CNRS Nantes University UFIP UFIP
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***  6cf7  ***

elNémo ID: 200202062853107173

Job options:

ID        	=	 200202062853107173
JOBID     	=	 6cf7
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 6cf7

HEADER    VIRAL PROTEIN                           13-FEB-18   6CF7              
TITLE     CRYSTAL STRUCTURE OF THE A/SOLOMON ISLANDS/3/2006(H1N1) INFLUENZA     
TITLE    2 VIRUS HEMAGGLUTININ IN COMPLEX WITH SMALL MOLECULE JNJ4796           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMAGGLUTININ;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HEMAGGLUTININ;                                             
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;                              
SOURCE   3 ORGANISM_COMMON: A/SOLOMON ISLANDS/3/2006(H1N1);                     
SOURCE   4 ORGANISM_TAXID: 464623;                                              
SOURCE   5 GENE: HA;                                                            
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/SOLOMON                    
SOURCE  12 ISLANDS/3/2006(H1N1));                                               
SOURCE  13 ORGANISM_TAXID: 464623;                                              
SOURCE  14 STRAIN: A/HONG KONG/65446/2008(H1N1);                                
SOURCE  15 GENE: HA;                                                            
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  17 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    GLYCOPROTEIN, ECTODOMAIN, N-GLYCOSYLATION, VIRAL PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.U.KADAM,I.A.WILSON                                                  
REVDAT   6   18-DEC-19 6CF7    1       REMARK                                   
REVDAT   5   10-APR-19 6CF7    1       REMARK                                   
REVDAT   4   27-MAR-19 6CF7    1       JRNL                                     
REVDAT   3   20-MAR-19 6CF7    1       JRNL                                     
REVDAT   2   13-MAR-19 6CF7    1       JRNL                                     
REVDAT   1   13-FEB-19 6CF7    0                                                
JRNL        AUTH   M.J.P.VAN DONGEN,R.U.KADAM,J.JURASZEK,E.LAWSON,              
JRNL        AUTH 2 B.BRANDENBURG,F.SCHMITZ,W.B.G.SCHEPENS,B.STOOPS,             
JRNL        AUTH 3 H.A.VAN DIEPEN,M.JONGENEELEN,C.TANG,J.VERMOND,               
JRNL        AUTH 4 A.VAN EIJGEN-OBREGOSO REAL,S.BLOKLAND,D.GARG,W.YU,W.GOUTIER, 
JRNL        AUTH 5 E.LANCKACKER,J.M.KLAP,D.C.G.PEETERS,J.WU,C.BUYCK,            
JRNL        AUTH 6 T.H.M.JONCKERS,D.ROYMANS,P.ROEVENS,R.VOGELS,W.KOUDSTAAL,     
JRNL        AUTH 7 R.H.E.FRIESEN,P.RABOISSON,D.DHANAK,J.GOUDSMIT,I.A.WILSON     
JRNL        TITL   A SMALL-MOLECULE FUSION INHIBITOR OF INFLUENZA VIRUS IS      
JRNL        TITL 2 ORALLY ACTIVE IN MICE.                                       
JRNL        REF    SCIENCE                       V. 363       2019              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   30846569                                                     
JRNL        DOI    10.1126/SCIENCE.AAR6221                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.72 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10_2155                                     
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) : 2.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19834                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 996                             
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 44.7828 -  5.1994    0.98     2829   164  0.2164 0.2396        
REMARK   3     2  5.1994 -  4.1278    0.99     2710   158  0.1925 0.2146        
REMARK   3     3  4.1278 -  3.6063    1.00     2693   137  0.2184 0.2514        
REMARK   3     4  3.6063 -  3.2767    1.00     2690   121  0.2414 0.2475        
REMARK   3     5  3.2767 -  3.0419    1.00     2632   135  0.2742 0.2993        
REMARK   3     6  3.0419 -  2.8626    1.00     2653   140  0.2674 0.2870        
REMARK   3     7  2.8626 -  2.7192    1.00     2631   141  0.2807 0.3279        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.00                          
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      :  0.004           4220                                  
REMARK   3   ANGLE     :  0.565           5745                                  
REMARK   3   CHIRALITY :  0.041            633                                  
REMARK   3   PLANARITY :  0.004            733                                  
REMARK   3   DIHEDRAL  : 11.939           2513                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2751  27.7487  11.7739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3627 T22:   0.3355                                     
REMARK   3      T33:   0.4205 T12:   0.0322                                     
REMARK   3      T13:  -0.0057 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7774 L22:   1.9436                                     
REMARK   3      L33:   1.7766 L12:   0.3297                                     
REMARK   3      L13:   0.5369 L23:   0.6311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0834 S12:   0.1028 S13:   0.3473                       
REMARK   3      S21:  -0.1970 S22:  -0.0513 S23:   0.3527                       
REMARK   3      S31:  -0.2802 S32:  -0.2357 S33:   0.0841                       
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 6CF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232653.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.719                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 12.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200   FOR THE DATA SET  : 22.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.89000                            
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5W5S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M DISODIUM HYDROGEN PHOSPHATE, 20%    
REMARK 280  W/V PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       80.72250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.72250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       80.72250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.72250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       80.72250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       80.72250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       80.72250            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       80.72250            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       80.72250            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       80.72250            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       80.72250            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       80.72250            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       80.72250            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       80.72250            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       80.72250            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       80.72250            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       80.72250            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       80.72250            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      121.08375            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       40.36125            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      121.08375            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      121.08375            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      121.08375            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       40.36125            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      121.08375            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       40.36125            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      121.08375            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       40.36125            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      121.08375            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       40.36125            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       40.36125            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      121.08375            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       40.36125            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      121.08375            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      121.08375            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      121.08375            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       40.36125            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      121.08375            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      121.08375            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       40.36125            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       40.36125            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       40.36125            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      121.08375            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       40.36125            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      121.08375            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       40.36125            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      121.08375            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      121.08375            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      121.08375            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 34830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        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     ILE A   326                                                      
REMARK 465     GLN A   327                                                      
REMARK 465     SER A   328                                                      
REMARK 465     ARG A   329                                                      
REMARK 465     LYS B   172                                                      
REMARK 465     ILE B   173                                                      
REMARK 465     ASP B   174                                                      
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    SER A 125C      -0.93    175.69                                   
REMARK 500    CYS A 139       56.25   -111.17                                   
REMARK 500    THR A 155     -163.43   -120.42                                   
REMARK 500    ASN A 171       53.80   -101.11                                   
REMARK 500    HIS A 196       16.51     59.19                                   
REMARK 500    SER A 206     -161.63   -126.76                                   
REMARK 500    ALA B   5      -71.70    -90.23                                   
REMARK 500    LYS B 127     -135.69     60.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ7 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  405 through BMA A 407 bound to ASN A 21                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  410 through NAG A 411 bound to ASN A 33                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 412 bound   
REMARK 800  to ASN A 63                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  408 through NAG A 409 bound to ASN A 95                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  401 through MAN A 404 bound to ASN A 289                            
DBREF  6CF7 A   11   329  UNP    A7Y8I1   A7Y8I1_9INFA    18    343             
DBREF  6CF7 B    1   174  UNP    F2NZB4   F2NZB4_9INFA   344    517             
SEQADV 6CF7 ARG A   53  UNP  A7Y8I1    LEU    60 ENGINEERED MUTATION            
SEQRES   1 A  326  ASP THR ILE CYS ILE GLY TYR HIS ALA ASN ASN SER THR          
SEQRES   2 A  326  ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR VAL          
SEQRES   3 A  326  THR HIS SER VAL ASN LEU LEU GLU ASP SER HIS ASN GLY          
SEQRES   4 A  326  LYS LEU CYS ARG LEU LYS GLY ILE ALA PRO LEU GLN LEU          
SEQRES   5 A  326  GLY ASN CYS SER VAL ALA GLY TRP ILE LEU GLY ASN PRO          
SEQRES   6 A  326  GLU CYS GLU LEU LEU ILE SER ARG GLU SER TRP SER TYR          
SEQRES   7 A  326  ILE VAL GLU LYS PRO ASN PRO GLU ASN GLY THR CYS TYR          
SEQRES   8 A  326  PRO GLY HIS PHE ALA ASP TYR GLU GLU LEU ARG GLU GLN          
SEQRES   9 A  326  LEU SER SER VAL SER SER PHE GLU ARG PHE GLU ILE PHE          
SEQRES  10 A  326  PRO LYS GLU SER SER TRP PRO ASN HIS THR THR THR GLY          
SEQRES  11 A  326  VAL SER ALA SER CYS SER HIS ASN GLY GLU SER SER PHE          
SEQRES  12 A  326  TYR LYS ASN LEU LEU TRP LEU THR GLY LYS ASN GLY LEU          
SEQRES  13 A  326  TYR PRO ASN LEU SER LYS SER TYR ALA ASN ASN LYS GLU          
SEQRES  14 A  326  LYS GLU VAL LEU VAL LEU TRP GLY VAL HIS HIS PRO PRO          
SEQRES  15 A  326  ASN ILE GLY ASP GLN ARG ALA LEU TYR HIS LYS GLU ASN          
SEQRES  16 A  326  ALA TYR VAL SER VAL VAL SER SER HIS TYR SER ARG LYS          
SEQRES  17 A  326  PHE THR PRO GLU ILE ALA LYS ARG PRO LYS VAL ARG ASP          
SEQRES  18 A  326  GLN GLU GLY ARG ILE ASN TYR TYR TRP THR LEU LEU GLU          
SEQRES  19 A  326  PRO GLY ASP THR ILE ILE PHE GLU ALA ASN GLY ASN LEU          
SEQRES  20 A  326  ILE ALA PRO ARG TYR ALA PHE ALA LEU SER ARG GLY PHE          
SEQRES  21 A  326  GLY SER GLY ILE ILE ASN SER ASN ALA PRO MET ASP GLU          
SEQRES  22 A  326  CYS ASP ALA LYS CYS GLN THR PRO GLN GLY ALA ILE ASN          
SEQRES  23 A  326  SER SER LEU PRO PHE GLN ASN VAL HIS PRO VAL THR ILE          
SEQRES  24 A  326  GLY GLU CYS PRO LYS TYR VAL ARG SER ALA LYS LEU ARG          
SEQRES  25 A  326  MET VAL THR GLY LEU ARG ASN ILE PRO SER ILE GLN SER          
SEQRES  26 A  326  ARG                                                          
SEQRES   1 B  174  GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU GLY GLY          
SEQRES   2 B  174  TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR HIS HIS          
SEQRES   3 B  174  GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP GLN LYS          
SEQRES   4 B  174  SER THR GLN ASN ALA ILE ASN GLY ILE THR ASN LYS VAL          
SEQRES   5 B  174  ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE THR ALA          
SEQRES   6 B  174  VAL GLY LYS GLU PHE ASN LYS LEU GLU ARG ARG MET GLU          
SEQRES   7 B  174  ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE ILE ASP ILE          
SEQRES   8 B  174  TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU GLU ASN          
SEQRES   9 B  174  GLU ARG THR LEU ASP PHE HIS ASP SER ASN VAL LYS ASN          
SEQRES  10 B  174  LEU TYR GLU LYS VAL LYS SER GLN LEU LYS ASN ASN ALA          
SEQRES  11 B  174  LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR HIS LYS          
SEQRES  12 B  174  CYS ASN ASP GLU CYS MET GLU SER VAL LYS ASN GLY THR          
SEQRES  13 B  174  TYR ASP TYR PRO LYS TYR SER GLU GLU SER LYS LEU ASN          
SEQRES  14 B  174  ARG GLU LYS ILE ASP                                          
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    BMA  A 403      11                                                       
HET    MAN  A 404      11                                                       
HET    NAG  A 405      14                                                       
HET    NAG  A 406      14                                                       
HET    BMA  A 407      11                                                       
HET    NAG  A 408      14                                                       
HET    NAG  A 409      14                                                       
HET    NAG  A 410      14                                                       
HET    NAG  A 411      14                                                       
HET    NAG  A 412      14                                                       
HET    EZ7  B 201      40                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     EZ7 N-[2-(2-{4-[(R)-(2-METHYL-2H-TETRAZOL-5-YL)(PHENYL)              
HETNAM   2 EZ7  METHYL]PIPERAZINE-1-CARBONYL}PYRIDIN-4-YL)-1,3-                 
HETNAM   3 EZ7  BENZOXAZOL-5-YL]ACETAMIDE                                       
FORMUL   3  NAG    9(C8 H15 N O6)                                               
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   8  EZ7    C28 H27 N9 O3                                                
FORMUL   9  HOH   *52(H2 O)                                                     
HELIX    1 AA1 SER A   65  GLY A   72  1                                   8    
HELIX    2 AA2 ASN A   73  ILE A   80  5                                   8    
HELIX    3 AA3 ASP A  104  SER A  113  1                                  10    
HELIX    4 AA4 ASN A  187  HIS A  196  1                                  10    
HELIX    5 AA5 ASP B   37  LYS B   58  1                                  22    
HELIX    6 AA6 GLU B   74  LYS B  127  1                                  54    
HELIX    7 AA7 ASN B  145  ASN B  154  1                                  10    
HELIX    8 AA8 TYR B  159  LYS B  161  5                                   3    
HELIX    9 AA9 TYR B  162  ARG B  170  1                                   9    
SHEET    1 AA1 5 GLY B  31  ALA B  36  0                                        
SHEET    2 AA1 5 TYR B  22  ASN B  28 -1  N  ASN B  28   O  GLY B  31           
SHEET    3 AA1 5 THR A  12  TYR A  17 -1  N  THR A  12   O  GLN B  27           
SHEET    4 AA1 5 CYS B 137  PHE B 140 -1  O  PHE B 138   N  ILE A  13           
SHEET    5 AA1 5 ALA B 130  LYS B 131 -1  N  LYS B 131   O  GLU B 139           
SHEET    1 AA2 2 THR A  25  VAL A  26  0                                        
SHEET    2 AA2 2 VAL A  34  THR A  35 -1  O  VAL A  34   N  VAL A  26           
SHEET    1 AA3 2 SER A  39  ASN A  41  0                                        
SHEET    2 AA3 2 ARG A 315  VAL A 317 -1  O  MET A 316   N  VAL A  40           
SHEET    1 AA4 3 LEU A  43  GLU A  44  0                                        
SHEET    2 AA4 3 PHE A 294  GLN A 295  1  O  PHE A 294   N  GLU A  44           
SHEET    3 AA4 3 LYS A 307  TYR A 308  1  O  LYS A 307   N  GLN A 295           
SHEET    1 AA5 2 LEU A  51  LEU A  54  0                                        
SHEET    2 AA5 2 MET A 274  ALA A 279  1  O  CYS A 277   N  ARG A  53           
SHEET    1 AA6 3 LEU A  59  GLN A  60  0                                        
SHEET    2 AA6 3 ILE A  87  GLU A  89  1  O  VAL A  88   N  LEU A  59           
SHEET    3 AA6 3 ILE A 267  ASN A 269  1  O  ILE A 268   N  GLU A  89           
SHEET    1 AA7 5 VAL A 115  GLU A 122  0                                        
SHEET    2 AA7 5 TYR A 256  ARG A 262 -1  O  ALA A 257   N  PHE A 121           
SHEET    3 AA7 5 GLU A 175  HIS A 184 -1  N  GLU A 175   O  LEU A 260           
SHEET    4 AA7 5 LEU A 251  PRO A 254 -1  O  ILE A 252   N  GLY A 181           
SHEET    5 AA7 5 LEU A 151  TRP A 153 -1  N  LEU A 152   O  ALA A 253           
SHEET    1 AA8 4 VAL A 115  GLU A 122  0                                        
SHEET    2 AA8 4 TYR A 256  ARG A 262 -1  O  ALA A 257   N  PHE A 121           
SHEET    3 AA8 4 GLU A 175  HIS A 184 -1  N  GLU A 175   O  LEU A 260           
SHEET    4 AA8 4 ARG A 229  LEU A 237 -1  O  TYR A 233   N  TRP A 180           
SHEET    1 AA9 2 SER A 136  HIS A 141  0                                        
SHEET    2 AA9 2 GLU A 144  SER A 146 -1  O  GLU A 144   N  HIS A 141           
SHEET    1 AB1 4 LEU A 164  ALA A 169  0                                        
SHEET    2 AB1 4 THR A 242  ALA A 247 -1  O  ALA A 247   N  LEU A 164           
SHEET    3 AB1 4 VAL A 202  VAL A 205 -1  N  VAL A 205   O  ILE A 244           
SHEET    4 AB1 4 SER A 210  PHE A 213 -1  O  ARG A 211   N  VAL A 204           
SHEET    1 AB2 3 GLY A 286  ILE A 288  0                                        
SHEET    2 AB2 3 CYS A 281  THR A 283 -1  N  CYS A 281   O  ILE A 288           
SHEET    3 AB2 3 ILE A 302  GLY A 303 -1  O  ILE A 302   N  GLN A 282           
SSBOND   1 CYS A   14    CYS B  137                          1555   1555  2.03  
SSBOND   2 CYS A   52    CYS A  277                          1555   1555  2.03  
SSBOND   3 CYS A   64    CYS A   76                          1555   1555  2.03  
SSBOND   4 CYS A   97    CYS A  139                          1555   1555  2.03  
SSBOND   5 CYS A  281    CYS A  305                          1555   1555  2.03  
SSBOND   6 CYS B  144    CYS B  148                          1555   1555  2.03  
LINK         ND2 ASN A  21                 C1  NAG A 405     1555   1555  1.44  
LINK         ND2 ASN A  33                 C1  NAG A 410     1555   1555  1.44  
LINK         ND2 ASN A  63                 C1  NAG A 412     1555   1555  1.44  
LINK         ND2 ASN A  95                 C1  NAG A 408     1555   1555  1.44  
LINK         ND2 ASN A 289                 C1  NAG A 401     1555   1555  1.44  
LINK         O4  NAG A 401                 C1  NAG A 402     1555   1555  1.44  
LINK         O4  NAG A 402                 C1  BMA A 403     1555   1555  1.44  
LINK         O3  BMA A 403                 C1  MAN A 404     1555   1555  1.45  
LINK         O4  NAG A 405                 C1  NAG A 406     1555   1555  1.44  
LINK         O4  NAG A 406                 C1  BMA A 407     1555   1555  1.44  
LINK         O4  NAG A 408                 C1  NAG A 409     1555   1555  1.44  
LINK         O4  NAG A 410                 C1  NAG A 411     1555   1555  1.44  
SITE     1 AC1 15 HIS A  18  HIS A  38  THR A 318  NAG A 402                    
SITE     2 AC1 15 BMA A 403  VAL B  18  GLY B  20  TRP B  21                    
SITE     3 AC1 15 THR B  41  ILE B  45  ILE B  48  THR B  49                    
SITE     4 AC1 15 VAL B  52  ASN B  53  ILE B  56                               
SITE     1 AC2  2 ASN A  21  GLU B  57                                          
SITE     1 AC3  1 ASN A  33                                                     
SITE     1 AC4  1 ASN A  63                                                     
SITE     1 AC5  5 ASN A  73  GLU A  94  ASN A  95  CYS A  97                    
SITE     2 AC5  5 ARG A 224                                                     
SITE     1 AC6  6 ASN A  41  ASN A 289  LEU A 292  ARG A 315                    
SITE     2 AC6  6 ASN B  53  EZ7 B 201                                          
CRYST1  161.445  161.445  161.445  90.00  90.00  90.00 P 41 3 2     24          
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      0.006194  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006194  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006194        0.00000                         
ATOM      1  N   ASP A  11      33.614  63.913  49.533  1.00111.63           N  
ANISOU    1  N   ASP A  11    16008  10574  15831  -2379  -2797  -5540       N  
ATOM      2  CA  ASP A  11      33.460  63.601  48.117  1.00113.79           C  
ANISOU    2  CA  ASP A  11    16190  10773  16270  -2394  -2698  -5296       C  
ATOM      3  C   ASP A  11      33.631  62.111  47.860  1.00111.81           C  
ANISOU    3  C   ASP A  11    15803  10793  15889  -2347  -2677  -5151       C  
ATOM      4  O   ASP A  11      34.634  61.513  48.250  1.00115.87           O  
ANISOU    4  O   ASP A  11    16204  11493  16327  -2439  -2786  -5157       O  
ATOM      5  CB  ASP A  11      34.458  64.399  47.279  1.00116.10           C  
ANISOU    5  CB  ASP A  11    16412  10878  16824  -2627  -2747  -5201       C  
ATOM      6  CG  ASP A  11      34.112  65.871  47.213  1.00120.75           C  
ANISOU    6  CG  ASP A  11    17148  11151  17581  -2662  -2740  -5292       C  
ATOM      7  OD1 ASP A  11      33.391  66.350  48.113  1.00122.95           O  
ANISOU    7  OD1 ASP A  11    17570  11384  17763  -2533  -2742  -5486       O  
ATOM      8  OD2 ASP A  11      34.557  66.549  46.263  1.00123.11           O  
ANISOU    8  OD2 ASP A  11    17423  11249  18104  -2821  -2730  -5169       O  
ATOM      9  N   THR A  12      32.642  61.515  47.198  1.00101.89           N  
ANISOU    9  N   THR A  12    14551   9551  14611  -2200  -2542  -5024       N  
ATOM     10  CA  THR A  12      32.628  60.083  46.943  1.00 94.29           C  
ANISOU   10  CA  THR A  12    13477   8829  13519  -2132  -2509  -4892       C  
ATOM     11  C   THR A  12      32.048  59.810  45.564  1.00 87.88           C  
ANISOU   11  C   THR A  12    12617   7925  12847  -2093  -2378  -4678       C  
ATOM     12  O   THR A  12      31.219  60.571  45.057  1.00 89.62           O  
ANISOU   12  O   THR A  12    12933   7932  13188  -2035  -2292  -4658       O  
ATOM     13  CB  THR A  12      31.807  59.324  47.996  1.00 93.62           C  
ANISOU   13  CB  THR A  12    13478   8948  13145  -1946  -2480  -5006       C  
ATOM     14  OG1 THR A  12      30.569  60.010  48.221  1.00 90.27           O  
ANISOU   14  OG1 THR A  12    13206   8384  12709  -1804  -2379  -5108       O  
ATOM     15  CG2 THR A  12      32.573  59.212  49.306  1.00104.77           C  
ANISOU   15  CG2 THR A  12    14907  10524  14376  -1998  -2626  -5173       C  
ATOM     16  N   ILE A  13      32.494  58.710  44.965  1.00 85.25           N  
ANISOU   16  N   ILE A  13    12138   7757  12498  -2120  -2369  -4520       N  
ATOM     17  CA  ILE A  13      31.925  58.194  43.727  1.00 82.49           C  
ANISOU   17  CA  ILE A  13    11736   7372  12234  -2068  -2245  -4317       C  
ATOM     18  C   ILE A  13      31.687  56.701  43.909  1.00 79.83           C  
ANISOU   18  C   ILE A  13    11330   7300  11701  -1949  -2221  -4267       C  
ATOM     19  O   ILE A  13      32.475  56.009  44.564  1.00 80.00           O  
ANISOU   19  O   ILE A  13    11275   7524  11598  -1984  -2323  -4311       O  
ATOM     20  CB  ILE A  13      32.832  58.474  42.507  1.00 82.50           C  
ANISOU   20  CB  ILE A  13    11614   7265  12466  -2267  -2244  -4142       C  
ATOM     21  CG1 ILE A  13      32.067  58.235  41.204  1.00 80.17           C  
ANISOU   21  CG1 ILE A  13    11314   6876  12273  -2212  -2107  -3942       C  
ATOM     22  CG2 ILE A  13      34.094  57.621  42.546  1.00 82.11           C  
ANISOU   22  CG2 ILE A  13    11378   7430  12389  -2385  -2331  -4098       C  
ATOM     23  CD1 ILE A  13      32.887  58.501  39.961  1.00 80.28           C  
ANISOU   23  CD1 ILE A  13    11222   6791  12492  -2413  -2085  -3758       C  
ATOM     24  N   CYS A  14      30.583  56.211  43.356  1.00 77.54           N  
ANISOU   24  N   CYS A  14    11073   7007  11382  -1803  -2094  -4177       N  
ATOM     25  CA  CYS A  14      30.191  54.820  43.510  1.00 85.22           C  
ANISOU   25  CA  CYS A  14    12003   8213  12166  -1680  -2057  -4130       C  
ATOM     26  C   CYS A  14      29.917  54.208  42.145  1.00 72.42           C  
ANISOU   26  C   CYS A  14    10290   6568  10658  -1671  -1957  -3919       C  
ATOM     27  O   CYS A  14      29.619  54.906  41.173  1.00 72.40           O  
ANISOU   27  O   CYS A  14    10304   6359  10844  -1708  -1890  -3820       O  
ATOM     28  CB  CYS A  14      28.950  54.681  44.403  1.00 85.83           C  
ANISOU   28  CB  CYS A  14    12223   8353  12036  -1490  -1988  -4260       C  
ATOM     29  SG  CYS A  14      29.188  55.153  46.133  1.00 95.59           S  
ANISOU   29  SG  CYS A  14    13576   9673  13070  -1485  -2093  -4513       S  
ATOM     30  N   ILE A  15      30.030  52.885  42.085  1.00 70.33           N  
ANISOU   30  N   ILE A  15     9936   6516  10271  -1623  -1955  -3847       N  
ATOM     31  CA  ILE A  15      29.674  52.106  40.907  1.00 67.69           C  
ANISOU   31  CA  ILE A  15     9518   6196  10003  -1591  -1857  -3663       C  
ATOM     32  C   ILE A  15      28.560  51.150  41.306  1.00 65.89           C  
ANISOU   32  C   ILE A  15     9356   6113   9567  -1401  -1781  -3685       C  
ATOM     33  O   ILE A  15      28.708  50.386  42.267  1.00 65.90           O  
ANISOU   33  O   ILE A  15     9369   6315   9355  -1348  -1841  -3764       O  
ATOM     34  CB  ILE A  15      30.880  51.336  40.334  1.00 68.24           C  
ANISOU   34  CB  ILE A  15     9400   6391  10139  -1717  -1915  -3548       C  
ATOM     35  CG1 ILE A  15      31.809  52.271  39.554  1.00 68.35           C  
ANISOU   35  CG1 ILE A  15     9335   6244  10392  -1918  -1934  -3478       C  
ATOM     36  CG2 ILE A  15      30.411  50.195  39.446  1.00 64.04           C  
ANISOU   36  CG2 ILE A  15     8794   5946   9592  -1643  -1821  -3397       C  
ATOM     37  CD1 ILE A  15      32.765  53.066  40.417  1.00 71.20           C  
ANISOU   37  CD1 ILE A  15     9697   6587  10768  -2036  -2063  -3616       C  
ATOM     38  N   GLY A  16      27.445  51.206  40.584  1.00 64.56           N  
ANISOU   38  N   GLY A  16     9234   5842   9454  -1301  -1652  -3612       N  
ATOM     39  CA  GLY A  16      26.315  50.347  40.880  1.00 64.32           C  
ANISOU   39  CA  GLY A  16     9257   5942   9240  -1128  -1561  -3629       C  
ATOM     40  C   GLY A  16      25.547  49.943  39.640  1.00 66.00           C  
ANISOU   40  C   GLY A  16     9429   6117   9529  -1063  -1418  -3422       C  
ATOM     41  O   GLY A  16      26.021  50.153  38.519  1.00 62.88           O  
ANISOU   41  O   GLY A  16     8957   5619   9316  -1164  -1404  -3261       O  
ATOM     42  N   TYR A  17      24.357  49.374  39.818  1.00 60.03           N  
ANISOU   42  N   TYR A  17     8725   5459   8624   -902  -1299  -3406       N  
ATOM     43  CA  TYR A  17      23.594  48.866  38.690  1.00 57.49           C  
ANISOU   43  CA  TYR A  17     8359   5141   8342   -831  -1162  -3192       C  
ATOM     44  C   TYR A  17      22.110  49.167  38.869  1.00 57.57           C  
ANISOU   44  C   TYR A  17     8457   5097   8320   -668  -1055  -3271       C  
ATOM     45  O   TYR A  17      21.642  49.500  39.962  1.00 58.99           O  
ANISOU   45  O   TYR A  17     8723   5297   8394   -597  -1065  -3486       O  
ATOM     46  CB  TYR A  17      23.831  47.364  38.491  1.00 55.36           C  
ANISOU   46  CB  TYR A  17     8002   5119   7914   -816  -1118  -3021       C  
ATOM     47  CG  TYR A  17      23.728  46.526  39.743  1.00 55.47           C  
ANISOU   47  CG  TYR A  17     8061   5350   7665   -750  -1140  -3121       C  
ATOM     48  CD1 TYR A  17      22.505  46.033  40.171  1.00 54.86           C  
ANISOU   48  CD1 TYR A  17     8050   5374   7422   -613  -1025  -3145       C  
ATOM     49  CD2 TYR A  17      24.857  46.212  40.487  1.00 56.34           C  
ANISOU   49  CD2 TYR A  17     8146   5570   7691   -832  -1279  -3186       C  
ATOM     50  CE1 TYR A  17      22.405  45.261  41.311  1.00 55.16           C  
ANISOU   50  CE1 TYR A  17     8145   5611   7202   -571  -1038  -3221       C  
ATOM     51  CE2 TYR A  17      24.767  45.439  41.631  1.00 56.63           C  
ANISOU   51  CE2 TYR A  17     8245   5801   7471   -776  -1312  -3262       C  
ATOM     52  CZ  TYR A  17      23.538  44.966  42.037  1.00 56.05           C  
ANISOU   52  CZ  TYR A  17     8253   5821   7221   -651  -1186  -3273       C  
ATOM     53  OH  TYR A  17      23.437  44.197  43.173  1.00 75.22           O  
ANISOU   53  OH  TYR A  17    10759   8442   9378   -611  -1211  -3334       O  
ATOM     54  N   HIS A  18      21.379  49.032  37.763  1.00 56.88           N  
ANISOU   54  N   HIS A  18     8338   4952   8323   -610   -954  -3099       N  
ATOM     55  CA  HIS A  18      19.992  49.463  37.658  1.00 56.37           C  
ANISOU   55  CA  HIS A  18     8328   4795   8295   -459   -864  -3154       C  
ATOM     56  C   HIS A  18      19.055  48.540  38.435  1.00 55.63           C  
ANISOU   56  C   HIS A  18     8244   4927   7967   -328   -759  -3213       C  
ATOM     57  O   HIS A  18      19.337  47.361  38.663  1.00 54.28           O  
ANISOU   57  O   HIS A  18     8031   4976   7616   -347   -734  -3123       O  
ATOM     58  CB  HIS A  18      19.573  49.513  36.186  1.00 55.11           C  
ANISOU   58  CB  HIS A  18     8126   4521   8294   -446   -806  -2932       C  
ATOM     59  CG  HIS A  18      18.139  49.887  35.966  1.00 58.18           C  
ANISOU   59  CG  HIS A  18     8549   4819   8736   -281   -726  -2970       C  
ATOM     60  ND1 HIS A  18      17.714  51.195  35.884  1.00 57.25           N  
ANISOU   60  ND1 HIS A  18     8506   4440   8808   -235   -774  -3085       N  
ATOM     61  CD2 HIS A  18      17.034  49.122  35.797  1.00 53.99           C  
ANISOU   61  CD2 HIS A  18     7980   4423   8109   -150   -609  -2913       C  
ATOM     62  CE1 HIS A  18      16.409  51.221  35.681  1.00 57.85           C  
ANISOU   62  CE1 HIS A  18     8579   4498   8903    -71   -693  -3102       C  
ATOM     63  NE2 HIS A  18      15.972  49.976  35.625  1.00 56.08           N  
ANISOU   63  NE2 HIS A  18     8282   4518   8506    -23   -589  -3000       N  
ATOM     64  N   ALA A  19      17.919  49.106  38.839  1.00 58.40           N  
ANISOU   64  N   ALA A  19     8649   5214   8327   -196   -696  -3370       N  
ATOM     65  CA  ALA A  19      16.829  48.358  39.445  1.00 56.28           C  
ANISOU   65  CA  ALA A  19     8379   5140   7864    -71   -568  -3428       C  
ATOM     66  C   ALA A  19      15.521  49.047  39.083  1.00 56.96           C  
ANISOU   66  C   ALA A  19     8466   5090   8085     75   -489  -3498       C  
ATOM     67  O   ALA A  19      15.505  50.223  38.711  1.00 58.32           O  
ANISOU   67  O   ALA A  19     8675   5010   8475     89   -556  -3563       O  
ATOM     68  CB  ALA A  19      16.993  48.255  40.965  1.00 57.78           C  
ANISOU   68  CB  ALA A  19     8645   5478   7832    -74   -585  -3649       C  
ATOM     69  N   ASN A  20      14.421  48.306  39.188  1.00 56.15           N  
ANISOU   69  N   ASN A  20     8322   5151   7862    184   -351  -3483       N  
ATOM     70  CA  ASN A  20      13.105  48.858  38.887  1.00 56.89           C  
ANISOU   70  CA  ASN A  20     8391   5146   8079    339   -272  -3561       C  
ATOM     71  C   ASN A  20      12.043  48.006  39.571  1.00 56.69           C  
ANISOU   71  C   ASN A  20     8327   5366   7848    430   -114  -3633       C  
ATOM     72  O   ASN A  20      12.350  47.073  40.317  1.00 59.31           O  
ANISOU   72  O   ASN A  20     8676   5920   7938    368    -74  -3623       O  
ATOM     73  CB  ASN A  20      12.871  48.952  37.373  1.00 57.59           C  
ANISOU   73  CB  ASN A  20     8421   5088   8374    356   -288  -3335       C  
ATOM     74  CG  ASN A  20      13.063  47.627  36.663  1.00 58.89           C  
ANISOU   74  CG  ASN A  20     8512   5429   8433    295   -238  -3076       C  
ATOM     75  OD1 ASN A  20      13.214  46.582  37.295  1.00 70.55           O  
ANISOU   75  OD1 ASN A  20     9977   7136   9693    259   -181  -3061       O  
ATOM     76  ND2 ASN A  20      13.056  47.665  35.335  1.00 57.77           N  
ANISOU   76  ND2 ASN A  20     8332   5174   8445    283   -263  -2871       N  
ATOM     77  N   ASN A  21      10.778  48.341  39.308  1.00 57.31           N  
ANISOU   77  N   ASN A  21     8351   5398   8027    577    -27  -3703       N  
ATOM     78  CA  ASN A  21       9.638  47.628  39.869  1.00 65.24           C  
ANISOU   78  CA  ASN A  21     9296   6624   8868    664    140  -3781       C  
ATOM     79  C   ASN A  21       9.179  46.474  38.987  1.00 59.84           C  
ANISOU   79  C   ASN A  21     8516   6070   8152    659    217  -3532       C  
ATOM     80  O   ASN A  21       8.024  46.045  39.093  1.00 72.52           O  
ANISOU   80  O   ASN A  21    10042   7804   9708    748    353  -3574       O  
ATOM     81  CB  ASN A  21       8.477  48.595  40.108  1.00 80.02           C  
ANISOU   81  CB  ASN A  21    11137   8413  10855    821    199  -3952       C  
ATOM     82  CG  ASN A  21       8.013  49.268  38.832  1.00 84.90           C  
ANISOU   82  CG  ASN A  21    11698   8798  11761    911    135  -3848       C  
ATOM     83  OD1 ASN A  21       8.753  49.331  37.851  1.00 82.86           O  
ANISOU   83  OD1 ASN A  21    11461   8381  11642    843     22  -3694       O  
ATOM     84  ND2 ASN A  21       6.786  49.777  38.837  1.00103.68           N  
ANISOU   84  ND2 ASN A  21    14006  11159  14227   1060    203  -3927       N  
ATOM     85  N   SER A  22      10.057  45.966  38.126  1.00 61.81           N  
ANISOU   85  N   SER A  22     8763   6291   8431    554    137  -3288       N  
ATOM     86  CA  SER A  22       9.686  44.906  37.200  1.00 50.93           C  
ANISOU   86  CA  SER A  22     7300   5014   7037    547    195  -3056       C  
ATOM     87  C   SER A  22       9.419  43.607  37.948  1.00 50.23           C  
ANISOU   87  C   SER A  22     7199   5202   6685    510    312  -3035       C  
ATOM     88  O   SER A  22      10.197  43.205  38.818  1.00 51.20           O  
ANISOU   88  O   SER A  22     7397   5434   6625    421    288  -3066       O  
ATOM     89  CB  SER A  22      10.791  44.702  36.167  1.00 49.26           C  
ANISOU   89  CB  SER A  22     7096   4714   6908    437     85  -2824       C  
ATOM     90  OG  SER A  22      10.542  43.558  35.370  1.00 47.22           O  
ANISOU   90  OG  SER A  22     6765   4575   6600    420    140  -2612       O  
ATOM     91  N   THR A  23       8.311  42.953  37.608  1.00 49.61           N  
ANISOU   91  N   THR A  23     7030   5232   6588    573    432  -2980       N  
ATOM     92  CA  THR A  23       7.989  41.632  38.126  1.00 51.00           C  
ANISOU   92  CA  THR A  23     7191   5654   6533    523    546  -2918       C  
ATOM     93  C   THR A  23       8.330  40.527  37.136  1.00 49.27           C  
ANISOU   93  C   THR A  23     6933   5480   6309    455    524  -2648       C  
ATOM     94  O   THR A  23       7.950  39.373  37.355  1.00 46.25           O  
ANISOU   94  O   THR A  23     6529   5275   5768    418    615  -2568       O  
ATOM     95  CB  THR A  23       6.508  41.554  38.506  1.00 55.79           C  
ANISOU   95  CB  THR A  23     7714   6375   7110    621    710  -3051       C  
ATOM     96  OG1 THR A  23       5.700  41.755  37.339  1.00 61.53           O  
ANISOU   96  OG1 THR A  23     8326   7004   8049    713    714  -2974       O  
ATOM     97  CG2 THR A  23       6.167  42.610  39.544  1.00 52.60           C  
ANISOU   97  CG2 THR A  23     7345   5943   6697    695    745  -3343       C  
ATOM     98  N   ASP A  24       9.029  40.860  36.051  1.00 47.01           N  
ANISOU   98  N   ASP A  24     6639   5033   6189    433    408  -2511       N  
ATOM     99  CA  ASP A  24       9.437  39.859  35.074  1.00 43.90           C  
ANISOU   99  CA  ASP A  24     6209   4678   5792    369    385  -2272       C  
ATOM    100  C   ASP A  24      10.326  38.811  35.727  1.00 42.93           C  
ANISOU  100  C   ASP A  24     6144   4702   5465    264    369  -2204       C  
ATOM    101  O   ASP A  24      11.311  39.141  36.394  1.00 52.95           O  
ANISOU  101  O   ASP A  24     7487   5951   6680    208    286  -2271       O  
ATOM    102  CB  ASP A  24      10.183  40.518  33.914  1.00 48.65           C  
ANISOU  102  CB  ASP A  24     6809   5088   6588    346    266  -2159       C  
ATOM    103  CG  ASP A  24       9.280  41.357  33.037  1.00 57.31           C  
ANISOU  103  CG  ASP A  24     7855   6035   7887    449    264  -2165       C  
ATOM    104  OD1 ASP A  24       8.047  41.169  33.086  1.00 58.94           O  
ANISOU  104  OD1 ASP A  24     7993   6308   8093    541    356  -2218       O  
ATOM    105  OD2 ASP A  24       9.810  42.202  32.285  1.00 53.94           O  
ANISOU  105  OD2 ASP A  24     7454   5421   7620    434    165  -2113       O  
ATOM    106  N   THR A  25       9.979  37.545  35.528  1.00 41.39           N  
ANISOU  106  N   THR A  25     5917   4647   5164    239    436  -2073       N  
ATOM    107  CA  THR A  25      10.757  36.430  36.043  1.00 40.75           C  
ANISOU  107  CA  THR A  25     5892   4692   4900    151    409  -1984       C  
ATOM    108  C   THR A  25      11.184  35.525  34.898  1.00 38.83           C  
ANISOU  108  C   THR A  25     5599   4444   4709    115    372  -1771       C  
ATOM    109  O   THR A  25      10.435  35.321  33.938  1.00 39.06           O  
ANISOU  109  O   THR A  25     5552   4453   4835    154    422  -1689       O  
ATOM    110  CB  THR A  25       9.963  35.626  37.073  1.00 41.48           C  
ANISOU  110  CB  THR A  25     6017   4964   4778    142    528  -2033       C  
ATOM    111  OG1 THR A  25       8.694  35.261  36.518  1.00 50.03           O  
ANISOU  111  OG1 THR A  25     7008   6090   5911    190    648  -1996       O  
ATOM    112  CG2 THR A  25       9.746  36.445  38.335  1.00 43.58           C  
ANISOU  112  CG2 THR A  25     6349   5260   4949    163    562  -2256       C  
ATOM    113  N   VAL A  26      12.402  34.997  35.000  1.00 41.10           N  
ANISOU  113  N   VAL A  26     5926   4751   4938     44    277  -1694       N  
ATOM    114  CA  VAL A  26      12.914  34.014  34.060  1.00 36.67           C  
ANISOU  114  CA  VAL A  26     5323   4206   4404     10    243  -1512       C  
ATOM    115  C   VAL A  26      13.518  32.869  34.858  1.00 36.64           C  
ANISOU  115  C   VAL A  26     5383   4322   4217    -42    206  -1463       C  
ATOM    116  O   VAL A  26      13.774  32.983  36.058  1.00 41.37           O  
ANISOU  116  O   VAL A  26     6064   4977   4679    -61    179  -1561       O  
ATOM    117  CB  VAL A  26      13.959  34.608  33.090  1.00 36.13           C  
ANISOU  117  CB  VAL A  26     5215   4013   4500    -19    145  -1455       C  
ATOM    118  CG1 VAL A  26      13.360  35.756  32.300  1.00 36.38           C  
ANISOU  118  CG1 VAL A  26     5208   3909   4708     28    167  -1485       C  
ATOM    119  CG2 VAL A  26      15.187  35.066  33.851  1.00 37.05           C  
ANISOU  119  CG2 VAL A  26     5379   4109   4590    -73     36  -1534       C  
ATOM    120  N   ASP A  27      13.731  31.750  34.176  1.00 35.37           N  
ANISOU  120  N   ASP A  27     5191   4197   4052    -59    196  -1312       N  
ATOM    121  CA  ASP A  27      14.386  30.596  34.769  1.00 35.34           C  
ANISOU  121  CA  ASP A  27     5247   4280   3903    -99    137  -1242       C  
ATOM    122  C   ASP A  27      15.842  30.556  34.331  1.00 34.93           C  
ANISOU  122  C   ASP A  27     5162   4180   3931   -124      3  -1196       C  
ATOM    123  O   ASP A  27      16.168  30.899  33.191  1.00 37.25           O  
ANISOU  123  O   ASP A  27     5372   4398   4385   -122     -7  -1149       O  
ATOM    124  CB  ASP A  27      13.684  29.297  34.372  1.00 34.81           C  
ANISOU  124  CB  ASP A  27     5170   4276   3781   -101    206  -1116       C  
ATOM    125  CG  ASP A  27      12.325  29.149  35.014  1.00 45.19           C  
ANISOU  125  CG  ASP A  27     6516   5668   4985    -97    340  -1162       C  
ATOM    126  OD1 ASP A  27      12.124  29.695  36.118  1.00 50.85           O  
ANISOU  126  OD1 ASP A  27     7298   6429   5593   -103    365  -1284       O  
ATOM    127  OD2 ASP A  27      11.453  28.485  34.413  1.00 53.07           O  
ANISOU  127  OD2 ASP A  27     7467   6691   6004    -94    423  -1086       O  
ATOM    128  N   THR A  28      16.714  30.146  35.245  1.00 35.70           N  
ANISOU  128  N   THR A  28     5324   4328   3914   -150   -100  -1212       N  
ATOM    129  CA  THR A  28      18.129  29.984  34.957  1.00 35.57           C  
ANISOU  129  CA  THR A  28     5261   4287   3968   -171   -234  -1179       C  
ATOM    130  C   THR A  28      18.548  28.573  35.342  1.00 35.55           C  
ANISOU  130  C   THR A  28     5304   4357   3846   -168   -305  -1085       C  
ATOM    131  O   THR A  28      17.778  27.813  35.932  1.00 49.60           O  
ANISOU  131  O   THR A  28     7172   6199   5476   -166   -253  -1045       O  
ATOM    132  CB  THR A  28      18.980  31.028  35.694  1.00 36.89           C  
ANISOU  132  CB  THR A  28     5447   4424   4147   -200   -334  -1311       C  
ATOM    133  OG1 THR A  28      18.789  30.900  37.108  1.00 40.68           O  
ANISOU  133  OG1 THR A  28     6050   4980   4428   -205   -363  -1387       O  
ATOM    134  CG2 THR A  28      18.586  32.431  35.260  1.00 37.06           C  
ANISOU  134  CG2 THR A  28     5431   4344   4305   -202   -275  -1400       C  
ATOM    135  N   VAL A  29      19.783  28.216  34.988  1.00 36.24           N  
ANISOU  135  N   VAL A  29     5329   4432   4009   -171   -424  -1049       N  
ATOM    136  CA  VAL A  29      20.243  26.860  35.262  1.00 37.10           C  
ANISOU  136  CA  VAL A  29     5475   4587   4033   -151   -511   -959       C  
ATOM    137  C   VAL A  29      20.517  26.676  36.750  1.00 37.11           C  
ANISOU  137  C   VAL A  29     5607   4646   3845   -162   -615  -1002       C  
ATOM    138  O   VAL A  29      20.360  25.572  37.283  1.00 43.12           O  
ANISOU  138  O   VAL A  29     6465   5450   4469   -153   -652   -920       O  
ATOM    139  CB  VAL A  29      21.475  26.527  34.396  1.00 36.92           C  
ANISOU  139  CB  VAL A  29     5327   4540   4162   -137   -605   -923       C  
ATOM    140  CG1 VAL A  29      22.669  27.371  34.800  1.00 57.54           C  
ANISOU  140  CG1 VAL A  29     7886   7142   6833   -163   -728  -1026       C  
ATOM    141  CG2 VAL A  29      21.808  25.048  34.481  1.00 36.90           C  
ANISOU  141  CG2 VAL A  29     5354   4564   4103    -96   -686   -825       C  
ATOM    142  N   LEU A  30      20.900  27.744  37.452  1.00 38.20           N  
ANISOU  142  N   LEU A  30     5765   4784   3966   -187   -668  -1130       N  
ATOM    143  CA  LEU A  30      21.185  27.660  38.877  1.00 39.91           C  
ANISOU  143  CA  LEU A  30     6113   5063   3987   -201   -775  -1185       C  
ATOM    144  C   LEU A  30      20.006  28.047  39.758  1.00 45.86           C  
ANISOU  144  C   LEU A  30     6993   5867   4566   -223   -655  -1250       C  
ATOM    145  O   LEU A  30      20.007  27.703  40.944  1.00 48.05           O  
ANISOU  145  O   LEU A  30     7409   6216   4630   -241   -715  -1265       O  
ATOM    146  CB  LEU A  30      22.379  28.554  39.238  1.00 40.99           C  
ANISOU  146  CB  LEU A  30     6201   5181   4192   -221   -922  -1306       C  
ATOM    147  CG  LEU A  30      23.723  28.239  38.581  1.00 45.54           C  
ANISOU  147  CG  LEU A  30     6640   5731   4931   -208  -1059  -1273       C  
ATOM    148  CD1 LEU A  30      24.742  29.301  38.946  1.00 41.99           C  
ANISOU  148  CD1 LEU A  30     6133   5264   4559   -247  -1180  -1411       C  
ATOM    149  CD2 LEU A  30      24.212  26.862  38.992  1.00 41.26           C  
ANISOU  149  CD2 LEU A  30     6152   5236   4290   -164  -1191  -1173       C  
ATOM    150  N   GLU A  31      19.008  28.744  39.218  1.00 39.94           N  
ANISOU  150  N   GLU A  31     6197   5085   3896   -220   -491  -1293       N  
ATOM    151  CA  GLU A  31      17.938  29.283  40.047  1.00 40.93           C  
ANISOU  151  CA  GLU A  31     6411   5259   3880   -232   -372  -1393       C  
ATOM    152  C   GLU A  31      16.697  29.495  39.194  1.00 45.67           C  
ANISOU  152  C   GLU A  31     6940   5831   4583   -210   -189  -1376       C  
ATOM    153  O   GLU A  31      16.779  30.096  38.118  1.00 42.36           O  
ANISOU  153  O   GLU A  31     6404   5321   4369   -188   -170  -1376       O  
ATOM    154  CB  GLU A  31      18.376  30.602  40.698  1.00 42.25           C  
ANISOU  154  CB  GLU A  31     6597   5402   4056   -244   -431  -1574       C  
ATOM    155  CG  GLU A  31      17.384  31.190  41.692  1.00 43.66           C  
ANISOU  155  CG  GLU A  31     6874   5642   4074   -250   -319  -1711       C  
ATOM    156  CD  GLU A  31      17.783  32.582  42.156  1.00 53.98           C  
ANISOU  156  CD  GLU A  31     8185   6895   5429   -253   -374  -1905       C  
ATOM    157  OE1 GLU A  31      16.914  33.306  42.687  1.00 59.82           O  
ANISOU  157  OE1 GLU A  31     8968   7654   6108   -240   -263  -2046       O  
ATOM    158  OE2 GLU A  31      18.963  32.959  41.984  1.00 50.02           O  
ANISOU  158  OE2 GLU A  31     7638   6332   5037   -270   -526  -1927       O  
ATOM    159  N   LYS A  32      15.561  29.002  39.673  1.00 53.63           N  
ANISOU  159  N   LYS A  32     8014   6919   5443   -221    -60  -1359       N  
ATOM    160  CA  LYS A  32      14.278  29.260  39.039  1.00 55.36           C  
ANISOU  160  CA  LYS A  32     8160   7129   5745   -197    111  -1370       C  
ATOM    161  C   LYS A  32      13.661  30.542  39.589  1.00 59.30           C  
ANISOU  161  C   LYS A  32     8664   7627   6241   -176    192  -1558       C  
ATOM    162  O   LYS A  32      13.986  30.996  40.689  1.00 64.77           O  
ANISOU  162  O   LYS A  32     9450   8363   6797   -195    147  -1676       O  
ATOM    163  CB  LYS A  32      13.313  28.096  39.262  1.00 55.24           C  
ANISOU  163  CB  LYS A  32     8195   7206   5590   -229    222  -1269       C  
ATOM    164  CG  LYS A  32      13.682  26.804  38.561  1.00 50.36           C  
ANISOU  164  CG  LYS A  32     7564   6567   5005   -240    164  -1086       C  
ATOM    165  CD  LYS A  32      12.493  25.858  38.566  1.00 52.39           C  
ANISOU  165  CD  LYS A  32     7843   6889   5174   -278    301  -1002       C  
ATOM    166  CE  LYS A  32      12.780  24.574  37.809  1.00 57.12           C  
ANISOU  166  CE  LYS A  32     8432   7449   5822   -285    245   -831       C  
ATOM    167  NZ  LYS A  32      13.584  23.620  38.618  1.00 68.86           N  
ANISOU  167  NZ  LYS A  32    10057   8957   7151   -318    115   -744       N  
ATOM    168  N   ASN A  33      12.760  31.126  38.795  1.00 47.99           N  
ANISOU  168  N   ASN A  33     7130   6142   4963   -131    302  -1592       N  
ATOM    169  CA  ASN A  33      11.934  32.258  39.221  1.00 49.40           C  
ANISOU  169  CA  ASN A  33     7296   6314   5159    -90    398  -1774       C  
ATOM    170  C   ASN A  33      12.791  33.450  39.648  1.00 43.02           C  
ANISOU  170  C   ASN A  33     6521   5425   4401    -82    290  -1919       C  
ATOM    171  O   ASN A  33      12.607  34.024  40.723  1.00 47.54           O  
ANISOU  171  O   ASN A  33     7168   6045   4850    -83    313  -2081       O  
ATOM    172  CB  ASN A  33      10.980  31.840  40.345  1.00 53.32           C  
ANISOU  172  CB  ASN A  33     7869   6962   5429   -118    531  -1839       C  
ATOM    173  CG  ASN A  33       9.808  32.790  40.506  1.00 65.95           C  
ANISOU  173  CG  ASN A  33     9408   8569   7081    -59    674  -2013       C  
ATOM    174  OD1 ASN A  33       9.314  33.358  39.532  1.00 63.38           O  
ANISOU  174  OD1 ASN A  33     8966   8147   6969      8    704  -2023       O  
ATOM    175  ND2 ASN A  33       9.357  32.968  41.746  1.00 82.10           N  
ANISOU  175  ND2 ASN A  33    11533  10731   8929    -79    760  -2155       N  
ATOM    176  N   VAL A  34      13.736  33.824  38.792  1.00 41.36           N  
ANISOU  176  N   VAL A  34     6254   5093   4368    -83    174  -1865       N  
ATOM    177  CA  VAL A  34      14.617  34.958  39.051  1.00 42.28           C  
ANISOU  177  CA  VAL A  34     6387   5113   4564    -91     62  -1990       C  
ATOM    178  C   VAL A  34      13.940  36.220  38.533  1.00 45.02           C  
ANISOU  178  C   VAL A  34     6676   5332   5096    -32    121  -2098       C  
ATOM    179  O   VAL A  34      13.666  36.341  37.335  1.00 41.42           O  
ANISOU  179  O   VAL A  34     6133   4788   4816     -4    145  -2004       O  
ATOM    180  CB  VAL A  34      15.991  34.761  38.393  1.00 41.35           C  
ANISOU  180  CB  VAL A  34     6226   4932   4554   -135    -83  -1883       C  
ATOM    181  CG1 VAL A  34      16.842  36.015  38.555  1.00 42.40           C  
ANISOU  181  CG1 VAL A  34     6359   4951   4798   -159   -190  -2012       C  
ATOM    182  CG2 VAL A  34      16.696  33.552  38.984  1.00 41.33           C  
ANISOU  182  CG2 VAL A  34     6282   5043   4379   -175   -166  -1793       C  
ATOM    183  N   THR A  35      13.674  37.161  39.435  1.00 44.40           N  
ANISOU  183  N   THR A  35     6654   5240   4976    -10    135  -2297       N  
ATOM    184  CA  THR A  35      13.068  38.432  39.061  1.00 45.10           C  
ANISOU  184  CA  THR A  35     6701   5187   5248     59    171  -2422       C  
ATOM    185  C   THR A  35      14.117  39.304  38.381  1.00 44.94           C  
ANISOU  185  C   THR A  35     6659   4988   5427     25     36  -2407       C  
ATOM    186  O   THR A  35      15.186  39.553  38.947  1.00 45.68           O  
ANISOU  186  O   THR A  35     6805   5070   5482    -38    -80  -2464       O  
ATOM    187  CB  THR A  35      12.494  39.128  40.292  1.00 47.29           C  
ANISOU  187  CB  THR A  35     7047   5507   5412     96    229  -2660       C  
ATOM    188  OG1 THR A  35      11.576  38.247  40.954  1.00 47.60           O  
ANISOU  188  OG1 THR A  35     7107   5734   5246    103    368  -2663       O  
ATOM    189  CG2 THR A  35      11.772  40.405  39.898  1.00 48.18           C  
ANISOU  189  CG2 THR A  35     7112   5462   5730    187    264  -2798       C  
ATOM    190  N   VAL A  36      13.817  39.763  37.167  1.00 44.12           N  
ANISOU  190  N   VAL A  36     6482   4748   5533     59     47  -2328       N  
ATOM    191  CA  VAL A  36      14.783  40.491  36.357  1.00 43.92           C  
ANISOU  191  CA  VAL A  36     6435   4557   5696      7    -64  -2275       C  
ATOM    192  C   VAL A  36      14.218  41.859  35.994  1.00 45.04           C  
ANISOU  192  C   VAL A  36     6578   4506   6030     69    -64  -2378       C  
ATOM    193  O   VAL A  36      13.018  42.117  36.107  1.00 45.64           O  
ANISOU  193  O   VAL A  36     6643   4579   6121    169     26  -2461       O  
ATOM    194  CB  VAL A  36      15.178  39.707  35.090  1.00 41.97           C  
ANISOU  194  CB  VAL A  36     6114   4317   5517    -32    -72  -2047       C  
ATOM    195  CG1 VAL A  36      15.908  38.426  35.470  1.00 41.14           C  
ANISOU  195  CG1 VAL A  36     6010   4373   5247    -89   -101  -1959       C  
ATOM    196  CG2 VAL A  36      13.950  39.395  34.255  1.00 42.52           C  
ANISOU  196  CG2 VAL A  36     6128   4392   5636     46     33  -1961       C  
ATOM    197  N   THR A  37      15.112  42.746  35.549  1.00 45.54           N  
ANISOU  197  N   THR A  37     6652   4400   6250      5   -170  -2374       N  
ATOM    198  CA  THR A  37      14.715  44.121  35.264  1.00 46.92           C  
ANISOU  198  CA  THR A  37     6852   4358   6617     54   -197  -2472       C  
ATOM    199  C   THR A  37      14.076  44.248  33.888  1.00 46.02           C  
ANISOU  199  C   THR A  37     6686   4139   6660    102   -168  -2316       C  
ATOM    200  O   THR A  37      13.098  44.986  33.721  1.00 46.96           O  
ANISOU  200  O   THR A  37     6809   4142   6890    208   -144  -2392       O  
ATOM    201  CB  THR A  37      15.921  45.056  35.368  1.00 48.09           C  
ANISOU  201  CB  THR A  37     7044   4355   6874    -51   -326  -2528       C  
ATOM    202  OG1 THR A  37      16.819  44.808  34.279  1.00 46.91           O  
ANISOU  202  OG1 THR A  37     6845   4168   6813   -155   -372  -2329       O  
ATOM    203  CG2 THR A  37      16.654  44.839  36.679  1.00 48.97           C  
ANISOU  203  CG2 THR A  37     7202   4584   6819   -106   -378  -2669       C  
ATOM    204  N   HIS A  38      14.616  43.548  32.892  1.00 51.51           N  
ANISOU  204  N   HIS A  38     7333   4873   7367     31   -176  -2107       N  
ATOM    205  CA  HIS A  38      14.105  43.605  31.532  1.00 43.56           C  
ANISOU  205  CA  HIS A  38     6287   3779   6484     62   -158  -1945       C  
ATOM    206  C   HIS A  38      14.161  42.214  30.922  1.00 51.97           C  
ANISOU  206  C   HIS A  38     7285   5018   7442     36   -101  -1769       C  
ATOM    207  O   HIS A  38      15.088  41.448  31.197  1.00 51.47           O  
ANISOU  207  O   HIS A  38     7208   5072   7275    -47   -118  -1727       O  
ATOM    208  CB  HIS A  38      14.907  44.596  30.678  1.00 44.23           C  
ANISOU  208  CB  HIS A  38     6402   3655   6747    -27   -250  -1869       C  
ATOM    209  CG  HIS A  38      15.012  45.967  31.276  1.00 48.78           C  
ANISOU  209  CG  HIS A  38     7055   4038   7443    -21   -323  -2041       C  
ATOM    210  ND1 HIS A  38      15.937  46.290  32.246  1.00 47.39           N  
ANISOU  210  ND1 HIS A  38     6915   3861   7229   -101   -383  -2176       N  
ATOM    211  CD2 HIS A  38      14.305  47.098  31.042  1.00 47.85           C  
ANISOU  211  CD2 HIS A  38     6985   3709   7487     61   -357  -2106       C  
ATOM    212  CE1 HIS A  38      15.797  47.560  32.582  1.00 49.37           C  
ANISOU  212  CE1 HIS A  38     7236   3910   7612    -76   -444  -2322       C  
ATOM    213  NE2 HIS A  38      14.814  48.073  31.866  1.00 51.07           N  
ANISOU  213  NE2 HIS A  38     7462   3989   7955     26   -430  -2282       N  
ATOM    214  N   SER A  39      13.165  41.892  30.099  1.00 40.76           N  
ANISOU  214  N   SER A  39     5824   3609   6055    111    -45  -1675       N  
ATOM    215  CA  SER A  39      13.097  40.584  29.465  1.00 38.97           C  
ANISOU  215  CA  SER A  39     5537   3532   5736     94      8  -1518       C  
ATOM    216  C   SER A  39      12.261  40.692  28.199  1.00 38.53           C  
ANISOU  216  C   SER A  39     5450   3408   5783    151     22  -1398       C  
ATOM    217  O   SER A  39      11.506  41.648  28.011  1.00 39.95           O  
ANISOU  217  O   SER A  39     5647   3450   6085    232      1  -1453       O  
ATOM    218  CB  SER A  39      12.513  39.533  30.412  1.00 38.51           C  
ANISOU  218  CB  SER A  39     5462   3668   5504    135     89  -1580       C  
ATOM    219  OG  SER A  39      11.211  39.887  30.824  1.00 47.02           O  
ANISOU  219  OG  SER A  39     6527   4743   6595    246    153  -1696       O  
ATOM    220  N   VAL A  40      12.408  39.693  27.331  1.00 37.04           N  
ANISOU  220  N   VAL A  40     5216   3314   5543    115     47  -1239       N  
ATOM    221  CA  VAL A  40      11.646  39.605  26.091  1.00 36.55           C  
ANISOU  221  CA  VAL A  40     5124   3217   5547    161     55  -1115       C  
ATOM    222  C   VAL A  40      11.037  38.213  25.991  1.00 35.20           C  
ANISOU  222  C   VAL A  40     4890   3227   5259    188    130  -1060       C  
ATOM    223  O   VAL A  40      11.736  37.208  26.162  1.00 34.19           O  
ANISOU  223  O   VAL A  40     4749   3220   5022    122    150  -1013       O  
ATOM    224  CB  VAL A  40      12.516  39.916  24.856  1.00 36.35           C  
ANISOU  224  CB  VAL A  40     5120   3099   5592     67      1   -960       C  
ATOM    225  CG1 VAL A  40      13.843  39.171  24.923  1.00 35.49           C  
ANISOU  225  CG1 VAL A  40     4992   3094   5399    -50      6   -910       C  
ATOM    226  CG2 VAL A  40      11.769  39.573  23.574  1.00 35.73           C  
ANISOU  226  CG2 VAL A  40     5017   3026   5535    107     10   -820       C  
ATOM    227  N   ASN A  41       9.734  38.157  25.738  1.00 42.67           N  
ANISOU  227  N   ASN A  41     5794   4184   6236    286    164  -1072       N  
ATOM    228  CA  ASN A  41       9.054  36.886  25.539  1.00 35.92           C  
ANISOU  228  CA  ASN A  41     4876   3484   5290    304    232  -1017       C  
ATOM    229  C   ASN A  41       9.254  36.415  24.104  1.00 33.26           C  
ANISOU  229  C   ASN A  41     4522   3144   4970    267    203   -845       C  
ATOM    230  O   ASN A  41       9.035  37.175  23.157  1.00 36.39           O  
ANISOU  230  O   ASN A  41     4934   3420   5472    292    147   -781       O  
ATOM    231  CB  ASN A  41       7.565  37.023  25.855  1.00 38.84           C  
ANISOU  231  CB  ASN A  41     5185   3878   5694    416    282  -1114       C  
ATOM    232  CG  ASN A  41       6.764  35.819  25.411  1.00 40.14           C  
ANISOU  232  CG  ASN A  41     5276   4179   5797    426    341  -1042       C  
ATOM    233  OD1 ASN A  41       6.797  34.765  26.049  1.00 50.89           O  
ANISOU  233  OD1 ASN A  41     6626   5681   7030    382    409  -1050       O  
ATOM    234  ND2 ASN A  41       6.034  35.969  24.312  1.00 40.92           N  
ANISOU  234  ND2 ASN A  41     5330   4231   5988    481    304   -970       N  
ATOM    235  N   LEU A  42       9.679  35.165  23.946  1.00 38.80           N  
ANISOU  235  N   LEU A  42     5203   3973   5565    209    237   -770       N  
ATOM    236  CA  LEU A  42       9.921  34.585  22.632  1.00 31.11           C  
ANISOU  236  CA  LEU A  42     4214   3020   4587    170    221   -625       C  
ATOM    237  C   LEU A  42       8.826  33.623  22.196  1.00 33.56           C  
ANISOU  237  C   LEU A  42     4466   3426   4861    216    261   -588       C  
ATOM    238  O   LEU A  42       8.962  32.991  21.146  1.00 37.73           O  
ANISOU  238  O   LEU A  42     4981   3988   5367    187    251   -481       O  
ATOM    239  CB  LEU A  42      11.270  33.860  22.616  1.00 30.30           C  
ANISOU  239  CB  LEU A  42     4122   2981   4410     75    221   -574       C  
ATOM    240  CG  LEU A  42      12.519  34.718  22.811  1.00 30.90           C  
ANISOU  240  CG  LEU A  42     4238   2974   4530      5    175   -592       C  
ATOM    241  CD1 LEU A  42      13.761  33.851  22.773  1.00 30.19           C  
ANISOU  241  CD1 LEU A  42     4127   2971   4373    -75    176   -552       C  
ATOM    242  CD2 LEU A  42      12.599  35.814  21.759  1.00 31.63           C  
ANISOU  242  CD2 LEU A  42     4362   2927   4728    -15    130   -519       C  
ATOM    243  N   LEU A  43       7.746  33.505  22.965  1.00 33.06           N  
ANISOU  243  N   LEU A  43     4360   3410   4790    281    309   -683       N  
ATOM    244  CA  LEU A  43       6.720  32.492  22.743  1.00 30.52           C  
ANISOU  244  CA  LEU A  43     3970   3195   4430    306    358   -664       C  
ATOM    245  C   LEU A  43       5.393  33.179  22.445  1.00 31.51           C  
ANISOU  245  C   LEU A  43     4035   3276   4663    406    346   -712       C  
ATOM    246  O   LEU A  43       4.825  33.849  23.312  1.00 32.58           O  
ANISOU  246  O   LEU A  43     4149   3391   4840    467    374   -838       O  
ATOM    247  CB  LEU A  43       6.601  31.572  23.956  1.00 30.34           C  
ANISOU  247  CB  LEU A  43     3942   3295   4293    275    439   -730       C  
ATOM    248  CG  LEU A  43       5.576  30.444  23.875  1.00 30.06           C  
ANISOU  248  CG  LEU A  43     3839   3371   4212    275    500   -713       C  
ATOM    249  CD1 LEU A  43       5.879  29.544  22.697  1.00 28.99           C  
ANISOU  249  CD1 LEU A  43     3700   3254   4061    234    465   -586       C  
ATOM    250  CD2 LEU A  43       5.575  29.661  25.172  1.00 30.38           C  
ANISOU  250  CD2 LEU A  43     3902   3514   4127    227    579   -768       C  
ATOM    251  N   GLU A  44       4.901  33.007  21.224  1.00 31.84           N  
ANISOU  251  N   GLU A  44     4045   3306   4748    428    299   -620       N  
ATOM    252  CA  GLU A  44       3.609  33.553  20.833  1.00 32.36           C  
ANISOU  252  CA  GLU A  44     4037   3335   4922    532    267   -657       C  
ATOM    253  C   GLU A  44       2.508  32.578  21.231  1.00 32.34           C  
ANISOU  253  C   GLU A  44     3929   3474   4886    546    346   -715       C  
ATOM    254  O   GLU A  44       2.541  31.404  20.850  1.00 31.39           O  
ANISOU  254  O   GLU A  44     3793   3446   4686    482    371   -644       O  
ATOM    255  CB  GLU A  44       3.571  33.816  19.331  1.00 32.37           C  
ANISOU  255  CB  GLU A  44     4062   3264   4975    545    165   -528       C  
ATOM    256  CG  GLU A  44       2.265  34.431  18.859  1.00 33.64           C  
ANISOU  256  CG  GLU A  44     4150   3374   5259    665     99   -559       C  
ATOM    257  CD  GLU A  44       2.001  35.779  19.496  1.00 40.96           C  
ANISOU  257  CD  GLU A  44     5085   4171   6307    759     68   -667       C  
ATOM    258  OE1 GLU A  44       2.883  36.660  19.417  1.00 44.68           O  
ANISOU  258  OE1 GLU A  44     5661   4509   6807    735     17   -632       O  
ATOM    259  OE2 GLU A  44       0.918  35.955  20.090  1.00 55.24           O  
ANISOU  259  OE2 GLU A  44     6791   6012   8187    854    100   -796       O  
