  N   LYS A 350     7986   4967   6527   -296      9     72       N  
ATOM   2602  CA  LYS A 350      -0.487  44.869  40.358  1.00 49.27           C  
ANISOU 2602  CA  LYS A 350     7887   4581   6254   -217     22     61       C  
ATOM   2603  C   LYS A 350       0.941  44.967  40.883  1.00 47.45           C  
ANISOU 2603  C   LYS A 350     7643   4352   6034    -34     22     93       C  
ATOM   2604  O   LYS A 350       1.703  45.863  40.506  1.00 53.19           O  
ANISOU 2604  O   LYS A 350     8249   5167   6792     57      9     78       O  
ATOM   2605  CB  LYS A 350      -0.541  45.024  38.845  1.00 49.94           C  
ANISOU 2605  CB  LYS A 350     7963   4664   6348   -237     20      1       C  
ATOM   2606  CG  LYS A 350      -1.931  44.876  38.265  1.00 65.93           C  
ANISOU 2606  CG  LYS A 350     9997   6704   8350   -427     15    -23       C  
ATOM   2607  CD  LYS A 350      -1.953  45.334  36.810  1.00 76.38           C  
ANISOU 2607  CD  LYS A 350    11267   8068   9687   -440      5    -78       C  
ATOM   2608  CE  LYS A 350      -3.052  44.649  36.004  1.00 80.92           C  
ANISOU 2608  CE  LYS A 350    11930   8605  10211   -622      3   -103       C  
ATOM   2609  NZ  LYS A 350      -4.249  45.526  35.841  1.00 79.31           N  
ANISOU 2609  NZ  LYS A 350    11557   8560  10018   -750    -19    -95       N  
ATOM   2610  N   ILE A 351       1.301  44.052  41.769  1.00 37.92           N  
ANISOU 2610  N   ILE A 351     6557   3058   4794     15     36    145       N  
ATOM   2611  CA  ILE A 351       2.635  44.011  42.342  1.00 46.88           C  
ANISOU 2611  CA  ILE A 351     7680   4206   5925    188     35    194       C  
ATOM   2612  C   ILE A 351       3.439  43.022  41.519  1.00 45.87           C  
ANISOU 2612  C   ILE A 351     7699   3953   5776    308     67    192       C  
ATOM   2613  O   ILE A 351       3.252  41.806  41.642  1.00 55.05           O  
ANISOU 2613  O   ILE A 351     9054   4965   6897    300     97    212       O  
ATOM   2614  CB  ILE A 351       2.598  43.610  43.819  1.00 44.91           C  
ANISOU 2614  CB  ILE A 351     7472   3944   5647    188     34    263       C  
ATOM   2615  CG1 ILE A 351       1.774  44.617  44.622  1.00 43.13           C  
ANISOU 2615  CG1 ILE A 351     7110   3841   5437     74     13    261       C  
ATOM   2616  CG2 ILE A 351       4.013  43.480  44.354  1.00 45.00           C  
ANISOU 2616  CG2 ILE A 351     7472   3981   5645    370     31    325       C  
ATOM   2617  CD1 ILE A 351       1.747  44.310  46.127  1.00 50.88           C  
ANISOU 2617  CD1 ILE A 351     8122   4825   6384     69     11    329       C  
ATOM   2618  N   LYS A 352       4.322  43.534  40.662  1.00 48.26           N  
ANISOU 2618  N   LYS A 352     7921   4314   6101    418     64    169       N  
ATOM   2619  CA  LYS A 352       5.119  42.673  39.794  1.00 54.27           C  
ANISOU 2619  CA  LYS A 352     8813   4968   6839    548    103    165       C  
ATOM   2620  C   LYS A 352       6.592  42.615  40.168  1.00 51.12           C  
ANISOU 2620  C   LYS A 352     8373   4620   6430    760    111    232       C  
ATOM   2621  O   LYS A 352       7.265  41.640  39.819  1.00 48.89           O  
ANISOU 2621  O   LYS A 352     8233   4229   6115    897    157    257       O  
ATOM   2622  CB  LYS A 352       5.007  43.125  38.328  1.00 49.46           C  
ANISOU 2622  CB  LYS A 352     8164   4379   6250    518    105     88       C  
ATOM   2623  CG  LYS A 352       3.652  43.674  37.897  1.00 52.71           C  
ANISOU 2623  CG  LYS A 352     8522   4825   6680    315     81     29       C  
ATOM   2624  CD  LYS A 352       3.772  44.341  36.531  1.00 58.77           C  
ANISOU 2624  CD  LYS A 352     9209   5652   7471    315     75    -34       C  
ATOM   2625  CE  LYS A 352       2.670  45.371  36.278  1.00 66.28           C  
ANISOU 2625  CE  LYS A 352    10019   6712   8452    157     41    -70       C  
ATOM   2626  NZ  LYS A 352       1.445  44.768  35.672  1.00 68.53           N  
ANISOU 2626  NZ  LYS A 352    10409   6924   8706    -13     46   -108       N  
ATOM   2627  N   LYS A 353       7.101  43.629  40.855  1.00 51.63           N  
ANISOU 2627  N   LYS A 353     8251   4850   6515    788     71    265       N  
ATOM   2628  CA  LYS A 353       8.490  43.703  41.273  1.00 53.89           C  
ANISOU 2628  CA  LYS A 353     8463   5228   6785    967     66    339       C  
ATOM   2629  C   LYS A 353       8.525  44.373  42.640  1.00 44.18           C  
ANISOU 2629  C   LYS A 353     7115   4121   5552    923     22    390       C  
ATOM   2630  O   LYS A 353       7.521  44.916  43.103  1.00 39.70           O  
ANISOU 2630  O   LYS A 353     6511   3571   5001    767      0    357       O  
ATOM   2631  CB  LYS A 353       9.329  44.475  40.243  1.00 56.90           C  
ANISOU 2631  CB  LYS A 353     8712   5721   7187   1045     60    312       C  
ATOM   2632  CG  LYS A 353      10.666  43.849  39.897  1.00 66.05           C  
ANISOU 2632  CG  LYS A 353     9898   6885   8314   1263     95    372       C  
ATOM   2633  CD  LYS A 353      11.407  44.699  38.864  1.00 73.85           C  
ANISOU 2633  CD  LYS A 353    10741   7999   9320   1317     86    343       C  
ATOM   2634  CE  LYS A 353      12.790  44.132  38.547  1.00 77.38           C  
ANISOU 2634  CE  LYS A 353    11188   8481   9730   1546    125    414       C  
ATOM   2635  NZ  LYS A 353      13.697  45.179  37.986  1.00 75.61           N  
ANISOU 2635  NZ  LYS A 353    10765   8450   9515   1589     98    417       N  
ATOM   2636  N   HIS A 354       9.688  44.334  43.290  1.00 43.42           N  
ANISOU 2636  N   HIS A 354     6956   4117   5425   1061     11    475       N  
ATOM   2637  CA  HIS A 354       9.904  45.069  44.540  1.00 47.84           C  
ANISOU 2637  CA  HIS A 354     7392   4817   5969   1020    -36    524       C  
ATOM   2638  C   HIS A 354       8.775  44.791  45.528  1.00 41.51           C  
ANISOU 2638  C   HIS A 354     6672   3939   5160    888    -38    523       C  
ATOM   2639  O   HIS A 354       8.090  45.694  46.006  1.00 39.14           O  
ANISOU 2639  O   HIS A 354     6291   3705   4874    752    -65    488       O  
ATOM   2640  CB  HIS A 354      10.035  46.568  44.267  1.00 41.92           C  
ANISOU 2640  CB  HIS A 354     6460   4225   5245    942    -77    475       C  
ATOM   2641  CG  HIS A 354      11.005  46.893  43.176  1.00 49.50           C  
ANISOU 2641  CG  HIS A 354     7337   5258   6213   1045    -74    467       C  
ATOM   2642  ND1 HIS A 354      12.369  46.918  43.377  1.00 48.79           N  
ANISOU 2642  ND1 HIS A 354     7155   5297   6086   1184    -88    548       N  
ATOM   2643  CD2 HIS A 354      10.814  47.188  41.866  1.00 47.82           C  
ANISOU 2643  CD2 HIS A 354     7115   5019   6037   1030    -58    393       C  
ATOM   2644  CE1 HIS A 354      12.974  47.222  42.242  1.00 47.90           C  
ANISOU 2644  CE1 HIS A 354     6979   5234   5986   1250    -78    523       C  
ATOM   2645  NE2 HIS A 354      12.054  47.394  41.312  1.00 46.36           N  
ANISOU 2645  NE2 HIS A 354     6837   4941   5837   1158    -60    427       N  
ATOM   2646  N   VAL A 355       8.548  43.508  45.786  1.00 34.19           N  
ANISOU 2646  N   VAL A 355     5921   2863   4208    930     -2    561       N  
ATOM   2647  CA  VAL A 355       7.304  43.078  46.417  1.00 43.13           C  
ANISOU 2647  CA  VAL A 355     7160   3894   5334    786      6    548       C  
ATOM   2648  C   VAL A 355       7.187  43.653  47.819  1.00 49.45           C  
ANISOU 2648  C   VAL A 355     7873   4803   6114    723    -30    591       C  
ATOM   2649  O   VAL A 355       6.264  44.424  48.117  1.00 43.22           O  
ANISOU 2649  O   VAL A 355     7020   4058   5342    574    -45    544       O  
ATOM   2650  CB  VAL A 355       7.211  41.545  46.433  1.00 41.29           C  
ANISOU 2650  CB  VAL A 355     7151   3470   5066    848     54    588       C  
ATOM   2651  CG1 VAL A 355       6.003  41.082  47.260  1.00 36.36           C  
ANISOU 2651  CG1 VAL A 355     6631   2759   4424    692     59    591       C  
ATOM   2652  CG2 VAL A 355       7.151  41.033  45.027  1.00 40.46           C  
ANISOU 2652  CG2 VAL A 355     7154   3246   4974    878     94    529       C  
ATOM   2653  N   LYS A 356       8.126  43.291  48.697  1.00 41.17           N  
ANISOU 2653  N   LYS A 356     6819   3804   5021    840    -41    687       N  
ATOM   2654  CA  LYS A 356       7.951  43.670  50.090  1.00 46.46           C  
ANISOU 2654  CA  LYS A 356     7436   4558   5657    770    -72    732       C  
ATOM   2655  C   LYS A 356       8.014  45.187  50.293  1.00 45.14           C  
ANISOU 2655  C   LYS A 356     7088   4562   5502    684   -114    689       C  
ATOM   2656  O   LYS A 356       7.273  45.727  51.123  1.00 43.07           O  
ANISOU 2656  O   LYS A 356     6800   4334   5229    559   -125    672       O  
ATOM   2657  CB  LYS A 356       8.962  42.955  50.974  1.00 48.91           C  
ANISOU 2657  CB  LYS A 356     7775   4899   5910    913    -79    852       C  
ATOM   2658  CG  LYS A 356       8.485  42.932  52.421  1.00 77.05           C  
ANISOU 2658  CG  LYS A 356    11356   8488   9433    823    -97    898       C  
ATOM   2659  CD  LYS A 356       9.613  43.123  53.447  1.00 83.29           C  
ANISOU 2659  CD  LYS A 356    12049   9435  10160    912   -138   1002       C  
ATOM   2660  CE  LYS A 356       9.384  42.229  54.640  1.00 74.75           C  
ANISOU 2660  CE  LYS A 356    11081   8294   9027    917   -131   1088       C  
ATOM   2661  NZ  LYS A 356      10.648  41.918  55.375  1.00 79.72           N  
ANISOU 2661  NZ  LYS A 356    11659   9039   9590   1067   -158   1218       N  
ATOM   2662  N   ILE A 357       8.838  45.908  49.531  1.00 44.44           N  
ANISOU 2662  N   ILE A 357     6883   4573   5430    744   -132    669       N  
ATOM   2663  CA  ILE A 357       8.842  47.358  49.723  1.00 45.57           C  
ANISOU 2663  CA  ILE A 357     6881   4857   5576    647   -166    625       C  
ATOM   2664  C   ILE A 357       7.566  47.983  49.160  1.00 47.35           C  
ANISOU 2664  C   ILE A 357     7109   5028   5852    512   -147    525       C  
ATOM   2665  O   ILE A 357       7.117  49.031  49.647  1.00 48.14           O  
ANISOU 2665  O   ILE A 357     7141   5201   5949    407   -159    490       O  
ATOM   2666  CB  ILE A 357      10.104  48.004  49.117  1.00 45.27           C  
ANISOU 2666  CB  ILE A 357     6714   4953   5531    733   -194    637       C  
ATOM   2667  CG1 ILE A 357      10.370  49.378  49.753  1.00 51.70           C  
ANISOU 2667  CG1 ILE A 357     7402   5926   6316    635   -237    625       C  
ATOM   2668  CG2 ILE A 357       9.968  48.172  47.604  1.00 44.64           C  
ANISOU 2668  CG2 ILE A 357     6628   4824   5510    751   -171    563       C  
ATOM   2669  CD1 ILE A 357      10.238  49.421  51.292  1.00 47.61           C  
ANISOU 2669  CD1 ILE A 357     6897   5455   5737    572   -258    676       C  
ATOM   2670  N   THR A 358       6.945  47.359  48.155  1.00 39.23           N  
ANISOU 2670  N   THR A 358     6164   3876   4864    510   -114    481       N  
ATOM   2671  CA  THR A 358       5.694  47.907  47.637  1.00 42.95           C  
ANISOU 2671  CA  THR A 358     6626   4316   5376    380    -98    400       C  
ATOM   2672  C   THR A 358       4.539  47.610  48.585  1.00 35.95           C  
ANISOU 2672  C   THR A 358     5804   3381   4473    269    -82    409       C  
ATOM   2673  O   THR A 358       3.636  48.445  48.749  1.00 33.51           O  
ANISOU 2673  O   THR A 358     5439   3115   4177    163    -75    367       O  
ATOM   2674  CB  THR A 358       5.415  47.367  46.227  1.00 40.10           C  
ANISOU 2674  CB  THR A 358     6327   3857   5053    397    -73    352       C  
ATOM   2675  OG1 THR A 358       6.490  47.757  45.366  1.00 39.97           O  
ANISOU 2675  OG1 THR A 358     6237   3901   5049    499    -85    343       O  
ATOM   2676  CG2 THR A 358       4.116  47.935  45.659  1.00 26.84           C  
ANISOU 2676  CG2 THR A 358     4622   2168   3408    263    -61    281       C  