ATOM    260  N   ASP A  45       1.536  33.059  21.997  1.00 33.56           N  
ANISOU  260  N   ASP A  45     4006   3643   5104    625    390   -850       N  
ATOM    261  CA  ASP A  45       0.415  32.233  22.411  1.00 33.89           C  
ANISOU  261  CA  ASP A  45     3929   3823   5124    629    479   -915       C  
ATOM    262  C   ASP A  45      -0.924  32.783  21.955  1.00 35.24           C  
ANISOU  262  C   ASP A  45     3973   3976   5440    747    440   -979       C  
ATOM    263  O   ASP A  45      -1.955  32.164  22.232  1.00 44.82           O  
ANISOU  263  O   ASP A  45     5062   5309   6658    751    514  -1044       O  
ATOM    264  CB  ASP A  45       0.405  32.063  23.937  1.00 37.21           C  
ANISOU  264  CB  ASP A  45     4349   4329   5459    597    605  -1040       C  
ATOM    265  CG  ASP A  45       0.147  33.368  24.674  1.00 49.98           C  
ANISOU  265  CG  ASP A  45     5957   5873   7161    694    611  -1191       C  
ATOM    266  OD1 ASP A  45       0.460  34.446  24.124  1.00 53.68           O  
ANISOU  266  OD1 ASP A  45     6470   6189   7738    761    505  -1176       O  
ATOM    267  OD2 ASP A  45      -0.364  33.314  25.812  1.00 56.30           O  
ANISOU  267  OD2 ASP A  45     6711   6766   7915    697    723  -1327       O  
ATOM    268  N   SER A  46      -0.942  33.910  21.256  1.00 35.98           N  
ANISOU  268  N   SER A  46     4092   3923   5656    840    321   -960       N  
ATOM    269  CA  SER A  46      -2.181  34.575  20.893  1.00 37.56           C  
ANISOU  269  CA  SER A  46     4172   4085   6012    977    260  -1033       C  
ATOM    270  C   SER A  46      -2.525  34.334  19.429  1.00 37.37           C  
ANISOU  270  C   SER A  46     4132   4038   6029    995    135   -900       C  
ATOM    271  O   SER A  46      -1.649  34.197  18.570  1.00 36.77           O  
ANISOU  271  O   SER A  46     4173   3907   5890    929     66   -751       O  
ATOM    272  CB  SER A  46      -2.090  36.077  21.167  1.00 39.93           C  
ANISOU  272  CB  SER A  46     4516   4216   6438   1089    192  -1115       C  
ATOM    273  OG  SER A  46      -2.023  36.332  22.558  1.00 70.82           O  
ANISOU  273  OG  SER A  46     8420   8167  10321   1091    308  -1275       O  
ATOM    274  N   HIS A  47      -3.826  34.285  19.159  1.00 38.54           N  
ANISOU  274  N   HIS A  47     4127   4236   6281   1085    108   -964       N  
ATOM    275  CA  HIS A  47      -4.350  34.167  17.808  1.00 38.81           C  
ANISOU  275  CA  HIS A  47     4129   4249   6367   1124    -31   -862       C  
ATOM    276  C   HIS A  47      -5.720  34.826  17.789  1.00 43.98           C  
ANISOU  276  C   HIS A  47     4619   4888   7203   1285    -94   -984       C  
ATOM    277  O   HIS A  47      -6.337  35.038  18.835  1.00 49.88           O  
ANISOU  277  O   HIS A  47     5250   5691   8013   1340      8  -1154       O  
ATOM    278  CB  HIS A  47      -4.437  32.705  17.361  1.00 37.58           C  
ANISOU  278  CB  HIS A  47     3939   4243   6099   1008     13   -789       C  
ATOM    279  CG  HIS A  47      -5.391  31.889  18.173  1.00 38.00           C  
ANISOU  279  CG  HIS A  47     3825   4457   6156    983    144   -912       C  
ATOM    280  ND1 HIS A  47      -6.718  31.742  17.834  1.00 39.32           N  
ANISOU  280  ND1 HIS A  47     3811   4693   6434   1053    107   -980       N  
ATOM    281  CD2 HIS A  47      -5.217  31.193  19.321  1.00 37.47           C  
ANISOU  281  CD2 HIS A  47     3746   4498   5994    889    311   -979       C  
ATOM    282  CE1 HIS A  47      -7.319  30.982  18.732  1.00 39.58           C  
ANISOU  282  CE1 HIS A  47     3721   4874   6442    991    260  -1084       C  
ATOM    283  NE2 HIS A  47      -6.430  30.635  19.644  1.00 38.48           N  
ANISOU  283  NE2 HIS A  47     3692   4759   6171    890    385  -1079       N  
ATOM    284  N   ASN A  48      -6.195  35.148  16.592  1.00 41.68           N  
ANISOU  284  N   ASN A  48     4316   4527   6992   1364   -266   -901       N  
ATOM    285  CA  ASN A  48      -7.452  35.870  16.460  1.00 43.88           C  
ANISOU  285  CA  ASN A  48     4439   4768   7464   1539   -364  -1009       C  
ATOM    286  C   ASN A  48      -8.668  34.957  16.386  1.00 44.45           C  
ANISOU  286  C   ASN A  48     4294   5018   7575   1543   -328  -1088       C  
ATOM    287  O   ASN A  48      -9.797  35.459  16.351  1.00 46.43           O  
ANISOU  287  O   ASN A  48     4376   5267   7998   1690   -397  -1202       O  
ATOM    288  CB  ASN A  48      -7.413  36.794  15.236  1.00 44.86           C  
ANISOU  288  CB  ASN A  48     4667   4711   7669   1637   -593   -881       C  
ATOM    289  CG  ASN A  48      -7.214  36.047  13.934  1.00 43.96           C  
ANISOU  289  CG  ASN A  48     4621   4638   7444   1551   -691   -702       C  
ATOM    290  OD1 ASN A  48      -7.222  34.817  13.896  1.00 51.66           O  
ANISOU  290  OD1 ASN A  48     5548   5775   8307   1434   -598   -687       O  
ATOM    291  ND2 ASN A  48      -7.039  36.794  12.851  1.00 44.78           N  
ANISOU  291  ND2 ASN A  48     4850   4592   7575   1608   -882   -565       N  
ATOM    292  N   GLY A  49      -8.468  33.642  16.363  1.00 42.93           N  
ANISOU  292  N   GLY A  49     4096   4974   7241   1387   -228  -1035       N  
ATOM    293  CA  GLY A  49      -9.589  32.717  16.362  1.00 43.54           C  
ANISOU  293  CA  GLY A  49     3968   5221   7354   1363   -180  -1112       C  
ATOM    294  C   GLY A  49     -10.434  32.768  15.112  1.00 44.69           C  
ANISOU  294  C   GLY A  49     4026   5354   7599   1449   -375  -1065       C  
ATOM    295  O   GLY A  49     -11.614  32.404  15.152  1.00 46.00           O  
ANISOU  295  O   GLY A  49     3974   5636   7869   1486   -370  -1173       O  
ATOM    296  N   LYS A  50      -9.864  33.216  13.997  1.00 44.40           N  
ANISOU  296  N   LYS A  50     4153   5187   7530   1476   -550   -908       N  
ATOM    297  CA  LYS A  50     -10.607  33.375  12.758  1.00 45.70           C  
ANISOU  297  CA  LYS A  50     4265   5325   7773   1565   -764   -849       C  
ATOM    298  C   LYS A  50      -9.783  32.845  11.594  1.00 44.34           C  
ANISOU  298  C   LYS A  50     4282   5134   7433   1456   -851   -654       C  
ATOM    299  O   LYS A  50      -8.550  32.834  11.640  1.00 42.78           O  
ANISOU  299  O   LYS A  50     4276   4880   7099   1360   -788   -555       O  
ATOM    300  CB  LYS A  50     -10.970  34.846  12.498  1.00 47.71           C  
ANISOU  300  CB  LYS A  50     4527   5403   8197   1765   -939   -867       C  
ATOM    301  CG  LYS A  50     -11.753  35.507  13.621  1.00 49.33           C  
ANISOU  301  CG  LYS A  50     4549   5611   8583   1897   -861  -1080       C  
ATOM    302  CD  LYS A  50     -11.850  37.010  13.412  1.00 54.92           C  
ANISOU  302  CD  LYS A  50     5316   6103   9450   2089  -1034  -1087       C  
ATOM    303  CE  LYS A  50     -12.470  37.689  14.621  1.00 65.30           C  
ANISOU  303  CE  LYS A  50     6467   7414  10932   2219   -933  -1318       C  
ATOM    304  NZ  LYS A  50     -12.445  39.175  14.509  1.00 88.29           N  
ANISOU  304  NZ  LYS A  50     9459  10085  14002   2404  -1097  -1332       N  
ATOM    305  N   LEU A  51     -10.478  32.406  10.548  1.00 45.11           N  
ANISOU  305  N   LEU A  51     4315   5286   7540   1472   -996   -612       N  
ATOM    306  CA  LEU A  51      -9.840  32.021   9.297  1.00 44.34           C  
ANISOU  306  CA  LEU A  51     4391   5170   7287   1391  -1106   -438       C  
ATOM    307  C   LEU A  51      -9.692  33.262   8.428  1.00 45.67           C  
ANISOU  307  C   LEU A  51     4698   5165   7492   1508  -1316   -322       C  
ATOM    308  O   LEU A  51     -10.687  33.909   8.085  1.00 58.10           O  
ANISOU  308  O   LEU A  51     6166   6691   9219   1662  -1486   -362       O  
ATOM    309  CB  LEU A  51     -10.656  30.948   8.580  1.00 46.43           C  
ANISOU  309  CB  LEU A  51     4533   5577   7532   1345  -1171   -453       C  
ATOM    310  CG  LEU A  51     -10.977  29.698   9.398  1.00 55.27           C  
ANISOU  310  CG  LEU A  51     5504   6861   8637   1225   -980   -567       C  
ATOM    311  CD1 LEU A  51     -11.758  28.715   8.549  1.00 54.94           C  
ANISOU  311  CD1 LEU A  51     5357   6935   8584   1175  -1073   -573       C  
ATOM    312  CD2 LEU A  51      -9.712  29.056   9.948  1.00 42.44           C  
ANISOU  312  CD2 LEU A  51     4033   5246   6845   1072   -796   -514       C  
ATOM    313  N   CYS A  52      -8.455  33.590   8.075  1.00 44.65           N  
ANISOU  313  N   CYS A  52     4801   4938   7227   1433  -1309   -179       N  
ATOM    314  CA  CYS A  52      -8.132  34.824   7.376  1.00 45.90           C  
ANISOU  314  CA  CYS A  52     5126   4910   7404   1514  -1480    -51       C  
ATOM    315  C   CYS A  52      -7.544  34.526   6.004  1.00 45.69           C  
ANISOU  315  C   CYS A  52     5282   4887   7189   1421  -1585    135       C  
ATOM    316  O   CYS A  52      -7.229  33.383   5.663  1.00 44.36           O  
ANISOU  316  O   CYS A  52     5123   4857   6873   1292  -1508    154       O  
ATOM    317  CB  CYS A  52      -7.148  35.673   8.188  1.00 45.31           C  
ANISOU  317  CB  CYS A  52     5173   4699   7342   1499  -1378    -44       C  
ATOM    318  SG  CYS A  52      -7.749  36.112   9.822  1.00 53.54           S  
ANISOU  318  SG  CYS A  52     6027   5735   8580   1607  -1248   -272       S  
ATOM    319  N   ARG A  53      -7.399  35.587   5.216  1.00 47.20           N  
ANISOU  319  N   ARG A  53     5629   4918   7386   1486  -1765    270       N  
ATOM    320  CA  ARG A  53      -6.721  35.484   3.935  1.00 47.25           C  
ANISOU  320  CA  ARG A  53     5843   4917   7194   1388  -1853    459       C  
ATOM    321  C   ARG A  53      -5.220  35.331   4.147  1.00 45.41           C  
ANISOU  321  C   ARG A  53     5771   4677   6805   1223  -1673    532       C  
ATOM    322  O   ARG A  53      -4.649  35.853   5.109  1.00 48.91           O  
ANISOU  322  O   ARG A  53     6229   5038   7318   1217  -1557    487       O  
ATOM    323  CB  ARG A  53      -7.004  36.720   3.084  1.00 49.77           C  
ANISOU  323  CB  ARG A  53     6297   5054   7561   1499  -2100    596       C  
ATOM    324  CG  ARG A  53      -8.472  37.091   2.997  1.00 55.04           C  
ANISOU  324  CG  ARG A  53     6793   5694   8425   1696  -2299    511       C  
ATOM    325  CD  ARG A  53      -8.645  38.486   2.422  1.00 61.09           C  
ANISOU  325  CD  ARG A  53     7705   6231   9274   1825  -2536    638       C  
ATOM    326  NE  ARG A  53     -10.049  38.871   2.327  1.00 72.38           N  
ANISOU  326  NE  ARG A  53     8962   7629  10911   2034  -2746    549       N  
ATOM    327  CZ  ARG A  53     -10.805  38.672   1.252  1.00 85.95           C  
ANISOU  327  CZ  ARG A  53    10670   9392  12594   2091  -2970    615       C  
ATOM    328  NH1 ARG A  53     -10.290  38.090   0.178  1.00 82.45           N  
ANISOU  328  NH1 ARG A  53    10393   9032  11902   1950  -3004    768       N  
ATOM    329  NH2 ARG A  53     -12.074  39.057   1.251  1.00 80.96           N  
ANISOU  329  NH2 ARG A  53     9857   8728  12175   2293  -3163    517       N  
ATOM    330  N   LEU A  54      -4.579  34.602   3.240  1.00 52.75           N  
ANISOU  330  N   LEU A  54     6814   5702   7527   1090  -1651    634       N  
ATOM    331  CA  LEU A  54      -3.133  34.402   3.274  1.00 53.91           C  
ANISOU  331  CA  LEU A  54     7104   5861   7520    931  -1490    704       C  
ATOM    332  C   LEU A  54      -2.517  35.296   2.204  1.00 65.33           C  
ANISOU  332  C   LEU A  54     8778   7190   8855    887  -1605    901       C  
ATOM    333  O   LEU A  54      -2.583  34.991   1.010  1.00 61.95           O  
ANISOU  333  O   LEU A  54     8442   6822   8273    845  -1704   1004       O  
ATOM    334  CB  LEU A  54      -2.779  32.936   3.056  1.00 52.24           C  
ANISOU  334  CB  LEU A  54     6853   5839   7156    810  -1365    662       C  
ATOM    335  CG  LEU A  54      -1.301  32.580   3.220  1.00 63.37           C  
ANISOU  335  CG  LEU A  54     8367   7283   8429    659  -1184    698       C  
ATOM    336  CD1 LEU A  54      -0.870  32.740   4.671  1.00 63.80           C  
ANISOU  336  CD1 LEU A  54     8348   7297   8597    661  -1031    595       C  
ATOM    337  CD2 LEU A  54      -1.033  31.169   2.723  1.00 74.56           C  
ANISOU  337  CD2 LEU A  54     9765   8871   9692    560  -1107    668       C  
ATOM    338  N   LYS A  54A     -1.919  36.406   2.644  1.00 67.88           N  
ANISOU  338  N   LYS A  54A    9198   7343   9249    890  -1591    953       N  
ATOM    339  CA  LYS A  54A     -1.308  37.392   1.752  1.00 68.44           C  
ANISOU  339  CA  LYS A  54A    9497   7274   9233    835  -1692   1150       C  
ATOM    340  C   LYS A  54A     -2.323  37.907   0.731  1.00 73.66           C  
ANISOU  340  C   LYS A  54A   10217   7864   9906    948  -1953   1251       C  
ATOM    341  O   LYS A  54A     -2.038  38.025  -0.462  1.00 76.59           O  
ANISOU  341  O   LYS A  54A   10763   8236  10101    873  -2046   1419       O  
ATOM    342  CB  LYS A  54A     -0.070  36.816   1.059  1.00 72.15           C  
ANISOU  342  CB  LYS A  54A   10098   7852   9464    639  -1564   1250       C  
ATOM    343  CG  LYS A  54A      0.968  36.252   2.019  1.00 76.95           C  
ANISOU  343  CG  LYS A  54A   10643   8535  10061    535  -1325   1150       C  
ATOM    344  CD  LYS A  54A      2.141  35.641   1.274  1.00 88.53           C  
ANISOU  344  CD  LYS A  54A   12214  10121  11304    357  -1204   1230       C  
ATOM    345  CE  LYS A  54A      3.088  34.922   2.222  1.00106.47           C  
ANISOU  345  CE  LYS A  54A   14396  12483  13575    274   -986   1113       C  
ATOM    346  NZ  LYS A  54A      3.640  35.827   3.272  1.00107.40           N  
ANISOU  346  NZ  LYS A  54A   14518  12458  13830    273   -927   1087       N  
ATOM    347  N   GLY A  55      -3.525  38.210   1.217  1.00 81.98           N  
ANISOU  347  N   GLY A  55    11119   8863  11168   1131  -2074   1143       N  
ATOM    348  CA  GLY A  55      -4.593  38.736   0.399  1.00 78.16           C  
ANISOU  348  CA  GLY A  55    10656   8301  10740   1271  -2342   1212       C  
ATOM    349  C   GLY A  55      -5.487  37.691  -0.239  1.00 81.34           C  
ANISOU  349  C   GLY A  55    10937   8891  11077   1300  -2424   1161       C  
ATOM    350  O   GLY A  55      -6.658  37.976  -0.511  1.00 91.33           O  
ANISOU  350  O   GLY A  55    12114  10121  12467   1460  -2632   1133       O  
ATOM    351  N   ILE A  56      -4.972  36.489  -0.483  1.00 71.45           N  
ANISOU  351  N   ILE A  56     9672   7831   9642   1155  -2274   1137       N  
ATOM    352  CA  ILE A  56      -5.742  35.459  -1.171  1.00 68.95           C  
ANISOU  352  CA  ILE A  56     9262   7689   9248   1162  -2354   1090       C  
ATOM    353  C   ILE A  56      -6.603  34.711  -0.161  1.00 63.21           C  
ANISOU  353  C   ILE A  56     8254   7066   8696   1235  -2271    872       C  
ATOM    354  O   ILE A  56      -6.108  34.222   0.861  1.00 64.43           O  
ANISOU  354  O   ILE A  56     8324   7273   8885   1172  -2049    764       O  
ATOM    355  CB  ILE A  56      -4.814  34.504  -1.937  1.00 69.70           C  
ANISOU  355  CB  ILE A  56     9479   7935   9071    976  -2237   1154       C  
ATOM    356  CG1 ILE A  56      -4.063  35.271  -3.028  1.00 78.49           C  
ANISOU  356  CG1 ILE A  56    10868   8961   9994    895  -2324   1376       C  
ATOM    357  CG2 ILE A  56      -5.609  33.366  -2.548  1.00 67.58           C  
ANISOU  357  CG2 ILE A  56     9102   7842   8732    978  -2309   1078       C  
ATOM    358  CD1 ILE A  56      -3.193  34.401  -3.914  1.00 86.58           C  
ANISOU  358  CD1 ILE A  56    12015  10143  10736    720  -2219   1435       C  
ATOM    359  N   ALA A  57      -7.897  34.623  -0.450  1.00 58.15           N  
ANISOU  359  N   ALA A  57     7469   6459   8166   1364  -2453    808       N  
ATOM    360  CA  ALA A  57      -8.863  34.000   0.438  1.00 55.48           C  
ANISOU  360  CA  ALA A  57     6851   6221   8009   1435  -2392    604       C  
ATOM    361  C   ALA A  57      -8.799  32.479   0.332  1.00 57.59           C  
ANISOU  361  C   ALA A  57     7037   6692   8152   1302  -2264    526       C  
ATOM    362  O   ALA A  57      -8.346  31.935  -0.677  1.00 56.12           O  
ANISOU  362  O   ALA A  57     6989   6577   7756   1198  -2297    618       O  
ATOM    363  CB  ALA A  57     -10.268  34.491   0.102  1.00 57.17           C  
ANISOU  363  CB  ALA A  57     6927   6399   8397   1621  -2646    561       C  
ATOM    364  N   PRO A  58      -9.238  31.763   1.374  1.00 50.26           N  
ANISOU  364  N   PRO A  58     5893   5858   7345   1296  -2112    352       N  
ATOM    365  CA  PRO A  58      -9.240  30.297   1.304  1.00 48.78           C  
ANISOU  365  CA  PRO A  58     5630   5843   7059   1169  -2002    277       C  
ATOM    366  C   PRO A  58     -10.512  29.732   0.694  1.00 48.34           C  
ANISOU  366  C   PRO A  58     5415   5891   7061   1218  -2170    205       C  
ATOM    367  O   PRO A  58     -11.375  30.478   0.220  1.00 53.35           O  
ANISOU  367  O   PRO A  58     6002   6470   7797   1357  -2391    224       O  
ATOM    368  CB  PRO A  58      -9.098  29.884   2.771  1.00 45.15           C  
ANISOU  368  CB  PRO A  58     5033   5418   6704   1131  -1763    141       C  
ATOM    369  CG  PRO A  58      -9.783  30.974   3.514  1.00 46.38           C  
ANISOU  369  CG  PRO A  58     5073   5474   7076   1288  -1811     76       C  
ATOM    370  CD  PRO A  58      -9.547  32.248   2.732  1.00 50.12           C  
ANISOU  370  CD  PRO A  58     5723   5786   7534   1380  -2000    225       C  
ATOM    371  N   LEU A  59     -10.634  28.409   0.709  1.00 47.37           N  
ANISOU  371  N   LEU A  59     5207   5912   6881   1105  -2077    120       N  
ATOM    372  CA  LEU A  59     -11.793  27.701   0.175  1.00 48.72           C  
ANISOU  372  CA  LEU A  59     5214   6195   7102   1119  -2217     35       C  
ATOM    373  C   LEU A  59     -12.512  27.020   1.335  1.00 48.22           C  
ANISOU  373  C   LEU A  59     4892   6215   7214   1099  -2067   -142       C  
ATOM    374  O   LEU A  59     -12.083  25.965   1.810  1.00 49.65           O  
ANISOU  374  O   LEU A  59     5064   6469   7333    961  -1881   -193       O  
ATOM    375  CB  LEU A  59     -11.368  26.693  -0.888  1.00 49.34           C  
ANISOU  375  CB  LEU A  59     5421   6366   6960    990  -2249     80       C  
ATOM    376  CG  LEU A  59     -12.444  25.735  -1.405  1.00 49.53           C  
ANISOU  376  CG  LEU A  59     5284   6518   7019    967  -2369    -24       C  
ATOM    377  CD1 LEU A  59     -13.535  26.491  -2.140  1.00 52.20           C  
ANISOU  377  CD1 LEU A  59     5548   6837   7448   1115  -2658     -7       C  
ATOM    378  CD2 LEU A  59     -11.835  24.672  -2.299  1.00 48.91           C  
ANISOU  378  CD2 LEU A  59     5350   6521   6712    826  -2355      1       C  
ATOM    379  N   GLN A  60     -13.602  27.631   1.795  1.00 53.27           N  
ANISOU  379  N   GLN A  60     5324   6843   8073   1235  -2146   -234       N  
ATOM    380  CA  GLN A  60     -14.434  27.030   2.830  1.00 54.87           C  
ANISOU  380  CA  GLN A  60     5260   7143   8444   1212  -2011   -407       C  
ATOM    381  C   GLN A  60     -15.389  26.029   2.193  1.00 54.74           C  
ANISOU  381  C   GLN A  60     5089   7260   8450   1157  -2120   -485       C  
ATOM    382  O   GLN A  60     -16.176  26.388   1.311  1.00 70.90           O  
ANISOU  382  O   GLN A  60     7078   9314  10549   1259  -2367   -478       O  
ATOM    383  CB  GLN A  60     -15.209  28.102   3.594  1.00 61.12           C  
ANISOU  383  CB  GLN A  60     5876   7880   9468   1383  -2037   -496       C  
ATOM    384  CG  GLN A  60     -14.403  28.812   4.669  1.00 67.18           C  
ANISOU  384  CG  GLN A  60     6727   8548  10250   1403  -1853   -488       C  
ATOM    385  CD  GLN A  60     -15.260  29.710   5.541  1.00 87.75           C  
ANISOU  385  CD  GLN A  60     9127  11121  13094   1563  -1850   -620       C  
ATOM    386  OE1 GLN A  60     -16.059  30.503   5.042  1.00 99.91           O  
ANISOU  386  OE1 GLN A  60    10582  12608  14771   1729  -2065   -634       O  
ATOM    387  NE2 GLN A  60     -15.103  29.584   6.854  1.00 88.54           N  
ANISOU  387  NE2 GLN A  60     9146  11253  13243   1518  -1609   -723       N  
ATOM    388  N   LEU A  61     -15.321  24.774   2.638  1.00 51.23           N  
ANISOU  388  N   LEU A  61     4582   6914   7968    996  -1949   -558       N  
ATOM    389  CA  LEU A  61     -16.158  23.729   2.066  1.00 63.02           C  
ANISOU  389  CA  LEU A  61     5939   8527   9480    916  -2039   -638       C  
ATOM    390  C   LEU A  61     -17.550  23.681   2.682  1.00 60.40           C  
ANISOU  390  C   LEU A  61     5275   8282   9392    961  -2045   -801       C  
ATOM    391  O   LEU A  61     -18.442  23.049   2.106  1.00 66.54           O  
ANISOU  391  O   LEU A  61     5903   9154  10225    927  -2174   -874       O  
ATOM    392  CB  LEU A  61     -15.483  22.364   2.226  1.00 49.03           C  
ANISOU  392  CB  LEU A  61     4255   6805   7571    717  -1866   -645       C  
ATOM    393  CG  LEU A  61     -14.140  22.169   1.520  1.00 47.47           C  
ANISOU  393  CG  LEU A  61     4357   6551   7130    654  -1854   -513       C  
ATOM    394  CD1 LEU A  61     -13.660  20.732   1.653  1.00 46.13           C  
ANISOU  394  CD1 LEU A  61     4236   6431   6862    474  -1710   -550       C  
ATOM    395  CD2 LEU A  61     -14.235  22.569   0.060  1.00 48.87           C  
ANISOU  395  CD2 LEU A  61     4650   6719   7197    721  -2112   -430       C  
ATOM    396  N   GLY A  62     -17.758  24.334   3.824  1.00 52.67           N  
ANISOU  396  N   GLY A  62     4172   7282   8560   1034  -1908   -869       N  
ATOM    397  CA  GLY A  62     -19.058  24.265   4.472  1.00 54.50           C  
ANISOU  397  CA  GLY A  62     4071   7615   9020   1067  -1881  -1039       C  
ATOM    398  C   GLY A  62     -19.344  22.861   4.968  1.00 66.70           C  
ANISOU  398  C   GLY A  62     5497   9282  10563    859  -1707  -1127       C  
ATOM    399  O   GLY A  62     -18.474  22.180   5.520  1.00 63.78           O  
ANISOU  399  O   GLY A  62     5271   8898  10063    715  -1505  -1084       O  
ATOM    400  N   ASN A  63     -20.580  22.410   4.758  1.00 69.46           N  
ANISOU  400  N   ASN A  63     5579   9747  11065    841  -1795  -1251       N  
ATOM    401  CA  ASN A  63     -20.988  21.063   5.138  1.00 66.28           C  
ANISOU  401  CA  ASN A  63     5048   9457  10680    631  -1654  -1336       C  
ATOM    402  C   ASN A  63     -20.556  20.006   4.130  1.00 56.81           C  
ANISOU  402  C   ASN A  63     4018   8255   9314    494  -1749  -1267       C  
ATOM    403  O   ASN A  63     -21.047  18.874   4.194  1.00 60.58           O  
ANISOU  403  O   ASN A  63     4379   8814   9823    327  -1697  -1343       O  
ATOM    404  CB  ASN A  63     -22.506  20.999   5.317  1.00 79.70           C  
ANISOU  404  CB  ASN A  63     6373  11288  12621    652  -1706  -1509       C  
ATOM    405  CG  ASN A  63     -23.024  22.034   6.290  1.00 98.89           C  
ANISOU  405  CG  ASN A  63     8608  13735  15232    799  -1612  -1608       C  
ATOM    406  OD1 ASN A  63     -22.321  22.449   7.212  1.00105.71           O  
ANISOU  406  OD1 ASN A  63     9583  14541  16042    811  -1417  -1577       O  
ATOM    407  ND2 ASN A  63     -24.265  22.460   6.086  1.00115.92           N  
ANISOU  407  ND2 ASN A  63    10464  15973  17608    918  -1757  -1740       N  
ATOM    408  N   CYS A  64     -19.659  20.344   3.211  1.00 54.37           N  
ANISOU  408  N   CYS A  64     3978   7853   8827    555  -1882  -1132       N  
ATOM    409  CA  CYS A  64     -19.235  19.453   2.141  1.00 53.93           C  
ANISOU  409  CA  CYS A  64     4092   7799   8601    449  -1989  -1078       C  
ATOM    410  C   CYS A  64     -17.839  18.916   2.425  1.00 51.30           C  
ANISOU  410  C   CYS A  64     4028   7393   8072    338  -1804   -983       C  
ATOM    411  O   CYS A  64     -16.970  19.645   2.913  1.00 49.86           O  
ANISOU  411  O   CYS A  64     3987   7128   7828    403  -1700   -900       O  
ATOM    412  CB  CYS A  64     -19.254  20.186   0.797  1.00 58.13           C  
ANISOU  412  CB  CYS A  64     4734   8297   9054    590  -2281   -998       C  
ATOM    413  SG  CYS A  64     -20.895  20.778   0.332  1.00 69.72           S  
ANISOU  413  SG  CYS A  64     5889   9845  10756    739  -2551  -1110       S  
ATOM    414  N   SER A  65     -17.631  17.637   2.124  1.00 50.84           N  
ANISOU  414  N   SER A  65     4030   7360   7926    172  -1770  -1003       N  
ATOM    415  CA  SER A  65     -16.318  17.030   2.249  1.00 48.62           C  
ANISOU  415  CA  SER A  65     3999   7010   7463     75  -1625   -924       C  
ATOM    416  C   SER A  65     -15.516  17.273   0.975  1.00 52.05           C  
ANISOU  416  C   SER A  65     4674   7402   7700    130  -1779   -826       C  
ATOM    417  O   SER A  65     -15.996  17.873   0.011  1.00 49.75           O  
ANISOU  417  O   SER A  65     4370   7134   7400    231  -2001   -809       O  
ATOM    418  CB  SER A  65     -16.438  15.536   2.542  1.00 50.60           C  
ANISOU  418  CB  SER A  65     4215   7288   7721   -123  -1518   -996       C  
ATOM    419  OG  SER A  65     -16.843  14.819   1.392  1.00 53.75           O  
ANISOU  419  OG  SER A  65     4616   7727   8078   -178  -1699  -1041       O  
ATOM    420  N   VAL A  66     -14.268  16.803   0.970  1.00 48.03           N  
ANISOU  420  N   VAL A  66     4388   6837   7025     60  -1661   -762       N  
ATOM    421  CA  VAL A  66     -13.455  16.886  -0.239  1.00 46.19           C  
ANISOU  421  CA  VAL A  66     4381   6583   6586     84  -1776   -683       C  
ATOM    422  C   VAL A  66     -14.074  16.048  -1.348  1.00 52.48           C  
ANISOU  422  C   VAL A  66     5153   7447   7338     22  -1953   -754       C  
ATOM    423  O   VAL A  66     -14.121  16.465  -2.513  1.00 48.84           O  
ANISOU  423  O   VAL A  66     4783   7011   6765     88  -2148   -713       O  
ATOM    424  CB  VAL A  66     -12.007  16.460   0.063  1.00 45.42           C  
ANISOU  424  CB  VAL A  66     4493   6422   6341     18  -1595   -625       C  
ATOM    425  CG1 VAL A  66     -11.219  16.291  -1.226  1.00 44.09           C  
ANISOU  425  CG1 VAL A  66     4538   6259   5956     12  -1691   -575       C  
ATOM    426  CG2 VAL A  66     -11.335  17.483   0.966  1.00 42.74           C  
ANISOU  426  CG2 VAL A  66     4201   6017   6023     96  -1462   -544       C  
ATOM    427  N   ALA A  67     -14.577  14.860  -1.002  1.00 62.79           N  
ANISOU  427  N   ALA A  67     6344   8784   8729   -112  -1895   -862       N  
ATOM    428  CA  ALA A  67     -15.245  14.016  -1.987  1.00 57.60           C  
ANISOU  428  CA  ALA A  67     5645   8189   8053   -183  -2067   -951       C  
ATOM    429  C   ALA A  67     -16.511  14.684  -2.511  1.00 57.45           C  
ANISOU  429  C   ALA A  67     5437   8243   8147    -89  -2293   -989       C  
ATOM    430  O   ALA A  67     -16.771  14.689  -3.719  1.00 56.35           O  
ANISOU  430  O   ALA A  67     5352   8147   7910    -59  -2513   -995       O  
ATOM    431  CB  ALA A  67     -15.567  12.652  -1.375  1.00 60.14           C  
ANISOU  431  CB  ALA A  67     5870   8509   8472   -356  -1949  -1056       C  
ATOM    432  N   GLY A  68     -17.316  15.250  -1.611  1.00 55.04           N  
ANISOU  432  N   GLY A  68     4907   7957   8048    -36  -2248  -1021       N  
ATOM    433  CA  GLY A  68     -18.525  15.929  -2.047  1.00 54.84           C  
ANISOU  433  CA  GLY A  68     4680   7998   8158     73  -2466  -1067       C  
ATOM    434  C   GLY A  68     -18.233  17.159  -2.886  1.00 55.31           C  
ANISOU  434  C   GLY A  68     4881   8025   8108    248  -2651   -951       C  
ATOM    435  O   GLY A  68     -18.946  17.451  -3.849  1.00 57.38           O  
ANISOU  435  O   GLY A  68     5094   8336   8371    322  -2911   -965       O  
ATOM    436  N   TRP A  69     -17.176  17.893  -2.533  1.00 53.54           N  
ANISOU  436  N   TRP A  69     4842   7715   7786    311  -2527   -831       N  
ATOM    437  CA  TRP A  69     -16.805  19.080  -3.298  1.00 54.01           C  
ANISOU  437  CA  TRP A  69     5064   7725   7734    458  -2687   -702       C  
ATOM    438  C   TRP A  69     -16.298  18.712  -4.686  1.00 55.32           C  
ANISOU  438  C   TRP A  69     5455   7914   7650    417  -2836   -647       C  
ATOM    439  O   TRP A  69     -16.651  19.365  -5.675  1.00 56.25           O  
ANISOU  439  O   TRP A  69     5627   8045   7702    515  -3081   -589       O  
ATOM    440  CB  TRP A  69     -15.753  19.883  -2.531  1.00 53.48           C  
ANISOU  440  CB  TRP A  69     5136   7557   7627    507  -2500   -595       C  
ATOM    441  CG  TRP A  69     -14.894  20.772  -3.388  1.00 51.97           C  
ANISOU  441  CG  TRP A  69     5204   7300   7242    584  -2599   -438       C  
ATOM    442  CD1 TRP A  69     -15.318  21.747  -4.244  1.00 53.86           C  
ANISOU  442  CD1 TRP A  69     5485   7520   7459    716  -2847   -360       C  
ATOM    443  CD2 TRP A  69     -13.461  20.783  -3.447  1.00 53.16           C  
ANISOU  443  CD2 TRP A  69     5606   7395   7195    528  -2450   -336       C  
ATOM    444  NE1 TRP A  69     -14.241  22.351  -4.844  1.00 53.30           N  
ANISOU  444  NE1 TRP A  69     5689   7384   7178    729  -2853   -207       N  
ATOM    445  CE2 TRP A  69     -13.089  21.780  -4.371  1.00 56.57           C  
ANISOU  445  CE2 TRP A  69     6225   7783   7487    614  -2605   -196       C  
ATOM    446  CE3 TRP A  69     -12.458  20.043  -2.813  1.00 51.67           C  
ANISOU  446  CE3 TRP A  69     5501   7191   6940    413  -2206   -349       C  
ATOM    447  CZ2 TRP A  69     -11.758  22.056  -4.676  1.00 49.79           C  
ANISOU  447  CZ2 TRP A  69     5618   6876   6424    575  -2507    -76       C  
ATOM    448  CZ3 TRP A  69     -11.137  20.319  -3.117  1.00 46.70           C  
ANISOU  448  CZ3 TRP A  69     5110   6514   6120    392  -2122   -240       C  
ATOM    449  CH2 TRP A  69     -10.799  21.317  -4.039  1.00 47.64           C  
ANISOU  449  CH2 TRP A  69     5398   6601   6102    466  -2263   -108       C  
ATOM    450  N   ILE A  70     -15.481  17.662  -4.785  1.00 58.63           N  
ANISOU  450  N   ILE A  70     6011   8340   7927    277  -2698   -668       N  
ATOM    451  CA  ILE A  70     -14.853  17.340  -6.060  1.00 55.19           C  
ANISOU  451  CA  ILE A  70     5806   7930   7233    238  -2804   -625       C  
ATOM    452  C   ILE A  70     -15.751  16.496  -6.957  1.00 60.17           C  
ANISOU  452  C   ILE A  70     6356   8654   7853    180  -3006   -739       C  
ATOM    453  O   ILE A  70     -15.543  16.470  -8.177  1.00 57.67           O  
ANISOU  453  O   ILE A  70     6206   8379   7328    182  -3168   -707       O  
ATOM    454  CB  ILE A  70     -13.503  16.641  -5.823  1.00 51.31           C  
ANISOU  454  CB  ILE A  70     5501   7402   6593    132  -2572   -609       C  
ATOM    455  CG1 ILE A  70     -12.531  16.964  -6.956  1.00 51.89           C  
ANISOU  455  CG1 ILE A  70     5848   7483   6386    145  -2630   -507       C  
ATOM    456  CG2 ILE A  70     -13.688  15.138  -5.680  1.00 51.14           C  
ANISOU  456  CG2 ILE A  70     5411   7412   6607    -13  -2501   -751       C  
ATOM    457  CD1 ILE A  70     -12.226  18.440  -7.084  1.00 55.72           C  
ANISOU  457  CD1 ILE A  70     6432   7914   6825    268  -2687   -346       C  
ATOM    458  N   LEU A  71     -16.749  15.813  -6.397  1.00 58.25           N  
ANISOU  458  N   LEU A  71     5862   8450   7821    119  -3000   -874       N  
ATOM    459  CA  LEU A  71     -17.676  15.020  -7.195  1.00 58.29           C  
ANISOU  459  CA  LEU A  71     5764   8542   7842     55  -3201   -996       C  
ATOM    460  C   LEU A  71     -18.888  15.811  -7.665  1.00 60.82           C  
ANISOU  460  C   LEU A  71     5911   8918   8280    181  -3476  -1006       C  
ATOM    461  O   LEU A  71     -19.642  15.314  -8.508  1.00 62.89           O  
ANISOU  461  O   LEU A  71     6107   9259   8530    148  -3693  -1094       O  
ATOM    462  CB  LEU A  71     -18.152  13.797  -6.404  1.00 58.03           C  
ANISOU  462  CB  LEU A  71     5546   8521   7981   -100  -3061  -1140       C  
ATOM    463  CG  LEU A  71     -17.173  12.631  -6.278  1.00 60.68           C  
ANISOU  463  CG  LEU A  71     6049   8809   8196   -247  -2874  -1172       C  
ATOM    464  CD1 LEU A  71     -17.757  11.547  -5.389  1.00 56.40           C  
ANISOU  464  CD1 LEU A  71     5317   8261   7853   -397  -2747  -1294       C  
ATOM    465  CD2 LEU A  71     -16.818  12.075  -7.649  1.00 57.35           C  
ANISOU  465  CD2 LEU A  71     5821   8425   7543   -285  -3028  -1203       C  
ATOM    466  N   GLY A  72     -19.096  17.016  -7.145  1.00 60.85           N  
ANISOU  466  N   GLY A  72     5839   8880   8403    329  -3485   -928       N  
ATOM    467  CA  GLY A  72     -20.245  17.807  -7.535  1.00 63.40           C  
ANISOU  467  CA  GLY A  72     5986   9242   8861    470  -3754   -943       C  
ATOM    468  C   GLY A  72     -21.506  17.412  -6.798  1.00 64.61           C  
ANISOU  468  C   GLY A  72     5775   9462   9313    442  -3748  -1105       C  
ATOM    469  O   GLY A  72     -22.541  17.158  -7.419  1.00 69.49           O  
ANISOU  469  O   GLY A  72     6226  10165  10012    448  -3982  -1201       O  
ATOM    470  N   ASN A  73     -21.428  17.344  -5.473  1.00 66.13           N  
ANISOU  470  N   ASN A  73     5837   9623   9665    403  -3480  -1141       N  
ATOM    471  CA  ASN A  73     -22.610  17.056  -4.679  1.00 64.35           C  
ANISOU  471  CA  ASN A  73     5257   9471   9724    370  -3441  -1291       C  
ATOM    472  C   ASN A  73     -23.625  18.186  -4.845  1.00 66.74           C  
ANISOU  472  C   ASN A  73     5353   9801  10204    572  -3668  -1310       C  
ATOM    473  O   ASN A  73     -23.247  19.361  -4.872  1.00 66.49           O  
ANISOU  473  O   ASN A  73     5435   9688  10138    740  -3718  -1194       O  
ATOM    474  CB  ASN A  73     -22.236  16.886  -3.206  1.00 62.45           C  
ANISOU  474  CB  ASN A  73     4952   9192   9584    296  -3100  -1307       C  
ATOM    475  CG  ASN A  73     -23.383  16.359  -2.365  1.00 63.64           C  
ANISOU  475  CG  ASN A  73     4751   9432   9997    208  -3012  -1468       C  
ATOM    476  OD1 ASN A  73     -24.340  17.078  -2.077  1.00 65.42           O  
ANISOU  476  OD1 ASN A  73     4719   9709  10428    328  -3093  -1536       O  
ATOM    477  ND2 ASN A  73     -23.286  15.099  -1.955  1.00 62.93           N  
ANISOU  477  ND2 ASN A  73     4647   9360   9904     -5  -2842  -1532       N  
ATOM    478  N   PRO A  74     -24.914  17.862  -4.979  1.00 71.93           N  
ANISOU  478  N   PRO A  74     5705  10564  11060    561  -3820  -1458       N  
ATOM    479  CA  PRO A  74     -25.910  18.913  -5.249  1.00 72.15           C  
ANISOU  479  CA  PRO A  74     5605  10597  11212    749  -3983  -1444       C  
ATOM    480  C   PRO A  74     -25.983  19.989  -4.179  1.00 78.71           C  
ANISOU  480  C   PRO A  74     6319  11372  12217    898  -3846  -1434       C  
ATOM    481  O   PRO A  74     -26.282  21.146  -4.501  1.00 83.69           O  
ANISOU  481  O   PRO A  74     6977  11944  12878   1094  -3995  -1364       O  
ATOM    482  CB  PRO A  74     -27.223  18.124  -5.348  1.00 77.95           C  
ANISOU  482  CB  PRO A  74     6079  11446  12094    643  -4008  -1587       C  
ATOM    483  CG  PRO A  74     -26.802  16.754  -5.768  1.00 73.46           C  
ANISOU  483  CG  PRO A  74     5614  10913  11386    425  -3986  -1631       C  
ATOM    484  CD  PRO A  74     -25.494  16.512  -5.075  1.00 74.34           C  
ANISOU  484  CD  PRO A  74     5880  10957  11409    355  -3784  -1589       C  
ATOM    485  N   GLU A  75     -25.717  19.653  -2.920  1.00 93.67           N  
ANISOU  485  N   GLU A  75     8094  13276  14220    808  -3566  -1504       N  
ATOM    486  CA  GLU A  75     -25.719  20.639  -1.847  1.00 97.80           C  
ANISOU  486  CA  GLU A  75     8519  13750  14892    940  -3413  -1507       C  
ATOM    487  C   GLU A  75     -24.424  21.442  -1.773  1.00 87.91           C  
ANISOU  487  C   GLU A  75     7566  12358  13477   1032  -3366  -1345       C  
ATOM    488  O   GLU A  75     -24.230  22.191  -0.810  1.00 83.57           O  
ANISOU  488  O   GLU A  75     6980  11752  13022   1119  -3203  -1343       O  
ATOM    489  CB  GLU A  75     -25.982  19.953  -0.504  1.00101.07           C  
ANISOU  489  CB  GLU A  75     8710  14237  15456    789  -3100  -1637       C  
ATOM    490  CG  GLU A  75     -27.373  19.346  -0.366  1.00 98.94           C  
ANISOU  490  CG  GLU A  75     8157  14089  15349    695  -3070  -1776       C  
ATOM    491  CD  GLU A  75     -28.443  20.372  -0.028  1.00105.17           C  
ANISOU  491  CD  GLU A  75     8736  14894  16329    874  -3096  -1836       C  
ATOM    492  OE1 GLU A  75     -28.590  21.363  -0.773  1.00103.40           O  
ANISOU  492  OE1 GLU A  75     8593  14604  16090   1074  -3328  -1767       O  
ATOM    493  OE2 GLU A  75     -29.136  20.186   0.994  1.00110.03           O  
ANISOU  493  OE2 GLU A  75     9115  15587  17103    809  -2880  -1953       O  
ATOM    494  N   CYS A  76     -23.540  21.313  -2.765  1.00 75.32           N  
ANISOU  494  N   CYS A  76     6293  10705  11620   1002  -3471  -1204       N  
ATOM    495  CA  CYS A  76     -22.259  22.010  -2.764  1.00 79.63           C  
ANISOU  495  CA  CYS A  76     7161  11118  11977   1052  -3388  -1031       C  
ATOM    496  C   CYS A  76     -22.100  22.922  -3.976  1.00 79.04           C  
ANISOU  496  C   CYS A  76     7284  10973  11773   1204  -3689   -891       C  
ATOM    497  O   CYS A  76     -20.975  23.305  -4.315  1.00 83.63           O  
ANISOU  497  O   CYS A  76     8174  11461  12141   1203  -3654   -733       O  
ATOM    498  CB  CYS A  76     -21.109  21.001  -2.693  1.00 77.27           C  
ANISOU  498  CB  CYS A  76     7095  10808  11457    853  -3170   -978       C  
ATOM    499  SG  CYS A  76     -21.317  19.772  -1.376  1.00 74.74           S  
ANISOU  499  SG  CYS A  76     6574  10561  11263    650  -2847  -1123       S  
ATOM    500  N   GLU A  77     -23.208  23.291  -4.627  1.00 86.25           N  
ANISOU  500  N   GLU A  77     8025  11932  12814   1331  -3988   -944       N  
ATOM    501  CA  GLU A  77     -23.142  24.158  -5.799  1.00 90.56           C  
ANISOU  501  CA  GLU A  77     8776  12407  13227   1470  -4282   -797       C  
ATOM    502  C   GLU A  77     -22.488  25.499  -5.498  1.00 82.71           C  
ANISOU  502  C   GLU A  77     7945  11252  12231   1628  -4277   -658       C  
ATOM    503  O   GLU A  77     -21.960  26.138  -6.415  1.00 80.14           O  
ANISOU  503  O   GLU A  77     7899  10840  11712   1685  -4442   -484       O  
ATOM    504  CB  GLU A  77     -24.544  24.393  -6.365  1.00102.63           C  
ANISOU  504  CB  GLU A  77    10129  13988  14877   1553  -4469   -859       C  
ATOM    505  CG  GLU A  77     -25.208  23.156  -6.940  1.00109.35           C  
ANISOU  505  CG  GLU A  77    10864  14984  15699   1401  -4530   -971       C  
ATOM    506  CD  GLU A  77     -26.556  23.465  -7.560  1.00129.24           C  
ANISOU  506  CD  GLU A  77    13222  17551  18332   1495  -4738  -1019       C  
ATOM    507  OE1 GLU A  77     -26.924  24.658  -7.617  1.00134.85           O  
ANISOU  507  OE1 GLU A  77    13934  18174  19128   1683  -4848   -957       O  
ATOM    508  OE2 GLU A  77     -27.248  22.518  -7.989  1.00130.88           O  
ANISOU  508  OE2 GLU A  77    13303  17877  18548   1380  -4795  -1122       O  
ATOM    509  N   LEU A  78     -22.510  25.939  -4.238  1.00 68.33           N  
ANISOU  509  N   LEU A  78     5975   9384  10602   1680  -4065   -725       N  
ATOM    510  CA  LEU A  78     -21.873  27.199  -3.876  1.00 72.45           C  
ANISOU  510  CA  LEU A  78     6657   9739  11129   1816  -4033   -604       C  
ATOM    511  C   LEU A  78     -20.362  27.152  -4.051  1.00 80.93           C  
ANISOU  511  C   LEU A  78     8095  10734  11920   1696  -3873   -433       C  
ATOM    512  O   LEU A  78     -19.723  28.207  -4.121  1.00 87.25           O  
ANISOU  512  O   LEU A  78     9098  11387  12664   1789  -3906   -291       O  
ATOM    513  CB  LEU A  78     -22.208  27.559  -2.429  1.00 81.15           C  
ANISOU  513  CB  LEU A  78     7519  10828  12487   1878  -3813   -740       C  
ATOM    514  CG  LEU A  78     -23.679  27.480  -2.018  1.00 78.12           C  
ANISOU  514  CG  LEU A  78     6780  10545  12359   1933  -3819   -928       C  
ATOM    515  CD1 LEU A  78     -23.839  27.854  -0.551  1.00 80.19           C  
ANISOU  515  CD1 LEU A  78     6847  10797  12827   1978  -3565  -1055       C  
ATOM    516  CD2 LEU A  78     -24.534  28.371  -2.904  1.00 79.90           C  
ANISOU  516  CD2 LEU A  78     7023  10712  12625   2094  -4084   -877       C  
ATOM    517  N   LEU A  79     -19.779  25.958  -4.125  1.00 75.26           N  
ANISOU  517  N   LEU A  79     7459  10105  11032   1491  -3702   -449       N  
ATOM    518  CA  LEU A  79     -18.335  25.790  -4.193  1.00 64.28           C  
ANISOU  518  CA  LEU A  79     6374   8658   9391   1370  -3519   -318       C  
ATOM    519  C   LEU A  79     -17.812  25.693  -5.619  1.00 61.50           C  
ANISOU  519  C   LEU A  79     6298   8311   8758   1325  -3700   -178       C  
ATOM    520  O   LEU A  79     -16.594  25.624  -5.813  1.00 66.57           O  
ANISOU  520  O   LEU A  79     7199   8914   9182   1231  -3565    -65       O  
ATOM    521  CB  LEU A  79     -17.918  24.542  -3.408  1.00 58.55           C  
ANISOU  521  CB  LEU A  79     5590   8013   8642   1180  -3222   -419       C  
ATOM    522  CG  LEU A  79     -17.708  24.640  -1.894  1.00 61.11           C  
ANISOU  522  CG  LEU A  79     5795   8307   9118   1166  -2938   -490       C  
ATOM    523  CD1 LEU A  79     -18.855  25.348  -1.181  1.00 70.29           C  
ANISOU  523  CD1 LEU A  79     6669   9470  10570   1318  -2991   -605       C  
ATOM    524  CD2 LEU A  79     -17.519  23.246  -1.327  1.00 58.56           C  
ANISOU  524  CD2 LEU A  79     5407   8076   8768    972  -2710   -588       C  
ATOM    525  N   ILE A  80     -18.695  25.689  -6.618  1.00 72.22           N  
ANISOU  525  N   ILE A  80     7604   9725  10112   1390  -4001   -188       N  
ATOM    526  CA  ILE A  80     -18.248  25.542  -7.998  1.00 76.73           C  
ANISOU  526  CA  ILE A  80     8441  10320  10392   1338  -4175    -64       C  
ATOM    527  C   ILE A  80     -17.570  26.813  -8.494  1.00 78.15           C  
ANISOU  527  C   ILE A  80     8896  10359  10438   1432  -4279    150       C  
ATOM    528  O   ILE A  80     -16.619  26.751  -9.283  1.00 75.92           O  
ANISOU  528  O   ILE A  80     8904  10074   9869   1339  -4264    283       O  
ATOM    529  CB  ILE A  80     -19.435  25.150  -8.895  1.00 91.00           C  
ANISOU  529  CB  ILE A  80    10108  12234  12232   1378  -4482   -145       C  
ATOM    530  CG1 ILE A  80     -20.185  23.962  -8.290  1.00 95.35           C  
ANISOU  530  CG1 ILE A  80    10358  12913  12959   1279  -4372   -363       C  
ATOM    531  CG2 ILE A  80     -18.954  24.814 -10.296  1.00 99.41           C  
ANISOU  531  CG2 ILE A  80    11453  13352  12967   1296  -4637    -41       C  
ATOM    532  CD1 ILE A  80     -21.419  23.561  -9.062  1.00101.67           C  
ANISOU  532  CD1 ILE A  80    10976  13823  13831   1311  -4668   -467       C  
ATOM    533  N   SER A  81     -18.031  27.982  -8.041  1.00 89.10           N  
ANISOU  533  N   SER A  81    10200  11624  12031   1611  -4380    182       N  
ATOM    534  CA  SER A  81     -17.488  29.242  -8.535  1.00 89.13           C  
ANISOU  534  CA  SER A  81    10466  11470  11930   1704  -4511    392       C  
ATOM    535  C   SER A  81     -16.076  29.516  -8.033  1.00 83.43           C  
ANISOU  535  C   SER A  81     9960  10658  11080   1605  -4229    498       C  
ATOM    536  O   SER A  81     -15.387  30.371  -8.599  1.00 84.55           O  
ANISOU  536  O   SER A  81    10373  10687  11064   1618  -4302    691       O  
ATOM    537  CB  SER A  81     -18.410  30.399  -8.146  1.00 92.82           C  
ANISOU  537  CB  SER A  81    10773  11814  12679   1932  -4697    378       C  
ATOM    538  OG  SER A  81     -18.590  30.464  -6.743  1.00 97.48           O  
ANISOU  538  OG  SER A  81    11125  12381  13531   1974  -4476    232       O  
ATOM    539  N   ARG A  82     -15.629  28.813  -6.997  1.00 69.94           N  
ANISOU  539  N   ARG A  82     8143   8998   9434   1499  -3917    382       N  
ATOM    540  CA  ARG A  82     -14.293  29.023  -6.451  1.00 69.63           C  
ANISOU  540  CA  ARG A  82     8283   8883   9290   1406  -3651    464       C  
ATOM    541  C   ARG A  82     -13.278  28.221  -7.256  1.00 72.88           C  
ANISOU  541  C   ARG A  82     8923   9382   9388   1226  -3557    534       C  
ATOM    542  O   ARG A  82     -13.356  26.989  -7.313  1.00 74.78           O  
ANISOU  542  O   ARG A  82     9081   9757   9575   1116  -3470    414       O  
ATOM    543  CB  ARG A  82     -14.248  28.618  -4.980  1.00 68.52           C  
ANISOU  543  CB  ARG A  82     7934   8756   9343   1377  -3372    311       C  
ATOM    544  CG  ARG A  82     -15.168  29.425  -4.077  1.00 71.77           C  
ANISOU  544  CG  ARG A  82     8116   9092  10062   1549  -3421    221       C  
ATOM    545  CD  ARG A  82     -14.776  30.891  -4.063  1.00 76.52           C  
ANISOU  545  CD  ARG A  82     8879   9501  10695   1673  -3506    365       C  
ATOM    546  NE  ARG A  82     -13.351  31.072  -3.797  1.00 70.36           N  
ANISOU  546  NE  ARG A  82     8329   8651   9755   1557  -3290    474       N  
ATOM    547  CZ  ARG A  82     -12.812  31.083  -2.583  1.00 64.15           C  
ANISOU  547  CZ  ARG A  82     7485   7831   9056   1520  -3032    405       C  
ATOM    548  NH1 ARG A  82     -13.579  30.917  -1.515  1.00 63.20           N  
ANISOU  548  NH1 ARG A  82     7096   7748   9169   1584  -2943    229       N  
ATOM    549  NH2 ARG A  82     -11.506  31.256  -2.436  1.00 66.25           N  
ANISOU  549  NH2 ARG A  82     7959   8038   9174   1415  -2861    507       N  
ATOM    550  N   GLU A  83     -12.324  28.917  -7.877  1.00 74.44           N  
ANISOU  550  N   GLU A  83     9405   9498   9379   1193  -3569    721       N  
ATOM    551  CA  GLU A  83     -11.273  28.263  -8.644  1.00 65.80           C  
ANISOU  551  CA  GLU A  83     8533   8490   7980   1025  -3461    785       C  
ATOM    552  C   GLU A  83      -9.877  28.743  -8.268  1.00 67.13           C  
ANISOU  552  C   GLU A  83     8884   8574   8048    943  -3233    895       C  
ATOM    553  O   GLU A  83      -8.923  28.444  -8.991  1.00 70.60           O  
ANISOU  553  O   GLU A  83     9529   9070   8225    815  -3154    973       O  
ATOM    554  CB  GLU A  83     -11.499  28.459 -10.146  1.00 64.97           C  
ANISOU  554  CB  GLU A  83     8620   8425   7642   1028  -3730    909       C  
ATOM    555  CG  GLU A  83     -12.704  27.712 -10.680  1.00 81.97           C  
ANISOU  555  CG  GLU A  83    10610  10699   9834   1066  -3942    785       C  
ATOM    556  CD  GLU A  83     -12.753  27.691 -12.191  1.00 84.96           C  
ANISOU  556  CD  GLU A  83    11206  11147   9926   1034  -4176    893       C  
ATOM    557  OE1 GLU A  83     -12.057  28.514 -12.822  1.00 92.48           O  
ANISOU  557  OE1 GLU A  83    12428  12029  10682   1016  -4221   1090       O  
ATOM    558  OE2 GLU A  83     -13.485  26.845 -12.746  1.00 78.66           O  
ANISOU  558  OE2 GLU A  83    10314  10479   9094   1017  -4313    780       O  
ATOM    559  N   SER A  83A     -9.729  29.475  -7.166  1.00 66.78           N  
ANISOU  559  N   SER A  83A    8765   8403   8205   1010  -3125    891       N  
ATOM    560  CA  SER A  83A     -8.413  29.870  -6.685  1.00 62.79           C  
ANISOU  560  CA  SER A  83A    8403   7822   7632    925  -2900    971       C  
ATOM    561  C   SER A  83A     -8.510  30.149  -5.193  1.00 64.61           C  
ANISOU  561  C   SER A  83A    8450   7971   8126    990  -2747    867       C  
ATOM    562  O   SER A  83A     -9.479  30.759  -4.735  1.00 75.10           O  
ANISOU  562  O   SER A  83A    9632   9226   9678   1138  -2873    821       O  
ATOM    563  CB  SER A  83A     -7.881  31.103  -7.425  1.00 63.64           C  
ANISOU  563  CB  SER A  83A    8771   7801   7608    933  -3019   1192       C  
ATOM    564  OG  SER A  83A     -8.478  32.292  -6.943  1.00 68.46           O  
ANISOU  564  OG  SER A  83A    9335   8240   8439   1091  -3156   1235       O  
ATOM    565  N   TRP A  84      -7.503  29.704  -4.445  1.00 53.17           N  
ANISOU  565  N   TRP A  84     7011   6543   6650    882  -2480    824       N  
ATOM    566  CA  TRP A  84      -7.522  29.840  -2.996  1.00 55.32           C  
ANISOU  566  CA  TRP A  84     7121   6759   7139    924  -2317    717       C  
ATOM    567  C   TRP A  84      -6.107  29.702  -2.461  1.00 48.92           C  
ANISOU  567  C   TRP A  84     6416   5935   6236    802  -2068    742       C  
ATOM    568  O   TRP A  84      -5.222  29.158  -3.126  1.00 50.28           O  
ANISOU  568  O   TRP A  84     6728   6180   6197    678  -1991    793       O  
ATOM    569  CB  TRP A  84      -8.434  28.794  -2.351  1.00 54.52           C  
ANISOU  569  CB  TRP A  84     6765   6770   7179    937  -2268    528       C  
ATOM    570  CG  TRP A  84      -8.073  27.403  -2.753  1.00 54.22           C  
ANISOU  570  CG  TRP A  84     6741   6877   6983    799  -2172    470       C  
ATOM    571  CD1 TRP A  84      -7.162  26.584  -2.152  1.00 51.42           C  
ANISOU  571  CD1 TRP A  84     6398   6568   6573    683  -1937    415       C  
ATOM    572  CD2 TRP A  84      -8.599  26.670  -3.865  1.00 48.17           C  
ANISOU  572  CD2 TRP A  84     5986   6219   6096    768  -2322    455       C  
ATOM    573  NE1 TRP A  84      -7.095  25.385  -2.816  1.00 46.17           N  
ANISOU  573  NE1 TRP A  84     5749   6023   5770    587  -1928    363       N  
ATOM    574  CE2 TRP A  84      -7.969  25.412  -3.871  1.00 46.65           C  
ANISOU  574  CE2 TRP A  84     5812   6128   5786    632  -2158    382       C  
ATOM    575  CE3 TRP A  84      -9.547  26.954  -4.852  1.00 50.51           C  
ANISOU  575  CE3 TRP A  84     6281   6534   6376    846  -2590    490       C  
ATOM    576  CZ2 TRP A  84      -8.254  24.439  -4.826  1.00 49.78           C  
ANISOU  576  CZ2 TRP A  84     6226   6640   6049    569  -2245    335       C  
ATOM    577  CZ3 TRP A  84      -9.829  25.989  -5.799  1.00 51.22           C  
ANISOU  577  CZ3 TRP A  84     6389   6751   6324    777  -2680    448       C  
ATOM    578  CH2 TRP A  84      -9.185  24.746  -5.779  1.00 49.66           C  
ANISOU  578  CH2 TRP A  84     6210   6649   6009    638  -2504    366       C  
ATOM    579  N   SER A  85      -5.911  30.195  -1.240  1.00 56.99           N  
ANISOU  579  N   SER A  85     7361   6870   7422    841  -1944    692       N  
ATOM    580  CA  SER A  85      -4.634  30.053  -0.555  1.00 53.55           C  
ANISOU  580  CA  SER A  85     6992   6423   6933    737  -1713    694       C  
ATOM    581  C   SER A  85      -4.532  28.752   0.228  1.00 49.77           C  
ANISOU  581  C   SER A  85     6374   6061   6475    667  -1531    546       C  
ATOM    582  O   SER A  85      -3.424  28.233   0.408  1.00 51.76           O  
ANISOU  582  O   SER A  85     6697   6349   6619    558  -1366    548       O  
ATOM    583  CB  SER A  85      -4.405  31.240   0.383  1.00 54.94           C  
ANISOU  583  CB  SER A  85     7171   6442   7261    806  -1676    712       C  
ATOM    584  OG  SER A  85      -5.525  31.446   1.225  1.00 57.37           O  
ANISOU  584  OG  SER A  85     7282   6724   7792    935  -1719    590       O  
ATOM    585  N   TYR A  86      -5.655  28.215   0.692  1.00 43.06           N  
ANISOU  585  N   TYR A  86     5327   5268   5764    724  -1562    420       N  
ATOM    586  CA  TYR A  86      -5.691  26.928   1.381  1.00 40.44           C  
ANISOU  586  CA  TYR A  86     4871   5041   5453    649  -1409    290       C  
ATOM    587  C   TYR A  86      -7.146  26.479   1.457  1.00 41.48           C  
ANISOU  587  C   TYR A  86     4800   5239   5721    710  -1509    180       C  
ATOM    588  O   TYR A  86      -8.063  27.216   1.083  1.00 43.24           O  
ANISOU  588  O   TYR A  86     4966   5425   6037    823  -1689    194       O  
ATOM    589  CB  TYR A  86      -5.047  27.009   2.767  1.00 38.83           C  
ANISOU  589  CB  TYR A  86     4631   4794   5327    626  -1209    239       C  
ATOM    590  CG  TYR A  86      -5.695  28.004   3.705  1.00 43.80           C  
ANISOU  590  CG  TYR A  86     5153   5339   6151    743  -1224    193       C  
ATOM    591  CD1 TYR A  86      -5.389  29.357   3.638  1.00 40.22           C  
ANISOU  591  CD1 TYR A  86     4800   4750   5730    816  -1293    281       C  
ATOM    592  CD2 TYR A  86      -6.604  27.587   4.668  1.00 39.40           C  
ANISOU  592  CD2 TYR A  86     4394   4834   5743    775  -1163     55       C  
ATOM    593  CE1 TYR A  86      -5.978  30.268   4.497  1.00 40.93           C  
ANISOU  593  CE1 TYR A  86     4792   4754   6006    934  -1309    221       C  
ATOM    594  CE2 TYR A  86      -7.196  28.490   5.530  1.00 40.14           C  
ANISOU  594  CE2 TYR A  86     4380   4862   6009    886  -1164     -7       C  
ATOM    595  CZ  TYR A  86      -6.880  29.828   5.441  1.00 40.89           C  
ANISOU  595  CZ  TYR A  86     4577   4817   6142    973  -1241     69       C  
ATOM    596  OH  TYR A  86      -7.467  30.730   6.298  1.00 51.29           O  
ANISOU  596  OH  TYR A  86     5789   6060   7640   1094  -1245    -11       O  
ATOM    597  N   ILE A  87      -7.351  25.263   1.956  1.00 40.55           N  
ANISOU  597  N   ILE A  87     4569   5214   5623    631  -1397     70       N  
ATOM    598  CA  ILE A  87      -8.660  24.620   1.963  1.00 41.55           C  
ANISOU  598  CA  ILE A  87     4500   5424   5865    648  -1472    -41       C  
ATOM    599  C   ILE A  87      -9.052  24.306   3.400  1.00 42.00           C  
ANISOU  599  C   ILE A  87     4383   5500   6077    636  -1308   -158       C  
ATOM    600  O   ILE A  87      -8.263  23.725   4.154  1.00 46.27           O  
ANISOU  600  O   ILE A  87     4966   6044   6571    546  -1125   -174       O  
ATOM    601  CB  ILE A  87      -8.663  23.345   1.102  1.00 41.54           C  
ANISOU  601  CB  ILE A  87     4528   5520   5735    542  -1505    -68       C  
ATOM    602  CG1 ILE A  87      -8.326  23.694  -0.348  1.00 43.59           C  
ANISOU  602  CG1 ILE A  87     4965   5777   5819    553  -1669     43       C  
ATOM    603  CG2 ILE A  87     -10.010  22.643   1.184  1.00 42.65           C  
ANISOU  603  CG2 ILE A  87     4452   5744   6008    540  -1575   -190       C  
ATOM    604  CD1 ILE A  87      -8.222  22.497  -1.263  1.00 49.47           C  
ANISOU  604  CD1 ILE A  87     5763   6617   6414    453  -1701      8       C  
ATOM    605  N   VAL A  88     -10.272  24.687   3.770  1.00 42.22           N  
ANISOU  605  N   VAL A  88     4213   5545   6285    726  -1376   -241       N  
ATOM    606  CA  VAL A  88     -10.834  24.408   5.085  1.00 42.01           C  
ANISOU  606  CA  VAL A  88     3999   5559   6404    712  -1223   -364       C  
ATOM    607  C   VAL A  88     -11.976  23.420   4.909  1.00 43.07           C  
ANISOU  607  C   VAL A  88     3941   5808   6615    658  -1266   -469       C  
ATOM    608  O   VAL A  88     -12.924  23.680   4.158  1.00 44.87           O  
ANISOU  608  O   VAL A  88     4066   6065   6916    736  -1456   -492       O  
ATOM    609  CB  VAL A  88     -11.325  25.686   5.783  1.00 44.28           C  
ANISOU  609  CB  VAL A  88     4188   5782   6855    858  -1238   -402       C  
ATOM    610  CG1 VAL A  88     -11.904  25.346   7.151  1.00 42.94           C  
ANISOU  610  CG1 VAL A  88     3824   5677   6813    829  -1058   -541       C  
ATOM    611  CG2 VAL A  88     -10.197  26.696   5.907  1.00 42.13           C  
ANISOU  611  CG2 VAL A  88     4113   5381   6514    901  -1210   -298       C  
ATOM    612  N   GLU A  89     -11.884  22.290   5.599  1.00 42.11           N  
ANISOU  612  N   GLU A  89     3775   5747   6480    522  -1100   -529       N  
ATOM    613  CA  GLU A  89     -12.943  21.297   5.656  1.00 43.12           C  
ANISOU  613  CA  GLU A  89     3711   5978   6696    441  -1102   -636       C  
ATOM    614  C   GLU A  89     -13.381  21.141   7.103  1.00 61.18           C  
ANISOU  614  C   GLU A  89     5838   8307   9102    399   -905   -732       C  
ATOM    615  O   GLU A  89     -12.544  21.110   8.009  1.00 67.25           O  
ANISOU  615  O   GLU A  89     6706   9036   9809    354   -733   -705       O  
ATOM    616  CB  GLU A  89     -12.467  19.950   5.089  1.00 42.32           C  
ANISOU  616  CB  GLU A  89     3717   5904   6460    293  -1088   -619       C  
ATOM    617  CG  GLU A  89     -13.310  18.756   5.506  1.00 42.98           C  
ANISOU  617  CG  GLU A  89     3631   6070   6628    162  -1021   -724       C  
ATOM    618  CD  GLU A  89     -12.806  17.448   4.925  1.00 43.95           C  
ANISOU  618  CD  GLU A  89     3876   6194   6628     24  -1020   -713       C  
ATOM    619  OE1 GLU A  89     -13.188  17.117   3.784  1.00 43.34           O  
ANISOU  619  OE1 GLU A  89     3799   6150   6518     19  -1190   -727       O  
ATOM    620  OE2 GLU A  89     -12.023  16.753   5.608  1.00 56.57           O  
ANISOU  620  OE2 GLU A  89     5574   7757   8162    -74   -859   -694       O  
ATOM    621  N   LYS A  90     -14.691  21.068   7.325  1.00 65.37           N  
ANISOU  621  N   LYS A  90     6117   8923   9796    413   -932   -846       N  
ATOM    622  CA  LYS A  90     -15.188  20.880   8.677  1.00 67.89           C  
ANISOU  622  CA  LYS A  90     6273   9304  10218    356   -732   -946       C  
ATOM    623  C   LYS A  90     -14.707  19.534   9.223  1.00 67.11           C  
ANISOU  623  C   LYS A  90     6250   9227  10021    157   -562   -933       C  
ATOM    624  O   LYS A  90     -14.503  18.586   8.458  1.00 58.55           O  
ANISOU  624  O   LYS A  90     5247   8142   8859     61   -629   -899       O  
ATOM    625  CB  LYS A  90     -16.712  20.961   8.705  1.00 80.25           C  
ANISOU  625  CB  LYS A  90     7535  10975  11981    394   -792  -1081       C  
ATOM    626  CG  LYS A  90     -17.246  22.342   8.353  1.00 89.09           C  
ANISOU  626  CG  LYS A  90     8560  12062  13226    611   -954  -1109       C  
ATOM    627  CD  LYS A  90     -16.565  23.425   9.176  1.00 92.35           C  
ANISOU  627  CD  LYS A  90     9071  12387  13630    716   -852  -1085       C  
ATOM    628  CE  LYS A  90     -16.784  24.804   8.575  1.00 89.75           C  
ANISOU  628  CE  LYS A  90     8740  11970  13390    934  -1055  -1066       C  
ATOM    629  NZ  LYS A  90     -18.228  25.140   8.468  1.00 84.13           N  
ANISOU  629  NZ  LYS A  90     7731  11338  12896   1043  -1167  -1204       N  
ATOM    630  N   PRO A  91     -14.496  19.435  10.543  1.00 80.85           N  
ANISOU  630  N   PRO A  91     7979  10980  11759     94   -349   -959       N  
ATOM    631  CA  PRO A  91     -13.893  18.208  11.103  1.00 85.34           C  
ANISOU  631  CA  PRO A  91     8662  11543  12221    -87   -201   -922       C  
ATOM    632  C   PRO A  91     -14.549  16.920  10.639  1.00 83.67           C  
ANISOU  632  C   PRO A  91     8368  11385  12037   -237   -235   -957       C  
ATOM    633  O   PRO A  91     -13.850  15.968  10.269  1.00 88.75           O  
ANISOU  633  O   PRO A  91     9173  11975  12571   -337   -243   -897       O  
ATOM    634  CB  PRO A  91     -14.037  18.422  12.615  1.00 89.42           C  
ANISOU  634  CB  PRO A  91     9106  12101  12768   -122     13   -974       C  
ATOM    635  CG  PRO A  91     -14.006  19.894  12.778  1.00 88.14           C  
ANISOU  635  CG  PRO A  91     8918  11911  12662     64    -22   -997       C  
ATOM    636  CD  PRO A  91     -14.722  20.457  11.579  1.00 84.22           C  
ANISOU  636  CD  PRO A  91     8314  11418  12268    191   -242  -1020       C  
ATOM    637  N   ASN A  92     -15.874  16.865  10.647  1.00 82.40           N  
ANISOU  637  N   ASN A  92     7954  11325  12028   -255   -258  -1064       N  
ATOM    638  CA  ASN A  92     -16.603  15.741  10.067  1.00 98.01           C  
ANISOU  638  CA  ASN A  92     9833  13353  14054   -392   -324  -1110       C  
ATOM    639  C   ASN A  92     -17.686  16.314   9.167  1.00 99.25           C  
ANISOU  639  C   ASN A  92     9784  13578  14349   -280   -521  -1189       C  
ATOM    640  O   ASN A  92     -18.724  16.785   9.660  1.00105.48           O  
ANISOU  640  O   ASN A  92    10322  14460  15296   -241   -485  -1295       O  
ATOM    641  CB  ASN A  92     -17.196  14.837  11.134  1.00103.47           C  
ANISOU  641  CB  ASN A  92    10401  14114  14800   -584   -129  -1167       C  
ATOM    642  CG  ASN A  92     -17.558  13.473  10.585  1.00121.34           C  
ANISOU  642  CG  ASN A  92    12651  16382  17073   -762   -180  -1182       C  
ATOM    643  OD1 ASN A  92     -16.783  12.522  10.691  1.00122.98           O  
ANISOU  643  OD1 ASN A  92    13051  16508  17170   -883   -126  -1111       O  
ATOM    644  ND2 ASN A  92     -18.734  13.374   9.974  1.00124.17           N  
ANISOU  644  ND2 ASN A  92    12780  16829  17572   -774   -298  -1280       N  
ATOM    645  N   PRO A  93     -17.474  16.305   7.854  1.00 83.02           N  
ANISOU  645  N   PRO A  93     7826  11484  12236   -221   -734  -1146       N  
ATOM    646  CA  PRO A  93     -18.452  16.911   6.947  1.00 69.89           C  
ANISOU  646  CA  PRO A  93     5989   9876  10690    -98   -954  -1208       C  
ATOM    647  C   PRO A  93     -19.719  16.077   6.853  1.00 69.52           C  
ANISOU  647  C   PRO A  93     5687   9940  10788   -221   -984  -1330       C  
ATOM    648  O   PRO A  93     -19.756  14.899   7.212  1.00 68.82           O  
ANISOU  648  O   PRO A  93     5599   9867  10684   -418   -868  -1348       O  
ATOM    649  CB  PRO A  93     -17.714  16.954   5.605  1.00 67.80           C  
ANISOU  649  CB  PRO A  93     5948   9539  10274    -39  -1152  -1113       C  
ATOM    650  CG  PRO A  93     -16.259  16.748   5.951  1.00 72.11           C  
ANISOU  650  CG  PRO A  93     6769   9987  10642    -82  -1014  -1004       C  
ATOM    651  CD  PRO A  93     -16.271  15.853   7.141  1.00 74.80           C  
ANISOU  651  CD  PRO A  93     7066  10347  11009   -246   -787  -1039       C  
ATOM    652  N   GLU A  94     -20.773  16.714   6.348  1.00 73.73           N  
ANISOU  652  N   GLU A  94     5997  10546  11473   -102  -1153  -1413       N  
ATOM    653  CA  GLU A  94     -22.090  16.098   6.261  1.00 82.15           C  
ANISOU  653  CA  GLU A  94     6771  11733  12710   -200  -1197  -1548       C  
ATOM    654  C   GLU A  94     -22.389  15.542   4.875  1.00 76.51           C  
ANISOU  654  C   GLU A  94     6074  11028  11968   -225  -1452  -1556       C  
ATOM    655  O   GLU A  94     -22.879  14.418   4.751  1.00 79.69           O  
ANISOU  655  O   GLU A  94     6389  11480  12410   -407  -1444  -1620       O  
ATOM    656  CB  GLU A  94     -23.166  17.117   6.655  1.00 95.41           C  
ANISOU  656  CB  GLU A  94     8148  13503  14601    -50  -1223  -1665       C  
ATOM    657  CG  GLU A  94     -22.923  17.788   7.998  1.00104.66           C  
ANISOU  657  CG  GLU A  94     9295  14672  15798     -5   -982  -1678       C  
ATOM    658  CD  GLU A  94     -23.026  16.820   9.161  1.00114.16           C  
ANISOU  658  CD  GLU A  94    10437  15938  16999   -234   -698  -1718       C  
ATOM    659  OE1 GLU A  94     -23.748  15.809   9.034  1.00115.87           O  
ANISOU  659  OE1 GLU A  94    10505  16235  17286   -410   -691  -1784       O  
ATOM    660  OE2 GLU A  94     -22.382  17.069  10.203  1.00108.22           O  
ANISOU  660  OE2 GLU A  94     9794  15154  16171   -246   -487  -1679       O  
ATOM    661  N   ASN A  95     -22.101  16.307   3.829  1.00 60.51           N  