ATOM   2677  N   GLU A 359       4.572  46.447  49.230  1.00 39.15           N  
ANISOU 2677  N   GLU A 359     6327   3704   4845    299    -72    470       N  
ATOM   2678  CA  GLU A 359       3.644  46.175  50.321  1.00 43.43           C  
ANISOU 2678  CA  GLU A 359     6921   4220   5359    199    -61    494       C  
ATOM   2679  C   GLU A 359       3.631  47.331  51.312  1.00 44.20           C  
ANISOU 2679  C   GLU A 359     6910   4448   5435    148    -79    495       C  
ATOM   2680  O   GLU A 359       2.565  47.858  51.657  1.00 42.16           O  
ANISOU 2680  O   GLU A 359     6628   4210   5180     38    -61    463       O  
ATOM   2681  CB  GLU A 359       4.022  44.868  51.019  1.00 40.06           C  
ANISOU 2681  CB  GLU A 359     6628   3705   4889    265    -54    576       C  
ATOM   2682  CG  GLU A 359       3.432  43.622  50.357  1.00 44.48           C  
ANISOU 2682  CG  GLU A 359     7352   4097   5453    245    -19    569       C  
ATOM   2683  CD  GLU A 359       4.212  42.359  50.681  1.00 44.98           C  
ANISOU 2683  CD  GLU A 359     7557   4058   5477    371     -6    649       C  
ATOM   2684  OE1 GLU A 359       3.975  41.336  50.016  1.00 50.60           O  
ANISOU 2684  OE1 GLU A 359     8424   4618   6185    379     27    642       O  
ATOM   2685  OE2 GLU A 359       5.066  42.386  51.594  1.00 50.67           O  
ANISOU 2685  OE2 GLU A 359     8241   4850   6163    461    -26    723       O  
ATOM   2686  N   GLU A 360       4.819  47.775  51.739  1.00 41.13           N  
ANISOU 2686  N   GLU A 360     6453   4156   5017    227   -112    531       N  
ATOM   2687  CA  GLU A 360       4.890  48.835  52.741  1.00 37.69           C  
ANISOU 2687  CA  GLU A 360     5938   3837   4544    168   -129    532       C  
ATOM   2688  C   GLU A 360       4.460  50.167  52.150  1.00 36.56           C  
ANISOU 2688  C   GLU A 360     5706   3750   4435    103   -121    451       C  
ATOM   2689  O   GLU A 360       3.795  50.967  52.820  1.00 35.81           O  
ANISOU 2689  O   GLU A 360     5589   3697   4322     18   -105    426       O  
ATOM   2690  CB  GLU A 360       6.303  48.935  53.309  1.00 45.23           C  
ANISOU 2690  CB  GLU A 360     6843   4895   5448    252   -173    598       C  
ATOM   2691  CG  GLU A 360       6.760  47.706  54.093  1.00 53.21           C  
ANISOU 2691  CG  GLU A 360     7936   5869   6413    328   -180    695       C  
ATOM   2692  CD  GLU A 360       8.031  47.968  54.883  1.00 63.84           C  
ANISOU 2692  CD  GLU A 360     9208   7356   7692    387   -227    771       C  
ATOM   2693  OE1 GLU A 360       9.120  47.618  54.385  1.00 64.06           O  
ANISOU 2693  OE1 GLU A 360     9201   7424   7715    512   -245    819       O  
ATOM   2694  OE2 GLU A 360       7.941  48.525  56.002  1.00 69.47           O  
ANISOU 2694  OE2 GLU A 360     9897   8149   8350    306   -245    785       O  
ATOM   2695  N   TYR A 361       4.820  50.420  50.889  1.00 38.44           N  
ANISOU 2695  N   TYR A 361     5901   3986   4719    149   -125    410       N  
ATOM   2696  CA  TYR A 361       4.370  51.647  50.242  1.00 37.67           C  
ANISOU 2696  CA  TYR A 361     5728   3930   4654     93   -113    338       C  
ATOM   2697  C   TYR A 361       2.848  51.714  50.211  1.00 39.49           C  
ANISOU 2697  C   TYR A 361     5985   4111   4909      2    -71    302       C  
ATOM   2698  O   TYR A 361       2.252  52.754  50.528  1.00 29.84           O  
ANISOU 2698  O   TYR A 361     4719   2937   3681    -58    -50    270       O  
ATOM   2699  CB  TYR A 361       4.938  51.748  48.821  1.00 37.86           C  
ANISOU 2699  CB  TYR A 361     5712   3951   4724    157   -123    306       C  
ATOM   2700  CG  TYR A 361       4.292  52.860  48.036  1.00 34.65           C  
ANISOU 2700  CG  TYR A 361     5244   3567   4356    101   -105    235       C  
ATOM   2701  CD1 TYR A 361       4.706  54.182  48.195  1.00 28.06           C  
ANISOU 2701  CD1 TYR A 361     4338   2820   3505     77   -115    211       C  
ATOM   2702  CD2 TYR A 361       3.239  52.602  47.174  1.00 24.38           C  
ANISOU 2702  CD2 TYR A 361     3963   2201   3100     64    -77    197       C  
ATOM   2703  CE1 TYR A 361       4.098  55.213  47.494  1.00 32.19           C  
ANISOU 2703  CE1 TYR A 361     4818   3354   4060     37    -92    152       C  
ATOM   2704  CE2 TYR A 361       2.629  53.626  46.463  1.00 39.08           C  
ANISOU 2704  CE2 TYR A 361     5762   4093   4994     24    -59    144       C  
ATOM   2705  CZ  TYR A 361       3.057  54.932  46.628  1.00 34.28           C  
ANISOU 2705  CZ  TYR A 361     5090   3560   4373     18    -63    123       C  
ATOM   2706  OH  TYR A 361       2.441  55.957  45.917  1.00 34.49           O  
ANISOU 2706  OH  TYR A 361     5067   3607   4429    -10    -39     76       O  
ATOM   2707  N   LEU A 362       2.196  50.606  49.859  1.00 25.98           N  
ANISOU 2707  N   LEU A 362     4347   2306   3215    -11    -55    312       N  
ATOM   2708  CA  LEU A 362       0.747  50.663  49.727  1.00 34.65           C  
ANISOU 2708  CA  LEU A 362     5450   3382   4331   -107    -19    286       C  
ATOM   2709  C   LEU A 362       0.074  50.870  51.075  1.00 36.46           C  
ANISOU 2709  C   LEU A 362     5689   3645   4517   -173      3    313       C  
ATOM   2710  O   LEU A 362      -0.974  51.521  51.147  1.00 39.79           O  
ANISOU 2710  O   LEU A 362     6069   4105   4944   -237     38    289       O  
ATOM   2711  CB  LEU A 362       0.237  49.401  49.031  1.00 31.36           C  
ANISOU 2711  CB  LEU A 362     5122   2863   3930   -130    -11    292       C  
ATOM   2712  CG  LEU A 362       0.494  49.398  47.514  1.00 28.86           C  
ANISOU 2712  CG  LEU A 362     4789   2519   3657    -94    -18    248       C  
ATOM   2713  CD1 LEU A 362       0.041  48.099  46.876  1.00 31.51           C  
ANISOU 2713  CD1 LEU A 362     5239   2740   3991   -128     -8    251       C  
ATOM   2714  CD2 LEU A 362      -0.165  50.602  46.841  1.00 31.01           C  
ANISOU 2714  CD2 LEU A 362     4954   2867   3963   -138     -6    196       C  
ATOM   2715  N   LEU A 363       0.660  50.342  52.156  1.00 36.23           N  
ANISOU 2715  N   LEU A 363     5713   3612   4441   -150    -14    367       N  
ATOM   2716  CA  LEU A 363       0.121  50.621  53.483  1.00 31.08           C  
ANISOU 2716  CA  LEU A 363     5070   3001   3739   -210      7    391       C  
ATOM   2717  C   LEU A 363       0.343  52.082  53.873  1.00 29.12           C  
ANISOU 2717  C   LEU A 363     4749   2844   3471   -217     14    356       C  
ATOM   2718  O   LEU A 363      -0.563  52.734  54.403  1.00 35.00           O  
ANISOU 2718  O   LEU A 363     5480   3622   4198   -274     57    339       O  
ATOM   2719  CB  LEU A 363       0.740  49.674  54.503  1.00 31.45           C  
ANISOU 2719  CB  LEU A 363     5192   3022   3735   -182    -16    462       C  
ATOM   2720  CG  LEU A 363       0.361  48.196  54.339  1.00 33.45           C  
ANISOU 2720  CG  LEU A 363     5552   3164   3993   -190     -9    502       C  
ATOM   2721  CD1 LEU A 363       1.274  47.288  55.153  1.00 38.86           C  
ANISOU 2721  CD1 LEU A 363     6314   3820   4631   -122    -35    579       C  
ATOM   2722  CD2 LEU A 363      -1.085  47.916  54.708  1.00 32.08           C  
ANISOU 2722  CD2 LEU A 363     5409   2970   3810   -305     31    504       C  
ATOM   2723  N   TYR A 364       1.526  52.628  53.580  1.00 35.07           N  
ANISOU 2723  N   TYR A 364     5463   3640   4221   -160    -23    345       N  
ATOM   2724  CA  TYR A 364       1.782  54.040  53.866  1.00 25.85           C  
ANISOU 2724  CA  TYR A 364     4248   2548   3027   -182    -16    307       C  
ATOM   2725  C   TYR A 364       0.847  54.943  53.063  1.00 37.99           C  
ANISOU 2725  C   TYR A 364     5743   4082   4609   -206     29    246       C  
ATOM   2726  O   TYR A 364       0.346  55.951  53.579  1.00 38.77           O  
ANISOU 2726  O   TYR A 364     5838   4214   4679   -242     70    220       O  
ATOM   2727  CB  TYR A 364       3.250  54.364  53.571  1.00 25.81           C  
ANISOU 2727  CB  TYR A 364     4203   2596   3007   -130    -70    313       C  
ATOM   2728  CG  TYR A 364       3.619  55.822  53.746  1.00 37.76           C  
ANISOU 2728  CG  TYR A 364     5681   4179   4485   -169    -68    270       C  
ATOM   2729  CD1 TYR A 364       3.456  56.731  52.705  1.00 27.97           C  
ANISOU 2729  CD1 TYR A 364     4400   2938   3290   -167    -50    212       C  
ATOM   2730  CD2 TYR A 364       4.151  56.293  54.952  1.00 33.38           C  
ANISOU 2730  CD2 TYR A 364     5148   3690   3845   -215    -84    290       C  
ATOM   2731  CE1 TYR A 364       3.797  58.073  52.862  1.00 39.01           C  
ANISOU 2731  CE1 TYR A 364     5789   4383   4649   -208    -44    173       C  
ATOM   2732  CE2 TYR A 364       4.489  57.640  55.114  1.00 27.26           C  
ANISOU 2732  CE2 TYR A 364     4366   2965   3025   -267    -80    247       C  
ATOM   2733  CZ  TYR A 364       4.309  58.516  54.067  1.00 33.84           C  
ANISOU 2733  CZ  TYR A 364     5170   3783   3905   -262    -57    189       C  
ATOM   2734  OH  TYR A 364       4.645  59.830  54.212  1.00 38.12           O  
ANISOU 2734  OH  TYR A 364     5726   4360   4398   -318    -48    147       O  
ATOM   2735  N   ALA A 365       0.588  54.591  51.801  1.00 35.08           N  
ANISOU 2735  N   ALA A 365     5349   3675   4304   -182     28    227       N  
ATOM   2736  CA  ALA A 365      -0.316  55.392  50.980  1.00 38.64           C  
ANISOU 2736  CA  ALA A 365     5751   4136   4796   -198     68    181       C  
ATOM   2737  C   ALA A 365      -1.731  55.375  51.554  1.00 32.94           C  
ANISOU 2737  C   ALA A 365     5035   3420   4061   -253    124    193       C  
ATOM   2738  O   ALA A 365      -2.376  56.420  51.696  1.00 31.25           O  
ANISOU 2738  O   ALA A 365     4792   3244   3839   -262    174    171       O  
ATOM   2739  CB  ALA A 365      -0.302  54.877  49.533  1.00 36.91           C  
ANISOU 2739  CB  ALA A 365     5508   3880   4638   -171     49    165       C  
ATOM   2740  N   ARG A 366      -2.223  54.191  51.900  1.00 31.31           N  
ANISOU 2740  N   ARG A 366     4871   3177   3847   -288    122    234       N  
ATOM   2741  CA  ARG A 366      -3.563  54.079  52.459  1.00 33.50           C  
ANISOU 2741  CA  ARG A 366     5146   3477   4107   -350    174    255       C  
ATOM   2742  C   ARG A 366      -3.733  54.986  53.673  1.00 36.25           C  
ANISOU 2742  C   ARG A 366     5501   3874   4399   -356    216    255       C  
ATOM   2743  O   ARG A 366      -4.788  55.611  53.846  1.00 40.15           O  
ANISOU 2743  O   ARG A 366     5959   4413   4883   -372    278    252       O  
ATOM   2744  CB  ARG A 366      -3.838  52.621  52.811  1.00 26.22           C  
ANISOU 2744  CB  ARG A 366     4290   2502   3170   -397    158    304       C  
ATOM   2745  CG  ARG A 366      -5.110  52.377  53.555  1.00 28.08           C  
ANISOU 2745  CG  ARG A 366     4526   2770   3373   -473    205    338       C  
ATOM   2746  CD  ARG A 366      -5.316  50.874  53.792  1.00 31.67           C  
ANISOU 2746  CD  ARG A 366     5063   3158   3811   -533    185    386       C  
ATOM   2747  NE  ARG A 366      -5.529  50.093  52.571  1.00 37.91           N  
ANISOU 2747  NE  ARG A 366     5871   3894   4641   -562    163    377       N  
ATOM   2748  CZ  ARG A 366      -6.723  49.903  52.008  1.00 36.02           C  
ANISOU 2748  CZ  ARG A 366     5591   3687   4407   -647    186    383       C  
ATOM   2749  NH1 ARG A 366      -7.794  50.460  52.547  1.00 28.06           N  
ANISOU 2749  NH1 ARG A 366     4512   2775   3376   -693    235    402       N  
ATOM   2750  NH2 ARG A 366      -6.855  49.162  50.908  1.00 30.20           N  
ANISOU 2750  NH2 ARG A 366     4886   2897   3693   -688    162    372       N  
ATOM   2751  N   LYS A 367      -2.685  55.108  54.500  1.00 30.82           N  
ANISOU 2751  N   LYS A 367     4858   3186   3666   -340    186    261       N  