ANISOU  661  N   ASN A  95     4170   8954   9869    -53  -1681  -1491       N  
ATOM    662  CA  ASN A  95     -22.482  15.968   2.461  1.00 58.78           C  
ANISOU  662  CA  ASN A  95     3957   8759   9619    -47  -1954  -1507       C  
ATOM    663  C   ASN A  95     -21.240  15.506   1.697  1.00 56.86           C  
ANISOU  663  C   ASN A  95     4060   8419   9124    -91  -1990  -1387       C  
ATOM    664  O   ASN A  95     -20.495  16.314   1.142  1.00 55.96           O  
ANISOU  664  O   ASN A  95     4149   8236   8877     48  -2083  -1278       O  
ATOM    665  CB  ASN A  95     -23.153  17.167   1.792  1.00 61.17           C  
ANISOU  665  CB  ASN A  95     4139   9086  10019    179  -2205  -1523       C  
ATOM    666  CG  ASN A  95     -24.470  17.532   2.450  1.00 65.52           C  
ANISOU  666  CG  ASN A  95     4310   9745  10840    227  -2187  -1672       C  
ATOM    667  OD1 ASN A  95     -24.691  18.677   2.848  1.00 69.57           O  
ANISOU  667  OD1 ASN A  95     4731  10246  11457    409  -2196  -1684       O  
ATOM    668  ND2 ASN A  95     -25.351  16.546   2.572  1.00 70.30           N  
ANISOU  668  ND2 ASN A  95     4689  10457  11566     58  -2158  -1796       N  
ATOM    669  N   GLY A  95A    -21.029  14.192   1.673  1.00 56.40           N  
ANISOU  669  N   GLY A  95A    4067   8357   9007   -288  -1913  -1412       N  
ATOM    670  CA  GLY A  95A    -19.936  13.604   0.924  1.00 54.92           C  
ANISOU  670  CA  GLY A  95A    4179   8091   8598   -338  -1945  -1333       C  
ATOM    671  C   GLY A  95A    -20.414  12.771  -0.248  1.00 56.48           C  
ANISOU  671  C   GLY A  95A    4365   8330   8763   -417  -2154  -1404       C  
ATOM    672  O   GLY A  95A    -20.983  13.307  -1.203  1.00 58.49           O  
ANISOU  672  O   GLY A  95A    4562   8637   9025   -307  -2399  -1422       O  
ATOM    673  N   THR A  96     -20.190  11.460  -0.191  1.00 59.98           N  
ANISOU  673  N   THR A  96     4875   8745   9171   -605  -2071  -1446       N  
ATOM    674  CA  THR A  96     -20.689  10.544  -1.216  1.00 57.79           C  
ANISOU  674  CA  THR A  96     4578   8503   8878   -704  -2257  -1537       C  
ATOM    675  C   THR A  96     -22.149  10.239  -0.910  1.00 66.04           C  
ANISOU  675  C   THR A  96     5284   9647  10163   -792  -2301  -1669       C  
ATOM    676  O   THR A  96     -22.457   9.377  -0.083  1.00 63.87           O  
ANISOU  676  O   THR A  96     4904   9366   9997   -971  -2133  -1724       O  
ATOM    677  CB  THR A  96     -19.857   9.268  -1.261  1.00 56.67           C  
ANISOU  677  CB  THR A  96     4643   8271   8617   -864  -2155  -1539       C  
ATOM    678  OG1 THR A  96     -19.800   8.684   0.046  1.00 73.48           O  
ANISOU  678  OG1 THR A  96     6717  10355  10847  -1001  -1905  -1539       O  
ATOM    679  CG2 THR A  96     -18.449   9.573  -1.736  1.00 54.67           C  
ANISOU  679  CG2 THR A  96     4702   7942   8128   -770  -2136  -1430       C  
ATOM    680  N   CYS A  97     -23.055  10.950  -1.583  1.00 62.20           N  
ANISOU  680  N   CYS A  97     4622   9250   9759   -670  -2531  -1719       N  
ATOM    681  CA  CYS A  97     -24.475  10.798  -1.288  1.00 64.70           C  
ANISOU  681  CA  CYS A  97     4580   9678  10325   -732  -2579  -1855       C  
ATOM    682  C   CYS A  97     -24.989   9.427  -1.716  1.00 66.19           C  
ANISOU  682  C   CYS A  97     4706   9888  10556   -948  -2645  -1969       C  
ATOM    683  O   CYS A  97     -25.840   8.840  -1.038  1.00 76.83           O  
ANISOU  683  O   CYS A  97     5807  11290  12096  -1106  -2544  -2068       O  
ATOM    684  CB  CYS A  97     -25.268  11.922  -1.953  1.00 66.62           C  
ANISOU  684  CB  CYS A  97     4658  10003  10650   -525  -2838  -1880       C  
ATOM    685  SG  CYS A  97     -24.939  12.139  -3.708  1.00 67.28           S  
ANISOU  685  SG  CYS A  97     4973  10078  10514   -410  -3185  -1832       S  
ATOM    686  N   TYR A  98     -24.486   8.899  -2.832  1.00 66.10           N  
ANISOU  686  N   TYR A  98     4914   9834  10366   -969  -2807  -1964       N  
ATOM    687  CA  TYR A  98     -24.760   7.515  -3.197  1.00 67.23           C  
ANISOU  687  CA  TYR A  98     5055   9962  10526  -1184  -2847  -2070       C  
ATOM    688  C   TYR A  98     -23.646   6.636  -2.648  1.00 65.01           C  
ANISOU  688  C   TYR A  98     5026   9545  10129  -1313  -2616  -2008       C  
ATOM    689  O   TYR A  98     -22.475   6.862  -2.984  1.00 63.05           O  
ANISOU  689  O   TYR A  98     5063   9221   9671  -1219  -2593  -1910       O  
ATOM    690  CB  TYR A  98     -24.864   7.354  -4.705  1.00 68.64           C  
ANISOU  690  CB  TYR A  98     5331  10173  10575  -1141  -3154  -2122       C  
ATOM    691  CG  TYR A  98     -25.775   6.222  -5.139  1.00 71.10           C  
ANISOU  691  CG  TYR A  98     5529  10513  10972  -1326  -3244  -2246       C  
ATOM    692  CD1 TYR A  98     -25.335   4.905  -5.133  1.00 78.82           C  
ANISOU  692  CD1 TYR A  98     6643  11397  11909  -1526  -3166  -2302       C  
ATOM    693  CD2 TYR A  98     -27.076   6.473  -5.554  1.00 80.87           C  
ANISOU  693  CD2 TYR A  98     6555  11854  12318  -1293  -3386  -2287       C  
ATOM    694  CE1 TYR A  98     -26.166   3.869  -5.529  1.00 73.11           C  
ANISOU  694  CE1 TYR A  98     5850  10680  11250  -1695  -3229  -2391       C  
ATOM    695  CE2 TYR A  98     -27.913   5.446  -5.951  1.00 76.35           C  
ANISOU  695  CE2 TYR A  98     5899  11301  11808  -1464  -3450  -2380       C  
ATOM    696  CZ  TYR A  98     -27.453   4.145  -5.936  1.00 75.90           C  
ANISOU  696  CZ  TYR A  98     5984  11147  11708  -1668  -3371  -2430       C  
ATOM    697  OH  TYR A  98     -28.284   3.120  -6.331  1.00 94.30           O  
ANISOU  697  OH  TYR A  98     8240  13486  14105  -1842  -3439  -2521       O  
ATOM    698  N   PRO A  99     -23.951   5.643  -1.813  1.00 70.59           N  
ANISOU  698  N   PRO A  99     5639  10215  10966  -1527  -2446  -2059       N  
ATOM    699  CA  PRO A  99     -22.894   4.935  -1.084  1.00 68.51           C  
ANISOU  699  CA  PRO A  99     5606   9812  10613  -1629  -2214  -1981       C  
ATOM    700  C   PRO A  99     -21.947   4.189  -2.011  1.00 67.03           C  
ANISOU  700  C   PRO A  99     5717   9521  10231  -1646  -2302  -1983       C  
ATOM    701  O   PRO A  99     -22.281   3.824  -3.141  1.00 83.05           O  
ANISOU  701  O   PRO A  99     7755  11581  12218  -1660  -2525  -2077       O  
ATOM    702  CB  PRO A  99     -23.671   3.965  -0.184  1.00 74.65           C  
ANISOU  702  CB  PRO A  99     6197  10582  11585  -1876  -2069  -2050       C  
ATOM    703  CG  PRO A  99     -24.992   3.795  -0.860  1.00 85.51           C  
ANISOU  703  CG  PRO A  99     7300  12074  13116  -1938  -2278  -2195       C  
ATOM    704  CD  PRO A  99     -25.291   5.121  -1.497  1.00 79.60           C  
ANISOU  704  CD  PRO A  99     6457  11441  12346  -1693  -2462  -2188       C  
ATOM    705  N   GLY A 100     -20.747   3.966  -1.505  1.00 60.30           N  
ANISOU  705  N   GLY A 100     5104   8549   9257  -1641  -2125  -1888       N  
ATOM    706  CA  GLY A 100     -19.719   3.280  -2.257  1.00 59.48           C  
ANISOU  706  CA  GLY A 100     5284   8343   8972  -1643  -2172  -1894       C  
ATOM    707  C   GLY A 100     -18.367   3.527  -1.631  1.00 56.81           C  
ANISOU  707  C   GLY A 100     5170   7908   8505  -1563  -1980  -1766       C  
ATOM    708  O   GLY A 100     -18.242   4.198  -0.608  1.00 55.61           O  
ANISOU  708  O   GLY A 100     4962   7765   8401  -1516  -1817  -1673       O  
ATOM    709  N   HIS A 101     -17.352   2.961  -2.273  1.00 56.05           N  
ANISOU  709  N   HIS A 101     5322   7726   8247  -1548  -2005  -1776       N  
ATOM    710  CA  HIS A 101     -15.975   3.125  -1.836  1.00 53.69           C  
ANISOU  710  CA  HIS A 101     5243   7338   7819  -1467  -1846  -1672       C  
ATOM    711  C   HIS A 101     -15.254   4.077  -2.776  1.00 58.75           C  
ANISOU  711  C   HIS A 101     6020   8042   8261  -1281  -1937  -1625       C  
ATOM    712  O   HIS A 101     -15.280   3.894  -3.997  1.00 53.95           O  
ANISOU  712  O   HIS A 101     5483   7474   7539  -1258  -2110  -1701       O  
ATOM    713  CB  HIS A 101     -15.246   1.783  -1.782  1.00 53.52           C  
ANISOU  713  CB  HIS A 101     5402   7163   7769  -1580  -1786  -1719       C  
ATOM    714  CG  HIS A 101     -13.792   1.903  -1.445  1.00 63.85           C  
ANISOU  714  CG  HIS A 101     6929   8385   8947  -1485  -1647  -1630       C  
ATOM    715  ND1 HIS A 101     -13.341   2.466  -0.271  1.00 58.71           N  
ANISOU  715  ND1 HIS A 101     6276   7710   8322  -1444  -1467  -1506       N  
ATOM    716  CD2 HIS A 101     -12.685   1.541  -2.136  1.00 61.14           C  
ANISOU  716  CD2 HIS A 101     6801   7984   8447  -1422  -1665  -1659       C  
ATOM    717  CE1 HIS A 101     -12.021   2.440  -0.250  1.00 60.05           C  
ANISOU  717  CE1 HIS A 101     6646   7805   8364  -1362  -1389  -1458       C  
ATOM    718  NE2 HIS A 101     -11.598   1.884  -1.371  1.00 60.51           N  
ANISOU  718  NE2 HIS A 101     6833   7845   8315  -1346  -1501  -1551       N  
ATOM    719  N   PHE A 102     -14.621   5.093  -2.200  1.00 51.07           N  
ANISOU  719  N   PHE A 102     5088   7077   7239  -1158  -1819  -1500       N  
ATOM    720  CA  PHE A 102     -13.814   6.046  -2.952  1.00 50.18           C  
ANISOU  720  CA  PHE A 102     5120   7007   6937   -996  -1871  -1430       C  
ATOM    721  C   PHE A 102     -12.374   5.544  -2.940  1.00 48.64           C  
ANISOU  721  C   PHE A 102     5160   6717   6604   -986  -1750  -1407       C  
ATOM    722  O   PHE A 102     -11.712   5.571  -1.898  1.00 51.07           O  
ANISOU  722  O   PHE A 102     5509   6950   6946   -986  -1571  -1334       O  
ATOM    723  CB  PHE A 102     -13.936   7.438  -2.339  1.00 49.31           C  
ANISOU  723  CB  PHE A 102     4920   6948   6867   -873  -1818  -1316       C  
ATOM    724  CG  PHE A 102     -13.547   8.552  -3.265  1.00 49.21           C  
ANISOU  724  CG  PHE A 102     5006   6998   6693   -719  -1933  -1247       C  
ATOM    725  CD1 PHE A 102     -12.356   8.511  -3.969  1.00 59.75           C  
ANISOU  725  CD1 PHE A 102     6573   8311   7820   -676  -1920  -1218       C  
ATOM    726  CD2 PHE A 102     -14.373   9.648  -3.425  1.00 50.13           C  
ANISOU  726  CD2 PHE A 102     4984   7194   6870   -620  -2054  -1212       C  
ATOM    727  CE1 PHE A 102     -12.000   9.535  -4.813  1.00 48.50           C  
ANISOU  727  CE1 PHE A 102     5248   6943   6235   -556  -2016  -1141       C  
ATOM    728  CE2 PHE A 102     -14.023  10.677  -4.270  1.00 50.24           C  
ANISOU  728  CE2 PHE A 102     5108   7248   6734   -487  -2170  -1131       C  
ATOM    729  CZ  PHE A 102     -12.834  10.619  -4.966  1.00 49.43           C  
ANISOU  729  CZ  PHE A 102     5246   7124   6409   -464  -2146  -1089       C  
ATOM    730  N   ALA A 103     -11.893   5.086  -4.093  1.00 49.27           N  
ANISOU  730  N   ALA A 103     5388   6804   6527   -976  -1850  -1479       N  
ATOM    731  CA  ALA A 103     -10.566   4.492  -4.169  1.00 48.19           C  
ANISOU  731  CA  ALA A 103     5454   6583   6272   -967  -1744  -1490       C  
ATOM    732  C   ALA A 103      -9.490   5.556  -4.003  1.00 52.86           C  
ANISOU  732  C   ALA A 103     6149   7195   6741   -837  -1638  -1364       C  
ATOM    733  O   ALA A 103      -9.509   6.586  -4.685  1.00 46.62           O  
ANISOU  733  O   ALA A 103     5376   6499   5837   -744  -1721  -1307       O  
ATOM    734  CB  ALA A 103     -10.387   3.764  -5.498  1.00 49.61           C  
ANISOU  734  CB  ALA A 103     5755   6784   6311   -987  -1878  -1622       C  
ATOM    735  N   ASP A 104      -8.550   5.300  -3.093  1.00 50.02           N  
ANISOU  735  N   ASP A 104     5861   6739   6406   -837  -1464  -1318       N  
ATOM    736  CA  ASP A 104      -7.402   6.177  -2.859  1.00 49.52           C  
ANISOU  736  CA  ASP A 104     5897   6681   6238   -730  -1350  -1212       C  
ATOM    737  C   ASP A 104      -7.851   7.604  -2.551  1.00 45.52           C  
ANISOU  737  C   ASP A 104     5295   6246   5756   -651  -1360  -1094       C  
ATOM    738  O   ASP A 104      -7.341   8.583  -3.101  1.00 47.44           O  
ANISOU  738  O   ASP A 104     5612   6547   5868   -558  -1380  -1023       O  
ATOM    739  CB  ASP A 104      -6.439   6.139  -4.046  1.00 43.45           C  
ANISOU  739  CB  ASP A 104     5295   5955   5258   -676  -1382  -1254       C  
ATOM    740  CG  ASP A 104      -5.920   4.745  -4.325  1.00 43.98           C  
ANISOU  740  CG  ASP A 104     5458   5942   5310   -735  -1366  -1389       C  
ATOM    741  OD1 ASP A 104      -5.077   4.255  -3.544  1.00 43.61           O  
ANISOU  741  OD1 ASP A 104     5463   5793   5313   -736  -1234  -1381       O  
ATOM    742  OD2 ASP A 104      -6.351   4.138  -5.327  1.00 45.60           O  
ANISOU  742  OD2 ASP A 104     5689   6182   5455   -775  -1495  -1507       O  
ATOM    743  N   TYR A 105      -8.828   7.708  -1.651  1.00 42.90           N  
ANISOU  743  N   TYR A 105     4796   5906   5600   -693  -1343  -1079       N  
ATOM    744  CA  TYR A 105      -9.381   9.006  -1.283  1.00 42.74           C  
ANISOU  744  CA  TYR A 105     4660   5943   5636   -613  -1357   -991       C  
ATOM    745  C   TYR A 105      -8.328   9.895  -0.633  1.00 40.95           C  
ANISOU  745  C   TYR A 105     4518   5684   5358   -527  -1219   -878       C  
ATOM    746  O   TYR A 105      -8.204  11.078  -0.974  1.00 47.16           O  
ANISOU  746  O   TYR A 105     5323   6514   6080   -427  -1263   -801       O  
ATOM    747  CB  TYR A 105     -10.573   8.791  -0.351  1.00 43.39           C  
ANISOU  747  CB  TYR A 105     4537   6027   5923   -688  -1334  -1022       C  
ATOM    748  CG  TYR A 105     -11.225  10.047   0.166  1.00 43.43           C  
ANISOU  748  CG  TYR A 105     4397   6086   6017   -602  -1336   -959       C  
ATOM    749  CD1 TYR A 105     -11.659  11.034  -0.703  1.00 44.33           C  
ANISOU  749  CD1 TYR A 105     4481   6274   6089   -495  -1497   -935       C  
ATOM    750  CD2 TYR A 105     -11.432  10.230   1.525  1.00 42.76           C  
ANISOU  750  CD2 TYR A 105     4210   5977   6061   -627  -1184   -930       C  
ATOM    751  CE1 TYR A 105     -12.264  12.180  -0.233  1.00 44.55           C  
ANISOU  751  CE1 TYR A 105     4376   6336   6217   -403  -1510   -889       C  
ATOM    752  CE2 TYR A 105     -12.037  11.370   2.006  1.00 45.32           C  
ANISOU  752  CE2 TYR A 105     4396   6349   6474   -540  -1182   -895       C  
ATOM    753  CZ  TYR A 105     -12.452  12.343   1.121  1.00 52.48           C  
ANISOU  753  CZ  TYR A 105     5269   7316   7356   -423  -1348   -878       C  
ATOM    754  OH  TYR A 105     -13.057  13.484   1.594  1.00 51.89           O  
ANISOU  754  OH  TYR A 105     5056   7273   7386   -322  -1358   -853       O  
ATOM    755  N   GLU A 106      -7.546   9.331   0.288  1.00 50.78           N  
ANISOU  755  N   GLU A 106     5820   6845   6628   -568  -1063   -867       N  
ATOM    756  CA  GLU A 106      -6.531  10.103   0.992  1.00 38.09           C  
ANISOU  756  CA  GLU A 106     4284   5205   4983   -497   -933   -771       C  
ATOM    757  C   GLU A 106      -5.430  10.578   0.054  1.00 37.69           C  
ANISOU  757  C   GLU A 106     4388   5179   4754   -424   -950   -737       C  
ATOM    758  O   GLU A 106      -4.916  11.690   0.222  1.00 36.92           O  
ANISOU  758  O   GLU A 106     4323   5092   4614   -347   -909   -645       O  
ATOM    759  CB  GLU A 106      -5.954   9.264   2.132  1.00 37.13           C  
ANISOU  759  CB  GLU A 106     4196   4988   4923   -562   -787   -773       C  
ATOM    760  CG  GLU A 106      -6.985   8.803   3.160  1.00 37.63           C  
ANISOU  760  CG  GLU A 106     4120   5031   5147   -656   -742   -792       C  
ATOM    761  CD  GLU A 106      -7.828   7.625   2.689  1.00 39.45           C  
ANISOU  761  CD  GLU A 106     4299   5251   5437   -770   -828   -892       C  
ATOM    762  OE1 GLU A 106      -7.308   6.775   1.933  1.00 43.34           O  
ANISOU  762  OE1 GLU A 106     4905   5703   5857   -793   -878   -954       O  
ATOM    763  OE2 GLU A 106      -9.014   7.549   3.074  1.00 41.04           O  
ANISOU  763  OE2 GLU A 106     4342   5486   5764   -839   -845   -919       O  
ATOM    764  N   GLU A 107      -5.057   9.759  -0.931  1.00 38.36           N  
ANISOU  764  N   GLU A 107     4569   5274   4733   -454  -1004   -814       N  
ATOM    765  CA  GLU A 107      -4.070  10.186  -1.914  1.00 38.33           C  
ANISOU  765  CA  GLU A 107     4704   5317   4542   -398  -1012   -793       C  
ATOM    766  C   GLU A 107      -4.595  11.343  -2.750  1.00 39.20           C  
ANISOU  766  C   GLU A 107     4810   5513   4573   -338  -1137   -726       C  
ATOM    767  O   GLU A 107      -3.838  12.254  -3.099  1.00 38.85           O  
ANISOU  767  O   GLU A 107     4856   5494   4410   -283  -1110   -641       O  
ATOM    768  CB  GLU A 107      -3.675   9.009  -2.806  1.00 39.17           C  
ANISOU  768  CB  GLU A 107     4904   5427   4553   -443  -1045   -916       C  
ATOM    769  CG  GLU A 107      -2.744   8.018  -2.140  1.00 38.33           C  
ANISOU  769  CG  GLU A 107     4851   5223   4489   -469   -919   -968       C  
ATOM    770  CD  GLU A 107      -1.395   8.629  -1.823  1.00 40.49           C  
ANISOU  770  CD  GLU A 107     5201   5492   4693   -405   -789   -899       C  
ATOM    771  OE1 GLU A 107      -0.845   9.331  -2.695  1.00 41.61           O  
ANISOU  771  OE1 GLU A 107     5415   5714   4680   -363   -797   -869       O  
ATOM    772  OE2 GLU A 107      -0.888   8.420  -0.701  1.00 46.38           O  
ANISOU  772  OE2 GLU A 107     5934   6154   5535   -405   -682   -871       O  
ATOM    773  N   LEU A 108      -5.888  11.322  -3.085  1.00 40.57           N  
ANISOU  773  N   LEU A 108     4877   5725   4811   -353  -1283   -760       N  
ATOM    774  CA  LEU A 108      -6.473  12.439  -3.818  1.00 41.56           C  
ANISOU  774  CA  LEU A 108     4991   5919   4880   -284  -1428   -689       C  
ATOM    775  C   LEU A 108      -6.486  13.700  -2.967  1.00 42.69           C  
ANISOU  775  C   LEU A 108     5079   6029   5112   -207  -1373   -573       C  
ATOM    776  O   LEU A 108      -6.223  14.800  -3.468  1.00 45.23           O  
ANISOU  776  O   LEU A 108     5475   6370   5340   -137  -1426   -474       O  
ATOM    777  CB  LEU A 108      -7.885  12.083  -4.279  1.00 43.60           C  
ANISOU  777  CB  LEU A 108     5124   6226   5216   -311  -1606   -766       C  
ATOM    778  CG  LEU A 108      -8.567  13.161  -5.117  1.00 44.72           C  
ANISOU  778  CG  LEU A 108     5254   6435   5302   -230  -1795   -700       C  
ATOM    779  CD1 LEU A 108      -7.716  13.492  -6.330  1.00 45.23           C  
ANISOU  779  CD1 LEU A 108     5525   6550   5113   -207  -1842   -650       C  
ATOM    780  CD2 LEU A 108      -9.954  12.718  -5.544  1.00 46.57           C  
ANISOU  780  CD2 LEU A 108     5344   6723   5628   -258  -1980   -793       C  
ATOM    781  N   ARG A 109      -6.791  13.559  -1.674  1.00 41.20           N  
ANISOU  781  N   ARG A 109     4768   5787   5098   -225  -1268   -584       N  
ATOM    782  CA  ARG A 109      -6.680  14.692  -0.759  1.00 40.10           C  
ANISOU  782  CA  ARG A 109     4586   5610   5039   -154  -1193   -494       C  
ATOM    783  C   ARG A 109      -5.266  15.263  -0.766  1.00 39.94           C  
ANISOU  783  C   ARG A 109     4723   5558   4895   -122  -1089   -409       C  
ATOM    784  O   ARG A 109      -5.073  16.484  -0.840  1.00 39.08           O  
ANISOU  784  O   ARG A 109     4650   5438   4760    -50  -1111   -313       O  
ATOM    785  CB  ARG A 109      -7.080  14.261   0.653  1.00 39.15           C  
ANISOU  785  CB  ARG A 109     4334   5449   5094   -199  -1070   -533       C  
ATOM    786  CG  ARG A 109      -8.528  13.827   0.787  1.00 40.40           C  
ANISOU  786  CG  ARG A 109     4307   5646   5397   -241  -1151   -614       C  
ATOM    787  CD  ARG A 109      -8.823  13.357   2.204  1.00 56.08           C  
ANISOU  787  CD  ARG A 109     6182   7598   7528   -308  -1002   -645       C  
ATOM    788  NE  ARG A 109      -8.461  14.362   3.199  1.00 47.64           N  
ANISOU  788  NE  ARG A 109     5103   6499   6501   -238   -891   -577       N  
ATOM    789  CZ  ARG A 109      -9.316  15.224   3.739  1.00 53.86           C  
ANISOU  789  CZ  ARG A 109     5742   7313   7411   -178   -901   -578       C  
ATOM    790  NH1 ARG A 109     -10.592  15.204   3.383  1.00 58.48           N  
ANISOU  790  NH1 ARG A 109     6162   7961   8099   -176  -1019   -642       N  
ATOM    791  NH2 ARG A 109      -8.897  16.103   4.638  1.00 56.19           N  
ANISOU  791  NH2 ARG A 109     6045   7572   7732   -117   -797   -528       N  
ATOM    792  N   GLU A 110      -4.261  14.387  -0.696  1.00 39.76           N  
ANISOU  792  N   GLU A 110     4790   5514   4802   -177   -980   -448       N  
ATOM    793  CA  GLU A 110      -2.879  14.853  -0.696  1.00 39.55           C  
ANISOU  793  CA  GLU A 110     4891   5468   4667   -155   -874   -383       C  
ATOM    794  C   GLU A 110      -2.533  15.559  -2.001  1.00 36.81           C  
ANISOU  794  C   GLU A 110     4663   5181   4143   -127   -960   -323       C  
ATOM    795  O   GLU A 110      -1.811  16.562  -2.001  1.00 38.65           O  
ANISOU  795  O   GLU A 110     4968   5400   4317    -93   -915   -226       O  
ATOM    796  CB  GLU A 110      -1.928  13.682  -0.451  1.00 37.98           C  
ANISOU  796  CB  GLU A 110     4750   5241   4439   -209   -760   -457       C  
ATOM    797  CG  GLU A 110      -0.499  14.092  -0.122  1.00 49.06           C  
ANISOU  797  CG  GLU A 110     6241   6620   5781   -189   -629   -406       C  
ATOM    798  CD  GLU A 110      -0.331  14.552   1.317  1.00 47.69           C  
ANISOU  798  CD  GLU A 110     6008   6378   5734   -170   -529   -356       C  
ATOM    799  OE1 GLU A 110      -1.328  14.564   2.071  1.00 51.85           O  
ANISOU  799  OE1 GLU A 110     6428   6883   6391   -174   -547   -362       O  
ATOM    800  OE2 GLU A 110       0.806  14.900   1.696  1.00 50.39           O  
ANISOU  800  OE2 GLU A 110     6406   6697   6043   -155   -430   -319       O  
ATOM    801  N   GLN A 111      -3.039  15.046  -3.126  1.00 38.20           N  
ANISOU  801  N   GLN A 111     4868   5423   4225   -150  -1086   -379       N  
ATOM    802  CA  GLN A 111      -2.817  15.701  -4.412  1.00 39.42           C  
ANISOU  802  CA  GLN A 111     5148   5644   4188   -133  -1181   -315       C  
ATOM    803  C   GLN A 111      -3.428  17.095  -4.430  1.00 40.02           C  
ANISOU  803  C   GLN A 111     5204   5701   4301    -60  -1287   -191       C  
ATOM    804  O   GLN A 111      -2.790  18.062  -4.859  1.00 42.26           O  
ANISOU  804  O   GLN A 111     5603   5984   4470    -40  -1282    -79       O  
ATOM    805  CB  GLN A 111      -3.405  14.852  -5.538  1.00 41.00           C  
ANISOU  805  CB  GLN A 111     5371   5919   4286   -171  -1316   -411       C  
ATOM    806  CG  GLN A 111      -2.722  13.517  -5.742  1.00 49.71           C  
ANISOU  806  CG  GLN A 111     6524   7036   5328   -234  -1227   -542       C  
ATOM    807  CD  GLN A 111      -1.412  13.645  -6.483  1.00 40.89           C  
ANISOU  807  CD  GLN A 111     5562   5972   4003   -246  -1136   -526       C  
ATOM    808  OE1 GLN A 111      -1.056  14.725  -6.953  1.00 41.28           O  
ANISOU  808  OE1 GLN A 111     5697   6056   3934   -224  -1147   -407       O  
ATOM    809  NE2 GLN A 111      -0.687  12.539  -6.598  1.00 44.27           N  
ANISOU  809  NE2 GLN A 111     6027   6404   4389   -283  -1044   -649       N  
ATOM    810  N   LEU A 112      -4.675  17.214  -3.970  1.00 40.45           N  
ANISOU  810  N   LEU A 112     5109   5737   4524    -23  -1386   -214       N  
ATOM    811  CA  LEU A 112      -5.341  18.509  -3.950  1.00 41.23           C  
ANISOU  811  CA  LEU A 112     5171   5807   4687     65  -1502   -115       C  
ATOM    812  C   LEU A 112      -4.732  19.461  -2.929  1.00 39.95           C  
ANISOU  812  C   LEU A 112     5010   5558   4609    108  -1376    -33       C  
ATOM    813  O   LEU A 112      -4.968  20.670  -3.015  1.00 40.62           O  
ANISOU  813  O   LEU A 112     5115   5599   4718    182  -1459     66       O  
ATOM    814  CB  LEU A 112      -6.833  18.328  -3.669  1.00 42.17           C  
ANISOU  814  CB  LEU A 112     5100   5939   4984     98  -1629   -186       C  
ATOM    815  CG  LEU A 112      -7.653  17.666  -4.778  1.00 51.93           C  
ANISOU  815  CG  LEU A 112     6322   7258   6152     72  -1812   -256       C  
ATOM    816  CD1 LEU A 112      -9.043  17.300  -4.281  1.00 44.69           C  
ANISOU  816  CD1 LEU A 112     5180   6357   5444     81  -1895   -353       C  
ATOM    817  CD2 LEU A 112      -7.743  18.584  -5.988  1.00 45.60           C  
ANISOU  817  CD2 LEU A 112     5648   6486   5192    130  -1996   -151       C  
ATOM    818  N   SER A 113      -3.957  18.949  -1.970  1.00 38.27           N  
ANISOU  818  N   SER A 113     4783   5314   4445     64  -1189    -73       N  
ATOM    819  CA  SER A 113      -3.314  19.827  -0.997  1.00 45.94           C  
ANISOU  819  CA  SER A 113     5763   6208   5485     97  -1072     -5       C  
ATOM    820  C   SER A 113      -2.256  20.726  -1.623  1.00 40.15           C  
ANISOU  820  C   SER A 113     5194   5458   4602     98  -1054    111       C  
ATOM    821  O   SER A 113      -1.903  21.747  -1.025  1.00 47.48           O  
ANISOU  821  O   SER A 113     6137   6313   5589    136  -1010    185       O  
ATOM    822  CB  SER A 113      -2.684  19.006   0.127  1.00 39.31           C  
ANISOU  822  CB  SER A 113     4881   5343   4712     47   -893    -74       C  
ATOM    823  OG  SER A 113      -3.669  18.556   1.036  1.00 44.75           O  
ANISOU  823  OG  SER A 113     5413   6023   5566     47   -884   -148       O  
ATOM    824  N   SER A 114      -1.740  20.375  -2.800  1.00 42.52           N  
ANISOU  824  N   SER A 114     5619   5827   4709     48  -1082    123       N  
ATOM    825  CA  SER A 114      -0.719  21.164  -3.478  1.00 46.22           C  
ANISOU  825  CA  SER A 114     6248   6298   5015     24  -1051    234       C  
ATOM    826  C   SER A 114      -1.260  21.839  -4.735  1.00 51.05           C  
ANISOU  826  C   SER A 114     6961   6941   5495     44  -1234    328       C  
ATOM    827  O   SER A 114      -0.512  22.101  -5.679  1.00 55.86           O  
ANISOU  827  O   SER A 114     7724   7596   5904     -8  -1223    400       O  
ATOM    828  CB  SER A 114       0.489  20.295  -3.821  1.00 51.87           C  
ANISOU  828  CB  SER A 114     7038   7079   5590    -57   -908    176       C  
ATOM    829  OG  SER A 114       0.124  19.230  -4.676  1.00 54.04           O  
ANISOU  829  OG  SER A 114     7326   7442   5766    -89   -971     80       O  
ATOM    830  N   VAL A 115      -2.557  22.126  -4.759  1.00 48.82           N  
ANISOU  830  N   VAL A 115     6592   6638   5321    119  -1406    329       N  
ATOM    831  CA  VAL A 115      -3.213  22.756  -5.898  1.00 45.82           C  
ANISOU  831  CA  VAL A 115     6298   6278   4835    155  -1617    418       C  
ATOM    832  C   VAL A 115      -3.555  24.189  -5.520  1.00 46.26           C  
ANISOU  832  C   VAL A 115     6356   6215   5006    246  -1702    539       C  
ATOM    833  O   VAL A 115      -4.162  24.433  -4.469  1.00 43.35           O  
ANISOU  833  O   VAL A 115     5834   5778   4858    318  -1694    493       O  
ATOM    834  CB  VAL A 115      -4.471  21.979  -6.322  1.00 45.13           C  
ANISOU  834  CB  VAL A 115     6103   6258   4787    179  -1781    316       C  
ATOM    835  CG1 VAL A 115      -5.206  22.722  -7.419  1.00 46.84           C  
ANISOU  835  CG1 VAL A 115     6401   6487   4910    234  -2026    414       C  
ATOM    836  CG2 VAL A 115      -4.098  20.576  -6.777  1.00 46.98           C  
ANISOU  836  CG2 VAL A 115     6357   6593   4899     87  -1707    192       C  
ATOM    837  N   SER A 116      -3.159  25.136  -6.371  1.00 47.42           N  
ANISOU  837  N   SER A 116     6683   6334   5002    238  -1781    693       N  
ATOM    838  CA  SER A 116      -3.433  26.547  -6.135  1.00 53.49           C  
ANISOU  838  CA  SER A 116     7486   6967   5871    324  -1883    821       C  
ATOM    839  C   SER A 116      -4.648  27.053  -6.895  1.00 57.75           C  
ANISOU  839  C   SER A 116     8030   7490   6422    421  -2161    877       C  
ATOM    840  O   SER A 116      -5.250  28.048  -6.477  1.00 64.54           O  
ANISOU  840  O   SER A 116     8844   8230   7448    533  -2274    930       O  
ATOM    841  CB  SER A 116      -2.213  27.395  -6.513  1.00 61.27           C  
ANISOU  841  CB  SER A 116     8675   7902   6702    249  -1800    975       C  
ATOM    842  OG  SER A 116      -1.837  27.164  -7.858  1.00 69.43           O  
ANISOU  842  OG  SER A 116     9883   9036   7462    163  -1847   1044       O  
ATOM    843  N   SER A 117      -5.019  26.389  -7.983  1.00 49.76           N  
ANISOU  843  N   SER A 117     7070   6594   5244    388  -2282    857       N  
ATOM    844  CA  SER A 117      -6.165  26.779  -8.790  1.00 52.14           C  
ANISOU  844  CA  SER A 117     7378   6895   5537    477  -2569    906       C  
ATOM    845  C   SER A 117      -6.423  25.680  -9.806  1.00 53.00           C  
ANISOU  845  C   SER A 117     7517   7162   5460    410  -2644    827       C  
ATOM    846  O   SER A 117      -5.537  24.877 -10.108  1.00 52.15           O  
ANISOU  846  O   SER A 117     7488   7147   5180    293  -2482    780       O  
ATOM    847  CB  SER A 117      -5.923  28.114  -9.500  1.00 66.38           C  
ANISOU  847  CB  SER A 117     9397   8599   7226    503  -2709   1121       C  
ATOM    848  OG  SER A 117      -4.851  28.011 -10.413  1.00 76.48           O  
ANISOU  848  OG  SER A 117    10903   9948   8207    367  -2623   1216       O  
ATOM    849  N   PHE A 118      -7.642  25.654 -10.339  1.00 56.92           N  
ANISOU  849  N   PHE A 118     7943   7687   5997    491  -2898    803       N  
ATOM    850  CA  PHE A 118      -7.908  24.763 -11.456  1.00 59.32           C  
ANISOU  850  CA  PHE A 118     8307   8134   6097    429  -3010    744       C  
ATOM    851  C   PHE A 118      -8.983  25.353 -12.358  1.00 67.57           C  
ANISOU  851  C   PHE A 118     9389   9178   7109    525  -3346    822       C  
ATOM    852  O   PHE A 118      -9.654  26.332 -12.017  1.00 63.28           O  
ANISOU  852  O   PHE A 118     8779   8519   6744    655  -3495    894       O  
ATOM    853  CB  PHE A 118      -8.274  23.341 -10.987  1.00 60.94           C  
ANISOU  853  CB  PHE A 118     8315   8430   6409    383  -2916    526       C  
ATOM    854  CG  PHE A 118      -9.432  23.264 -10.022  1.00 55.28           C  
ANISOU  854  CG  PHE A 118     7323   7671   6009    477  -2975    418       C  
ATOM    855  CD1 PHE A 118     -10.417  24.236  -9.982  1.00 58.76           C  
ANISOU  855  CD1 PHE A 118     7683   8040   6602    616  -3191    478       C  
ATOM    856  CD2 PHE A 118      -9.529  22.193  -9.152  1.00 52.83           C  
ANISOU  856  CD2 PHE A 118     6834   7394   5845    424  -2809    251       C  
ATOM    857  CE1 PHE A 118     -11.466  24.148  -9.104  1.00 57.33           C  
ANISOU  857  CE1 PHE A 118     7232   7839   6710    698  -3227    362       C  
ATOM    858  CE2 PHE A 118     -10.578  22.100  -8.266  1.00 52.72           C  
ANISOU  858  CE2 PHE A 118     6567   7358   6108    490  -2841    151       C  
ATOM    859  CZ  PHE A 118     -11.548  23.080  -8.243  1.00 64.03           C  
ANISOU  859  CZ  PHE A 118     7904   8736   7688    627  -3042    199       C  
ATOM    860  N   GLU A 119      -9.126  24.735 -13.526  1.00 69.16           N  
ANISOU  860  N   GLU A 119     9697   9506   7073    464  -3471    800       N  
ATOM    861  CA  GLU A 119     -10.103  25.118 -14.532  1.00 75.20           C  
ANISOU  861  CA  GLU A 119    10515  10297   7759    540  -3809    864       C  
ATOM    862  C   GLU A 119     -11.128  24.002 -14.651  1.00 72.74           C  
ANISOU  862  C   GLU A 119    10003  10097   7537    545  -3926    664       C  
ATOM    863  O   GLU A 119     -10.779  22.870 -15.005  1.00 63.55           O  
ANISOU  863  O   GLU A 119     8863   9052   6231    431  -3823    540       O  
ATOM    864  CB  GLU A 119      -9.427  25.359 -15.879  1.00 92.19           C  
ANISOU  864  CB  GLU A 119    12984  12518   9527    452  -3876   1011       C  
ATOM    865  CG  GLU A 119      -8.204  26.248 -15.830  1.00107.84           C  
ANISOU  865  CG  GLU A 119    15177  14417  11379    392  -3704   1195       C  
ATOM    866  CD  GLU A 119      -7.299  26.042 -17.030  1.00118.27           C  
ANISOU  866  CD  GLU A 119    16776  15860  12300    248  -3651   1274       C  
ATOM    867  OE1 GLU A 119      -7.811  25.670 -18.107  1.00116.38           O  
ANISOU  867  OE1 GLU A 119    16627  15735  11857    233  -3853   1259       O  
ATOM    868  OE2 GLU A 119      -6.072  26.235 -16.890  1.00115.87           O  
ANISOU  868  OE2 GLU A 119    16594  15548  11884    145  -3403   1339       O  
ATOM    869  N   ARG A 120     -12.385  24.319 -14.368  1.00 70.00           N  
ANISOU  869  N   ARG A 120     9455   9711   7431    677  -4141    623       N  
ATOM    870  CA  ARG A 120     -13.458  23.344 -14.488  1.00 67.58           C  
ANISOU  870  CA  ARG A 120     8938   9508   7233    679  -4275    436       C  
ATOM    871  C   ARG A 120     -14.075  23.423 -15.879  1.00 77.35           C  
ANISOU  871  C   ARG A 120    10300  10828   8263    703  -4608    484       C  
ATOM    872  O   ARG A 120     -14.454  24.505 -16.338  1.00 82.99           O  
ANISOU  872  O   ARG A 120    11105  11473   8954    815  -4845    640       O  
ATOM    873  CB  ARG A 120     -14.523  23.572 -13.417  1.00 65.82           C  
ANISOU  873  CB  ARG A 120     8397   9220   7391    799  -4319    342       C  
ATOM    874  CG  ARG A 120     -15.699  22.620 -13.499  1.00 66.89           C  
ANISOU  874  CG  ARG A 120     8288   9462   7666    794  -4460    148       C  
ATOM    875  CD  ARG A 120     -16.646  22.834 -12.335  1.00 66.57           C  
ANISOU  875  CD  ARG A 120     7920   9369   8003    894  -4447     47       C  
ATOM    876  NE  ARG A 120     -17.879  22.063 -12.464  1.00 70.25           N  
ANISOU  876  NE  ARG A 120     8134   9938   8621    893  -4611   -128       N  
ATOM    877  CZ  ARG A 120     -18.994  22.525 -13.021  1.00 85.54           C  
ANISOU  877  CZ  ARG A 120     9960  11897  10643   1015  -4939   -133       C  
ATOM    878  NH1 ARG A 120     -19.032  23.757 -13.510  1.00 83.59           N  
ANISOU  878  NH1 ARG A 120     9855  11565  10342   1145  -5096     40       N  
ATOM    879  NH2 ARG A 120     -20.071  21.754 -13.092  1.00 92.98           N  
ANISOU  879  NH2 ARG A 120    10658  12939  11731    988  -5037   -304       N  
ATOM    880  N   PHE A 121     -14.165  22.276 -16.547  1.00 69.76           N  
ANISOU  880  N   PHE A 121     9353  10006   7148    599  -4634    348       N  
ATOM    881  CA  PHE A 121     -14.716  22.205 -17.892  1.00 73.34           C  
ANISOU  881  CA  PHE A 121     9930  10559   7376    602  -4938    369       C  
ATOM    882  C   PHE A 121     -15.366  20.843 -18.073  1.00 76.74           C  
ANISOU  882  C   PHE A 121    10192  11115   7852    527  -4978    134       C  
ATOM    883  O   PHE A 121     -14.871  19.839 -17.555  1.00 71.05           O  
ANISOU  883  O   PHE A 121     9409  10421   7164    419  -4736     -7       O  
ATOM    884  CB  PHE A 121     -13.632  22.427 -18.954  1.00 76.67           C  
ANISOU  884  CB  PHE A 121    10703  11032   7395    506  -4869    514       C  
ATOM    885  CG  PHE A 121     -12.581  21.352 -18.984  1.00 76.51           C  
ANISOU  885  CG  PHE A 121    10778  11099   7192    349  -4610    400       C  
ATOM    886  CD1 PHE A 121     -11.506  21.389 -18.113  1.00 86.02           C  
ANISOU  886  CD1 PHE A 121    11993  12235   8456    298  -4273    421       C  
ATOM    887  CD2 PHE A 121     -12.667  20.307 -19.890  1.00 74.98           C  
ANISOU  887  CD2 PHE A 121    10650  11054   6786    256  -4678    261       C  
ATOM    888  CE1 PHE A 121     -10.538  20.401 -18.141  1.00 77.72           C  
ANISOU  888  CE1 PHE A 121    11006  11259   7264    167  -4015    306       C  
ATOM    889  CE2 PHE A 121     -11.703  19.318 -19.923  1.00 83.02           C  
ANISOU  889  CE2 PHE A 121    11739  12143   7662    123  -4412    139       C  
ATOM    890  CZ  PHE A 121     -10.637  19.365 -19.047  1.00 73.19           C  
ANISOU  890  CZ  PHE A 121    10495  10826   6487     84  -4082    163       C  
ATOM    891  N   GLU A 122     -16.477  20.813 -18.806  1.00 75.99           N  
ANISOU  891  N   GLU A 122    10002  11084   7786    570  -5190     97       N  
ATOM    892  CA  GLU A 122     -17.178  19.558 -19.055  1.00 83.65           C  
ANISOU  892  CA  GLU A 122    10811  12168   8803    490  -5244   -122       C  
ATOM    893  C   GLU A 122     -16.443  18.790 -20.146  1.00 80.99           C  
ANISOU  893  C   GLU A 122    10723  11951   8100    355  -5200   -160       C  
ATOM    894  O   GLU A 122     -16.454  19.184 -21.317  1.00 84.98           O  
ANISOU  894  O   GLU A 122    11414  12522   8352    358  -5319    -58       O  
ATOM    895  CB  GLU A 122     -18.639  19.808 -19.423  1.00 79.64           C  
ANISOU  895  CB  GLU A 122    10103  11689   8466    581  -5485   -153       C  
ATOM    896  CG  GLU A 122     -18.886  20.929 -20.410  1.00 92.05           C  
ANISOU  896  CG  GLU A 122    11843  13251   9882    677  -5676     41       C  
ATOM    897  CD  GLU A 122     -20.355  21.059 -20.763  1.00 95.41           C  
ANISOU  897  CD  GLU A 122    12056  13713  10484    765  -5920    -15       C  
ATOM    898  OE1 GLU A 122     -21.162  20.253 -20.252  1.00 85.96           O  
ANISOU  898  OE1 GLU A 122    10579  12557   9523    738  -5925   -205       O  
ATOM    899  OE2 GLU A 122     -20.705  21.965 -21.549  1.00 94.70           O  
ANISOU  899  OE2 GLU A 122    12076  13607  10298    857  -6104    132       O  
ATOM    900  N   ILE A 123     -15.797  17.690 -19.757  1.00 79.57           N  
ANISOU  900  N   ILE A 123    10543  11798   7890    238  -5022   -315       N  
ATOM    901  CA  ILE A 123     -14.989  16.928 -20.701  1.00 84.23           C  
ANISOU  901  CA  ILE A 123    11366  12497   8142    113  -4942   -376       C  
ATOM    902  C   ILE A 123     -15.881  16.132 -21.648  1.00 90.41           C  
ANISOU  902  C   ILE A 123    12086  13400   8866     64  -5108   -519       C  
ATOM    903  O   ILE A 123     -15.570  15.977 -22.835  1.00 88.54           O  
ANISOU  903  O   ILE A 123    12054  13272   8314      9  -5144   -507       O  
ATOM    904  CB  ILE A 123     -13.998  16.028 -19.935  1.00 79.89           C  
ANISOU  904  CB  ILE A 123    10823  11917   7613     16  -4662   -500       C  
ATOM    905  CG1 ILE A 123     -13.111  15.244 -20.902  1.00 96.11           C  
ANISOU  905  CG1 ILE A 123    13119  14083   9317   -102  -4573   -583       C  
ATOM    906  CG2 ILE A 123     -14.733  15.090 -18.980  1.00 74.44           C  
ANISOU  906  CG2 ILE A 123     9828  11189   7268    -12  -4607   -694       C  
ATOM    907  CD1 ILE A 123     -12.119  14.346 -20.201  1.00 72.09           C  
ANISOU  907  CD1 ILE A 123    10057  11003   6330   -190  -4227   -703       C  
ATOM    908  N   PHE A 124     -17.009  15.630 -21.144  1.00 99.99           N  
ANISOU  908  N   PHE A 124    13010  14601  10379     77  -5205   -658       N  
ATOM    909  CA  PHE A 124     -17.988  14.884 -21.935  1.00 90.19           C  
ANISOU  909  CA  PHE A 124    11673  13463   9131     27  -5376   -799       C  
ATOM    910  C   PHE A 124     -19.344  15.527 -21.683  1.00 84.45           C  
ANISOU  910  C   PHE A 124    10698  12708   8683    141  -5575   -761       C  
ATOM    911  O   PHE A 124     -20.040  15.176 -20.719  1.00 82.24           O  
ANISOU  911  O   PHE A 124    10136  12381   8732    144  -5550   -871       O  
ATOM    912  CB  PHE A 124     -17.993  13.401 -21.565  1.00 93.82           C  
ANISOU  912  CB  PHE A 124    12019  13938   9692   -106  -5266  -1043       C  
ATOM    913  CG  PHE A 124     -16.711  12.687 -21.893  1.00 97.31           C  
ANISOU  913  CG  PHE A 124    12699  14410   9866   -210  -5078  -1111       C  
ATOM    914  CD1 PHE A 124     -16.026  12.968 -23.063  1.00109.12           C  
ANISOU  914  CD1 PHE A 124    14476  16002  10985   -228  -5084  -1028       C  
ATOM    915  CD2 PHE A 124     -16.191  11.737 -21.029  1.00 84.76           C  
ANISOU  915  CD2 PHE A 124    11045  12754   8404   -289  -4885  -1262       C  
ATOM    916  CE1 PHE A 124     -14.846  12.315 -23.366  1.00105.24           C  
ANISOU  916  CE1 PHE A 124    14186  15548  10250   -319  -4892  -1107       C  
ATOM    917  CE2 PHE A 124     -15.011  11.080 -21.328  1.00 81.63           C  
ANISOU  917  CE2 PHE A 124    10861  12381   7774   -370  -4709  -1338       C  
ATOM    918  CZ  PHE A 124     -14.339  11.370 -22.497  1.00 85.39           C  
ANISOU  918  CZ  PHE A 124    11605  12962   7879   -384  -4707  -1266       C  
ATOM    919  N   PRO A 125     -19.638  16.542 -22.491  1.00 87.32           N  
ANISOU  919  N   PRO A 125    11153  13100   8924    234  -5766   -608       N  
ATOM    920  CA  PRO A 125     -20.844  17.345 -22.432  1.00 88.68           C  
ANISOU  920  CA  PRO A 125    11096  13230   9367    367  -5952   -562       C  
ATOM    921  C   PRO A 125     -21.982  16.386 -22.419  1.00 88.90           C  
ANISOU  921  C   PRO A 125    10842  13323   9615    319  -6060   -763       C  
ATOM    922  O   PRO A 125     -21.951  15.428 -23.143  1.00 89.90           O  
ANISOU  922  O   PRO A 125    11005  13546   9609    194  -6082   -904       O  
ATOM    923  CB  PRO A 125     -20.781  18.130 -23.717  1.00 90.42           C  
ANISOU  923  CB  PRO A 125    11528  13486   9342    448  -6144   -376       C  
ATOM    924  CG  PRO A 125     -19.336  18.230 -24.018  1.00 89.33           C  
ANISOU  924  CG  PRO A 125    11724  13361   8855    383  -5991   -265       C  
ATOM    925  CD  PRO A 125     -18.809  16.897 -23.645  1.00 87.34           C  
ANISOU  925  CD  PRO A 125    11480  13165   8539    229  -5803   -459       C  
ATOM    926  N   LYS A 125A    -22.979  16.661 -21.604  1.00 91.82           N  
ANISOU  926  N   LYS A 125A   10923  13635  10329    416  -6118   -779       N  
ATOM    927  CA  LYS A 125A    -24.118  15.781 -21.420  1.00 95.53           C  
ANISOU  927  CA  LYS A 125A   11092  14160  11043    367  -6202   -964       C  
ATOM    928  C   LYS A 125A    -25.103  15.677 -22.570  1.00104.39           C  
ANISOU  928  C   LYS A 125A   12260  15399  12006    354  -6454   -989       C  
ATOM    929  O   LYS A 125A    -25.922  14.783 -22.617  1.00 99.64           O  
ANISOU  929  O   LYS A 125A   11557  14876  11427    231  -6492  -1162       O  
ATOM    930  CB  LYS A 125A    -24.866  16.210 -20.171  1.00 96.85           C  
ANISOU  930  CB  LYS A 125A   10954  14257  11588    491  -6212   -961       C  
ATOM    931  CG  LYS A 125A    -26.351  15.991 -20.239  1.00 99.61           C  
ANISOU  931  CG  LYS A 125A   10961  14657  12227    424  -6236  -1156       C  
ATOM    932  CD  LYS A 125A    -27.025  16.504 -18.990  1.00 98.07           C  
ANISOU  932  CD  LYS A 125A   10472  14399  12389    550  -6207  -1153       C  
ATOM    933  CE  LYS A 125A    -28.103  15.552 -18.532  1.00 94.29           C  
ANISOU  933  CE  LYS A 125A    9646  13981  12200    466  -6199  -1346       C  
ATOM    934  NZ  LYS A 125A    -28.649  15.914 -17.207  1.00105.32           N  
ANISOU  934  NZ  LYS A 125A   10752  15327  13937    578  -6124  -1359       N  
ATOM    935  N   GLU A 125B    -25.024  16.596 -23.503  1.00113.68           N  
ANISOU  935  N   GLU A 125B   13594  16580  13020    475  -6632   -816       N  
ATOM    936  CA  GLU A 125B    -25.922  16.574 -24.603  1.00123.87           C  
ANISOU  936  CA  GLU A 125B   14956  17984  14124    469  -6882   -821       C  
ATOM    937  C   GLU A 125B    -25.134  16.764 -25.867  1.00119.95           C  
ANISOU  937  C   GLU A 125B   14839  17527  13209    467  -6915   -659       C  
ATOM    938  O   GLU A 125B    -25.292  17.799 -26.489  1.00120.53           O  
ANISOU  938  O   GLU A 125B   15048  17531  13216    591  -6967   -456       O  
ATOM    939  CB  GLU A 125B    -26.925  17.707 -24.430  1.00133.69           C  
ANISOU  939  CB  GLU A 125B   15989  19213  15592    624  -7119   -778       C  
ATOM    940  CG  GLU A 125B    -28.199  17.305 -23.720  1.00139.81           C  
ANISOU  940  CG  GLU A 125B   16375  20000  16747    604  -7126   -965       C  
ATOM    941  CD  GLU A 125B    -28.379  17.979 -22.379  1.00141.97           C  
ANISOU  941  CD  GLU A 125B   16447  20157  17337    666  -6929   -969       C  
ATOM    942  OE1 GLU A 125B    -27.729  19.007 -22.121  1.00142.07           O  
ANISOU  942  OE1 GLU A 125B   16607  20069  17304    762  -6840   -810       O  
ATOM    943  OE2 GLU A 125B    -29.185  17.474 -21.581  1.00143.26           O  
ANISOU  943  OE2 GLU A 125B   16306  20334  17793    613  -6858  -1130       O  
ATOM    944  N   SER A 125C    -24.301  15.766 -26.203  1.00111.65           N  
ANISOU  944  N   SER A 125C   13960  16585  11876    322  -6876   -751       N  
ATOM    945  CA  SER A 125C    -23.429  15.694 -27.398  1.00112.62           C  
ANISOU  945  CA  SER A 125C   13937  16768  12087    170  -6813   -993       C  
ATOM    946  C   SER A 125C    -22.559  14.457 -27.373  1.00104.67           C  
ANISOU  946  C   SER A 125C   13179  15816  10774     25  -6636  -1064       C  
ATOM    947  O   SER A 125C    -21.773  14.254 -28.290  1.00114.06           O  
ANISOU  947  O   SER A 125C   14566  17123  11650    -30  -6726  -1074       O  
ATOM    948  CB  SER A 125C    -22.429  16.873 -27.504  1.00122.63           C  
ANISOU  948  CB  SER A 125C   15065  18142  13385    152  -7073  -1100       C  
ATOM    949  OG  SER A 125C    -21.259  16.562 -28.249  1.00126.12           O  
ANISOU  949  OG  SER A 125C   15362  18624  13935     -4  -7011  -1331       O  
ATOM    950  N   SER A 126     -22.653  13.639 -26.343  1.00 97.02           N  
ANISOU  950  N   SER A 126    12199  14765   9897    -33  -6381  -1119       N  
ATOM    951  CA  SER A 126     -21.713  12.540 -26.270  1.00 95.52           C  
ANISOU  951  CA  SER A 126    12198  14618   9478   -174  -6200  -1232       C  
ATOM    952  C   SER A 126     -22.259  11.153 -26.378  1.00103.72           C  
ANISOU  952  C   SER A 126    13100  15701  10610   -315  -6216  -1480       C  
ATOM    953  O   SER A 126     -21.643  10.287 -26.968  1.00112.02           O  
ANISOU  953  O   SER A 126    14315  16802  11444   -432  -6116  -1598       O  
ATOM    954  CB  SER A 126     -20.905  12.655 -24.982  1.00 92.72           C  
ANISOU  954  CB  SER A 126    11887  14151   9191   -178  -5929  -1200       C  
ATOM    955  OG  SER A 126     -19.605  13.106 -25.265  1.00 90.37           O  
ANISOU  955  OG  SER A 126    11749  13809   8781    -67  -5898   -971       O  
ATOM    956  N   TRP A 127     -23.413  10.942 -25.795  1.00 97.66           N  
ANISOU  956  N   TRP A 127    12034  14911  10160   -310  -6332  -1564       N  
ATOM    957  CA  TRP A 127     -24.033   9.619 -25.784  1.00102.29           C  
ANISOU  957  CA  TRP A 127    12466  15520  10881   -454  -6346  -1792       C  
ATOM    958  C   TRP A 127     -25.400   9.730 -26.445  1.00101.50           C  
ANISOU  958  C   TRP A 127    12206  15505  10854   -428  -6627  -1820       C  
ATOM    959  O   TRP A 127     -26.433   9.769 -25.763  1.00101.92           O  
ANISOU  959  O   TRP A 127    11964  15524  11239   -402  -6688  -1860       O  
ATOM    960  CB  TRP A 127     -24.150   9.078 -24.358  1.00104.13           C  
ANISOU  960  CB  TRP A 127    12462  15632  11469   -504  -6163  -1885       C  
ATOM    961  CG  TRP A 127     -23.096   9.612 -23.440  1.00 95.70           C  
ANISOU  961  CG  TRP A 127    11475  14465  10422   -444  -5944  -1775       C  
ATOM    962  CD1 TRP A 127     -23.214  10.667 -22.582  1.00 98.63           C  
ANISOU  962  CD1 TRP A 127    11731  14765  10981   -312  -5916  -1633       C  
ATOM    963  CD2 TRP A 127     -21.756   9.128 -23.299  1.00 88.93           C  
ANISOU  963  CD2 TRP A 127    10832  13567   9390   -510  -5724  -1805       C  
ATOM    964  NE1 TRP A 127     -22.032  10.865 -21.911  1.00 86.75           N  
ANISOU  964  NE1 TRP A 127    10356  13179   9425   -299  -5699  -1568       N  
ATOM    965  CE2 TRP A 127     -21.121   9.933 -22.334  1.00 86.07           C  
ANISOU  965  CE2 TRP A 127    10471  13112   9118   -418  -5578  -1671       C  
ATOM    966  CE3 TRP A 127     -21.033   8.090 -23.894  1.00 89.02           C  
ANISOU  966  CE3 TRP A 127    11031  13610   9184   -633  -5635  -1942       C  
ATOM    967  CZ2 TRP A 127     -19.797   9.732 -21.950  1.00 83.32           C  
ANISOU  967  CZ2 TRP A 127    10303  12709   8648   -448  -5354  -1665       C  
ATOM    968  CZ3 TRP A 127     -19.720   7.892 -23.511  1.00 86.33           C  
ANISOU  968  CZ3 TRP A 127    10863  13210   8728   -655  -5404  -1941       C  
ATOM    969  CH2 TRP A 127     -19.115   8.709 -22.550  1.00 83.52           C  
ANISOU  969  CH2 TRP A 127    10502  12768   8463   -564  -5269  -1802       C  
ATOM    970  N   PRO A 128     -25.445   9.789 -27.779  1.00124.08           N  
ANISOU  970  N   PRO A 128    15250  18487  13408   -435  -6800  -1804       N  
ATOM    971  CA  PRO A 128     -26.745   9.879 -28.459  1.00125.09           C  
ANISOU  971  CA  PRO A 128    15232  18702  13594   -409  -7085  -1835       C  
ATOM    972  C   PRO A 128     -27.569   8.611 -28.344  1.00127.06           C  
ANISOU  972  C   PRO A 128    15272  18967  14039   -557  -7120  -2065       C  
ATOM    973  O   PRO A 128     -28.794   8.673 -28.501  1.00138.39           O  
ANISOU  973  O   PRO A 128    16490  20445  15646   -534  -7325  -2104       O  
ATOM    974  CB  PRO A 128     -26.359  10.164 -29.916  1.00130.79           C  
ANISOU  974  CB  PRO A 128    16249  19554  13891   -401  -7224  -1764       C  
ATOM    975  CG  PRO A 128     -25.015   9.530 -30.063  1.00126.64           C  
ANISOU  975  CG  PRO A 128    15973  19032  13112   -506  -6989  -1820       C  
ATOM    976  CD  PRO A 128     -24.324   9.715 -28.733  1.00122.15           C  
ANISOU  976  CD  PRO A 128    15347  18318  12746   -476  -6736  -1772       C  
ATOM    977  N   ASN A 129     -26.942   7.470 -28.070  1.00118.60           N  
ANISOU  977  N   ASN A 129    14258  17853  12954   -707  -6927  -2217       N  
ATOM    978  CA  ASN A 129     -27.640   6.200 -27.944  1.00118.38           C  
ANISOU  978  CA  ASN A 129    14056  17816  13108   -865  -6941  -2433       C  
ATOM    979  C   ASN A 129     -27.862   5.789 -26.496  1.00110.97           C  
ANISOU  979  C   ASN A 129    12866  16747  12552   -913  -6757  -2493       C  
ATOM    980  O   ASN A 129     -28.329   4.674 -26.248  1.00112.76           O  
ANISOU  980  O   ASN A 129    12958  16941  12945  -1062  -6726  -2665       O  
ATOM    981  CB  ASN A 129     -26.860   5.102 -28.674  1.00118.55           C  
ANISOU  981  CB  ASN A 129    14315  17865  12864  -1011  -6862  -2581       C  
ATOM    982  CG  ASN A 129     -26.442   5.513 -30.072  1.00126.68           C  
ANISOU  982  CG  ASN A 129    15623  19035  13474   -974  -6994  -2518       C  
ATOM    983  OD1 ASN A 129     -27.234   6.073 -30.831  1.00127.32           O  
ANISOU  983  OD1 ASN A 129    15672  19221  13484   -909  -7244  -2458       O  
ATOM    984  ND2 ASN A 129     -25.187   5.245 -30.416  1.00123.77           N  
ANISOU  984  ND2 ASN A 129    15527  18675  12824  -1015  -6823  -2533       N  
ATOM    985  N   HIS A 130     -27.540   6.655 -25.538  1.00114.96           N  
ANISOU  985  N   HIS A 130    13309  17175  13195   -797  -6632  -2354       N  
ATOM    986  CA  HIS A 130     -27.689   6.351 -24.125  1.00101.04           C  
ANISOU  986  CA  HIS A 130    11316  15298  11777   -838  -6441  -2398       C  
ATOM    987  C   HIS A 130     -28.506   7.441 -23.447  1.00101.22           C  
ANISOU  987  C   HIS A 130    11090  15313  12054   -691  -6506  -2283       C  
ATOM    988  O   HIS A 130     -28.604   8.569 -23.934  1.00102.32           O  
ANISOU  988  O   HIS A 130    11295  15498  12083   -534  -6653  -2134       O  
ATOM    989  CB  HIS A 130     -26.330   6.218 -23.427  1.00 97.17           C  
ANISOU  989  CB  HIS A 130    10994  14706  11222   -853  -6170  -2366       C  
ATOM    990  CG  HIS A 130     -25.394   5.265 -24.101  1.00 96.95           C  
ANISOU  990  CG  HIS A 130    11231  14680  10927   -969  -6089  -2472       C  
ATOM    991  ND1 HIS A 130     -24.597   5.630 -25.164  1.00 97.62           N  
ANISOU  991  ND1 HIS A 130    11611  14843  10636   -922  -6135  -2407       N  
ATOM    992  CD2 HIS A 130     -25.123   3.961 -23.858  1.00 96.32           C  
ANISOU  992  CD2 HIS A 130    11164  14528  10903  -1128  -5957  -2643       C  
ATOM    993  CE1 HIS A 130     -23.876   4.592 -25.548  1.00 97.39           C  
ANISOU  993  CE1 HIS A 130    11757  14801  10445  -1043  -6029  -2545       C  
ATOM    994  NE2 HIS A 130     -24.177   3.566 -24.772  1.00 96.59           N  
ANISOU  994  NE2 HIS A 130    11495  14600  10607  -1164  -5927  -2690       N  
ATOM    995  N   THR A 131     -29.094   7.085 -22.309  1.00100.28           N  
ANISOU  995  N   THR A 131    10690  15134  12280   -748  -6388  -2355       N  
ATOM    996  CA  THR A 131     -29.828   8.036 -21.488  1.00100.23           C  
ANISOU  996  CA  THR A 131    10425  15113  12546   -618  -6400  -2272       C  
ATOM    997  C   THR A 131     -28.893   8.653 -20.457  1.00 98.47           C  
ANISOU  997  C   THR A 131    10255  14790  12370   -538  -6175  -2161       C  
ATOM    998  O   THR A 131     -28.099   7.954 -19.822  1.00 93.85           O  
ANISOU  998  O   THR A 131     9736  14127  11794   -645  -5955  -2213       O  
ATOM    999  CB  THR A 131     -31.004   7.354 -20.788  1.00101.52           C  
ANISOU  999  CB  THR A 131    10240  15281  13052   -729  -6377  -2412       C  
ATOM   1000  OG1 THR A 131     -31.872   6.774 -21.769  1.00111.47           O  
ANISOU 1000  OG1 THR A 131    11451  16634  14267   -807  -6597  -2519       O  
ATOM   1001  CG2 THR A 131     -31.794   8.358 -19.961  1.00101.77           C  
ANISOU 1001  CG2 THR A 131     9994  15312  13362   -587  -6380  -2342       C  
ATOM   1002  N   THR A 132     -28.989   9.972 -20.298  1.00 96.43           N  
ANISOU 1002  N   THR A 132     9971  14525  12144   -348  -6237  -2008       N  
ATOM   1003  CA  THR A 132     -28.116  10.724 -19.407  1.00 93.19           C  
ANISOU 1003  CA  THR A 132     9624  14022  11762   -252  -6053  -1886       C  
ATOM   1004  C   THR A 132     -28.908  11.449 -18.323  1.00 93.06           C  
ANISOU 1004  C   THR A 132     9302  13973  12083   -149  -6007  -1862       C  
ATOM   1005  O   THR A 132     -28.506  12.520 -17.864  1.00 91.64           O  
ANISOU 1005  O   THR A 132     9160  13736  11923      0  -5959  -1728       O  
ATOM   1006  CB  THR A 132     -27.271  11.721 -20.200  1.00 93.01           C  
ANISOU 1006  CB  THR A 132     9909  14000  11432   -118  -6140  -1707       C  
ATOM   1007  OG1 THR A 132     -28.118  12.741 -20.742  1.00 95.91           O  
ANISOU 1007  OG1 THR A 132    10208  14409  11823     38  -6375  -1612       O  
ATOM   1008  CG2 THR A 132     -26.545  11.020 -21.341  1.00 93.59           C  
ANISOU 1008  CG2 THR A 132    10277  14129  11154   -221  -6181  -1742       C  
ATOM   1009  N   THR A 133     -30.036  10.877 -17.898  1.00 96.04           N  
ANISOU 1009  N   THR A 133     9374  14389  12727   -231  -6011  -1996       N  
ATOM   1010  CA  THR A 133     -30.931  11.540 -16.957  1.00 97.98           C  
ANISOU 1010  CA  THR A 133     9308  14629  13291   -136  -5974  -1995       C  
ATOM   1011  C   THR A 133     -31.112  10.770 -15.654  1.00 96.91           C  
ANISOU 1011  C   THR A 133     8943  14460  13417   -280  -5715  -2108       C  
ATOM   1012  O   THR A 133     -32.012  11.105 -14.874  1.00110.27           O  
ANISOU 1012  O   THR A 133    10340  16172  15386   -240  -5667  -2144       O  
ATOM   1013  CB  THR A 133     -32.301  11.777 -17.601  1.00102.68           C  
ANISOU 1013  CB  THR A 133     9704  15316  13991    -77  -6226  -2041       C  
ATOM   1014  OG1 THR A 133     -32.941  10.518 -17.838  1.00103.83           O  
ANISOU 1014  OG1 THR A 133     9728  15524  14198   -273  -6250  -2204       O  
ATOM   1015  CG2 THR A 133     -32.150  12.521 -18.920  1.00103.01           C  
ANISOU 1015  CG2 THR A 133     9984  15393  13764     57  -6490  -1922       C  
ATOM   1016  N   GLY A 134     -30.294   9.753 -15.397  1.00 91.38           N  
ANISOU 1016  N   GLY A 134     8374  13711  12637   -449  -5543  -2164       N  
ATOM   1017  CA  GLY A 134     -30.421   8.981 -14.176  1.00 89.98           C  
ANISOU 1017  CA  GLY A 134     8006  13492  12690   -602  -5294  -2256       C  
ATOM   1018  C   GLY A 134     -30.207   9.803 -12.922  1.00 87.83           C  
ANISOU 1018  C   GLY A 134     7613  13170  12587   -501  -5100  -2185       C  
ATOM   1019  O   GLY A 134     -29.214  10.527 -12.808  1.00 85.55           O  
ANISOU 1019  O   GLY A 134     7514  12822  12167   -384  -5051  -2070       O  
ATOM   1020  N   VAL A 135     -31.141   9.709 -11.975  1.00 88.70           N  
ANISOU 1020  N   VAL A 135     7408  13308  12985   -548  -4984  -2257       N  
ATOM   1021  CA  VAL A 135     -31.050  10.404 -10.696  1.00 86.96           C  
ANISOU 1021  CA  VAL A 135     7044  13053  12944   -471  -4776  -2215       C  
ATOM   1022  C   VAL A 135     -31.420   9.428  -9.588  1.00 86.60           C  
ANISOU 1022  C   VAL A 135     6793  13005  13105   -681  -4527  -2318       C  
ATOM   1023  O   VAL A 135     -31.926   8.332  -9.834  1.00 92.28           O  
ANISOU 1023  O   VAL A 135     7450  13750  13861   -867  -4545  -2418       O  
ATOM   1024  CB  VAL A 135     -31.957  11.652 -10.633  1.00 88.98           C  
ANISOU 1024  CB  VAL A 135     7102  13359  13349   -261  -4892  -2179       C  
ATOM   1025  CG1 VAL A 135     -31.448  12.732 -11.574  1.00 89.05           C  
ANISOU 1025  CG1 VAL A 135     7345  13340  13150    -51  -5106  -2043       C  
ATOM   1026  CG2 VAL A 135     -33.394  11.282 -10.963  1.00 92.71           C  
ANISOU 1026  CG2 VAL A 135     7309  13932  13986   -316  -5025  -2293       C  
ATOM   1027  N   SER A 136     -31.162   9.844  -8.351  1.00 84.70           N  
ANISOU 1027  N   SER A 136     6457  12730  12994   -654  -4292  -2288       N  
ATOM   1028  CA  SER A 136     -31.443   9.023  -7.185  1.00 84.29           C  
ANISOU 1028  CA  SER A 136     6229  12674  13123   -851  -4028  -2362       C  
ATOM   1029  C   SER A 136     -32.035   9.888  -6.084  1.00 93.25           C  
ANISOU 1029  C   SER A 136     7110  13849  14470   -751  -3876  -2359       C  
ATOM   1030  O   SER A 136     -31.745  11.084  -5.986  1.00 88.82           O  
ANISOU 1030  O   SER A 136     6582  13273  13893   -536  -3908  -2283       O  
ATOM   1031  CB  SER A 136     -30.182   8.317  -6.671  1.00 81.08           C  
ANISOU 1031  CB  SER A 136     6038  12163  12607   -982  -3829  -2334       C  
ATOM   1032  OG  SER A 136     -30.475   7.511  -5.544  1.00 81.80           O  
ANISOU 1032  OG  SER A 136     5976  12242  12863  -1183  -3574  -2389       O  
ATOM   1033  N   ALA A 137     -32.881   9.265  -5.261  1.00108.78           N  
ANISOU 1033  N   ALA A 137     8831  15868  16635   -914  -3705  -2446       N  
ATOM   1034  CA  ALA A 137     -33.414   9.939  -4.085  1.00110.12           C  
ANISOU 1034  CA  ALA A 137     8762  16082  16997   -852  -3510  -2460       C  
ATOM   1035  C   ALA A 137     -32.379  10.050  -2.975  1.00107.00           C  
ANISOU 1035  C   ALA A 137     8474  15612  16568   -877  -3237  -2398       C  
ATOM   1036  O   ALA A 137     -32.514  10.911  -2.099  1.00103.47           O  
ANISOU 1036  O   ALA A 137     7903  15187  16224   -762  -3096  -2387       O  
ATOM   1037  CB  ALA A 137     -34.656   9.210  -3.573  1.00109.12           C  
ANISOU 1037  CB  ALA A 137     8344  16045  17072  -1033  -3407  -2569       C  
ATOM   1038  N   SER A 138     -31.353   9.196  -2.992  1.00 99.96           N  
ANISOU 1038  N   SER A 138     7812  14632  15536  -1023  -3160  -2365       N  
ATOM   1039  CA  SER A 138     -30.268   9.307  -2.026  1.00 96.40           C  
ANISOU 1039  CA  SER A 138     7487  14104  15035  -1040  -2924  -2301       C  
ATOM   1040  C   SER A 138     -29.410  10.542  -2.263  1.00 91.28           C  
ANISOU 1040  C   SER A 138     6995  13413  14276   -792  -3011  -2208       C  
ATOM   1041  O   SER A 138     -28.760  11.022  -1.329  1.00 86.28           O  
ANISOU 1041  O   SER A 138     6390  12742  13651   -747  -2819  -2161       O  
ATOM   1042  CB  SER A 138     -29.399   8.050  -2.069  1.00 95.14           C  
ANISOU 1042  CB  SER A 138     7541  13850  14758  -1253  -2845  -2296       C  
ATOM   1043  OG  SER A 138     -29.018   7.745  -3.398  1.00 95.34           O  
ANISOU 1043  OG  SER A 138     7767  13842  14616  -1227  -3093  -2296       O  
ATOM   1044  N   CYS A 139     -29.388  11.063  -3.489  1.00 85.13           N  
ANISOU 1044  N   CYS A 139     6327  12637  13384   -637  -3294  -2174       N  
ATOM   1045  CA  CYS A 139     -28.692  12.309  -3.779  1.00 75.07           C  
ANISOU 1045  CA  CYS A 139     5200  11318  12006   -398  -3399  -2071       C  
ATOM   1046  C   CYS A 139     -29.703  13.398  -4.106  1.00 83.95           C  
ANISOU 1046  C   CYS A 139     6157  12500  13241   -194  -3567  -2073       C  
ATOM   1047  O   CYS A 139     -29.638  14.013  -5.175  1.00 83.23           O  
ANISOU 1047  O   CYS A 139     6197  12396  13032    -42  -3821  -2009       O  
ATOM   1048  CB  CYS A 139     -27.710  12.126  -4.938  1.00 74.51           C  
ANISOU 1048  CB  CYS A 139     5444  11189  11679   -376  -3586  -2003       C  
ATOM   1049  SG  CYS A 139     -26.349  10.987  -4.602  1.00 86.60           S  
ANISOU 1049  SG  CYS A 139     7206  12630  13067   -574  -3404  -2002       S  
ATOM   1050  N   SER A 140     -30.636  13.643  -3.192  1.00111.68           N  
ANISOU 1050  N   SER A 140     9389  16074  16971   -190  -3423  -2145       N  
ATOM   1051  CA  SER A 140     -31.736  14.558  -3.448  1.00126.60           C  
ANISOU 1051  CA  SER A 140    11085  18021  18997    -12  -3573  -2176       C  
ATOM   1052  C   SER A 140     -31.291  16.011  -3.308  1.00120.49           C  
ANISOU 1052  C   SER A 140    10393  17178  18209    247  -3616  -2086       C  
ATOM   1053  O   SER A 140     -30.301  16.331  -2.645  1.00116.59           O  
ANISOU 1053  O   SER A 140    10028  16613  17658    273  -3458  -2023       O  
ATOM   1054  CB  SER A 140     -32.900  14.280  -2.497  1.00131.59           C  
ANISOU 1054  CB  SER A 140    11385  18748  19863   -105  -3391  -2298       C  
ATOM   1055  OG  SER A 140     -33.406  12.969  -2.675  1.00135.21           O  
ANISOU 1055  OG  SER A 140    11764  19263  20347   -346  -3370  -2375       O  
ATOM   1056  N   HIS A 141     -32.053  16.896  -3.948  1.00123.04           N  
ANISOU 1056  N   HIS A 141    10642  17517  18592    438  -3841  -2081       N  
ATOM   1057  CA  HIS A 141     -31.826  18.333  -3.868  1.00121.28           C  
ANISOU 1057  CA  HIS A 141    10482  17216  18385    692  -3909  -2001       C  
ATOM   1058  C   HIS A 141     -33.170  19.035  -3.986  1.00127.63           C  
ANISOU 1058  C   HIS A 141    11038  18073  19383    841  -4039  -2076       C  
ATOM   1059  O   HIS A 141     -33.918  18.781  -4.936  1.00139.34           O  
ANISOU 1059  O   HIS A 141    12466  19613  20865    838  -4264  -2104       O  
ATOM   1060  CB  HIS A 141     -30.872  18.809  -4.969  1.00115.41           C  
ANISOU 1060  CB  HIS A 141    10072  16377  17401    799  -4134  -1846       C  
ATOM   1061  CG  HIS A 141     -30.575  20.275  -4.919  1.00119.04           C  
ANISOU 1061  CG  HIS A 141    10629  16732  17867   1046  -4209  -1744       C  
ATOM   1062  ND1 HIS A 141     -30.092  20.898  -3.788  1.00108.50           N  
ANISOU 1062  ND1 HIS A 141     9275  15336  16613   1112  -3993  -1736       N  
ATOM   1063  CD2 HIS A 141     -30.692  21.241  -5.860  1.00125.84           C  
ANISOU 1063  CD2 HIS A 141    11620  17532  18662   1235  -4476  -1644       C  
ATOM   1064  CE1 HIS A 141     -29.925  22.185  -4.035  1.00109.17           C  
ANISOU 1064  CE1 HIS A 141     9473  15318  16690   1332  -4126  -1639       C  
ATOM   1065  NE2 HIS A 141     -30.281  22.420  -5.285  1.00121.28           N  
ANISOU 1065  NE2 HIS A 141    11101  16845  18134   1409  -4419  -1576       N  
ATOM   1066  N   ASN A 142     -33.469  19.908  -3.021  1.00121.01           N  
ANISOU 1066  N   ASN A 142    10052  17219  18708    970  -3899  -2118       N  
ATOM   1067  CA  ASN A 142     -34.763  20.591  -2.942  1.00129.83           C  
ANISOU 1067  CA  ASN A 142    10906  18387  20038   1114  -3984  -2215       C  
ATOM   1068  C   ASN A 142     -35.913  19.588  -2.864  1.00131.10           C  
ANISOU 1068  C   ASN A 142    10784  18696  20334    941  -3943  -2360       C  
ATOM   1069  O   ASN A 142     -36.979  19.790  -3.449  1.00129.18           O  
ANISOU 1069  O   ASN A 142    10373  18510  20199   1020  -4139  -2423       O  
ATOM   1070  CB  ASN A 142     -34.958  21.558  -4.113  1.00134.24           C  
ANISOU 1070  CB  ASN A 142    11584  18875  20547   1337  -4328  -2127       C  
ATOM   1071  CG  ASN A 142     -34.076  22.786  -4.008  1.00138.07           C  
ANISOU 1071  CG  ASN A 142    12292  19207  20961   1534  -4354  -1998       C  
ATOM   1072  OD1 ASN A 142     -33.752  23.238  -2.910  1.00138.77           O  
ANISOU 1072  OD1 ASN A 142    12340  19255  21129   1573  -4128  -2023       O  
ATOM   1073  ND2 ASN A 142     -33.684  23.334  -5.153  1.00136.61           N  
ANISOU 1073  ND2 ASN A 142    12354  18935  20617   1652  -4628  -1856       N  
ATOM   1074  N   GLY A 143     -35.692  18.494  -2.134  1.00137.28           N  
ANISOU 1074  N   GLY A 143    11517  19534  21109    699  -3688  -2409       N  
ATOM   1075  CA  GLY A 143     -36.707  17.484  -1.920  1.00139.21           C  
ANISOU 1075  CA  GLY A 143    11505  19907  21480    503  -3608  -2537       C  
ATOM   1076  C   GLY A 143     -36.881  16.482  -3.039  1.00137.70           C  
ANISOU 1076  C   GLY A 143    11376  19751  21192    358  -3808  -2534       C  
ATOM   1077  O   GLY A 143     -37.540  15.455  -2.828  1.00140.55           O  
ANISOU 1077  O   GLY A 143    11565  20203  21635    148  -3717  -2627       O  
ATOM   1078  N   GLU A 144     -36.314  16.733  -4.214  1.00134.09           N  
ANISOU 1078  N   GLU A 144    11167  19225  20557    454  -4071  -2429       N  
ATOM   1079  CA  GLU A 144     -36.481  15.873  -5.375  1.00137.79           C  
ANISOU 1079  CA  GLU A 144    11714  19727  20913    338  -4285  -2430       C  
ATOM   1080  C   GLU A 144     -35.185  15.129  -5.670  1.00123.25           C  
ANISOU 1080  C   GLU A 144    10181  17813  18834    199  -4241  -2344       C  
ATOM   1081  O   GLU A 144     -34.092  15.601  -5.347  1.00122.69           O  
ANISOU 1081  O   GLU A 144    10312  17651  18653    269  -4150  -2247       O  
ATOM   1082  CB  GLU A 144     -36.906  16.692  -6.598  1.00151.69           C  
ANISOU 1082  CB  GLU A 144    13528  21478  22627    547  -4638  -2383       C  
ATOM   1083  CG  GLU A 144     -38.141  17.551  -6.361  1.00163.89           C  
ANISOU 1083  CG  GLU A 144    14783  23078  24410    718  -4708  -2468       C  
ATOM   1084  CD  GLU A 144     -38.287  18.668  -7.378  1.00169.17           C  
ANISOU 1084  CD  GLU A 144    15563  23689  25023    972  -5030  -2383       C  
ATOM   1085  OE1 GLU A 144     -37.448  18.751  -8.300  1.00167.89           O  
ANISOU 1085  OE1 GLU A 144    15709  23456  24624   1002  -5196  -2252       O  
ATOM   1086  OE2 GLU A 144     -39.238  19.469  -7.250  1.00169.53           O  
ANISOU 1086  OE2 GLU A 144    15395  23759  25259   1139  -5114  -2446       O  
ATOM   1087  N   SER A 145     -35.322  13.956  -6.288  1.00109.77           N  
ANISOU 1087  N   SER A 145     8507  16146  17056      3  -4310  -2388       N  
ATOM   1088  CA  SER A 145     -34.164  13.139  -6.626  1.00 94.22           C  
ANISOU 1088  CA  SER A 145     6821  14109  14867   -139  -4277  -2331       C  
ATOM   1089  C   SER A 145     -33.225  13.896  -7.558  1.00 92.79           C  
ANISOU 1089  C   SER A 145     6950  13852  14455     34  -4475  -2196       C  
ATOM   1090  O   SER A 145     -33.652  14.709  -8.382  1.00 90.99           O  
ANISOU 1090  O   SER A 145     6738  13635  14200    212  -4722  -2155       O  
ATOM   1091  CB  SER A 145     -34.611  11.831  -7.284  1.00 97.99           C  
ANISOU 1091  CB  SER A 145     7279  14638  15314   -356  -4362  -2414       C  
ATOM   1092  OG  SER A 145     -35.429  11.071  -6.412  1.00106.58           O  
ANISOU 1092  OG  SER A 145     8101  15789  16606   -541  -4168  -2524       O  
ATOM   1093  N   SER A 146     -31.931  13.626  -7.419  1.00102.61           N  
ANISOU 1093  N   SER A 146     8446  15014  15526    -24  -4363  -2124       N  
ATOM   1094  CA  SER A 146     -30.922  14.309  -8.222  1.00100.53           C  
ANISOU 1094  CA  SER A 146     8494  14677  15024    119  -4516  -1988       C  
ATOM   1095  C   SER A 146     -29.662  13.449  -8.252  1.00100.15           C  
ANISOU 1095  C   SER A 146     8699  14571  14781    -33  -4403  -1962       C  
ATOM   1096  O   SER A 146     -29.681  12.277  -7.860  1.00109.34           O  
ANISOU 1096  O   SER A 146     9807  15747  15989   -245  -4258  -2052       O  
ATOM   1097  CB  SER A 146     -30.644  15.714  -7.678  1.00 99.41           C  
ANISOU 1097  CB  SER A 146     8360  14473  14938    342  -4480  -1894       C  
ATOM   1098  OG  SER A 146     -29.759  16.418  -8.530  1.00 95.53           O  
ANISOU 1098  OG  SER A 146     8172  13909  14214    474  -4646  -1749       O  
ATOM   1099  N   PHE A 147     -28.561  14.038  -8.714  1.00 84.02           N  
ANISOU 1099  N   PHE A 147     6942  12459  12525     75  -4469  -1836       N  
ATOM   1100  CA  PHE A 147     -27.323  13.299  -8.917  1.00 78.06           C  
ANISOU 1100  CA  PHE A 147     6451  11651  11557    -45  -4395  -1812       C  
ATOM   1101  C   PHE A 147     -26.166  14.289  -8.952  1.00 79.40           C  
ANISOU 1101  C   PHE A 147     6863  11740  11564    108  -4397  -1663       C  
ATOM   1102  O   PHE A 147     -26.366  15.506  -8.953  1.00 82.52           O  
ANISOU 1102  O   PHE A 147     7240  12112  12000    299  -4481  -1573       O  
ATOM   1103  CB  PHE A 147     -27.391  12.468 -10.204  1.00 84.19           C  
ANISOU 1103  CB  PHE A 147     7376  12469  12144   -142  -4583  -1852       C  
ATOM   1104  CG  PHE A 147     -26.309  11.436 -10.323  1.00 76.54           C  
ANISOU 1104  CG  PHE A 147     6631  11453  10999   -300  -4479  -1879       C  
ATOM   1105  CD1 PHE A 147     -26.287  10.338  -9.481  1.00 75.55           C  
ANISOU 1105  CD1 PHE A 147     6401  11302  11001   -495  -4269  -1984       C  
ATOM   1106  CD2 PHE A 147     -25.320  11.557 -11.285  1.00 75.80           C  
ANISOU 1106  CD2 PHE A 147     6858  11336  10607   -257  -4586  -1801       C  
ATOM   1107  CE1 PHE A 147     -25.294   9.385  -9.589  1.00 75.18           C  
ANISOU 1107  CE1 PHE A 147     6566  11196  10805   -631  -4179  -2016       C  
ATOM   1108  CE2 PHE A 147     -24.326  10.606 -11.399  1.00 74.08           C  
ANISOU 1108  CE2 PHE A 147     6843  11075  10230   -392  -4486  -1844       C  
ATOM   1109  CZ  PHE A 147     -24.313   9.518 -10.551  1.00 73.09           C  
ANISOU 1109  CZ  PHE A 147     6609  10911  10250   -572  -4288  -1956       C  
ATOM   1110  N   TYR A 148     -24.949  13.747  -8.976  1.00 77.37           N  
ANISOU 1110  N   TYR A 148     6837  11432  11126     19  -4302  -1639       N  
ATOM   1111  CA  TYR A 148     -23.751  14.576  -9.008  1.00 72.70           C  
ANISOU 1111  CA  TYR A 148     6497  10764  10361    135  -4281  -1494       C  
ATOM   1112  C   TYR A 148     -23.718  15.431 -10.269  1.00 75.36           C  
ANISOU 1112  C   TYR A 148     7031  11108  10494    281  -4545  -1373       C  
ATOM   1113  O   TYR A 148     -24.159  15.015 -11.344  1.00 90.30           O  
ANISOU 1113  O   TYR A 148     8982  13063  12267    241  -4720  -1401       O  
ATOM   1114  CB  TYR A 148     -22.492  13.707  -8.945  1.00 67.96           C  
ANISOU 1114  CB  TYR A 148     6167  10102   9553    -11  -4049  -1463       C  
ATOM   1115  CG  TYR A 148     -22.415  12.804  -7.735  1.00 66.40           C  
ANISOU 1115  CG  TYR A 148     5847   9871   9511   -171  -3752  -1543       C  
ATOM   1116  CD1 TYR A 148     -21.991  13.290  -6.506  1.00 64.40           C  
ANISOU 1116  CD1 TYR A 148     5563   9553   9354   -138  -3494  -1475       C  
ATOM   1117  CD2 TYR A 148     -22.754  11.462  -7.826  1.00 67.08           C  
ANISOU 1117  CD2 TYR A 148     5864   9984   9639   -360  -3738  -1682       C  
ATOM   1118  CE1 TYR A 148     -21.916  12.466  -5.400  1.00 63.16           C  
ANISOU 1118  CE1 TYR A 148     5313   9367   9318   -289  -3231  -1535       C  
ATOM   1119  CE2 TYR A 148     -22.683  10.631  -6.726  1.00 65.86           C  
ANISOU 1119  CE2 TYR A 148     5619   9786   9619   -515  -3475  -1738       C  
ATOM   1120  CZ  TYR A 148     -22.263  11.137  -5.516  1.00 63.92           C  
ANISOU 1120  CZ  TYR A 148     5349   9484   9453   -479  -3223  -1659       C  
ATOM   1121  OH  TYR A 148     -22.191  10.314  -4.416  1.00 62.89           O  
ANISOU 1121  OH  TYR A 148     5146   9312   9437   -638  -2969  -1702       O  
ATOM   1122  N   LYS A 149     -23.179  16.639 -10.130  1.00 71.23           N  
ANISOU 1122  N   LYS A 149     6624  10514   9925    443  -4560  -1227       N  
ATOM   1123  CA  LYS A 149     -23.082  17.571 -11.244  1.00 77.90           C  
ANISOU 1123  CA  LYS A 149     7683  11344  10573    577  -4781  -1077       C  
ATOM   1124  C   LYS A 149     -21.822  17.371 -12.075  1.00 71.64           C  
ANISOU 1124  C   LYS A 149     7252  10535   9432    524  -4801   -983       C  
ATOM   1125  O   LYS A 149     -21.726  17.930 -13.172  1.00 86.72           O  
ANISOU 1125  O   LYS A 149     9369  12454  11128    590  -4978   -865       O  
ATOM   1126  CB  LYS A 149     -23.138  19.014 -10.731  1.00 82.21           C  
ANISOU 1126  CB  LYS A 149     8197  11802  11238    773  -4791   -956       C  
ATOM   1127  CG  LYS A 149     -23.577  20.026 -11.779  1.00104.13           C  
ANISOU 1127  CG  LYS A 149    11089  14561  13914    922  -5042   -827       C  
ATOM   1128  CD  LYS A 149     -23.662  21.430 -11.206  1.00107.50           C  
ANISOU 1128  CD  LYS A 149    11480  14877  14486   1113  -5043   -722       C  
ATOM   1129  CE  LYS A 149     -24.135  22.420 -12.257  1.00104.01           C  
ANISOU 1129  CE  LYS A 149    11159  14404  13956   1256  -5301   -592       C  
ATOM   1130  NZ  LYS A 149     -24.226  23.805 -11.718  1.00 94.67           N  
ANISOU 1130  NZ  LYS A 149     9956  13092  12924   1444  -5309   -495       N  
ATOM   1131  N   ASN A 150     -20.860  16.593 -11.585  1.00 69.08           N  
ANISOU 1131  N   ASN A 150     7043  10180   9025    384  -4511  -1003       N  
ATOM   1132  CA  ASN A 150     -19.649  16.288 -12.333  1.00 68.07           C  
ANISOU 1132  CA  ASN A 150     7252  10043   8568    312  -4442   -927       C  
ATOM   1133  C   ASN A 150     -19.636  14.870 -12.883  1.00 68.48           C  
ANISOU 1133  C   ASN A 150     7338  10166   8516    146  -4446  -1078       C  
ATOM   1134  O   ASN A 150     -18.650  14.473 -13.513  1.00 67.80           O  
ANISOU 1134  O   ASN A 150     7515  10085   8161     78  -4377  -1051       O  
ATOM   1135  CB  ASN A 150     -18.412  16.514 -11.457  1.00 65.00           C  
ANISOU 1135  CB  ASN A 150     6999   9557   8141    293  -4113   -830       C  
ATOM   1136  CG  ASN A 150     -18.221  17.969 -11.087  1.00 64.67           C  
ANISOU 1136  CG  ASN A 150     6994   9432   8146    451  -4117   -667       C  
ATOM   1137  OD1 ASN A 150     -18.617  18.869 -11.829  1.00 66.66           O  
ANISOU 1137  OD1 ASN A 150     7300   9687   8340    574  -4371   -574       O  
ATOM   1138  ND2 ASN A 150     -17.610  18.210  -9.933  1.00 62.30           N  
ANISOU 1138  ND2 ASN A 150     6672   9049   7950    449  -3845   -631       N  
ATOM   1139  N   LEU A 151     -20.697  14.099 -12.660  1.00 82.19           N  
ANISOU 1139  N   LEU A 151     8812  11955  10463     75  -4521  -1246       N  
ATOM   1140  CA  LEU A 151     -20.820  12.756 -13.203  1.00 74.51           C  
ANISOU 1140  CA  LEU A 151     7855  11036   9418    -84  -4558  -1404       C  
ATOM   1141  C   LEU A 151     -22.130  12.642 -13.969  1.00 73.76           C  
ANISOU 1141  C   LEU A 151     7604  11032   9389    -77  -4820  -1480       C  
ATOM   1142  O   LEU A 151     -23.019  13.488 -13.850  1.00 75.23           O  
ANISOU 1142  O   LEU A 151     7620  11233   9731     42  -4924  -1428       O  
ATOM   1143  CB  LEU A 151     -20.756  11.691 -12.100  1.00 74.94           C  
ANISOU 1143  CB  LEU A 151     7769  11041   9664   -236  -4288  -1519       C  
ATOM   1144  CG  LEU A 151     -19.450  11.623 -11.307  1.00 65.69           C  
ANISOU 1144  CG  LEU A 151     6766   9769   8424   -266  -3957  -1434       C  
ATOM   1145  CD1 LEU A 151     -19.554  10.582 -10.209  1.00 64.50           C  
ANISOU 1145  CD1 LEU A 151     6464   9566   8476   -413  -3731  -1541       C  
ATOM   1146  CD2 LEU A 151     -18.276  11.322 -12.226  1.00 72.90           C  
ANISOU 1146  CD2 LEU A 151     8007  10681   9010   -296  -3932  -1398       C  
ATOM   1147  N   LEU A 152     -22.239  11.576 -14.758  1.00 77.99           N  
ANISOU 1147  N   LEU A 152     8211  11619   9801   -207  -4876  -1594       N  
ATOM   1148  CA  LEU A 152     -23.394  11.361 -15.625  1.00 78.29           C  
ANISOU 1148  CA  LEU A 152     8147  11745   9856   -223  -5084  -1652       C  
ATOM   1149  C   LEU A 152     -23.771   9.889 -15.545  1.00 78.82           C  
ANISOU 1149  C   LEU A 152     8110  11824  10013   -418  -5024  -1841       C  
ATOM   1150  O   LEU A 152     -23.011   9.027 -15.997  1.00 78.22           O  
ANISOU 1150  O   LEU A 152     8234  11737   9750   -524  -4971  -1909       O  
ATOM   1151  CB  LEU A 152     -23.082  11.775 -17.064  1.00 81.20           C  
ANISOU 1151  CB  LEU A 152     8788  12175   9889   -164  -5273  -1562       C  
ATOM   1152  CG  LEU A 152     -24.265  12.080 -17.982  1.00 83.65           C  
ANISOU 1152  CG  LEU A 152     9008  12574  10203   -111  -5532  -1559       C  
ATOM   1153  CD1 LEU A 152     -25.139  13.163 -17.373  1.00 84.41           C  
ANISOU 1153  CD1 LEU A 152     8869  12647  10554     42  -5597  -1482       C  
ATOM   1154  CD2 LEU A 152     -23.769  12.498 -19.357  1.00 90.93           C  
ANISOU 1154  CD2 LEU A 152    10235  13553  10759    -65  -5686  -1454       C  
ATOM   1155  N   TRP A 153     -24.937   9.599 -14.970  1.00 80.08           N  
ANISOU 1155  N   TRP A 153     7963  12002  10461   -468  -5024  -1928       N  
ATOM   1156  CA  TRP A 153     -25.394   8.221 -14.803  1.00 80.80           C  
ANISOU 1156  CA  TRP A 153     7938  12090  10670   -667  -4961  -2095       C  
ATOM   1157  C   TRP A 153     -26.044   7.763 -16.103  1.00 87.48           C  
ANISOU 1157  C   TRP A 153     8832  13022  11385   -713  -5188  -2164       C  
ATOM   1158  O   TRP A 153     -27.213   8.057 -16.365  1.00 98.24           O  
ANISOU 1158  O   TRP A 153     9999  14456  12872   -675  -5346  -2179       O  
ATOM   1159  CB  TRP A 153     -26.361   8.114 -13.629  1.00 81.01           C  
ANISOU 1159  CB  TRP A 153     7622  12109  11049   -718  -4848  -2150       C  
ATOM   1160  CG  TRP A 153     -26.626   6.703 -13.181  1.00 81.18           C  
ANISOU 1160  CG  TRP A 153     7546  12094  11204   -943  -4720  -2295       C  
ATOM   1161  CD1 TRP A 153     -26.412   5.557 -13.894  1.00 81.99           C  
ANISOU 1161  CD1 TRP A 153     7796  12180  11176  -1088  -4760  -2398       C  
ATOM   1162  CD2 TRP A 153     -27.142   6.293 -11.911  1.00 80.68           C  
ANISOU 1162  CD2 TRP A 153     7232  11998  11427  -1054  -4524  -2347       C  
ATOM   1163  NE1 TRP A 153     -26.771   4.462 -13.147  1.00 82.05           N  
ANISOU 1163  NE1 TRP A 153     7664  12130  11380  -1281  -4612  -2503       N  
ATOM   1164  CE2 TRP A 153     -27.221   4.887 -11.925  1.00 81.27           C  
ANISOU 1164  CE2 TRP A 153     7322  12025  11531  -1271  -4461  -2468       C  
ATOM   1165  CE3 TRP A 153     -27.548   6.979 -10.764  1.00 80.01           C  
ANISOU 1165  CE3 TRP A 153     6915  11916  11567   -994  -4388  -2303       C  
ATOM   1166  CZ2 TRP A 153     -27.689   4.155 -10.837  1.00 81.19           C  
ANISOU 1166  CZ2 TRP A 153     7116  11970  11762  -1438  -4270  -2527       C  
ATOM   1167  CZ3 TRP A 153     -28.012   6.251  -9.685  1.00 83.26           C  
ANISOU 1167  CZ3 TRP A 153     7126  12302  12208  -1160  -4186  -2372       C  
ATOM   1168  CH2 TRP A 153     -28.078   4.854  -9.729  1.00 87.90           C  
ANISOU 1168  CH2 TRP A 153     7743  12840  12813  -1385  -4130  -2475       C  
ATOM   1169  N   LEU A 154     -25.288   7.031 -16.917  1.00 83.91           N  
ANISOU 1169  N   LEU A 154     8636  12566  10679   -794  -5200  -2216       N  
ATOM   1170  CA  LEU A 154     -25.796   6.523 -18.185  1.00 86.92           C  
ANISOU 1170  CA  LEU A 154     9089  13031  10907   -850  -5404  -2294       C  
ATOM   1171  C   LEU A 154     -26.723   5.342 -17.930  1.00 95.78           C  
ANISOU 1171  C   LEU A 154    10001  14146  12246  -1029  -5394  -2459       C  
ATOM   1172  O   LEU A 154     -26.303   4.329 -17.360  1.00 93.08           O  
ANISOU 1172  O   LEU A 154     9677  13715  11975  -1174  -5218  -2552       O  
ATOM   1173  CB  LEU A 154     -24.644   6.115 -19.098  1.00 86.41           C  
ANISOU 1173  CB  LEU A 154     9368  12969  10497   -880  -5393  -2308       C  
ATOM   1174  CG  LEU A 154     -23.614   7.200 -19.412  1.00 84.97           C  
ANISOU 1174  CG  LEU A 154     9426  12795  10063   -730  -5382  -2141       C  
ATOM   1175  CD1 LEU A 154     -22.617   6.705 -20.444  1.00 85.17           C  
ANISOU 1175  CD1 LEU A 154     9772  12852   9736   -779  -5374  -2178       C  
ATOM   1176  CD2 LEU A 154     -24.297   8.471 -19.886  1.00 91.43           C  
ANISOU 1176  CD2 LEU A 154    10192  13687  10861   -569  -5587  -1998       C  
ATOM   1177  N   THR A 155     -27.981   5.471 -18.353  1.00106.11           N  
ANISOU 1177  N   THR A 155    11113  15540  13661  -1021  -5585  -2493       N  
ATOM   1178  CA  THR A 155     -28.954   4.397 -18.192  1.00 95.00           C  
ANISOU 1178  CA  THR A 155     9500  14138  12457  -1197  -5596  -2644       C  
ATOM   1179  C   THR A 155     -29.480   3.971 -19.561  1.00101.20           C  
ANISOU 1179  C   THR A 155    10361  15015  13075  -1241  -5841  -2725       C  
ATOM   1180  O   THR A 155     -28.875   4.303 -20.583  1.00 97.30           O  
ANISOU 1180  O   THR A 155    10121  14567  12281  -1164  -5953  -2676       O  
ATOM   1181  CB  THR A 155     -30.095   4.837 -17.272  1.00 99.75           C  
ANISOU 1181  CB  THR A 155     9744  14765  13390  -1173  -5574  -2635       C  
ATOM   1182  OG1 THR A 155     -29.570   5.673 -16.233  1.00116.09           O  
ANISOU 1182  OG1 THR A 155    11778  16780  15551  -1062  -5399  -2523       O  
ATOM   1183  CG2 THR A 155     -30.760   3.621 -16.630  1.00 99.17           C  
ANISOU 1183  CG2 THR A 155     9473  14654  13554  -1393  -5462  -2773       C  
ATOM   1184  N   GLY A 156     -30.603   3.253 -19.604  1.00122.92           N  
ANISOU 1184  N   GLY A 156    12897  17800  16008  -1369  -5922  -2846       N  
ATOM   1185  CA  GLY A 156     -31.080   2.694 -20.855  1.00121.11           C  
ANISOU 1185  CA  GLY A 156    12739  17650  15628  -1437  -6144  -2944       C  
ATOM   1186  C   GLY A 156     -31.793   3.713 -21.729  1.00125.44           C  
ANISOU 1186  C   GLY A 156    13241  18328  16093  -1277  -6413  -2870       C  
ATOM   1187  O   GLY A 156     -32.519   4.584 -21.254  1.00124.64           O  
ANISOU 1187  O   GLY A 156    12915  18262  16182  -1161  -6459  -2798       O  
ATOM   1188  N   LYS A 157     -31.588   3.582 -23.041  1.00136.94           N  
ANISOU 1188  N   LYS A 157    14919  19858  17256  -1273  -6594  -2893       N  
ATOM   1189  CA  LYS A 157     -32.169   4.482 -24.035  1.00145.66           C  
ANISOU 1189  CA  LYS A 157    16032  21085  18228  -1131  -6869  -2817       C  
ATOM   1190  C   LYS A 157     -32.864   3.647 -25.103  1.00147.65           C  
ANISOU 1190  C   LYS A 157    16287  21424  18390  -1253  -7078  -2961       C  
ATOM   1191  O   LYS A 157     -32.205   2.904 -25.838  1.00150.55           O  
ANISOU 1191  O   LYS A 157    16898  21792  18511  -1349  -7073  -3039       O  
ATOM   1192  CB  LYS A 157     -31.096   5.376 -24.657  1.00147.69           C  
ANISOU 1192  CB  LYS A 157    16602  21359  18155   -984  -6887  -2663       C  
ATOM   1193  CG  LYS A 157     -31.527   6.111 -25.923  1.00148.19           C  
ANISOU 1193  CG  LYS A 157    16759  21549  17999   -870  -7178  -2590       C  
ATOM   1194  CD  LYS A 157     -32.402   7.315 -25.615  1.00148.68           C  
ANISOU 1194  CD  LYS A 157    16603  21633  18254   -691  -7312  -2470       C  
ATOM   1195  CE  LYS A 157     -32.662   8.130 -26.874  1.00155.81           C  
ANISOU 1195  CE  LYS A 157    17648  22643  18911   -564  -7595  -2369       C  
ATOM   1196  NZ  LYS A 157     -33.452   9.365 -26.612  1.00157.18           N  
ANISOU 1196  NZ  LYS A 157    17635  22820  19267   -369  -7734  -2245       N  
ATOM   1197  N   ASN A 158     -34.190   3.775 -25.185  1.00139.27           N  
ANISOU 1197  N   ASN A 158    14950  20436  17529  -1246  -7261  -3005       N  
ATOM   1198  CA  ASN A 158     -35.006   3.051 -26.163  1.00140.49           C  
ANISOU 1198  CA  ASN A 158    15066  20681  17631  -1357  -7485  -3143       C  
ATOM   1199  C   ASN A 158     -34.824   1.537 -26.059  1.00137.75           C  
ANISOU 1199  C   ASN A 158    14757  20265  17316  -1596  -7363  -3322       C  
ATOM   1200  O   ASN A 158     -35.018   0.809 -27.035  1.00131.37           O  
ANISOU 1200  O   ASN A 158    14049  19512  16354  -1700  -7512  -3441       O  
ATOM   1201  CB  ASN A 158     -34.721   3.531 -27.591  1.00134.21           C  
ANISOU 1201  CB  ASN A 158    14533  19994  16465  -1263  -7714  -3086       C  
ATOM   1202  CG  ASN A 158     -35.269   4.922 -27.858  1.00132.62           C  
ANISOU 1202  CG  ASN A 158    14254  19868  16268  -1045  -7911  -2930       C  
ATOM   1203  OD1 ASN A 158     -36.361   5.268 -27.407  1.00137.84           O  
ANISOU 1203  OD1 ASN A 158    14607  20552  17214   -995  -7999  -2938       O  
ATOM   1204  ND2 ASN A 158     -34.509   5.728 -28.591  1.00128.17           N  
ANISOU 1204  ND2 ASN A 158    13969  19340  15388   -915  -7977  -2787       N  
ATOM   1205  N   GLY A 159     -34.452   1.052 -24.877  1.00139.33           N  
ANISOU 1205  N   GLY A 159    14885  20339  17716  -1684  -7095  -3342       N  
ATOM   1206  CA  GLY A 159     -34.361  -0.374 -24.635  1.00132.17           C  
ANISOU 1206  CA  GLY A 159    13991  19340  16887  -1912  -6972  -3501       C  
ATOM   1207  C   GLY A 159     -33.050  -1.028 -25.007  1.00135.06           C  
ANISOU 1207  C   GLY A 159    14701  19626  16992  -1969  -6846  -3542       C  
ATOM   1208  O   GLY A 159     -33.010  -2.256 -25.146  1.00125.30           O  
ANISOU 1208  O   GLY A 159    13520  18321  15767  -2151  -6806  -3693       O  
ATOM   1209  N   LEU A 160     -31.976  -0.258 -25.169  1.00147.78           N  
ANISOU 1209  N   LEU A 160    16542  21237  18371  -1822  -6779  -3417       N  
ATOM   1210  CA  LEU A 160     -30.682  -0.827 -25.514  1.00148.03           C  
ANISOU 1210  CA  LEU A 160    16896  21201  18150  -1864  -6646  -3459       C  
ATOM   1211  C   LEU A 160     -29.574   0.000 -24.880  1.00136.11           C  
ANISOU 1211  C   LEU A 160    15511  19636  16568  -1726  -6455  -3305       C  
ATOM   1212  O   LEU A 160     -29.726   1.203 -24.650  1.00138.17           O  
ANISOU 1212  O   LEU A 160    15695  19949  16855  -1565  -6498  -3150       O  
ATOM   1213  CB  LEU A 160     -30.475  -0.899 -27.033  1.00151.47           C  
ANISOU 1213  CB  LEU A 160    17572  21752  18227  -1852  -6838  -3509       C  
ATOM   1214  CG  LEU A 160     -31.166  -2.043 -27.778  1.00156.90           C  
ANISOU 1214  CG  LEU A 160    18239  22465  18910  -2024  -6985  -3704       C  
ATOM   1215  CD1 LEU A 160     -30.913  -1.946 -29.273  1.00164.37           C  
ANISOU 1215  CD1 LEU A 160    19433  23546  19476  -1992  -7171  -3736       C  
ATOM   1216  CD2 LEU A 160     -30.701  -3.389 -27.241  1.00153.67           C  
ANISOU 1216  CD2 LEU A 160    17884  21892  18611  -2201  -6785  -3851       C  
ATOM   1217  N   TYR A 161     -28.453  -0.666 -24.602  1.00121.35           N  
ANISOU 1217  N   TYR A 161    13838  17654  14614  -1789  -6247  -3353       N  
ATOM   1218  CA  TYR A 161     -27.255  -0.033 -24.055  1.00102.04           C  
ANISOU 1218  CA  TYR A 161    11543  15151  12075  -1677  -6054  -3228       C  
ATOM   1219  C   TYR A 161     -26.094  -0.402 -24.967  1.00101.86           C  
ANISOU 1219  C   TYR A 161    11862  15139  11702  -1683  -6013  -3280       C  
ATOM   1220  O   TYR A 161     -25.390  -1.391 -24.724  1.00100.70           O  
ANISOU 1220  O   TYR A 161    11830  14877  11554  -1784  -5849  -3392       O  
ATOM   1221  CB  TYR A 161     -26.999  -0.477 -22.616  1.00 99.38           C  
ANISOU 1221  CB  TYR A 161    11082  14658  12019  -1745  -5808  -3236       C  
ATOM   1222  CG  TYR A 161     -26.103   0.456 -21.829  1.00109.35           C  
ANISOU 1222  CG  TYR A 161    12398  15878  13270  -1608  -5641  -3080       C  
ATOM   1223  CD1 TYR A 161     -24.760   0.599 -22.150  1.00101.60           C  
ANISOU 1223  CD1 TYR A 161    11705  14878  12020  -1546  -5535  -3045       C  
ATOM   1224  CD2 TYR A 161     -26.600   1.183 -20.756  1.00107.35           C  
ANISOU 1224  CD2 TYR A 161    11904  15609  13276  -1544  -5582  -2977       C  
ATOM   1225  CE1 TYR A 161     -23.940   1.447 -21.433  1.00 90.72           C  
ANISOU 1225  CE1 TYR A 161    10376  13462  10633  -1427  -5388  -2905       C  
ATOM   1226  CE2 TYR A 161     -25.786   2.033 -20.031  1.00 98.42           C  
ANISOU 1226  CE2 TYR A 161    10822  14436  12136  -1422  -5435  -2841       C  
ATOM   1227  CZ  TYR A 161     -24.456   2.161 -20.373  1.00 95.98           C  
ANISOU 1227  CZ  TYR A 161    10805  14105  11560  -1366  -5344  -2803       C  
ATOM   1228  OH  TYR A 161     -23.638   3.005 -19.656  1.00 96.26           O  
ANISOU 1228  OH  TYR A 161    10891  14099  11586  -1250  -5203  -2669       O  
ATOM   1229  N   PRO A 162     -25.863   0.368 -26.028  1.00103.18           N  
ANISOU 1229  N   PRO A 162    12198  15442  11565  -1578  -6152  -3201       N  
ATOM   1230  CA  PRO A 162     -24.823   0.005 -26.998  1.00103.55           C  
ANISOU 1230  CA  PRO A 162    12563  15526  11255  -1597  -6112  -3262       C  
ATOM   1231  C   PRO A 162     -23.427   0.078 -26.394  1.00 99.98           C  
ANISOU 1231  C   PRO A 162    12281  14980  10729  -1554  -5851  -3215       C  
ATOM   1232  O   PRO A 162     -23.208   0.580 -25.290  1.00 97.16           O  
ANISOU 1232  O   PRO A 162    11818  14541  10559  -1490  -5717  -3108       O  
ATOM   1233  CB  PRO A 162     -24.997   1.040 -28.115  1.00105.75           C  
ANISOU 1233  CB  PRO A 162    12949  15982  11250  -1484  -6316  -3144       C  
ATOM   1234  CG  PRO A 162     -26.384   1.572 -27.937  1.00107.56           C  
ANISOU 1234  CG  PRO A 162    12899  16260  11711  -1442  -6520  -3087       C  
ATOM   1235  CD  PRO A 162     -26.640   1.538 -26.465  1.00104.96           C  
ANISOU 1235  CD  PRO A 162    12326  15797  11758  -1449  -6367  -3064       C  
ATOM   1236  N   ASN A 163     -22.469  -0.445 -27.157  1.00107.35           N  
ANISOU 1236  N   ASN A 163    13480  15931  11379  -1590  -5776  -3304       N  
ATOM   1237  CA  ASN A 163     -21.064  -0.434 -26.764  1.00 98.32           C  
ANISOU 1237  CA  ASN A 163    12522  14714  10122  -1549  -5533  -3280       C  
ATOM   1238  C   ASN A 163     -20.497   0.960 -27.001  1.00103.13           C  
ANISOU 1238  C   ASN A 163    13245  15429  10509  -1400  -5532  -3072       C  
ATOM   1239  O   ASN A 163     -20.342   1.388 -28.150  1.00 98.50           O  
ANISOU 1239  O   ASN A 163    12828  14991   9606  -1371  -5638  -3036       O  
ATOM   1240  CB  ASN A 163     -20.283  -1.483 -27.550  1.00101.77           C  
ANISOU 1240  CB  ASN A 163    13192  15141  10337  -1637  -5454  -3461       C  
ATOM   1241  CG  ASN A 163     -20.742  -2.896 -27.254  1.00109.43           C  
ANISOU 1241  CG  ASN A 163    14071  15972  11536  -1783  -5439  -3661       C  
ATOM   1242  OD1 ASN A 163     -21.746  -3.105 -26.573  1.00111.20           O  
ANISOU 1242  OD1 ASN A 163    14052  16133  12066  -1838  -5505  -3666       O  
ATOM   1243  ND2 ASN A 163     -20.008  -3.877 -27.769  1.00107.28           N  
ANISOU 1243  ND2 ASN A 163    13993  15649  11118  -1850  -5347  -3829       N  
ATOM   1244  N   LEU A 164     -20.187   1.669 -25.920  1.00105.15           N  
ANISOU 1244  N   LEU A 164    13416  15610  10928  -1313  -5410  -2934       N  
ATOM   1245  CA  LEU A 164     -19.624   3.008 -26.006  1.00101.97           C  
ANISOU 1245  CA  LEU A 164    13118  15279  10348  -1173  -5396  -2726       C  
ATOM   1246  C   LEU A 164     -18.112   2.949 -25.835  1.00 97.64           C  
ANISOU 1246  C   LEU A 164    12788  14690   9622  -1155  -5152  -2721       C  
ATOM   1247  O   LEU A 164     -17.596   2.161 -25.035  1.00 96.63           O  
ANISOU 1247  O   LEU A 164    12637  14428   9650  -1206  -4971  -2824       O  
ATOM   1248  CB  LEU A 164     -20.246   3.935 -24.956  1.00 95.11           C  
ANISOU 1248  CB  LEU A 164    12019  14355   9762  -1077  -5427  -2571       C  
ATOM   1249  CG  LEU A 164     -20.052   3.636 -23.467  1.00 91.54           C  
ANISOU 1249  CG  LEU A 164    11408  13745   9630  -1093  -5236  -2589       C  
ATOM   1250  CD1 LEU A 164     -18.869   4.410 -22.896  1.00 84.57           C  
ANISOU 1250  CD1 LEU A 164    10653  12820   8659   -995  -5056  -2452       C  
ATOM   1251  CD2 LEU A 164     -21.323   3.946 -22.691  1.00 87.88           C  
ANISOU 1251  CD2 LEU A 164    10629  13253   9510  -1078  -5336  -2550       C  
ATOM   1252  N   SER A 165     -17.406   3.786 -26.597  1.00 99.00           N  
ANISOU 1252  N   SER A 165    13170  14980   9466  -1085  -5146  -2599       N  
ATOM   1253  CA  SER A 165     -15.944   3.836 -26.550  1.00 96.30           C  
ANISOU 1253  CA  SER A 165    13040  14628   8921  -1066  -4912  -2586       C  
ATOM   1254  C   SER A 165     -15.521   5.263 -26.905  1.00 93.96           C  
ANISOU 1254  C   SER A 165    12869  14434   8397   -956  -4931  -2351       C  
ATOM   1255  O   SER A 165     -15.374   5.606 -28.080  1.00100.41           O  
ANISOU 1255  O   SER A 165    13853  15403   8893   -957  -5006  -2311       O  
ATOM   1256  CB  SER A 165     -15.321   2.815 -27.491  1.00100.96           C  
ANISOU 1256  CB  SER A 165    13821  15271   9267  -1164  -4839  -2777       C  
ATOM   1257  OG  SER A 165     -13.913   2.962 -27.542  1.00103.55           O  
ANISOU 1257  OG  SER A 165    14350  15614   9380  -1140  -4613  -2760       O  
ATOM   1258  N   LYS A 166     -15.329   6.082 -25.878  1.00 94.92           N  
ANISOU 1258  N   LYS A 166    12911  14467   8687   -865  -4861  -2196       N  
ATOM   1259  CA  LYS A 166     -14.904   7.463 -26.044  1.00 99.40           C  
ANISOU 1259  CA  LYS A 166    13596  15089   9084   -759  -4865  -1957       C  
ATOM   1260  C   LYS A 166     -13.481   7.639 -25.531  1.00 92.72           C  
ANISOU 1260  C   LYS A 166    12896  14195   8138   -741  -4602  -1914       C  
ATOM   1261  O   LYS A 166     -12.909   6.755 -24.890  1.00 96.16           O  
ANISOU 1261  O   LYS A 166    13310  14540   8686   -790  -4428  -2062       O  
ATOM   1262  CB  LYS A 166     -15.861   8.421 -25.323  1.00 93.89           C  
ANISOU 1262  CB  LYS A 166    12695  14325   8654   -659  -5012  -1795       C  
ATOM   1263  CG  LYS A 166     -17.232   8.531 -25.975  1.00107.81           C  
ANISOU 1263  CG  LYS A 166    14330  16160  10472   -650  -5287  -1797       C  
ATOM   1264  CD  LYS A 166     -17.131   9.051 -27.403  1.00111.68           C  
ANISOU 1264  CD  LYS A 166    15033  16810  10590   -634  -5411  -1711       C  
ATOM   1265  CE  LYS A 166     -18.501   9.135 -28.063  1.00113.66           C  
ANISOU 1265  CE  LYS A 166    15156  17133  10895   -621  -5698  -1721       C  
ATOM   1266  NZ  LYS A 166     -18.421   9.607 -29.474  1.00110.65           N  
ANISOU 1266  NZ  LYS A 166    14986  16913  10142   -608  -5828  -1641       N  
ATOM   1267  N   SER A 167     -12.909   8.802 -25.829  1.00 82.72           N  
ANISOU 1267  N   SER A 167    11782  12985   6665   -671  -4573  -1705       N  
ATOM   1268  CA  SER A 167     -11.539   9.104 -25.439  1.00 81.84           C  
ANISOU 1268  CA  SER A 167    11821  12844   6430   -658  -4325  -1641       C  
ATOM   1269  C   SER A 167     -11.373  10.615 -25.383  1.00 81.50           C  
ANISOU 1269  C   SER A 167    11857  12798   6312   -567  -4356  -1357       C  
ATOM   1270  O   SER A 167     -12.208  11.372 -25.884  1.00 82.22           O  
ANISOU 1270  O   SER A 167    11925  12930   6383   -513  -4565  -1223       O  
ATOM   1271  CB  SER A 167     -10.532   8.473 -26.405  1.00 81.77           C  
ANISOU 1271  CB  SER A 167    12020  12961   6087   -733  -4169  -1769       C  
ATOM   1272  OG  SER A 167     -10.819   8.827 -27.745  1.00 85.07           O  
ANISOU 1272  OG  SER A 167    12559  13549   6214   -742  -4303  -1720       O  
ATOM   1273  N   TYR A 168     -10.278  11.046 -24.761  1.00 77.90           N  
ANISOU 1273  N   TYR A 168    11495  12281   5822   -552  -4145  -1264       N  
ATOM   1274  CA  TYR A 168      -9.988  12.467 -24.629  1.00 77.49           C  
ANISOU 1274  CA  TYR A 168    11533  12200   5711   -483  -4142   -989       C  
ATOM   1275  C   TYR A 168      -8.483  12.681 -24.644  1.00 82.97           C  
ANISOU 1275  C   TYR A 168    12425  12917   6181   -527  -3867   -933       C  
ATOM   1276  O   TYR A 168      -7.744  11.967 -23.959  1.00 82.46           O  
ANISOU 1276  O   TYR A 168    12331  12799   6203   -565  -3657  -1063       O  
ATOM   1277  CB  TYR A 168     -10.591  13.039 -23.341  1.00 75.36           C  
ANISOU 1277  CB  TYR A 168    11066  11768   5798   -400  -4213   -892       C  
ATOM   1278  CG  TYR A 168     -10.127  14.444 -23.024  1.00 76.09           C  
ANISOU 1278  CG  TYR A 168    11254  11797   5859   -335  -4172   -623       C  
ATOM   1279  CD1 TYR A 168     -10.687  15.542 -23.662  1.00 76.72           C  
ANISOU 1279  CD1 TYR A 168    11387  11899   5865   -267  -4349   -424       C  
ATOM   1280  CD2 TYR A 168      -9.132  14.671 -22.081  1.00 73.85           C  
ANISOU 1280  CD2 TYR A 168    10951  11421   5687   -340  -3870   -561       C  
ATOM   1281  CE1 TYR A 168     -10.266  16.826 -23.375  1.00 78.98           C  
ANISOU 1281  CE1 TYR A 168    11765  12105   6138   -212  -4312   -179       C  
ATOM   1282  CE2 TYR A 168      -8.705  15.951 -21.787  1.00 73.56           C  
ANISOU 1282  CE2 TYR A 168    10989  11318   5644   -290  -3814   -320       C  
ATOM   1283  CZ  TYR A 168      -9.276  17.025 -22.437  1.00 82.08           C  
ANISOU 1283  CZ  TYR A 168    12180  12408   6600   -232  -4073   -129       C  
ATOM   1284  OH  TYR A 168      -8.854  18.303 -22.149  1.00 87.65           O  
ANISOU 1284  OH  TYR A 168    12970  13025   7307   -187  -4025    111       O  
ATOM   1285  N   ALA A 169      -8.041  13.662 -25.425  1.00 95.41           N  
ANISOU 1285  N   ALA A 169    14183  14571   7497   -520  -3848   -738       N  
ATOM   1286  CA  ALA A 169      -6.645  14.068 -25.473  1.00 98.70           C  
ANISOU 1286  CA  ALA A 169    14775  15016   7710   -567  -3580   -647       C  
ATOM   1287  C   ALA A 169      -6.459  15.339 -24.656  1.00 98.32           C  
ANISOU 1287  C   ALA A 169    14731  14837   7789   -520  -3558   -389       C  
ATOM   1288  O   ALA A 169      -7.327  16.217 -24.649  1.00101.52           O  
ANISOU 1288  O   ALA A 169    15092  15183   8299   -440  -3769   -226       O  
ATOM   1289  CB  ALA A 169      -6.185  14.294 -26.913  1.00 94.03           C  
ANISOU 1289  CB  ALA A 169    14389  14599   6741   -602  -3543   -607       C  
ATOM   1290  N   ASN A 170      -5.321  15.435 -23.974  1.00 91.96           N  
ANISOU 1290  N   ASN A 170    13953  13985   7002   -561  -3284   -361       N  
ATOM   1291  CA  ASN A 170      -5.065  16.530 -23.040  1.00 90.96           C  
ANISOU 1291  CA  ASN A 170    13769  13717   7075   -508  -3193   -148       C  
ATOM   1292  C   ASN A 170      -4.667  17.775 -23.823  1.00 95.06           C  
ANISOU 1292  C   ASN A 170    14536  14281   7302   -539  -3241    107       C  
ATOM   1293  O   ASN A 170      -3.495  17.998 -24.132  1.00 98.79           O  
ANISOU 1293  O   ASN A 170    15147  14818   7572   -619  -3003    160       O  
ATOM   1294  CB  ASN A 170      -3.988  16.133 -22.038  1.00 92.71           C  
ANISOU 1294  CB  ASN A 170    13886  13875   7467   -531  -2852   -225       C  
ATOM   1295  CG  ASN A 170      -3.989  17.011 -20.805  1.00 94.25           C  
ANISOU 1295  CG  ASN A 170    13947  13899   7965   -461  -2785    -68       C  
ATOM   1296  OD1 ASN A 170      -4.396  18.172 -20.853  1.00 95.89           O  
ANISOU 1296  OD1 ASN A 170    14210  14047   8177   -414  -2932    143       O  
ATOM   1297  ND2 ASN A 170      -3.534  16.458 -19.686  1.00 92.13           N  
ANISOU 1297  ND2 ASN A 170    13510  13546   7951   -451  -2571   -174       N  
ATOM   1298  N   ASN A 171      -5.656  18.602 -24.142  1.00 92.73           N  
ANISOU 1298  N   ASN A 171    14232  13938   7062   -453  -3495    260       N  
ATOM   1299  CA  ASN A 171      -5.430  19.887 -24.806  1.00 92.29           C  
ANISOU 1299  CA  ASN A 171    14349  13875   6842   -446  -3519    520       C  
ATOM   1300  C   ASN A 171      -5.496  21.039 -23.811  1.00 88.26           C  
ANISOU 1300  C   ASN A 171    13795  13175   6566   -379  -3548    726       C  
ATOM   1301  O   ASN A 171      -6.245  21.998 -23.991  1.00 94.40           O  
ANISOU 1301  O   ASN A 171    14580  13869   7418   -290  -3753    894       O  
ATOM   1302  CB  ASN A 171      -6.439  20.082 -25.931  1.00104.62           C  
ANISOU 1302  CB  ASN A 171    15952  15509   8289   -393  -3785    557       C  
ATOM   1303  CG  ASN A 171      -6.234  19.108 -27.073  1.00121.20           C  
ANISOU 1303  CG  ASN A 171    18139  17808  10104   -465  -3743    379       C  
ATOM   1304  OD1 ASN A 171      -5.109  18.709 -27.369  1.00129.68           O  
ANISOU 1304  OD1 ASN A 171    19320  18977  10974   -557  -3489    310       O  
ATOM   1305  ND2 ASN A 171      -7.326  18.721 -27.723  1.00115.93           N  
ANISOU 1305  ND2 ASN A 171    17413  17208   9428   -419  -3990    293       N  
ATOM   1306  N   LYS A 172      -4.707  20.955 -22.739  1.00 76.31           N  
ANISOU 1306  N   LYS A 172    12230  11587   5179   -416  -3338    707       N  
ATOM   1307  CA  LYS A 172      -4.736  21.974 -21.697  1.00 82.39           C  
ANISOU 1307  CA  LYS A 172    12905  12169   6231   -337  -3310    866       C  
ATOM   1308  C   LYS A 172      -3.370  22.360 -21.151  1.00 85.24           C  
ANISOU 1308  C   LYS A 172    13311  12490   6587   -414  -2984    938       C  
ATOM   1309  O   LYS A 172      -3.302  23.309 -20.364  1.00 91.78           O  
ANISOU 1309  O   LYS A 172    14095  13162   7615   -361  -2960   1083       O  
ATOM   1310  CB  LYS A 172      -5.620  21.514 -20.529  1.00 77.83           C  
ANISOU 1310  CB  LYS A 172    12018  11483   6069   -224  -3356    724       C  
ATOM   1311  CG  LYS A 172      -7.112  21.561 -20.816  1.00 77.87           C  
ANISOU 1311  CG  LYS A 172    11934  11476   6175   -119  -3710    708       C  
ATOM   1312  CD  LYS A 172      -7.604  22.994 -20.928  1.00 92.27           C  
ANISOU 1312  CD  LYS A 172    13845  13182   8030    -26  -3932    956       C  
ATOM   1313  CE  LYS A 172      -9.112  23.043 -21.101  1.00 91.81           C  
ANISOU 1313  CE  LYS A 172    13634  13106   8143    101  -4253    917       C  
ATOM   1314  NZ  LYS A 172      -9.614  24.442 -21.184  1.00 96.13           N  
ANISOU 1314  NZ  LYS A 172    14214  13521   8791    215  -4412   1132       N  
ATOM   1315  N   GLU A 173      -2.292  21.666 -21.522  1.00 90.62           N  
ANISOU 1315  N   GLU A 173    14068  13305   7060   -531  -2736    830       N  
ATOM   1316  CA  GLU A 173      -0.926  21.985 -21.107  1.00 92.52           C  
ANISOU 1316  CA  GLU A 173    14345  13533   7274   -616  -2423    884       C  
ATOM   1317  C   GLU A 173      -0.717  21.852 -19.601  1.00 83.29           C  
ANISOU 1317  C   GLU A 173    12936  12222   6489   -551  -2260    811       C  
ATOM   1318  O   GLU A 173       0.277  22.352 -19.064  1.00 77.24           O  
ANISOU 1318  O   GLU A 173    12177  11405   5767   -598  -2043    886       O  
ATOM   1319  CB  GLU A 173      -0.517  23.387 -21.573  1.00 98.60           C  
ANISOU 1319  CB  GLU A 173    15340  14259   7865   -673  -2452   1171       C  
ATOM   1320  CG  GLU A 173      -0.545  23.569 -23.078  1.00102.30           C  
ANISOU 1320  CG  GLU A 173    16023  14864   7980   -735  -2537   1246       C  
ATOM   1321  CD  GLU A 173      -0.179  24.975 -23.497  1.00107.36           C  
ANISOU 1321  CD  GLU A 173    16826  15425   8541   -767  -2526   1519       C  
ATOM   1322  OE1 GLU A 173      -0.096  25.854 -22.614  1.00110.32           O  
ANISOU 1322  OE1 GLU A 173    17174  15625   9118   -738  -2527   1664       O  
ATOM   1323  OE2 GLU A 173       0.027  25.202 -24.708  1.00102.13           O  
ANISOU 1323  OE2 GLU A 173    16322  14868   7615   -824  -2516   1586       O  
ATOM   1324  N   LYS A 174      -1.635  21.184 -18.905  1.00 83.55           N  
ANISOU 1324  N   LYS A 174    12756  12194   6794   -453  -2359    665       N  
ATOM   1325  CA  LYS A 174      -1.525  20.960 -17.470  1.00 76.98           C  
ANISOU 1325  CA  LYS A 174    11699  11238   6310   -395  -2214    586       C  
ATOM   1326  C   LYS A 174      -2.081  19.581 -17.143  1.00 74.88           C  
ANISOU 1326  C   LYS A 174    11256  11006   6190   -367  -2225    342       C  
ATOM   1327  O   LYS A 174      -2.666  18.906 -17.994  1.00 81.20           O  
ANISOU 1327  O   LYS A 174    12094  11907   6850   -380  -2373    240       O  
ATOM   1328  CB  LYS A 174      -2.267  22.039 -16.668  1.00 81.55           C  
ANISOU 1328  CB  LYS A 174    12192  11645   7146   -289  -2352    735       C  
ATOM   1329  CG  LYS A 174      -1.674  23.434 -16.781  1.00 92.65           C  
ANISOU 1329  CG  LYS A 174    13761  12974   8466   -315  -2328    977       C  
ATOM   1330  CD  LYS A 174      -2.574  24.474 -16.134  1.00105.13           C  
ANISOU 1330  CD  LYS A 174    15267  14381  10295   -190  -2513   1105       C  
ATOM   1331  CE  LYS A 174      -2.028  25.880 -16.336  1.00116.02           C  
ANISOU 1331  CE  LYS A 174    16835  15664  11584   -220  -2518   1353       C  
ATOM   1332  NZ  LYS A 174      -2.935  26.922 -15.777  1.00119.44           N  
ANISOU 1332  NZ  LYS A 174    17206  15915  12258    -84  -2720   1469       N  
ATOM   1333  N   GLU A 175      -1.888  19.163 -15.895  1.00 77.79           N  
ANISOU 1333  N   GLU A 175    11437  11282   6837   -335  -2072    250       N  
ATOM   1334  CA  GLU A 175      -2.472  17.913 -15.426  1.00 71.31           C  
ANISOU 1334  CA  GLU A 175    10442  10459   6193   -313  -2084     40       C  
ATOM   1335  C   GLU A 175      -3.990  18.029 -15.373  1.00 66.52           C  
ANISOU 1335  C   GLU A 175     9723   9812   5741   -235  -2353     42       C  
ATOM   1336  O   GLU A 175      -4.535  19.049 -14.943  1.00 73.08           O  
ANISOU 1336  O   GLU A 175    10509  10549   6709   -160  -2458    182       O  
ATOM   1337  CB  GLU A 175      -1.929  17.553 -14.043  1.00 74.16           C  
ANISOU 1337  CB  GLU A 175    10645  10721   6813   -299  -1868    -27       C  
ATOM   1338  CG  GLU A 175      -0.523  16.986 -14.042  1.00 79.68           C  
ANISOU 1338  CG  GLU A 175    11398  11471   7403   -367  -1613   -109       C  
ATOM   1339  CD  GLU A 175      -0.052  16.612 -12.650  1.00 84.86           C  
ANISOU 1339  CD  GLU A 175    11900  12023   8320   -344  -1433   -171       C  
ATOM   1340  OE1 GLU A 175      -0.360  17.358 -11.696  1.00 77.80           O  
ANISOU 1340  OE1 GLU A 175    10917  11017   7626   -292  -1442    -68       O  
ATOM   1341  OE2 GLU A 175       0.616  15.566 -12.508  1.00 82.19           O  
ANISOU 1341  OE2 GLU A 175    11534  11711   7985   -374  -1290   -326       O  
ATOM   1342  N   VAL A 176      -4.676  16.977 -15.811  1.00 56.98           N  
ANISOU 1342  N   VAL A 176     8460   8671   4519   -250  -2466   -126       N  
ATOM   1343  CA  VAL A 176      -6.134  16.963 -15.870  1.00 58.23           C  
ANISOU 1343  CA  VAL A 176     8495   8814   4815   -189  -2730   -151       C  
ATOM   1344  C   VAL A 176      -6.645  15.856 -14.960  1.00 56.66           C  
ANISOU 1344  C   VAL A 176     8076   8568   4886   -194  -2676   -336       C  
ATOM   1345  O   VAL A 176      -6.375  14.674 -15.199  1.00 56.64           O  
ANISOU 1345  O   VAL A 176     8079   8615   4827   -261  -2606   -507       O  
ATOM   1346  CB  VAL A 176      -6.647  16.777 -17.306  1.00 61.00           C  
ANISOU 1346  CB  VAL A 176     8984   9293   4900   -214  -2960   -176       C  
ATOM   1347  CG1 VAL A 176      -8.142  16.507 -17.303  1.00 62.13           C  
ANISOU 1347  CG1 VAL A 176     8959   9430   5217   -160  -3223   -252       C  
ATOM   1348  CG2 VAL A 176      -6.330  18.009 -18.141  1.00 62.72           C  
ANISOU 1348  CG2 VAL A 176     9422   9540   4868   -206  -3049     43       C  
ATOM   1349  N   LEU A 177      -7.395  16.236 -13.930  1.00 55.66           N  
ANISOU 1349  N   LEU A 177     7759   8343   5048   -127  -2710   -305       N  
ATOM   1350  CA  LEU A 177      -7.973  15.277 -12.997  1.00 54.50           C  
ANISOU 1350  CA  LEU A 177     7396   8147   5162   -143  -2660   -458       C  
ATOM   1351  C   LEU A 177      -9.281  14.742 -13.566  1.00 56.48           C  
ANISOU 1351  C   LEU A 177     7546   8457   5456   -146  -2909   -566       C  
ATOM   1352  O   LEU A 177     -10.209  15.513 -13.829  1.00 64.92           O  
ANISOU 1352  O   LEU A 177     8562   9533   6571    -72  -3125   -490       O  
ATOM   1353  CB  LEU A 177      -8.208  15.925 -11.634  1.00 52.78           C  
ANISOU 1353  CB  LEU A 177     7016   7816   5221    -79  -2573   -386       C  
ATOM   1354  CG  LEU A 177      -9.033  15.098 -10.646  1.00 52.00           C  
ANISOU 1354  CG  LEU A 177     6682   7674   5400    -99  -2547   -520       C  
ATOM   1355  CD1 LEU A 177      -8.314  13.807 -10.286  1.00 50.70           C  
ANISOU 1355  CD1 LEU A 177     6530   7495   5239   -193  -2356   -654       C  
ATOM   1356  CD2 LEU A 177      -9.347  15.909  -9.402  1.00 50.75           C  
ANISOU 1356  CD2 LEU A 177     6374   7425   5483    -27  -2479   -443       C  
ATOM   1357  N   VAL A 178      -9.358  13.426 -13.747  1.00 57.85           N  
ANISOU 1357  N   VAL A 178     7689   8664   5626   -228  -2888   -748       N  
ATOM   1358  CA  VAL A 178     -10.548  12.772 -14.279  1.00 58.62           C  
ANISOU 1358  CA  VAL A 178     7685   8817   5771   -253  -3115   -877       C  
ATOM   1359  C   VAL A 178     -11.133  11.865 -13.205  1.00 57.55           C  
ANISOU 1359  C   VAL A 178     7324   8610   5933   -302  -3038  -1007       C  
ATOM   1360  O   VAL A 178     -10.403  11.123 -12.540  1.00 60.43           O  
ANISOU 1360  O   VAL A 178     7693   8912   6355   -359  -2822  -1072       O  
ATOM   1361  CB  VAL A 178     -10.229  11.977 -15.561  1.00 60.33           C  
ANISOU 1361  CB  VAL A 178     8075   9138   5709   -324  -3187   -993       C  
ATOM   1362  CG1 VAL A 178     -11.497  11.372 -16.145  1.00 62.56           C  
ANISOU 1362  CG1 VAL A 178     8253   9479   6038   -351  -3448  -1126       C  
ATOM   1363  CG2 VAL A 178      -9.549  12.873 -16.581  1.00 61.44           C  
ANISOU 1363  CG2 VAL A 178     8457   9358   5530   -295  -3228   -852       C  
ATOM   1364  N   LEU A 179     -12.452  11.932 -13.036  1.00 58.73           N  
ANISOU 1364  N   LEU A 179     7275   8768   6272   -282  -3219  -1044       N  
ATOM   1365  CA  LEU A 179     -13.166  11.103 -12.077  1.00 58.19           C  
ANISOU 1365  CA  LEU A 179     6979   8647   6484   -346  -3163  -1164       C  
ATOM   1366  C   LEU A 179     -14.287  10.355 -12.781  1.00 60.57           C  
ANISOU 1366  C   LEU A 179     7178   9018   6819   -405  -3395  -1314       C  
ATOM   1367  O   LEU A 179     -14.878  10.852 -13.741  1.00 63.35           O  
ANISOU 1367  O   LEU A 179     7556   9454   7061   -353  -3642  -1292       O  
ATOM   1368  CB  LEU A 179     -13.751  11.934 -10.927  1.00 57.30           C  
ANISOU 1368  CB  LEU A 179     6665   8478   6627   -274  -3118  -1078       C  
ATOM   1369  CG  LEU A 179     -12.782  12.766 -10.085  1.00 66.75           C  
ANISOU 1369  CG  LEU A 179     7932   9599   7831   -213  -2903   -935       C  
ATOM   1370  CD1 LEU A 179     -12.682  14.186 -10.619  1.00 55.72           C  
ANISOU 1370  CD1 LEU A 179     6636   8219   6316    -91  -3022   -770       C  
ATOM   1371  CD2 LEU A 179     -13.205  12.763  -8.625  1.00 53.71           C  
ANISOU 1371  CD2 LEU A 179     6067   7878   6463   -218  -2758   -946       C  
ATOM   1372  N   TRP A 180     -14.578   9.153 -12.291  1.00 60.38           N  
ANISOU 1372  N   TRP A 180     7042   8951   6950   -520  -3324  -1463       N  
ATOM   1373  CA  TRP A 180     -15.672   8.354 -12.823  1.00 62.64           C  
ANISOU 1373  CA  TRP A 180     7204   9289   7308   -598  -3530  -1622       C  
ATOM   1374  C   TRP A 180     -16.120   7.377 -11.745  1.00 61.98           C  
ANISOU 1374  C   TRP A 180     6930   9124   7498   -716  -3400  -1727       C  
ATOM   1375  O   TRP A 180     -15.541   7.312 -10.659  1.00 73.31           O  
ANISOU 1375  O   TRP A 180     8353  10467   9036   -731  -3161  -1673       O  
ATOM   1376  CB  TRP A 180     -15.260   7.615 -14.101  1.00 64.09           C  
ANISOU 1376  CB  TRP A 180     7591   9531   7230   -652  -3633  -1733       C  
ATOM   1377  CG  TRP A 180     -14.251   6.540 -13.873  1.00 62.79           C  
ANISOU 1377  CG  TRP A 180     7553   9288   7017   -739  -3421  -1826       C  
ATOM   1378  CD1 TRP A 180     -14.494   5.205 -13.727  1.00 63.30           C  
ANISOU 1378  CD1 TRP A 180     7565   9294   7194   -865  -3403  -2001       C  
ATOM   1379  CD2 TRP A 180     -12.833   6.704 -13.762  1.00 60.95           C  
ANISOU 1379  CD2 TRP A 180     7515   9018   6625   -703  -3204  -1753       C  
ATOM   1380  NE1 TRP A 180     -13.315   4.528 -13.534  1.00 61.92           N  
ANISOU 1380  NE1 TRP A 180     7546   9039   6941   -895  -3198  -2042       N  
ATOM   1381  CE2 TRP A 180     -12.280   5.426 -13.550  1.00 60.45           C  
ANISOU 1381  CE2 TRP A 180     7504   8875   6591   -796  -3071  -1897       C  
ATOM   1382  CE3 TRP A 180     -11.977   7.807 -13.822  1.00 59.82           C  
ANISOU 1382  CE3 TRP A 180     7504   8899   6327   -605  -3114  -1584       C  
ATOM   1383  CZ2 TRP A 180     -10.911   5.221 -13.398  1.00 58.90           C  
ANISOU 1383  CZ2 TRP A 180     7471   8629   6278   -779  -2856  -1884       C  
ATOM   1384  CZ3 TRP A 180     -10.618   7.601 -13.670  1.00 58.26           C  
ANISOU 1384  CZ3 TRP A 180     7464   8661   6011   -606  -2891  -1571       C  
ATOM   1385  CH2 TRP A 180     -10.099   6.319 -13.460  1.00 57.81           C  
ANISOU 1385  CH2 TRP A 180     7441   8534   5991   -686  -2767  -1724       C  
ATOM   1386  N   GLY A 181     -17.164   6.609 -12.064  1.00 64.02           N  
ANISOU 1386  N   GLY A 181     7043   9416   7867   -810  -3566  -1875       N  
ATOM   1387  CA  GLY A 181     -17.718   5.665 -11.119  1.00 63.89           C  
ANISOU 1387  CA  GLY A 181     6839   9325   8110   -946  -3463  -1974       C  
ATOM   1388  C   GLY A 181     -18.094   4.360 -11.791  1.00 65.76           C  
ANISOU 1388  C   GLY A 181     7088   9558   8339  -1088  -3584  -2165       C  
ATOM   1389  O   GLY A 181     -18.166   4.261 -13.017  1.00 67.50           O  
ANISOU 1389  O   GLY A 181     7419   9858   8371  -1072  -3786  -2236       O  
ATOM   1390  N   VAL A 182     -18.327   3.353 -10.954  1.00 71.60           N  
ANISOU 1390  N   VAL A 182     7723  10200   9283  -1233  -3458  -2247       N  
ATOM   1391  CA  VAL A 182     -18.762   2.032 -11.392  1.00 67.34           C  
ANISOU 1391  CA  VAL A 182     7170   9624   8792  -1392  -3555  -2435       C  
ATOM   1392  C   VAL A 182     -19.933   1.616 -10.514  1.00 70.14           C  
ANISOU 1392  C   VAL A 182     7235   9957   9458  -1527  -3544  -2487       C  
ATOM   1393  O   VAL A 182     -19.804   1.568  -9.285  1.00 69.56           O  
ANISOU 1393  O   VAL A 182     7085   9802   9542  -1571  -3324  -2412       O  
ATOM   1394  CB  VAL A 182     -17.633   0.992 -11.319  1.00 72.36           C  
ANISOU 1394  CB  VAL A 182     8028  10125   9340  -1458  -3392  -2493       C  
ATOM   1395  CG1 VAL A 182     -18.174  -0.393 -11.634  1.00 70.74           C  
ANISOU 1395  CG1 VAL A 182     7792   9854   9231  -1634  -3491  -2691       C  
ATOM   1396  CG2 VAL A 182     -16.514   1.357 -12.279  1.00 70.08           C  
ANISOU 1396  CG2 VAL A 182     8007   9883   8738  -1337  -3403  -2469       C  
ATOM   1397  N   HIS A 183     -21.065   1.313 -11.141  1.00 78.17           N  
ANISOU 1397  N   HIS A 183     8097  11051  10552  -1598  -3766  -2605       N  
ATOM   1398  CA  HIS A 183     -22.287   0.989 -10.420  1.00 72.32           C  
ANISOU 1398  CA  HIS A 183     7079  10313  10087  -1724  -3730  -2625       C  
ATOM   1399  C   HIS A 183     -22.358  -0.503 -10.122  1.00 73.06           C  
ANISOU 1399  C   HIS A 183     7202  10273  10286  -1939  -3635  -2728       C  
ATOM   1400  O   HIS A 183     -22.026  -1.337 -10.969  1.00 74.04           O  
ANISOU 1400  O   HIS A 183     7509  10348  10273  -1990  -3708  -2823       O  
ATOM   1401  CB  HIS A 183     -23.513   1.418 -11.226  1.00 75.08           C  
ANISOU 1401  CB  HIS A 183     7275  10803  10451  -1684  -3948  -2637       C  
ATOM   1402  CG  HIS A 183     -24.800   1.310 -10.471  1.00 81.75           C  
ANISOU 1402  CG  HIS A 183     7806  11680  11575  -1784  -3908  -2649       C  
ATOM   1403  ND1 HIS A 183     -25.986   0.945 -11.071  1.00 85.65           N  
ANISOU 1403  ND1 HIS A 183     8156  12247  12139  -1858  -4064  -2722       N  
ATOM   1404  CD2 HIS A 183     -25.089   1.526  -9.166  1.00 84.24           C  
ANISOU 1404  CD2 HIS A 183     7924  11974  12108  -1826  -3721  -2600       C  
ATOM   1405  CE1 HIS A 183     -26.950   0.936 -10.167  1.00 88.59           C  
ANISOU 1405  CE1 HIS A 183     8252  12645  12765  -1941  -3973  -2719       C  
ATOM   1406  NE2 HIS A 183     -26.432   1.286  -9.003  1.00 90.77           N  
ANISOU 1406  NE2 HIS A 183     8494  12867  13129  -1924  -3759  -2645       N  
ATOM   1407  N   HIS A 184     -22.797  -0.830  -8.909  1.00 74.90           N  
ANISOU 1407  N   HIS A 184     7259  10443  10756  -2066  -3466  -2706       N  
ATOM   1408  CA  HIS A 184     -22.960  -2.212  -8.461  1.00 79.56           C  
ANISOU 1408  CA  HIS A 184     7865  10891  11473  -2286  -3364  -2774       C  
ATOM   1409  C   HIS A 184     -24.366  -2.377  -7.902  1.00 84.68           C  
ANISOU 1409  C   HIS A 184     8224  11595  12357  -2423  -3345  -2774       C  
ATOM   1410  O   HIS A 184     -24.615  -2.049  -6.727  1.00 81.64           O  
ANISOU 1410  O   HIS A 184     7675  11212  12133  -2460  -3173  -2699       O  
ATOM   1411  CB  HIS A 184     -21.913  -2.581  -7.418  1.00 80.53           C  
ANISOU 1411  CB  HIS A 184     8111  10856  11633  -2332  -3140  -2729       C  
ATOM   1412  CG  HIS A 184     -20.504  -2.424  -7.898  1.00 75.10           C  
ANISOU 1412  CG  HIS A 184     7706  10115  10715  -2191  -3127  -2718       C  
ATOM   1413  ND1 HIS A 184     -19.705  -3.498  -8.226  1.00 69.24           N  
ANISOU 1413  ND1 HIS A 184     7195   9224   9891  -2252  -3105  -2802       N  
ATOM   1414  CD2 HIS A 184     -19.753  -1.318  -8.112  1.00 67.41           C  
ANISOU 1414  CD2 HIS A 184     6842   9216   9555  -1983  -3095  -2599       C  
ATOM   1415  CE1 HIS A 184     -18.522  -3.061  -8.618  1.00 67.50           C  
ANISOU 1415  CE1 HIS A 184     7198   9003   9444  -2085  -3054  -2743       C  
ATOM   1416  NE2 HIS A 184     -18.525  -1.742  -8.558  1.00 66.35           N  
ANISOU 1416  NE2 HIS A 184     6989   8993   9229  -1929  -3045  -2614       N  
ATOM   1417  N   PRO A 185     -25.305  -2.874  -8.701  1.00 80.55           N  
ANISOU 1417  N   PRO A 185     7628  11125  11853  -2502  -3511  -2860       N  
ATOM   1418  CA  PRO A 185     -26.696  -2.977  -8.253  1.00 81.63           C  
ANISOU 1418  CA  PRO A 185     7473  11335  12208  -2624  -3507  -2868       C  
ATOM   1419  C   PRO A 185     -26.860  -4.074  -7.218  1.00 93.55           C  
ANISOU 1419  C   PRO A 185     8950  12704  13889  -2863  -3314  -2866       C  
ATOM   1420  O   PRO A 185     -25.987  -4.943  -7.071  1.00 92.12           O  
ANISOU 1420  O   PRO A 185     8993  12352  13656  -2944  -3231  -2880       O  
ATOM   1421  CB  PRO A 185     -27.460  -3.311  -9.546  1.00 83.86           C  
ANISOU 1421  CB  PRO A 185     7740  11697  12426  -2643  -3756  -2972       C  
ATOM   1422  CG  PRO A 185     -26.522  -2.965 -10.660  1.00 82.90           C  
ANISOU 1422  CG  PRO A 185     7874  11591  12033  -2477  -3895  -2990       C  
ATOM   1423  CD  PRO A 185     -25.158  -3.235 -10.119  1.00 80.79           C  
ANISOU 1423  CD  PRO A 185     7832  11176  11689  -2465  -3718  -2955       C  
ATOM   1424  N   PRO A 186     -27.970  -4.068  -6.478  1.00101.53           N  
ANISOU 1424  N   PRO A 186     9694  13779  15106  -2978  -3236  -2844       N  
ATOM   1425  CA  PRO A 186     -28.164  -5.068  -5.419  1.00101.98           C  
ANISOU 1425  CA  PRO A 186     9723  13706  15317  -3219  -3040  -2817       C  
ATOM   1426  C   PRO A 186     -28.522  -6.453  -5.938  1.00107.61           C  
ANISOU 1426  C   PRO A 186    10521  14308  16056  -3426  -3128  -2909       C  
ATOM   1427  O   PRO A 186     -27.978  -7.456  -5.468  1.00121.46           O  
ANISOU 1427  O   PRO A 186    12447  15874  17828  -3575  -3015  -2895       O  
ATOM   1428  CB  PRO A 186     -29.311  -4.475  -4.594  1.00 96.75           C  
ANISOU 1428  CB  PRO A 186     8731  13186  14842  -3254  -2945  -2771       C  
ATOM   1429  CG  PRO A 186     -30.059  -3.615  -5.560  1.00 96.22           C  
ANISOU 1429  CG  PRO A 186     8507  13303  14751  -3091  -3168  -2825       C  
ATOM   1430  CD  PRO A 186     -29.021  -3.036  -6.468  1.00 96.89           C  
ANISOU 1430  CD  PRO A 186     8818  13383  14611  -2876  -3303  -2827       C  
ATOM   1431  N   ASN A 187     -29.441  -6.526  -6.895  1.00 89.16           N  
ANISOU 1431  N   ASN A 187     8071  12080  13727  -3437  -3335  -3002       N  
ATOM   1432  CA  ASN A 187     -29.919  -7.796  -7.422  1.00 99.17           C  
ANISOU 1432  CA  ASN A 187     9390  13258  15030  -3639  -3433  -3101       C  
ATOM   1433  C   ASN A 187     -29.797  -7.796  -8.942  1.00108.43           C  
ANISOU 1433  C   ASN A 187    10691  14484  16023  -3528  -3688  -3214       C  
ATOM   1434  O   ASN A 187     -29.409  -6.800  -9.561  1.00110.67           O  
ANISOU 1434  O   ASN A 187    11014  14878  16158  -3304  -3788  -3203       O  
ATOM   1435  CB  ASN A 187     -31.366  -8.072  -6.991  1.00101.98           C  
ANISOU 1435  CB  ASN A 187     9449  13696  15603  -3823  -3421  -3110       C  
ATOM   1436  CG  ASN A 187     -32.320  -6.970  -7.404  1.00101.67           C  
ANISOU 1436  CG  ASN A 187     9138  13890  15602  -3677  -3553  -3129       C  
ATOM   1437  OD1 ASN A 187     -32.715  -6.877  -8.566  1.00 99.88           O  
ANISOU 1437  OD1 ASN A 187     8902  13751  15299  -3611  -3786  -3219       O  
ATOM   1438  ND2 ASN A 187     -32.706  -6.135  -6.447  1.00104.18           N  
ANISOU 1438  ND2 ASN A 187     9237  14307  16039  -3625  -3404  -3045       N  
ATOM   1439  N   ILE A 188     -30.137  -8.938  -9.542  1.00115.57           N  
ANISOU 1439  N   ILE A 188    11669  15305  16936  -3695  -3792  -3321       N  
ATOM   1440  CA  ILE A 188     -30.035  -9.092 -10.989  1.00121.08           C  
ANISOU 1440  CA  ILE A 188    12505  16046  17454  -3617  -4024  -3442       C  
ATOM   1441  C   ILE A 188     -31.172  -8.369 -11.702  1.00129.13           C  
ANISOU 1441  C   ILE A 188    13289  17283  18492  -3547  -4225  -3479       C  
ATOM   1442  O   ILE A 188     -31.002  -7.901 -12.837  1.00125.02           O  
ANISOU 1442  O   ILE A 188    12859  16860  17784  -3392  -4414  -3529       O  
ATOM   1443  CB  ILE A 188     -30.011 -10.586 -11.354  1.00119.50           C  
ANISOU 1443  CB  ILE A 188    12467  15675  17263  -3823  -4061  -3554       C  
ATOM   1444  CG1 ILE A 188     -29.065 -11.350 -10.426  1.00115.61           C  
ANISOU 1444  CG1 ILE A 188    12169  14950  16809  -3917  -3849  -3499       C  
ATOM   1445  CG2 ILE A 188     -29.601 -10.776 -12.804  1.00115.17           C  
ANISOU 1445  CG2 ILE A 188    12123  15149  16489  -3726  -4263  -3682       C  
ATOM   1446  CD1 ILE A 188     -29.050 -12.842 -10.675  1.00122.13           C  
ANISOU 1446  CD1 ILE A 188    13158  15581  17665  -4123  -3875  -3601       C  
ATOM   1447  N   GLY A 189     -32.340  -8.270 -11.063  1.00132.62           N  
ANISOU 1447  N   GLY A 189    13431  17807  19152  -3657  -4189  -3454       N  
ATOM   1448  CA  GLY A 189     -33.471  -7.615 -11.700  1.00130.08           C  
ANISOU 1448  CA  GLY A 189    12867  17685  18871  -3588  -4383  -3494       C  
ATOM   1449  C   GLY A 189     -33.213  -6.150 -11.993  1.00131.94           C  
ANISOU 1449  C   GLY A 189    13072  18067  18992  -3305  -4452  -3424       C  
ATOM   1450  O   GLY A 189     -33.542  -5.656 -13.074  1.00130.17           O  
ANISOU 1450  O   GLY A 189    12840  17967  18653  -3180  -4682  -3470       O  
ATOM   1451  N   ASP A 190     -32.622  -5.433 -11.034  1.00127.01           N  
ANISOU 1451  N   ASP A 190    12439  17425  18394  -3204  -4261  -3308       N  
ATOM   1452  CA  ASP A 190     -32.275  -4.037 -11.274  1.00115.53           C  
ANISOU 1452  CA  ASP A 190    10982  16086  16827  -2935  -4320  -3233       C  
ATOM   1453  C   ASP A 190     -31.090  -3.910 -12.225  1.00102.49           C  
ANISOU 1453  C   ASP A 190     9655  14393  14894  -2795  -4418  -3240       C  
ATOM   1454  O   ASP A 190     -30.998  -2.928 -12.970  1.00 99.54           O  
ANISOU 1454  O   ASP A 190     9313  14133  14375  -2593  -4573  -3208       O  
ATOM   1455  CB  ASP A 190     -31.981  -3.332  -9.949  1.00113.41           C  
ANISOU 1455  CB  ASP A 190    10611  15808  16671  -2876  -4081  -3115       C  
ATOM   1456  CG  ASP A 190     -33.214  -3.204  -9.072  1.00124.97           C  
ANISOU 1456  CG  ASP A 190    11733  17358  18393  -2972  -3988  -3106       C  
ATOM   1457  OD1 ASP A 190     -33.928  -2.186  -9.194  1.00135.01           O  
ANISOU 1457  OD1 ASP A 190    12794  18781  19723  -2822  -4079  -3092       O  
ATOM   1458  OD2 ASP A 190     -33.469  -4.120  -8.262  1.00124.75           O  
ANISOU 1458  OD2 ASP A 190    11649  17243  18506  -3198  -3823  -3112       O  
ATOM   1459  N   GLN A 191     -30.185  -4.891 -12.219  1.00 93.51           N  
ANISOU 1459  N   GLN A 191     8765  13092  13672  -2899  -4330  -3279       N  
ATOM   1460  CA  GLN A 191     -29.061  -4.886 -13.151  1.00 92.24           C  
ANISOU 1460  CA  GLN A 191     8914  12894  13239  -2781  -4409  -3305       C  
ATOM   1461  C   GLN A 191     -29.548  -4.946 -14.594  1.00 95.01           C  
ANISOU 1461  C   GLN A 191     9309  13353  13439  -2747  -4677  -3400       C  
ATOM   1462  O   GLN A 191     -29.316  -4.020 -15.384  1.00 94.79           O  
ANISOU 1462  O   GLN A 191     9353  13439  13223  -2559  -4816  -3363       O  
ATOM   1463  CB  GLN A 191     -28.127  -6.058 -12.844  1.00 91.08           C  
ANISOU 1463  CB  GLN A 191     8999  12542  13065  -2912  -4263  -3351       C  
ATOM   1464  CG  GLN A 191     -27.139  -6.381 -13.955  1.00 90.79           C  
ANISOU 1464  CG  GLN A 191     9273  12464  12759  -2834  -4356  -3428       C  