ATOM   2752  CA  LYS A 367      -2.774  55.973  55.673  1.00 39.56           C  
ANISOU 2752  CA  LYS A 367     5990   4333   4706   -357    225    256       C  
ATOM   2753  C   LYS A 367      -2.777  57.439  55.274  1.00 42.66           C  
ANISOU 2753  C   LYS A 367     6356   4751   5101   -331    262    201       C  
ATOM   2754  O   LYS A 367      -3.529  58.241  55.838  1.00 47.71           O  
ANISOU 2754  O   LYS A 367     7008   5414   5705   -337    332    189       O  
ATOM   2755  CB  LYS A 367      -1.626  55.688  56.645  1.00 47.18           C  
ANISOU 2755  CB  LYS A 367     7010   5305   5612   -361    175    282       C  
ATOM   2756  CG  LYS A 367      -1.538  54.231  57.098  1.00 50.25           C  
ANISOU 2756  CG  LYS A 367     7441   5660   5992   -373    142    344       C  
ATOM   2757  CD  LYS A 367      -0.821  54.081  58.420  1.00 46.52           C  
ANISOU 2757  CD  LYS A 367     7021   5217   5439   -388    116    383       C  
ATOM   2758  CE  LYS A 367       0.497  54.810  58.422  1.00 46.59           C  
ANISOU 2758  CE  LYS A 367     7013   5271   5418   -365     69    366       C  
ATOM   2759  NZ  LYS A 367       1.173  54.711  59.746  1.00 47.38           N  
ANISOU 2759  NZ  LYS A 367     7156   5420   5426   -393     40    409       N  
ATOM   2760  N   ARG A 368      -1.960  57.812  54.290  1.00 47.77           N  
ANISOU 2760  N   ARG A 368     6974   5389   5787   -296    223    170       N  
ATOM   2761  CA  ARG A 368      -1.951  59.207  53.860  1.00 43.21           C  
ANISOU 2761  CA  ARG A 368     6385   4824   5210   -275    259    120       C  
ATOM   2762  C   ARG A 368      -3.294  59.608  53.247  1.00 39.09           C  
ANISOU 2762  C   ARG A 368     5815   4310   4726   -254    329    114       C  
ATOM   2763  O   ARG A 368      -3.807  60.699  53.524  1.00 49.22           O  
ANISOU 2763  O   ARG A 368     7116   5605   5980   -235    398     93       O  
ATOM   2764  CB  ARG A 368      -0.783  59.447  52.902  1.00 37.86           C  
ANISOU 2764  CB  ARG A 368     5680   4142   4563   -250    199     96       C  
ATOM   2765  CG  ARG A 368       0.574  59.551  53.626  1.00 46.34           C  
ANISOU 2765  CG  ARG A 368     6791   5243   5575   -273    144    103       C  
ATOM   2766  CD  ARG A 368       0.841  60.972  54.192  1.00 51.38           C  
ANISOU 2766  CD  ARG A 368     7481   5897   6143   -309    176     62       C  
ATOM   2767  NE  ARG A 368       1.715  61.736  53.305  1.00 63.29           N  
ANISOU 2767  NE  ARG A 368     8966   7416   7664   -304    146     29       N  
ATOM   2768  CZ  ARG A 368       1.313  62.747  52.538  1.00 76.67           C  
ANISOU 2768  CZ  ARG A 368    10659   9086   9385   -286    191    -13       C  
ATOM   2769  NH1 ARG A 368       0.050  63.148  52.568  1.00 77.83           N  
ANISOU 2769  NH1 ARG A 368    10822   9205   9547   -259    273    -24       N  
ATOM   2770  NH2 ARG A 368       2.177  63.365  51.743  1.00 83.27           N  
ANISOU 2770  NH2 ARG A 368    11475   9934  10229   -289    158    -38       N  
ATOM   2771  N   LEU A 369      -3.902  58.715  52.459  1.00 35.73           N  
ANISOU 2771  N   LEU A 369     5336   3884   4357   -256    315    137       N  
ATOM   2772  CA  LEU A 369      -5.249  58.956  51.936  1.00 41.41           C  
ANISOU 2772  CA  LEU A 369     5992   4639   5103   -248    375    148       C  
ATOM   2773  C   LEU A 369      -6.295  59.061  53.049  1.00 40.60           C  
ANISOU 2773  C   LEU A 369     5901   4576   4948   -265    448    180       C  
ATOM   2774  O   LEU A 369      -7.255  59.827  52.933  1.00 36.28           O  
ANISOU 2774  O   LEU A 369     5314   4074   4398   -230    522    185       O  
ATOM   2775  CB  LEU A 369      -5.635  57.845  50.957  1.00 31.55           C  
ANISOU 2775  CB  LEU A 369     4694   3386   3907   -276    335    170       C  
ATOM   2776  CG  LEU A 369      -4.754  57.776  49.702  1.00 44.12           C  
ANISOU 2776  CG  LEU A 369     6269   4945   5551   -249    277    138       C  
ATOM   2777  CD1 LEU A 369      -4.832  56.408  49.024  1.00 43.00           C  
ANISOU 2777  CD1 LEU A 369     6128   4771   5439   -289    229    157       C  
ATOM   2778  CD2 LEU A 369      -5.089  58.901  48.722  1.00 39.95           C  
ANISOU 2778  CD2 LEU A 369     5678   4448   5053   -205    309    111       C  
ATOM   2779  N   ALA A 370      -6.154  58.280  54.121  1.00 36.06           N  
ANISOU 2779  N   ALA A 370     5379   3991   4330   -311    432    208       N  
ATOM   2780  CA  ALA A 370      -7.134  58.380  55.200  1.00 35.47           C  
ANISOU 2780  CA  ALA A 370     5316   3960   4201   -329    505    239       C  
ATOM   2781  C   ALA A 370      -7.012  59.706  55.940  1.00 42.88           C  
ANISOU 2781  C   ALA A 370     6309   4901   5081   -287    570    206       C  
ATOM   2782  O   ALA A 370      -8.028  60.297  56.335  1.00 46.83           O  
ANISOU 2782  O   ALA A 370     6797   5445   5552   -258    661    219       O  
ATOM   2783  CB  ALA A 370      -6.977  57.212  56.175  1.00 35.58           C  
ANISOU 2783  CB  ALA A 370     5382   3959   4179   -392    471    279       C  
ATOM   2784  N   ALA A 371      -5.784  60.196  56.122  1.00 41.30           N  
ANISOU 2784  N   ALA A 371     6175   4659   4859   -285    530    165       N  
ATOM   2785  CA  ALA A 371      -5.572  61.453  56.825  1.00 37.07           C  
ANISOU 2785  CA  ALA A 371     5719   4111   4254   -267    588    127       C  
ATOM   2786  C   ALA A 371      -5.787  62.674  55.934  1.00 49.27           C  
ANISOU 2786  C   ALA A 371     7252   5644   5826   -202    639     89       C  
ATOM   2787  O   ALA A 371      -5.965  63.779  56.451  1.00 57.44           O  
ANISOU 2787  O   ALA A 371     8363   6661   6802   -173    717     61       O  
ATOM   2788  CB  ALA A 371      -4.166  61.476  57.420  1.00 34.15           C  
ANISOU 2788  CB  ALA A 371     5424   3717   3835   -315    518    105       C  
ATOM   2789  N   ASP A 372      -5.784  62.514  54.613  1.00 54.89           N  
ANISOU 2789  N   ASP A 372     7881   6357   6617   -175    603     88       N  
ATOM   2790  CA  ASP A 372      -6.033  63.632  53.703  1.00 49.58           C  
ANISOU 2790  CA  ASP A 372     7191   5676   5971   -109    651     62       C  
ATOM   2791  C   ASP A 372      -6.903  63.125  52.567  1.00 52.80           C  
ANISOU 2791  C   ASP A 372     7476   6130   6453    -81    648     98       C  
ATOM   2792  O   ASP A 372      -6.405  62.714  51.514  1.00 48.04           O  
ANISOU 2792  O   ASP A 372     6824   5519   5910    -91    577     89       O  
ATOM   2793  CB  ASP A 372      -4.728  64.232  53.180  1.00 44.83           C  
ANISOU 2793  CB  ASP A 372     6633   5027   5373   -120    594     13       C  
ATOM   2794  CG  ASP A 372      -4.925  65.602  52.556  1.00 54.54           C  
ANISOU 2794  CG  ASP A 372     7891   6229   6603    -57    660    -18       C  
ATOM   2795  OD1 ASP A 372      -3.916  66.246  52.192  1.00 59.72           O  
ANISOU 2795  OD1 ASP A 372     8595   6846   7249    -76    625    -59       O  
ATOM   2796  OD2 ASP A 372      -6.088  66.042  52.435  1.00 59.24           O  
ANISOU 2796  OD2 ASP A 372     8460   6847   7204     13    749      5       O  
ATOM   2797  N   PRO A 373      -8.222  63.145  52.747  1.00 57.79           N  
ANISOU 2797  N   PRO A 373     8055   6824   7078    -49    724    142       N  
ATOM   2798  CA  PRO A 373      -9.103  62.497  51.763  1.00 59.06           C  
ANISOU 2798  CA  PRO A 373     8090   7053   7296    -51    711    186       C  
ATOM   2799  C   PRO A 373      -9.051  63.124  50.380  1.00 57.93           C  
ANISOU 2799  C   PRO A 373     7890   6913   7206      2    703    172       C  
ATOM   2800  O   PRO A 373      -9.348  62.434  49.395  1.00 58.93           O  
ANISOU 2800  O   PRO A 373     7929   7079   7384    -27    655    194       O  
ATOM   2801  CB  PRO A 373     -10.493  62.640  52.397  1.00 63.58           C  
ANISOU 2801  CB  PRO A 373     8617   7712   7829    -20    809    243       C  
ATOM   2802  CG  PRO A 373     -10.361  63.839  53.328  1.00 59.43           C  
ANISOU 2802  CG  PRO A 373     8199   7144   7238     47    898    213       C  
ATOM   2803  CD  PRO A 373      -8.965  63.751  53.865  1.00 54.52           C  
ANISOU 2803  CD  PRO A 373     7692   6431   6594    -12    829    156       C  
ATOM   2804  N   LYS A 374      -8.665  64.391  50.259  1.00 52.57           N  
ANISOU 2804  N   LYS A 374     7271   6191   6514     69    747    135       N  
ATOM   2805  CA  LYS A 374      -8.645  65.013  48.943  1.00 53.09           C  
ANISOU 2805  CA  LYS A 374     7285   6260   6628    122    743    127       C  
ATOM   2806  C   LYS A 374      -7.459  64.571  48.093  1.00 46.97           C  
ANISOU 2806  C   LYS A 374     6511   5438   5899     72    637     86       C  
ATOM   2807  O   LYS A 374      -7.434  64.877  46.896  1.00 51.15           O  
ANISOU 2807  O   LYS A 374     6986   5977   6473    102    620     83       O  
ATOM   2808  CB  LYS A 374      -8.655  66.546  49.074  1.00 57.22           C  
ANISOU 2808  CB  LYS A 374     7889   6739   7114    213    833    104       C  
ATOM   2809  CG  LYS A 374      -7.545  67.116  49.924  1.00 56.22           C  
ANISOU 2809  CG  LYS A 374     7912   6518   6932    181    829     44       C  
ATOM   2810  CD  LYS A 374      -7.645  68.623  50.038  1.00 56.49           C  
ANISOU 2810  CD  LYS A 374     8050   6495   6920    262    928     21       C  
ATOM   2811  CE  LYS A 374      -6.499  69.180  50.896  1.00 60.81           C  
ANISOU 2811  CE  LYS A 374     8758   6951   7396    199    916    -42       C  
ATOM   2812  NZ  LYS A 374      -5.153  68.720  50.433  1.00 58.53           N  
ANISOU 2812  NZ  LYS A 374     8458   6645   7134    108    793    -77       N  
ATOM   2813  N   LEU A 375      -6.484  63.866  48.675  1.00 46.64           N  
ANISOU 2813  N   LEU A 375     6525   5352   5843      5    569     63       N  
ATOM   2814  CA  LEU A 375      -5.332  63.406  47.903  1.00 41.41           C  
ANISOU 2814  CA  LEU A 375     5858   4657   5220    -27    476     33       C  
ATOM   2815  C   LEU A 375      -5.765  62.525  46.739  1.00 42.91           C  
ANISOU 2815  C   LEU A 375     5953   4880   5469    -41    432     55       C  
ATOM   2816  O   LEU A 375      -5.204  62.617  45.641  1.00 40.74           O  
ANISOU 2816  O   LEU A 375     5652   4594   5234    -30    389     33       O  
ATOM   2817  CB  LEU A 375      -4.358  62.646  48.802  1.00 33.62           C  
ANISOU 2817  CB  LEU A 375     4933   3638   4202    -83    417     25       C  
ATOM   2818  CG  LEU A 375      -3.537  63.499  49.767  1.00 53.09           C  
ANISOU 2818  CG  LEU A 375     7497   6073   6602    -95    430     -6       C  
ATOM   2819  CD1 LEU A 375      -2.316  62.732  50.265  1.00 56.84           C  
ANISOU 2819  CD1 LEU A 375     8003   6538   7056   -145    348     -7       C  
ATOM   2820  CD2 LEU A 375      -3.120  64.815  49.121  1.00 42.20           C  
ANISOU 2820  CD2 LEU A 375     6145   4669   5221    -62    453    -45       C  
ATOM   2821  N   ALA A 376      -6.765  61.667  46.962  1.00 37.17           N  
ANISOU 2821  N   ALA A 376     5181   4200   4742    -75    444    100       N  
ATOM   2822  CA  ALA A 376      -7.146  60.693  45.947  1.00 40.15           C  
ANISOU 2822  CA  ALA A 376     5490   4605   5160   -118    397    119       C  
ATOM   2823  C   ALA A 376      -7.562  61.380  44.649  1.00 44.36           C  
ANISOU 2823  C   ALA A 376     5944   5182   5729    -76    410    120       C  
ATOM   2824  O   ALA A 376      -7.140  60.973  43.555  1.00 31.07           O  
ANISOU 2824  O   ALA A 376     4238   3486   4082    -94    354    102       O  
ATOM   2825  CB  ALA A 376      -8.271  59.804  46.474  1.00 24.13           C  
ANISOU 2825  CB  ALA A 376     3428   2631   3111   -179    417    172       C  
ATOM   2826  N   LYS A 377      -8.387  62.426  44.755  1.00 45.05           N  
ANISOU 2826  N   LYS A 377     5995   5322   5801    -12    489    144       N  
ATOM   2827  CA  LYS A 377      -8.754  63.202  43.579  1.00 46.55           C  