ATOM   1465  CD  GLN A 191     -26.177  -5.245 -14.235  1.00 96.09           C  
ANISOU 1465  CD  GLN A 191    10080  13208  13221  -2600  -4357  -3343       C  
ATOM   1466  OE1 GLN A 191     -25.686  -4.590 -13.315  1.00 92.57           O  
ANISOU 1466  OE1 GLN A 191     9601  12742  12831  -2523  -4203  -3233       O  
ATOM   1467  NE2 GLN A 191     -25.904  -5.002 -15.512  1.00 98.18           N  
ANISOU 1467  NE2 GLN A 191    10505  13562  13237  -2494  -4529  -3392       N  
ATOM   1468  N   ARG A 192     -30.226  -6.040 -14.957  1.00111.58           N  
ANISOU 1468  N   ARG A 192    11373  15412  15610  -2937  -4755  -3519       N  
ATOM   1469  CA  ARG A 192     -30.776  -6.154 -16.303  1.00104.18           C  
ANISOU 1469  CA  ARG A 192    10463  14581  14540  -2924  -5014  -3620       C  
ATOM   1470  C   ARG A 192     -31.778  -5.046 -16.590  1.00102.36           C  
ANISOU 1470  C   ARG A 192     9991  14544  14355  -2799  -5178  -3570       C  
ATOM   1471  O   ARG A 192     -31.876  -4.575 -17.728  1.00103.76           O  
ANISOU 1471  O   ARG A 192    10243  14837  14343  -2682  -5392  -3590       O  
ATOM   1472  CB  ARG A 192     -31.442  -7.517 -16.491  1.00112.43           C  
ANISOU 1472  CB  ARG A 192    11475  15545  15697  -3167  -5060  -3756       C  
ATOM   1473  CG  ARG A 192     -30.520  -8.710 -16.336  1.00117.46           C  
ANISOU 1473  CG  ARG A 192    12364  15974  16290  -3292  -4928  -3821       C  
ATOM   1474  CD  ARG A 192     -31.305 -10.001 -16.490  1.00120.37           C  
ANISOU 1474  CD  ARG A 192    12681  16262  16792  -3538  -4986  -3948       C  
ATOM   1475  NE  ARG A 192     -30.495 -11.182 -16.208  1.00120.80           N  
ANISOU 1475  NE  ARG A 192    12963  16091  16844  -3665  -4852  -4004       N  
ATOM   1476  CZ  ARG A 192     -30.989 -12.408 -16.072  1.00117.78           C  
ANISOU 1476  CZ  ARG A 192    12570  15582  16601  -3899  -4849  -4092       C  
ATOM   1477  NH1 ARG A 192     -32.293 -12.615 -16.189  1.00112.04           N  
ANISOU 1477  NH1 ARG A 192    11605  14941  16025  -4039  -4967  -4138       N  
ATOM   1478  NH2 ARG A 192     -30.180 -13.426 -15.813  1.00123.37           N  
ANISOU 1478  NH2 ARG A 192    13503  16071  17301  -3990  -4729  -4135       N  
ATOM   1479  N   ALA A 193     -32.524  -4.614 -15.571  1.00102.30           N  
ANISOU 1479  N   ALA A 193     9700  14575  14593  -2819  -5079  -3503       N  
ATOM   1480  CA  ALA A 193     -33.518  -3.567 -15.755  1.00103.95           C  
ANISOU 1480  CA  ALA A 193     9660  14958  14878  -2691  -5225  -3463       C  
ATOM   1481  C   ALA A 193     -32.887  -2.214 -16.053  1.00109.01           C  
ANISOU 1481  C   ALA A 193    10400  15673  15345  -2424  -5278  -3348       C  
ATOM   1482  O   ALA A 193     -33.547  -1.357 -16.650  1.00103.72           O  
ANISOU 1482  O   ALA A 193     9617  15141  14651  -2286  -5472  -3323       O  
ATOM   1483  CB  ALA A 193     -34.406  -3.465 -14.514  1.00104.37           C  
ANISOU 1483  CB  ALA A 193     9388  15029  15238  -2778  -5072  -3429       C  
ATOM   1484  N   LEU A 194     -31.633  -2.003 -15.657  1.00117.28           N  
ANISOU 1484  N   LEU A 194    11659  16629  16275  -2351  -5118  -3274       N  
ATOM   1485  CA  LEU A 194     -30.974  -0.720 -15.861  1.00116.57           C  
ANISOU 1485  CA  LEU A 194    11671  16596  16022  -2111  -5151  -3153       C  
ATOM   1486  C   LEU A 194     -30.011  -0.706 -17.039  1.00110.23           C  
ANISOU 1486  C   LEU A 194    11199  15796  14886  -2027  -5266  -3161       C  
ATOM   1487  O   LEU A 194     -29.887   0.329 -17.702  1.00107.87           O  
ANISOU 1487  O   LEU A 194    10967  15595  14422  -1843  -5408  -3080       O  
ATOM   1488  CB  LEU A 194     -30.218  -0.302 -14.595  1.00113.35           C  
ANISOU 1488  CB  LEU A 194    11262  16104  15701  -2066  -4894  -3052       C  
ATOM   1489  CG  LEU A 194     -31.066   0.236 -13.440  1.00114.73           C  
ANISOU 1489  CG  LEU A 194    11115  16320  16158  -2062  -4778  -3001       C  
ATOM   1490  CD1 LEU A 194     -30.185   0.619 -12.263  1.00108.40           C  
ANISOU 1490  CD1 LEU A 194    10352  15434  15402  -2020  -4525  -2906       C  
ATOM   1491  CD2 LEU A 194     -31.902   1.421 -13.894  1.00118.05           C  
ANISOU 1491  CD2 LEU A 194    11364  16889  16601  -1878  -4969  -2955       C  
ATOM   1492  N   TYR A 195     -29.325  -1.813 -17.324  1.00 95.88           N  
ANISOU 1492  N   TYR A 195     9595  13875  12961  -2154  -5207  -3255       N  
ATOM   1493  CA  TYR A 195     -28.302  -1.811 -18.361  1.00 95.38           C  
ANISOU 1493  CA  TYR A 195     9851  13816  12573  -2075  -5274  -3269       C  
ATOM   1494  C   TYR A 195     -28.525  -2.839 -19.461  1.00104.73           C  
ANISOU 1494  C   TYR A 195    11156  15006  13630  -2196  -5420  -3422       C  
ATOM   1495  O   TYR A 195     -27.664  -2.974 -20.339  1.00 98.03           O  
ANISOU 1495  O   TYR A 195    10581  14163  12504  -2150  -5456  -3455       O  
ATOM   1496  CB  TYR A 195     -26.918  -2.018 -17.732  1.00 96.30           C  
ANISOU 1496  CB  TYR A 195    10173  13798  12620  -2062  -5044  -3236       C  
ATOM   1497  CG  TYR A 195     -26.594  -0.984 -16.678  1.00 89.12           C  
ANISOU 1497  CG  TYR A 195     9168  12882  11812  -1939  -4901  -3089       C  
ATOM   1498  CD1 TYR A 195     -26.245   0.312 -17.035  1.00 88.24           C  
ANISOU 1498  CD1 TYR A 195     9120  12865  11541  -1736  -4977  -2965       C  
ATOM   1499  CD2 TYR A 195     -26.649  -1.300 -15.328  1.00 87.55           C  
ANISOU 1499  CD2 TYR A 195     8820  12580  11864  -2033  -4692  -3070       C  
ATOM   1500  CE1 TYR A 195     -25.955   1.264 -16.075  1.00 93.27           C  
ANISOU 1500  CE1 TYR A 195     9672  13490  12275  -1623  -4852  -2836       C  
ATOM   1501  CE2 TYR A 195     -26.360  -0.355 -14.361  1.00 92.80           C  
ANISOU 1501  CE2 TYR A 195     9397  13246  12618  -1923  -4558  -2945       C  
ATOM   1502  CZ  TYR A 195     -26.012   0.924 -14.740  1.00 87.50           C  
ANISOU 1502  CZ  TYR A 195     8787  12665  11795  -1715  -4642  -2834       C  
ATOM   1503  OH  TYR A 195     -25.724   1.865 -13.779  1.00 81.96           O  
ANISOU 1503  OH  TYR A 195     8000  11955  11186  -1606  -4514  -2716       O  
ATOM   1504  N   HIS A 196     -29.644  -3.565 -19.441  1.00110.57           N  
ANISOU 1504  N   HIS A 196    11701  15751  14560  -2353  -5498  -3520       N  
ATOM   1505  CA  HIS A 196     -30.039  -4.486 -20.507  1.00107.79           C  
ANISOU 1505  CA  HIS A 196    11430  15419  14108  -2471  -5665  -3671       C  
ATOM   1506  C   HIS A 196     -29.014  -5.588 -20.753  1.00107.83           C  
ANISOU 1506  C   HIS A 196    11713  15281  13977  -2565  -5558  -3777       C  
ATOM   1507  O   HIS A 196     -29.044  -6.240 -21.801  1.00114.08           O  
ANISOU 1507  O   HIS A 196    12644  16092  14608  -2625  -5691  -3903       O  
ATOM   1508  CB  HIS A 196     -30.312  -3.738 -21.817  1.00114.65           C  
ANISOU 1508  CB  HIS A 196    12365  16461  14737  -2339  -5921  -3658       C  
ATOM   1509  CG  HIS A 196     -31.297  -2.621 -21.682  1.00123.47           C  
ANISOU 1509  CG  HIS A 196    13226  17710  15976  -2222  -6051  -3556       C  
ATOM   1510  ND1 HIS A 196     -32.592  -2.819 -21.253  1.00127.16           N  
ANISOU 1510  ND1 HIS A 196    13380  18212  16724  -2317  -6108  -3599       N  
ATOM   1511  CD2 HIS A 196     -31.180  -1.295 -21.926  1.00123.76           C  
ANISOU 1511  CD2 HIS A 196    13276  17850  15899  -2014  -6134  -3417       C  
ATOM   1512  CE1 HIS A 196     -33.229  -1.662 -21.236  1.00127.91           C  
ANISOU 1512  CE1 HIS A 196    13299  18425  16877  -2162  -6220  -3499       C  
ATOM   1513  NE2 HIS A 196     -32.395  -0.721 -21.640  1.00127.22           N  
ANISOU 1513  NE2 HIS A 196    13409  18373  16555  -1975  -6243  -3384       N  
ATOM   1514  N   LYS A 197     -28.096  -5.809 -19.816  1.00112.26           N  
ANISOU 1514  N   LYS A 197    12359  15697  14596  -2573  -5321  -3734       N  
ATOM   1515  CA  LYS A 197     -27.071  -6.828 -19.970  1.00114.06           C  
ANISOU 1515  CA  LYS A 197    12849  15775  14715  -2641  -5208  -3833       C  
ATOM   1516  C   LYS A 197     -26.885  -7.555 -18.648  1.00119.71           C  
ANISOU 1516  C   LYS A 197    13502  16301  15681  -2771  -4984  -3822       C  
ATOM   1517  O   LYS A 197     -27.241  -7.050 -17.581  1.00116.84           O  
ANISOU 1517  O   LYS A 197    12937  15937  15520  -2769  -4881  -3712       O  
ATOM   1518  CB  LYS A 197     -25.738  -6.229 -20.440  1.00102.41           C  
ANISOU 1518  CB  LYS A 197    11640  14325  12947  -2468  -5154  -3783       C  
ATOM   1519  CG  LYS A 197     -25.801  -5.554 -21.799  1.00 99.11           C  
ANISOU 1519  CG  LYS A 197    11330  14089  12240  -2353  -5362  -3783       C  
ATOM   1520  CD  LYS A 197     -24.445  -5.013 -22.203  1.00 96.97           C  
ANISOU 1520  CD  LYS A 197    11326  13840  11677  -2205  -5280  -3729       C  
ATOM   1521  CE  LYS A 197     -24.529  -4.229 -23.500  1.00 98.81           C  
ANISOU 1521  CE  LYS A 197    11668  14265  11611  -2097  -5477  -3697       C  
ATOM   1522  NZ  LYS A 197     -24.930  -5.088 -24.646  1.00123.23           N  
ANISOU 1522  NZ  LYS A 197    14849  17400  14571  -2201  -5636  -3864       N  
ATOM   1523  N   GLU A 198     -26.311  -8.753 -18.732  1.00129.30           N  
ANISOU 1523  N   GLU A 198    14899  17352  16876  -2882  -4909  -3936       N  
ATOM   1524  CA  GLU A 198     -26.082  -9.582 -17.556  1.00130.05           C  
ANISOU 1524  CA  GLU A 198    14977  17244  17191  -3018  -4708  -3928       C  
ATOM   1525  C   GLU A 198     -24.624  -9.613 -17.121  1.00124.12           C  
ANISOU 1525  C   GLU A 198    14449  16365  16344  -2924  -4519  -3891       C  
ATOM   1526  O   GLU A 198     -24.350  -9.779 -15.928  1.00121.78           O  
ANISOU 1526  O   GLU A 198    14110  15939  16222  -2975  -4336  -3813       O  
ATOM   1527  CB  GLU A 198     -26.569 -11.013 -17.820  1.00148.08           C  
ANISOU 1527  CB  GLU A 198    17293  19402  19571  -3230  -4757  -4079       C  
ATOM   1528  CG  GLU A 198     -26.616 -11.901 -16.586  1.00153.33           C  
ANISOU 1528  CG  GLU A 198    17909  19860  20490  -3408  -4576  -4054       C  
ATOM   1529  CD  GLU A 198     -27.229 -13.262 -16.868  1.00158.73           C  
ANISOU 1529  CD  GLU A 198    18610  20424  21277  -3629  -4645  -4194       C  
ATOM   1530  OE1 GLU A 198     -27.757 -13.460 -17.983  1.00160.93           O  
ANISOU 1530  OE1 GLU A 198    18897  20798  21452  -3648  -4841  -4314       O  
ATOM   1531  OE2 GLU A 198     -27.185 -14.133 -15.973  1.00159.76           O  
ANISOU 1531  OE2 GLU A 198    18751  20361  21588  -3788  -4506  -4181       O  
ATOM   1532  N   ASN A 199     -23.685  -9.445 -18.053  1.00126.16           N  
ANISOU 1532  N   ASN A 199    14944  16663  16327  -2791  -4556  -3942       N  
ATOM   1533  CA  ASN A 199     -22.250  -9.457 -17.760  1.00123.77           C  
ANISOU 1533  CA  ASN A 199    14858  16256  15914  -2687  -4384  -3921       C  
ATOM   1534  C   ASN A 199     -21.628  -8.247 -18.452  1.00116.68           C  
ANISOU 1534  C   ASN A 199    14057  15533  14744  -2482  -4432  -3853       C  
ATOM   1535  O   ASN A 199     -21.177  -8.341 -19.596  1.00117.31           O  
ANISOU 1535  O   ASN A 199    14324  15681  14568  -2424  -4514  -3942       O  
ATOM   1536  CB  ASN A 199     -21.608 -10.765 -18.220  1.00133.51           C  
ANISOU 1536  CB  ASN A 199    16317  17327  17086  -2758  -4351  -4084       C  
ATOM   1537  CG  ASN A 199     -22.308 -11.989 -17.658  1.00139.17           C  
ANISOU 1537  CG  ASN A 199    16953  17868  18058  -2974  -4331  -4149       C  
ATOM   1538  OD1 ASN A 199     -22.658 -12.031 -16.478  1.00139.63           O  
ANISOU 1538  OD1 ASN A 199    16862  17841  18351  -3063  -4222  -4050       O  
ATOM   1539  ND2 ASN A 199     -22.522 -12.989 -18.505  1.00139.00           N  
ANISOU 1539  ND2 ASN A 199    17034  17794  17986  -3069  -4435  -4315       N  
ATOM   1540  N   ALA A 200     -21.602  -7.115 -17.756  1.00 87.15           N  
ANISOU 1540  N   ALA A 200    10195  11865  11051  -2380  -4377  -3694       N  
ATOM   1541  CA  ALA A 200     -21.073  -5.876 -18.302  1.00 85.99           C  
ANISOU 1541  CA  ALA A 200    10130  11878  10665  -2192  -4422  -3602       C  
ATOM   1542  C   ALA A 200     -19.615  -5.695 -17.889  1.00 83.08           C  
ANISOU 1542  C   ALA A 200     9946  11431  10189  -2088  -4232  -3562       C  
ATOM   1543  O   ALA A 200     -19.041  -6.499 -17.151  1.00 81.93           O  
ANISOU 1543  O   ALA A 200     9856  11107  10167  -2150  -4073  -3602       O  
ATOM   1544  CB  ALA A 200     -21.923  -4.686 -17.853  1.00 85.57           C  
ANISOU 1544  CB  ALA A 200     9836  11951  10724  -2128  -4490  -3455       C  
ATOM   1545  N   TYR A 201     -19.009  -4.614 -18.377  1.00 85.23           N  
ANISOU 1545  N   TYR A 201    10319  11838  10228  -1928  -4253  -3475       N  
ATOM   1546  CA  TYR A 201     -17.615  -4.325 -18.078  1.00 85.48           C  
ANISOU 1546  CA  TYR A 201    10523  11824  10132  -1820  -4081  -3435       C  
ATOM   1547  C   TYR A 201     -17.366  -2.837 -18.262  1.00 86.21           C  
ANISOU 1547  C   TYR A 201    10624  12074  10057  -1662  -4118  -3278       C  
ATOM   1548  O   TYR A 201     -18.032  -2.178 -19.064  1.00 88.19           O  
ANISOU 1548  O   TYR A 201    10842  12478  10189  -1622  -4296  -3233       O  
ATOM   1549  CB  TYR A 201     -16.667  -5.130 -18.975  1.00 89.54           C  
ANISOU 1549  CB  TYR A 201    11296  12304  10423  -1815  -4038  -3581       C  
ATOM   1550  CG  TYR A 201     -16.485  -4.546 -20.362  1.00 98.36           C  
ANISOU 1550  CG  TYR A 201    12562  13610  11200  -1734  -4161  -3588       C  
ATOM   1551  CD1 TYR A 201     -17.447  -4.729 -21.347  1.00110.58           C  
ANISOU 1551  CD1 TYR A 201    14082  15259  12676  -1797  -4364  -3652       C  
ATOM   1552  CD2 TYR A 201     -15.348  -3.816 -20.687  1.00 97.08           C  
ANISOU 1552  CD2 TYR A 201    12574  13528  10782  -1604  -4069  -3526       C  
ATOM   1553  CE1 TYR A 201     -17.285  -4.197 -22.616  1.00108.99           C  
ANISOU 1553  CE1 TYR A 201    14028  15232  12150  -1734  -4476  -3648       C  
ATOM   1554  CE2 TYR A 201     -15.177  -3.280 -21.953  1.00 97.19           C  
ANISOU 1554  CE2 TYR A 201    12738  13718  10471  -1549  -4168  -3517       C  
ATOM   1555  CZ  TYR A 201     -16.148  -3.474 -22.913  1.00101.22           C  
ANISOU 1555  CZ  TYR A 201    13225  14325  10910  -1614  -4373  -3575       C  
ATOM   1556  OH  TYR A 201     -15.983  -2.944 -24.172  1.00109.77           O  
ANISOU 1556  OH  TYR A 201    14465  15585  11658  -1569  -4473  -3559       O  
ATOM   1557  N   VAL A 202     -16.403  -2.316 -17.504  1.00 84.28           N  
ANISOU 1557  N   VAL A 202    10428  11786   9808  -1573  -3956  -3191       N  
ATOM   1558  CA  VAL A 202     -15.891  -0.967 -17.709  1.00 74.16           C  
ANISOU 1558  CA  VAL A 202     9212  10633   8333  -1421  -3965  -3046       C  
ATOM   1559  C   VAL A 202     -14.381  -1.065 -17.860  1.00 72.70           C  
ANISOU 1559  C   VAL A 202     9260  10421   7941  -1351  -3798  -3076       C  
ATOM   1560  O   VAL A 202     -13.733  -1.863 -17.178  1.00 77.71           O  
ANISOU 1560  O   VAL A 202     9928  10907   8693  -1390  -3637  -3152       O  
ATOM   1561  CB  VAL A 202     -16.276  -0.017 -16.554  1.00 72.23           C  
ANISOU 1561  CB  VAL A 202     8764  10381   8299  -1369  -3933  -2892       C  
ATOM   1562  CG1 VAL A 202     -15.825   1.402 -16.858  1.00 71.31           C  
ANISOU 1562  CG1 VAL A 202     8728  10388   7980  -1211  -3967  -2731       C  
ATOM   1563  CG2 VAL A 202     -17.777  -0.050 -16.319  1.00 74.43           C  
ANISOU 1563  CG2 VAL A 202     8784  10681   8815  -1447  -4065  -2885       C  
ATOM   1564  N   SER A 203     -13.823  -0.278 -18.775  1.00 85.22           N  
ANISOU 1564  N   SER A 203    11010  12150   9218  -1253  -3833  -3016       N  
ATOM   1565  CA  SER A 203     -12.396  -0.332 -19.065  1.00 81.15           C  
ANISOU 1565  CA  SER A 203    10715  11643   8476  -1190  -3668  -3051       C  
ATOM   1566  C   SER A 203     -11.880   1.085 -19.233  1.00 77.22           C  
ANISOU 1566  C   SER A 203    10295  11270   7777  -1069  -3642  -2854       C  
ATOM   1567  O   SER A 203     -12.338   1.810 -20.122  1.00 91.63           O  
ANISOU 1567  O   SER A 203    12165  13237   9412  -1036  -3816  -2785       O  
ATOM   1568  CB  SER A 203     -12.119  -1.161 -20.324  1.00 90.35           C  
ANISOU 1568  CB  SER A 203    12059  12854   9416  -1238  -3694  -3210       C  
ATOM   1569  OG  SER A 203     -10.737  -1.168 -20.635  1.00103.04           O  
ANISOU 1569  OG  SER A 203    13863  14487  10802  -1173  -3518  -3247       O  
ATOM   1570  N   VAL A 204     -10.937   1.479 -18.382  1.00 70.56           N  
ANISOU 1570  N   VAL A 204     9469  10355   6986  -1012  -3392  -2721       N  
ATOM   1571  CA  VAL A 204     -10.306   2.792 -18.459  1.00 67.35           C  
ANISOU 1571  CA  VAL A 204     9145  10036   6408   -911  -3309  -2510       C  
ATOM   1572  C   VAL A 204      -8.819   2.568 -18.682  1.00 72.34           C  
ANISOU 1572  C   VAL A 204     9962  10674   6849   -882  -3084  -2551       C  
ATOM   1573  O   VAL A 204      -8.170   1.862 -17.899  1.00 67.50           O  
ANISOU 1573  O   VAL A 204     9328   9930   6391   -894  -2897  -2612       O  
ATOM   1574  CB  VAL A 204     -10.552   3.627 -17.192  1.00 65.06           C  
ANISOU 1574  CB  VAL A 204     8689   9668   6363   -865  -3217  -2306       C  
ATOM   1575  CG1 VAL A 204     -10.022   5.041 -17.383  1.00 64.33           C  
ANISOU 1575  CG1 VAL A 204     8688   9661   6093   -767  -3174  -2090       C  
ATOM   1576  CG2 VAL A 204     -12.030   3.641 -16.840  1.00 65.92           C  
ANISOU 1576  CG2 VAL A 204     8576   9760   6710   -904  -3410  -2308       C  
ATOM   1577  N   VAL A 205      -8.277   3.158 -19.746  1.00 81.16           N  
ANISOU 1577  N   VAL A 205    11260  11945   7633   -845  -3105  -2518       N  
ATOM   1578  CA  VAL A 205      -6.870   2.969 -20.084  1.00 80.20           C  
ANISOU 1578  CA  VAL A 205    11305  11861   7307   -823  -2889  -2574       C  
ATOM   1579  C   VAL A 205      -6.250   4.301 -20.485  1.00 75.07           C  
ANISOU 1579  C   VAL A 205    10774  11337   6413   -768  -2826  -2366       C  
ATOM   1580  O   VAL A 205      -6.875   5.097 -21.198  1.00 81.44           O  
ANISOU 1580  O   VAL A 205    11632  12256   7056   -759  -3015  -2260       O  
ATOM   1581  CB  VAL A 205      -6.683   1.922 -21.204  1.00 82.72           C  
ANISOU 1581  CB  VAL A 205    11761  12251   7419   -871  -2951  -2838       C  
ATOM   1582  CG1 VAL A 205      -6.808   0.514 -20.641  1.00 82.17           C  
ANISOU 1582  CG1 VAL A 205    11606  12012   7604   -920  -2922  -3049       C  
ATOM   1583  CG2 VAL A 205      -7.696   2.146 -22.319  1.00 94.78           C  
ANISOU 1583  CG2 VAL A 205    13338  13916   8756   -903  -3238  -2864       C  
ATOM   1584  N   SER A 206      -5.033   4.539 -20.029  1.00 77.32           N  
ANISOU 1584  N   SER A 206    11103  11597   6679   -733  -2572  -2306       N  
ATOM   1585  CA  SER A 206      -4.241   5.681 -20.475  1.00 85.08           C  
ANISOU 1585  CA  SER A 206    12219  12699   7409   -703  -2475  -2133       C  
ATOM   1586  C   SER A 206      -2.896   5.135 -20.948  1.00106.02           C  
ANISOU 1586  C   SER A 206    14999  15416   9866   -711  -2258  -2279       C  
ATOM   1587  O   SER A 206      -2.739   3.941 -21.229  1.00115.61           O  
ANISOU 1587  O   SER A 206    16231  16613  11084   -734  -2242  -2523       O  
ATOM   1588  CB  SER A 206      -4.091   6.729 -19.366  1.00 76.32           C  
ANISOU 1588  CB  SER A 206    11010  11500   6487   -652  -2374  -1892       C  
ATOM   1589  OG  SER A 206      -3.084   6.351 -18.447  1.00 76.52           O  
ANISOU 1589  OG  SER A 206    10984  11425   6664   -634  -2124  -1924       O  
ATOM   1590  N   SER A 207      -1.896   6.015 -21.039  1.00129.59           N  
ANISOU 1590  N   SER A 207    18071  18477  12688   -694  -2085  -2138       N  
ATOM   1591  CA  SER A 207      -0.566   5.561 -21.427  1.00142.04           C  
ANISOU 1591  CA  SER A 207    19742  20128  14097   -700  -1856  -2276       C  
ATOM   1592  C   SER A 207       0.088   4.741 -20.323  1.00150.17           C  
ANISOU 1592  C   SER A 207    20645  20998  15416   -662  -1675  -2385       C  
ATOM   1593  O   SER A 207       0.831   3.795 -20.611  1.00151.86           O  
ANISOU 1593  O   SER A 207    20894  21224  15580   -656  -1558  -2606       O  
ATOM   1594  CB  SER A 207       0.314   6.755 -21.798  1.00141.52           C  
ANISOU 1594  CB  SER A 207    19790  20190  13789   -709  -1715  -2087       C  
ATOM   1595  OG  SER A 207       0.440   7.658 -20.714  1.00138.73           O  
ANISOU 1595  OG  SER A 207    19338  19728  13646   -674  -1642  -1863       O  
ATOM   1596  N   HIS A 208      -0.178   5.080 -19.060  1.00151.38           N  
ANISOU 1596  N   HIS A 208    20653  20997  15866   -631  -1656  -2239       N  
ATOM   1597  CA  HIS A 208       0.387   4.356 -17.932  1.00151.53           C  
ANISOU 1597  CA  HIS A 208    20560  20855  16162   -595  -1504  -2313       C  
ATOM   1598  C   HIS A 208      -0.643   3.942 -16.889  1.00138.96           C  
ANISOU 1598  C   HIS A 208    18817  19085  14899   -599  -1618  -2290       C  
ATOM   1599  O   HIS A 208      -0.282   3.223 -15.949  1.00142.32           O  
ANISOU 1599  O   HIS A 208    19162  19361  15553   -580  -1518  -2355       O  
ATOM   1600  CB  HIS A 208       1.488   5.189 -17.258  1.00157.30           C  
ANISOU 1600  CB  HIS A 208    21269  21580  16917   -558  -1288  -2158       C  
ATOM   1601  CG  HIS A 208       2.639   5.508 -18.162  1.00163.87           C  
ANISOU 1601  CG  HIS A 208    22227  22582  17454   -567  -1132  -2194       C  
ATOM   1602  ND1 HIS A 208       3.496   4.542 -18.645  1.00166.09           N  
ANISOU 1602  ND1 HIS A 208    22550  22909  17646   -556  -1010  -2434       N  
ATOM   1603  CD2 HIS A 208       3.074   6.685 -18.673  1.00165.91           C  
ANISOU 1603  CD2 HIS A 208    22576  22977  17486   -592  -1072  -2024       C  
ATOM   1604  CE1 HIS A 208       4.408   5.110 -19.414  1.00167.75           C  
ANISOU 1604  CE1 HIS A 208    22861  23294  17584   -577   -869  -2416       C  
ATOM   1605  NE2 HIS A 208       4.175   6.410 -19.447  1.00167.72           N  
ANISOU 1605  NE2 HIS A 208    22894  23344  17487   -608   -903  -2161       N  
ATOM   1606  N   TYR A 209      -1.898   4.365 -17.016  1.00110.22           N  
ANISOU 1606  N   TYR A 209    15134  15457  11289   -626  -1824  -2200       N  
ATOM   1607  CA  TYR A 209      -2.988   3.866 -16.190  1.00 78.58           C  
ANISOU 1607  CA  TYR A 209    10976  11308   7572   -650  -1942  -2212       C  
ATOM   1608  C   TYR A 209      -3.821   2.882 -16.998  1.00 75.75           C  
ANISOU 1608  C   TYR A 209    10639  10968   7174   -708  -2131  -2413       C  
ATOM   1609  O   TYR A 209      -4.113   3.119 -18.174  1.00 86.42           O  
ANISOU 1609  O   TYR A 209    12093  12466   8276   -725  -2264  -2449       O  
ATOM   1610  CB  TYR A 209      -3.874   5.009 -15.686  1.00 79.81           C  
ANISOU 1610  CB  TYR A 209    11033  11462   7829   -635  -2042  -1991       C  
ATOM   1611  CG  TYR A 209      -5.029   4.564 -14.810  1.00 74.38           C  
ANISOU 1611  CG  TYR A 209    10170  10650   7440   -668  -2146  -2002       C  
ATOM   1612  CD1 TYR A 209      -6.263   4.234 -15.361  1.00 74.41           C  
ANISOU 1612  CD1 TYR A 209    10124  10688   7461   -717  -2375  -2080       C  
ATOM   1613  CD2 TYR A 209      -4.888   4.484 -13.432  1.00 73.41           C  
ANISOU 1613  CD2 TYR A 209     9930  10386   7576   -660  -2014  -1934       C  
ATOM   1614  CE1 TYR A 209      -7.319   3.830 -14.563  1.00 70.61           C  
ANISOU 1614  CE1 TYR A 209     9467  10105   7257   -763  -2455  -2095       C  
ATOM   1615  CE2 TYR A 209      -5.938   4.083 -12.626  1.00 69.90           C  
ANISOU 1615  CE2 TYR A 209     9327   9841   7391   -707  -2089  -1941       C  
ATOM   1616  CZ  TYR A 209      -7.151   3.757 -13.197  1.00 73.71           C  
ANISOU 1616  CZ  TYR A 209     9749  10363   7895   -762  -2303  -2023       C  
ATOM   1617  OH  TYR A 209      -8.198   3.357 -12.399  1.00 66.63           O  
ANISOU 1617  OH  TYR A 209     8679   9378   7260   -823  -2365  -2036       O  
ATOM   1618  N   SER A 210      -4.210   1.782 -16.360  1.00 64.24           N  
ANISOU 1618  N   SER A 210     9090   9357   5960   -747  -2148  -2541       N  
ATOM   1619  CA  SER A 210      -4.968   0.733 -17.037  1.00 67.83           C  
ANISOU 1619  CA  SER A 210     9558   9802   6413   -815  -2322  -2751       C  
ATOM   1620  C   SER A 210      -5.706  -0.081 -15.989  1.00 72.17           C  
ANISOU 1620  C   SER A 210     9959  10162   7300   -875  -2356  -2788       C  
ATOM   1621  O   SER A 210      -5.068  -0.735 -15.157  1.00 74.51           O  
ANISOU 1621  O   SER A 210    10240  10310   7761   -867  -2208  -2825       O  
ATOM   1622  CB  SER A 210      -4.042  -0.161 -17.862  1.00 71.54           C  
ANISOU 1622  CB  SER A 210    10175  10302   6705   -807  -2248  -2980       C  
ATOM   1623  OG  SER A 210      -4.746  -1.263 -18.409  1.00 84.46           O  
ANISOU 1623  OG  SER A 210    11823  11899   8370   -875  -2412  -3201       O  
ATOM   1624  N   ARG A 211      -7.036  -0.048 -16.024  1.00 78.67           N  
ANISOU 1624  N   ARG A 211    10672  10992   8226   -937  -2552  -2775       N  
ATOM   1625  CA  ARG A 211      -7.817  -0.845 -15.092  1.00 74.78           C  
ANISOU 1625  CA  ARG A 211    10034  10335   8045  -1020  -2585  -2815       C  
ATOM   1626  C   ARG A 211      -9.148  -1.227 -15.726  1.00 80.16           C  
ANISOU 1626  C   ARG A 211    10644  11058   8756  -1109  -2835  -2924       C  
ATOM   1627  O   ARG A 211      -9.698  -0.496 -16.559  1.00 71.78           O  
ANISOU 1627  O   ARG A 211     9590  10154   7529  -1089  -2996  -2885       O  
ATOM   1628  CB  ARG A 211      -8.046  -0.110 -13.766  1.00 72.10           C  
ANISOU 1628  CB  ARG A 211     9547   9930   7917  -1003  -2486  -2601       C  
ATOM   1629  CG  ARG A 211      -8.550  -1.017 -12.654  1.00 75.33           C  
ANISOU 1629  CG  ARG A 211     9834  10155   8632  -1096  -2452  -2634       C  
ATOM   1630  CD  ARG A 211      -8.518  -0.337 -11.301  1.00 88.88           C  
ANISOU 1630  CD  ARG A 211    11437  11811  10522  -1071  -2310  -2435       C  
ATOM   1631  NE  ARG A 211      -9.182  -1.146 -10.282  1.00 89.77           N  
ANISOU 1631  NE  ARG A 211    11429  11771  10910  -1182  -2293  -2453       N  
ATOM   1632  CZ  ARG A 211      -9.315  -0.784  -9.011  1.00 93.87           C  
ANISOU 1632  CZ  ARG A 211    11840  12224  11604  -1192  -2175  -2307       C  
ATOM   1633  NH1 ARG A 211      -8.829   0.379  -8.598  1.00 80.56           N  
ANISOU 1633  NH1 ARG A 211    10146  10603   9859  -1090  -2071  -2141       N  
ATOM   1634  NH2 ARG A 211      -9.935  -1.583  -8.153  1.00101.27           N  
ANISOU 1634  NH2 ARG A 211    12681  13029  12768  -1312  -2159  -2328       N  
ATOM   1635  N   LYS A 212      -9.653  -2.388 -15.309  1.00 86.26           N  
ANISOU 1635  N   LYS A 212    11348  11681   9746  -1212  -2874  -3059       N  
ATOM   1636  CA  LYS A 212     -10.890  -2.971 -15.807  1.00 85.10           C  
ANISOU 1636  CA  LYS A 212    11118  11543   9672  -1321  -3102  -3193       C  
ATOM   1637  C   LYS A 212     -11.769  -3.340 -14.621  1.00 84.59           C  
ANISOU 1637  C   LYS A 212    10855  11339   9944  -1426  -3093  -3142       C  
ATOM   1638  O   LYS A 212     -11.339  -4.083 -13.733  1.00 87.24           O  
ANISOU 1638  O   LYS A 212    11197  11497  10452  -1468  -2947  -3154       O  
ATOM   1639  CB  LYS A 212     -10.596  -4.207 -16.663  1.00 88.32           C  
ANISOU 1639  CB  LYS A 212    11667  11902   9990  -1371  -3161  -3451       C  
ATOM   1640  CG  LYS A 212     -11.814  -4.866 -17.280  1.00 94.28           C  
ANISOU 1640  CG  LYS A 212    12359  12657  10807  -1492  -3338  -3532       C  
ATOM   1641  CD  LYS A 212     -11.424  -6.172 -17.955  1.00 92.62           C  
ANISOU 1641  CD  LYS A 212    12297  12349  10544  -1540  -3314  -3725       C  
ATOM   1642  CE  LYS A 212     -12.591  -6.787 -18.704  1.00 98.12           C  
ANISOU 1642  CE  LYS A 212    12949  13068  11266  -1660  -3499  -3815       C  
ATOM   1643  NZ  LYS A 212     -12.998  -5.957 -19.870  1.00113.26           N  
ANISOU 1643  NZ  LYS A 212    14901  15212  12920  -1620  -3651  -3782       N  
ATOM   1644  N   PHE A 213     -12.993  -2.820 -14.607  1.00 72.18           N  
ANISOU 1644  N   PHE A 213     9109   9852   8463  -1468  -3248  -3084       N  
ATOM   1645  CA  PHE A 213     -13.936  -3.016 -13.516  1.00 72.29           C  
ANISOU 1645  CA  PHE A 213     8908   9775   8785  -1573  -3234  -3028       C  
ATOM   1646  C   PHE A 213     -15.074  -3.930 -13.954  1.00 74.79           C  
ANISOU 1646  C   PHE A 213     9126  10068   9221  -1724  -3430  -3199       C  
ATOM   1647  O   PHE A 213     -15.625  -3.776 -15.053  1.00 72.00           O  
ANISOU 1647  O   PHE A 213     8790   9845   8722  -1715  -3594  -3237       O  
ATOM   1648  CB  PHE A 213     -14.506  -1.678 -13.035  1.00 66.23           C  
ANISOU 1648  CB  PHE A 213     7977   9121   8068  -1503  -3239  -2829       C  
ATOM   1649  CG  PHE A 213     -13.460  -0.630 -12.768  1.00 66.42           C  
ANISOU 1649  CG  PHE A 213     8101   9185   7949  -1353  -3074  -2653       C  
ATOM   1650  CD1 PHE A 213     -12.853  -0.535 -11.528  1.00 66.35           C  
ANISOU 1650  CD1 PHE A 213     8076   9065   8070  -1338  -2845  -2533       C  
ATOM   1651  CD2 PHE A 213     -13.090   0.265 -13.758  1.00 64.24           C  
ANISOU 1651  CD2 PHE A 213     7943   9059   7405  -1238  -3152  -2605       C  
ATOM   1652  CE1 PHE A 213     -11.894   0.428 -11.285  1.00 72.81           C  
ANISOU 1652  CE1 PHE A 213     8979   9920   8765  -1209  -2701  -2380       C  
ATOM   1653  CE2 PHE A 213     -12.132   1.230 -13.518  1.00 63.86           C  
ANISOU 1653  CE2 PHE A 213     7987   9044   7234  -1119  -2999  -2442       C  
ATOM   1654  CZ  PHE A 213     -11.534   1.311 -12.281  1.00 73.04           C  
ANISOU 1654  CZ  PHE A 213     9118  10093   8541  -1103  -2775  -2336       C  
ATOM   1655  N   THR A 214     -15.421  -4.874 -13.079  1.00 81.07           N  
ANISOU 1655  N   THR A 214     9839  10693  10270  -1864  -3354  -3230       N  
ATOM   1656  CA  THR A 214     -16.519  -5.806 -13.258  1.00 87.28           C  
ANISOU 1656  CA  THR A 214    10532  11429  11204  -2027  -3446  -3310       C  
ATOM   1657  C   THR A 214     -17.557  -5.579 -12.167  1.00 88.07           C  
ANISOU 1657  C   THR A 214    10370  11515  11576  -2130  -3418  -3212       C  
ATOM   1658  O   THR A 214     -17.195  -5.503 -10.984  1.00 94.55           O  
ANISOU 1658  O   THR A 214    11146  12236  12542  -2148  -3259  -3131       O  
ATOM   1659  CB  THR A 214     -16.022  -7.264 -13.203  1.00 92.70           C  
ANISOU 1659  CB  THR A 214    11369  11905  11948  -2124  -3370  -3434       C  
ATOM   1660  OG1 THR A 214     -14.951  -7.447 -14.137  1.00 99.45           O  
ANISOU 1660  OG1 THR A 214    12457  12775  12553  -2013  -3362  -3531       O  
ATOM   1661  CG2 THR A 214     -17.150  -8.233 -13.532  1.00 93.61           C  
ANISOU 1661  CG2 THR A 214    11406  11975  12187  -2297  -3483  -3526       C  
ATOM   1662  N   PRO A 215     -18.841  -5.460 -12.509  1.00 77.90           N  
ANISOU 1662  N   PRO A 215     8904  10333  10362  -2200  -3560  -3218       N  
ATOM   1663  CA  PRO A 215     -19.863  -5.236 -11.476  1.00 77.51           C  
ANISOU 1663  CA  PRO A 215     8589  10290  10572  -2298  -3515  -3134       C  
ATOM   1664  C   PRO A 215     -20.037  -6.466 -10.596  1.00 79.91           C  
ANISOU 1664  C   PRO A 215     8876  10396  11091  -2495  -3390  -3162       C  
ATOM   1665  O   PRO A 215     -20.109  -7.594 -11.087  1.00 90.63           O  
ANISOU 1665  O   PRO A 215    10341  11650  12445  -2602  -3437  -3275       O  
ATOM   1666  CB  PRO A 215     -21.131  -4.936 -12.288  1.00 85.85           C  
ANISOU 1666  CB  PRO A 215     9485  11508  11626  -2316  -3718  -3163       C  
ATOM   1667  CG  PRO A 215     -20.636  -4.540 -13.645  1.00 91.61           C  
ANISOU 1667  CG  PRO A 215    10397  12349  12061  -2176  -3863  -3209       C  
ATOM   1668  CD  PRO A 215     -19.400  -5.352 -13.866  1.00 92.10           C  
ANISOU 1668  CD  PRO A 215    10726  12275  11993  -2172  -3767  -3292       C  
ATOM   1669  N   GLU A 216     -20.118  -6.235  -9.288  1.00 84.23           N  
ANISOU 1669  N   GLU A 216     9295  10889  11821  -2547  -3230  -3054       N  
ATOM   1670  CA  GLU A 216     -20.335  -7.287  -8.301  1.00 87.87           C  
ANISOU 1670  CA  GLU A 216     9734  11167  12487  -2745  -3095  -3041       C  
ATOM   1671  C   GLU A 216     -21.743  -7.124  -7.742  1.00 96.43           C  
ANISOU 1671  C   GLU A 216    10530  12340  13770  -2878  -3094  -2992       C  
ATOM   1672  O   GLU A 216     -22.039  -6.129  -7.072  1.00100.04           O  
ANISOU 1672  O   GLU A 216    10807  12908  14296  -2820  -3025  -2893       O  
ATOM   1673  CB  GLU A 216     -19.292  -7.217  -7.188  1.00 90.88           C  
ANISOU 1673  CB  GLU A 216    10209  11413  12908  -2716  -2894  -2949       C  
ATOM   1674  CG  GLU A 216     -17.878  -6.985  -7.676  1.00 96.26           C  
ANISOU 1674  CG  GLU A 216    11128  12062  13385  -2536  -2886  -2980       C  
ATOM   1675  CD  GLU A 216     -16.898  -6.774  -6.540  1.00106.65           C  
ANISOU 1675  CD  GLU A 216    12541  13274  14708  -2473  -2649  -2819       C  
ATOM   1676  OE1 GLU A 216     -17.135  -7.316  -5.440  1.00110.03           O  
ANISOU 1676  OE1 GLU A 216    12919  13571  15316  -2619  -2523  -2752       O  
ATOM   1677  OE2 GLU A 216     -15.894  -6.059  -6.744  1.00111.79           O  
ANISOU 1677  OE2 GLU A 216    13323  13979  15175  -2282  -2586  -2748       O  
ATOM   1678  N   ILE A 217     -22.603  -8.099  -8.013  1.00 99.91           N  
ANISOU 1678  N   ILE A 217    10923  12733  14304  -3056  -3165  -3066       N  
ATOM   1679  CA  ILE A 217     -23.999  -8.057  -7.597  1.00101.28           C  
ANISOU 1679  CA  ILE A 217    10820  12999  14663  -3196  -3174  -3039       C  
ATOM   1680  C   ILE A 217     -24.146  -8.880  -6.325  1.00111.47           C  
ANISOU 1680  C   ILE A 217    12086  14125  16141  -3406  -2983  -2968       C  
ATOM   1681  O   ILE A 217     -23.842 -10.080  -6.312  1.00114.13           O  
ANISOU 1681  O   ILE A 217    12597  14270  16500  -3540  -2964  -3012       O  
ATOM   1682  CB  ILE A 217     -24.932  -8.574  -8.704  1.00102.71           C  
ANISOU 1682  CB  ILE A 217    10950  13247  14829  -3272  -3382  -3163       C  
ATOM   1683  CG1 ILE A 217     -25.059  -7.546  -9.832  1.00104.45           C  
ANISOU 1683  CG1 ILE A 217    11137  13669  14879  -3071  -3573  -3197       C  
ATOM   1684  CG2 ILE A 217     -26.300  -8.908  -8.135  1.00107.01           C  
ANISOU 1684  CG2 ILE A 217    11235  13829  15594  -3471  -3362  -3145       C  
ATOM   1685  CD1 ILE A 217     -23.951  -7.610 -10.866  1.00109.15           C  
ANISOU 1685  CD1 ILE A 217    12015  14236  15221  -2931  -3656  -3268       C  
ATOM   1686  N   ALA A 218     -24.611  -8.237  -5.256  1.00113.23           N  
ANISOU 1686  N   ALA A 218    12104  14423  16494  -3434  -2840  -2855       N  
ATOM   1687  CA  ALA A 218     -24.806  -8.909  -3.979  1.00119.08           C  
ANISOU 1687  CA  ALA A 218    12815  15034  17397  -3638  -2645  -2764       C  
ATOM   1688  C   ALA A 218     -25.748  -8.077  -3.123  1.00121.93           C  
ANISOU 1688  C   ALA A 218    12875  15562  17892  -3663  -2536  -2677       C  
ATOM   1689  O   ALA A 218     -25.964  -6.889  -3.378  1.00114.66           O  
ANISOU 1689  O   ALA A 218    11804  14828  16933  -3486  -2588  -2674       O  
ATOM   1690  CB  ALA A 218     -23.477  -9.139  -3.252  1.00110.41           C  
ANISOU 1690  CB  ALA A 218    11951  13750  16249  -3606  -2487  -2690       C  
ATOM   1691  N   LYS A 219     -26.306  -8.720  -2.100  1.00139.36           N  
ANISOU 1691  N   LYS A 219    15003  17697  20251  -3882  -2385  -2605       N  
ATOM   1692  CA  LYS A 219     -27.207  -8.050  -1.171  1.00141.55           C  
ANISOU 1692  CA  LYS A 219    14998  18126  20658  -3925  -2246  -2526       C  
ATOM   1693  C   LYS A 219     -26.386  -7.292  -0.135  1.00134.15           C  
ANISOU 1693  C   LYS A 219    14101  17185  19684  -3825  -2039  -2409       C  
ATOM   1694  O   LYS A 219     -25.620  -7.897   0.623  1.00138.65           O  
ANISOU 1694  O   LYS A 219    14861  17576  20243  -3914  -1896  -2329       O  
ATOM   1695  CB  LYS A 219     -28.131  -9.062  -0.499  1.00148.15           C  
ANISOU 1695  CB  LYS A 219    15741  18893  21654  -4210  -2160  -2489       C  
ATOM   1696  CG  LYS A 219     -28.946  -9.900  -1.471  1.00151.81           C  
ANISOU 1696  CG  LYS A 219    16170  19346  22164  -4336  -2360  -2607       C  
ATOM   1697  CD  LYS A 219     -29.846 -10.879  -0.736  1.00153.29           C  
ANISOU 1697  CD  LYS A 219    16263  19460  22519  -4629  -2268  -2558       C  
ATOM   1698  CE  LYS A 219     -30.661 -11.714  -1.709  1.00156.17           C  
ANISOU 1698  CE  LYS A 219    16591  19814  22933  -4764  -2472  -2681       C  
ATOM   1699  NZ  LYS A 219     -31.582 -12.648  -1.005  1.00161.42           N  
ANISOU 1699  NZ  LYS A 219    17151  20412  23771  -5059  -2391  -2629       N  
ATOM   1700  N   ARG A 220     -26.546  -5.971  -0.102  1.00122.39           N  
ANISOU 1700  N   ARG A 220    12438  15887  18176  -3637  -2032  -2399       N  
ATOM   1701  CA  ARG A 220     -25.742  -5.126   0.763  1.00101.51           C  
ANISOU 1701  CA  ARG A 220     9830  13257  15483  -3517  -1856  -2305       C  
ATOM   1702  C   ARG A 220     -26.627  -4.337   1.722  1.00 95.10           C  
ANISOU 1702  C   ARG A 220     8737  12613  14782  -3526  -1697  -2246       C  
ATOM   1703  O   ARG A 220     -27.798  -4.083   1.424  1.00 99.18           O  
ANISOU 1703  O   ARG A 220     9011  13278  15395  -3535  -1776  -2301       O  
ATOM   1704  CB  ARG A 220     -24.887  -4.159  -0.065  1.00 93.71           C  
ANISOU 1704  CB  ARG A 220     8932  12327  14345  -3251  -1988  -2343       C  
ATOM   1705  CG  ARG A 220     -23.867  -4.856  -0.948  1.00 96.38           C  
ANISOU 1705  CG  ARG A 220     9563  12507  14549  -3217  -2116  -2404       C  
ATOM   1706  CD  ARG A 220     -23.029  -3.859  -1.724  1.00110.02           C  
ANISOU 1706  CD  ARG A 220    11380  14308  16116  -2960  -2233  -2430       C  
ATOM   1707  NE  ARG A 220     -22.004  -4.516  -2.530  1.00116.88           N  
ANISOU 1707  NE  ARG A 220    12532  15035  16842  -2920  -2332  -2494       N  
ATOM   1708  CZ  ARG A 220     -22.208  -4.987  -3.755  1.00105.33           C  
ANISOU 1708  CZ  ARG A 220    11143  13578  15301  -2909  -2534  -2601       C  
ATOM   1709  NH1 ARG A 220     -23.404  -4.876  -4.318  1.00 88.82           N  
ANISOU 1709  NH1 ARG A 220     8862  11621  13264  -2941  -2670  -2651       N  
ATOM   1710  NH2 ARG A 220     -21.218  -5.570  -4.418  1.00102.71           N  
ANISOU 1710  NH2 ARG A 220    11073  13120  14831  -2863  -2597  -2664       N  
ATOM   1711  N   PRO A 221     -26.101  -3.951   2.885  1.00 88.40           N  
ANISOU 1711  N   PRO A 221     7919  11748  13921  -3522  -1469  -2141       N  
ATOM   1712  CA  PRO A 221     -26.907  -3.178   3.836  1.00 89.24           C  
ANISOU 1712  CA  PRO A 221     7769  12019  14118  -3519  -1300  -2096       C  
ATOM   1713  C   PRO A 221     -27.323  -1.832   3.261  1.00 98.33           C  
ANISOU 1713  C   PRO A 221     8719  13369  15274  -3276  -1422  -2159       C  
ATOM   1714  O   PRO A 221     -26.640  -1.249   2.416  1.00100.77           O  
ANISOU 1714  O   PRO A 221     9128  13681  15479  -3081  -1580  -2193       O  
ATOM   1715  CB  PRO A 221     -25.971  -3.004   5.038  1.00 88.13           C  
ANISOU 1715  CB  PRO A 221     7771  11802  13911  -3530  -1058  -1976       C  
ATOM   1716  CG  PRO A 221     -24.994  -4.124   4.922  1.00 88.65           C  
ANISOU 1716  CG  PRO A 221     8146  11632  13907  -3639  -1075  -1943       C  
ATOM   1717  CD  PRO A 221     -24.794  -4.327   3.451  1.00 91.74           C  
ANISOU 1717  CD  PRO A 221     8617  11990  14251  -3543  -1345  -2061       C  
ATOM   1718  N   LYS A 222     -28.463  -1.341   3.739  1.00108.32           N  
ANISOU 1718  N   LYS A 222     9702  14794  16659  -3285  -1349  -2171       N  
ATOM   1719  CA  LYS A 222     -28.983  -0.059   3.285  1.00108.22           C  
ANISOU 1719  CA  LYS A 222     9484  14960  16676  -3052  -1463  -2226       C  
ATOM   1720  C   LYS A 222     -28.120   1.082   3.807  1.00106.05           C  
ANISOU 1720  C   LYS A 222     9261  14712  16322  -2853  -1360  -2168       C  
ATOM   1721  O   LYS A 222     -27.836   1.163   5.006  1.00101.06           O  
ANISOU 1721  O   LYS A 222     8644  14065  15688  -2916  -1113  -2094       O  
ATOM   1722  CB  LYS A 222     -30.426   0.121   3.755  1.00111.57           C  
ANISOU 1722  CB  LYS A 222     9591  15539  17262  -3117  -1392  -2263       C  
ATOM   1723  CG  LYS A 222     -31.429  -0.816   3.107  1.00119.52           C  
ANISOU 1723  CG  LYS A 222    10496  16552  18364  -3286  -1531  -2336       C  
ATOM   1724  CD  LYS A 222     -31.989  -0.222   1.826  1.00123.88           C  
ANISOU 1724  CD  LYS A 222    10927  17211  18929  -3108  -1818  -2433       C  
ATOM   1725  CE  LYS A 222     -33.194  -1.011   1.339  1.00121.18           C  
ANISOU 1725  CE  LYS A 222    10420  16915  18709  -3275  -1933  -2513       C  
ATOM   1726  NZ  LYS A 222     -33.764  -0.448   0.084  1.00123.67           N  
ANISOU 1726  NZ  LYS A 222    10626  17336  19027  -3104  -2222  -2604       N  
ATOM   1727  N   VAL A 223     -27.700   1.962   2.903  1.00105.75           N  
ANISOU 1727  N   VAL A 223     9260  14710  16208  -2617  -1555  -2198       N  
ATOM   1728  CA  VAL A 223     -27.016   3.202   3.255  1.00101.99           C  
ANISOU 1728  CA  VAL A 223     8802  14275  15675  -2402  -1499  -2153       C  
ATOM   1729  C   VAL A 223     -27.718   4.320   2.501  1.00107.97           C  
ANISOU 1729  C   VAL A 223     9379  15169  16475  -2173  -1700  -2204       C  
ATOM   1730  O   VAL A 223     -27.637   4.387   1.268  1.00120.11           O  
ANISOU 1730  O   VAL A 223    10990  16702  17943  -2075  -1956  -2241       O  
ATOM   1731  CB  VAL A 223     -25.519   3.171   2.917  1.00 88.24           C  
ANISOU 1731  CB  VAL A 223     7368  12400  13760  -2326  -1535  -2098       C  
ATOM   1732  CG1 VAL A 223     -24.878   4.508   3.254  1.00 82.54           C  
ANISOU 1732  CG1 VAL A 223     6716  11707  12938  -2073  -1471  -1999       C  
ATOM   1733  CG2 VAL A 223     -24.823   2.044   3.664  1.00 88.28           C  
ANISOU 1733  CG2 VAL A 223     7591  12244  13709  -2528  -1342  -2022       C  
ATOM   1734  N   ARG A 224     -28.411   5.192   3.236  1.00 95.62           N  
ANISOU 1734  N   ARG A 224     7592  13722  15015  -2086  -1586  -2208       N  
ATOM   1735  CA  ARG A 224     -29.204   6.272   2.648  1.00 85.44           C  
ANISOU 1735  CA  ARG A 224     6115  12553  13795  -1867  -1764  -2256       C  
ATOM   1736  C   ARG A 224     -30.254   5.712   1.689  1.00 88.35           C  
ANISOU 1736  C   ARG A 224     6365  12973  14231  -1933  -1971  -2335       C  
ATOM   1737  O   ARG A 224     -30.421   6.187   0.563  1.00 84.38           O  
ANISOU 1737  O   ARG A 224     5869  12500  13690  -1775  -2235  -2361       O  
ATOM   1738  CB  ARG A 224     -28.308   7.302   1.954  1.00 88.75           C  
ANISOU 1738  CB  ARG A 224     6684  12943  14094  -1612  -1933  -2215       C  
ATOM   1739  CG  ARG A 224     -27.315   7.979   2.887  1.00 94.03           C  
ANISOU 1739  CG  ARG A 224     7448  13571  14710  -1530  -1742  -2143       C  
ATOM   1740  CD  ARG A 224     -26.407   8.939   2.137  1.00 81.02           C  
ANISOU 1740  CD  ARG A 224     5982  11877  12924  -1288  -1916  -2080       C  
ATOM   1741  NE  ARG A 224     -27.164   9.935   1.382  1.00 84.78           N  
ANISOU 1741  NE  ARG A 224     6310  12437  13464  -1078  -2147  -2115       N  
ATOM   1742  CZ  ARG A 224     -27.612  11.078   1.891  1.00 80.44           C  
ANISOU 1742  CZ  ARG A 224     5605  11947  13011   -904  -2104  -2115       C  
ATOM   1743  NH1 ARG A 224     -28.291  11.924   1.129  1.00 75.24           N  
ANISOU 1743  NH1 ARG A 224     4856  11338  12395   -711  -2328  -2129       N  
ATOM   1744  NH2 ARG A 224     -27.383  11.373   3.163  1.00 68.30           N  
ANISOU 1744  NH2 ARG A 224     4016  10414  11521   -923  -1839  -2101       N  
ATOM   1745  N   ASP A 225     -30.960   4.678   2.154  1.00 93.66           N  
ANISOU 1745  N   ASP A 225     6937  13653  14998  -2177  -1850  -2366       N  
ATOM   1746  CA  ASP A 225     -32.037   4.035   1.400  1.00106.06           C  
ANISOU 1746  CA  ASP A 225     8370  15274  16653  -2279  -2016  -2447       C  
ATOM   1747  C   ASP A 225     -31.536   3.509   0.054  1.00105.92           C  
ANISOU 1747  C   ASP A 225     8561  15176  16507  -2272  -2276  -2466       C  
ATOM   1748  O   ASP A 225     -32.160   3.706  -0.991  1.00111.50           O  
ANISOU 1748  O   ASP A 225     9195  15949  17223  -2185  -2522  -2525       O  
ATOM   1749  CB  ASP A 225     -33.223   4.988   1.214  1.00104.92           C  
ANISOU 1749  CB  ASP A 225     7937  15287  16643  -2116  -2116  -2512       C  
ATOM   1750  CG  ASP A 225     -34.469   4.280   0.717  1.00109.54           C  
ANISOU 1750  CG  ASP A 225     8330  15942  17349  -2257  -2232  -2600       C  
ATOM   1751  OD1 ASP A 225     -34.663   3.100   1.076  1.00112.24           O  
ANISOU 1751  OD1 ASP A 225     8684  16237  17726  -2520  -2119  -2605       O  
ATOM   1752  OD2 ASP A 225     -35.251   4.899  -0.036  1.00109.09           O  
ANISOU 1752  OD2 ASP A 225     8116  15981  17353  -2106  -2443  -2661       O  
ATOM   1753  N   GLN A 226     -30.389   2.831   0.085  1.00 96.90           N  
ANISOU 1753  N   GLN A 226     7690  13890  15237  -2361  -2219  -2420       N  
ATOM   1754  CA  GLN A 226     -29.817   2.249  -1.123  1.00 89.82           C  
ANISOU 1754  CA  GLN A 226     7017  12908  14201  -2365  -2436  -2448       C  
ATOM   1755  C   GLN A 226     -29.104   0.951  -0.775  1.00 87.99           C  
ANISOU 1755  C   GLN A 226     6997  12513  13923  -2589  -2309  -2429       C  
ATOM   1756  O   GLN A 226     -28.308   0.913   0.167  1.00 80.96           O  
ANISOU 1756  O   GLN A 226     6212  11543  13006  -2629  -2098  -2357       O  
ATOM   1757  CB  GLN A 226     -28.839   3.215  -1.807  1.00 84.06           C  
ANISOU 1757  CB  GLN A 226     6462  12170  13307  -2116  -2577  -2409       C  
ATOM   1758  CG  GLN A 226     -29.495   4.345  -2.583  1.00 89.08           C  
ANISOU 1758  CG  GLN A 226     6962  12932  13951  -1888  -2796  -2426       C  
ATOM   1759  CD  GLN A 226     -30.400   3.850  -3.696  1.00100.82           C  
ANISOU 1759  CD  GLN A 226     8384  14473  15450  -1935  -3035  -2509       C  
ATOM   1760  OE1 GLN A 226     -30.186   2.776  -4.259  1.00105.66           O  
ANISOU 1760  OE1 GLN A 226     9143  15011  15992  -2085  -3100  -2552       O  
ATOM   1761  NE2 GLN A 226     -31.424   4.635  -4.016  1.00104.15           N  
ANISOU 1761  NE2 GLN A 226     8587  15019  15965  -1805  -3169  -2537       N  
ATOM   1762  N   GLU A 227     -29.392  -0.103  -1.540  1.00 99.91           N  
ANISOU 1762  N   GLU A 227     8573  13965  15421  -2732  -2445  -2494       N  
ATOM   1763  CA  GLU A 227     -28.681  -1.369  -1.414  1.00107.52           C  
ANISOU 1763  CA  GLU A 227     9771  14749  16334  -2924  -2373  -2487       C  
ATOM   1764  C   GLU A 227     -27.550  -1.519  -2.420  1.00107.20           C  
ANISOU 1764  C   GLU A 227    10019  14612  16100  -2820  -2530  -2512       C  
ATOM   1765  O   GLU A 227     -26.610  -2.279  -2.162  1.00103.33           O  
ANISOU 1765  O   GLU A 227     9756  13958  15547  -2910  -2438  -2490       O  
ATOM   1766  CB  GLU A 227     -29.649  -2.548  -1.573  1.00119.01           C  
ANISOU 1766  CB  GLU A 227    11142  16176  17900  -3163  -2412  -2547       C  
ATOM   1767  CG  GLU A 227     -30.581  -2.752  -0.393  1.00128.02           C  
ANISOU 1767  CG  GLU A 227    12055  17368  19220  -3334  -2203  -2509       C  
ATOM   1768  CD  GLU A 227     -31.505  -3.940  -0.577  1.00133.73           C  
ANISOU 1768  CD  GLU A 227    12704  18055  20051  -3582  -2250  -2563       C  
ATOM   1769  OE1 GLU A 227     -31.335  -4.684  -1.566  1.00133.65           O  
ANISOU 1769  OE1 GLU A 227    12845  17960  19977  -3631  -2434  -2631       O  
ATOM   1770  OE2 GLU A 227     -32.405  -4.129   0.268  1.00137.79           O  
ANISOU 1770  OE2 GLU A 227    13012  18629  20713  -3731  -2102  -2541       O  
ATOM   1771  N   GLY A 228     -27.620  -0.825  -3.555  1.00 77.39           N  
ANISOU 1771  N   GLY A 228     6248  10931  12225  -2634  -2761  -2555       N  
ATOM   1772  CA  GLY A 228     -26.517  -0.825  -4.488  1.00 75.81           C  
ANISOU 1772  CA  GLY A 228     6324  10664  11817  -2518  -2894  -2571       C  
ATOM   1773  C   GLY A 228     -25.448   0.182  -4.114  1.00 78.98           C  
ANISOU 1773  C   GLY A 228     6827  11064  12120  -2333  -2813  -2489       C  
ATOM   1774  O   GLY A 228     -25.665   1.106  -3.331  1.00 72.02           O  
ANISOU 1774  O   GLY A 228     5783  10259  11322  -2249  -2704  -2426       O  
ATOM   1775  N   ARG A 229     -24.265  -0.008  -4.686  1.00 76.65           N  
ANISOU 1775  N   ARG A 229     6805  10678  11642  -2269  -2865  -2497       N  
ATOM   1776  CA  ARG A 229     -23.127   0.858  -4.425  1.00 71.73           C  
ANISOU 1776  CA  ARG A 229     6343  10035  10878  -2089  -2771  -2386       C  
ATOM   1777  C   ARG A 229     -22.651   1.498  -5.721  1.00 68.04           C  
ANISOU 1777  C   ARG A 229     6037   9627  10187  -1896  -2981  -2385       C  
ATOM   1778  O   ARG A 229     -23.069   1.127  -6.819  1.00 69.95           O  
ANISOU 1778  O   ARG A 229     6280   9914  10383  -1921  -3214  -2504       O  
ATOM   1779  CB  ARG A 229     -21.978   0.082  -3.769  1.00 66.30           C  
ANISOU 1779  CB  ARG A 229     5908   9167  10117  -2163  -2556  -2317       C  
ATOM   1780  CG  ARG A 229     -22.282  -0.440  -2.378  1.00 66.28           C  
ANISOU 1780  CG  ARG A 229     5795   9095  10294  -2343  -2325  -2276       C  
ATOM   1781  CD  ARG A 229     -22.469   0.689  -1.381  1.00 65.19           C  
ANISOU 1781  CD  ARG A 229     5503   9049  10216  -2244  -2167  -2166       C  
ATOM   1782  NE  ARG A 229     -22.713   0.176  -0.036  1.00 65.28           N  
ANISOU 1782  NE  ARG A 229     5430   9004  10368  -2425  -1932  -2123       N  
ATOM   1783  CZ  ARG A 229     -23.916  -0.127   0.438  1.00 67.47           C  
ANISOU 1783  CZ  ARG A 229     5431   9354  10853  -2600  -1901  -2193       C  
ATOM   1784  NH1 ARG A 229     -24.988   0.034  -0.325  1.00 69.73           N  
ANISOU 1784  NH1 ARG A 229     5508   9764  11223  -2593  -2091  -2295       N  
ATOM   1785  NH2 ARG A 229     -24.049  -0.591   1.673  1.00 69.76           N  
ANISOU 1785  NH2 ARG A 229     5675   9592  11239  -2773  -1670  -2138       N  
ATOM   1786  N   ILE A 230     -21.771   2.484  -5.574  1.00 65.83           N  
ANISOU 1786  N   ILE A 230     5899   9350   9762  -1710  -2895  -2247       N  
ATOM   1787  CA  ILE A 230     -21.063   3.095  -6.693  1.00 65.31           C  
ANISOU 1787  CA  ILE A 230     6043   9323   9450  -1537  -3040  -2211       C  
ATOM   1788  C   ILE A 230     -19.626   3.302  -6.239  1.00 62.48           C  
ANISOU 1788  C   ILE A 230     5936   8866   8938  -1458  -2829  -2085       C  
ATOM   1789  O   ILE A 230     -19.356   4.178  -5.411  1.00 60.88           O  
ANISOU 1789  O   ILE A 230     5700   8667   8765  -1365  -2683  -1961       O  
ATOM   1790  CB  ILE A 230     -21.683   4.427  -7.143  1.00 66.13           C  
ANISOU 1790  CB  ILE A 230     6012   9567   9549  -1362  -3212  -2165       C  
ATOM   1791  CG1 ILE A 230     -23.059   4.199  -7.769  1.00 69.21           C  
ANISOU 1791  CG1 ILE A 230     6160  10063  10074  -1425  -3463  -2305       C  
ATOM   1792  CG2 ILE A 230     -20.767   5.133  -8.134  1.00 65.32           C  
ANISOU 1792  CG2 ILE A 230     6166   9484   9167  -1193  -3312  -2085       C  
ATOM   1793  CD1 ILE A 230     -23.702   5.459  -8.302  1.00 70.39           C  
ANISOU 1793  CD1 ILE A 230     6182  10341  10223  -1241  -3674  -2267       C  
ATOM   1794  N   ASN A 231     -18.709   2.491  -6.756  1.00 67.82           N  
ANISOU 1794  N   ASN A 231     6853   9454   9461  -1495  -2814  -2127       N  
ATOM   1795  CA  ASN A 231     -17.300   2.668  -6.443  1.00 59.55           C  
ANISOU 1795  CA  ASN A 231     6038   8324   8263  -1412  -2633  -2023       C  
ATOM   1796  C   ASN A 231     -16.735   3.812  -7.272  1.00 58.96           C  
ANISOU 1796  C   ASN A 231     6090   8338   7972  -1225  -2719  -1940       C  
ATOM   1797  O   ASN A 231     -16.871   3.829  -8.499  1.00 60.41           O  
ANISOU 1797  O   ASN A 231     6346   8597   8011  -1191  -2919  -2006       O  
ATOM   1798  CB  ASN A 231     -16.522   1.379  -6.703  1.00 61.82           C  
ANISOU 1798  CB  ASN A 231     6525   8485   8480  -1508  -2588  -2113       C  
ATOM   1799  CG  ASN A 231     -16.778   0.325  -5.648  1.00 66.64           C  
ANISOU 1799  CG  ASN A 231     7065   8963   9291  -1685  -2451  -2144       C  
ATOM   1800  OD1 ASN A 231     -17.176   0.638  -4.526  1.00 65.05           O  
ANISOU 1800  OD1 ASN A 231     6715   8758   9242  -1722  -2318  -2061       O  
ATOM   1801  ND2 ASN A 231     -16.546  -0.935  -6.001  1.00 71.59           N  
ANISOU 1801  ND2 ASN A 231     7808   9477   9915  -1799  -2482  -2263       N  
ATOM   1802  N   TYR A 232     -16.110   4.772  -6.599  1.00 56.98           N  
ANISOU 1802  N   TYR A 232     5875   8079   7694  -1112  -2572  -1793       N  
ATOM   1803  CA  TYR A 232     -15.586   5.966  -7.245  1.00 56.43           C  
ANISOU 1803  CA  TYR A 232     5920   8081   7440   -945  -2635  -1689       C  
ATOM   1804  C   TYR A 232     -14.097   5.807  -7.522  1.00 54.88           C  
ANISOU 1804  C   TYR A 232     5989   7828   7033   -906  -2514  -1651       C  
ATOM   1805  O   TYR A 232     -13.353   5.269  -6.697  1.00 53.34           O  
ANISOU 1805  O   TYR A 232     5856   7529   6881   -952  -2318  -1636       O  
ATOM   1806  CB  TYR A 232     -15.837   7.202  -6.379  1.00 55.46           C  
ANISOU 1806  CB  TYR A 232     5666   7981   7425   -842  -2562  -1560       C  
ATOM   1807  CG  TYR A 232     -17.293   7.396  -6.023  1.00 57.09           C  
ANISOU 1807  CG  TYR A 232     5584   8252   7857   -869  -2660  -1610       C  
ATOM   1808  CD1 TYR A 232     -18.166   8.021  -6.903  1.00 59.07           C  
ANISOU 1808  CD1 TYR A 232     5736   8608   8101   -791  -2910  -1633       C  
ATOM   1809  CD2 TYR A 232     -17.798   6.945  -4.811  1.00 56.86           C  
ANISOU 1809  CD2 TYR A 232     5376   8183   8045   -977  -2505  -1637       C  
ATOM   1810  CE1 TYR A 232     -19.501   8.197  -6.585  1.00 60.77           C  
ANISOU 1810  CE1 TYR A 232     5660   8889   8538   -807  -3004  -1694       C  
ATOM   1811  CE2 TYR A 232     -19.132   7.118  -4.482  1.00 58.55           C  
ANISOU 1811  CE2 TYR A 232     5305   8473   8471  -1009  -2578  -1697       C  
ATOM   1812  CZ  TYR A 232     -19.980   7.743  -5.373  1.00 63.12           C  
ANISOU 1812  CZ  TYR A 232     5769   9158   9057   -919  -2829  -1732       C  
ATOM   1813  OH  TYR A 232     -21.308   7.916  -5.053  1.00 62.37           O  
ANISOU 1813  OH  TYR A 232     5365   9144   9188   -942  -2907  -1806       O  
ATOM   1814  N   TYR A 233     -13.672   6.279  -8.693  1.00 55.47           N  
ANISOU 1814  N   TYR A 233     6219   7978   6880   -823  -2634  -1635       N  
ATOM   1815  CA  TYR A 233     -12.289   6.158  -9.127  1.00 54.42           C  
ANISOU 1815  CA  TYR A 233     6326   7821   6529   -788  -2529  -1617       C  
ATOM   1816  C   TYR A 233     -11.859   7.457  -9.792  1.00 54.32           C  
ANISOU 1816  C   TYR A 233     6424   7894   6322   -660  -2585  -1486       C  
ATOM   1817  O   TYR A 233     -12.682   8.222 -10.299  1.00 55.67           O  
ANISOU 1817  O   TYR A 233     6525   8146   6482   -604  -2770  -1445       O  
ATOM   1818  CB  TYR A 233     -12.107   4.973 -10.085  1.00 55.84           C  
ANISOU 1818  CB  TYR A 233     6624   8001   6590   -868  -2610  -1785       C  
ATOM   1819  CG  TYR A 233     -12.557   3.652  -9.504  1.00 56.25           C  
ANISOU 1819  CG  TYR A 233     6584   7949   6838  -1007  -2575  -1914       C  
ATOM   1820  CD1 TYR A 233     -11.724   2.921  -8.669  1.00 54.95           C  
ANISOU 1820  CD1 TYR A 233     6486   7651   6742  -1050  -2376  -1922       C  
ATOM   1821  CD2 TYR A 233     -13.817   3.142  -9.783  1.00 58.28           C  
ANISOU 1821  CD2 TYR A 233     6690   8235   7220  -1099  -2750  -2023       C  
ATOM   1822  CE1 TYR A 233     -12.131   1.717  -8.129  1.00 60.06           C  
ANISOU 1822  CE1 TYR A 233     7069   8184   7567  -1185  -2351  -2023       C  
ATOM   1823  CE2 TYR A 233     -14.232   1.938  -9.250  1.00 58.84           C  
ANISOU 1823  CE2 TYR A 233     6683   8200   7473  -1245  -2716  -2133       C  
ATOM   1824  CZ  TYR A 233     -13.387   1.230  -8.423  1.00 60.13           C  
ANISOU 1824  CZ  TYR A 233     6932   8219   7694  -1289  -2515  -2127       C  
ATOM   1825  OH  TYR A 233     -13.797   0.029  -7.890  1.00 66.16           O  
ANISOU 1825  OH  TYR A 233     7639   8860   8638  -1443  -2488  -2221       O  
ATOM   1826  N   TRP A 234     -10.551   7.699  -9.784  1.00 52.87           N  
ANISOU 1826  N   TRP A 234     6413   7686   5988   -616  -2427  -1420       N  
ATOM   1827  CA  TRP A 234      -9.998   8.929 -10.327  1.00 52.71           C  
ANISOU 1827  CA  TRP A 234     6515   7731   5780   -515  -2446  -1280       C  
ATOM   1828  C   TRP A 234      -8.606   8.653 -10.872  1.00 52.18           C  
ANISOU 1828  C   TRP A 234     6663   7674   5488   -517  -2319  -1297       C  
ATOM   1829  O   TRP A 234      -8.001   7.617 -10.586  1.00 51.54           O  
ANISOU 1829  O   TRP A 234     6617   7530   5434   -573  -2193  -1403       O  
ATOM   1830  CB  TRP A 234      -9.944  10.032  -9.264  1.00 51.10           C  
ANISOU 1830  CB  TRP A 234     6226   7479   5710   -439  -2342  -1124       C  
ATOM   1831  CG  TRP A 234      -9.083   9.680  -8.089  1.00 48.90           C  
ANISOU 1831  CG  TRP A 234     5948   7099   5533   -463  -2097  -1110       C  
ATOM   1832  CD1 TRP A 234      -9.465   9.007  -6.966  1.00 48.13           C  
ANISOU 1832  CD1 TRP A 234     5712   6921   5655   -526  -2002  -1159       C  
ATOM   1833  CD2 TRP A 234      -7.689   9.972  -7.928  1.00 51.18           C  
ANISOU 1833  CD2 TRP A 234     6385   7360   5701   -430  -1922  -1041       C  
ATOM   1834  NE1 TRP A 234      -8.396   8.865  -6.115  1.00 46.23           N  
ANISOU 1834  NE1 TRP A 234     5535   6599   5430   -526  -1793  -1120       N  
ATOM   1835  CE2 TRP A 234      -7.294   9.448  -6.682  1.00 45.72           C  
ANISOU 1835  CE2 TRP A 234     5636   6567   5169   -464  -1743  -1053       C  
ATOM   1836  CE3 TRP A 234      -6.737  10.626  -8.715  1.00 47.43           C  
ANISOU 1836  CE3 TRP A 234     6084   6940   4997   -384  -1900   -968       C  
ATOM   1837  CZ2 TRP A 234      -5.990   9.558  -6.205  1.00 48.61           C  
ANISOU 1837  CZ2 TRP A 234     6101   6885   5483   -440  -1559  -1004       C  
ATOM   1838  CZ3 TRP A 234      -5.444  10.734  -8.240  1.00 45.82           C  
ANISOU 1838  CZ3 TRP A 234     5967   6694   4749   -372  -1700   -923       C  
ATOM   1839  CH2 TRP A 234      -5.082  10.203  -6.997  1.00 44.17           C  
ANISOU 1839  CH2 TRP A 234     5687   6383   4712   -393  -1539   -946       C  
ATOM   1840  N   THR A 235      -8.103   9.598 -11.663  1.00 52.64           N  
ANISOU 1840  N   THR A 235     6862   7811   5326   -456  -2355  -1192       N  
ATOM   1841  CA  THR A 235      -6.757   9.497 -12.206  1.00 52.32           C  
ANISOU 1841  CA  THR A 235     7015   7805   5060   -459  -2219  -1199       C  
ATOM   1842  C   THR A 235      -6.295  10.873 -12.654  1.00 52.44           C  
ANISOU 1842  C   THR A 235     7145   7880   4901   -395  -2226  -1019       C  
ATOM   1843  O   THR A 235      -7.103  11.761 -12.949  1.00 53.85           O  
ANISOU 1843  O   THR A 235     7295   8091   5075   -349  -2398   -916       O  
ATOM   1844  CB  THR A 235      -6.680   8.511 -13.377  1.00 55.60           C  
ANISOU 1844  CB  THR A 235     7541   8296   5288   -516  -2302  -1369       C  
ATOM   1845  OG1 THR A 235      -5.315   8.363 -13.785  1.00 58.43           O  
ANISOU 1845  OG1 THR A 235     8063   8690   5449   -516  -2136  -1395       O  
ATOM   1846  CG2 THR A 235      -7.497   9.015 -14.556  1.00 63.14           C  
ANISOU 1846  CG2 THR A 235     8548   9369   6072   -504  -2550  -1346       C  
ATOM   1847  N   LEU A 236      -4.976  11.034 -12.694  1.00 51.55           N  
ANISOU 1847  N   LEU A 236     7158   7775   4652   -395  -2039   -983       N  
ATOM   1848  CA  LEU A 236      -4.339  12.232 -13.219  1.00 51.87           C  
ANISOU 1848  CA  LEU A 236     7337   7874   4495   -363  -2018   -820       C  
ATOM   1849  C   LEU A 236      -3.861  11.962 -14.637  1.00 55.05           C  
ANISOU 1849  C   LEU A 236     7927   8411   4578   -407  -2055   -882       C  
ATOM   1850  O   LEU A 236      -3.219  10.939 -14.898  1.00 60.07           O  
ANISOU 1850  O   LEU A 236     8608   9074   5142   -449  -1949  -1043       O  
ATOM   1851  CB  LEU A 236      -3.162  12.667 -12.347  1.00 50.21           C  
ANISOU 1851  CB  LEU A 236     7137   7600   4339   -349  -1780   -738       C  
ATOM   1852  CG  LEU A 236      -3.492  13.266 -10.982  1.00 47.99           C  
ANISOU 1852  CG  LEU A 236     6708   7200   4324   -300  -1733   -640       C  
ATOM   1853  CD1 LEU A 236      -2.220  13.772 -10.326  1.00 46.95           C  
ANISOU 1853  CD1 LEU A 236     6619   7026   4195   -291  -1516   -558       C  
ATOM   1854  CD2 LEU A 236      -4.513  14.381 -11.122  1.00 48.90           C  
ANISOU 1854  CD2 LEU A 236     6787   7314   4479   -242  -1921   -506       C  
ATOM   1855  N   LEU A 237      -4.171  12.880 -15.545  1.00 65.80           N  
ANISOU 1855  N   LEU A 237     9402   9854   5745   -393  -2206   -758       N  
ATOM   1856  CA  LEU A 237      -3.824  12.760 -16.954  1.00 66.09           C  
ANISOU 1856  CA  LEU A 237     9633  10036   5443   -440  -2261   -795       C  
ATOM   1857  C   LEU A 237      -2.743  13.787 -17.259  1.00 66.75           C  
ANISOU 1857  C   LEU A 237     9874  10164   5325   -452  -2125   -628       C  
ATOM   1858  O   LEU A 237      -2.979  14.997 -17.148  1.00 67.68           O  
ANISOU 1858  O   LEU A 237    10019  10243   5452   -415  -2199   -426       O  
ATOM   1859  CB  LEU A 237      -5.054  12.963 -17.835  1.00 64.82           C  
ANISOU 1859  CB  LEU A 237     9498   9940   5191   -427  -2563   -779       C  
ATOM   1860  CG  LEU A 237      -4.906  12.541 -19.294  1.00 75.80           C  
ANISOU 1860  CG  LEU A 237    11077  11488   6236   -485  -2652   -870       C  
ATOM   1861  CD1 LEU A 237      -4.593  11.055 -19.385  1.00 78.43           C  
ANISOU 1861  CD1 LEU A 237    11383  11841   6576   -537  -2555  -1131       C  
ATOM   1862  CD2 LEU A 237      -6.164  12.876 -20.076  1.00 65.12           C  
ANISOU 1862  CD2 LEU A 237     9743  10191   4808   -462  -2977   -829       C  
ATOM   1863  N   GLU A 238      -1.562  13.297 -17.627  1.00 73.41           N  
ANISOU 1863  N   GLU A 238    10813  11081   5997   -506  -1925   -719       N  
ATOM   1864  CA  GLU A 238      -0.445  14.172 -17.935  1.00 77.80           C  
ANISOU 1864  CA  GLU A 238    11509  11695   6357   -541  -1766   -580       C  
ATOM   1865  C   GLU A 238      -0.756  15.000 -19.183  1.00 83.24           C  
ANISOU 1865  C   GLU A 238    12394  12496   6739   -573  -1932   -440       C  
ATOM   1866  O   GLU A 238      -1.576  14.599 -20.015  1.00 73.27           O  