ANISOU 2827  CA  LYS A 377     6113   5555   6017     44    508    154       C  
ATOM   2828  C   LYS A 377      -7.514  63.808  42.936  1.00 49.88           C  
ANISOU 2828  C   LYS A 377     6587   5903   6463     72    470     97       C  
ATOM   2829  O   LYS A 377      -7.312  63.695  41.721  1.00 46.76           O  
ANISOU 2829  O   LYS A 377     6144   5519   6105     66    427     88       O  
ATOM   2830  CB  LYS A 377      -9.762  64.286  43.963  1.00 50.27           C  
ANISOU 2830  CB  LYS A 377     6555   6084   6459    133    612    196       C  
ATOM   2831  CG  LYS A 377     -10.527  64.859  42.790  1.00 63.09           C  
ANISOU 2831  CG  LYS A 377     8075   7791   8105    191    638    237       C  
ATOM   2832  CD  LYS A 377     -11.254  66.147  43.162  1.00 67.44           C  
ANISOU 2832  CD  LYS A 377     8627   8373   8625    316    752    274       C  
ATOM   2833  CE  LYS A 377     -10.283  67.316  43.348  1.00 67.27           C  
ANISOU 2833  CE  LYS A 377     8737   8231   8592    379    783    215       C  
ATOM   2834  NZ  LYS A 377     -10.234  68.246  42.180  1.00 55.75           N  
ANISOU 2834  NZ  LYS A 377     7254   6771   7157    454    797    220       N  
ATOM   2835  N   LEU A 378      -6.649  64.421  43.753  1.00 46.31           N  
ANISOU 2835  N   LEU A 378     6233   5379   5982     89    483     58       N  
ATOM   2836  CA  LEU A 378      -5.433  65.043  43.236  1.00 39.62           C  
ANISOU 2836  CA  LEU A 378     5435   4475   5145    100    448      9       C  
ATOM   2837  C   LEU A 378      -4.533  64.023  42.555  1.00 36.75           C  
ANISOU 2837  C   LEU A 378     5053   4095   4815     49    354    -12       C  
ATOM   2838  O   LEU A 378      -4.017  64.261  41.459  1.00 38.74           O  
ANISOU 2838  O   LEU A 378     5279   4343   5097     61    322    -32       O  
ATOM   2839  CB  LEU A 378      -4.680  65.730  44.370  1.00 35.61           C  
ANISOU 2839  CB  LEU A 378     5040   3907   4584     97    471    -23       C  
ATOM   2840  CG  LEU A 378      -5.454  66.827  45.077  1.00 50.01           C  
ANISOU 2840  CG  LEU A 378     6916   5724   6363    156    576    -11       C  
ATOM   2841  CD1 LEU A 378      -4.783  67.127  46.404  1.00 65.56           C  
ANISOU 2841  CD1 LEU A 378     9006   7639   8266    120    589    -41       C  
ATOM   2842  CD2 LEU A 378      -5.512  68.058  44.190  1.00 45.85           C  
ANISOU 2842  CD2 LEU A 378     6398   5179   5845    224    619    -18       C  
ATOM   2843  N   TYR A 379      -4.304  62.893  43.215  1.00 40.26           N  
ANISOU 2843  N   TYR A 379     5520   4527   5251     -2    316     -6       N  
ATOM   2844  CA  TYR A 379      -3.451  61.862  42.644  1.00 41.20           C  
ANISOU 2844  CA  TYR A 379     5638   4621   5395    -33    239    -21       C  
ATOM   2845  C   TYR A 379      -4.002  61.382  41.302  1.00 42.28           C  
ANISOU 2845  C   TYR A 379     5706   4788   5572    -43    218    -13       C  
ATOM   2846  O   TYR A 379      -3.239  61.158  40.352  1.00 35.12           O  
ANISOU 2846  O   TYR A 379     4792   3862   4689    -38    172    -38       O  
ATOM   2847  CB  TYR A 379      -3.328  60.713  43.649  1.00 38.40           C  
ANISOU 2847  CB  TYR A 379     5329   4243   5017    -76    215     -4       C  
ATOM   2848  CG  TYR A 379      -2.101  59.857  43.472  1.00 43.81           C  
ANISOU 2848  CG  TYR A 379     6047   4888   5709    -81    148    -17       C  
ATOM   2849  CD1 TYR A 379      -0.976  60.031  44.282  1.00 42.13           C  
ANISOU 2849  CD1 TYR A 379     5884   4661   5464    -73    125    -25       C  
ATOM   2850  CD2 TYR A 379      -2.065  58.862  42.494  1.00 34.73           C  
ANISOU 2850  CD2 TYR A 379     4885   3721   4591    -93    110    -18       C  
ATOM   2851  CE1 TYR A 379       0.158  59.234  44.114  1.00 43.93           C  
ANISOU 2851  CE1 TYR A 379     6128   4869   5693    -60     68    -23       C  
ATOM   2852  CE2 TYR A 379      -0.940  58.065  42.319  1.00 37.25           C  
ANISOU 2852  CE2 TYR A 379     5241   4000   4911    -75     61    -25       C  
ATOM   2853  CZ  TYR A 379       0.171  58.253  43.122  1.00 43.49           C  
ANISOU 2853  CZ  TYR A 379     6062   4788   5672    -50     41    -23       C  
ATOM   2854  OH  TYR A 379       1.282  57.450  42.926  1.00 39.89           O  
ANISOU 2854  OH  TYR A 379     5631   4311   5216    -16     -3    -17       O  
ATOM   2855  N   ASN A 380      -5.333  61.239  41.209  1.00 39.11           N  
ANISOU 2855  N   ASN A 380     5248   4442   5170    -61    254     25       N  
ATOM   2856  CA  ASN A 380      -5.980  60.821  39.966  1.00 39.93           C  
ANISOU 2856  CA  ASN A 380     5280   4592   5297    -88    234     39       C  
ATOM   2857  C   ASN A 380      -5.668  61.787  38.829  1.00 45.50           C  
ANISOU 2857  C   ASN A 380     5947   5313   6028    -36    233     20       C  
ATOM   2858  O   ASN A 380      -5.594  61.389  37.659  1.00 37.73           O  
ANISOU 2858  O   ASN A 380     4930   4342   5065    -58    194     10       O  
ATOM   2859  CB  ASN A 380      -7.497  60.740  40.165  1.00 37.62           C  
ANISOU 2859  CB  ASN A 380     4916   4389   4987   -116    278     96       C  
ATOM   2860  CG  ASN A 380      -7.973  59.342  40.496  1.00 55.04           C  
ANISOU 2860  CG  ASN A 380     7138   6598   7176   -213    250    118       C  
ATOM   2861  OD1 ASN A 380      -7.313  58.348  40.178  1.00 58.40           O  
ANISOU 2861  OD1 ASN A 380     7622   6958   7609   -259    195     91       O  
ATOM   2862  ND2 ASN A 380      -9.122  59.258  41.164  1.00 63.01           N  
ANISOU 2862  ND2 ASN A 380     8101   7682   8157   -242    294    171       N  
ATOM   2863  N   GLN A 381      -5.509  63.065  39.151  1.00 36.25           N  
ANISOU 2863  N   GLN A 381     4790   4135   4848     29    280     15       N  
ATOM   2864  CA  GLN A 381      -5.210  64.084  38.165  1.00 37.54           C  
ANISOU 2864  CA  GLN A 381     4931   4304   5029     80    287      1       C  
ATOM   2865  C   GLN A 381      -3.727  64.404  38.095  1.00 34.22           C  
ANISOU 2865  C   GLN A 381     4573   3819   4610     86    250    -49       C  
ATOM   2866  O   GLN A 381      -3.361  65.494  37.638  1.00 34.04           O  
ANISOU 2866  O   GLN A 381     4560   3785   4587    126    269    -63       O  
ATOM   2867  CB  GLN A 381      -6.037  65.327  38.463  1.00 35.15           C  
ANISOU 2867  CB  GLN A 381     4615   4031   4708    151    371     33       C  
ATOM   2868  CG  GLN A 381      -7.441  64.945  38.870  1.00 37.63           C  
ANISOU 2868  CG  GLN A 381     4863   4426   5009    146    413     93       C  
ATOM   2869  CD  GLN A 381      -8.406  66.100  38.813  1.00 51.42           C  
ANISOU 2869  CD  GLN A 381     6568   6228   6740    239    500    142       C  
ATOM   2870  OE1 GLN A 381      -8.617  66.795  39.804  1.00 52.66           O  
ANISOU 2870  OE1 GLN A 381     6782   6360   6865    293    572    149       O  
ATOM   2871  NE2 GLN A 381      -9.004  66.309  37.650  1.00 61.10           N  
ANISOU 2871  NE2 GLN A 381     7700   7532   7984    262    497    179       N  
ATOM   2872  N   ASN A 382      -2.878  63.484  38.562  1.00 36.36           N  
ANISOU 2872  N   ASN A 382     4887   4052   4876     48    201    -70       N  
ATOM   2873  CA  ASN A 382      -1.427  63.537  38.372  1.00 42.23           C  
ANISOU 2873  CA  ASN A 382     5665   4762   5618     50    155   -105       C  
ATOM   2874  C   ASN A 382      -0.786  64.713  39.120  1.00 37.06           C  
ANISOU 2874  C   ASN A 382     5067   4086   4928     61    181   -120       C  
ATOM   2875  O   ASN A 382       0.177  65.321  38.651  1.00 41.02           O  
ANISOU 2875  O   ASN A 382     5578   4582   5424     64    159   -143       O  
ATOM   2876  CB  ASN A 382      -1.069  63.561  36.878  1.00 33.38           C  
ANISOU 2876  CB  ASN A 382     4498   3657   4529     62    123   -121       C  
ATOM   2877  CG  ASN A 382      -1.538  62.289  36.147  1.00 42.85           C  
ANISOU 2877  CG  ASN A 382     5667   4866   5749     33     92   -114       C  
ATOM   2878  OD1 ASN A 382      -1.207  61.165  36.546  1.00 42.28           O  
ANISOU 2878  OD1 ASN A 382     5632   4762   5670     10     63   -116       O  
ATOM   2879  ND2 ASN A 382      -2.331  62.468  35.087  1.00 35.56           N  
ANISOU 2879  ND2 ASN A 382     4684   3986   4843     30    100   -103       N  
ATOM   2880  N   HIS A 383      -1.317  65.035  40.291  1.00 34.78           N  
ANISOU 2880  N   HIS A 383     4823   3786   4606     59    228   -108       N  
ATOM   2881  CA  HIS A 383      -0.677  65.967  41.215  1.00 42.40           C  
ANISOU 2881  CA  HIS A 383     5869   4721   5520     48    250   -127       C  
ATOM   2882  C   HIS A 383      -0.486  65.255  42.551  1.00 45.89           C  
ANISOU 2882  C   HIS A 383     6355   5156   5926     11    238   -118       C  
ATOM   2883  O   HIS A 383      -1.439  64.686  43.093  1.00 41.11           O  
ANISOU 2883  O   HIS A 383     5740   4559   5322     13    265    -93       O  
ATOM   2884  CB  HIS A 383      -1.512  67.234  41.380  1.00 31.39           C  
ANISOU 2884  CB  HIS A 383     4512   3309   4105     89    335   -122       C  
ATOM   2885  CG  HIS A 383      -1.580  68.071  40.141  1.00 42.81           C  
ANISOU 2885  CG  HIS A 383     5930   4757   5577    128    350   -126       C  
ATOM   2886  ND1 HIS A 383      -0.481  68.717  39.616  1.00 43.16           N  
ANISOU 2886  ND1 HIS A 383     6005   4782   5611    107    320   -155       N  
ATOM   2887  CD2 HIS A 383      -2.615  68.357  39.314  1.00 43.80           C  
ANISOU 2887  CD2 HIS A 383     5996   4914   5733    185    389    -96       C  
ATOM   2888  CE1 HIS A 383      -0.838  69.374  38.527  1.00 41.15           C  
ANISOU 2888  CE1 HIS A 383     5720   4533   5383    151    342   -148       C  
ATOM   2889  NE2 HIS A 383      -2.128  69.174  38.324  1.00 42.30           N  
ANISOU 2889  NE2 HIS A 383     5808   4710   5552    203    384   -110       N  
ATOM   2890  N   GLY A 384       0.745  65.263  43.064  1.00 38.46           N  
ANISOU 2890  N   GLY A 384     5453   4212   4948    -26    194   -133       N  
ATOM   2891  CA  GLY A 384       1.071  64.601  44.312  1.00 23.85           C  
ANISOU 2891  CA  GLY A 384     3642   2363   3057    -60    174   -119       C  
ATOM   2892  C   GLY A 384       1.671  63.216  44.167  1.00 34.24           C  
ANISOU 2892  C   GLY A 384     4919   3695   4395    -59    108    -98       C  
ATOM   2893  O   GLY A 384       2.009  62.595  45.182  1.00 38.89           O  
ANISOU 2893  O   GLY A 384     5539   4289   4949    -81     87    -78       O  
ATOM   2894  N   ILE A 385       1.807  62.710  42.942  1.00 40.50           N  
ANISOU 2894  N   ILE A 385     5656   4492   5239    -31     78   -101       N  
ATOM   2895  CA  ILE A 385       2.469  61.425  42.730  1.00 39.76           C  
ANISOU 2895  CA  ILE A 385     5548   4400   5161    -15     25    -83       C  
ATOM   2896  C   ILE A 385       3.865  61.450  43.326  1.00 35.34           C  
ANISOU 2896  C   ILE A 385     4998   3875   4554    -22    -20    -72       C  
ATOM   2897  O   ILE A 385       4.235  60.588  44.127  1.00 28.33           O  
ANISOU 2897  O   ILE A 385     4131   2991   3642    -19    -44    -40       O  
ATOM   2898  CB  ILE A 385       2.548  61.092  41.232  1.00 45.88           C  
ANISOU 2898  CB  ILE A 385     6273   5173   5986     17      6    -97       C  
ATOM   2899  CG1 ILE A 385       1.281  61.529  40.495  1.00 52.16           C  
ANISOU 2899  CG1 ILE A 385     7040   5964   6816     14     48   -107       C  
ATOM   2900  CG2 ILE A 385       2.887  59.628  41.038  1.00 37.88           C  
ANISOU 2900  CG2 ILE A 385     5270   4136   4985     41    -28    -78       C  
ATOM   2901  CD1 ILE A 385       0.062  60.904  41.002  1.00 48.90           C  
ANISOU 2901  CD1 ILE A 385     6636   5538   6405     -8     76    -85       C  
ATOM   2902  N   ILE A 386       4.667  62.427  42.895  1.00 36.51           N  
ANISOU 2902  N   ILE A 386     5128   4060   4686    -33    -33    -91       N  
ATOM   2903  CA  ILE A 386       6.071  62.517  43.279  1.00 39.16           C  
ANISOU 2903  CA  ILE A 386     5452   4458   4971    -50    -82    -73       C  
ATOM   2904  C   ILE A 386       6.216  62.781  44.775  1.00 39.95           C  
ANISOU 2904  C   ILE A 386     5606   4574   4999   -107    -81    -58       C  
ATOM   2905  O   ILE A 386       7.047  62.158  45.449  1.00 38.38           O  
ANISOU 2905  O   ILE A 386     5398   4425   4761   -108   -123    -19       O  
ATOM   2906  CB  ILE A 386       6.755  63.609  42.436  1.00 30.37           C  
ANISOU 2906  CB  ILE A 386     4309   3381   3849    -71    -91    -97       C  
ATOM   2907  CG1 ILE A 386       6.562  63.324  40.943  1.00 21.35           C  
ANISOU 2907  CG1 ILE A 386     3114   2225   2774    -16    -90   -112       C  
ATOM   2908  CG2 ILE A 386       8.252  63.716  42.797  1.00 23.91           C  
ANISOU 2908  CG2 ILE A 386     3461   2656   2969   -103   -147    -70       C  
ATOM   2909  CD1 ILE A 386       7.426  64.216  40.044  1.00 28.37           C  
ANISOU 2909  CD1 ILE A 386     3965   3162   3653    -32   -108   -127       C  
ATOM   2910  N   LYS A 387       5.426  63.714  45.311  1.00 32.53           N  
ANISOU 2910  N   LYS A 387     4728   3597   4037   -149    -28    -85       N  
ATOM   2911  CA  LYS A 387       5.509  64.029  46.734  1.00 39.96           C  
ANISOU 2911  CA  LYS A 387     5736   4547   4900   -209    -20    -78       C  
ATOM   2912  C   LYS A 387       5.178  62.814  47.602  1.00 49.29           C  
ANISOU 2912  C   LYS A 387     6925   5724   6081   -190    -29    -39       C  
ATOM   2913  O   LYS A 387       5.867  62.549  48.599  1.00 40.56           O  
ANISOU 2913  O   LYS A 387     5837   4664   4912   -225    -63     -9       O  
ATOM   2914  CB  LYS A 387       4.573  65.190  47.059  1.00 34.37           C  
ANISOU 2914  CB  LYS A 387     5105   3783   4170   -236     55   -115       C  
ATOM   2915  CG  LYS A 387       4.411  65.480  48.524  1.00 47.80           C  
ANISOU 2915  CG  LYS A 387     6893   5477   5791   -293     81   -114       C  
ATOM   2916  CD  LYS A 387       5.457  66.438  49.060  1.00 58.91           C  
ANISOU 2916  CD  LYS A 387     8360   6919   7103   -387     57   -131       C  
ATOM   2917  CE  LYS A 387       4.867  67.208  50.236  1.00 68.14           C  
ANISOU 2917  CE  LYS A 387     9654   8040   8194   -438    123   -155       C  
ATOM   2918  NZ  LYS A 387       3.737  66.443  50.866  1.00 65.74           N  
ANISOU 2918  NZ  LYS A 387     9353   7707   7917   -385    167   -135       N  
ATOM   2919  N   LEU A 388       4.120  62.070  47.252  1.00 43.30           N  
ANISOU 2919  N   LEU A 388     6154   4914   5383   -144      0    -34       N  
ATOM   2920  CA  LEU A 388       3.758  60.891  48.037  1.00 41.83           C  
ANISOU 2920  CA  LEU A 388     5987   4714   5194   -135     -5      4       C  
ATOM   2921  C   LEU A 388       4.879  59.865  48.037  1.00 48.67           C  
ANISOU 2921  C   LEU A 388     6825   5614   6052   -102    -69     47       C  
ATOM   2922  O   LEU A 388       5.175  59.249  49.071  1.00 49.44           O  
ANISOU 2922  O   LEU A 388     6950   5730   6106   -111    -89     88       O  
ATOM   2923  CB  LEU A 388       2.484  60.259  47.488  1.00 41.52           C  
ANISOU 2923  CB  LEU A 388     5936   4625   5217   -109     31      3       C  
ATOM   2924  CG  LEU A 388       2.028  59.020  48.250  1.00 38.90           C  
ANISOU 2924  CG  LEU A 388     5634   4268   4878   -113     29     44       C  
ATOM   2925  CD1 LEU A 388       1.640  59.388  49.675  1.00 36.38           C  
ANISOU 2925  CD1 LEU A 388     5367   3958   4496   -157     61     54       C  
ATOM   2926  CD2 LEU A 388       0.889  58.338  47.500  1.00 42.39           C  
ANISOU 2926  CD2 LEU A 388     6059   4671   5376   -106     54     45       C  
ATOM   2927  N   ARG A 389       5.503  59.655  46.875  1.00 45.16           N  
ANISOU 2927  N   ARG A 389     6328   5183   5648    -54    -98     43       N  
ATOM   2928  CA  ARG A 389       6.630  58.739  46.802  1.00 42.61           C  
ANISOU 2928  CA  ARG A 389     5976   4900   5314      0   -149     90       C  
ATOM   2929  C   ARG A 389       7.789  59.229  47.663  1.00 46.21           C  
ANISOU 2929  C   ARG A 389     6415   5453   5690    -37   -190    121       C  
ATOM   2930  O   ARG A 389       8.382  58.447  48.423  1.00 43.69           O  
ANISOU 2930  O   ARG A 389     6097   5173   5331    -12   -221    180       O  
ATOM   2931  CB  ARG A 389       7.066  58.564  45.345  1.00 38.16           C  
ANISOU 2931  CB  ARG A 389     5361   4337   4801     60   -161     75       C  
ATOM   2932  CG  ARG A 389       8.454  57.960  45.172  1.00 48.49           C  
ANISOU 2932  CG  ARG A 389     6624   5715   6087    127   -207    125       C  
ATOM   2933  CD  ARG A 389       9.266  58.727  44.148  1.00 56.65           C  
ANISOU 2933  CD  ARG A 389     7587   6814   7125    135   -225    106       C  
ATOM   2934  NE  ARG A 389       8.505  58.868  42.915  1.00 64.55           N  
ANISOU 2934  NE  ARG A 389     8588   7748   8192    147   -195     53       N  
ATOM   2935  CZ  ARG A 389       8.874  59.616  41.885  1.00 63.60           C  
ANISOU 2935  CZ  ARG A 389     8418   7661   8087    145   -198     25       C  
ATOM   2936  NH1 ARG A 389      10.014  60.305  41.936  1.00 57.18           N  
ANISOU 2936  NH1 ARG A 389     7550   6950   7226    123   -231     42       N  
ATOM   2937  NH2 ARG A 389       8.094  59.667  40.810  1.00 59.56           N  
ANISOU 2937  NH2 ARG A 389     7909   7090   7632    156   -171    -17       N  
ATOM   2938  N   ASN A 390       8.111  60.523  47.571  1.00 35.24           N  
ANISOU 2938  N   ASN A 390     5014   4107   4268   -102   -191     88       N  
ATOM   2939  CA  ASN A 390       9.240  61.055  48.324  1.00 40.56           C  
ANISOU 2939  CA  ASN A 390     5672   4887   4853   -164   -235    116       C  
ATOM   2940  C   ASN A 390       8.962  61.080  49.818  1.00 38.50           C  
ANISOU 2940  C   ASN A 390     5477   4630   4522   -227   -230    133       C  
ATOM   2941  O   ASN A 390       9.886  60.890  50.614  1.00 42.39           O  
ANISOU 2941  O   ASN A 390     5949   5218   4940   -255   -278    186       O  
ATOM   2942  CB  ASN A 390       9.607  62.457  47.833  1.00 38.42           C  
ANISOU 2942  CB  ASN A 390     5396   4648   4555   -238   -234     72       C  
ATOM   2943  CG  ASN A 390      10.427  62.427  46.566  1.00 47.45           C  
ANISOU 2943  CG  ASN A 390     6452   5844   5732   -190   -263     78       C  
ATOM   2944  OD1 ASN A 390      10.149  63.166  45.615  1.00 56.21           O  
ANISOU 2944  OD1 ASN A 390     7561   6919   6879   -199   -239     31       O  
ATOM   2945  ND2 ASN A 390      11.437  61.556  46.533  1.00 42.85           N  
ANISOU 2945  ND2 ASN A 390     5797   5350   5135   -130   -311    142       N  
ATOM   2946  N   ASP A 391       7.708  61.306  50.221  1.00 35.83           N  
ANISOU 2946  N   ASP A 391     5211   4202   4200   -248   -170     96       N  
ATOM   2947  CA  ASP A 391       7.372  61.227  51.643  1.00 38.46           C  
ANISOU 2947  CA  ASP A 391     5611   4535   4467   -300   -158    113       C  
ATOM   2948  C   ASP A 391       7.615  59.823  52.197  1.00 40.35           C  
ANISOU 2948  C   ASP A 391     5833   4792   4704   -246   -192    183       C  
ATOM   2949  O   ASP A 391       8.193  59.670  53.281  1.00 38.85           O  
ANISOU 2949  O   ASP A 391     5656   4670   4435   -285   -225    228       O  
ATOM   2950  CB  ASP A 391       5.919  61.630  51.869  1.00 30.33           C  
ANISOU 2950  CB  ASP A 391     4650   3413   3462   -312    -79     67       C  
ATOM   2951  CG  ASP A 391       5.706  63.108  51.741  1.00 41.64           C  
ANISOU 2951  CG  ASP A 391     6133   4825   4864   -369    -36      8       C  
ATOM   2952  OD1 ASP A 391       4.551  63.529  51.524  1.00 55.13           O  
ANISOU 2952  OD1 ASP A 391     7875   6463   6608   -347     35    -26       O  
ATOM   2953  OD2 ASP A 391       6.692  63.854  51.853  1.00 49.81           O  
ANISOU 2953  OD2 ASP A 391     7175   5917   5834   -435    -70      1       O  
ATOM   2954  N   PHE A 392       7.170  58.788  51.468  1.00 37.34           N  
ANISOU 2954  N   PHE A 392     5434   4349   4403   -160   -182    196       N  
ATOM   2955  CA  PHE A 392       7.386  57.414  51.910  1.00 40.00           C  
ANISOU 2955  CA  PHE A 392     5778   4680   4739   -100   -206    263       C  
ATOM   2956  C   PHE A 392       8.870  57.110  52.037  1.00 46.24           C  
ANISOU 2956  C   PHE A 392     6508   5581   5480    -61   -270    329       C  
ATOM   2957  O   PHE A 392       9.311  56.529  53.038  1.00 61.07           O  
ANISOU 2957  O   PHE A 392     8397   7508   7300    -56   -298    395       O  
ATOM   2958  CB  PHE A 392       6.724  56.418  50.952  1.00 37.50           C  
ANISOU 2958  CB  PHE A 392     5470   4268   4509    -25   -182    258       C  
ATOM   2959  CG  PHE A 392       7.098  54.967  51.224  1.00 34.57           C  
ANISOU 2959  CG  PHE A 392     5125   3876   4135     51   -203    329       C  
ATOM   2960  CD1 PHE A 392       6.717  54.342  52.413  1.00 26.70           C  
ANISOU 2960  CD1 PHE A 392     4188   2858   3098     29   -197    373       C  
ATOM   2961  CD2 PHE A 392       7.836  54.237  50.300  1.00 34.50           C  
ANISOU 2961  CD2 PHE A 392     5089   3862   4158    150   -222    355       C  
ATOM   2962  CE1 PHE A 392       7.064  53.003  52.672  1.00 30.91           C  
ANISOU 2962  CE1 PHE A 392     4760   3360   3624    106   -212    444       C  
ATOM   2963  CE2 PHE A 392       8.193  52.898  50.548  1.00 35.65           C  
ANISOU 2963  CE2 PHE A 392     5278   3973   4295    236   -231    424       C  
ATOM   2964  CZ  PHE A 392       7.801  52.277  51.734  1.00 33.78           C  
ANISOU 2964  CZ  PHE A 392     5108   3709   4020    214   -226    470       C  
ATOM   2965  N   LEU A 393       9.661  57.504  51.032  1.00 38.94           N  
ANISOU 2965  N   LEU A 393     5512   4709   4573    -33   -293    319       N  
ATOM   2966  CA  LEU A 393      11.101  57.263  51.096  1.00 41.67           C  
ANISOU 2966  CA  LEU A 393     5780   5186   4866      8   -352    391       C  
ATOM   2967  C   LEU A 393      11.726  57.981  52.290  1.00 45.40           C  
ANISOU 2967  C   LEU A 393     6243   5777   5228    -98   -391    419       C  
ATOM   2968  O   LEU A 393      12.617  57.434  52.951  1.00 49.46           O  
ANISOU 2968  O   LEU A 393     6715   6398   5680    -71   -438    505       O  
ATOM   2969  CB  LEU A 393      11.764  57.685  49.790  1.00 41.32           C  
ANISOU 2969  CB  LEU A 393     5658   5186   4856     43   -364    370       C  
ATOM   2970  CG  LEU A 393      11.461  56.800  48.575  1.00 52.65           C  
ANISOU 2970  CG  LEU A 393     7094   6528   6381    161   -336    359       C  
ATOM   2971  CD1 LEU A 393      11.922  57.476  47.287  1.00 53.34           C  
ANISOU 2971  CD1 LEU A 393     7114   6653   6499    170   -339    321       C  
ATOM   2972  CD2 LEU A 393      12.092  55.413  48.707  1.00 49.80           C  
ANISOU 2972  CD2 LEU A 393     6728   6181   6014    290   -350    444       C  
ATOM   2973  N   GLU A 394      11.254  59.197  52.592  1.00 46.74           N  
ANISOU 2973  N   GLU A 394     6462   5931   5368   -220   -370    351       N  
ATOM   2974  CA  GLU A 394      11.651  59.874  53.824  1.00 49.80           C  
ANISOU 2974  CA  GLU A 394     6877   6405   5640   -341   -397    366       C  
ATOM   2975  C   GLU A 394      11.309  59.034  55.044  1.00 49.03           C  
ANISOU 2975  C   GLU A 394     6828   6295   5506   -331   -397    417       C  
ATOM   2976  O   GLU A 394      12.176  58.753  55.876  1.00 45.68           O  
ANISOU 2976  O   GLU A 394     6369   5992   4995   -352   -451    492       O  
ATOM   2977  CB  GLU A 394      10.970  61.233  53.927  1.00 55.60           C  
ANISOU 2977  CB  GLU A 394     7695   7078   6353   -456   -351    275       C  