ANISOU 1866  O   GLU A 238    11180  11307   5351   -579  -2136   -512       O  
ATOM   1867  CB  GLU A 238       0.823  13.351 -18.162  1.00 89.19           C  
ANISOU 1867  CB  GLU A 238    12994  13217   7678   -592  -1525   -743       C  
ATOM   1868  CG  GLU A 238       1.147  12.361 -17.053  1.00 93.83           C  
ANISOU 1868  CG  GLU A 238    13412  13695   8546   -558  -1385   -901       C  
ATOM   1869  CD  GLU A 238       2.028  12.957 -15.973  1.00 96.98           C  
ANISOU 1869  CD  GLU A 238    13738  14003   9106   -538  -1189   -793       C  
ATOM   1870  OE1 GLU A 238       2.103  14.201 -15.876  1.00 96.37           O  
ANISOU 1870  OE1 GLU A 238    13707  13911   8999   -540  -1197   -585       O  
ATOM   1871  OE2 GLU A 238       2.654  12.178 -15.224  1.00103.78           O  
ANISOU 1871  OE2 GLU A 238    14502  14804  10127   -520  -1038   -919       O  
ATOM   1872  N   PRO A 239      -0.126  16.164 -19.335  1.00 86.60           N  
ANISOU 1872  N   PRO A 239    12937  12930   7036   -601  -1860   -234       N  
ATOM   1873  CA  PRO A 239      -0.305  16.944 -20.569  1.00 81.71           C  
ANISOU 1873  CA  PRO A 239    12537  12417   6091   -647  -2005    -85       C  
ATOM   1874  C   PRO A 239       0.156  16.156 -21.785  1.00 87.81           C  
ANISOU 1874  C   PRO A 239    13458  13382   6525   -730  -1957   -238       C  
ATOM   1875  O   PRO A 239       1.317  15.753 -21.885  1.00 86.26           O  
ANISOU 1875  O   PRO A 239    13290  13264   6220   -791  -1704   -335       O  
ATOM   1876  CB  PRO A 239       0.564  18.184 -20.330  1.00 83.31           C  
ANISOU 1876  CB  PRO A 239    12828  12577   6249   -683  -1863    140       C  
ATOM   1877  CG  PRO A 239       0.662  18.298 -18.846  1.00 88.48           C  
ANISOU 1877  CG  PRO A 239    13278  13064   7276   -615  -1756    145       C  
ATOM   1878  CD  PRO A 239       0.668  16.890 -18.331  1.00 76.06           C  
ANISOU 1878  CD  PRO A 239    11542  11490   5866   -592  -1669   -112       C  
ATOM   1879  N   GLY A 240      -0.774  15.930 -22.712  1.00 95.09           N  
ANISOU 1879  N   GLY A 240    14466  14383   7281   -729  -2207   -273       N  
ATOM   1880  CA  GLY A 240      -0.490  15.239 -23.950  1.00 84.17           C  
ANISOU 1880  CA  GLY A 240    13242  13190   5550   -806  -2200   -420       C  
ATOM   1881  C   GLY A 240      -0.982  13.809 -24.015  1.00 83.76           C  
ANISOU 1881  C   GLY A 240    13082  13160   5582   -785  -2261   -709       C  
ATOM   1882  O   GLY A 240      -0.979  13.220 -25.103  1.00 82.12           O  
ANISOU 1882  O   GLY A 240    12998  13101   5105   -829  -2306   -846       O  
ATOM   1883  N   ASP A 241      -1.402  13.235 -22.894  1.00 87.01           N  
ANISOU 1883  N   ASP A 241    13269  13422   6369   -717  -2256   -806       N  
ATOM   1884  CA  ASP A 241      -1.860  11.856 -22.869  1.00 85.23           C  
ANISOU 1884  CA  ASP A 241    12939  13190   6255   -709  -2308  -1074       C  
ATOM   1885  C   ASP A 241      -3.344  11.779 -23.214  1.00 78.06           C  
ANISOU 1885  C   ASP A 241    11994  12273   5393   -679  -2643  -1082       C  
ATOM   1886  O   ASP A 241      -4.097  12.743 -23.059  1.00 76.62           O  
ANISOU 1886  O   ASP A 241    11791  12037   5283   -633  -2822   -886       O  
ATOM   1887  CB  ASP A 241      -1.597  11.229 -21.498  1.00 93.41           C  
ANISOU 1887  CB  ASP A 241    13762  14067   7663   -666  -2143  -1168       C  
ATOM   1888  CG  ASP A 241      -1.801   9.728 -21.495  1.00 98.99           C  
ANISOU 1888  CG  ASP A 241    14389  14756   8465   -674  -2149  -1453       C  
ATOM   1889  OD1 ASP A 241      -1.836   9.129 -22.591  1.00 97.56           O  
ANISOU 1889  OD1 ASP A 241    14331  14705   8033   -718  -2218  -1607       O  
ATOM   1890  OD2 ASP A 241      -1.920   9.144 -20.397  1.00100.23           O  
ANISOU 1890  OD2 ASP A 241    14373  14767   8943   -642  -2087  -1523       O  
ATOM   1891  N   THR A 242      -3.756  10.610 -23.695  1.00 73.07           N  
ANISOU 1891  N   THR A 242    11347  11690   4726   -704  -2733  -1323       N  
ATOM   1892  CA  THR A 242      -5.133  10.354 -24.091  1.00 78.78           C  
ANISOU 1892  CA  THR A 242    12022  12421   5490   -690  -3051  -1377       C  
ATOM   1893  C   THR A 242      -5.709   9.257 -23.208  1.00 80.50           C  
ANISOU 1893  C   THR A 242    12016  12508   6063   -677  -3060  -1566       C  
ATOM   1894  O   THR A 242      -5.085   8.205 -23.033  1.00 82.80           O  
ANISOU 1894  O   THR A 242    12287  12778   6396   -707  -2890  -1767       O  
ATOM   1895  CB  THR A 242      -5.214   9.947 -25.565  1.00 76.75           C  
ANISOU 1895  CB  THR A 242    11932  12346   4885   -736  -3157  -1495       C  
ATOM   1896  OG1 THR A 242      -4.686  10.999 -26.381  1.00 78.68           O  
ANISOU 1896  OG1 THR A 242    12346  12701   4847   -730  -3102  -1295       O  
ATOM   1897  CG2 THR A 242      -6.655   9.670 -25.969  1.00 77.77           C  
ANISOU 1897  CG2 THR A 242    11951  12488   5110   -718  -3455  -1549       C  
ATOM   1898  N   ILE A 243      -6.893   9.505 -22.653  1.00 80.53           N  
ANISOU 1898  N   ILE A 243    11851  12423   6325   -635  -3257  -1502       N  
ATOM   1899  CA  ILE A 243      -7.580   8.543 -21.801  1.00 75.52           C  
ANISOU 1899  CA  ILE A 243    10996  11666   6031   -640  -3282  -1658       C  
ATOM   1900  C   ILE A 243      -8.751   7.959 -22.579  1.00 79.34           C  
ANISOU 1900  C   ILE A 243    11456  12214   6477   -671  -3578  -1800       C  
ATOM   1901  O   ILE A 243      -9.472   8.681 -23.278  1.00 74.09           O  
ANISOU 1901  O   ILE A 243    10843  11631   5676   -646  -3823  -1695       O  
ATOM   1902  CB  ILE A 243      -8.045   9.180 -20.475  1.00 74.14           C  
ANISOU 1902  CB  ILE A 243    10617  11348   6206   -580  -3254  -1505       C  
ATOM   1903  CG1 ILE A 243      -8.733   8.138 -19.591  1.00 68.53           C  
ANISOU 1903  CG1 ILE A 243     9687  10521   5831   -609  -3260  -1664       C  
ATOM   1904  CG2 ILE A 243      -8.954  10.378 -20.727  1.00 75.05           C  
ANISOU 1904  CG2 ILE A 243    10716  11491   6309   -517  -3494  -1312       C  
ATOM   1905  CD1 ILE A 243      -9.016   8.617 -18.187  1.00 63.92           C  
ANISOU 1905  CD1 ILE A 243     8907   9803   5579   -563  -3171  -1542       C  
ATOM   1906  N   ILE A 244      -8.929   6.645 -22.468  1.00 79.18           N  
ANISOU 1906  N   ILE A 244    11360  12149   6576   -728  -3566  -2041       N  
ATOM   1907  CA  ILE A 244      -9.916   5.908 -23.245  1.00 81.58           C  
ANISOU 1907  CA  ILE A 244    11638  12509   6851   -784  -3802  -2205       C  
ATOM   1908  C   ILE A 244     -10.850   5.185 -22.286  1.00 77.42           C  
ANISOU 1908  C   ILE A 244    10863  11843   6710   -809  -3872  -2310       C  
ATOM   1909  O   ILE A 244     -10.399   4.406 -21.432  1.00 72.16           O  
ANISOU 1909  O   ILE A 244    10123  11052   6243   -836  -3683  -2409       O  
ATOM   1910  CB  ILE A 244      -9.258   4.917 -24.216  1.00 80.04           C  
ANISOU 1910  CB  ILE A 244    11599  12389   6422   -862  -3700  -2401       C  
ATOM   1911  CG1 ILE A 244      -8.331   5.653 -25.184  1.00 81.56           C  
ANISOU 1911  CG1 ILE A 244    12023  12744   6222   -854  -3608  -2296       C  
ATOM   1912  CG2 ILE A 244     -10.320   4.141 -24.979  1.00 82.38           C  
ANISOU 1912  CG2 ILE A 244    11842  12721   6739   -943  -3893  -2535       C  
ATOM   1913  CD1 ILE A 244      -7.656   4.747 -26.189  1.00 94.23           C  
ANISOU 1913  CD1 ILE A 244    13786  14436   7581   -936  -3497  -2489       C  
ATOM   1914  N   PHE A 245     -12.146   5.454 -22.430  1.00 75.73           N  
ANISOU 1914  N   PHE A 245    10503  11647   6622   -813  -4096  -2258       N  
ATOM   1915  CA  PHE A 245     -13.216   4.756 -21.732  1.00 75.35           C  
ANISOU 1915  CA  PHE A 245    10211  11501   6919   -865  -4180  -2360       C  
ATOM   1916  C   PHE A 245     -13.937   3.841 -22.714  1.00 78.32           C  
ANISOU 1916  C   PHE A 245    10589  11933   7237   -963  -4317  -2517       C  
ATOM   1917  O   PHE A 245     -14.390   4.294 -23.771  1.00 81.56           O  
ANISOU 1917  O   PHE A 245    11068  12475   7445   -955  -4482  -2461       O  
ATOM   1918  CB  PHE A 245     -14.220   5.743 -21.130  1.00 75.03           C  
ANISOU 1918  CB  PHE A 245     9971  11444   7092   -795  -4326  -2197       C  
ATOM   1919  CG  PHE A 245     -13.694   6.521 -19.959  1.00 72.09           C  
ANISOU 1919  CG  PHE A 245     9542  10982   6867   -718  -4160  -2042       C  
ATOM   1920  CD1 PHE A 245     -12.889   7.632 -20.149  1.00 71.35           C  
ANISOU 1920  CD1 PHE A 245     9608  10927   6573   -636  -4074  -1844       C  
ATOM   1921  CD2 PHE A 245     -14.029   6.157 -18.666  1.00 70.26           C  
ANISOU 1921  CD2 PHE A 245     9089  10621   6986   -746  -4033  -2059       C  
ATOM   1922  CE1 PHE A 245     -12.415   8.354 -19.070  1.00 72.65           C  
ANISOU 1922  CE1 PHE A 245     9710  10999   6897   -578  -3871  -1680       C  
ATOM   1923  CE2 PHE A 245     -13.557   6.874 -17.584  1.00 67.71           C  
ANISOU 1923  CE2 PHE A 245     8708  10214   6804   -685  -3827  -1894       C  
ATOM   1924  CZ  PHE A 245     -12.749   7.973 -17.786  1.00 66.94           C  
ANISOU 1924  CZ  PHE A 245     8767  10152   6515   -598  -3751  -1710       C  
ATOM   1925  N   GLU A 246     -14.044   2.562 -22.363  1.00 80.36           N  
ANISOU 1925  N   GLU A 246    10776  12086   7672  -1057  -4253  -2709       N  
ATOM   1926  CA  GLU A 246     -14.853   1.609 -23.112  1.00 93.51           C  
ANISOU 1926  CA  GLU A 246    12412  13771   9346  -1162  -4389  -2866       C  
ATOM   1927  C   GLU A 246     -15.791   0.910 -22.142  1.00 98.38           C  
ANISOU 1927  C   GLU A 246    12779  14253  10346  -1237  -4416  -2939       C  
ATOM   1928  O   GLU A 246     -15.339   0.339 -21.146  1.00 97.94           O  
ANISOU 1928  O   GLU A 246    12674  14053  10484  -1265  -4249  -2994       O  
ATOM   1929  CB  GLU A 246     -13.987   0.579 -23.842  1.00100.13           C  
ANISOU 1929  CB  GLU A 246    13455  14606   9985  -1225  -4277  -3048       C  
ATOM   1930  CG  GLU A 246     -13.129   1.160 -24.945  1.00103.26           C  
ANISOU 1930  CG  GLU A 246    14096  15158   9978  -1181  -4244  -2997       C  
ATOM   1931  CD  GLU A 246     -12.376   0.094 -25.711  1.00106.33           C  
ANISOU 1931  CD  GLU A 246    14668  15548  10184  -1247  -4137  -3198       C  
ATOM   1932  OE1 GLU A 246     -12.331  -1.062 -25.241  1.00104.79           O  
ANISOU 1932  OE1 GLU A 246    14422  15201  10190  -1304  -4063  -3365       O  
ATOM   1933  OE2 GLU A 246     -11.833   0.412 -26.789  1.00111.54           O  
ANISOU 1933  OE2 GLU A 246    15525  16354  10501  -1244  -4126  -3186       O  
ATOM   1934  N   ALA A 247     -17.090   0.951 -22.430  1.00 82.71           N  
ANISOU 1934  N   ALA A 247    10635  12319   8470  -1277  -4619  -2938       N  
ATOM   1935  CA  ALA A 247     -18.062   0.379 -21.512  1.00 82.57           C  
ANISOU 1935  CA  ALA A 247    10362  12194   8816  -1360  -4638  -2992       C  
ATOM   1936  C   ALA A 247     -19.300  -0.072 -22.270  1.00104.00           C  
ANISOU 1936  C   ALA A 247    12974  14974  11565  -1445  -4853  -3079       C  
ATOM   1937  O   ALA A 247     -19.621   0.451 -23.341  1.00101.01           O  
ANISOU 1937  O   ALA A 247    12669  14742  10969  -1404  -5024  -3040       O  
ATOM   1938  CB  ALA A 247     -18.455   1.379 -20.419  1.00 80.63           C  
ANISOU 1938  CB  ALA A 247     9915  11929   8794  -1280  -4623  -2829       C  
ATOM   1939  N   ASN A 248     -19.990  -1.060 -21.695  1.00105.90           N  
ANISOU 1939  N   ASN A 248    13050  15106  12080  -1572  -4840  -3193       N  
ATOM   1940  CA  ASN A 248     -21.288  -1.502 -22.185  1.00104.19           C  
ANISOU 1940  CA  ASN A 248    12686  14940  11964  -1666  -5035  -3274       C  
ATOM   1941  C   ASN A 248     -22.337  -1.497 -21.081  1.00104.77           C  
ANISOU 1941  C   ASN A 248    12449  14953  12405  -1720  -5034  -3240       C  
ATOM   1942  O   ASN A 248     -23.406  -2.091 -21.254  1.00108.09           O  
ANISOU 1942  O   ASN A 248    12719  15382  12969  -1831  -5153  -3329       O  
ATOM   1943  CB  ASN A 248     -21.187  -2.899 -22.810  1.00105.32           C  
ANISOU 1943  CB  ASN A 248    12948  15019  12048  -1803  -5037  -3478       C  
ATOM   1944  CG  ASN A 248     -20.826  -3.968 -21.797  1.00104.91           C  
ANISOU 1944  CG  ASN A 248    12868  14765  12228  -1906  -4845  -3567       C  
ATOM   1945  OD1 ASN A 248     -20.295  -3.675 -20.727  1.00110.80           O  
ANISOU 1945  OD1 ASN A 248    13572  15423  13104  -1863  -4677  -3481       O  
ATOM   1946  ND2 ASN A 248     -21.109  -5.221 -22.135  1.00106.43           N  
ANISOU 1946  ND2 ASN A 248    13090  14875  12471  -2045  -4874  -3738       N  
ATOM   1947  N   GLY A 249     -22.060  -0.851 -19.960  1.00 95.57           N  
ANISOU 1947  N   GLY A 249    11185  13734  11392  -1652  -4896  -3120       N  
ATOM   1948  CA  GLY A 249     -22.994  -0.791 -18.857  1.00 92.86           C  
ANISOU 1948  CA  GLY A 249    10548  13345  11388  -1704  -4864  -3085       C  
ATOM   1949  C   GLY A 249     -22.282  -0.534 -17.552  1.00 84.26           C  
ANISOU 1949  C   GLY A 249     9428  12149  10439  -1672  -4639  -3004       C  
ATOM   1950  O   GLY A 249     -21.078  -0.756 -17.411  1.00 91.00           O  
ANISOU 1950  O   GLY A 249    10480  12925  11171  -1649  -4493  -3013       O  
ATOM   1951  N   ASN A 250     -23.055  -0.034 -16.585  1.00 85.65           N  
ANISOU 1951  N   ASN A 250     9342  12328  10874  -1669  -4609  -2928       N  
ATOM   1952  CA  ASN A 250     -22.591   0.184 -15.213  1.00 86.06           C  
ANISOU 1952  CA  ASN A 250     9314  12283  11102  -1662  -4394  -2856       C  
ATOM   1953  C   ASN A 250     -21.471   1.218 -15.136  1.00 85.90           C  
ANISOU 1953  C   ASN A 250     9452  12281  10904  -1491  -4330  -2735       C  
ATOM   1954  O   ASN A 250     -20.669   1.209 -14.199  1.00 81.65           O  
ANISOU 1954  O   ASN A 250     8948  11648  10429  -1487  -4140  -2700       O  
ATOM   1955  CB  ASN A 250     -22.147  -1.130 -14.565  1.00 92.08           C  
ANISOU 1955  CB  ASN A 250    10130  12877  11978  -1825  -4218  -2955       C  
ATOM   1956  CG  ASN A 250     -23.256  -2.159 -14.521  1.00 99.51           C  
ANISOU 1956  CG  ASN A 250    10913  13783  13111  -2011  -4266  -3060       C  
ATOM   1957  OD1 ASN A 250     -23.506  -2.862 -15.500  1.00104.43           O  
ANISOU 1957  OD1 ASN A 250    11626  14421  13632  -2077  -4396  -3171       O  
ATOM   1958  ND2 ASN A 250     -23.931  -2.252 -13.381  1.00102.72           N  
ANISOU 1958  ND2 ASN A 250    11087  14148  13794  -2105  -4156  -3025       N  
ATOM   1959  N   LEU A 251     -21.414   2.126 -16.106  1.00 94.83           N  
ANISOU 1959  N   LEU A 251    10686  13534  11811  -1355  -4488  -2662       N  
ATOM   1960  CA  LEU A 251     -20.426   3.197 -16.120  1.00 75.67           C  
ANISOU 1960  CA  LEU A 251     8416  11134   9202  -1197  -4446  -2528       C  
ATOM   1961  C   LEU A 251     -21.086   4.508 -15.711  1.00 75.59           C  
ANISOU 1961  C   LEU A 251     8222  11187   9310  -1067  -4521  -2383       C  
ATOM   1962  O   LEU A 251     -21.990   4.993 -16.399  1.00 77.90           O  
ANISOU 1962  O   LEU A 251     8436  11578   9585  -1016  -4717  -2353       O  
ATOM   1963  CB  LEU A 251     -19.786   3.344 -17.500  1.00 76.78           C  
ANISOU 1963  CB  LEU A 251     8834  11358   8980  -1139  -4551  -2527       C  
ATOM   1964  CG  LEU A 251     -18.968   4.631 -17.674  1.00 75.40           C  
ANISOU 1964  CG  LEU A 251     8814  11235   8598   -976  -4546  -2358       C  
ATOM   1965  CD1 LEU A 251     -17.723   4.609 -16.797  1.00 72.26           C  
ANISOU 1965  CD1 LEU A 251     8517  10740   8200   -957  -4318  -2337       C  
ATOM   1966  CD2 LEU A 251     -18.603   4.867 -19.131  1.00 77.23           C  
ANISOU 1966  CD2 LEU A 251     9292  11579   8471   -935  -4670  -2338       C  
ATOM   1967  N   ILE A 252     -20.634   5.075 -14.596  1.00 84.95           N  
ANISOU 1967  N   ILE A 252     9344  12313  10621  -1010  -4367  -2299       N  
ATOM   1968  CA  ILE A 252     -20.990   6.436 -14.213  1.00 72.69           C  
ANISOU 1968  CA  ILE A 252     7668  10804   9148   -858  -4418  -2152       C  
ATOM   1969  C   ILE A 252     -19.994   7.346 -14.924  1.00 71.95           C  
ANISOU 1969  C   ILE A 252     7845  10744   8751   -719  -4468  -2025       C  
ATOM   1970  O   ILE A 252     -18.896   7.596 -14.426  1.00 69.53           O  
ANISOU 1970  O   ILE A 252     7688  10365   8364   -687  -4228  -1919       O  
ATOM   1971  CB  ILE A 252     -20.962   6.629 -12.697  1.00 70.53           C  
ANISOU 1971  CB  ILE A 252     7215  10450   9132   -866  -4192  -2105       C  
ATOM   1972  CG1 ILE A 252     -21.771   5.535 -12.001  1.00 71.26           C  
ANISOU 1972  CG1 ILE A 252     7077  10506   9494  -1045  -4131  -2250       C  
ATOM   1973  CG2 ILE A 252     -21.502   8.004 -12.327  1.00 70.62           C  
ANISOU 1973  CG2 ILE A 252     7071  10506   9254   -706  -4256  -1978       C  
ATOM   1974  CD1 ILE A 252     -23.221   5.472 -12.431  1.00 74.28           C  
ANISOU 1974  CD1 ILE A 252     7248  10974  10003  -1075  -4294  -2296       C  
ATOM   1975  N   ALA A 253     -20.381   7.832 -16.100  1.00 80.05           N  
ANISOU 1975  N   ALA A 253     8959  11864   9593   -652  -4673  -1973       N  
ATOM   1976  CA  ALA A 253     -19.453   8.515 -16.983  1.00 74.13           C  
ANISOU 1976  CA  ALA A 253     8501  11155   8508   -561  -4719  -1859       C  
ATOM   1977  C   ALA A 253     -18.994   9.846 -16.387  1.00 72.39           C  
ANISOU 1977  C   ALA A 253     8303  10898   8302   -413  -4672  -1672       C  
ATOM   1978  O   ALA A 253     -19.705  10.460 -15.586  1.00 72.18           O  
ANISOU 1978  O   ALA A 253     8047  10846   8531   -346  -4682  -1622       O  
ATOM   1979  CB  ALA A 253     -20.099   8.756 -18.345  1.00 77.32           C  
ANISOU 1979  CB  ALA A 253     8977  11672   8728   -533  -4954  -1836       C  
ATOM   1980  N   PRO A 254     -17.799  10.305 -16.756  1.00 71.25           N  
ANISOU 1980  N   PRO A 254     8434  10745   7892   -371  -4554  -1549       N  
ATOM   1981  CA  PRO A 254     -17.361  11.640 -16.334  1.00 69.97           C  
ANISOU 1981  CA  PRO A 254     8324  10538   7723   -241  -4478  -1336       C  
ATOM   1982  C   PRO A 254     -18.092  12.729 -17.099  1.00 72.35           C  
ANISOU 1982  C   PRO A 254     8632  10902   7955   -114  -4790  -1227       C  
ATOM   1983  O   PRO A 254     -18.347  12.608 -18.300  1.00 79.01           O  
ANISOU 1983  O   PRO A 254     9595  11835   8590   -131  -4957  -1237       O  
ATOM   1984  CB  PRO A 254     -15.863  11.647 -16.662  1.00 68.50           C  
ANISOU 1984  CB  PRO A 254     8437  10339   7251   -265  -4274  -1262       C  
ATOM   1985  CG  PRO A 254     -15.494  10.210 -16.867  1.00 68.37           C  
ANISOU 1985  CG  PRO A 254     8470  10330   7176   -401  -4176  -1454       C  
ATOM   1986  CD  PRO A 254     -16.717   9.553 -17.413  1.00 84.87           C  
ANISOU 1986  CD  PRO A 254    10417  12487   9342   -453  -4439  -1613       C  
ATOM   1987  N   ARG A 255     -18.421  13.807 -16.392  1.00 71.81           N  
ANISOU 1987  N   ARG A 255     8438  10775   8072      8  -4791  -1099       N  
ATOM   1988  CA  ARG A 255     -19.030  14.980 -17.003  1.00 73.98           C  
ANISOU 1988  CA  ARG A 255     8729  11071   8308    146  -5026   -957       C  
ATOM   1989  C   ARG A 255     -18.066  16.159 -17.035  1.00 72.95           C  
ANISOU 1989  C   ARG A 255     8830  10878   8009    241  -4985   -743       C  
ATOM   1990  O   ARG A 255     -17.746  16.661 -18.114  1.00 74.53           O  
ANISOU 1990  O   ARG A 255     9270  11120   7929    262  -5080   -619       O  
ATOM   1991  CB  ARG A 255     -20.324  15.348 -16.265  1.00 74.84           C  
ANISOU 1991  CB  ARG A 255     8499  11160   8778    225  -5098   -991       C  
ATOM   1992  CG  ARG A 255     -21.053  16.543 -16.849  1.00 77.35           C  
ANISOU 1992  CG  ARG A 255     8811  11481   9097    377  -5309   -850       C  
ATOM   1993  CD  ARG A 255     -22.550  16.303 -16.912  1.00 80.16           C  
ANISOU 1993  CD  ARG A 255     8876  11895   9686    391  -5458   -963       C  
ATOM   1994  NE  ARG A 255     -23.319  17.523 -16.679  1.00 81.29           N  
ANISOU 1994  NE  ARG A 255     8883  11992  10011    567  -5576   -862       N  
ATOM   1995  CZ  ARG A 255     -23.503  18.482 -17.581  1.00 83.56           C  
ANISOU 1995  CZ  ARG A 255     9316  12277  10157    683  -5771   -714       C  
ATOM   1996  NH1 ARG A 255     -22.966  18.378 -18.788  1.00 90.77           N  
ANISOU 1996  NH1 ARG A 255    10514  13245  10728    635  -5862   -642       N  
ATOM   1997  NH2 ARG A 255     -24.221  19.552 -17.270  1.00 84.88           N  
ANISOU 1997  NH2 ARG A 255     9344  12383  10522    847  -5868   -643       N  
ATOM   1998  N   TYR A 256     -17.579  16.603 -15.878  1.00 70.46           N  
ANISOU 1998  N   TYR A 256     8452  10458   7861    274  -4736   -674       N  
ATOM   1999  CA  TYR A 256     -16.626  17.699 -15.782  1.00 69.35           C  
ANISOU 1999  CA  TYR A 256     8516  10240   7594    342  -4626   -468       C  
ATOM   2000  C   TYR A 256     -15.267  17.195 -15.312  1.00 66.58           C  
ANISOU 2000  C   TYR A 256     8304   9854   7139    236  -4278   -469       C  
ATOM   2001  O   TYR A 256     -15.172  16.214 -14.568  1.00 64.95           O  
ANISOU 2001  O   TYR A 256     7970   9637   7073    148  -4086   -608       O  
ATOM   2002  CB  TYR A 256     -17.119  18.784 -14.819  1.00 75.71           C  
ANISOU 2002  CB  TYR A 256     9144  10943   8680    483  -4631   -382       C  
ATOM   2003  CG  TYR A 256     -18.240  19.633 -15.365  1.00 73.10           C  
ANISOU 2003  CG  TYR A 256     8730  10623   8423    629  -4986   -329       C  
ATOM   2004  CD1 TYR A 256     -19.552  19.193 -15.317  1.00 76.37           C  
ANISOU 2004  CD1 TYR A 256     8863  11096   9056    643  -5119   -475       C  
ATOM   2005  CD2 TYR A 256     -17.986  20.880 -15.919  1.00 76.52           C  
ANISOU 2005  CD2 TYR A 256     9363  10995   8718    736  -5106   -120       C  
ATOM   2006  CE1 TYR A 256     -20.583  19.964 -15.815  1.00 76.38           C  
ANISOU 2006  CE1 TYR A 256     8782  11101   9140    764  -5325   -417       C  
ATOM   2007  CE2 TYR A 256     -19.010  21.661 -16.418  1.00 81.93           C  
ANISOU 2007  CE2 TYR A 256     9974  11670   9486    858  -5315    -57       C  
ATOM   2008  CZ  TYR A 256     -20.307  21.197 -16.363  1.00 84.35           C  
ANISOU 2008  CZ  TYR A 256     9996  12040  10012    877  -5429   -210       C  
ATOM   2009  OH  TYR A 256     -21.332  21.969 -16.857  1.00 83.16           O  
ANISOU 2009  OH  TYR A 256     9767  11881   9949   1005  -5644   -155       O  
ATOM   2010  N   ALA A 257     -14.215  17.889 -15.743  1.00 66.21           N  
ANISOU 2010  N   ALA A 257     8520   9786   6850    245  -4203   -307       N  
ATOM   2011  CA  ALA A 257     -12.846  17.589 -15.350  1.00 63.81           C  
ANISOU 2011  CA  ALA A 257     8352   9452   6439    161  -3885   -290       C  
ATOM   2012  C   ALA A 257     -12.171  18.863 -14.856  1.00 66.42           C  
ANISOU 2012  C   ALA A 257     8775   9681   6783    234  -3777    -93       C  
ATOM   2013  O   ALA A 257     -12.735  19.958 -14.922  1.00 80.10           O  
ANISOU 2013  O   ALA A 257    10493  11360   8581    348  -3958     33       O  
ATOM   2014  CB  ALA A 257     -12.051  16.973 -16.508  1.00 64.67           C  
ANISOU 2014  CB  ALA A 257     8709   9665   6197     60  -3866   -322       C  
ATOM   2015  N   PHE A 258     -10.941  18.713 -14.363  1.00 60.50           N  
ANISOU 2015  N   PHE A 258     8118   8894   5973    168  -3488    -71       N  
ATOM   2016  CA  PHE A 258     -10.208  19.810 -13.740  1.00 59.19           C  
ANISOU 2016  CA  PHE A 258     8021   8624   5845    217  -3349     92       C  
ATOM   2017  C   PHE A 258      -8.776  19.845 -14.250  1.00 68.69           C  
ANISOU 2017  C   PHE A 258     9473   9859   6768    128  -3168    168       C  
ATOM   2018  O   PHE A 258      -8.051  18.851 -14.144  1.00 57.39           O  
ANISOU 2018  O   PHE A 258     8057   8473   5273     36  -2974     49       O  
ATOM   2019  CB  PHE A 258     -10.205  19.676 -12.215  1.00 56.74           C  
ANISOU 2019  CB  PHE A 258     7501   8222   5836    235  -3146     29       C  
ATOM   2020  CG  PHE A 258     -11.574  19.633 -11.607  1.00 57.29           C  
ANISOU 2020  CG  PHE A 258     7304   8272   6193    310  -3281    -57       C  
ATOM   2021  CD1 PHE A 258     -12.243  18.430 -11.465  1.00 57.38           C  
ANISOU 2021  CD1 PHE A 258     7147   8344   6309    247  -3294   -240       C  
ATOM   2022  CD2 PHE A 258     -12.191  20.793 -11.175  1.00 57.90           C  
ANISOU 2022  CD2 PHE A 258     7290   8267   6442    441  -3393     36       C  
ATOM   2023  CE1 PHE A 258     -13.502  18.384 -10.907  1.00 58.08           C  
ANISOU 2023  CE1 PHE A 258     6974   8429   6664    301  -3403   -325       C  
ATOM   2024  CE2 PHE A 258     -13.453  20.753 -10.615  1.00 58.61           C  
ANISOU 2024  CE2 PHE A 258     7112   8353   6802    512  -3505    -61       C  
ATOM   2025  CZ  PHE A 258     -14.108  19.547 -10.480  1.00 58.70           C  
ANISOU 2025  CZ  PHE A 258     6949   8443   6912    436  -3505   -241       C  
ATOM   2026  N   ALA A 259      -8.370  20.997 -14.781  1.00 69.53           N  
ANISOU 2026  N   ALA A 259     9768   9934   6715    156  -3230    364       N  
ATOM   2027  CA  ALA A 259      -6.990  21.228 -15.197  1.00 68.71           C  
ANISOU 2027  CA  ALA A 259     9891   9858   6359     66  -3044    457       C  
ATOM   2028  C   ALA A 259      -6.241  21.865 -14.032  1.00 67.06           C  
ANISOU 2028  C   ALA A 259     9635   9524   6320     83  -2823    531       C  
ATOM   2029  O   ALA A 259      -6.519  23.007 -13.658  1.00 70.70           O  
ANISOU 2029  O   ALA A 259    10091   9872   6901    167  -2904    670       O  
ATOM   2030  CB  ALA A 259      -6.941  22.112 -16.439  1.00 71.48           C  
ANISOU 2030  CB  ALA A 259    10488  10245   6427     62  -3228    639       C  
ATOM   2031  N   LEU A 260      -5.283  21.133 -13.471  1.00 57.99           N  
ANISOU 2031  N   LEU A 260     8457   8393   5183      8  -2556    433       N  
ATOM   2032  CA  LEU A 260      -4.671  21.499 -12.202  1.00 52.72           C  
ANISOU 2032  CA  LEU A 260     7702   7616   4713     23  -2350    458       C  
ATOM   2033  C   LEU A 260      -3.470  22.415 -12.393  1.00 62.38           C  
ANISOU 2033  C   LEU A 260     9110   8809   5781    -26  -2219    619       C  
ATOM   2034  O   LEU A 260      -2.662  22.226 -13.307  1.00 59.10           O  
ANISOU 2034  O   LEU A 260     8867   8493   5097   -119  -2152    641       O  
ATOM   2035  CB  LEU A 260      -4.244  20.243 -11.443  1.00 50.66           C  
ANISOU 2035  CB  LEU A 260     7315   7378   4556    -28  -2144    276       C  
ATOM   2036  CG  LEU A 260      -5.344  19.201 -11.239  1.00 50.74           C  
ANISOU 2036  CG  LEU A 260     7147   7416   4716    -11  -2245    108       C  
ATOM   2037  CD1 LEU A 260      -4.803  17.990 -10.505  1.00 48.87           C  
ANISOU 2037  CD1 LEU A 260     6822   7179   4567    -71  -2038    -49       C  
ATOM   2038  CD2 LEU A 260      -6.523  19.805 -10.492  1.00 50.80           C  
ANISOU 2038  CD2 LEU A 260     6977   7340   4985     91  -2378    134       C  
ATOM   2039  N   SER A 261      -3.359  23.405 -11.510  1.00 71.43           N  
ANISOU 2039  N   SER A 261    10216   9822   7103     29  -2177    721       N  
ATOM   2040  CA  SER A 261      -2.203  24.293 -11.434  1.00 62.94           C  
ANISOU 2040  CA  SER A 261     9280   8692   5941    -25  -2032    864       C  
ATOM   2041  C   SER A 261      -1.577  24.121 -10.056  1.00 65.91           C  
ANISOU 2041  C   SER A 261     9518   8998   6528    -24  -1808    791       C  
ATOM   2042  O   SER A 261      -2.197  24.455  -9.040  1.00 63.93           O  
ANISOU 2042  O   SER A 261     9120   8644   6529     65  -1838    773       O  
ATOM   2043  CB  SER A 261      -2.603  25.746 -11.686  1.00 58.58           C  
ANISOU 2043  CB  SER A 261     8835   8024   5397     38  -2211   1066       C  
ATOM   2044  OG  SER A 261      -3.126  25.907 -12.993  1.00 60.77           O  
ANISOU 2044  OG  SER A 261     9263   8368   5457     34  -2430   1148       O  
ATOM   2045  N   ARG A 262      -0.355  23.598 -10.024  1.00 79.00           N  
ANISOU 2045  N   ARG A 262    11219  10717   8079   -120  -1587    741       N  
ATOM   2046  CA  ARG A 262       0.302  23.301  -8.762  1.00 68.56           C  
ANISOU 2046  CA  ARG A 262     9771   9341   6937   -123  -1383    662       C  
ATOM   2047  C   ARG A 262       0.712  24.584  -8.043  1.00 69.74           C  
ANISOU 2047  C   ARG A 262     9942   9357   7197   -102  -1337    796       C  
ATOM   2048  O   ARG A 262       0.833  25.658  -8.640  1.00 76.97           O  
ANISOU 2048  O   ARG A 262    11005  10230   8012   -116  -1416    960       O  
ATOM   2049  CB  ARG A 262       1.526  22.414  -8.992  1.00 71.79           C  
ANISOU 2049  CB  ARG A 262    10218   9853   7205   -221  -1178    568       C  
ATOM   2050  CG  ARG A 262       1.199  21.055  -9.587  1.00 75.27           C  
ANISOU 2050  CG  ARG A 262    10632  10409   7559   -239  -1206    406       C  
ATOM   2051  CD  ARG A 262       0.424  20.189  -8.607  1.00 74.39           C  
ANISOU 2051  CD  ARG A 262    10331  10250   7685   -181  -1222    267       C  
ATOM   2052  NE  ARG A 262       0.138  18.869  -9.164  1.00 80.85           N  
ANISOU 2052  NE  ARG A 262    11129  11158   8432   -209  -1252    109       N  
ATOM   2053  CZ  ARG A 262      -0.456  17.885  -8.496  1.00 65.97           C  
ANISOU 2053  CZ  ARG A 262     9102   9247   6718   -189  -1257    -26       C  
ATOM   2054  NH1 ARG A 262      -0.829  18.064  -7.237  1.00 60.90           N  
ANISOU 2054  NH1 ARG A 262     8321   8504   6314   -142  -1225    -21       N  
ATOM   2055  NH2 ARG A 262      -0.673  16.719  -9.088  1.00 61.92           N  
ANISOU 2055  NH2 ARG A 262     8589   8805   6132   -223  -1292   -169       N  
ATOM   2056  N   GLY A 263       0.923  24.456  -6.737  1.00 71.93           N  
ANISOU 2056  N   GLY A 263    10081   9564   7684    -71  -1214    726       N  
ATOM   2057  CA  GLY A 263       1.327  25.577  -5.912  1.00 69.79           C  
ANISOU 2057  CA  GLY A 263     9814   9165   7539    -50  -1160    821       C  
ATOM   2058  C   GLY A 263       1.699  25.146  -4.511  1.00 72.85           C  
ANISOU 2058  C   GLY A 263    10053   9511   8114    -35  -1001    711       C  
ATOM   2059  O   GLY A 263       1.043  24.278  -3.927  1.00 74.19           O  
ANISOU 2059  O   GLY A 263    10084   9702   8404      7  -1005    586       O  
ATOM   2060  N   PHE A 264       2.753  25.740  -3.963  1.00 75.60           N  
ANISOU 2060  N   PHE A 264    10435   9803   8485    -78   -865    760       N  
ATOM   2061  CA  PHE A 264       3.219  25.405  -2.628  1.00 73.79           C  
ANISOU 2061  CA  PHE A 264    10086   9537   8415    -68   -721    668       C  
ATOM   2062  C   PHE A 264       2.598  26.338  -1.595  1.00 68.84           C  
ANISOU 2062  C   PHE A 264     9390   8776   7992     19   -775    696       C  
ATOM   2063  O   PHE A 264       2.178  27.456  -1.902  1.00 70.48           O  
ANISOU 2063  O   PHE A 264     9666   8897   8218     59   -895    808       O  
ATOM   2064  CB  PHE A 264       4.745  25.482  -2.554  1.00 76.33           C  
ANISOU 2064  CB  PHE A 264    10464   9882   8658   -163   -545    684       C  
ATOM   2065  CG  PHE A 264       5.443  24.832  -3.717  1.00 94.77           C  
ANISOU 2065  CG  PHE A 264    12886  12351  10773   -251   -486    669       C  
ATOM   2066  CD1 PHE A 264       5.740  23.479  -3.701  1.00100.37           C  
ANISOU 2066  CD1 PHE A 264    13527  13154  11453   -265   -402    523       C  
ATOM   2067  CD2 PHE A 264       5.806  25.578  -4.827  1.00103.03           C  
ANISOU 2067  CD2 PHE A 264    14087  13424  11634   -322   -514    799       C  
ATOM   2068  CE1 PHE A 264       6.381  22.883  -4.772  1.00 99.21           C  
ANISOU 2068  CE1 PHE A 264    13455  13134  11106   -337   -343    487       C  
ATOM   2069  CE2 PHE A 264       6.446  24.988  -5.900  1.00103.05           C  
ANISOU 2069  CE2 PHE A 264    14169  13567  11419   -408   -446    774       C  
ATOM   2070  CZ  PHE A 264       6.734  23.639  -5.872  1.00102.61           C  
ANISOU 2070  CZ  PHE A 264    14033  13611  11343   -410   -358    609       C  
ATOM   2071  N   GLY A 264A      2.548  25.861  -0.352  1.00 57.74           N  
ANISOU 2071  N   GLY A 264A    7851   7349   6737     50   -686    590       N  
ATOM   2072  CA  GLY A 264A      2.029  26.642   0.747  1.00 59.58           C  
ANISOU 2072  CA  GLY A 264A    8007   7471   7159    129   -707    585       C  
ATOM   2073  C   GLY A 264A      0.572  26.405   1.073  1.00 55.54           C  
ANISOU 2073  C   GLY A 264A    7367   6959   6778    222   -815    516       C  
ATOM   2074  O   GLY A 264A      0.101  26.885   2.111  1.00 71.76           O  
ANISOU 2074  O   GLY A 264A    9330   8942   8995    289   -807    477       O  
ATOM   2075  N   SER A 265      -0.154  25.687   0.225  1.00 54.08           N  
ANISOU 2075  N   SER A 265     7165   6856   6527    223   -912    488       N  
ATOM   2076  CA  SER A 265      -1.554  25.386   0.461  1.00 45.78           C  
ANISOU 2076  CA  SER A 265     5972   5820   5602    298  -1016    412       C  
ATOM   2077  C   SER A 265      -1.693  24.054   1.191  1.00 42.45           C  
ANISOU 2077  C   SER A 265     5430   5466   5234    258   -908    278       C  
ATOM   2078  O   SER A 265      -0.735  23.294   1.344  1.00 43.86           O  
ANISOU 2078  O   SER A 265     5649   5680   5338    182   -779    247       O  
ATOM   2079  CB  SER A 265      -2.322  25.359  -0.860  1.00 51.18           C  
ANISOU 2079  CB  SER A 265     6700   6554   6194    319  -1203    454       C  
ATOM   2080  OG  SER A 265      -3.704  25.140  -0.642  1.00 56.88           O  
ANISOU 2080  OG  SER A 265     7264   7291   7056    394  -1316    375       O  
ATOM   2081  N   GLY A 266      -2.906  23.777   1.649  1.00 41.80           N  
ANISOU 2081  N   GLY A 266     5196   5397   5289    308   -963    199       N  
ATOM   2082  CA  GLY A 266      -3.160  22.545   2.372  1.00 35.84           C  
ANISOU 2082  CA  GLY A 266     4330   4695   4592    258   -868     84       C  
ATOM   2083  C   GLY A 266      -4.607  22.476   2.804  1.00 40.78           C  
ANISOU 2083  C   GLY A 266     4778   5339   5377    311   -939      8       C  
ATOM   2084  O   GLY A 266      -5.385  23.417   2.616  1.00 45.32           O  
ANISOU 2084  O   GLY A 266     5304   5882   6032    403  -1061     34       O  
ATOM   2085  N   ILE A 267      -4.954  21.334   3.389  1.00 42.20           N  
ANISOU 2085  N   ILE A 267     4859   5567   5608    248   -860    -89       N  
ATOM   2086  CA  ILE A 267      -6.303  21.052   3.868  1.00 43.88           C  
ANISOU 2086  CA  ILE A 267     4883   5818   5972    265   -895   -178       C  
ATOM   2087  C   ILE A 267      -6.253  21.014   5.389  1.00 48.34           C  
ANISOU 2087  C   ILE A 267     5368   6362   6639    250   -730   -227       C  
ATOM   2088  O   ILE A 267      -5.459  20.264   5.970  1.00 50.23           O  
ANISOU 2088  O   ILE A 267     5664   6594   6826    170   -597   -236       O  
ATOM   2089  CB  ILE A 267      -6.838  19.730   3.296  1.00 41.64           C  
ANISOU 2089  CB  ILE A 267     4551   5609   5662    183   -940   -249       C  
ATOM   2090  CG1 ILE A 267      -6.938  19.809   1.772  1.00 49.52           C  
ANISOU 2090  CG1 ILE A 267     5634   6640   6542    201  -1115   -209       C  
ATOM   2091  CG2 ILE A 267      -8.178  19.368   3.920  1.00 37.69           C  
ANISOU 2091  CG2 ILE A 267     3839   5154   5328    174   -947   -347       C  
ATOM   2092  CD1 ILE A 267      -7.346  18.506   1.121  1.00 44.52           C  
ANISOU 2092  CD1 ILE A 267     4976   6075   5867    116  -1168   -287       C  
ATOM   2093  N   ILE A 268      -7.086  21.826   6.038  1.00 36.16           N  
ANISOU 2093  N   ILE A 268     3696   4808   5237    330   -741   -263       N  
ATOM   2094  CA  ILE A 268      -7.136  21.860   7.493  1.00 35.60           C  
ANISOU 2094  CA  ILE A 268     3544   4730   5251    317   -583   -320       C  
ATOM   2095  C   ILE A 268      -8.571  21.655   7.956  1.00 38.47           C  
ANISOU 2095  C   ILE A 268     3690   5163   5765    326   -588   -425       C  
ATOM   2096  O   ILE A 268      -9.528  21.980   7.248  1.00 44.78           O  
ANISOU 2096  O   ILE A 268     4386   5990   6639    393   -735   -449       O  
ATOM   2097  CB  ILE A 268      -6.565  23.176   8.073  1.00 35.27           C  
ANISOU 2097  CB  ILE A 268     3563   4605   5234    404   -548   -280       C  
ATOM   2098  CG1 ILE A 268      -7.396  24.378   7.627  1.00 36.84           C  
ANISOU 2098  CG1 ILE A 268     3692   4768   5537    540   -696   -277       C  
ATOM   2099  CG2 ILE A 268      -5.111  23.352   7.669  1.00 52.53           C  
ANISOU 2099  CG2 ILE A 268     5948   6731   7278    375   -527   -181       C  
ATOM   2100  CD1 ILE A 268      -6.947  25.679   8.250  1.00 36.78           C  
ANISOU 2100  CD1 ILE A 268     3735   4662   5578    627   -667   -254       C  
ATOM   2101  N   ASN A 269      -8.711  21.095   9.154  1.00 40.14           N  
ANISOU 2101  N   ASN A 269     3827   5407   6017    253   -427   -487       N  
ATOM   2102  CA  ASN A 269     -10.000  20.947   9.817  1.00 42.41           C  
ANISOU 2102  CA  ASN A 269     3897   5772   6446    244   -384   -595       C  
ATOM   2103  C   ASN A 269     -10.127  22.043  10.867  1.00 39.76           C  
ANISOU 2103  C   ASN A 269     3499   5416   6192    335   -300   -639       C  
ATOM   2104  O   ASN A 269      -9.288  22.141  11.769  1.00 52.92           O  
ANISOU 2104  O   ASN A 269     5265   7047   7797    306   -168   -619       O  
ATOM   2105  CB  ASN A 269     -10.135  19.570  10.466  1.00 50.88           C  
ANISOU 2105  CB  ASN A 269     4934   6899   7498     83   -252   -634       C  
ATOM   2106  CG  ASN A 269      -9.981  18.438   9.474  1.00 62.13           C  
ANISOU 2106  CG  ASN A 269     6427   8331   8850     -8   -333   -608       C  
ATOM   2107  OD1 ASN A 269     -10.508  18.491   8.363  1.00 62.64           O  
ANISOU 2107  OD1 ASN A 269     6450   8417   8933     31   -493   -614       O  
ATOM   2108  ND2 ASN A 269      -9.251  17.403   9.872  1.00 73.52           N  
ANISOU 2108  ND2 ASN A 269     7979   9748  10206   -125   -232   -582       N  
ATOM   2109  N   SER A 270     -11.170  22.860  10.752  1.00 39.76           N  
ANISOU 2109  N   SER A 270     3335   5437   6336    451   -385   -708       N  
ATOM   2110  CA  SER A 270     -11.333  23.980  11.666  1.00 40.30           C  
ANISOU 2110  CA  SER A 270     3341   5476   6494    558   -321   -768       C  
ATOM   2111  C   SER A 270     -12.798  24.379  11.732  1.00 42.49           C  
ANISOU 2111  C   SER A 270     3361   5825   6957    647   -374   -893       C  
ATOM   2112  O   SER A 270     -13.529  24.284  10.743  1.00 43.63           O  
ANISOU 2112  O   SER A 270     3416   5997   7165    687   -539   -899       O  
ATOM   2113  CB  SER A 270     -10.477  25.176  11.235  1.00 39.80           C  
ANISOU 2113  CB  SER A 270     3444   5283   6396    675   -417   -679       C  
ATOM   2114  OG  SER A 270     -10.749  26.313  12.036  1.00 44.04           O  
ANISOU 2114  OG  SER A 270     3912   5778   7044    793   -381   -754       O  
ATOM   2115  N   ASN A 271     -13.215  24.823  12.916  1.00 57.93           N  
ANISOU 2115  N   ASN A 271     5194   7818   8999    680   -233  -1004       N  
ATOM   2116  CA  ASN A 271     -14.535  25.400  13.126  1.00 53.51           C  
ANISOU 2116  CA  ASN A 271     4375   7322   8632    791   -264  -1146       C  
ATOM   2117  C   ASN A 271     -14.496  26.915  13.266  1.00 53.01           C  
ANISOU 2117  C   ASN A 271     4321   7154   8666    989   -337  -1178       C  
ATOM   2118  O   ASN A 271     -15.538  27.528  13.514  1.00 59.84           O  
ANISOU 2118  O   ASN A 271     4970   8059   9708   1110   -363  -1313       O  
ATOM   2119  CB  ASN A 271     -15.192  24.790  14.368  1.00 63.66           C  
ANISOU 2119  CB  ASN A 271     5485   8745   9957    683    -39  -1276       C  
ATOM   2120  CG  ASN A 271     -15.738  23.398  14.117  1.00 71.78           C  
ANISOU 2120  CG  ASN A 271     6421   9884  10968    510     -7  -1280       C  
ATOM   2121  OD1 ASN A 271     -16.192  23.083  13.016  1.00 78.66           O  
ANISOU 2121  OD1 ASN A 271     7240  10765  11883    519   -178  -1257       O  
ATOM   2122  ND2 ASN A 271     -15.701  22.555  15.145  1.00 80.29           N  
ANISOU 2122  ND2 ASN A 271     7486  11041  11979    345    207  -1308       N  
ATOM   2123  N   ALA A 272     -13.324  27.530  13.120  1.00 44.86           N  
ANISOU 2123  N   ALA A 272     3525   5986   7533   1023   -371  -1066       N  
ATOM   2124  CA  ALA A 272     -13.225  28.975  13.218  1.00 49.45           C  
ANISOU 2124  CA  ALA A 272     4139   6442   8209   1200   -452  -1086       C  
ATOM   2125  C   ALA A 272     -13.935  29.636  12.037  1.00 47.36           C  
ANISOU 2125  C   ALA A 272     3811   6116   8066   1352   -709  -1063       C  
ATOM   2126  O   ALA A 272     -13.915  29.116  10.920  1.00 49.50           O  
ANISOU 2126  O   ALA A 272     4139   6396   8272   1309   -847   -961       O  
ATOM   2127  CB  ALA A 272     -11.763  29.411  13.258  1.00 43.88           C  
ANISOU 2127  CB  ALA A 272     3706   5604   7364   1174   -435   -959       C  
ATOM   2128  N   PRO A 273     -14.582  30.776  12.262  1.00 50.15           N  
ANISOU 2128  N   PRO A 273     4050   6407   8598   1537   -785  -1161       N  
ATOM   2129  CA  PRO A 273     -15.301  31.443  11.174  1.00 51.13           C  
ANISOU 2129  CA  PRO A 273     4114   6462   8851   1698  -1051  -1138       C  
ATOM   2130  C   PRO A 273     -14.376  32.251  10.280  1.00 50.62           C  
ANISOU 2130  C   PRO A 273     4319   6210   8703   1754  -1224   -956       C  
ATOM   2131  O   PRO A 273     -13.349  32.779  10.711  1.00 51.73           O  
ANISOU 2131  O   PRO A 273     4645   6241   8768   1735  -1147   -897       O  
ATOM   2132  CB  PRO A 273     -16.283  32.368  11.909  1.00 53.45           C  
ANISOU 2132  CB  PRO A 273     4182   6750   9377   1881  -1047  -1328       C  
ATOM   2133  CG  PRO A 273     -16.208  31.978  13.364  1.00 52.81           C  
ANISOU 2133  CG  PRO A 273     4017   6778   9270   1784   -754  -1463       C  
ATOM   2134  CD  PRO A 273     -14.846  31.411  13.560  1.00 50.07           C  
ANISOU 2134  CD  PRO A 273     3928   6404   8691   1608   -630  -1323       C  
ATOM   2135  N   MET A 274     -14.766  32.344   9.012  1.00 60.34           N  
ANISOU 2135  N   MET A 274     5569   7411   9946   1815  -1464   -866       N  
ATOM   2136  CA  MET A 274     -14.079  33.218   8.074  1.00 62.32           C  
ANISOU 2136  CA  MET A 274     6062   7483  10133   1880  -1655   -691       C  
ATOM   2137  C   MET A 274     -14.350  34.679   8.421  1.00 60.24           C  
ANISOU 2137  C   MET A 274     5784   7051  10054   2083  -1752   -743       C  
ATOM   2138  O   MET A 274     -15.427  35.035   8.905  1.00 71.34           O  
ANISOU 2138  O   MET A 274     6951   8487  11668   2225  -1776   -912       O  
ATOM   2139  CB  MET A 274     -14.535  32.917   6.645  1.00 72.84           C  
ANISOU 2139  CB  MET A 274     7414   8839  11421   1895  -1895   -590       C  
ATOM   2140  CG  MET A 274     -13.956  33.828   5.574  1.00 85.74           C  
ANISOU 2140  CG  MET A 274     9300  10298  12979   1959  -2112   -397       C  
ATOM   2141  SD  MET A 274     -12.209  33.535   5.243  1.00 82.12           S  
ANISOU 2141  SD  MET A 274     9174   9792  12235   1763  -1991   -204       S  
ATOM   2142  CE  MET A 274     -11.875  34.841   4.063  1.00 85.61           C  
ANISOU 2142  CE  MET A 274     9862  10022  12644   1867  -2264      0       C  
ATOM   2143  N   ASP A 275     -13.354  35.528   8.179  1.00 61.43           N  
ANISOU 2143  N   ASP A 275     6187   7020  10132   2094  -1805   -603       N  
ATOM   2144  CA  ASP A 275     -13.495  36.954   8.433  1.00 69.02           C  
ANISOU 2144  CA  ASP A 275     7177   7784  11263   2279  -1916   -633       C  
ATOM   2145  C   ASP A 275     -12.662  37.727   7.421  1.00 76.87           C  
ANISOU 2145  C   ASP A 275     8465   8583  12159   2281  -2096   -407       C  
ATOM   2146  O   ASP A 275     -11.796  37.169   6.742  1.00 72.29           O  
ANISOU 2146  O   ASP A 275     8071   8035  11363   2120  -2076   -245       O  
ATOM   2147  CB  ASP A 275     -13.076  37.314   9.864  1.00 78.16           C  
ANISOU 2147  CB  ASP A 275     8311   8917  12471   2274  -1690   -768       C  
ATOM   2148  CG  ASP A 275     -13.570  38.684  10.287  1.00 91.63           C  
ANISOU 2148  CG  ASP A 275     9962  10447  14405   2493  -1794   -875       C  
ATOM   2149  OD1 ASP A 275     -14.724  38.781  10.753  1.00 86.42           O  
ANISOU 2149  OD1 ASP A 275     9040   9859  13938   2631  -1798  -1068       O  
ATOM   2150  OD2 ASP A 275     -12.808  39.663  10.144  1.00 99.35           O  
ANISOU 2150  OD2 ASP A 275    11157  11214  15377   2527  -1872   -771       O  
ATOM   2151  N   GLU A 276     -12.936  39.029   7.329  1.00 95.25           N  
ANISOU 2151  N   GLU A 276    10835  10706  14650   2462  -2272   -400       N  
ATOM   2152  CA  GLU A 276     -12.231  39.916   6.405  1.00101.84           C  
ANISOU 2152  CA  GLU A 276    11954  11327  15414   2472  -2458   -181       C  
ATOM   2153  C   GLU A 276     -10.897  40.368   7.008  1.00 98.86           C  
ANISOU 2153  C   GLU A 276    11782  10833  14946   2358  -2296   -121       C  
ATOM   2154  O   GLU A 276     -10.610  41.554   7.168  1.00114.09           O  
ANISOU 2154  O   GLU A 276    13834  12539  16976   2446  -2378    -90       O  
ATOM   2155  CB  GLU A 276     -13.114  41.104   6.041  1.00108.47           C  
ANISOU 2155  CB  GLU A 276    12760  11977  16478   2716  -2733   -193       C  
ATOM   2156  CG  GLU A 276     -13.814  41.749   7.231  1.00119.26           C  
ANISOU 2156  CG  GLU A 276    13913  13293  18107   2895  -2673   -436       C  
ATOM   2157  CD  GLU A 276     -14.768  42.856   6.819  1.00128.45           C  
ANISOU 2157  CD  GLU A 276    15058  14331  19417   3062  -2878   -451       C  
ATOM   2158  OE1 GLU A 276     -14.735  43.263   5.638  1.00133.20           O  
ANISOU 2158  OE1 GLU A 276    15840  14826  19943   3068  -3101   -254       O  
ATOM   2159  OE2 GLU A 276     -15.552  43.318   7.675  1.00123.53           O  
ANISOU 2159  OE2 GLU A 276    14248  13725  18965   3173  -2805   -660       O  
ATOM   2160  N   CYS A 277     -10.074  39.380   7.346  1.00 73.21           N  
ANISOU 2160  N   CYS A 277     8567   7735  11512   2159  -2070   -111       N  
ATOM   2161  CA  CYS A 277      -8.750  39.607   7.899  1.00 66.36           C  
ANISOU 2161  CA  CYS A 277     7876   6798  10541   2027  -1906    -58       C  
ATOM   2162  C   CYS A 277      -7.696  39.030   6.966  1.00 58.65           C  
ANISOU 2162  C   CYS A 277     7105   5865   9315   1836  -1888    144       C  
ATOM   2163  O   CYS A 277      -7.955  38.103   6.194  1.00 67.00           O  
ANISOU 2163  O   CYS A 277     8133   7068  10256   1775  -1921    195       O  
ATOM   2164  CB  CYS A 277      -8.615  38.985   9.294  1.00 65.21           C  
ANISOU 2164  CB  CYS A 277     7586   6790  10403   1966  -1641   -244       C  
ATOM   2165  SG  CYS A 277      -9.329  37.332   9.446  1.00 71.50           S  
ANISOU 2165  SG  CYS A 277     8156   7880  11130   1883  -1510   -349       S  
ATOM   2166  N   ASP A 278      -6.500  39.599   7.041  1.00 62.91           N  
ANISOU 2166  N   ASP A 278     7849   6278   9777   1741  -1833    250       N  
ATOM   2167  CA  ASP A 278      -5.365  39.142   6.256  1.00 62.28           C  
ANISOU 2167  CA  ASP A 278     7960   6239   9465   1553  -1785    427       C  
ATOM   2168  C   ASP A 278      -4.198  38.864   7.188  1.00 59.90           C  
ANISOU 2168  C   ASP A 278     7696   5974   9089   1413  -1552    382       C  
ATOM   2169  O   ASP A 278      -3.932  39.637   8.113  1.00 60.42           O  
ANISOU 2169  O   ASP A 278     7768   5920   9268   1453  -1500    305       O  
ATOM   2170  CB  ASP A 278      -4.958  40.173   5.198  1.00 67.47           C  
ANISOU 2170  CB  ASP A 278     8852   6701  10081   1551  -1972    637       C  
ATOM   2171  CG  ASP A 278      -3.972  39.615   4.196  1.00 74.02           C  
ANISOU 2171  CG  ASP A 278     9858   7610  10657   1361  -1933    815       C  
ATOM   2172  OD1 ASP A 278      -4.167  38.464   3.756  1.00 83.35           O  
ANISOU 2172  OD1 ASP A 278    10969   8987  11714   1301  -1893    801       O  
ATOM   2173  OD2 ASP A 278      -2.999  40.319   3.856  1.00 84.22           O  
ANISOU 2173  OD2 ASP A 278    11353   8770  11876   1266  -1937    961       O  
ATOM   2174  N   ALA A 279      -3.508  37.753   6.947  1.00 46.06           N  
ANISOU 2174  N   ALA A 279     5967   4385   7151   1254  -1422    423       N  
ATOM   2175  CA  ALA A 279      -2.382  37.366   7.781  1.00 48.30           C  
ANISOU 2175  CA  ALA A 279     6277   4717   7356   1123  -1215    383       C  
ATOM   2176  C   ALA A 279      -1.377  36.600   6.937  1.00 43.42           C  
ANISOU 2176  C   ALA A 279     5778   4196   6522    953  -1155    512       C  
ATOM   2177  O   ALA A 279      -1.672  36.157   5.825  1.00 46.76           O  
ANISOU 2177  O   ALA A 279     6235   4685   6845    935  -1248    601       O  
ATOM   2178  CB  ALA A 279      -2.832  36.527   8.981  1.00 47.34           C  
ANISOU 2178  CB  ALA A 279     5961   4739   7286   1140  -1060    192       C  
ATOM   2179  N   LYS A 280      -0.173  36.456   7.483  1.00 47.59           N  
ANISOU 2179  N   LYS A 280     6365   4737   6980    832  -1001    511       N  
ATOM   2180  CA  LYS A 280       0.874  35.658   6.866  1.00 52.09           C  
ANISOU 2180  CA  LYS A 280     7018   5415   7359    674   -912    597       C  
ATOM   2181  C   LYS A 280       0.953  34.251   7.440  1.00 44.49           C  
ANISOU 2181  C   LYS A 280     5932   4635   6336    623   -765    485       C  
ATOM   2182  O   LYS A 280       1.715  33.430   6.922  1.00 42.41           O  
ANISOU 2182  O   LYS A 280     5715   4475   5925    510   -694    532       O  
ATOM   2183  CB  LYS A 280       2.230  36.358   7.026  1.00 64.41           C  
ANISOU 2183  CB  LYS A 280     8713   6877   8883    565   -843    669       C  
ATOM   2184  CG  LYS A 280       2.242  37.790   6.506  1.00 88.17           C  
ANISOU 2184  CG  LYS A 280    11867   9679  11956    595   -984    792       C  
ATOM   2185  CD  LYS A 280       3.574  38.478   6.764  1.00 94.41           C  
ANISOU 2185  CD  LYS A 280    12775  10370  12727    471   -906    850       C  
ATOM   2186  CE  LYS A 280       3.562  39.913   6.256  1.00 88.77           C  
ANISOU 2186  CE  LYS A 280    12218   9427  12084    490  -1053    981       C  
ATOM   2187  NZ  LYS A 280       4.857  40.605   6.505  1.00 98.60           N  
ANISOU 2187  NZ  LYS A 280    13573  10570  13321    351   -976   1036       N  
ATOM   2188  N   CYS A 281       0.175  33.954   8.479  1.00 38.19           N  
ANISOU 2188  N   CYS A 281     4984   3879   5649    701   -718    338       N  
ATOM   2189  CA  CYS A 281       0.234  32.681   9.184  1.00 36.04           C  
ANISOU 2189  CA  CYS A 281     4607   3757   5331    648   -578    237       C  
ATOM   2190  C   CYS A 281      -1.166  32.283   9.627  1.00 35.70           C  
ANISOU 2190  C   CYS A 281     4394   3780   5391    743   -597    119       C  
ATOM   2191  O   CYS A 281      -1.851  33.060  10.299  1.00 39.95           O  
ANISOU 2191  O   CYS A 281     4860   4248   6071    850   -624     38       O  
ATOM   2192  CB  CYS A 281       1.161  32.771  10.402  1.00 43.96           C  
ANISOU 2192  CB  CYS A 281     5620   4741   6340    596   -439    172       C  
ATOM   2193  SG  CYS A 281       1.081  31.327  11.475  1.00 49.08           S  
ANISOU 2193  SG  CYS A 281     6149   5549   6950    548   -285     48       S  
ATOM   2194  N   GLN A 282      -1.579  31.070   9.265  1.00 35.15           N  
ANISOU 2194  N   GLN A 282     4253   3845   5256    701   -579    100       N  
ATOM   2195  CA  GLN A 282      -2.907  30.565   9.582  1.00 35.68           C  
ANISOU 2195  CA  GLN A 282     4148   3994   5416    765   -592     -8       C  
ATOM   2196  C   GLN A 282      -2.807  29.193  10.235  1.00 34.34           C  
ANISOU 2196  C   GLN A 282     3907   3956   5185    670   -447    -80       C  
ATOM   2197  O   GLN A 282      -2.072  28.320   9.762  1.00 33.32           O  
ANISOU 2197  O   GLN A 282     3851   3881   4928    572   -410    -27       O  
ATOM   2198  CB  GLN A 282      -3.783  30.472   8.326  1.00 36.90           C  
ANISOU 2198  CB  GLN A 282     4277   4172   5572    814   -758     43       C  
ATOM   2199  CG  GLN A 282      -5.218  30.052   8.601  1.00 37.78           C  
ANISOU 2199  CG  GLN A 282     4186   4366   5803    883   -787    -75       C  
ATOM   2200  CD  GLN A 282      -6.012  31.128   9.316  1.00 39.16           C  
ANISOU 2200  CD  GLN A 282     4256   4463   6160   1024   -823   -164       C  
ATOM   2201  OE1 GLN A 282      -5.914  32.307   8.984  1.00 40.22           O  
ANISOU 2201  OE1 GLN A 282     4472   4459   6351   1112   -938   -105       O  
ATOM   2202  NE2 GLN A 282      -6.795  30.727  10.309  1.00 44.93           N  
ANISOU 2202  NE2 GLN A 282     4808   5280   6984   1043   -722   -310       N  
ATOM   2203  N   THR A 283      -3.546  29.010  11.323  1.00 34.53           N  
ANISOU 2203  N   THR A 283     3793   4026   5299    700   -366   -203       N  
ATOM   2204  CA  THR A 283      -3.643  27.749  12.035  1.00 33.63           C  
ANISOU 2204  CA  THR A 283     3609   4028   5141    610   -235   -269       C  
ATOM   2205  C   THR A 283      -5.117  27.389  12.210  1.00 34.77           C  
ANISOU 2205  C   THR A 283     3564   4255   5391    651   -247   -368       C  
ATOM   2206  O   THR A 283      -5.984  28.259  12.118  1.00 36.20           O  
ANISOU 2206  O   THR A 283     3654   4402   5698    767   -331   -414       O  
ATOM   2207  CB  THR A 283      -2.959  27.820  13.410  1.00 32.84           C  
ANISOU 2207  CB  THR A 283     3536   3918   5021    574    -89   -323       C  
ATOM   2208  OG1 THR A 283      -3.801  28.518  14.336  1.00 33.92           O  
ANISOU 2208  OG1 THR A 283     3560   4049   5278    658    -53   -436       O  
ATOM   2209  CG2 THR A 283      -1.619  28.533  13.309  1.00 32.17           C  
ANISOU 2209  CG2 THR A 283     3610   3735   4879    558    -96   -244       C  
ATOM   2210  N   PRO A 284      -5.421  26.110  12.449  1.00 34.32           N  
ANISOU 2210  N   PRO A 284     3441   4304   5294    555   -168   -405       N  
ATOM   2211  CA  PRO A 284      -6.828  25.737  12.693  1.00 35.56           C  
ANISOU 2211  CA  PRO A 284     3401   4552   5558    571   -160   -507       C  
ATOM   2212  C   PRO A 284      -7.465  26.477  13.855  1.00 36.54           C  
ANISOU 2212  C   PRO A 284     3404   4685   5796    643    -77   -626       C  
ATOM   2213  O   PRO A 284      -8.688  26.663  13.863  1.00 48.55           O  
ANISOU 2213  O   PRO A 284     4744   6258   7444    709   -110   -717       O  
ATOM   2214  CB  PRO A 284      -6.743  24.229  12.965  1.00 34.75           C  
ANISOU 2214  CB  PRO A 284     3292   4538   5374    425    -59   -513       C  
ATOM   2215  CG  PRO A 284      -5.522  23.789  12.254  1.00 33.40           C  
ANISOU 2215  CG  PRO A 284     3300   4322   5068    366    -91   -405       C  
ATOM   2216  CD  PRO A 284      -4.550  24.929  12.339  1.00 32.92           C  
ANISOU 2216  CD  PRO A 284     3363   4163   4984    429   -104   -352       C  
ATOM   2217  N   GLN A 285      -6.675  26.900  14.844  1.00 38.28           N  
ANISOU 2217  N   GLN A 285     3709   4863   5974    635     30   -639       N  
ATOM   2218  CA  GLN A 285      -7.225  27.699  15.933  1.00 38.88           C  
ANISOU 2218  CA  GLN A 285     3683   4943   6147    712    109   -765       C  
ATOM   2219  C   GLN A 285      -7.492  29.131  15.497  1.00 38.14           C  
ANISOU 2219  C   GLN A 285     3578   4735   6178    876    -25   -780       C  
ATOM   2220  O   GLN A 285      -8.414  29.773  16.009  1.00 39.70           O  
ANISOU 2220  O   GLN A 285     3629   4946   6509    978    -12   -907       O  
ATOM   2221  CB  GLN A 285      -6.275  27.682  17.130  1.00 43.63           C  
ANISOU 2221  CB  GLN A 285     4392   5536   6651    647    253   -779       C  
ATOM   2222  CG  GLN A 285      -6.072  26.314  17.739  1.00 41.95           C  
ANISOU 2222  CG  GLN A 285     4194   5424   6322    495    384   -769       C  
ATOM   2223  CD  GLN A 285      -7.318  25.793  18.422  1.00 48.40           C  
ANISOU 2223  CD  GLN A 285     4828   6369   7194    459    491   -882       C  
ATOM   2224  OE1 GLN A 285      -7.988  26.520  19.154  1.00 51.41           O  
ANISOU 2224  OE1 GLN A 285     5096   6779   7658    532    553  -1004       O  
ATOM   2225  NE2 GLN A 285      -7.639  24.527  18.180  1.00 59.35           N  
ANISOU 2225  NE2 GLN A 285     6179   7832   8539    341    519   -849       N  
ATOM   2226  N   GLY A 286      -6.705  29.644  14.566  1.00 37.61           N  
ANISOU 2226  N   GLY A 286     3665   4555   6072    900   -151   -656       N  
ATOM   2227  CA  GLY A 286      -6.851  31.014  14.125  1.00 38.83           C  
ANISOU 2227  CA  GLY A 286     3845   4573   6336   1043   -290   -645       C  
ATOM   2228  C   GLY A 286      -5.575  31.501  13.476  1.00 37.91           C  
ANISOU 2228  C   GLY A 286     3945   4333   6127   1012   -359   -498       C  
ATOM   2229  O   GLY A 286      -4.576  30.787  13.392  1.00 36.35           O  
ANISOU 2229  O   GLY A 286     3859   4165   5787    888   -293   -420       O  
ATOM   2230  N   ALA A 287      -5.637  32.744  13.009  1.00 39.11           N  
ANISOU 2230  N   ALA A 287     4151   4341   6370   1126   -496   -463       N  
ATOM   2231  CA  ALA A 287      -4.490  33.360  12.362  1.00 38.65           C  
ANISOU 2231  CA  ALA A 287     4295   4153   6236   1090   -564   -319       C  
ATOM   2232  C   ALA A 287      -3.527  33.920  13.401  1.00 38.03           C  
ANISOU 2232  C   ALA A 287     4302   4002   6145   1059   -456   -356       C  
ATOM   2233  O   ALA A 287      -3.932  34.388  14.469  1.00 38.69           O  
ANISOU 2233  O   ALA A 287     4304   4072   6324   1127   -391   -493       O  
ATOM   2234  CB  ALA A 287      -4.937  34.469  11.411  1.00 40.42           C  
ANISOU 2234  CB  ALA A 287     4563   4235   6558   1213   -768   -247       C  
ATOM   2235  N   ILE A 288      -2.239  33.865  13.077  1.00 36.89           N  
ANISOU 2235  N   ILE A 288     4317   3819   5881    952   -436   -241       N  
ATOM   2236  CA  ILE A 288      -1.178  34.348  13.952  1.00 36.29           C  
ANISOU 2236  CA  ILE A 288     4331   3676   5783    903   -349   -264       C  
ATOM   2237  C   ILE A 288      -0.536  35.562  13.299  1.00 39.62           C  
ANISOU 2237  C   ILE A 288     4900   3917   6236    918   -462   -156       C  
ATOM   2238  O   ILE A 288      -0.147  35.513  12.126  1.00 49.14           O  
ANISOU 2238  O   ILE A 288     6202   5100   7367    867   -541    -11       O  
ATOM   2239  CB  ILE A 288      -0.136  33.253  14.237  1.00 34.44           C  
ANISOU 2239  CB  ILE A 288     4143   3549   5395    757   -224   -233       C  
ATOM   2240  CG1 ILE A 288      -0.772  32.106  15.023  1.00 33.85           C  
ANISOU 2240  CG1 ILE A 288     3940   3629   5293    734   -111   -336       C  
ATOM   2241  CG2 ILE A 288       1.057  33.826  14.991  1.00 34.00           C  
ANISOU 2241  CG2 ILE A 288     4186   3417   5316    704   -164   -243       C  
ATOM   2242  CD1 ILE A 288       0.198  31.017  15.409  1.00 32.26           C  
ANISOU 2242  CD1 ILE A 288     3787   3515   4954    607     -3   -313       C  
ATOM   2243  N   ASN A 289      -0.437  36.649  14.056  1.00 38.02           N  
ANISOU 2243  N   ASN A 289     4722   3585   6139    981   -467   -229       N  
ATOM   2244  CA  ASN A 289       0.193  37.893  13.624  1.00 39.03           C  
ANISOU 2244  CA  ASN A 289     4997   3515   6317    986   -568   -138       C  
ATOM   2245  C   ASN A 289       1.339  38.154  14.599  1.00 38.30           C  
ANISOU 2245  C   ASN A 289     4970   3387   6193    900   -462   -187       C  
ATOM   2246  O   ASN A 289       1.151  38.764  15.654  1.00 38.95           O  
ANISOU 2246  O   ASN A 289     5019   3411   6368    966   -430   -325       O  
ATOM   2247  CB  ASN A 289      -0.833  39.027  13.586  1.00 41.16           C  
ANISOU 2247  CB  ASN A 289     5234   3634   6772   1158   -703   -193       C  
ATOM   2248  CG  ASN A 289      -0.201  40.400  13.602  1.00 50.00           C  
ANISOU 2248  CG  ASN A 289     6500   4524   7974   1170   -783   -149       C  
ATOM   2249  OD1 ASN A 289       0.515  40.784  12.676  1.00 49.82           O  
ANISOU 2249  OD1 ASN A 289     6628   4403   7896   1089   -859     21       O  
ATOM   2250  ND2 ASN A 289      -0.476  41.157  14.656  1.00 49.80           N  
ANISOU 2250  ND2 ASN A 289     6432   4409   8080   1264   -764   -308       N  
ATOM   2251  N   SER A 290       2.529  37.671  14.251  1.00 37.07           N  
ANISOU 2251  N   SER A 290     4902   3277   5906    754   -409    -85       N  
ATOM   2252  CA  SER A 290       3.652  37.709  15.176  1.00 36.28           C  
ANISOU 2252  CA  SER A 290     4842   3177   5764    663   -309   -135       C  
ATOM   2253  C   SER A 290       4.953  37.646  14.394  1.00 36.48           C  
ANISOU 2253  C   SER A 290     4981   3189   5691    519   -305     10       C  
ATOM   2254  O   SER A 290       4.993  37.186  13.250  1.00 41.98           O  
ANISOU 2254  O   SER A 290     5708   3936   6308    476   -338    132       O  
ATOM   2255  CB  SER A 290       3.573  36.556  16.185  1.00 35.97           C  
ANISOU 2255  CB  SER A 290     4700   3316   5650    639   -176   -249       C  
ATOM   2256  OG  SER A 290       4.699  36.531  17.044  1.00 34.26           O  
ANISOU 2256  OG  SER A 290     4527   3107   5381    552    -98   -290       O  
ATOM   2257  N   SER A 291       6.020  38.127  15.030  1.00 45.17           N  
ANISOU 2257  N   SER A 291     6139   4229   6796    442   -263    -16       N  
ATOM   2258  CA  SER A 291       7.374  37.977  14.513  1.00 48.62           C  
ANISOU 2258  CA  SER A 291     6650   4682   7142    292   -228     88       C  
ATOM   2259  C   SER A 291       8.261  37.196  15.473  1.00 40.51           C  
ANISOU 2259  C   SER A 291     5575   3774   6044    219   -116      4       C  
ATOM   2260  O   SER A 291       9.489  37.212  15.324  1.00 42.25           O  
ANISOU 2260  O   SER A 291     5836   3998   6218    101    -84     52       O  
ATOM   2261  CB  SER A 291       7.990  39.346  14.211  1.00 58.43           C  
ANISOU 2261  CB  SER A 291     8013   5726   8462    242   -299    160       C  
ATOM   2262  OG  SER A 291       7.927  40.195  15.342  1.00 72.36           O  
ANISOU 2262  OG  SER A 291     9778   7374  10341    296   -310     32       O  
ATOM   2263  N   LEU A 292       7.670  36.513  16.452  1.00 34.04           N  
ANISOU 2263  N   LEU A 292     4667   3054   5214    283    -60   -119       N  
ATOM   2264  CA  LEU A 292       8.399  35.722  17.427  1.00 32.04           C  
ANISOU 2264  CA  LEU A 292     4378   2911   4886    227     28   -195       C  
ATOM   2265  C   LEU A 292       8.808  34.376  16.830  1.00 30.77           C  
ANISOU 2265  C   LEU A 292     4187   2898   4608    162     76   -127       C  
ATOM   2266  O   LEU A 292       8.145  33.862  15.926  1.00 30.60           O  
ANISOU 2266  O   LEU A 292     4146   2923   4558    187     57    -64       O  
ATOM   2267  CB  LEU A 292       7.547  35.501  18.673  1.00 32.05           C  
ANISOU 2267  CB  LEU A 292     4312   2963   4904    311     73   -340       C  
ATOM   2268  CG  LEU A 292       7.189  36.767  19.454  1.00 33.41           C  