ATOM   2978  CG  GLU A 394      11.559  62.267  53.014  1.00 79.19           C  
ANISOU 2978  CG  GLU A 394    10647  10106   9337   -505   -363    236       C  
ATOM   2979  CD  GLU A 394      11.589  63.636  53.640  1.00 94.57           C  
ANISOU 2979  CD  GLU A 394    12682  12064  11188   -659   -351    185       C  
ATOM   2980  OE1 GLU A 394      11.387  63.726  54.872  1.00 92.63           O  
ANISOU 2980  OE1 GLU A 394    12510  11824  10861   -731   -346    191       O  
ATOM   2981  OE2 GLU A 394      11.812  64.618  52.895  1.00100.57           O  
ANISOU 2981  OE2 GLU A 394    13448  12818  11946   -710   -343    139       O  
ATOM   2982  N   TYR A 395      10.038  58.629  55.167  1.00 45.49           N  
ANISOU 2982  N   TYR A 395     6455   5713   5117   -303   -338    382       N  
ATOM   2983  CA  TYR A 395       9.622  57.797  56.291  1.00 51.94           C  
ANISOU 2983  CA  TYR A 395     7324   6508   5901   -296   -332    431       C  
ATOM   2984  C   TYR A 395      10.520  56.574  56.433  1.00 55.10           C  
ANISOU 2984  C   TYR A 395     7669   6976   6289   -198   -384    535       C  
ATOM   2985  O   TYR A 395      10.916  56.211  57.544  1.00 59.43           O  
ANISOU 2985  O   TYR A 395     8226   7596   6757   -219   -416    602       O  
ATOM   2986  CB  TYR A 395       8.158  57.388  56.113  1.00 50.16           C  
ANISOU 2986  CB  TYR A 395     7165   6137   5754   -267   -262    388       C  
ATOM   2987  CG  TYR A 395       7.685  56.231  56.977  1.00 48.45           C  
ANISOU 2987  CG  TYR A 395     6999   5881   5529   -237   -254    445       C  
ATOM   2988  CD1 TYR A 395       7.213  55.061  56.399  1.00 46.86           C  
ANISOU 2988  CD1 TYR A 395     6810   5590   5404   -149   -237    468       C  
ATOM   2989  CD2 TYR A 395       7.677  56.321  58.364  1.00 53.57           C  
ANISOU 2989  CD2 TYR A 395     7693   6575   6084   -307   -261    475       C  
ATOM   2990  CE1 TYR A 395       6.757  54.001  57.177  1.00 52.57           C  
ANISOU 2990  CE1 TYR A 395     7592   6266   6115   -131   -228    522       C  
ATOM   2991  CE2 TYR A 395       7.221  55.266  59.153  1.00 52.14           C  
ANISOU 2991  CE2 TYR A 395     7562   6356   5894   -283   -252    531       C  
ATOM   2992  CZ  TYR A 395       6.762  54.109  58.555  1.00 57.01           C  
ANISOU 2992  CZ  TYR A 395     8192   6879   6590   -196   -235    555       C  
ATOM   2993  OH  TYR A 395       6.309  53.057  59.330  1.00 64.54           O  
ANISOU 2993  OH  TYR A 395     9207   7787   7528   -181   -225    613       O  
ATOM   2994  N   LYS A 396      10.882  55.948  55.315  1.00 55.29           N  
ANISOU 2994  N   LYS A 396     7641   6982   6386    -84   -389    552       N  
ATOM   2995  CA  LYS A 396      11.769  54.793  55.334  1.00 50.39           C  
ANISOU 2995  CA  LYS A 396     6975   6417   5755     36   -426    655       C  
ATOM   2996  C   LYS A 396      13.241  55.161  55.471  1.00 47.22           C  
ANISOU 2996  C   LYS A 396     6464   6208   5271     32   -493    723       C  
ATOM   2997  O   LYS A 396      14.079  54.253  55.537  1.00 41.02           O  
ANISOU 2997  O   LYS A 396     5626   5496   4465    146   -522    824       O  
ATOM   2998  CB  LYS A 396      11.590  53.961  54.063  1.00 45.27           C  
ANISOU 2998  CB  LYS A 396     6329   5667   5205    165   -396    646       C  
ATOM   2999  CG  LYS A 396      10.225  53.308  53.918  1.00 48.76           C  
ANISOU 2999  CG  LYS A 396     6874   5934   5717    173   -338    602       C  
ATOM   3000  CD  LYS A 396       9.765  52.602  55.174  1.00 47.33           C  
ANISOU 3000  CD  LYS A 396     6769   5720   5493    155   -332    653       C  
ATOM   3001  CE  LYS A 396      10.577  51.363  55.481  1.00 54.33           C  
ANISOU 3001  CE  LYS A 396     7661   6630   6352    279   -356    763       C  
ATOM   3002  NZ  LYS A 396      10.553  51.125  56.976  1.00 69.31           N  
ANISOU 3002  NZ  LYS A 396     9595   8573   8168    231   -375    827       N  
ATOM   3003  N   ASN A 397      13.581  56.448  55.488  1.00 43.62           N  
ANISOU 3003  N   ASN A 397     5972   5838   4764    -93   -515    677       N  
ATOM   3004  CA  ASN A 397      14.974  56.870  55.559  1.00 50.92           C  
ANISOU 3004  CA  ASN A 397     6783   6963   5601   -124   -583    743       C  
ATOM   3005  C   ASN A 397      15.824  56.204  54.471  1.00 53.09           C  
ANISOU 3005  C   ASN A 397     6955   7294   5923     30   -596    801       C  
ATOM   3006  O   ASN A 397      16.961  55.787  54.708  1.00 55.84           O  
ANISOU 3006  O   ASN A 397     7203   7807   6207     90   -646    910       O  
ATOM   3007  CB  ASN A 397      15.532  56.583  56.952  1.00 55.00           C  
ANISOU 3007  CB  ASN A 397     7287   7610   6003   -166   -633    837       C  
ATOM   3008  CG  ASN A 397      16.596  57.563  57.372  1.00 69.12           C  
ANISOU 3008  CG  ASN A 397     8995   9601   7667   -305   -700    866       C  
ATOM   3009  OD1 ASN A 397      17.488  57.897  56.595  1.00 63.93           O  
ANISOU 3009  OD1 ASN A 397     8231   9058   7002   -294   -732    888       O  
ATOM   3010  ND2 ASN A 397      16.517  58.023  58.621  1.00 82.94           N  
ANISOU 3010  ND2 ASN A 397    10799  11403   9311   -446   -723    869       N  
ATOM   3011  N   MET A 398      15.273  56.085  53.264  1.00 53.70           N  
ANISOU 3011  N   MET A 398     7056   7242   6108    100   -548    733       N  
ATOM   3012  CA  MET A 398      16.016  55.518  52.146  1.00 52.90           C  
ANISOU 3012  CA  MET A 398     6872   7179   6050    244   -549    775       C  
ATOM   3013  C   MET A 398      16.059  56.484  50.976  1.00 56.22           C  
ANISOU 3013  C   MET A 398     7253   7598   6512    195   -540    694       C  
ATOM   3014  O   MET A 398      15.163  57.308  50.797  1.00 51.97           O  
ANISOU 3014  O   MET A 398     6782   6959   6007     93   -510    595       O  
ATOM   3015  CB  MET A 398      15.422  54.215  51.611  1.00 40.60           C  
ANISOU 3015  CB  MET A 398     5388   5459   4580    400   -498    780       C  
ATOM   3016  CG  MET A 398      14.781  53.284  52.598  1.00 46.83           C  
ANISOU 3016  CG  MET A 398     6276   6155   5361    427   -481    817       C  
ATOM   3017  SD  MET A 398      14.600  51.643  51.853  1.00 60.87           S  
ANISOU 3017  SD  MET A 398     8129   7784   7213    630   -430    855       S  
ATOM   3018  CE  MET A 398      15.840  50.698  52.737  1.00 71.67           C  
ANISOU 3018  CE  MET A 398     9444   9294   8493    766   -467   1021       C  
ATOM   3019  N   LYS A 399      17.113  56.358  50.178  1.00 64.75           N  
ANISOU 3019  N   LYS A 399     8222   8796   7586    279   -561    746       N  
ATOM   3020  CA  LYS A 399      17.109  56.900  48.832  1.00 65.51           C  
ANISOU 3020  CA  LYS A 399     8287   8863   7742    285   -540    679       C  
ATOM   3021  C   LYS A 399      16.344  55.941  47.932  1.00 61.08           C  
ANISOU 3021  C   LYS A 399     7799   8123   7286    420   -480    641       C  
ATOM   3022  O   LYS A 399      16.306  54.728  48.180  1.00 60.55           O  
ANISOU 3022  O   LYS A 399     7773   8002   7232    545   -463    698       O  
ATOM   3023  CB  LYS A 399      18.536  57.090  48.305  1.00 68.19           C  
ANISOU 3023  CB  LYS A 399     8475   9408   8029    325   -582    753       C  
ATOM   3024  CG  LYS A 399      19.512  57.764  49.273  1.00 72.81           C  
ANISOU 3024  CG  LYS A 399     8968  10211   8485    202   -652    824       C  
ATOM   3025  CD  LYS A 399      19.111  59.211  49.584  1.00 77.18           C  
ANISOU 3025  CD  LYS A 399     9574  10750   8999    -20   -665    734       C  
ATOM   3026  CE  LYS A 399      20.117  59.908  50.520  1.00 84.28           C  
ANISOU 3026  CE  LYS A 399    10397  11871   9756   -171   -739    801       C  
ATOM   3027  NZ  LYS A 399      20.139  59.379  51.924  1.00 87.97           N  
ANISOU 3027  NZ  LYS A 399    10887  12387  10150   -185   -768    870       N  
ATOM   3028  N   GLY A 400      15.721  56.493  46.882  1.00 49.76           N  
ANISOU 3028  N   GLY A 400     6390   6594   5922    388   -448    547       N  
ATOM   3029  CA  GLY A 400      14.951  55.654  45.974  1.00 39.85           C  
ANISOU 3029  CA  GLY A 400     5209   5176   4758    489   -395    505       C  
ATOM   3030  C   GLY A 400      15.764  54.522  45.371  1.00 48.07           C  
ANISOU 3030  C   GLY A 400     6217   6242   5804    669   -385    576       C  
ATOM   3031  O   GLY A 400      15.232  53.442  45.097  1.00 45.37           O  
ANISOU 3031  O   GLY A 400     5969   5761   5507    765   -344    573       O  
ATOM   3032  N   THR A 401      17.065  54.745  45.171  1.00 60.30           N  
ANISOU 3032  N   THR A 401     7640   7970   7299    715   -418    644       N  
ATOM   3033  CA  THR A 401      17.930  53.714  44.607  1.00 56.69           C  
ANISOU 3033  CA  THR A 401     7144   7556   6838    907   -400    723       C  
ATOM   3034  C   THR A 401      18.009  52.494  45.514  1.00 56.22           C  
ANISOU 3034  C   THR A 401     7145   7463   6752   1020   -390    810       C  
ATOM   3035  O   THR A 401      17.816  51.358  45.065  1.00 57.77           O  
ANISOU 3035  O   THR A 401     7431   7533   6985   1165   -340    822       O  
ATOM   3036  CB  THR A 401      19.322  54.293  44.360  1.00 56.16           C  
ANISOU 3036  CB  THR A 401     6907   7725   6705    920   -441    793       C  
ATOM   3037  OG1 THR A 401      19.298  55.046  43.145  1.00 56.24           O  
ANISOU 3037  OG1 THR A 401     6881   7732   6755    878   -429    718       O  
ATOM   3038  CG2 THR A 401      20.365  53.188  44.244  1.00 61.61           C  
ANISOU 3038  CG2 THR A 401     7540   8509   7362   1133   -426    914       C  
ATOM   3039  N   ASP A 402      18.307  52.707  46.795  1.00 63.66           N  
ANISOU 3039  N   ASP A 402     8049   8514   7623    954   -437    874       N  
ATOM   3040  CA  ASP A 402      18.466  51.572  47.696  1.00 73.25           C  
ANISOU 3040  CA  ASP A 402     9314   9714   8805   1066   -431    971       C  
ATOM   3041  C   ASP A 402      17.148  50.852  47.918  1.00 64.90           C  
ANISOU 3041  C   ASP A 402     8434   8420   7807   1057   -386    911       C  
ATOM   3042  O   ASP A 402      17.132  49.622  48.038  1.00 61.91           O  
ANISOU 3042  O   ASP A 402     8142   7947   7432   1197   -350    968       O  
ATOM   3043  CB  ASP A 402      19.058  52.024  49.028  1.00 79.86           C  
ANISOU 3043  CB  ASP A 402    10066  10733   9543    978   -497   1052       C  
ATOM   3044  CG  ASP A 402      20.225  52.965  48.852  1.00 90.12           C  
ANISOU 3044  CG  ASP A 402    11191  12278  10774    923   -551   1096       C  
ATOM   3045  OD1 ASP A 402      20.166  54.084  49.410  1.00 98.08           O  
ANISOU 3045  OD1 ASP A 402    12166  13366  11733    730   -598   1058       O  
ATOM   3046  OD2 ASP A 402      21.193  52.585  48.153  1.00 88.61           O  
ANISOU 3046  OD2 ASP A 402    10900  12198  10569   1069   -544   1168       O  
ATOM   3047  N   ALA A 403      16.039  51.594  47.969  1.00 56.29           N  
ANISOU 3047  N   ALA A 403     7400   7230   6756    894   -382    803       N  
ATOM   3048  CA  ALA A 403      14.732  50.954  48.056  1.00 42.74           C  
ANISOU 3048  CA  ALA A 403     5838   5306   5096    873   -338    746       C  
ATOM   3049  C   ALA A 403      14.494  50.044  46.857  1.00 45.76           C  
ANISOU 3049  C   ALA A 403     6302   5545   5539    993   -283    719       C  
ATOM   3050  O   ALA A 403      13.955  48.936  46.998  1.00 42.07           O  
ANISOU 3050  O   ALA A 403     5967   4930   5088   1053   -246    732       O  
ATOM   3051  CB  ALA A 403      13.639  52.016  48.169  1.00 29.88           C  
ANISOU 3051  CB  ALA A 403     4232   3624   3496    692   -337    641       C  
ATOM   3052  N   ALA A 404      14.909  50.484  45.669  1.00 50.74           N  
ANISOU 3052  N   ALA A 404     6865   6215   6197   1023   -276    680       N  
ATOM   3053  CA  ALA A 404      14.777  49.640  44.492  1.00 52.83           C  