ANISOU 2268  CG  LEU A 292     4504   3002   5188    383     40   -448       C  
ATOM   2269  CD1 LEU A 292       6.341  36.435  20.672  1.00 36.28           C  
ANISOU 2269  CD1 LEU A 292     4793   3450   5542    456    108   -600       C  
ATOM   2270  CD2 LEU A 292       8.449  37.517  19.860  1.00 36.06           C  
ANISOU 2270  CD2 LEU A 292     4916   3244   5541    301     25   -459       C  
ATOM   2271  N   PRO A 293       9.906  33.788  17.314  1.00 30.02           N  
ANISOU 2271  N   PRO A 293     4087   2871   4448     85    129   -147       N  
ATOM   2272  CA  PRO A 293      10.387  32.535  16.715  1.00 29.01           C  
ANISOU 2272  CA  PRO A 293     3933   2868   4223     31    167    -93       C  
ATOM   2273  C   PRO A 293       9.618  31.295  17.142  1.00 28.20           C  
ANISOU 2273  C   PRO A 293     3770   2877   4066     76    206   -140       C  
ATOM   2274  O   PRO A 293       9.741  30.261  16.474  1.00 37.54           O  
ANISOU 2274  O   PRO A 293     4934   4144   5183     50    223    -95       O  
ATOM   2275  CB  PRO A 293      11.847  32.465  17.184  1.00 28.79           C  
ANISOU 2275  CB  PRO A 293     3912   2858   4171    -54    195   -113       C  
ATOM   2276  CG  PRO A 293      11.847  33.198  18.479  1.00 29.29           C  
ANISOU 2276  CG  PRO A 293     3985   2856   4286    -28    186   -214       C  
ATOM   2277  CD  PRO A 293      10.834  34.302  18.338  1.00 30.27           C  
ANISOU 2277  CD  PRO A 293     4138   2861   4500     42    140   -220       C  
ATOM   2278  N   PHE A 294       8.829  31.355  18.212  1.00 28.37           N  
ANISOU 2278  N   PHE A 294     3763   2904   4113    136    225   -232       N  
ATOM   2279  CA  PHE A 294       8.133  30.184  18.723  1.00 27.80           C  
ANISOU 2279  CA  PHE A 294     3640   2938   3986    155    273   -273       C  
ATOM   2280  C   PHE A 294       6.657  30.497  18.931  1.00 28.47           C  
ANISOU 2280  C   PHE A 294     3672   3017   4129    237    275   -327       C  
ATOM   2281  O   PHE A 294       6.263  31.649  19.118  1.00 29.41           O  
ANISOU 2281  O   PHE A 294     3795   3046   4333    294    244   -369       O  
ATOM   2282  CB  PHE A 294       8.751  29.695  20.041  1.00 27.50           C  
ANISOU 2282  CB  PHE A 294     3612   2948   3887    125    318   -342       C  
ATOM   2283  CG  PHE A 294      10.212  29.358  19.940  1.00 27.02           C  
ANISOU 2283  CG  PHE A 294     3581   2899   3785     56    307   -307       C  
ATOM   2284  CD1 PHE A 294      10.627  28.220  19.273  1.00 26.30           C  
ANISOU 2284  CD1 PHE A 294     3478   2876   3640     24    314   -251       C  
ATOM   2285  CD2 PHE A 294      11.168  30.174  20.520  1.00 39.49           C  
ANISOU 2285  CD2 PHE A 294     5192   4424   5387     27    288   -344       C  
ATOM   2286  CE1 PHE A 294      11.965  27.904  19.181  1.00 26.05           C  
ANISOU 2286  CE1 PHE A 294     3453   2863   3584    -27    305   -236       C  
ATOM   2287  CE2 PHE A 294      12.511  29.865  20.430  1.00 27.17           C  
ANISOU 2287  CE2 PHE A 294     3636   2885   3803    -35    275   -323       C  
ATOM   2288  CZ  PHE A 294      12.910  28.730  19.760  1.00 31.92           C  
ANISOU 2288  CZ  PHE A 294     4212   3559   4355    -57    286   -271       C  
ATOM   2289  N   GLN A 295       5.840  29.446  18.897  1.00 28.13           N  
ANISOU 2289  N   GLN A 295     3572   3067   4051    243    308   -332       N  
ATOM   2290  CA  GLN A 295       4.413  29.560  19.163  1.00 28.86           C  
ANISOU 2290  CA  GLN A 295     3585   3183   4199    310    324   -397       C  
ATOM   2291  C   GLN A 295       3.905  28.242  19.727  1.00 28.47           C  
ANISOU 2291  C   GLN A 295     3489   3250   4080    271    398   -425       C  
ATOM   2292  O   GLN A 295       4.387  27.175  19.343  1.00 27.65           O  
ANISOU 2292  O   GLN A 295     3408   3192   3906    211    402   -364       O  
ATOM   2293  CB  GLN A 295       3.631  29.939  17.896  1.00 32.13           C  
ANISOU 2293  CB  GLN A 295     3965   3559   4684    365    245   -343       C  
ATOM   2294  CG  GLN A 295       3.843  29.005  16.710  1.00 30.55           C  
ANISOU 2294  CG  GLN A 295     3778   3408   4423    315    215   -245       C  
ATOM   2295  CD  GLN A 295       2.755  27.951  16.571  1.00 32.50           C  
ANISOU 2295  CD  GLN A 295     3938   3750   4661    317    235   -267       C  
ATOM   2296  OE1 GLN A 295       1.841  27.865  17.390  1.00 33.05           O  
ANISOU 2296  OE1 GLN A 295     3929   3862   4767    345    284   -351       O  
ATOM   2297  NE2 GLN A 295       2.851  27.145  15.522  1.00 37.46           N  
ANISOU 2297  NE2 GLN A 295     4577   4418   5239    279    200   -198       N  
ATOM   2298  N   ASN A 296       2.944  28.321  20.649  1.00 29.24           N  
ANISOU 2298  N   ASN A 296     3521   3391   4196    302    461   -520       N  
ATOM   2299  CA  ASN A 296       2.295  27.139  21.206  1.00 29.21           C  
ANISOU 2299  CA  ASN A 296     3469   3496   4131    251    540   -543       C  
ATOM   2300  C   ASN A 296       0.809  27.095  20.863  1.00 30.07           C  
ANISOU 2300  C   ASN A 296     3452   3652   4320    295    551   -586       C  
ATOM   2301  O   ASN A 296       0.017  26.470  21.573  1.00 44.68           O  
ANISOU 2301  O   ASN A 296     5237   5593   6145    260    639   -642       O  
ATOM   2302  CB  ASN A 296       2.500  27.064  22.719  1.00 29.56           C  
ANISOU 2302  CB  ASN A 296     3548   3585   4098    218    628   -618       C  
ATOM   2303  CG  ASN A 296       1.942  28.266  23.460  1.00 30.76           C  
ANISOU 2303  CG  ASN A 296     3661   3716   4312    292    660   -739       C  
ATOM   2304  OD1 ASN A 296       1.217  29.085  22.900  1.00 36.34           O  
ANISOU 2304  OD1 ASN A 296     4297   4377   5136    377    620   -774       O  
ATOM   2305  ND2 ASN A 296       2.278  28.370  24.740  1.00 31.17           N  
ANISOU 2305  ND2 ASN A 296     3762   3800   4282    265    725   -811       N  
ATOM   2306  N   VAL A 297       0.422  27.757  19.774  1.00 30.39           N  
ANISOU 2306  N   VAL A 297     3456   3634   4455    366    459   -559       N  
ATOM   2307  CA  VAL A 297      -0.984  27.821  19.397  1.00 31.41           C  
ANISOU 2307  CA  VAL A 297     3452   3803   4679    424    445   -608       C  
ATOM   2308  C   VAL A 297      -1.438  26.511  18.767  1.00 33.46           C  
ANISOU 2308  C   VAL A 297     3666   4144   4903    354    444   -557       C  
ATOM   2309  O   VAL A 297      -2.411  25.898  19.217  1.00 42.83           O  
ANISOU 2309  O   VAL A 297     4748   5422   6104    325    514   -617       O  
ATOM   2310  CB  VAL A 297      -1.224  29.014  18.456  1.00 32.11           C  
ANISOU 2310  CB  VAL A 297     3531   3788   4880    531    322   -588       C  
ATOM   2311  CG1 VAL A 297      -2.677  29.071  18.018  1.00 33.32           C  
ANISOU 2311  CG1 VAL A 297     3535   3984   5143    604    283   -641       C  
ATOM   2312  CG2 VAL A 297      -0.807  30.312  19.132  1.00 32.69           C  
ANISOU 2312  CG2 VAL A 297     3655   3764   5003    596    320   -648       C  
ATOM   2313  N   HIS A 298      -0.748  26.061  17.721  1.00 30.10           N  
ANISOU 2313  N   HIS A 298     3316   3690   4432    320    371   -454       N  
ATOM   2314  CA  HIS A 298      -1.133  24.838  17.025  1.00 29.83           C  
ANISOU 2314  CA  HIS A 298     3249   3718   4367    258    356   -415       C  
ATOM   2315  C   HIS A 298       0.004  24.350  16.134  1.00 28.76           C  
ANISOU 2315  C   HIS A 298     3226   3549   4151    214    303   -318       C  
ATOM   2316  O   HIS A 298       0.714  25.163  15.532  1.00 28.57           O  
ANISOU 2316  O   HIS A 298     3272   3458   4127    250    241   -269       O  
ATOM   2317  CB  HIS A 298      -2.397  25.068  16.193  1.00 30.88           C  
ANISOU 2317  CB  HIS A 298     3261   3873   4599    319    279   -438       C  
ATOM   2318  CG  HIS A 298      -3.180  23.821  15.924  1.00 34.72           C  
ANISOU 2318  CG  HIS A 298     3667   4445   5079    247    294   -448       C  
ATOM   2319  ND1 HIS A 298      -2.870  22.953  14.900  1.00 34.26           N  
ANISOU 2319  ND1 HIS A 298     3659   4392   4966    195    231   -380       N  
ATOM   2320  CD2 HIS A 298      -4.266  23.300  16.543  1.00 33.66           C  
ANISOU 2320  CD2 HIS A 298     3403   4395   4990    211    368   -525       C  
ATOM   2321  CE1 HIS A 298      -3.728  21.949  14.902  1.00 32.83           C  
ANISOU 2321  CE1 HIS A 298     3389   4282   4802    131    255   -414       C  
ATOM   2322  NE2 HIS A 298      -4.585  22.136  15.888  1.00 34.46           N  
ANISOU 2322  NE2 HIS A 298     3483   4540   5070    133    341   -496       N  
ATOM   2323  N   PRO A 299       0.211  23.033  16.025  1.00 37.18           N  
ANISOU 2323  N   PRO A 299     4315   4660   5151    133    328   -294       N  
ATOM   2324  CA  PRO A 299       1.278  22.527  15.142  1.00 27.37           C  
ANISOU 2324  CA  PRO A 299     3167   3394   3838    100    283   -224       C  
ATOM   2325  C   PRO A 299       0.955  22.598  13.661  1.00 27.67           C  
ANISOU 2325  C   PRO A 299     3195   3433   3884    125    185   -184       C  
ATOM   2326  O   PRO A 299       1.888  22.624  12.849  1.00 33.18           O  
ANISOU 2326  O   PRO A 299     3974   4109   4523    115    149   -130       O  
ATOM   2327  CB  PRO A 299       1.444  21.069  15.593  1.00 26.97           C  
ANISOU 2327  CB  PRO A 299     3137   3380   3732     17    335   -228       C  
ATOM   2328  CG  PRO A 299       0.144  20.716  16.214  1.00 27.77           C  
ANISOU 2328  CG  PRO A 299     3138   3533   3880     -8    384   -281       C  
ATOM   2329  CD  PRO A 299      -0.379  21.966  16.854  1.00 28.41           C  
ANISOU 2329  CD  PRO A 299     3158   3613   4023     60    410   -333       C  
ATOM   2330  N   VAL A 300      -0.318  22.610  13.284  1.00 33.49           N  
ANISOU 2330  N   VAL A 300     3835   4205   4686    152    140   -213       N  
ATOM   2331  CA  VAL A 300      -0.704  22.732  11.883  1.00 31.44           C  
ANISOU 2331  CA  VAL A 300     3571   3949   4427    180     27   -176       C  
ATOM   2332  C   VAL A 300      -0.637  24.201  11.492  1.00 32.15           C  
ANISOU 2332  C   VAL A 300     3688   3972   4555    265    -44   -137       C  
ATOM   2333  O   VAL A 300      -1.332  25.041  12.073  1.00 42.52           O  
ANISOU 2333  O   VAL A 300     4930   5261   5964    333    -47   -182       O  
ATOM   2334  CB  VAL A 300      -2.106  22.155  11.643  1.00 30.45           C  
ANISOU 2334  CB  VAL A 300     3319   3887   4365    175     -9   -227       C  
ATOM   2335  CG1 VAL A 300      -2.523  22.358  10.199  1.00 30.66           C  
ANISOU 2335  CG1 VAL A 300     3347   3920   4384    212   -148   -190       C  
ATOM   2336  CG2 VAL A 300      -2.128  20.681  11.999  1.00 29.55           C  
ANISOU 2336  CG2 VAL A 300     3197   3818   4213     75     57   -254       C  
ATOM   2337  N   THR A 301       0.209  24.515  10.516  1.00 30.23           N  
ANISOU 2337  N   THR A 301     3550   3696   4239    257    -98    -58       N  
ATOM   2338  CA  THR A 301       0.451  25.887  10.103  1.00 34.65           C  
ANISOU 2338  CA  THR A 301     4169   4175   4822    315   -166      2       C  
ATOM   2339  C   THR A 301       0.374  25.993   8.587  1.00 36.71           C  
ANISOU 2339  C   THR A 301     4489   4441   5018    318   -280     82       C  
ATOM   2340  O   THR A 301       0.634  25.029   7.863  1.00 43.77           O  
ANISOU 2340  O   THR A 301     5412   5400   5818    259   -281     94       O  
ATOM   2341  CB  THR A 301       1.822  26.390  10.588  1.00 39.42           C  
ANISOU 2341  CB  THR A 301     4868   4722   5387    281    -97     33       C  
ATOM   2342  OG1 THR A 301       2.859  25.539  10.083  1.00 51.78           O  
ANISOU 2342  OG1 THR A 301     6500   6333   6841    202    -58     66       O  
ATOM   2343  CG2 THR A 301       1.879  26.407  12.109  1.00 31.77           C  
ANISOU 2343  CG2 THR A 301     3854   3747   4470    284      0    -47       C  
ATOM   2344  N   ILE A 302       0.008  27.182   8.119  1.00 31.81           N  
ANISOU 2344  N   ILE A 302     3895   3746   4445    388   -383    135       N  
ATOM   2345  CA  ILE A 302      -0.043  27.497   6.697  1.00 32.76           C  
ANISOU 2345  CA  ILE A 302     4099   3858   4491    393   -507    231       C  
ATOM   2346  C   ILE A 302       0.509  28.903   6.515  1.00 33.46           C  
ANISOU 2346  C   ILE A 302     4295   3825   4592    418   -552    323       C  
ATOM   2347  O   ILE A 302       0.125  29.824   7.243  1.00 33.96           O  
ANISOU 2347  O   ILE A 302     4322   3799   4781    494   -571    294       O  
ATOM   2348  CB  ILE A 302      -1.475  27.385   6.133  1.00 45.92           C  
ANISOU 2348  CB  ILE A 302     5673   5558   6217    464   -640    207       C  
ATOM   2349  CG1 ILE A 302      -1.893  25.916   6.039  1.00 44.06           C  
ANISOU 2349  CG1 ILE A 302     5356   5440   5944    407   -605    133       C  
ATOM   2350  CG2 ILE A 302      -1.581  28.066   4.777  1.00 35.34           C  
ANISOU 2350  CG2 ILE A 302     4438   4181   4810    490   -797    321       C  
ATOM   2351  CD1 ILE A 302      -3.313  25.716   5.589  1.00 53.16           C  
ANISOU 2351  CD1 ILE A 302     6392   6638   7170    464   -729     90       C  
ATOM   2352  N   GLY A 303       1.421  29.064   5.561  1.00 35.95           N  
ANISOU 2352  N   GLY A 303     4744   4136   4778    348   -563    427       N  
ATOM   2353  CA  GLY A 303       2.059  30.345   5.338  1.00 42.52           C  
ANISOU 2353  CA  GLY A 303     5695   4850   5611    340   -596    528       C  
ATOM   2354  C   GLY A 303       3.428  30.434   5.979  1.00 43.42           C  
ANISOU 2354  C   GLY A 303     5854   4947   5698    255   -458    525       C  
ATOM   2355  O   GLY A 303       4.194  29.466   5.963  1.00 43.30           O  
ANISOU 2355  O   GLY A 303     5832   5028   5592    177   -357    494       O  
ATOM   2356  N   GLU A 304       3.747  31.590   6.547  1.00 51.86           N  
ANISOU 2356  N   GLU A 304     6963   5888   6853    273   -462    547       N  
ATOM   2357  CA  GLU A 304       5.024  31.825   7.216  1.00 50.63           C  
ANISOU 2357  CA  GLU A 304     6841   5705   6691    194   -348    538       C  
ATOM   2358  C   GLU A 304       4.726  32.001   8.701  1.00 48.64           C  
ANISOU 2358  C   GLU A 304     6498   5412   6571    258   -302    419       C  
ATOM   2359  O   GLU A 304       4.273  33.066   9.131  1.00 54.97           O  
ANISOU 2359  O   GLU A 304     7306   6091   7488    331   -362    409       O  
ATOM   2360  CB  GLU A 304       5.728  33.039   6.619  1.00 60.73           C  
ANISOU 2360  CB  GLU A 304     8257   6867   7951    138   -390    664       C  
ATOM   2361  CG  GLU A 304       5.764  33.024   5.098  1.00 66.87           C  
ANISOU 2361  CG  GLU A 304     9139   7679   8589     85   -456    794       C  
ATOM   2362  CD  GLU A 304       6.557  34.175   4.516  1.00 70.91           C  
ANISOU 2362  CD  GLU A 304     9798   8079   9064     -1   -479    933       C  
ATOM   2363  OE1 GLU A 304       7.803  34.102   4.525  1.00 70.37           O  
ANISOU 2363  OE1 GLU A 304     9759   8047   8930   -122   -363    948       O  
ATOM   2364  OE2 GLU A 304       5.933  35.154   4.057  1.00 77.62           O  
ANISOU 2364  OE2 GLU A 304    10733   8801   9957     51   -616   1027       O  
ATOM   2365  N   CYS A 305       4.976  30.954   9.477  1.00 31.21           N  
ANISOU 2365  N   CYS A 305     4213   3304   4343    233   -198    326       N  
ATOM   2366  CA  CYS A 305       4.580  30.875  10.872  1.00 30.72           C  
ANISOU 2366  CA  CYS A 305     4063   3238   4370    285   -145    208       C  
ATOM   2367  C   CYS A 305       5.792  30.703  11.778  1.00 29.81           C  
ANISOU 2367  C   CYS A 305     3963   3133   4230    216    -43    168       C  
ATOM   2368  O   CYS A 305       6.879  30.334  11.319  1.00 38.52           O  
ANISOU 2368  O   CYS A 305     5112   4275   5249    130     -2    214       O  
ATOM   2369  CB  CYS A 305       3.616  29.701  11.099  1.00 34.41           C  
ANISOU 2369  CB  CYS A 305     4423   3815   4834    315   -124    134       C  
ATOM   2370  SG  CYS A 305       1.973  29.879  10.376  1.00 44.48           S  
ANISOU 2370  SG  CYS A 305     5630   5092   6179    414   -249    136       S  
ATOM   2371  N   PRO A 306       5.640  30.969  13.072  1.00 34.48           N  
ANISOU 2371  N   PRO A 306     4511   3697   4892    253     -2     74       N  
ATOM   2372  CA  PRO A 306       6.673  30.569  14.030  1.00 28.81           C  
ANISOU 2372  CA  PRO A 306     3796   3012   4138    193     84     23       C  
ATOM   2373  C   PRO A 306       6.694  29.060  14.217  1.00 28.49           C  
ANISOU 2373  C   PRO A 306     3708   3096   4023    163    143     -8       C  
ATOM   2374  O   PRO A 306       5.745  28.347  13.887  1.00 45.68           O  
ANISOU 2374  O   PRO A 306     5835   5331   6191    190    131    -16       O  
ATOM   2375  CB  PRO A 306       6.260  31.281  15.324  1.00 31.50           C  
ANISOU 2375  CB  PRO A 306     4110   3296   4564    252    100    -76       C  
ATOM   2376  CG  PRO A 306       5.338  32.364  14.896  1.00 30.46           C  
ANISOU 2376  CG  PRO A 306     3981   3063   4530    336     15    -63       C  
ATOM   2377  CD  PRO A 306       4.625  31.837  13.692  1.00 30.58           C  
ANISOU 2377  CD  PRO A 306     3977   3128   4516    352    -41      8       C  
ATOM   2378  N   LYS A 307       7.805  28.577  14.764  1.00 27.80           N  
ANISOU 2378  N   LYS A 307     3636   3040   3888    105    198    -27       N  
ATOM   2379  CA  LYS A 307       7.984  27.150  14.999  1.00 26.51           C  
ANISOU 2379  CA  LYS A 307     3444   2969   3659     77    243    -52       C  
ATOM   2380  C   LYS A 307       7.200  26.719  16.233  1.00 28.21           C  
ANISOU 2380  C   LYS A 307     3616   3213   3889    106    280   -129       C  
ATOM   2381  O   LYS A 307       7.335  27.319  17.304  1.00 44.27           O  
ANISOU 2381  O   LYS A 307     5658   5215   5949    119    301   -183       O  
ATOM   2382  CB  LYS A 307       9.467  26.827  15.172  1.00 28.46           C  
ANISOU 2382  CB  LYS A 307     3718   3234   3863     18    273    -50       C  
ATOM   2383  CG  LYS A 307       9.749  25.409  15.634  1.00 37.41           C  
ANISOU 2383  CG  LYS A 307     4832   4438   4944      3    304    -84       C  
ATOM   2384  CD  LYS A 307       9.532  24.401  14.519  1.00 47.80           C  
ANISOU 2384  CD  LYS A 307     6139   5808   6215     -8    297    -54       C  
ATOM   2385  CE  LYS A 307      10.636  24.478  13.479  1.00 47.91           C  
ANISOU 2385  CE  LYS A 307     6172   5839   6192    -48    300    -17       C  
ATOM   2386  NZ  LYS A 307      10.462  23.430  12.437  1.00 49.35           N  
ANISOU 2386  NZ  LYS A 307     6349   6081   6319    -55    296    -10       N  
ATOM   2387  N   TYR A 308       6.395  25.668  16.086  1.00 26.00           N  
ANISOU 2387  N   TYR A 308     3295   2996   3587    107    292   -137       N  
ATOM   2388  CA  TYR A 308       5.541  25.212  17.174  1.00 26.13           C  
ANISOU 2388  CA  TYR A 308     3267   3051   3610    116    340   -201       C  
ATOM   2389  C   TYR A 308       6.347  24.488  18.245  1.00 25.68           C  
ANISOU 2389  C   TYR A 308     3249   3018   3491     71    385   -224       C  
ATOM   2390  O   TYR A 308       7.174  23.625  17.937  1.00 30.41           O  
ANISOU 2390  O   TYR A 308     3879   3633   4042     35    377   -192       O  
ATOM   2391  CB  TYR A 308       4.444  24.287  16.654  1.00 26.24           C  
ANISOU 2391  CB  TYR A 308     3223   3121   3626    111    336   -199       C  
ATOM   2392  CG  TYR A 308       3.619  23.694  17.771  1.00 26.53           C  
ANISOU 2392  CG  TYR A 308     3213   3208   3659     93    403   -257       C  
ATOM   2393  CD1 TYR A 308       2.643  24.448  18.407  1.00 37.62           C  
ANISOU 2393  CD1 TYR A 308     4553   4619   5124    137    433   -323       C  
ATOM   2394  CD2 TYR A 308       3.829  22.390  18.206  1.00 26.17           C  
ANISOU 2394  CD2 TYR A 308     3193   3201   3551     28    440   -249       C  
ATOM   2395  CE1 TYR A 308       1.892  23.922  19.435  1.00 27.82           C  
ANISOU 2395  CE1 TYR A 308     3265   3440   3866    106    514   -380       C  
ATOM   2396  CE2 TYR A 308       3.081  21.855  19.237  1.00 26.64           C  
ANISOU 2396  CE2 TYR A 308     3224   3306   3593     -8    509   -289       C  
ATOM   2397  CZ  TYR A 308       2.113  22.628  19.847  1.00 27.47           C  
ANISOU 2397  CZ  TYR A 308     3257   3436   3745     25    554   -355       C  
ATOM   2398  OH  TYR A 308       1.360  22.109  20.873  1.00 39.38           O  
ANISOU 2398  OH  TYR A 308     4732   5007   5224    -25    642   -398       O  
ATOM   2399  N   VAL A 309       6.085  24.830  19.508  1.00 26.06           N  
ANISOU 2399  N   VAL A 309     3296   3070   3537     79    429   -284       N  
ATOM   2400  CA  VAL A 309       6.677  24.155  20.657  1.00 25.92           C  
ANISOU 2400  CA  VAL A 309     3324   3078   3444     38    463   -303       C  
ATOM   2401  C   VAL A 309       5.584  23.912  21.692  1.00 26.56           C  
ANISOU 2401  C   VAL A 309     3378   3212   3503     29    533   -358       C  
ATOM   2402  O   VAL A 309       4.550  24.580  21.702  1.00 29.37           O  
ANISOU 2402  O   VAL A 309     3669   3575   3916     69    558   -406       O  
ATOM   2403  CB  VAL A 309       7.842  24.968  21.274  1.00 32.56           C  
ANISOU 2403  CB  VAL A 309     4216   3877   4276     41    443   -326       C  
ATOM   2404  CG1 VAL A 309       8.956  25.155  20.257  1.00 25.50           C  
ANISOU 2404  CG1 VAL A 309     3337   2947   3404     31    392   -274       C  
ATOM   2405  CG2 VAL A 309       7.345  26.314  21.764  1.00 26.67           C  
ANISOU 2405  CG2 VAL A 309     3457   3093   3585     85    455   -392       C  
ATOM   2406  N   ARG A 310       5.817  22.933  22.567  1.00 26.58           N  
ANISOU 2406  N   ARG A 310     3429   3250   3420    -25    563   -350       N  
ATOM   2407  CA  ARG A 310       4.864  22.587  23.618  1.00 29.82           C  
ANISOU 2407  CA  ARG A 310     3826   3722   3781    -60    646   -392       C  
ATOM   2408  C   ARG A 310       5.035  23.425  24.877  1.00 28.06           C  
ANISOU 2408  C   ARG A 310     3638   3510   3512    -48    685   -466       C  
ATOM   2409  O   ARG A 310       4.400  23.129  25.894  1.00 43.82           O  
ANISOU 2409  O   ARG A 310     5641   5570   5436    -88    764   -503       O  
ATOM   2410  CB  ARG A 310       4.981  21.108  23.998  1.00 27.35           C  
ANISOU 2410  CB  ARG A 310     3572   3434   3385   -136    657   -335       C  
ATOM   2411  CG  ARG A 310       4.749  20.131  22.873  1.00 30.67           C  
ANISOU 2411  CG  ARG A 310     3966   3842   3844   -157    623   -279       C  
ATOM   2412  CD  ARG A 310       4.539  18.733  23.426  1.00 28.84           C  
ANISOU 2412  CD  ARG A 310     3789   3625   3543   -241    648   -235       C  
ATOM   2413  NE  ARG A 310       5.047  17.705  22.523  1.00 36.05           N  
ANISOU 2413  NE  ARG A 310     4731   4492   4474   -251    579   -180       N  
ATOM   2414  CZ  ARG A 310       4.346  17.150  21.542  1.00 45.54           C  
ANISOU 2414  CZ  ARG A 310     5876   5695   5730   -268    570   -171       C  
ATOM   2415  NH1 ARG A 310       3.093  17.521  21.322  1.00 45.87           N  
ANISOU 2415  NH1 ARG A 310     5821   5787   5822   -276    617   -206       N  
ATOM   2416  NH2 ARG A 310       4.903  16.224  20.777  1.00 52.71           N  
ANISOU 2416  NH2 ARG A 310     6822   6558   6649   -271    507   -137       N  
ATOM   2417  N   SER A 311       5.871  24.454  24.834  1.00 28.48           N  
ANISOU 2417  N   SER A 311     3716   3506   3598     -3    634   -490       N  
ATOM   2418  CA  SER A 311       6.206  25.208  26.030  1.00 28.57           C  
ANISOU 2418  CA  SER A 311     3775   3521   3560      4    655   -568       C  
ATOM   2419  C   SER A 311       5.088  26.170  26.414  1.00 29.58           C  
ANISOU 2419  C   SER A 311     3837   3667   3737     52    721   -673       C  
ATOM   2420  O   SER A 311       4.334  26.658  25.568  1.00 29.66           O  
ANISOU 2420  O   SER A 311     3762   3651   3856    105    715   -683       O  
ATOM   2421  CB  SER A 311       7.505  25.980  25.817  1.00 28.19           C  
ANISOU 2421  CB  SER A 311     3768   3397   3545     25    572   -565       C  
ATOM   2422  OG  SER A 311       8.525  25.107  25.374  1.00 29.57           O  
ANISOU 2422  OG  SER A 311     3979   3563   3693     -7    513   -483       O  
ATOM   2423  N   ALA A 312       4.992  26.437  27.714  1.00 30.54           N  
ANISOU 2423  N   ALA A 312     3996   3834   3772     38    781   -757       N  
ATOM   2424  CA  ALA A 312       4.063  27.417  28.256  1.00 31.75           C  
ANISOU 2424  CA  ALA A 312     4091   4009   3966     92    851   -887       C  
ATOM   2425  C   ALA A 312       4.703  28.779  28.484  1.00 35.84           C  
ANISOU 2425  C   ALA A 312     4643   4438   4538    152    796   -968       C  
ATOM   2426  O   ALA A 312       3.979  29.767  28.642  1.00 41.79           O  
ANISOU 2426  O   ALA A 312     5338   5170   5370    223    827  -1079       O  
ATOM   2427  CB  ALA A 312       3.471  26.911  29.576  1.00 32.90           C  
ANISOU 2427  CB  ALA A 312     4258   4272   3971     33    968   -950       C  
ATOM   2428  N   LYS A 313       6.033  28.855  28.499  1.00 31.49           N  
ANISOU 2428  N   LYS A 313     4177   3831   3959    126    712   -922       N  
ATOM   2429  CA  LYS A 313       6.733  30.096  28.804  1.00 33.29           C  
ANISOU 2429  CA  LYS A 313     4444   3972   4233    160    657   -999       C  
ATOM   2430  C   LYS A 313       8.157  30.000  28.278  1.00 33.52           C  
ANISOU 2430  C   LYS A 313     4523   3938   4274    122    555   -910       C  
ATOM   2431  O   LYS A 313       8.879  29.056  28.613  1.00 46.13           O  
ANISOU 2431  O   LYS A 313     6170   5585   5771     66    534   -852       O  
ATOM   2432  CB  LYS A 313       6.728  30.362  30.314  1.00 38.04           C  
ANISOU 2432  CB  LYS A 313     5104   4633   4716    146    709  -1123       C  
ATOM   2433  CG  LYS A 313       7.436  31.638  30.734  1.00 60.62           C  
ANISOU 2433  CG  LYS A 313     8011   7401   7621    176    648  -1224       C  
ATOM   2434  CD  LYS A 313       7.382  31.818  32.245  1.00 62.53           C  
ANISOU 2434  CD  LYS A 313     8317   7718   7722    159    701  -1357       C  
ATOM   2435  CE  LYS A 313       8.141  33.059  32.691  1.00 60.25           C  
ANISOU 2435  CE  LYS A 313     8081   7333   7478    181    629  -1468       C  
ATOM   2436  NZ  LYS A 313       8.131  33.213  34.173  1.00 71.10           N  
ANISOU 2436  NZ  LYS A 313     9530   8791   8695    162    674  -1606       N  
ATOM   2437  N   LEU A 314       8.557  30.979  27.447  1.00 33.64           N  
ANISOU 2437  N   LEU A 314     4525   3841   4417    152    491   -898       N  
ATOM   2438  CA  LEU A 314       9.916  31.073  26.898  1.00 30.31           C  
ANISOU 2438  CA  LEU A 314     4133   3360   4022    108    407   -828       C  
ATOM   2439  C   LEU A 314      10.342  32.541  26.957  1.00 31.14           C  
ANISOU 2439  C   LEU A 314     4261   3346   4225    124    357   -898       C  
ATOM   2440  O   LEU A 314      10.337  33.256  25.952  1.00 32.61           O  
ANISOU 2440  O   LEU A 314     4430   3435   4526    140    321   -852       O  
ATOM   2441  CB  LEU A 314       9.994  30.526  25.473  1.00 29.29           C  
ANISOU 2441  CB  LEU A 314     3963   3221   3943     97    387   -702       C  
ATOM   2442  CG  LEU A 314      10.246  29.024  25.324  1.00 43.39           C  
ANISOU 2442  CG  LEU A 314     5747   5096   5641     58    397   -623       C  
ATOM   2443  CD1 LEU A 314      10.284  28.633  23.858  1.00 31.99           C  
ANISOU 2443  CD1 LEU A 314     4265   3639   4252     54    379   -521       C  
ATOM   2444  CD2 LEU A 314      11.536  28.626  26.021  1.00 38.14           C  
ANISOU 2444  CD2 LEU A 314     5131   4454   4908     12    351   -626       C  
ATOM   2445  N   ARG A 315      10.719  32.990  28.150  1.00 32.01           N  
ANISOU 2445  N   ARG A 315     4420   3458   4283    114    350  -1007       N  
ATOM   2446  CA  ARG A 315      11.108  34.373  28.385  1.00 33.04           C  
ANISOU 2446  CA  ARG A 315     4580   3469   4503    124    300  -1096       C  
ATOM   2447  C   ARG A 315      12.619  34.455  28.552  1.00 33.60           C  
ANISOU 2447  C   ARG A 315     4686   3518   4562     46    221  -1080       C  
ATOM   2448  O   ARG A 315      13.196  33.752  29.388  1.00 32.92           O  
ANISOU 2448  O   ARG A 315     4628   3521   4358     11    209  -1099       O  
ATOM   2449  CB  ARG A 315      10.399  34.943  29.616  1.00 35.42           C  
ANISOU 2449  CB  ARG A 315     4908   3786   4764    174    345  -1262       C  
ATOM   2450  CG  ARG A 315      10.743  36.392  29.910  1.00 47.14           C  
ANISOU 2450  CG  ARG A 315     6431   5131   6349    191    288  -1374       C  
ATOM   2451  CD  ARG A 315       9.776  37.004  30.911  1.00 42.60           C  
ANISOU 2451  CD  ARG A 315     5863   4565   5757    266    348  -1552       C  
ATOM   2452  NE  ARG A 315       8.440  37.151  30.344  1.00 42.75           N  
ANISOU 2452  NE  ARG A 315     5809   4571   5864    358    405  -1558       N  
ATOM   2453  CZ  ARG A 315       8.047  38.188  29.612  1.00 43.63           C  
ANISOU 2453  CZ  ARG A 315     5901   4528   6148    427    357  -1569       C  
ATOM   2454  NH1 ARG A 315       8.891  39.176  29.357  1.00 38.43           N  
ANISOU 2454  NH1 ARG A 315     5300   3710   5590    400    263  -1570       N  
ATOM   2455  NH2 ARG A 315       6.811  38.235  29.135  1.00 53.75           N  
ANISOU 2455  NH2 ARG A 315     7104   5811   7506    519    397  -1578       N  
ATOM   2456  N   MET A 316      13.248  35.316  27.759  1.00 36.47           N  
ANISOU 2456  N   MET A 316     5047   3761   5049     16    165  -1044       N  
ATOM   2457  CA  MET A 316      14.693  35.488  27.744  1.00 33.78           C  
ANISOU 2457  CA  MET A 316     4713   3396   4728    -70     95  -1028       C  
ATOM   2458  C   MET A 316      15.053  36.810  28.407  1.00 44.20           C  
ANISOU 2458  C   MET A 316     6078   4599   6115    -86     43  -1150       C  
ATOM   2459  O   MET A 316      14.521  37.860  28.035  1.00 45.67           O  
ANISOU 2459  O   MET A 316     6283   4655   6415    -53     37  -1175       O  
ATOM   2460  CB  MET A 316      15.217  35.446  26.309  1.00 32.59           C  
ANISOU 2460  CB  MET A 316     4521   3204   4658   -119     83   -891       C  
ATOM   2461  CG  MET A 316      16.718  35.579  26.180  1.00 48.97           C  
ANISOU 2461  CG  MET A 316     6576   5269   6763   -217     27   -874       C  
ATOM   2462  SD  MET A 316      17.283  35.102  24.538  1.00 38.67           S  
ANISOU 2462  SD  MET A 316     5210   3982   5499   -276     49   -715       S  
ATOM   2463  CE  MET A 316      16.928  33.351  24.566  1.00 42.43           C  
ANISOU 2463  CE  MET A 316     5652   4619   5850   -223     90   -670       C  
ATOM   2464  N   VAL A 317      15.956  36.759  29.381  1.00 44.89           N  
ANISOU 2464  N   VAL A 317     6189   4728   6140   -133     -8  -1229       N  
ATOM   2465  CA  VAL A 317      16.333  37.954  30.128  1.00 40.80           C  
ANISOU 2465  CA  VAL A 317     5719   4108   5676   -154    -66  -1366       C  
ATOM   2466  C   VAL A 317      17.278  38.803  29.288  1.00 44.16           C  
ANISOU 2466  C   VAL A 317     6127   4403   6250   -242   -126  -1314       C  
ATOM   2467  O   VAL A 317      18.222  38.290  28.675  1.00 40.13           O  
ANISOU 2467  O   VAL A 317     5562   3937   5748   -316   -145  -1218       O  
ATOM   2468  CB  VAL A 317      16.967  37.578  31.478  1.00 37.30           C  
ANISOU 2468  CB  VAL A 317     5310   3763   5099   -179   -113  -1470       C  
ATOM   2469  CG1 VAL A 317      18.119  36.611  31.288  1.00 36.54           C  
ANISOU 2469  CG1 VAL A 317     5166   3760   4959   -243   -164  -1381       C  
ATOM   2470  CG2 VAL A 317      17.439  38.825  32.218  1.00 38.98           C  
ANISOU 2470  CG2 VAL A 317     5572   3867   5370   -211   -185  -1623       C  
ATOM   2471  N   THR A 318      17.008  40.104  29.240  1.00 38.36           N  
ANISOU 2471  N   THR A 318     5437   3501   5635   -236   -152  -1381       N  
ATOM   2472  CA  THR A 318      17.902  41.084  28.639  1.00 39.23           C  
ANISOU 2472  CA  THR A 318     5553   3464   5888   -337   -214  -1350       C  
ATOM   2473  C   THR A 318      18.562  41.983  29.668  1.00 40.84           C  
ANISOU 2473  C   THR A 318     5802   3589   6128   -387   -293  -1510       C  
ATOM   2474  O   THR A 318      19.711  42.381  29.488  1.00 41.47           O  
ANISOU 2474  O   THR A 318     5860   3619   6279   -507   -352  -1498       O  
ATOM   2475  CB  THR A 318      17.141  41.956  27.638  1.00 39.65           C  
ANISOU 2475  CB  THR A 318     5641   3350   6075   -305   -204  -1279       C  
ATOM   2476  OG1 THR A 318      16.030  42.577  28.296  1.00 42.34           O  
ANISOU 2476  OG1 THR A 318     6033   3617   6438   -188   -199  -1410       O  
ATOM   2477  CG2 THR A 318      16.635  41.117  26.481  1.00 38.21           C  
ANISOU 2477  CG2 THR A 318     5415   3242   5861   -276   -143  -1113       C  
ATOM   2478  N   GLY A 319      17.857  42.306  30.742  1.00 41.66           N  
ANISOU 2478  N   GLY A 319     5962   3688   6181   -303   -291  -1669       N  
ATOM   2479  CA  GLY A 319      18.370  43.155  31.794  1.00 43.35           C  
ANISOU 2479  CA  GLY A 319     6229   3831   6412   -339   -367  -1846       C  
ATOM   2480  C   GLY A 319      19.116  42.386  32.860  1.00 43.32           C  
ANISOU 2480  C   GLY A 319     6214   3994   6251   -374   -406  -1918       C  
ATOM   2481  O   GLY A 319      19.759  41.365  32.596  1.00 42.18           O  
ANISOU 2481  O   GLY A 319     6007   3981   6039   -416   -409  -1810       O  
ATOM   2482  N   LEU A 320      19.021  42.882  34.087  1.00 53.70           N  
ANISOU 2482  N   LEU A 320     7596   5303   7504   -350   -444  -2107       N  
ATOM   2483  CA  LEU A 320      19.774  42.374  35.222  1.00 54.15           C  
ANISOU 2483  CA  LEU A 320     7669   5496   7411   -387   -512  -2198       C  
ATOM   2484  C   LEU A 320      18.840  41.680  36.203  1.00 53.46           C  
ANISOU 2484  C   LEU A 320     7636   5560   7118   -291   -442  -2272       C  
ATOM   2485  O   LEU A 320      17.616  41.724  36.071  1.00 55.78           O  
ANISOU 2485  O   LEU A 320     7944   5846   7405   -198   -339  -2282       O  
ATOM   2486  CB  LEU A 320      20.521  43.511  35.931  1.00 65.73           C  
ANISOU 2486  CB  LEU A 320     9182   6846   8947   -458   -623  -2370       C  
ATOM   2487  CG  LEU A 320      21.722  44.203  35.282  1.00 55.63           C  
ANISOU 2487  CG  LEU A 320     7851   5436   7850   -595   -714  -2330       C  
ATOM   2488  CD1 LEU A 320      21.373  44.924  33.990  1.00 57.87           C  
ANISOU 2488  CD1 LEU A 320     8123   5538   8327   -611   -667  -2215       C  
ATOM   2489  CD2 LEU A 320      22.307  45.180  36.270  1.00 54.58           C  
ANISOU 2489  CD2 LEU A 320     7776   5217   7745   -653   -826  -2534       C  
ATOM   2490  N   ARG A 321      19.439  41.035  37.202  1.00 56.26           N  
ANISOU 2490  N   ARG A 321     8020   6056   7302   -319   -502  -2322       N  
ATOM   2491  CA  ARG A 321      18.669  40.542  38.336  1.00 53.85           C  
ANISOU 2491  CA  ARG A 321     7794   5889   6780   -255   -447  -2417       C  
ATOM   2492  C   ARG A 321      18.155  41.732  39.136  1.00 53.28           C  
ANISOU 2492  C   ARG A 321     7798   5729   6716   -218   -440  -2641       C  
ATOM   2493  O   ARG A 321      18.945  42.534  39.643  1.00 53.57           O  
ANISOU 2493  O   ARG A 321     7870   5689   6795   -275   -552  -2771       O  
ATOM   2494  CB  ARG A 321      19.523  39.626  39.210  1.00 51.48           C  
ANISOU 2494  CB  ARG A 321     7525   5745   6291   -300   -539  -2408       C  
ATOM   2495  CG  ARG A 321      18.748  38.977  40.350  1.00 73.94           C  
ANISOU 2495  CG  ARG A 321    10467   8748   8880   -252   -474  -2472       C  
ATOM   2496  CD  ARG A 321      19.562  37.909  41.063  1.00 72.87           C  
ANISOU 2496  CD  ARG A 321    10372   8760   8556   -292   -577  -2414       C  
ATOM   2497  NE  ARG A 321      20.315  37.077  40.130  1.00 61.86           N  
ANISOU 2497  NE  ARG A 321     8880   7371   7252   -319   -628  -2227       N  
ATOM   2498  CZ  ARG A 321      20.481  35.766  40.264  1.00 64.13           C  
ANISOU 2498  CZ  ARG A 321     9180   7780   7406   -312   -649  -2099       C  
ATOM   2499  NH1 ARG A 321      19.931  35.126  41.286  1.00 65.85           N  
ANISOU 2499  NH1 ARG A 321     9514   8122   7385   -294   -619  -2118       N  
ATOM   2500  NH2 ARG A 321      21.187  35.092  39.366  1.00 62.92           N  
ANISOU 2500  NH2 ARG A 321     8928   7620   7358   -327   -695  -1953       N  
ATOM   2501  N   ASN A 322      16.834  41.856  39.236  1.00 49.45           N  
ANISOU 2501  N   ASN A 322     7331   5255   6203   -122   -312  -2699       N  
ATOM   2502  CA  ASN A 322      16.206  43.025  39.848  1.00 50.11           C  
ANISOU 2502  CA  ASN A 322     7471   5240   6327    -63   -289  -2922       C  
ATOM   2503  C   ASN A 322      16.350  42.925  41.361  1.00 51.85           C  
ANISOU 2503  C   ASN A 322     7791   5596   6314    -76   -310  -3101       C  
ATOM   2504  O   ASN A 322      15.643  42.157  42.017  1.00 51.82           O  
ANISOU 2504  O   ASN A 322     7820   5767   6101    -40   -210  -3115       O  
ATOM   2505  CB  ASN A 322      14.743  43.120  39.433  1.00 53.54           C  
ANISOU 2505  CB  ASN A 322     7868   5659   6815     53   -144  -2929       C  
ATOM   2506  CG  ASN A 322      14.152  44.488  39.694  1.00 51.80           C  
ANISOU 2506  CG  ASN A 322     7679   5276   6726    130   -137  -3142       C  
ATOM   2507  OD1 ASN A 322      14.877  45.476  39.807  1.00 53.01           O  
ANISOU 2507  OD1 ASN A 322     7876   5271   6996     87   -250  -3240       O  
ATOM   2508  ND2 ASN A 322      12.829  44.556  39.786  1.00 58.96           N  
ANISOU 2508  ND2 ASN A 322     8559   6217   7627    245     -8  -3222       N  
ATOM   2509  N   ILE A 323      17.270  43.707  41.919  1.00 53.28           N  
ANISOU 2509  N   ILE A 323     8024   5698   6523   -137   -443  -3238       N  
ATOM   2510  CA  ILE A 323      17.524  43.716  43.358  1.00 67.04           C  
ANISOU 2510  CA  ILE A 323     9872   7560   8040   -158   -490  -3421       C  
ATOM   2511  C   ILE A 323      17.300  45.128  43.890  1.00 73.96           C  
ANISOU 2511  C   ILE A 323    10809   8290   9005   -125   -514  -3684       C  
ATOM   2512  O   ILE A 323      18.273  45.859  44.127  1.00 76.73           O  
ANISOU 2512  O   ILE A 323    11187   8531   9434   -199   -660  -3780       O  
ATOM   2513  CB  ILE A 323      18.945  43.226  43.676  1.00 57.44           C  
ANISOU 2513  CB  ILE A 323     8666   6409   6749   -265   -658  -3359       C  
ATOM   2514  CG1 ILE A 323      19.289  41.999  42.832  1.00 55.43           C  
ANISOU 2514  CG1 ILE A 323     8327   6235   6498   -290   -653  -3093       C  
ATOM   2515  CG2 ILE A 323      19.077  42.904  45.157  1.00 68.79           C  
ANISOU 2515  CG2 ILE A 323    10225   8018   7893   -280   -700  -3501       C  
ATOM   2516  CD1 ILE A 323      20.717  41.535  42.985  1.00 52.79           C  
ANISOU 2516  CD1 ILE A 323     7971   5950   6138   -381   -824  -3028       C  
ATOM   2517  N   PRO A 324      16.051  45.557  44.089  1.00 84.83           N  
ANISOU 2517  N   PRO A 324    12198   9652  10381    -17   -377  -3817       N  
ATOM   2518  CA  PRO A 324      15.807  46.935  44.528  1.00 85.45           C  
ANISOU 2518  CA  PRO A 324    12329   9566  10571     31   -402  -4079       C  
ATOM   2519  C   PRO A 324      15.522  47.059  46.018  1.00 86.20           C  
ANISOU 2519  C   PRO A 324    12531   9811  10409     48   -360  -4269       C  
ATOM   2520  O   PRO A 324      15.109  46.090  46.663  1.00 94.75           O  
ANISOU 2520  O   PRO A 324    13646  11124  11230     53   -268  -4263       O  
ATOM   2521  CB  PRO A 324      14.586  47.342  43.694  1.00 84.27           C  
ANISOU 2521  CB  PRO A 324    12107   9302  10610    155   -278  -4065       C  
ATOM   2522  CG  PRO A 324      13.887  46.019  43.347  1.00 84.69           C  
ANISOU 2522  CG  PRO A 324    12093   9555  10530    183   -139  -3869       C  
ATOM   2523  CD  PRO A 324      14.793  44.874  43.751  1.00 87.78           C  
ANISOU 2523  CD  PRO A 324    12518  10132  10704     73   -198  -3731       C  
ATOM   2524  N   SER A 325      15.736  48.258  46.558  1.00101.38           N  
ANISOU 2524  N   SER A 325    14517  11603  12401     46   -421  -4413       N  
ATOM   2525  CA  SER A 325      15.451  48.587  47.958  1.00106.88           C  
ANISOU 2525  CA  SER A 325    15324  12411  12876     63   -380  -4594       C  
ATOM   2526  C   SER A 325      15.950  47.527  48.939  1.00109.67           C  
ANISOU 2526  C   SER A 325    15759  13015  12896    -15   -408  -4581       C  
ATOM   2527  O   SER A 325      16.992  47.694  49.573  1.00109.44           O  
ANISOU 2527  O   SER A 325    15803  12995  12785   -108   -558  -4626       O  
ATOM   2528  CB  SER A 325      13.948  48.813  48.157  1.00101.97           C  
ANISOU 2528  CB  SER A 325    14680  11831  12234    201   -184  -4683       C  
ATOM   2529  OG  SER A 325      13.201  47.642  47.881  1.00101.60           O  
ANISOU 2529  OG  SER A 325    14571  11964  12068    235    -45  -4573       O  
TER    2530      SER A 325                                                      
ATOM   2531  N   GLY B   1      26.808  35.630  41.777  1.00 49.29           N  
ANISOU 2531  N   GLY B   1     7091   5984   5652   -533  -1517  -2255       N  
ATOM   2532  CA  GLY B   1      27.307  35.930  40.449  1.00 48.22           C  
ANISOU 2532  CA  GLY B   1     6784   5762   5776   -575  -1473  -2190       C  
ATOM   2533  C   GLY B   1      28.691  35.361  40.213  1.00 48.59           C  
ANISOU 2533  C   GLY B   1     6685   5859   5917   -599  -1626  -2152       C  
ATOM   2534  O   GLY B   1      29.460  35.190  41.153  1.00 50.16           O  
ANISOU 2534  O   GLY B   1     6904   6125   6030   -605  -1808  -2229       O  
ATOM   2535  N   LEU B   2      29.006  35.068  38.948  1.00 47.61           N  
ANISOU 2535  N   LEU B   2     6411   5710   5969   -610  -1556  -2042       N  
ATOM   2536  CA  LEU B   2      30.296  34.459  38.631  1.00 55.99           C  
ANISOU 2536  CA  LEU B   2     7309   6830   7135   -622  -1683  -2012       C  
ATOM   2537  C   LEU B   2      31.455  35.397  38.942  1.00 49.57           C  
ANISOU 2537  C   LEU B   2     6395   5991   6450   -723  -1824  -2156       C  
ATOM   2538  O   LEU B   2      32.537  34.946  39.338  1.00 50.76           O  
ANISOU 2538  O   LEU B   2     6451   6218   6617   -720  -1999  -2192       O  
ATOM   2539  CB  LEU B   2      30.342  34.040  37.163  1.00 55.84           C  
ANISOU 2539  CB  LEU B   2     7149   6793   7272   -621  -1552  -1882       C  
ATOM   2540  CG  LEU B   2      29.696  32.710  36.780  1.00 44.50           C  
ANISOU 2540  CG  LEU B   2     5751   5414   5743   -517  -1478  -1735       C  
ATOM   2541  CD1 LEU B   2      30.104  32.335  35.368  1.00 43.44           C  
ANISOU 2541  CD1 LEU B   2     5448   5278   5779   -528  -1390  -1643       C  
ATOM   2542  CD2 LEU B   2      30.081  31.620  37.760  1.00 45.31           C  
ANISOU 2542  CD2 LEU B   2     5911   5612   5694   -439  -1643  -1725       C  
ATOM   2543  N   PHE B   3      31.251  36.701  38.769  1.00 50.02           N  
ANISOU 2543  N   PHE B   3     6465   5933   6607   -811  -1761  -2240       N  
ATOM   2544  CA  PHE B   3      32.311  37.689  38.904  1.00 56.95           C  
ANISOU 2544  CA  PHE B   3     7238   6761   7638   -933  -1874  -2371       C  
ATOM   2545  C   PHE B   3      32.190  38.505  40.184  1.00 53.61           C  
ANISOU 2545  C   PHE B   3     6955   6308   7105   -957  -1985  -2546       C  
ATOM   2546  O   PHE B   3      32.869  39.527  40.324  1.00 55.19           O  
ANISOU 2546  O   PHE B   3     7100   6435   7436  -1068  -2064  -2672       O  
ATOM   2547  CB  PHE B   3      32.324  38.601  37.676  1.00 51.36           C  
ANISOU 2547  CB  PHE B   3     6436   5927   7150  -1038  -1734  -2335       C  
ATOM   2548  CG  PHE B   3      32.633  37.878  36.402  1.00 50.01           C  
ANISOU 2548  CG  PHE B   3     6111   5800   7090  -1035  -1636  -2187       C  
ATOM   2549  CD1 PHE B   3      31.628  37.264  35.673  1.00 52.06           C  
ANISOU 2549  CD1 PHE B   3     6428   6060   7292   -952  -1475  -2044       C  
ATOM   2550  CD2 PHE B   3      33.934  37.792  35.945  1.00 50.93           C  
ANISOU 2550  CD2 PHE B   3     6019   5968   7367  -1116  -1704  -2202       C  
ATOM   2551  CE1 PHE B   3      31.919  36.586  34.501  1.00 46.88           C  
ANISOU 2551  CE1 PHE B   3     5637   5449   6727   -949  -1387  -1921       C  
ATOM   2552  CE2 PHE B   3      34.228  37.118  34.775  1.00 57.71           C  
ANISOU 2552  CE2 PHE B   3     6731   6878   8317  -1112  -1602  -2083       C  
ATOM   2553  CZ  PHE B   3      33.220  36.515  34.053  1.00 47.85           C  
ANISOU 2553  CZ  PHE B   3     5556   5624   6999  -1027  -1445  -1943       C  
ATOM   2554  N   GLY B   4      31.338  38.078  41.114  1.00 53.53           N  
ANISOU 2554  N   GLY B   4     7129   6354   6855   -863  -1987  -2559       N  
ATOM   2555  CA  GLY B   4      31.273  38.650  42.445  1.00 55.42           C  
ANISOU 2555  CA  GLY B   4     7511   6604   6944   -874  -2104  -2731       C  
ATOM   2556  C   GLY B   4      30.851  40.098  42.544  1.00 56.53           C  
ANISOU 2556  C   GLY B   4     7717   6598   7164   -943  -2046  -2875       C  
ATOM   2557  O   GLY B   4      30.931  40.670  43.633  1.00 58.17           O  
ANISOU 2557  O   GLY B   4     8030   6808   7266   -963  -2156  -3047       O  
ATOM   2558  N   ALA B   5      30.395  40.717  41.459  1.00 61.60           N  
ANISOU 2558  N   ALA B   5     8313   7108   7987   -977  -1886  -2816       N  
ATOM   2559  CA  ALA B   5      29.977  42.123  41.517  1.00 57.98           C  
ANISOU 2559  CA  ALA B   5     7925   6481   7625  -1034  -1842  -2950       C  
ATOM   2560  C   ALA B   5      28.495  42.226  41.858  1.00 55.60           C  
ANISOU 2560  C   ALA B   5     7792   6159   7175   -930  -1701  -2972       C  
ATOM   2561  O   ALA B   5      28.132  42.628  42.969  1.00 57.08           O  
ANISOU 2561  O   ALA B   5     8115   6360   7213   -904  -1746  -3136       O  
ATOM   2562  CB  ALA B   5      30.298  42.830  40.200  1.00 55.74           C  
ANISOU 2562  CB  ALA B   5     7514   6049   7616  -1134  -1763  -2875       C  
ATOM   2563  N   ILE B   6      27.629  41.865  40.912  1.00 53.62           N  
ANISOU 2563  N   ILE B   6     7528   5883   6961   -870  -1528  -2818       N  
ATOM   2564  CA  ILE B   6      26.192  41.925  41.145  1.00 53.07           C  
ANISOU 2564  CA  ILE B   6     7588   5802   6773   -769  -1384  -2836       C  
ATOM   2565  C   ILE B   6      25.812  40.886  42.189  1.00 58.01           C  
ANISOU 2565  C   ILE B   6     8315   6612   7113   -690  -1401  -2840       C  
ATOM   2566  O   ILE B   6      26.194  39.713  42.087  1.00 52.19           O  
ANISOU 2566  O   ILE B   6     7533   5999   6299   -669  -1437  -2706       O  
ATOM   2567  CB  ILE B   6      25.428  41.719  39.830  1.00 51.02           C  
ANISOU 2567  CB  ILE B   6     7274   5482   6629   -729  -1215  -2662       C  
ATOM   2568  CG1 ILE B   6      25.761  42.850  38.854  1.00 51.33           C  
ANISOU 2568  CG1 ILE B   6     7245   5327   6933   -817  -1204  -2656       C  
ATOM   2569  CG2 ILE B   6      23.928  41.639  40.084  1.00 50.49           C  
ANISOU 2569  CG2 ILE B   6     7316   5430   6440   -617  -1071  -2679       C  
ATOM   2570  CD1 ILE B   6      25.042  42.755  37.529  1.00 49.60           C  
ANISOU 2570  CD1 ILE B   6     6984   5037   6824   -785  -1055  -2487       C  
ATOM   2571  N   ALA B   7      25.066  41.320  43.209  1.00 54.39           N  
ANISOU 2571  N   ALA B   7     8000   6170   6496   -649  -1375  -2998       N  
ATOM   2572  CA  ALA B   7      24.755  40.503  44.382  1.00 55.06           C  
ANISOU 2572  CA  ALA B   7     8209   6430   6281   -599  -1400  -3029       C  
ATOM   2573  C   ALA B   7      26.023  39.974  45.047  1.00 56.15           C  
ANISOU 2573  C   ALA B   7     8334   6669   6329   -648  -1614  -3037       C  
ATOM   2574  O   ALA B   7      26.008  38.924  45.695  1.00 56.23           O  
ANISOU 2574  O   ALA B   7     8418   6830   6117   -611  -1659  -2971       O  
ATOM   2575  CB  ALA B   7      23.807  39.351  44.035  1.00 53.23           C  
ANISOU 2575  CB  ALA B   7     7995   6298   5933   -522  -1249  -2852       C  
ATOM   2576  N   GLY B   8      27.126  40.703  44.887  1.00 60.96           N  
ANISOU 2576  N   GLY B   8     8851   7193   7118   -734  -1754  -3117       N  
ATOM   2577  CA  GLY B   8      28.386  40.357  45.511  1.00 61.99           C  
ANISOU 2577  CA  GLY B   8     8947   7410   7198   -782  -1978  -3154       C  
ATOM   2578  C   GLY B   8      28.868  41.454  46.436  1.00 63.96           C  
ANISOU 2578  C   GLY B   8     9257   7610   7434   -850  -2118  -3394       C  
ATOM   2579  O   GLY B   8      28.167  41.812  47.387  1.00 63.47           O  
ANISOU 2579  O   GLY B   8     9357   7576   7181   -818  -2090  -3537       O  
ATOM   2580  N   PHE B   9      30.057  42.008  46.174  1.00 68.43           N  
ANISOU 2580  N   PHE B   9     9690   8107   8202   -949  -2264  -3452       N  
ATOM   2581  CA  PHE B   9      30.532  43.101  47.011  1.00 64.55           C  
ANISOU 2581  CA  PHE B   9     9253   7553   7720  -1026  -2404  -3690       C  
ATOM   2582  C   PHE B   9      29.714  44.369  46.803  1.00 67.08           C  
ANISOU 2582  C   PHE B   9     9640   7692   8154  -1039  -2267  -3809       C  
ATOM   2583  O   PHE B   9      29.751  45.260  47.656  1.00 82.20           O  
ANISOU 2583  O   PHE B   9    11646   9571  10015  -1074  -2296  -3951       O  
ATOM   2584  CB  PHE B   9      32.029  43.362  46.783  1.00 65.68           C  
ANISOU 2584  CB  PHE B   9     9219   7675   8061  -1142  -2582  -3704       C  
ATOM   2585  CG  PHE B   9      32.391  43.774  45.380  1.00 64.49           C  
ANISOU 2585  CG  PHE B   9     8889   7384   8231  -1222  -2507  -3618       C  
ATOM   2586  CD1 PHE B   9      32.271  45.093  44.974  1.00 65.22           C  
ANISOU 2586  CD1 PHE B   9     8980   7282   8520  -1309  -2435  -3693       C  
ATOM   2587  CD2 PHE B   9      32.903  42.850  44.485  1.00 62.91           C  
ANISOU 2587  CD2 PHE B   9     8525   7255   8125  -1214  -2485  -3425       C  
ATOM   2588  CE1 PHE B   9      32.621  45.475  43.693  1.00 64.37           C  
ANISOU 2588  CE1 PHE B   9     8723   7045   8691  -1400  -2370  -3605       C  
ATOM   2589  CE2 PHE B   9      33.255  43.226  43.203  1.00 62.04           C  
ANISOU 2589  CE2 PHE B   9     8254   7036   8284  -1299  -2393  -3331       C  
ATOM   2590  CZ  PHE B   9      33.114  44.541  42.807  1.00 62.79           C  
ANISOU 2590  CZ  PHE B   9     8360   6935   8562  -1398  -2334  -3413       C  
ATOM   2591  N   ILE B  10      28.976  44.463  45.702  1.00 62.97           N  
ANISOU 2591  N   ILE B  10     9076   7069   7782  -1007  -2080  -3684       N  
ATOM   2592  CA  ILE B  10      27.922  45.456  45.532  1.00 63.14           C  
ANISOU 2592  CA  ILE B  10     9183   6932   7874   -974  -1937  -3777       C  
ATOM   2593  C   ILE B  10      26.606  44.743  45.820  1.00 63.89           C  
ANISOU 2593  C   ILE B  10     9388   7141   7747   -840  -1773  -3724       C  
ATOM   2594  O   ILE B  10      26.192  43.856  45.067  1.00 75.63           O  
ANISOU 2594  O   ILE B  10    10818   8686   9232   -788  -1658  -3519       O  
ATOM   2595  CB  ILE B  10      27.936  46.071  44.128  1.00 62.03           C  
ANISOU 2595  CB  ILE B  10     8929   6599   8039  -1027  -1846  -3665       C  
ATOM   2596  CG1 ILE B  10      29.308  46.677  43.829  1.00 63.27           C  
ANISOU 2596  CG1 ILE B  10     8964   6665   8411  -1184  -1998  -3701       C  
ATOM   2597  CG2 ILE B  10      26.854  47.129  44.003  1.00 62.50           C  
ANISOU 2597  CG2 ILE B  10     9087   6479   8182   -978  -1727  -3769       C  
ATOM   2598  CD1 ILE B  10      29.429  47.259  42.442  1.00 62.44           C  
ANISOU 2598  CD1 ILE B  10     8754   6380   8590  -1263  -1912  -3574       C  
ATOM   2599  N   GLU B  11      25.945  45.129  46.912  1.00 67.04           N  
ANISOU 2599  N   GLU B  11     9940   7576   7957   -791  -1756  -3918       N  
ATOM   2600  CA  GLU B  11      24.883  44.298  47.470  1.00 64.47           C  
ANISOU 2600  CA  GLU B  11     9721   7415   7361   -689  -1626  -3884       C  
ATOM   2601  C   GLU B  11      23.554  44.461  46.736  1.00 61.68           C  
ANISOU 2601  C   GLU B  11     9360   6985   7091   -601  -1401  -3826       C  
ATOM   2602  O   GLU B  11      22.826  43.480  46.555  1.00 60.16           O  
ANISOU 2602  O   GLU B  11     9172   6914   6773   -536  -1274  -3679       O  
ATOM   2603  CB  GLU B  11      24.708  44.606  48.958  1.00 83.81           C  
ANISOU 2603  CB  GLU B  11    12332   9962   9551   -682  -1669  -4087       C  
ATOM   2604  CG  GLU B  11      25.835  44.079  49.835  1.00 99.65           C  
ANISOU 2604  CG  GLU B  11    14366  12109  11387   -748  -1871  -4080       C  
ATOM   2605  CD  GLU B  11      25.689  44.486  51.289  1.00104.49           C  
ANISOU 2605  CD  GLU B  11    15141  12813  11749   -762  -1888  -4236       C  
ATOM   2606  OE1 GLU B  11      25.310  45.647  51.552  1.00106.85           O  
ANISOU 2606  OE1 GLU B  11    15485  12994  12120   -767  -1821  -4386       O  
ATOM   2607  OE2 GLU B  11      25.949  43.641  52.172  1.00110.74           O  
ANISOU 2607  OE2 GLU B  11    16020  13790  12267   -767  -1972  -4204       O  
ATOM   2608  N   GLY B  12      23.210  45.678  46.315  1.00 62.30           N  
ANISOU 2608  N   GLY B  12     9428   6860   7383   -596  -1357  -3940       N  
ATOM   2609  CA  GLY B  12      21.895  45.936  45.763  1.00 63.64           C  
ANISOU 2609  CA  GLY B  12     9599   6956   7626   -496  -1165  -3923       C  
ATOM   2610  C   GLY B  12      21.947  46.818  44.532  1.00 67.81           C  
ANISOU 2610  C   GLY B  12    10041   7240   8484   -518  -1152  -3863       C  
ATOM   2611  O   GLY B  12      23.017  47.230  44.080  1.00 72.75           O  
ANISOU 2611  O   GLY B  12    10603   7756   9283   -626  -1276  -3829       O  
ATOM   2612  N   GLY B  13      20.759  47.102  43.998  1.00 62.14           N  
ANISOU 2612  N   GLY B  13     9321   6441   7848   -418  -1000  -3849       N  
ATOM   2613  CA  GLY B  13      20.621  47.939  42.822  1.00 59.82           C  
ANISOU 2613  CA  GLY B  13     8970   5910   7850   -422   -981  -3780       C  
ATOM   2614  C   GLY B  13      20.032  49.303  43.118  1.00 69.65           C  
ANISOU 2614  C   GLY B  13    10288   6959   9215   -367   -971  -3983       C  
ATOM   2615  O   GLY B  13      19.457  49.522  44.189  1.00 66.11           O  
ANISOU 2615  O   GLY B  13     9923   6597   8600   -300   -918  -4136       O  
ATOM   2616  N   TRP B  14      20.160  50.228  42.170  1.00 72.64           N  
ANISOU 2616  N   TRP B  14    10639   7095   9864   -399   -998  -3918       N  
ATOM   2617  CA  TRP B  14      19.716  51.607  42.343  1.00 64.35           C  
ANISOU 2617  CA  TRP B  14     9658   5847   8945   -356   -992  -4027       C  
ATOM   2618  C   TRP B  14      18.486  51.852  41.478  1.00 63.65           C  
ANISOU 2618  C   TRP B  14     9548   5642   8995   -224   -879  -3962       C  
ATOM   2619  O   TRP B  14      18.590  51.927  40.249  1.00 65.33           O  
ANISOU 2619  O   TRP B  14     9709   5713   9401   -255   -892  -3797       O  
ATOM   2620  CB  TRP B  14      20.831  52.585  41.979  1.00 65.62           C  
ANISOU 2620  CB  TRP B  14     9822   5806   9306   -504  -1124  -3999       C  
ATOM   2621  CG  TRP B  14      22.036  52.486  42.855  1.00 77.77           C  
ANISOU 2621  CG  TRP B  14    11371   7448  10731   -631  -1248  -4078       C  
ATOM   2622  CD1 TRP B  14      22.088  52.003  44.129  1.00 76.94           C  
ANISOU 2622  CD1 TRP B  14    11318   7550  10367   -608  -1262  -4213       C  
ATOM   2623  CD2 TRP B  14      23.372  52.875  42.517  1.00 67.32           C  
ANISOU 2623  CD2 TRP B  14     9999   6032   9545   -806  -1378  -4021       C  
ATOM   2624  NE1 TRP B  14      23.374  52.071  44.608  1.00 72.30           N  
ANISOU 2624  NE1 TRP B  14    10719   6999   9752   -748  -1407  -4244       N  
ATOM   2625  CE2 TRP B  14      24.181  52.601  43.636  1.00 68.45           C  
ANISOU 2625  CE2 TRP B  14    10160   6336   9513   -871  -1477  -4134       C  
ATOM   2626  CE3 TRP B  14      23.961  53.428  41.376  1.00 67.17           C  
ANISOU 2626  CE3 TRP B  14     9925   5820   9777   -922  -1416  -3881       C  
ATOM   2627  CZ2 TRP B  14      25.548  52.862  43.649  1.00 69.42           C  
ANISOU 2627  CZ2 TRP B  14    10228   6433   9717  -1039  -1615  -4120       C  
ATOM   2628  CZ3 TRP B  14      25.316  53.687  41.390  1.00 68.15           C  
ANISOU 2628  CZ3 TRP B  14     9997   5923   9974  -1100  -1537  -3866       C  
ATOM   2629  CH2 TRP B  14      26.096  53.405  42.520  1.00 69.25           C  
ANISOU 2629  CH2 TRP B  14    10137   6227   9949  -1153  -1637  -3990       C  
ATOM   2630  N   THR B  15      17.325  51.989  42.120  1.00 64.59           N  
ANISOU 2630  N   THR B  15     9703   5825   9014    -79   -769  -4091       N  
ATOM   2631  CA  THR B  15      16.128  52.396  41.395  1.00 64.49           C  
ANISOU 2631  CA  THR B  15     9663   5690   9151     59   -679  -4054       C  
ATOM   2632  C   THR B  15      16.216  53.835  40.904  1.00 66.32           C  
ANISOU 2632  C   THR B  15     9939   5625   9634     53   -756  -4057       C  
ATOM   2633  O   THR B  15      15.520  54.194  39.948  1.00 66.01           O  
ANISOU 2633  O   THR B  15     9873   5436   9770    133   -729  -3960       O  
ATOM   2634  CB  THR B  15      14.886  52.238  42.273  1.00 65.43           C  
ANISOU 2634  CB  THR B  15     9792   5961   9105    210   -540  -4207       C  
ATOM   2635  OG1 THR B  15      15.083  52.933  43.510  1.00 68.02           O  
ANISOU 2635  OG1 THR B  15    10210   6305   9329    199   -568  -4407       O  
ATOM   2636  CG2 THR B  15      14.607  50.772  42.554  1.00 63.54           C  
ANISOU 2636  CG2 THR B  15     9508   6003   8631    221   -442  -4166       C  
ATOM   2637  N   GLY B  16      17.051  54.663  41.534  1.00 70.57           N  
ANISOU 2637  N   GLY B  16    10548   6075  10190    -44   -856  -4162       N  
ATOM   2638  CA  GLY B  16      17.183  56.059  41.153  1.00 78.09           C  
ANISOU 2638  CA  GLY B  16    11558   6743  11371    -64   -932  -4173       C  
ATOM   2639  C   GLY B  16      17.891  56.292  39.834  1.00 75.94           C  
ANISOU 2639  C   GLY B  16    11260   6283  11310   -186  -1009  -3957       C  
ATOM   2640  O   GLY B  16      17.824  57.408  39.306  1.00 78.23           O  
ANISOU 2640  O   GLY B  16    11601   6322  11800   -191  -1058  -3925       O  
ATOM   2641  N   MET B  17      18.569  55.282  39.297  1.00 67.29           N  
ANISOU 2641  N   MET B  17    10093   5303  10173   -288  -1020  -3807       N  
ATOM   2642  CA  MET B  17      19.224  55.374  37.996  1.00 70.65           C  
ANISOU 2642  CA  MET B  17    10484   5580  10780   -413  -1072  -3588       C  
ATOM   2643  C   MET B  17      18.294  54.759  36.956  1.00 64.14           C  
ANISOU 2643  C   MET B  17     9608   4760  10001   -305   -988  -3431       C  
ATOM   2644  O   MET B  17      18.054  53.548  36.970  1.00 71.74           O  
ANISOU 2644  O   MET B  17    10502   5929  10828   -263   -922  -3400       O  
ATOM   2645  CB  MET B  17      20.579  54.672  38.018  1.00 65.15           C  
ANISOU 2645  CB  MET B  17     9724   5007  10022   -595  -1137  -3527       C  
ATOM   2646  CG  MET B  17      21.332  54.752  36.705  1.00 74.22           C  
ANISOU 2646  CG  MET B  17    10827   6025  11348   -747  -1175  -3305       C  
ATOM   2647  SD  MET B  17      22.985  54.047  36.816  1.00 76.90           S  
ANISOU 2647  SD  MET B  17    11065   6516  11637   -962  -1255  -3262       S  
ATOM   2648  CE  MET B  17      22.613  52.374  37.332  1.00 77.60           C  
ANISOU 2648  CE  MET B  17    11082   6918  11485   -853  -1194  -3297       C  
ATOM   2649  N   VAL B  18      17.773  55.594  36.056  1.00 70.90           N  
ANISOU 2649  N   VAL B  18    10502   5389  11046   -260   -999  -3330       N  
ATOM   2650  CA  VAL B  18      16.712  55.203  35.140  1.00 75.61           C  
ANISOU 2650  CA  VAL B  18    11063   5971  11696   -128   -932  -3203       C  
ATOM   2651  C   VAL B  18      17.118  55.353  33.679  1.00 74.68           C  
ANISOU 2651  C   VAL B  18    10947   5688  11741   -235   -976  -2948       C  
ATOM   2652  O   VAL B  18      16.274  55.227  32.794  1.00 76.35           O  
ANISOU 2652  O   VAL B  18    11146   5842  12020   -134   -945  -2822       O  
ATOM   2653  CB  VAL B  18      15.421  55.997  35.420  1.00 78.20           C  
ANISOU 2653  CB  VAL B  18    11430   6203  12080     69   -899  -3319       C  
ATOM   2654  CG1 VAL B  18      14.972  55.803  36.858  1.00 73.40           C  
ANISOU 2654  CG1 VAL B  18    10817   5780  11290    167   -833  -3567       C  
ATOM   2655  CG2 VAL B  18      15.635  57.472  35.111  1.00 68.16           C  
ANISOU 2655  CG2 VAL B  18    10256   4640  11001     30   -993  -3305       C  
ATOM   2656  N   ASP B  19      18.393  55.624  33.402  1.00 73.43           N  
ANISOU 2656  N   ASP B  19    10801   5458  11641   -442  -1046  -2866       N  
ATOM   2657  CA  ASP B  19      18.842  55.853  32.033  1.00 73.71           C  
ANISOU 2657  CA  ASP B  19    10849   5340  11818   -570  -1076  -2619       C  
ATOM   2658  C   ASP B  19      19.864  54.828  31.558  1.00 70.73           C  
ANISOU 2658  C   ASP B  19    10377   5107  11392   -737  -1064  -2491       C  
ATOM   2659  O   ASP B  19      20.456  55.015  30.488  1.00 72.30           O  
ANISOU 2659  O   ASP B  19    10578   5202  11692   -885  -1081  -2290       O  
ATOM   2660  CB  ASP B  19      19.419  57.265  31.892  1.00 79.34           C  
ANISOU 2660  CB  ASP B  19    11661   5805  12680   -689  -1157  -2602       C  
ATOM   2661  CG  ASP B  19      20.534  57.541  32.878  1.00 89.39           C  
ANISOU 2661  CG  ASP B  19    12930   7125  13911   -832  -1208  -2753       C  
ATOM   2662  OD1 ASP B  19      20.557  56.885  33.938  1.00101.93           O  
ANISOU 2662  OD1 ASP B  19    14468   8915  15344   -777  -1190  -2924       O  
ATOM   2663  OD2 ASP B  19      21.385  58.413  32.596  1.00 81.00           O  
ANISOU 2663  OD2 ASP B  19    11914   5900  12960  -1002  -1268  -2698       O  
ATOM   2664  N   GLY B  20      20.086  53.756  32.307  1.00 71.22           N  
ANISOU 2664  N   GLY B  20    10351   5445  11264   -717  -1016  -2569       N  
ATOM   2665  CA  GLY B  20      21.056  52.763  31.882  1.00 57.76           C  
ANISOU 2665  CA  GLY B  20     8537   3951   9458   -854   -977  -2407       C  
ATOM   2666  C   GLY B  20      21.130  51.619  32.866  1.00 56.42           C  
ANISOU 2666  C   GLY B  20     8293   4079   9064   -794   -935  -2505       C  
ATOM   2667  O   GLY B  20      20.431  51.592  33.884  1.00 56.82           O  
ANISOU 2667  O   GLY B  20     8383   4186   9021   -660   -924  -2692       O  
ATOM   2668  N   TRP B  21      22.004  50.667  32.543  1.00 54.98           N  
ANISOU 2668  N   TRP B  21     8007   4088   8795   -897   -911  -2374       N  
ATOM   2669  CA  TRP B  21      22.180  49.459  33.343  1.00 53.67           C  
ANISOU 2669  CA  TRP B  21     7772   4202   8417   -851   -883  -2423       C  
ATOM   2670  C   TRP B  21      23.290  49.629  34.375  1.00 55.00           C  