ANISOU 3053  CA  ALA A 404     7212   6353   6508   1138   -223    653       C  
ATOM   3054  C   ALA A 404      15.684  48.417  44.558  1.00 51.08           C  
ANISOU 3054  C   ALA A 404     7024   6136   6249   1341   -197    758       C  
ATOM   3055  O   ALA A 404      15.383  47.402  43.927  1.00 44.17           O  
ANISOU 3055  O   ALA A 404     6281   5102   5398   1438   -141    744       O  
ATOM   3056  CB  ALA A 404      15.069  50.448  43.223  1.00 55.01           C  
ANISOU 3056  CB  ALA A 404     7402   6686   6814   1123   -223    593       C  
ATOM   3057  N   ASN A 405      16.776  48.471  45.312  1.00 58.06           N  
ANISOU 3057  N   ASN A 405     7799   7196   7067   1410   -232    867       N  
ATOM   3058  CA  ASN A 405      17.751  47.394  45.235  1.00 61.40           C  
ANISOU 3058  CA  ASN A 405     8231   7648   7451   1632   -200    978       C  
ATOM   3059  C   ASN A 405      17.468  46.264  46.216  1.00 68.57           C  
ANISOU 3059  C   ASN A 405     9272   8447   8335   1702   -179   1049       C  
ATOM   3060  O   ASN A 405      18.163  45.242  46.182  1.00 75.57           O  
ANISOU 3060  O   ASN A 405    10201   9322   9189   1904   -140   1145       O  
ATOM   3061  CB  ASN A 405      19.171  47.950  45.425  1.00 60.97           C  
ANISOU 3061  CB  ASN A 405     7971   7864   7328   1692   -245   1080       C  
ATOM   3062  CG  ASN A 405      19.682  48.708  44.180  1.00 71.95           C  
ANISOU 3062  CG  ASN A 405     9250   9350   8739   1691   -244   1033       C  
ATOM   3063  OD1 ASN A 405      20.245  49.799  44.285  1.00 77.87           O  
ANISOU 3063  OD1 ASN A 405     9842  10291   9455   1588   -300   1041       O  
ATOM   3064  ND2 ASN A 405      19.467  48.130  42.998  1.00 72.45           N  
ANISOU 3064  ND2 ASN A 405     9405   9272   8849   1793   -180    981       N  
ATOM   3065  N   LEU A 406      16.445  46.402  47.053  1.00 68.10           N  
ANISOU 3065  N   LEU A 406     9287   8301   8287   1550   -197   1005       N  
ATOM   3066  CA  LEU A 406      16.040  45.337  47.961  1.00 64.40           C  
ANISOU 3066  CA  LEU A 406     8961   7712   7797   1594   -176   1063       C  
ATOM   3067  C   LEU A 406      15.583  44.095  47.190  1.00 72.00           C  
ANISOU 3067  C   LEU A 406    10122   8444   8793   1705    -98   1040       C  
ATOM   3068  O   LEU A 406      15.986  42.969  47.505  1.00 81.30           O  
ANISOU 3068  O   LEU A 406    11401   9556   9935   1867    -60   1133       O  
ATOM   3069  CB  LEU A 406      14.922  45.830  48.880  1.00 58.03           C  
ANISOU 3069  CB  LEU A 406     8191   6857   6999   1390   -205   1005       C  
ATOM   3070  CG  LEU A 406      15.132  47.192  49.547  1.00 59.26           C  
ANISOU 3070  CG  LEU A 406     8190   7201   7124   1242   -273    994       C  
ATOM   3071  CD1 LEU A 406      13.926  47.574  50.393  1.00 55.94           C  
ANISOU 3071  CD1 LEU A 406     7835   6707   6713   1062   -282    933       C  
ATOM   3072  CD2 LEU A 406      16.380  47.171  50.403  1.00 58.51           C  
ANISOU 3072  CD2 LEU A 406     7977   7310   6943   1324   -317   1127       C  
TER    3073      LEU A 406                                                      
HETATM 3074  S   SO4 A 501       5.973  58.652  32.397  1.00 44.61           S  
ANISOU 3074  S   SO4 A 501     5949   5045   5957    266   -110   -203       S  
HETATM 3075  O1  SO4 A 501       5.086  57.499  32.477  1.00 30.45           O  
ANISOU 3075  O1  SO4 A 501     4228   3174   4167    245    -99   -206       O  
HETATM 3076  O2  SO4 A 501       6.160  59.063  31.006  1.00 49.97           O  
ANISOU 3076  O2  SO4 A 501     6588   5753   6647    275   -111   -229       O  
HETATM 3077  O3  SO4 A 501       7.280  58.345  33.000  1.00 40.40           O  
ANISOU 3077  O3  SO4 A 501     5411   4544   5397    328   -125   -173       O  
HETATM 3078  O4  SO4 A 501       5.332  59.729  33.136  1.00 54.37           O  
ANISOU 3078  O4  SO4 A 501     7160   6302   7197    210   -101   -198       O  
HETATM 3079  PG  ATP A 502       6.636  56.252  21.388  1.00 58.61           P  
ANISOU 3079  PG  ATP A 502     7843   6785   7642    346    -60   -454       P  
HETATM 3080  O1G ATP A 502       6.548  57.328  20.328  1.00 51.45           O  
ANISOU 3080  O1G ATP A 502     6844   5965   6740    314    -74   -461       O  
HETATM 3081  O2G ATP A 502       5.509  55.249  21.252  1.00 64.05           O  
ANISOU 3081  O2G ATP A 502     8644   7387   8306    258    -58   -479       O  
HETATM 3082  O3G ATP A 502       7.991  55.584  21.566  1.00 58.08           O  
ANISOU 3082  O3G ATP A 502     7817   6697   7554    477    -32   -446       O  
HETATM 3083  PB  ATP A 502       6.617  56.636  24.337  1.00 43.12           P  
ANISOU 3083  PB  ATP A 502     5837   4816   5732    360    -77   -379       P  
HETATM 3084  O1B ATP A 502       6.093  55.235  24.507  1.00 47.12           O  
ANISOU 3084  O1B ATP A 502     6476   5214   6215    342    -62   -393       O  
HETATM 3085  O2B ATP A 502       6.097  57.778  25.159  1.00 35.49           O  
ANISOU 3085  O2B ATP A 502     4787   3901   4796    307    -95   -352       O  
HETATM 3086  O3B ATP A 502       6.418  57.103  22.775  1.00 64.01           O  
ANISOU 3086  O3B ATP A 502     8448   7506   8368    328    -79   -410       O  
HETATM 3087  PA  ATP A 502       9.231  56.945  25.639  1.00 46.69           P  
ANISOU 3087  PA  ATP A 502     6202   5367   6170    542    -76   -309       P  
HETATM 3088  O1A ATP A 502       9.772  55.684  26.264  1.00 49.13           O  
ANISOU 3088  O1A ATP A 502     6594   5616   6457    631    -57   -286       O  
HETATM 3089  O2A ATP A 502       8.639  58.056  26.467  1.00 48.82           O  
ANISOU 3089  O2A ATP A 502     6411   5673   6467    460    -99   -294       O  
HETATM 3090  O3A ATP A 502       8.226  56.548  24.444  1.00 46.55           O  
ANISOU 3090  O3A ATP A 502     6247   5290   6151    483    -66   -358       O  
HETATM 3091  O5' ATP A 502      10.414  57.588  24.722  1.00 56.42           O  
ANISOU 3091  O5' ATP A 502     7347   6702   7386    600    -75   -304       O  
HETATM 3092  C5' ATP A 502      10.155  58.252  23.470  1.00 37.27           C  
ANISOU 3092  C5' ATP A 502     4885   4311   4965    558    -77   -335       C  
HETATM 3093  C4' ATP A 502       9.755  59.684  23.799  1.00 36.68           C  
ANISOU 3093  C4' ATP A 502     4730   4291   4914    475   -101   -324       C  
HETATM 3094  O4' ATP A 502      10.775  60.307  24.561  1.00 35.21           O  
ANISOU 3094  O4' ATP A 502     4478   4183   4717    495   -115   -286       O  
HETATM 3095  C3' ATP A 502       9.540  60.641  22.639  1.00 36.44           C  
ANISOU 3095  C3' ATP A 502     4648   4310   4889    431   -106   -342       C  
HETATM 3096  O3' ATP A 502       8.195  60.531  22.171  1.00 34.40           O  
ANISOU 3096  O3' ATP A 502     4426   4000   4646    366   -105   -366       O  
HETATM 3097  C2' ATP A 502       9.823  62.012  23.249  1.00 37.46           C  
ANISOU 3097  C2' ATP A 502     4707   4502   5025    388   -122   -314       C  
HETATM 3098  O2' ATP A 502       8.596  62.639  23.645  1.00 25.25           O  
ANISOU 3098  O2' ATP A 502     3172   2916   3504    319   -123   -316       O  
HETATM 3099  C1' ATP A 502      10.595  61.732  24.525  1.00 31.70           C  
ANISOU 3099  C1' ATP A 502     3974   3788   4281    421   -129   -282       C  
HETATM 3100  N9  ATP A 502      11.961  62.316  24.613  1.00 32.22           N  
ANISOU 3100  N9  ATP A 502     3967   3961   4315    440   -142   -250       N  
HETATM 3101  C8  ATP A 502      12.455  62.903  25.714  1.00 31.40           C  
ANISOU 3101  C8  ATP A 502     3835   3904   4194    406   -160   -218       C  
HETATM 3102  N7  ATP A 502      13.731  63.303  25.518  1.00 37.93           N  
ANISOU 3102  N7  ATP A 502     4586   4846   4981    417   -173   -187       N  
HETATM 3103  C5  ATP A 502      14.085  62.957  24.262  1.00 35.10           C  
ANISOU 3103  C5  ATP A 502     4204   4515   4618    474   -157   -199       C  
HETATM 3104  C6  ATP A 502      15.301  63.084  23.417  1.00 36.74           C  
ANISOU 3104  C6  ATP A 502     4330   4841   4787    517   -155   -175       C  
HETATM 3105  N6  ATP A 502      16.433  63.669  23.876  1.00 35.34           N  
ANISOU 3105  N6  ATP A 502     4069   4795   4565    493   -177   -125       N  
HETATM 3106  N1  ATP A 502      15.254  62.590  22.162  1.00 43.13           N  
ANISOU 3106  N1  ATP A 502     5151   5636   5599    575   -129   -202       N  
HETATM 3107  C2  ATP A 502      14.142  62.002  21.688  1.00 41.04           C  
ANISOU 3107  C2  ATP A 502     4972   5255   5368    580   -112   -250       C  
HETATM 3108  N3  ATP A 502      13.009  61.849  22.402  1.00 35.72           N  
ANISOU 3108  N3  ATP A 502     4365   4481   4728    533   -118   -268       N  
HETATM 3109  C4  ATP A 502      12.914  62.301  23.671  1.00 33.76           C  
ANISOU 3109  C4  ATP A 502     4111   4232   4485    487   -137   -244       C  
HETATM 3110 MN    MN A 503       5.086  53.785  23.072  1.00 64.10          MN  
HETATM 3111 MN    MN A 504       8.329  59.672  27.921  1.00 45.42          MN  
HETATM 3112  O   HOH A 601       7.190  60.636  29.857  1.00 25.85           O  
HETATM 3113  O   HOH A 602       7.274  65.264  36.373  1.00 36.07           O  
HETATM 3114  O   HOH A 603       7.938  61.589  26.178  1.00 29.41           O  
HETATM 3115  O   HOH A 604      11.896  66.541  -0.679  1.00 44.37           O  
HETATM 3116  O   HOH A 605       8.539  58.106  29.752  1.00 34.25           O  
HETATM 3117  O   HOH A 606      -4.320  73.738  16.534  1.00 39.75           O  
HETATM 3118  O   HOH A 607     -10.954  70.280  41.103  1.00 45.29           O  
HETATM 3119  O   HOH A 608      11.381  50.323  12.309  1.00 57.98           O  
HETATM 3120  O   HOH A 609      -2.356  77.820   3.338  1.00 33.84           O  
HETATM 3121  O   HOH A 610      15.486  52.645  17.204  1.00 48.04           O  
HETATM 3122  O   HOH A 611      13.112  46.708  46.279  1.00 45.35           O  
HETATM 3123  O   HOH A 612       6.663  50.607  56.486  1.00 46.39           O  
HETATM 3124  O   HOH A 613       5.351  75.679  36.467  1.00 47.53           O  
HETATM 3125  O   HOH A 614       0.406  52.804  21.008  1.00 53.58           O  
HETATM 3126  O   HOH A 615      16.258  67.584  33.252  1.00 55.36           O  
HETATM 3127  O   HOH A 616      -3.202  43.642  45.050  1.00 48.10           O  
HETATM 3128  O   HOH A 617      -0.680  56.952  35.513  1.00 52.01           O  
HETATM 3129  O   HOH A 618      -4.966  77.023  16.408  1.00 40.39           O  
HETATM 3130  O   HOH A 619      12.529  64.104   8.237  1.00 31.36           O  
HETATM 3131  O   HOH A 620       2.905  58.860  13.187  1.00 29.93           O  
HETATM 3132  O   HOH A 621      -5.152  59.138  36.463  1.00 43.29           O  
HETATM 3133  O   HOH A 622       7.324  78.229  29.155  1.00 23.34           O  
HETATM 3134  O   HOH A 623       3.660  58.033  44.161  1.00 33.31           O  
HETATM 3135  O   HOH A 624       6.307  58.907  27.520  1.00 40.65           O  
HETATM 3136  O   HOH A 625       3.609  75.540  -0.531  1.00 37.75           O  
HETATM 3137  O   HOH A 626      18.967  61.115   7.604  1.00 32.57           O  
HETATM 3138  O   HOH A 627       4.592  80.023   8.328  1.00 30.09           O  
HETATM 3139  O   HOH A 628       6.440  73.087  38.165  1.00 36.23           O  
HETATM 3140  O   HOH A 629      -9.136  82.240  14.997  1.00 74.66           O  
HETATM 3141  O   HOH A 630       7.697  53.168  23.881  1.00 54.06           O  
HETATM 3142  O   HOH A 631      -4.943  59.834  13.945  1.00 42.23           O  
HETATM 3143  O   HOH A 632      14.102  58.034  15.281  1.00 31.15           O  
HETATM 3144  O   HOH A 633      18.507  50.262  32.988  1.00 42.51           O  
HETATM 3145  O   HOH A 634       5.007  67.444  32.872  1.00 29.53           O  
HETATM 3146  O   HOH A 635      20.976  76.846  11.562  1.00 27.61           O  
HETATM 3147  O   HOH A 636       9.564  76.830  27.783  1.00 35.14           O  
HETATM 3148  O   HOH A 637       1.965  69.071  40.948  1.00 32.26           O  
HETATM 3149  O   HOH A 638       0.279  81.833  14.451  1.00 44.46           O  
HETATM 3150  O   HOH A 639      -1.152  48.221  39.547  1.00 45.53           O  
HETATM 3151  O   HOH A 640       0.425  46.104  51.537  1.00 41.70           O  
HETATM 3152  O   HOH A 641       0.436  74.763   5.163  1.00 28.12           O  
HETATM 3153  O   HOH A 642      17.214  67.173  15.913  1.00 25.79           O  
HETATM 3154  O   HOH A 643      11.737  77.796  27.944  1.00 28.52           O  
HETATM 3155  O   HOH A 644      18.718  68.793  29.532  1.00 32.25           O  
HETATM 3156  O   HOH A 645      -2.058  74.043   5.412  1.00 35.07           O  
HETATM 3157  O   HOH A 646      35.173  60.372  23.132  1.00 60.29           O  
HETATM 3158  O   HOH A 647      -8.203  55.716  40.580  1.00 51.22           O  
HETATM 3159  O   HOH A 648      15.476  56.237  14.211  1.00 38.89           O  
HETATM 3160  O   HOH A 649      23.491  41.398  21.512  1.00 51.10           O  
HETATM 3161  O   HOH A 650      10.900  53.169  12.654  1.00 42.68           O  
HETATM 3162  O   HOH A 651       4.261  65.961  44.067  1.00 39.11           O  
HETATM 3163  O   HOH A 652      10.139  60.828  28.192  1.00 39.21           O  
HETATM 3164  O   HOH A 653      -5.066  68.213  21.520  1.00 39.12           O  
HETATM 3165  O   HOH A 654      16.684  80.542  13.942  1.00 33.12           O  
HETATM 3166  O   HOH A 655      18.567  71.479  23.017  1.00 39.40           O  
HETATM 3167  O   HOH A 656       1.659  48.142  38.816  1.00 63.47           O  
HETATM 3168  O   HOH A 657      12.183  83.613   9.613  1.00 48.75           O  
HETATM 3169  O   HOH A 658       2.103  64.444  23.302  1.00 37.86           O  
HETATM 3170  O   HOH A 659     -11.709  46.629  45.896  1.00 36.67           O  
HETATM 3171  O   HOH A 660      18.713  78.997  15.244  1.00 45.31           O  
HETATM 3172  O   HOH A 661      20.849  57.345  53.792  1.00 62.82           O  
HETATM 3173  O   HOH A 662       5.540  56.868  42.388  1.00 42.29           O  
HETATM 3174  O   HOH A 663       7.044  74.131   9.329  1.00 32.29           O  
HETATM 3175  O   HOH A 664      13.145  55.581  32.754  1.00 43.43           O  
HETATM 3176  O   HOH A 665      11.450  64.519  43.455  1.00 46.08           O  
HETATM 3177  O   HOH A 666       6.473  73.108   6.870  1.00 33.82           O  
HETATM 3178  O   HOH A 667      15.710  70.633  -1.807  1.00 34.98           O  
HETATM 3179  O   HOH A 668      -6.122  70.238   4.438  1.00 30.29           O  
HETATM 3180  O   HOH A 669       7.005  66.392  33.460  1.00 37.37           O  
HETATM 3181  O   HOH A 670      -6.467  72.736   4.890  1.00 33.71           O  
HETATM 3182  O   HOH A 671      -6.308  60.229  16.901  1.00 59.09           O  
HETATM 3183  O   HOH A 672     -10.366  58.583   9.458  1.00 97.67           O  
HETATM 3184  O   HOH A 673      -3.227  49.346  50.959  1.00 38.49           O  
HETATM 3185  O   HOH A 674       8.498  61.514  17.386  1.00 21.23           O  
HETATM 3186  O   HOH A 675       0.378  61.998  14.162  1.00 39.29           O  
HETATM 3187  O   HOH A 676       4.048  61.270  27.587  1.00 45.41           O  
HETATM 3188  O   HOH A 677      -3.604  67.022  23.378  1.00 29.80           O  
HETATM 3189  O   HOH A 678      -1.634  63.290  21.435  1.00 38.14           O  
HETATM 3190  O   HOH A 679      15.569  59.357  46.191  1.00 44.83           O  
HETATM 3191  O   HOH A 680      19.728  69.294  22.373  1.00 29.35           O  
HETATM 3192  O   HOH A 681      -4.926  75.643   4.382  1.00 38.02           O  
HETATM 3193  O   HOH A 682       5.748  60.577  24.214  1.00 44.87           O  
HETATM 3194  O   HOH A 683       9.944  75.409   2.903  1.00 44.93           O  
HETATM 3195  O   HOH A 684       3.089  73.325   6.156  1.00 47.32           O  
HETATM 3196  O   HOH A 685       6.422  79.155   1.566  1.00 49.56           O  
HETATM 3197  O   HOH A 686      14.553  53.808  14.969  1.00 36.67           O  
HETATM 3198  O   HOH A 687      11.341  44.876  48.127  1.00 32.42           O  
HETATM 3199  O   HOH A 688       9.335  51.993  28.149  1.00 64.96           O  
HETATM 3200  O   HOH A 689       2.943  66.401  30.121  1.00 37.97           O  
HETATM 3201  O   HOH A 690      -1.941  75.384  16.991  1.00 34.41           O  
HETATM 3202  O   HOH A 691       1.016  56.860  21.945  1.00 58.31           O  
HETATM 3203  O   HOH A 692       7.329  53.596  26.817  1.00 34.10           O  
HETATM 3204  O   HOH A 693      21.079  61.465  13.906  1.00 31.67           O  
HETATM 3205  O   HOH A 694      26.814  72.996  30.382  1.00 57.82           O  
HETATM 3206  O   HOH A 695      24.962  70.565   6.194  1.00 37.14           O  
HETATM 3207  O   HOH A 696      17.613  58.329  45.244  1.00 52.91           O  
HETATM 3208  O   HOH A 697      -8.928  44.438  39.459  1.00 61.36           O  
HETATM 3209  O   HOH A 698      10.750  57.112   6.927  1.00 49.67           O  
HETATM 3210  O   HOH A 699      12.133  63.296  40.888  1.00 53.31           O  
HETATM 3211  O   HOH A 700       2.765  54.944  22.792  1.00 87.13           O  
HETATM 3212  O   HOH A 701      -4.934  65.917  25.343  1.00 33.07           O  
HETATM 3213  O   HOH A 702     -11.644  66.726  15.475  1.00 41.22           O  
HETATM 3214  O   HOH A 703       8.848  65.664  47.122  1.00 46.63           O  
HETATM 3215  O   HOH A 704      21.478  48.513  36.581  1.00 59.43           O  
HETATM 3216  O   HOH A 705      16.109  51.093   9.038  1.00 68.30           O  
HETATM 3217  O   HOH A 706       6.197  55.831  27.732  1.00 49.01           O  
HETATM 3218  O   HOH A 707       8.990  73.140   1.289  1.00 52.54           O  
HETATM 3219  O   HOH A 708      21.343  76.791  30.081  1.00 48.25           O  
HETATM 3220  O   HOH A 709     -11.279  60.985   4.891  1.00 64.80           O  
HETATM 3221  O   HOH A 710      17.225  64.829  41.174  1.00 52.22           O  
HETATM 3222  O   HOH A 711      -8.669  64.889  19.932  1.00 55.37           O  
HETATM 3223  O   HOH A 712      26.610  57.155   2.873  1.00 63.01           O  
HETATM 3224  O   HOH A 713      11.217  42.112  47.329  1.00 47.76           O  
HETATM 3225  O   HOH A 714      13.998  64.252  39.807  1.00 49.02           O  
HETATM 3226  O   HOH A 715       0.331  62.001  29.486  1.00 52.39           O  
HETATM 3227  O   HOH A 716      -2.036  84.231   3.440  1.00 51.36           O  
HETATM 3228  O   HOH A 717       1.061  59.432  33.382  1.00 79.41           O  
HETATM 3229  O   HOH A 718       7.289  91.492  23.833  1.00 67.92           O  
HETATM 3230  O   HOH A 719      13.271  76.233  -1.676  1.00 39.77           O  
HETATM 3231  O   HOH A 720      15.368  79.117  29.368  1.00 57.86           O  
HETATM 3232  O   HOH A 721      18.444  75.857  29.321  1.00 42.49           O  
HETATM 3233  O   HOH A 722      -2.007  76.547   5.741  1.00 45.05           O  
HETATM 3234  O   HOH A 723       3.521  61.686  24.590  1.00 21.36           O  
HETATM 3235  O   HOH A 724       4.431  52.185  25.445  1.00 74.62           O  
HETATM 3236  O   HOH A 725      -9.378  82.513  12.588  1.00 58.71           O  
HETATM 3237  O   HOH A 726      -4.204  56.177  34.541  1.00 48.71           O  
HETATM 3238  O   HOH A 727      23.168  74.195  38.918  1.00 51.53           O  
HETATM 3239  O   HOH A 728      32.553  43.745  23.435  1.00 48.10           O  
HETATM 3240  O   HOH A 729       5.910  81.860   6.121  1.00 49.63           O  
HETATM 3241  O   HOH A 730      -6.944  81.917  -2.799  1.00 64.18           O  
HETATM 3242  O   HOH A 731      36.436  73.529  20.530  1.00 55.45           O  
HETATM 3243  O   HOH A 732      23.140  84.327  15.632  1.00 63.66           O  
HETATM 3244  O   HOH A 733      21.777  57.749  59.282  1.00 61.49           O  
HETATM 3245  O   HOH A 734       6.136  68.591  55.177  1.00 66.69           O  
HETATM 3246  O   HOH A 735      23.896  52.108  52.949  1.00 73.84           O  
HETATM 3247  O   HOH A 736      21.057  36.716  19.030  1.00 73.83           O  
HETATM 3248  O   HOH A 737     -13.589  81.622   9.842  1.00 56.05           O  
HETATM 3249  O   HOH A 738     -10.708  86.734  13.082  1.00 57.02           O  
HETATM 3250  O   HOH A 739     -12.813  47.542  -6.760  1.00 70.90           O  
CONECT 3074 3075 3076 3077 3078                                                 
CONECT 3075 3074                                                                
CONECT 3076 3074                                                                
CONECT 3077 3074                                                                
CONECT 3078 3074                                                                
CONECT 3079 3080 3081 3082 3086                                                 
CONECT 3080 3079                                                                
CONECT 3081 3079 3110                                                           
CONECT 3082 3079                                                                
CONECT 3083 3084 3085 3086 3090                                                 
CONECT 3084 3083 3110                                                           
CONECT 3085 3083                                                                
CONECT 3086 3079 3083                                                           
CONECT 3087 3088 3089 3090 3091                                                 
CONECT 3088 3087                                                                
CONECT 3089 3087 3111                                                           
CONECT 3090 3083 3087                                                           
CONECT 3091 3087 3092                                                           
CONECT 3092 3091 3093                                                           
CONECT 3093 3092 3094 3095                                                      
CONECT 3094 3093 3099                                                           
CONECT 3095 3093 3096 3097                                                      
CONECT 3096 3095                                                                
CONECT 3097 3095 3098 3099                                                      
CONECT 3098 3097                                                                
CONECT 3099 3094 3097 3100                                                      
CONECT 3100 3099 3101 3109                                                      
CONECT 3101 3100 3102                                                           
CONECT 3102 3101 3103                                                           
CONECT 3103 3102 3104 3109                                                      
CONECT 3104 3103 3105 3106                                                      
CONECT 3105 3104                                                                
CONECT 3106 3104 3107                                                           
CONECT 3107 3106 3108                                                           
CONECT 3108 3107 3109                                                           
CONECT 3109 3100 3103 3108                                                      
CONECT 3110 3081 3084 3211                                                      
CONECT 3111 3089 3112 3114 3116                                                 
CONECT 3111 3135 3163                                                           
CONECT 3112 3111                                                                
CONECT 3114 3111                                                                
CONECT 3116 3111                                                                
CONECT 3135 3111                                                                
CONECT 3163 3111                                                                
CONECT 3211 3110                                                                
MASTER      380    0    4   13   15    0   12    6 3249    1   45   34          
END                                                                             



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