ANISOU 2670  C   TRP B  21     7927   4417   8554   -958   -991  -2585       C  
ATOM   2671  O   TRP B  21      23.063  49.461  35.576  1.00 55.52           O  
ANISOU 2671  O   TRP B  21     8033   4578   8483   -883  -1018  -2765       O  
ATOM   2672  CB  TRP B  21      22.481  48.266  32.430  1.00 53.76           C  
ANISOU 2672  CB  TRP B  21     7676   4394   8357   -882   -809  -2203       C  
ATOM   2673  CG  TRP B  21      21.271  47.644  31.810  1.00 49.84           C  
ANISOU 2673  CG  TRP B  21     7181   3955   7799   -740   -702  -2085       C  
ATOM   2674  CD1 TRP B  21      20.015  47.587  32.339  1.00 58.40           C  
ANISOU 2674  CD1 TRP B  21     8318   5057   8814   -574   -654  -2179       C  
ATOM   2675  CD2 TRP B  21      21.201  46.987  30.540  1.00 48.24           C  
ANISOU 2675  CD2 TRP B  21     6918   3808   7601   -757   -629  -1861       C  
ATOM   2676  NE1 TRP B  21      19.170  46.931  31.479  1.00 48.12           N  
ANISOU 2676  NE1 TRP B  21     6985   3816   7482   -490   -564  -2025       N  
ATOM   2677  CE2 TRP B  21      19.873  46.555  30.366  1.00 47.17           C  
ANISOU 2677  CE2 TRP B  21     6804   3717   7402   -597   -552  -1829       C  
ATOM   2678  CE3 TRP B  21      22.134  46.723  29.532  1.00 47.75           C  
ANISOU 2678  CE3 TRP B  21     6782   3772   7588   -895   -618  -1696       C  
ATOM   2679  CZ2 TRP B  21      19.452  45.873  29.226  1.00 45.86           C  
ANISOU 2679  CZ2 TRP B  21     6595   3611   7218   -571   -478  -1637       C  
ATOM   2680  CZ3 TRP B  21      21.716  46.046  28.402  1.00 46.22           C  
ANISOU 2680  CZ3 TRP B  21     6552   3644   7366   -866   -534  -1508       C  
ATOM   2681  CH2 TRP B  21      20.386  45.629  28.257  1.00 45.16           C  
ANISOU 2681  CH2 TRP B  21     6448   3543   7166   -705   -472  -1480       C  
ATOM   2682  N   TYR B  22      24.495  49.949  33.917  1.00 55.71           N  
ANISOU 2682  N   TYR B  22     7956   4450   8762  -1139  -1052  -2525       N  
ATOM   2683  CA  TYR B  22      25.647  50.149  34.784  1.00 66.94           C  
ANISOU 2683  CA  TYR B  22     9344   5910  10182  -1258  -1171  -2671       C  
ATOM   2684  C   TYR B  22      25.980  51.634  34.824  1.00 62.97           C  
ANISOU 2684  C   TYR B  22     8915   5128   9881  -1372  -1259  -2778       C  
ATOM   2685  O   TYR B  22      26.057  52.283  33.774  1.00 67.55           O  
ANISOU 2685  O   TYR B  22     9508   5525  10634  -1463  -1238  -2644       O  
ATOM   2686  CB  TYR B  22      26.850  49.344  34.289  1.00 58.83           C  
ANISOU 2686  CB  TYR B  22     8162   5043   9148  -1387  -1178  -2542       C  
ATOM   2687  CG  TYR B  22      26.477  48.120  33.478  1.00 53.87           C  
ANISOU 2687  CG  TYR B  22     7462   4587   8420  -1310  -1061  -2343       C  
ATOM   2688  CD1 TYR B  22      25.808  47.052  34.061  1.00 52.40           C  
ANISOU 2688  CD1 TYR B  22     7286   4590   8032  -1155  -1020  -2357       C  
ATOM   2689  CD2 TYR B  22      26.807  48.027  32.132  1.00 53.19           C  
ANISOU 2689  CD2 TYR B  22     7302   4474   8434  -1402   -991  -2143       C  
ATOM   2690  CE1 TYR B  22      25.471  45.932  33.327  1.00 50.28           C  
ANISOU 2690  CE1 TYR B  22     6956   4465   7682  -1090   -921  -2184       C  
ATOM   2691  CE2 TYR B  22      26.474  46.909  31.389  1.00 51.07           C  
ANISOU 2691  CE2 TYR B  22     6972   4360   8072  -1331   -889  -1978       C  
ATOM   2692  CZ  TYR B  22      25.806  45.864  31.993  1.00 49.60           C  
ANISOU 2692  CZ  TYR B  22     6796   4347   7703  -1173   -859  -2002       C  
ATOM   2693  OH  TYR B  22      25.468  44.745  31.267  1.00 47.62           O  
ANISOU 2693  OH  TYR B  22     6488   4237   7368  -1107   -765  -1845       O  
ATOM   2694  N   GLY B  23      26.178  52.171  36.023  1.00 63.12           N  
ANISOU 2694  N   GLY B  23     8994   5111   9876  -1373  -1363  -3016       N  
ATOM   2695  CA  GLY B  23      26.401  53.594  36.146  1.00 63.97           C  
ANISOU 2695  CA  GLY B  23     9189   4989  10128  -1455  -1422  -3087       C  
ATOM   2696  C   GLY B  23      27.137  53.978  37.413  1.00 65.97           C  
ANISOU 2696  C   GLY B  23     9459   5306  10302  -1510  -1526  -3277       C  
ATOM   2697  O   GLY B  23      27.733  53.140  38.095  1.00 67.92           O  
ANISOU 2697  O   GLY B  23     9631   5765  10410  -1522  -1580  -3343       O  
ATOM   2698  N   TYR B  24      27.076  55.271  37.714  1.00 75.36           N  
ANISOU 2698  N   TYR B  24    10753   6301  11579  -1538  -1561  -3362       N  
ATOM   2699  CA  TYR B  24      27.832  55.909  38.779  1.00 70.82           C  
ANISOU 2699  CA  TYR B  24    10207   5730  10971  -1620  -1666  -3534       C  
ATOM   2700  C   TYR B  24      26.885  56.582  39.767  1.00 73.36           C  
ANISOU 2700  C   TYR B  24    10674   5988  11212  -1468  -1658  -3725       C  
ATOM   2701  O   TYR B  24      25.665  56.598  39.593  1.00 81.54           O  
ANISOU 2701  O   TYR B  24    11776   6973  12233  -1303  -1570  -3721       O  
ATOM   2702  CB  TYR B  24      28.805  56.947  38.215  1.00 72.85           C  
ANISOU 2702  CB  TYR B  24    10450   5800  11429  -1832  -1719  -3470       C  
ATOM   2703  CG  TYR B  24      29.769  56.436  37.170  1.00 71.81           C  
ANISOU 2703  CG  TYR B  24    10169   5722  11394  -2004  -1708  -3281       C  
ATOM   2704  CD1 TYR B  24      30.910  55.736  37.534  1.00 71.69           C  
ANISOU 2704  CD1 TYR B  24    10008   5910  11322  -2109  -1778  -3308       C  
ATOM   2705  CD2 TYR B  24      29.558  56.685  35.820  1.00 71.20           C  
ANISOU 2705  CD2 TYR B  24    10094   5495  11464  -2064  -1628  -3077       C  
ATOM   2706  CE1 TYR B  24      31.803  55.279  36.583  1.00 70.97           C  
ANISOU 2706  CE1 TYR B  24     9760   5880  11325  -2264  -1756  -3149       C  
ATOM   2707  CE2 TYR B  24      30.447  56.234  34.861  1.00 70.47           C  
ANISOU 2707  CE2 TYR B  24     9862   5465  11450  -2231  -1600  -2909       C  
ATOM   2708  CZ  TYR B  24      31.567  55.531  35.248  1.00 74.50           C  
ANISOU 2708  CZ  TYR B  24    10212   6186  11910  -2330  -1659  -2952       C  
ATOM   2709  OH  TYR B  24      32.454  55.078  34.298  1.00 81.95           O  
ANISOU 2709  OH  TYR B  24    10996   7207  12935  -2491  -1619  -2797       O  
ATOM   2710  N   HIS B  25      27.480  57.164  40.811  1.00 92.11           N  
ANISOU 2710  N   HIS B  25    13090   8368  13539  -1530  -1752  -3897       N  
ATOM   2711  CA  HIS B  25      26.734  57.967  41.780  1.00 97.94           C  
ANISOU 2711  CA  HIS B  25    13966   9031  14216  -1415  -1750  -4096       C  
ATOM   2712  C   HIS B  25      27.750  58.864  42.486  1.00 98.60           C  
ANISOU 2712  C   HIS B  25    14078   9044  14343  -1565  -1872  -4228       C  
ATOM   2713  O   HIS B  25      28.514  58.388  43.330  1.00 97.59           O  
ANISOU 2713  O   HIS B  25    13907   9098  14076  -1622  -1955  -4319       O  
ATOM   2714  CB  HIS B  25      25.981  57.092  42.767  1.00 99.85           C  
ANISOU 2714  CB  HIS B  25    14236   9501  14202  -1245  -1703  -4216       C  
ATOM   2715  CG  HIS B  25      25.483  57.828  43.969  1.00111.69           C  
ANISOU 2715  CG  HIS B  25    15860  10976  15602  -1161  -1712  -4447       C  
ATOM   2716  ND1 HIS B  25      24.371  58.642  43.940  1.00111.74           N  
ANISOU 2716  ND1 HIS B  25    15960  10819  15678  -1028  -1637  -4516       N  
ATOM   2717  CD2 HIS B  25      25.951  57.876  45.239  1.00115.65           C  
ANISOU 2717  CD2 HIS B  25    16406  11599  15938  -1190  -1790  -4626       C  
ATOM   2718  CE1 HIS B  25      24.173  59.155  45.141  1.00109.21           C  
ANISOU 2718  CE1 HIS B  25    15732  10522  15240   -979  -1658  -4736       C  
ATOM   2719  NE2 HIS B  25      25.118  58.706  45.947  1.00112.83           N  
ANISOU 2719  NE2 HIS B  25    16170  11153  15548  -1081  -1750  -4804       N  
ATOM   2720  N   HIS B  26      27.747  60.148  42.141  1.00 95.04           N  
ANISOU 2720  N   HIS B  26    13703   8327  14080  -1627  -1888  -4238       N  
ATOM   2721  CA  HIS B  26      28.741  61.077  42.656  1.00 84.72           C  
ANISOU 2721  CA  HIS B  26    12422   6923  12846  -1792  -2001  -4349       C  
ATOM   2722  C   HIS B  26      28.112  62.028  43.665  1.00 97.98           C  
ANISOU 2722  C   HIS B  26    14248   8493  14486  -1691  -2018  -4575       C  
ATOM   2723  O   HIS B  26      26.949  62.418  43.535  1.00 88.90           O  
ANISOU 2723  O   HIS B  26    13185   7227  13366  -1530  -1939  -4601       O  
ATOM   2724  CB  HIS B  26      29.398  61.875  41.521  1.00 87.42           C  
ANISOU 2724  CB  HIS B  26    12742   7037  13435  -1980  -2016  -4190       C  
ATOM   2725  CG  HIS B  26      28.514  62.924  40.923  1.00 89.78           C  
ANISOU 2725  CG  HIS B  26    13167   7052  13894  -1912  -1963  -4153       C  
ATOM   2726  ND1 HIS B  26      28.373  64.179  41.474  1.00100.20           N  
ANISOU 2726  ND1 HIS B  26    14614   8168  15292  -1913  -2013  -4310       N  
ATOM   2727  CD2 HIS B  26      27.731  62.908  39.818  1.00 97.80           C  
ANISOU 2727  CD2 HIS B  26    14202   7950  15007  -1837  -1875  -3976       C  
ATOM   2728  CE1 HIS B  26      27.539  64.890  40.737  1.00 96.33           C  
ANISOU 2728  CE1 HIS B  26    14213   7444  14945  -1835  -1960  -4231       C  
ATOM   2729  NE2 HIS B  26      27.136  64.143  39.725  1.00 88.96           N  
ANISOU 2729  NE2 HIS B  26    13217   6560  14022  -1788  -1879  -4025       N  
ATOM   2730  N   GLN B  27      28.896  62.393  44.678  1.00114.95           N  
ANISOU 2730  N   GLN B  27    16418  10688  16571  -1786  -2126  -4746       N  
ATOM   2731  CA  GLN B  27      28.457  63.331  45.711  1.00119.37           C  
ANISOU 2731  CA  GLN B  27    17116  11150  17088  -1715  -2154  -4981       C  
ATOM   2732  C   GLN B  27      29.653  64.201  46.082  1.00117.75           C  
ANISOU 2732  C   GLN B  27    16919  10842  16979  -1921  -2287  -5072       C  
ATOM   2733  O   GLN B  27      30.551  63.753  46.799  1.00120.18           O  
ANISOU 2733  O   GLN B  27    17168  11332  17164  -2014  -2382  -5143       O  
ATOM   2734  CB  GLN B  27      27.907  62.602  46.932  1.00119.89           C  
ANISOU 2734  CB  GLN B  27    17218  11462  16871  -1564  -2131  -5145       C  
ATOM   2735  CG  GLN B  27      27.468  63.541  48.045  1.00130.52           C  
ANISOU 2735  CG  GLN B  27    18706  12727  18157  -1494  -2152  -5401       C  
ATOM   2736  CD  GLN B  27      27.385  62.862  49.396  1.00132.00           C  
ANISOU 2736  CD  GLN B  27    18930  13182  18042  -1426  -2166  -5569       C  
ATOM   2737  OE1 GLN B  27      27.673  61.673  49.527  1.00124.44           O  
ANISOU 2737  OE1 GLN B  27    17895  12470  16918  -1430  -2170  -5490       O  
ATOM   2738  NE2 GLN B  27      26.994  63.620  50.415  1.00132.09           N  
ANISOU 2738  NE2 GLN B  27    19065  13146  17976  -1366  -2175  -5801       N  
ATOM   2739  N   ASN B  28      29.661  65.436  45.596  1.00109.46           N  
ANISOU 2739  N   ASN B  28    15943   9499  16147  -1993  -2300  -5067       N  
ATOM   2740  CA  ASN B  28      30.706  66.399  45.906  1.00100.87           C  
ANISOU 2740  CA  ASN B  28    14879   8277  15172  -2193  -2419  -5159       C  
ATOM   2741  C   ASN B  28      30.073  67.672  46.469  1.00123.04           C  
ANISOU 2741  C   ASN B  28    17852  10851  18046  -2118  -2432  -5353       C  
ATOM   2742  O   ASN B  28      28.870  67.724  46.748  1.00120.50           O  
ANISOU 2742  O   ASN B  28    17613  10511  17660  -1904  -2353  -5434       O  
ATOM   2743  CB  ASN B  28      31.566  66.686  44.670  1.00100.78           C  
ANISOU 2743  CB  ASN B  28    14787   8126  15380  -2408  -2429  -4945       C  
ATOM   2744  CG  ASN B  28      30.753  67.170  43.478  1.00100.14           C  
ANISOU 2744  CG  ASN B  28    14768   7808  15475  -2351  -2331  -4775       C  
ATOM   2745  OD1 ASN B  28      29.594  67.561  43.609  1.00100.45           O  
ANISOU 2745  OD1 ASN B  28    14919   7735  15515  -2160  -2277  -4843       O  
ATOM   2746  ND2 ASN B  28      31.369  67.149  42.301  1.00 99.43           N  
ANISOU 2746  ND2 ASN B  28    14602   7646  15530  -2520  -2309  -4552       N  
ATOM   2747  N   GLU B  29      30.901  68.709  46.623  1.00129.71           N  
ANISOU 2747  N   GLU B  29    18738  11516  19028  -2298  -2531  -5431       N  
ATOM   2748  CA  GLU B  29      30.418  69.975  47.165  1.00133.94           C  
ANISOU 2748  CA  GLU B  29    19432  11813  19645  -2245  -2558  -5626       C  
ATOM   2749  C   GLU B  29      29.292  70.551  46.314  1.00133.12           C  
ANISOU 2749  C   GLU B  29    19412  11467  19699  -2103  -2464  -5533       C  
ATOM   2750  O   GLU B  29      28.367  71.184  46.839  1.00138.74           O  
ANISOU 2750  O   GLU B  29    20241  12064  20409  -1936  -2442  -5699       O  
ATOM   2751  CB  GLU B  29      31.577  70.968  47.273  1.00147.34           C  
ANISOU 2751  CB  GLU B  29    21150  13341  21493  -2492  -2680  -5688       C  
ATOM   2752  CG  GLU B  29      31.193  72.333  47.822  1.00152.04           C  
ANISOU 2752  CG  GLU B  29    21911  13667  22189  -2459  -2722  -5896       C  
ATOM   2753  CD  GLU B  29      30.772  72.288  49.278  1.00156.76           C  
ANISOU 2753  CD  GLU B  29    22583  14405  22572  -2316  -2751  -6179       C  
ATOM   2754  OE1 GLU B  29      31.152  71.331  49.984  1.00156.31           O  
ANISOU 2754  OE1 GLU B  29    22451  14646  22294  -2316  -2779  -6229       O  
ATOM   2755  OE2 GLU B  29      30.057  73.213  49.718  1.00159.80           O  
ANISOU 2755  OE2 GLU B  29    23105  14603  23008  -2204  -2746  -6353       O  
ATOM   2756  N   GLN B  30      29.346  70.335  44.998  1.00118.67           N  
ANISOU 2756  N   GLN B  30    17523   9561  18004  -2164  -2411  -5269       N  
ATOM   2757  CA  GLN B  30      28.319  70.861  44.108  1.00118.51           C  
ANISOU 2757  CA  GLN B  30    17580   9310  18137  -2035  -2336  -5156       C  
ATOM   2758  C   GLN B  30      27.024  70.063  44.164  1.00124.08           C  
ANISOU 2758  C   GLN B  30    18272  10165  18709  -1765  -2229  -5153       C  
ATOM   2759  O   GLN B  30      26.018  70.505  43.597  1.00117.63           O  
ANISOU 2759  O   GLN B  30    17519   9172  18002  -1617  -2174  -5098       O  
ATOM   2760  CB  GLN B  30      28.833  70.897  42.668  1.00118.20           C  
ANISOU 2760  CB  GLN B  30    17492   9146  18272  -2205  -2314  -4868       C  
ATOM   2761  CG  GLN B  30      30.207  71.536  42.512  1.00116.39           C  
ANISOU 2761  CG  GLN B  30    17248   8809  18167  -2503  -2400  -4843       C  
ATOM   2762  CD  GLN B  30      30.565  71.797  41.062  1.00119.75           C  
ANISOU 2762  CD  GLN B  30    17658   9065  18775  -2668  -2359  -4566       C  
ATOM   2763  OE1 GLN B  30      31.658  71.459  40.609  1.00112.96           O  
ANISOU 2763  OE1 GLN B  30    16689   8293  17937  -2894  -2368  -4443       O  
ATOM   2764  NE2 GLN B  30      29.644  72.409  40.327  1.00127.94           N  
ANISOU 2764  NE2 GLN B  30    18806   9863  19943  -2555  -2313  -4467       N  
ATOM   2765  N   GLY B  31      27.017  68.914  44.827  1.00129.58           N  
ANISOU 2765  N   GLY B  31    18886  11176  19173  -1700  -2202  -5208       N  
ATOM   2766  CA  GLY B  31      25.831  68.097  44.938  1.00124.99           C  
ANISOU 2766  CA  GLY B  31    18285  10757  18448  -1462  -2093  -5211       C  
ATOM   2767  C   GLY B  31      26.107  66.664  44.549  1.00118.54           C  
ANISOU 2767  C   GLY B  31    17332  10209  17499  -1484  -2047  -5044       C  
ATOM   2768  O   GLY B  31      27.238  66.269  44.271  1.00117.20           O  
ANISOU 2768  O   GLY B  31    17075  10119  17337  -1675  -2104  -4941       O  
ATOM   2769  N   SER B  32      25.041  65.877  44.532  1.00104.61           N  
ANISOU 2769  N   SER B  32    15544   8587  15614  -1284  -1942  -5024       N  
ATOM   2770  CA  SER B  32      25.106  64.459  44.221  1.00102.17           C  
ANISOU 2770  CA  SER B  32    15117   8536  15165  -1271  -1888  -4882       C  
ATOM   2771  C   SER B  32      24.218  64.154  43.020  1.00102.33           C  
ANISOU 2771  C   SER B  32    15108   8488  15285  -1160  -1790  -4681       C  
ATOM   2772  O   SER B  32      23.515  65.015  42.501  1.00 93.28           O  
ANISOU 2772  O   SER B  32    14032   7108  14301  -1081  -1770  -4657       O  
ATOM   2773  CB  SER B  32      24.692  63.623  45.432  1.00 93.82           C  
ANISOU 2773  CB  SER B  32    14059   7760  13829  -1146  -1851  -5050       C  
ATOM   2774  OG  SER B  32      23.414  64.022  45.890  1.00 94.17           O  
ANISOU 2774  OG  SER B  32    14184   7760  13835   -940  -1768  -5193       O  
ATOM   2775  N   GLY B  33      24.259  62.909  42.581  1.00101.45           N  
ANISOU 2775  N   GLY B  33    14891   8580  15074  -1153  -1739  -4535       N  
ATOM   2776  CA  GLY B  33      23.450  62.482  41.460  1.00105.52           C  
ANISOU 2776  CA  GLY B  33    15370   9060  15662  -1053  -1650  -4343       C  
ATOM   2777  C   GLY B  33      23.893  61.153  40.892  1.00 94.86           C  
ANISOU 2777  C   GLY B  33    13896   7918  14230  -1114  -1620  -4170       C  
ATOM   2778  O   GLY B  33      25.027  60.690  41.079  1.00 97.05           O  
ANISOU 2778  O   GLY B  33    14101   8318  14453  -1272  -1683  -4150       O  
ATOM   2779  N   TYR B  34      22.953  60.520  40.195  1.00 93.06           N  
ANISOU 2779  N   TYR B  34    13635   7730  13995   -978  -1526  -4049       N  
ATOM   2780  CA  TYR B  34      23.186  59.301  39.439  1.00 77.88           C  
ANISOU 2780  CA  TYR B  34    11601   5965  12024  -1015  -1485  -3863       C  
ATOM   2781  C   TYR B  34      23.411  59.634  37.970  1.00 75.17           C  
ANISOU 2781  C   TYR B  34    11244   5432  11886  -1116  -1483  -3624       C  
ATOM   2782  O   TYR B  34      22.881  60.619  37.452  1.00 82.38           O  
ANISOU 2782  O   TYR B  34    12242   6107  12953  -1076  -1483  -3583       O  
ATOM   2783  CB  TYR B  34      22.002  58.342  39.558  1.00 73.56           C  
ANISOU 2783  CB  TYR B  34    11026   5589  11334   -811  -1377  -3874       C  
ATOM   2784  CG  TYR B  34      21.733  57.780  40.941  1.00 76.58           C  
ANISOU 2784  CG  TYR B  34    11420   6204  11473   -719  -1353  -4078       C  
ATOM   2785  CD1 TYR B  34      22.487  56.728  41.445  1.00 73.44           C  
ANISOU 2785  CD1 TYR B  34    10957   6046  10900   -794  -1382  -4085       C  
ATOM   2786  CD2 TYR B  34      20.689  58.267  41.721  1.00 75.28           C  
ANISOU 2786  CD2 TYR B  34    11330   6026  11245   -554  -1298  -4257       C  
ATOM   2787  CE1 TYR B  34      22.229  56.195  42.694  1.00 76.81           C  
ANISOU 2787  CE1 TYR B  34    11413   6688  11083   -717  -1362  -4251       C  
ATOM   2788  CE2 TYR B  34      20.425  57.739  42.971  1.00 75.86           C  
ANISOU 2788  CE2 TYR B  34    11423   6323  11077   -483  -1261  -4432       C  
ATOM   2789  CZ  TYR B  34      21.198  56.704  43.452  1.00 84.51           C  
ANISOU 2789  CZ  TYR B  34    12473   7651  11988   -569  -1295  -4421       C  
ATOM   2790  OH  TYR B  34      20.942  56.175  44.695  1.00 80.03           O  
ANISOU 2790  OH  TYR B  34    11942   7304  11159   -507  -1262  -4578       O  
ATOM   2791  N   ALA B  35      24.198  58.798  37.298  1.00 73.27           N  
ANISOU 2791  N   ALA B  35    10898   5301  11640  -1247  -1482  -3462       N  
ATOM   2792  CA  ALA B  35      24.422  58.954  35.867  1.00 72.66           C  
ANISOU 2792  CA  ALA B  35    10802   5082  11725  -1354  -1462  -3219       C  
ATOM   2793  C   ALA B  35      24.950  57.642  35.314  1.00 75.10           C  
ANISOU 2793  C   ALA B  35    10973   5596  11964  -1425  -1427  -3078       C  
ATOM   2794  O   ALA B  35      25.943  57.111  35.819  1.00 85.18           O  
ANISOU 2794  O   ALA B  35    12160   7038  13166  -1535  -1473  -3132       O  
ATOM   2795  CB  ALA B  35      25.404  60.091  35.579  1.00 75.21           C  
ANISOU 2795  CB  ALA B  35    11168   5203  12206  -1565  -1532  -3182       C  
ATOM   2796  N   ALA B  36      24.300  57.138  34.269  1.00 68.08           N  
ANISOU 2796  N   ALA B  36    10066   4694  11109  -1360  -1354  -2901       N  
ATOM   2797  CA  ALA B  36      24.658  55.850  33.696  1.00 65.50           C  
ANISOU 2797  CA  ALA B  36     9612   4557  10720  -1405  -1311  -2772       C  
ATOM   2798  C   ALA B  36      25.848  55.984  32.756  1.00 67.85           C  
ANISOU 2798  C   ALA B  36     9838   4807  11134  -1646  -1324  -2598       C  
ATOM   2799  O   ALA B  36      25.890  56.890  31.916  1.00 71.98           O  
ANISOU 2799  O   ALA B  36    10433   5119  11797  -1737  -1320  -2467       O  
ATOM   2800  CB  ALA B  36      23.465  55.257  32.949  1.00 65.23           C  
ANISOU 2800  CB  ALA B  36     9585   4527  10671  -1241  -1226  -2656       C  
ATOM   2801  N   ASP B  37      26.811  55.075  32.892  1.00 74.10           N  
ANISOU 2801  N   ASP B  37    10487   5804  11862  -1751  -1335  -2596       N  
ATOM   2802  CA  ASP B  37      27.922  55.006  31.951  1.00 76.10           C  
ANISOU 2802  CA  ASP B  37    10637   6064  12214  -1975  -1321  -2431       C  
ATOM   2803  C   ASP B  37      27.413  54.495  30.609  1.00 74.00           C  
ANISOU 2803  C   ASP B  37    10354   5775  11987  -1961  -1226  -2205       C  
ATOM   2804  O   ASP B  37      26.906  53.373  30.516  1.00 81.24           O  
ANISOU 2804  O   ASP B  37    11213   6913  12741  -1818  -1144  -2140       O  
ATOM   2805  CB  ASP B  37      29.025  54.101  32.490  1.00 76.11           C  
ANISOU 2805  CB  ASP B  37    10468   6311  12138  -2062  -1362  -2504       C  
ATOM   2806  CG  ASP B  37      30.254  54.089  31.603  1.00 84.13           C  
ANISOU 2806  CG  ASP B  37    11350   7354  13261  -2300  -1339  -2361       C  
ATOM   2807  OD1 ASP B  37      30.472  55.081  30.877  1.00 89.45           O  
ANISOU 2807  OD1 ASP B  37    12089   7838  14061  -2441  -1318  -2249       O  
ATOM   2808  OD2 ASP B  37      31.003  53.091  31.631  1.00 85.77           O  
ANISOU 2808  OD2 ASP B  37    11388   7786  13414  -2345  -1335  -2356       O  
ATOM   2809  N   GLN B  38      27.555  55.317  29.569  1.00 68.47           N  
ANISOU 2809  N   GLN B  38     9717   4888  11412  -2091  -1199  -2030       N  
ATOM   2810  CA  GLN B  38      26.922  55.022  28.289  1.00 71.04           C  
ANISOU 2810  CA  GLN B  38    10070   5170  11753  -2061  -1113  -1802       C  
ATOM   2811  C   GLN B  38      27.726  54.038  27.448  1.00 70.60           C  
ANISOU 2811  C   GLN B  38     9855   5353  11616  -2180  -1010  -1626       C  
ATOM   2812  O   GLN B  38      27.146  53.316  26.628  1.00 76.32           O  
ANISOU 2812  O   GLN B  38    10567   6187  12245  -2090   -914  -1461       O  
ATOM   2813  CB  GLN B  38      26.702  56.321  27.515  1.00 82.89           C  
ANISOU 2813  CB  GLN B  38    11725   6389  13380  -2138  -1122  -1671       C  
ATOM   2814  CG  GLN B  38      25.893  57.351  28.285  1.00105.60           C  
ANISOU 2814  CG  GLN B  38    14752   9080  16289  -1988  -1188  -1821       C  
ATOM   2815  CD  GLN B  38      26.261  58.778  27.925  1.00123.91           C  
ANISOU 2815  CD  GLN B  38    17192  11148  18739  -2133  -1221  -1762       C  
ATOM   2816  OE1 GLN B  38      26.918  59.029  26.914  1.00127.37           O  
ANISOU 2816  OE1 GLN B  38    17628  11532  19236  -2332  -1179  -1570       O  
ATOM   2817  NE2 GLN B  38      25.845  59.722  28.762  1.00122.93           N  
ANISOU 2817  NE2 GLN B  38    17176  10875  18657  -2038  -1288  -1930       N  
ATOM   2818  N   LYS B  39      29.046  53.989  27.631  1.00 73.62           N  
ANISOU 2818  N   LYS B  39    10108   5825  12041  -2376  -1031  -1669       N  
ATOM   2819  CA  LYS B  39      29.867  53.087  26.830  1.00 78.20           C  
ANISOU 2819  CA  LYS B  39    10520   6634  12560  -2489   -929  -1523       C  
ATOM   2820  C   LYS B  39      29.612  51.631  27.204  1.00 71.85           C  
ANISOU 2820  C   LYS B  39     9607   6132  11562  -2304   -882  -1552       C  
ATOM   2821  O   LYS B  39      29.321  50.798  26.337  1.00 74.61           O  
ANISOU 2821  O   LYS B  39     9913   6619  11818  -2251   -774  -1392       O  
ATOM   2822  CB  LYS B  39      31.347  53.438  26.993  1.00 78.99           C  
ANISOU 2822  CB  LYS B  39    10487   6753  12772  -2742   -969  -1586       C  
ATOM   2823  CG  LYS B  39      32.275  52.606  26.121  1.00 87.77           C  
ANISOU 2823  CG  LYS B  39    11407   8094  13846  -2873   -856  -1452       C  
ATOM   2824  CD  LYS B  39      33.703  53.126  26.166  1.00 96.63           C  
ANISOU 2824  CD  LYS B  39    12394   9208  15113  -3147   -888  -1507       C  
ATOM   2825  CE  LYS B  39      34.311  52.974  27.550  1.00108.92           C  
ANISOU 2825  CE  LYS B  39    13852  10857  16674  -3119  -1025  -1755       C  
ATOM   2826  NZ  LYS B  39      35.720  53.457  27.582  1.00106.80           N  
ANISOU 2826  NZ  LYS B  39    13450  10640  16488  -3357  -1049  -1784       N  
ATOM   2827  N   SER B  40      29.712  51.308  28.495  1.00 67.88           N  
ANISOU 2827  N   SER B  40     9070   5729  10992  -2209   -967  -1755       N  
ATOM   2828  CA  SER B  40      29.507  49.931  28.936  1.00 63.23           C  
ANISOU 2828  CA  SER B  40     8394   5413  10218  -2044   -937  -1780       C  
ATOM   2829  C   SER B  40      28.069  49.487  28.693  1.00 56.99           C  
ANISOU 2829  C   SER B  40     7708   4629   9317  -1831   -866  -1706       C  
ATOM   2830  O   SER B  40      27.821  48.396  28.160  1.00 58.66           O  
ANISOU 2830  O   SER B  40     7854   5020   9414  -1752   -778  -1589       O  
ATOM   2831  CB  SER B  40      29.874  49.798  30.415  1.00 64.04           C  
ANISOU 2831  CB  SER B  40     8471   5598  10262  -1997  -1059  -2009       C  
ATOM   2832  OG  SER B  40      29.134  50.710  31.207  1.00 69.16           O  
ANISOU 2832  OG  SER B  40     9279   6058  10938  -1921  -1130  -2157       O  
ATOM   2833  N   THR B  41      27.106  50.326  29.083  1.00 56.67           N  
ANISOU 2833  N   THR B  41     7822   4392   9317  -1735   -906  -1783       N  
ATOM   2834  CA  THR B  41      25.702  50.018  28.835  1.00 57.10           C  
ANISOU 2834  CA  THR B  41     7964   4440   9293  -1537   -842  -1724       C  
ATOM   2835  C   THR B  41      25.442  49.786  27.352  1.00 53.14           C  
ANISOU 2835  C   THR B  41     7456   3928   8806  -1568   -745  -1482       C  
ATOM   2836  O   THR B  41      24.758  48.825  26.978  1.00 51.19           O  
ANISOU 2836  O   THR B  41     7183   3829   8439  -1440   -668  -1395       O  
ATOM   2837  CB  THR B  41      24.818  51.146  29.368  1.00 55.52           C  
ANISOU 2837  CB  THR B  41     7918   3998   9180  -1448   -906  -1852       C  
ATOM   2838  OG1 THR B  41      24.857  51.146  30.800  1.00 56.10           O  
ANISOU 2838  OG1 THR B  41     8001   4129   9184  -1381   -977  -2088       O  
ATOM   2839  CG2 THR B  41      23.381  50.975  28.907  1.00 54.39           C  
ANISOU 2839  CG2 THR B  41     7848   3821   8996  -1260   -842  -1775       C  
ATOM   2840  N   GLN B  42      26.001  50.639  26.490  1.00 54.66           N  
ANISOU 2840  N   GLN B  42     7676   3952   9138  -1748   -749  -1371       N  
ATOM   2841  CA  GLN B  42      25.784  50.473  25.057  1.00 54.07           C  
ANISOU 2841  CA  GLN B  42     7615   3869   9061  -1792   -660  -1136       C  
ATOM   2842  C   GLN B  42      26.416  49.186  24.540  1.00 52.42           C  
ANISOU 2842  C   GLN B  42     7246   3939   8731  -1829   -564  -1044       C  
ATOM   2843  O   GLN B  42      25.846  48.517  23.671  1.00 50.98           O  
ANISOU 2843  O   GLN B  42     7062   3845   8463  -1757   -482   -899       O  
ATOM   2844  CB  GLN B  42      26.328  51.679  24.296  1.00 56.45           C  
ANISOU 2844  CB  GLN B  42     7991   3931   9524  -2002   -683  -1032       C  
ATOM   2845  CG  GLN B  42      25.974  51.656  22.823  1.00 59.35           C  
ANISOU 2845  CG  GLN B  42     8414   4261   9876  -2044   -603   -784       C  
ATOM   2846  CD  GLN B  42      24.479  51.572  22.598  1.00 62.33           C  
ANISOU 2846  CD  GLN B  42     8903   4573  10206  -1819   -610   -738       C  
ATOM   2847  OE1 GLN B  42      23.698  52.210  23.305  1.00 73.65           O  
ANISOU 2847  OE1 GLN B  42    10435   5842  11706  -1687   -693   -861       O  
ATOM   2848  NE2 GLN B  42      24.070  50.776  21.618  1.00 55.96           N  
ANISOU 2848  NE2 GLN B  42     8073   3901   9288  -1771   -524   -573       N  
ATOM   2849  N   ASN B  43      27.598  48.829  25.051  1.00 52.75           N  
ANISOU 2849  N   ASN B  43     7148   4120   8774  -1936   -582  -1134       N  
ATOM   2850  CA  ASN B  43      28.207  47.561  24.660  1.00 51.32           C  
ANISOU 2850  CA  ASN B  43     6804   4204   8489  -1946   -503  -1075       C  
ATOM   2851  C   ASN B  43      27.320  46.386  25.047  1.00 49.02           C  
ANISOU 2851  C   ASN B  43     6509   4079   8038  -1721   -479  -1097       C  
ATOM   2852  O   ASN B  43      27.132  45.452  24.257  1.00 47.55           O  
ANISOU 2852  O   ASN B  43     6269   4035   7762  -1675   -390   -978       O  
ATOM   2853  CB  ASN B  43      29.590  47.421  25.295  1.00 52.44           C  
ANISOU 2853  CB  ASN B  43     6790   4457   8676  -2075   -554  -1197       C  
ATOM   2854  CG  ASN B  43      30.643  48.253  24.588  1.00 80.99           C  
ANISOU 2854  CG  ASN B  43    10354   7982  12437  -2334   -531  -1134       C  
ATOM   2855  OD1 ASN B  43      30.570  48.466  23.377  1.00 78.02           O  
ANISOU 2855  OD1 ASN B  43    10009   7557  12078  -2427   -436   -958       O  
ATOM   2856  ND2 ASN B  43      31.632  48.726  25.342  1.00 82.91           N  
ANISOU 2856  ND2 ASN B  43    10518   8206  12778  -2461   -619  -1276       N  
ATOM   2857  N   ALA B  44      26.758  46.420  26.258  1.00 48.85           N  
ANISOU 2857  N   ALA B  44     6546   4041   7973  -1586   -554  -1253       N  
ATOM   2858  CA  ALA B  44      25.859  45.353  26.684  1.00 46.91           C  
ANISOU 2858  CA  ALA B  44     6308   3943   7573  -1388   -526  -1273       C  
ATOM   2859  C   ALA B  44      24.622  45.288  25.796  1.00 45.88           C  
ANISOU 2859  C   ALA B  44     6262   3755   7415  -1284   -451  -1138       C  
ATOM   2860  O   ALA B  44      24.163  44.197  25.432  1.00 44.15           O  
ANISOU 2860  O   ALA B  44     6001   3689   7083  -1188   -385  -1063       O  
ATOM   2861  CB  ALA B  44      25.466  45.558  28.146  1.00 47.34           C  
ANISOU 2861  CB  ALA B  44     6425   3980   7581  -1285   -610  -1468       C  
ATOM   2862  N   ILE B  45      24.072  46.450  25.433  1.00 47.08           N  
ANISOU 2862  N   ILE B  45     6532   3679   7677  -1301   -473  -1108       N  
ATOM   2863  CA  ILE B  45      22.901  46.484  24.562  1.00 46.40           C  
ANISOU 2863  CA  ILE B  45     6527   3524   7580  -1200   -426   -980       C  
ATOM   2864  C   ILE B  45      23.225  45.877  23.203  1.00 45.61           C  
ANISOU 2864  C   ILE B  45     6369   3521   7439  -1280   -340   -784       C  
ATOM   2865  O   ILE B  45      22.426  45.119  22.641  1.00 44.51           O  
ANISOU 2865  O   ILE B  45     6230   3472   7210  -1171   -284   -696       O  
ATOM   2866  CB  ILE B  45      22.377  47.926  24.426  1.00 51.61           C  
ANISOU 2866  CB  ILE B  45     7328   3897   8387  -1209   -491   -985       C  
ATOM   2867  CG1 ILE B  45      21.872  48.443  25.773  1.00 48.99           C  
ANISOU 2867  CG1 ILE B  45     7052   3483   8079  -1096   -564  -1202       C  
ATOM   2868  CG2 ILE B  45      21.280  47.999  23.381  1.00 47.81           C  
ANISOU 2868  CG2 ILE B  45     6923   3337   7906  -1118   -461   -832       C  
ATOM   2869  CD1 ILE B  45      21.459  49.893  25.744  1.00 51.08           C  
ANISOU 2869  CD1 ILE B  45     7452   3447   8509  -1100   -642  -1238       C  
ATOM   2870  N   ASN B  46      24.398  46.200  22.653  1.00 46.69           N  
ANISOU 2870  N   ASN B  46     6455   3647   7640  -1476   -325   -721       N  
ATOM   2871  CA  ASN B  46      24.788  45.643  21.361  1.00 47.73           C  
ANISOU 2871  CA  ASN B  46     6528   3886   7721  -1566   -229   -549       C  
ATOM   2872  C   ASN B  46      24.952  44.130  21.443  1.00 44.28           C  
ANISOU 2872  C   ASN B  46     5961   3714   7151  -1482   -170   -567       C  
ATOM   2873  O   ASN B  46      24.450  43.391  20.587  1.00 43.09           O  
ANISOU 2873  O   ASN B  46     5805   3657   6911  -1423   -100   -454       O  
ATOM   2874  CB  ASN B  46      26.082  46.296  20.875  1.00 48.03           C  
ANISOU 2874  CB  ASN B  46     6518   3877   7854  -1808   -212   -502       C  
ATOM   2875  CG  ASN B  46      25.927  47.781  20.620  1.00 55.79           C  
ANISOU 2875  CG  ASN B  46     7649   4576   8973  -1911   -268   -451       C  
ATOM   2876  OD1 ASN B  46      24.816  48.283  20.467  1.00 61.18           O  
ANISOU 2876  OD1 ASN B  46     8473   5099   9674  -1799   -309   -409       O  
ATOM   2877  ND2 ASN B  46      27.049  48.493  20.570  1.00 57.69           N  
ANISOU 2877  ND2 ASN B  46     7854   4747   9320  -2128   -276   -458       N  
ATOM   2878  N   GLY B  47      25.647  43.650  22.476  1.00 44.10           N  
ANISOU 2878  N   GLY B  47     5838   3806   7112  -1473   -209   -710       N  
ATOM   2879  CA  GLY B  47      25.890  42.220  22.589  1.00 42.54           C  
ANISOU 2879  CA  GLY B  47     5523   3840   6802  -1396   -171   -726       C  
ATOM   2880  C   GLY B  47      24.615  41.423  22.785  1.00 40.79           C  
ANISOU 2880  C   GLY B  47     5358   3675   6466  -1202   -155   -717       C  
ATOM   2881  O   GLY B  47      24.413  40.381  22.154  1.00 39.50           O  
ANISOU 2881  O   GLY B  47     5146   3645   6215  -1148    -90   -640       O  
ATOM   2882  N   ILE B  48      23.731  41.907  23.658  1.00 40.89           N  
ANISOU 2882  N   ILE B  48     5468   3585   6481  -1098   -211   -805       N  
ATOM   2883  CA  ILE B  48      22.488  41.189  23.922  1.00 39.45           C  
ANISOU 2883  CA  ILE B  48     5330   3463   6197   -924   -189   -810       C  
ATOM   2884  C   ILE B  48      21.548  41.280  22.724  1.00 38.99           C  
ANISOU 2884  C   ILE B  48     5328   3346   6140   -886   -134   -666       C  
ATOM   2885  O   ILE B  48      20.843  40.316  22.394  1.00 39.80           O  
ANISOU 2885  O   ILE B  48     5414   3557   6150   -788    -87   -614       O  
ATOM   2886  CB  ILE B  48      21.841  41.723  25.211  1.00 39.98           C  
ANISOU 2886  CB  ILE B  48     5474   3453   6265   -833   -251   -962       C  
ATOM   2887  CG1 ILE B  48      22.738  41.416  26.407  1.00 40.35           C  
ANISOU 2887  CG1 ILE B  48     5467   3592   6272   -860   -313  -1100       C  
ATOM   2888  CG2 ILE B  48      20.463  41.126  25.414  1.00 43.20           C  
ANISOU 2888  CG2 ILE B  48     5922   3911   6583   -668   -212   -965       C  
ATOM   2889  CD1 ILE B  48      22.265  42.044  27.686  1.00 54.64           C  
ANISOU 2889  CD1 ILE B  48     7359   5330   8073   -795   -374  -1264       C  
ATOM   2890  N   THR B  49      21.528  42.432  22.049  1.00 40.29           N  
ANISOU 2890  N   THR B  49     5568   3333   6409   -966   -151   -595       N  
ATOM   2891  CA  THR B  49      20.750  42.559  20.821  1.00 40.13           C  
ANISOU 2891  CA  THR B  49     5610   3254   6385   -944   -117   -442       C  
ATOM   2892  C   THR B  49      21.209  41.541  19.786  1.00 39.18           C  
ANISOU 2892  C   THR B  49     5409   3301   6174   -996    -34   -324       C  
ATOM   2893  O   THR B  49      20.388  40.877  19.140  1.00 38.12           O  
ANISOU 2893  O   THR B  49     5286   3233   5965   -909      2   -247       O  
ATOM   2894  CB  THR B  49      20.870  43.981  20.266  1.00 42.03           C  
ANISOU 2894  CB  THR B  49     5953   3266   6751  -1048   -160   -371       C  
ATOM   2895  OG1 THR B  49      20.244  44.904  21.165  1.00 42.97           O  
ANISOU 2895  OG1 THR B  49     6154   3213   6959   -967   -240   -490       O  
ATOM   2896  CG2 THR B  49      20.201  44.078  18.899  1.00 42.08           C  
ANISOU 2896  CG2 THR B  49     6030   3221   6736  -1042   -137   -190       C  
ATOM   2897  N   ASN B  50      22.526  41.398  19.623  1.00 39.67           N  
ANISOU 2897  N   ASN B  50     5383   3440   6248  -1139     -4   -323       N  
ATOM   2898  CA  ASN B  50      23.050  40.418  18.679  1.00 38.97           C  
ANISOU 2898  CA  ASN B  50     5206   3523   6079  -1187     82   -238       C  
ATOM   2899  C   ASN B  50      22.769  38.992  19.134  1.00 37.21           C  
ANISOU 2899  C   ASN B  50     4907   3478   5753  -1052     99   -299       C  
ATOM   2900  O   ASN B  50      22.609  38.098  18.297  1.00 45.32           O  
ANISOU 2900  O   ASN B  50     5900   4620   6700  -1026    161   -225       O  
ATOM   2901  CB  ASN B  50      24.551  40.631  18.483  1.00 44.01           C  
ANISOU 2901  CB  ASN B  50     5744   4208   6771  -1369    114   -247       C  
ATOM   2902  CG  ASN B  50      25.121  39.775  17.373  1.00 60.28           C  
ANISOU 2902  CG  ASN B  50     7713   6436   8757  -1431    217   -164       C  
ATOM   2903  OD1 ASN B  50      25.058  40.139  16.197  1.00 70.03           O  
ANISOU 2903  OD1 ASN B  50     9000   7637   9970  -1521    277    -30       O  
ATOM   2904  ND2 ASN B  50      25.693  38.634  17.740  1.00 66.18           N  
ANISOU 2904  ND2 ASN B  50     8325   7360   9460  -1382    235   -247       N  
ATOM   2905  N   LYS B  51      22.707  38.756  20.445  1.00 36.82           N  
ANISOU 2905  N   LYS B  51     4841   3450   5700   -971     41   -431       N  
ATOM   2906  CA  LYS B  51      22.395  37.417  20.937  1.00 36.98           C  
ANISOU 2906  CA  LYS B  51     4812   3621   5620   -850     49   -476       C  
ATOM   2907  C   LYS B  51      20.958  37.030  20.606  1.00 48.39           C  
ANISOU 2907  C   LYS B  51     6327   5059   7002   -725     73   -420       C  
ATOM   2908  O   LYS B  51      20.711  35.977  20.003  1.00 49.84           O  
ANISOU 2908  O   LYS B  51     6474   5354   7109   -681    121   -365       O  
ATOM   2909  CB  LYS B  51      22.642  37.336  22.443  1.00 35.69           C  
ANISOU 2909  CB  LYS B  51     4637   3475   5449   -805    -24   -620       C  
ATOM   2910  CG  LYS B  51      21.985  36.133  23.086  1.00 41.08           C  
ANISOU 2910  CG  LYS B  51     5319   4270   6021   -672    -24   -654       C  
ATOM   2911  CD  LYS B  51      22.144  36.132  24.592  1.00 38.46           C  
ANISOU 2911  CD  LYS B  51     5003   3951   5657   -634    -99   -786       C  
ATOM   2912  CE  LYS B  51      23.430  35.455  25.010  1.00 40.66           C  
ANISOU 2912  CE  LYS B  51     5183   4341   5925   -674   -147   -834       C  
ATOM   2913  NZ  LYS B  51      23.369  35.038  26.435  1.00 41.90           N  
ANISOU 2913  NZ  LYS B  51     5374   4547   5999   -606   -222   -937       N  
ATOM   2914  N   VAL B  52      19.994  37.869  21.000  1.00 36.16           N  
ANISOU 2914  N   VAL B  52     4869   3379   5491   -665     38   -446       N  
ATOM   2915  CA  VAL B  52      18.595  37.593  20.678  1.00 33.93           C  
ANISOU 2915  CA  VAL B  52     4634   3088   5169   -547     55   -404       C  
ATOM   2916  C   VAL B  52      18.406  37.492  19.170  1.00 33.81           C  
ANISOU 2916  C   VAL B  52     4632   3077   5140   -582     95   -256       C  
ATOM   2917  O   VAL B  52      17.683  36.616  18.675  1.00 36.00           O  
ANISOU 2917  O   VAL B  52     4896   3439   5345   -510    126   -209       O  
ATOM   2918  CB  VAL B  52      17.680  38.671  21.289  1.00 40.44           C  
ANISOU 2918  CB  VAL B  52     5541   3760   6064   -478      7   -470       C  
ATOM   2919  CG1 VAL B  52      16.224  38.395  20.936  1.00 34.18           C  
ANISOU 2919  CG1 VAL B  52     4773   2968   5246   -353     23   -435       C  
ATOM   2920  CG2 VAL B  52      17.867  38.733  22.794  1.00 35.01           C  
ANISOU 2920  CG2 VAL B  52     4850   3088   5366   -447    -25   -627       C  
ATOM   2921  N   ASN B  53      19.057  38.384  18.417  1.00 35.18           N  
ANISOU 2921  N   ASN B  53     4836   3158   5374   -704     93   -179       N  
ATOM   2922  CA  ASN B  53      18.976  38.319  16.962  1.00 35.15           C  
ANISOU 2922  CA  ASN B  53     4857   3167   5333   -757    133    -32       C  
ATOM   2923  C   ASN B  53      19.491  36.986  16.441  1.00 36.28           C  
ANISOU 2923  C   ASN B  53     4907   3503   5376   -771    204    -13       C  
ATOM   2924  O   ASN B  53      18.890  36.395  15.541  1.00 38.87           O  
ANISOU 2924  O   ASN B  53     5248   3890   5630   -731    233     65       O  
ATOM   2925  CB  ASN B  53      19.756  39.473  16.333  1.00 36.84           C  
ANISOU 2925  CB  ASN B  53     5121   3259   5616   -914    129     47       C  
ATOM   2926  CG  ASN B  53      18.953  40.753  16.270  1.00 38.02           C  
ANISOU 2926  CG  ASN B  53     5399   3191   5855   -887     53     89       C  
ATOM   2927  OD1 ASN B  53      17.731  40.742  16.417  1.00 37.59           O  
ANISOU 2927  OD1 ASN B  53     5388   3092   5803   -745     11     76       O  
ATOM   2928  ND2 ASN B  53      19.635  41.865  16.034  1.00 39.69           N  
ANISOU 2928  ND2 ASN B  53     5669   3261   6150  -1026     32    136       N  
ATOM   2929  N   SER B  54      20.601  36.495  16.994  1.00 41.16           N  
ANISOU 2929  N   SER B  54     5427   4216   5994   -821    224    -91       N  
ATOM   2930  CA  SER B  54      21.131  35.206  16.561  1.00 38.96           C  
ANISOU 2930  CA  SER B  54     5054   4112   5639   -818    283    -93       C  
ATOM   2931  C   SER B  54      20.157  34.080  16.876  1.00 41.00           C  
ANISOU 2931  C   SER B  54     5312   4443   5824   -674    275   -120       C  
ATOM   2932  O   SER B  54      19.971  33.162  16.066  1.00 57.23           O  
ANISOU 2932  O   SER B  54     7343   6594   7806   -649    319    -76       O  
ATOM   2933  CB  SER B  54      22.483  34.944  17.225  1.00 40.66           C  
ANISOU 2933  CB  SER B  54     5157   4403   5891   -880    281   -187       C  
ATOM   2934  OG  SER B  54      23.449  35.896  16.814  1.00 47.20           O  
ANISOU 2934  OG  SER B  54     5964   5182   6789  -1036    303   -159       O  
ATOM   2935  N   VAL B  55      19.521  34.138  18.048  1.00 37.82           N  
ANISOU 2935  N   VAL B  55     4938   3997   5435   -585    224   -198       N  
ATOM   2936  CA  VAL B  55      18.552  33.112  18.422  1.00 35.40           C  
ANISOU 2936  CA  VAL B  55     4634   3756   5060   -466    224   -222       C  
ATOM   2937  C   VAL B  55      17.391  33.091  17.436  1.00 39.78           C  
ANISOU 2937  C   VAL B  55     5238   4288   5587   -421    240   -134       C  
ATOM   2938  O   VAL B  55      16.962  32.026  16.977  1.00 47.66           O  
ANISOU 2938  O   VAL B  55     6214   5377   6518   -375    266   -110       O  
ATOM   2939  CB  VAL B  55      18.065  33.336  19.865  1.00 37.91           C  
ANISOU 2939  CB  VAL B  55     4981   4033   5389   -398    179   -321       C  
ATOM   2940  CG1 VAL B  55      16.949  32.358  20.213  1.00 39.78           C  
ANISOU 2940  CG1 VAL B  55     5228   4334   5555   -294    193   -334       C  
ATOM   2941  CG2 VAL B  55      19.224  33.200  20.839  1.00 30.61           C  
ANISOU 2941  CG2 VAL B  55     4010   3148   4472   -438    145   -408       C  
ATOM   2942  N   ILE B  56      16.873  34.270  17.086  1.00 36.31           N  
ANISOU 2942  N   ILE B  56     4869   3722   5206   -431    213    -87       N  
ATOM   2943  CA  ILE B  56      15.757  34.329  16.146  1.00 33.42           C  
ANISOU 2943  CA  ILE B  56     4551   3328   4820   -381    205     -2       C  
ATOM   2944  C   ILE B  56      16.199  33.898  14.750  1.00 40.43           C  
ANISOU 2944  C   ILE B  56     5434   4288   5641   -452    247    100       C  
ATOM   2945  O   ILE B  56      15.454  33.225  14.027  1.00 39.25           O  
ANISOU 2945  O   ILE B  56     5289   4197   5429   -403    253    144       O  
ATOM   2946  CB  ILE B  56      15.144  35.742  16.144  1.00 35.76           C  
ANISOU 2946  CB  ILE B  56     4929   3452   5206   -364    146     21       C  
ATOM   2947  CG1 ILE B  56      14.587  36.073  17.530  1.00 31.85           C  
ANISOU 2947  CG1 ILE B  56     4432   2903   4766   -278    116   -104       C  
ATOM   2948  CG2 ILE B  56      14.062  35.861  15.082  1.00 32.07           C  
ANISOU 2948  CG2 ILE B  56     4510   2950   4725   -311    115    119       C  
ATOM   2949  CD1 ILE B  56      13.995  37.452  17.638  1.00 34.19           C  
ANISOU 2949  CD1 ILE B  56     4803   3021   5169   -243     52   -110       C  
ATOM   2950  N   GLU B  57      17.422  34.262  14.356  1.00 43.82           N  
ANISOU 2950  N   GLU B  57     5849   4724   6078   -574    280    128       N  
ATOM   2951  CA  GLU B  57      17.904  33.943  13.016  1.00 46.82           C  
ANISOU 2951  CA  GLU B  57     6224   5181   6382   -656    337    218       C  
ATOM   2952  C   GLU B  57      18.116  32.447  12.841  1.00 44.85           C  
ANISOU 2952  C   GLU B  57     5893   5095   6054   -616    386    171       C  
ATOM   2953  O   GLU B  57      17.876  31.904  11.757  1.00 48.02           O  
ANISOU 2953  O   GLU B  57     6306   5568   6371   -621    418    228       O  
ATOM   2954  CB  GLU B  57      19.199  34.699  12.728  1.00 61.06           C  
ANISOU 2954  CB  GLU B  57     8016   6965   8219   -810    377    246       C  
ATOM   2955  CG  GLU B  57      19.015  36.179  12.458  1.00 82.21           C  
ANISOU 2955  CG  GLU B  57    10804   9469  10961   -878    333    333       C  
ATOM   2956  CD  GLU B  57      20.324  36.942  12.514  1.00 81.58           C  
ANISOU 2956  CD  GLU B  57    10699   9356  10941  -1040    368    335       C  
ATOM   2957  OE1 GLU B  57      21.388  36.293  12.590  1.00 84.53           O  
ANISOU 2957  OE1 GLU B  57    10958   9863  11298  -1099    434    275       O  
ATOM   2958  OE2 GLU B  57      20.288  38.190  12.488  1.00 78.75           O  
ANISOU 2958  OE2 GLU B  57    10432   8833  10656  -1106    323    393       O  
ATOM   2959  N   LYS B  58      18.574  31.762  13.890  1.00 51.54           N  
ANISOU 2959  N   LYS B  58     6664   5997   6923   -576    385     66       N  
ATOM   2960  CA  LYS B  58      18.741  30.318  13.784  1.00 42.21           C  
ANISOU 2960  CA  LYS B  58     5413   4943   5680   -527    415     20       C  
ATOM   2961  C   LYS B  58      17.415  29.570  13.778  1.00 47.36           C  
ANISOU 2961  C   LYS B  58     6101   5607   6288   -421    389     26       C  
ATOM   2962  O   LYS B  58      17.411  28.361  13.526  1.00 48.14           O  
ANISOU 2962  O   LYS B  58     6161   5796   6335   -383    409     -1       O  
ATOM   2963  CB  LYS B  58      19.621  29.800  14.920  1.00 39.57           C  
ANISOU 2963  CB  LYS B  58     5000   4651   5384   -511    400    -83       C  
ATOM   2964  CG  LYS B  58      21.024  30.378  14.917  1.00 40.83           C  
ANISOU 2964  CG  LYS B  58     5093   4824   5597   -619    424   -108       C  
ATOM   2965  CD  LYS B  58      21.676  30.238  13.554  1.00 36.13           C  
ANISOU 2965  CD  LYS B  58     4459   4312   4959   -705    508    -60       C  
ATOM   2966  CE  LYS B  58      23.031  30.920  13.527  1.00 42.61           C  
ANISOU 2966  CE  LYS B  58     5201   5147   5841   -833    544    -82       C  
ATOM   2967  NZ  LYS B  58      23.668  30.849  12.184  1.00 49.17           N  
ANISOU 2967  NZ  LYS B  58     5993   6072   6619   -934    647    -36       N  
ATOM   2968  N   MET B  59      16.301  30.245  14.052  1.00 61.85           N  
ANISOU 2968  N   MET B  59     7999   7350   8152   -372    344     50       N  
ATOM   2969  CA  MET B  59      14.973  29.639  13.974  1.00 52.97           C  
ANISOU 2969  CA  MET B  59     6892   6238   6996   -283    322     55       C  
ATOM   2970  C   MET B  59      14.356  30.079  12.649  1.00 59.90           C  
ANISOU 2970  C   MET B  59     7824   7093   7841   -297    308    154       C  
ATOM   2971  O   MET B  59      13.711  31.124  12.557  1.00 76.28           O  
ANISOU 2971  O   MET B  59     9955   9065   9962   -282    261    198       O  
ATOM   2972  CB  MET B  59      14.112  30.039  15.167  1.00 56.02           C  
ANISOU 2972  CB  MET B  59     7292   6556   7437   -212    285      1       C  
ATOM   2973  CG  MET B  59      14.621  29.538  16.507  1.00 53.41           C  
ANISOU 2973  CG  MET B  59     6926   6257   7110   -197    291    -90       C  
ATOM   2974  SD  MET B  59      14.890  27.756  16.534  1.00 58.56           S  
ANISOU 2974  SD  MET B  59     7530   7030   7691   -175    314   -117       S  
ATOM   2975  CE  MET B  59      13.289  27.147  16.012  1.00 70.01           C  
ANISOU 2975  CE  MET B  59     8994   8497   9109   -114    313    -86       C  
ATOM   2976  N   ASN B  60      14.570  29.272  11.614  1.00 59.46           N  
ANISOU 2976  N   ASN B  60     7757   7131   7703   -323    342    183       N  
ATOM   2977  CA  ASN B  60      14.074  29.603  10.288  1.00 62.97           C  
ANISOU 2977  CA  ASN B  60     8265   7573   8089   -346    324    280       C  
ATOM   2978  C   ASN B  60      12.553  29.486  10.236  1.00 76.19           C  
ANISOU 2978  C   ASN B  60     9959   9217   9773   -251    256    290       C  
ATOM   2979  O   ASN B  60      11.929  28.759  11.015  1.00 80.76           O  
ANISOU 2979  O   ASN B  60    10489   9819  10377   -181    249    219       O  
ATOM   2980  CB  ASN B  60      14.707  28.693   9.236  1.00 72.36           C  
ANISOU 2980  CB  ASN B  60     9433   8885   9173   -396    384    286       C  
ATOM   2981  CG  ASN B  60      16.214  28.839   9.170  1.00 77.44           C  
ANISOU 2981  CG  ASN B  60    10036   9574   9814   -493    460    268       C  
ATOM   2982  OD1 ASN B  60      16.949  27.859   9.287  1.00 89.45           O  
ANISOU 2982  OD1 ASN B  60    11480  11189  11317   -490    509    190       O  
ATOM   2983  ND2 ASN B  60      16.682  30.068   8.984  1.00 81.85           N  
ANISOU 2983  ND2 ASN B  60    10640  10061  10398   -579    465    336       N  
ATOM   2984  N   THR B  61      11.962  30.216   9.292  1.00 76.34           N  
ANISOU 2984  N   THR B  61    10050   9186   9771   -255    202    385       N  
ATOM   2985  CA  THR B  61      10.510  30.289   9.188  1.00 69.71           C  
ANISOU 2985  CA  THR B  61     9218   8309   8960   -162    119    395       C  
ATOM   2986  C   THR B  61       9.908  28.914   8.928  1.00 63.13           C  
ANISOU 2986  C   THR B  61     8331   7586   8068   -122    126    348       C  
ATOM   2987  O   THR B  61      10.317  28.206   8.003  1.00 74.31           O  
ANISOU 2987  O   THR B  61     9759   9091   9384   -169    155    366       O  
ATOM   2988  CB  THR B  61      10.110  31.253   8.069  1.00 71.07           C  
ANISOU 2988  CB  THR B  61     9488   8411   9106   -177     43    518       C  
ATOM   2989  OG1 THR B  61      10.529  32.581   8.404  1.00 83.52           O  
ANISOU 2989  OG1 THR B  61    11122   9852  10759   -209     22    561       O  
ATOM   2990  CG2 THR B  61       8.604  31.237   7.865  1.00 69.46           C  
ANISOU 2990  CG2 THR B  61     9274   8183   8936    -70    -57    521       C  
ATOM   2991  N   GLN B  62       8.935  28.539   9.754  1.00 52.05           N  
ANISOU 2991  N   GLN B  62     6869   6178   6729    -43    105    279       N  
ATOM   2992  CA  GLN B  62       8.182  27.308   9.545  1.00 45.79           C  
ANISOU 2992  CA  GLN B  62     6026   5471   5901    -12     99    237       C  
ATOM   2993  C   GLN B  62       7.118  27.543   8.482  1.00 48.35           C  
ANISOU 2993  C   GLN B  62     6375   5792   6205     24      8    294       C  
ATOM   2994  O   GLN B  62       6.203  28.350   8.680  1.00 55.97           O  
ANISOU 2994  O   GLN B  62     7330   6684   7250     89    -61    306       O  
ATOM   2995  CB  GLN B  62       7.539  26.846  10.850  1.00 49.92           C  
ANISOU 2995  CB  GLN B  62     6478   5995   6496     40    121    148       C  
ATOM   2996  CG  GLN B  62       6.549  25.706  10.678  1.00 58.58           C  
ANISOU 2996  CG  GLN B  62     7520   7160   7577     64    107    110       C  
ATOM   2997  CD  GLN B  62       7.224  24.385  10.374  1.00 68.81           C  
ANISOU 2997  CD  GLN B  62     8816   8532   8796     17    150     86       C  
ATOM   2998  OE1 GLN B  62       8.261  24.057  10.949  1.00 76.74           O  
ANISOU 2998  OE1 GLN B  62     9826   9544   9789    -12    206     59       O  
ATOM   2999  NE2 GLN B  62       6.637  23.617   9.463  1.00 74.64           N  
ANISOU 2999  NE2 GLN B  62     9549   9324   9489     15    115     87       N  
ATOM   3000  N   PHE B  63       7.230  26.839   7.360  1.00 45.18           N  
ANISOU 3000  N   PHE B  63     5999   5469   5698    -13      0    322       N  
ATOM   3001  CA  PHE B  63       6.281  26.989   6.269  1.00 45.03           C  
ANISOU 3001  CA  PHE B  63     6011   5460   5638     15   -101    377       C  
ATOM   3002  C   PHE B  63       5.164  25.953   6.410  1.00 46.91           C  
ANISOU 3002  C   PHE B  63     6165   5756   5904     62   -133    302       C  
ATOM   3003  O   PHE B  63       5.036  25.282   7.437  1.00 53.60           O  
ANISOU 3003  O   PHE B  63     6939   6618   6810     74    -76    220       O  
ATOM   3004  CB  PHE B  63       7.009  26.907   4.929  1.00 46.25           C  
ANISOU 3004  CB  PHE B  63     6254   5673   5646    -61    -95    448       C  
ATOM   3005  CG  PHE B  63       7.885  28.098   4.648  1.00 54.25           C  
ANISOU 3005  CG  PHE B  63     7357   6620   6635   -120    -78    544       C  
ATOM   3006  CD1 PHE B  63       7.337  29.281   4.180  1.00 52.63           C  
ANISOU 3006  CD1 PHE B  63     7229   6320   6449    -98   -182    648       C  
ATOM   3007  CD2 PHE B  63       9.252  28.040   4.865  1.00 44.45           C  
ANISOU 3007  CD2 PHE B  63     6118   5406   5364   -201     34    530       C  
ATOM   3008  CE1 PHE B  63       8.136  30.382   3.927  1.00 51.71           C  
ANISOU 3008  CE1 PHE B  63     7207   6126   6314   -167   -169    746       C  
ATOM   3009  CE2 PHE B  63      10.056  29.138   4.614  1.00 44.77           C  
ANISOU 3009  CE2 PHE B  63     6234   5386   5390   -275     54    619       C  
ATOM   3010  CZ  PHE B  63       9.495  30.310   4.144  1.00 46.92           C  
ANISOU 3010  CZ  PHE B  63     6599   5554   5676   -265    -45    731       C  
ATOM   3011  N   THR B  64       4.343  25.818   5.371  1.00 42.72           N  
ANISOU 3011  N   THR B  64     5648   5258   5325     81   -229    333       N  
ATOM   3012  CA  THR B  64       3.109  25.048   5.474  1.00 38.87           C  
ANISOU 3012  CA  THR B  64     5068   4812   4887    125   -281    266       C  
ATOM   3013  C   THR B  64       3.386  23.583   5.782  1.00 36.45           C  
ANISOU 3013  C   THR B  64     4719   4579   4552     80   -202    180       C  
ATOM   3014  O   THR B  64       4.172  22.923   5.095  1.00 42.87           O  
ANISOU 3014  O   THR B  64     5585   5446   5257     27   -167    178       O  
ATOM   3015  CB  THR B  64       2.308  25.169   4.180  1.00 45.28           C  
ANISOU 3015  CB  THR B  64     5913   5652   5639    146   -415    316       C  
ATOM   3016  OG1 THR B  64       1.941  26.537   3.973  1.00 49.56           O  
ANISOU 3016  OG1 THR B  64     6498   6105   6229    202   -510    400       O  
ATOM   3017  CG2 THR B  64       1.051  24.315   4.250  1.00 46.78           C  
ANISOU 3017  CG2 THR B  64     5991   5894   5888    179   -471    236       C  
ATOM   3018  N   ALA B  65       2.727  23.077   6.822  1.00 44.71           N  
ANISOU 3018  N   ALA B  65     5671   5624   5694    101   -172    107       N  
ATOM   3019  CA  ALA B  65       2.842  21.674   7.211  1.00 46.32           C  
ANISOU 3019  CA  ALA B  65     5841   5873   5886     57   -111     35       C  
ATOM   3020  C   ALA B  65       1.542  21.276   7.891  1.00 42.38           C  
ANISOU 3020  C   ALA B  65     5234   5384   5485     76   -126    -23       C  
ATOM   3021  O   ALA B  65       1.307  21.649   9.043  1.00 47.04           O  
ANISOU 3021  O   ALA B  65     5774   5945   6155     96    -74    -47       O  
ATOM   3022  CB  ALA B  65       4.037  21.450   8.134  1.00 47.40           C  
ANISOU 3022  CB  ALA B  65     6004   5989   6019     29     -6     18       C  
ATOM   3023  N   VAL B  66       0.703  20.527   7.185  1.00 37.41           N  
ANISOU 3023  N   VAL B  66     4565   4803   4847     62   -191    -53       N  
ATOM   3024  CA  VAL B  66      -0.599  20.132   7.691  1.00 40.38           C  
ANISOU 3024  CA  VAL B  66     4821   5201   5321     65   -208   -111       C  
ATOM   3025  C   VAL B  66      -0.603  18.626   7.935  1.00 39.49           C  
ANISOU 3025  C   VAL B  66     4696   5113   5196    -12   -161   -168       C  
ATOM   3026  O   VAL B  66       0.312  17.904   7.542  1.00 42.76           O  
ANISOU 3026  O   VAL B  66     5192   5526   5529    -49   -139   -169       O  
ATOM   3027  CB  VAL B  66      -1.740  20.547   6.741  1.00 41.90           C  
ANISOU 3027  CB  VAL B  66     4956   5421   5542    110   -343   -106       C  
ATOM   3028  CG1 VAL B  66      -1.670  22.035   6.460  1.00 42.75           C  
ANISOU 3028  CG1 VAL B  66     5101   5480   5663    190   -406    -37       C  
ATOM   3029  CG2 VAL B  66      -1.674  19.753   5.448  1.00 47.35           C  
ANISOU 3029  CG2 VAL B  66     5701   6159   6130     71   -419   -108       C  
ATOM   3030  N   GLY B  67      -1.652  18.158   8.601  1.00 38.66           N  
ANISOU 3030  N   GLY B  67     4485   5027   5177    -38   -143   -220       N  
ATOM   3031  CA  GLY B  67      -1.813  16.747   8.862  1.00 39.66           C  
ANISOU 3031  CA  GLY B  67     4601   5162   5307   -123   -107   -266       C  
ATOM   3032  C   GLY B  67      -2.133  15.972   7.601  1.00 43.64           C  
ANISOU 3032  C   GLY B  67     5115   5695   5770   -153   -203   -294       C  
ATOM   3033  O   GLY B  67      -2.288  16.516   6.508  1.00 42.24           O  
ANISOU 3033  O   GLY B  67     4952   5546   5552   -108   -301   -275       O  
ATOM   3034  N   LYS B  68      -2.228  14.656   7.766  1.00 47.26           N  
ANISOU 3034  N   LYS B  68     5578   6143   6238   -233   -181   -339       N  
ATOM   3035  CA  LYS B  68      -2.526  13.755   6.665  1.00 45.04           C  
ANISOU 3035  CA  LYS B  68     5309   5880   5922   -273   -268   -386       C  
ATOM   3036  C   LYS B  68      -3.607  12.772   7.086  1.00 41.28           C  
ANISOU 3036  C   LYS B  68     4740   5406   5538   -363   -268   -443       C  
ATOM   3037  O   LYS B  68      -3.762  12.464   8.270  1.00 45.91           O  
ANISOU 3037  O   LYS B  68     5295   5964   6183   -414   -174   -438       O  
ATOM   3038  CB  LYS B  68      -1.279  12.991   6.206  1.00 48.64           C  
ANISOU 3038  CB  LYS B  68     5894   6301   6285   -285   -250   -398       C  
ATOM   3039  CG  LYS B  68      -0.139  13.885   5.758  1.00 43.15           C  
ANISOU 3039  CG  LYS B  68     5284   5616   5496   -217   -234   -348       C  
ATOM   3040  CD  LYS B  68       1.032  13.073   5.240  1.00 44.35           C  
ANISOU 3040  CD  LYS B  68     5536   5751   5564   -226   -212   -384       C  
ATOM   3041  CE  LYS B  68       2.147  13.981   4.756  1.00 45.65           C  
ANISOU 3041  CE  LYS B  68     5768   5941   5634   -176   -184   -337       C  
ATOM   3042  NZ  LYS B  68       3.260  13.197   4.161  1.00 75.42           N  
ANISOU 3042  NZ  LYS B  68     9614   9715   9325   -181   -156   -392       N  
ATOM   3043  N   GLU B  69      -4.350  12.282   6.099  1.00 33.00           N  
ANISOU 3043  N   GLU B  69     3652   4393   4495   -393   -374   -495       N  
ATOM   3044  CA  GLU B  69      -5.404  11.306   6.319  1.00 34.03           C  
ANISOU 3044  CA  GLU B  69     3688   4526   4717   -495   -388   -556       C  
ATOM   3045  C   GLU B  69      -4.921   9.914   5.936  1.00 34.19           C  
ANISOU 3045  C   GLU B  69     3806   4484   4700   -570   -402   -603       C  
ATOM   3046  O   GLU B  69      -4.072   9.749   5.056  1.00 33.93           O  
ANISOU 3046  O   GLU B  69     3883   4441   4568   -529   -444   -616       O  
ATOM   3047  CB  GLU B  69      -6.657  11.662   5.517  1.00 45.48           C  
ANISOU 3047  CB  GLU B  69     5007   6054   6218   -483   -513   -599       C  
ATOM   3048  CG  GLU B  69      -7.311  12.964   5.936  1.00 59.82           C  
ANISOU 3048  CG  GLU B  69     6703   7921   8105   -402   -512   -571       C  
ATOM   3049  CD  GLU B  69      -7.915  12.894   7.325  1.00 73.10           C  
ANISOU 3049  CD  GLU B  69     8270   9607   9898   -459   -387   -584       C  
ATOM   3050  OE1 GLU B  69      -8.352  11.798   7.734  1.00 87.78           O  
ANISOU 3050  OE1 GLU B  69    10091  11455  11807   -583   -343   -624       O  
ATOM   3051  OE2 GLU B  69      -7.950  13.938   8.010  1.00 75.63           O  
ANISOU 3051  OE2 GLU B  69     8543   9941  10251   -386   -330   -557       O  
ATOM   3052  N   PHE B  70      -5.474   8.912   6.617  1.00 39.21           N  
ANISOU 3052  N   PHE B  70     4403   5076   5420   -683   -362   -632       N  
ATOM   3053  CA  PHE B  70      -5.125   7.516   6.402  1.00 35.18           C  
ANISOU 3053  CA  PHE B  70     3985   4479   4903   -763   -379   -679       C  
ATOM   3054  C   PHE B  70      -6.375   6.669   6.564  1.00 36.64           C  
ANISOU 3054  C   PHE B  70     4066   4658   5198   -899   -405   -730       C  
ATOM   3055  O   PHE B  70      -7.163   6.888   7.488  1.00 43.86           O  
ANISOU 3055  O   PHE B  70     4868   5602   6194   -958   -334   -706       O  
ATOM   3056  CB  PHE B  70      -4.047   7.048   7.388  1.00 34.26           C  
ANISOU 3056  CB  PHE B  70     3987   4262   4768   -771   -278   -630       C  
ATOM   3057  CG  PHE B  70      -2.830   7.925   7.417  1.00 34.63           C  
ANISOU 3057  CG  PHE B  70     4111   4320   4727   -651   -239   -579       C  
ATOM   3058  CD1 PHE B  70      -1.767   7.684   6.567  1.00 36.04           C  
ANISOU 3058  CD1 PHE B  70     4396   4478   4821   -589   -274   -611       C  
ATOM   3059  CD2 PHE B  70      -2.750   8.998   8.293  1.00 32.13           C  
ANISOU 3059  CD2 PHE B  70     3755   4039   4415   -605   -162   -511       C  
ATOM   3060  CE1 PHE B  70      -0.649   8.493   6.593  1.00 33.32           C  
ANISOU 3060  CE1 PHE B  70     4107   4150   4402   -495   -231   -568       C  
ATOM   3061  CE2 PHE B  70      -1.634   9.808   8.320  1.00 31.57           C  
ANISOU 3061  CE2 PHE B  70     3751   3971   4272   -508   -130   -468       C  
ATOM   3062  CZ  PHE B  70      -0.583   9.555   7.468  1.00 32.05           C  
ANISOU 3062  CZ  PHE B  70     3909   4015   4254   -459   -163   -493       C  
ATOM   3063  N   ASN B  71      -6.556   5.702   5.669  1.00 45.26           N  
ANISOU 3063  N   ASN B  71     5191   5715   6289   -954   -501   -810       N  
ATOM   3064  CA  ASN B  71      -7.734   4.855   5.745  1.00 50.30           C  
ANISOU 3064  CA  ASN B  71     5730   6344   7040  -1099   -536   -867       C  
ATOM   3065  C   ASN B  71      -7.541   3.773   6.807  1.00 52.09           C  
ANISOU 3065  C   ASN B  71     6027   6441   7322  -1222   -444   -836       C  
ATOM   3066  O   ASN B  71      -6.514   3.702   7.489  1.00 49.87           O  
ANISOU 3066  O   ASN B  71     5869   6085   6994  -1182   -366   -772       O  
ATOM   3067  CB  ASN B  71      -8.053   4.253   4.379  1.00 50.28           C  
ANISOU 3067  CB  ASN B  71     5736   6350   7018  -1118   -686   -973       C  
ATOM   3068  CG  ASN B  71      -6.908   3.450   3.813  1.00 48.44           C  
ANISOU 3068  CG  ASN B  71     5686   6019   6701  -1087   -713  -1015       C  
ATOM   3069  OD1 ASN B  71      -6.682   2.308   4.208  1.00 46.71           O  
ANISOU 3069  OD1 ASN B  71     5545   5671   6530  -1174   -690  -1036       O  
ATOM   3070  ND2 ASN B  71      -6.185   4.038   2.870  1.00 71.86           N  
ANISOU 3070  ND2 ASN B  71     8722   9043   9539   -964   -761  -1029       N  
ATOM   3071  N   LYS B  72      -8.550   2.908   6.942  1.00 64.16           N  
ANISOU 3071  N   LYS B  72     7480   7943   8956  -1379   -462   -879       N  
ATOM   3072  CA  LYS B  72      -8.589   1.951   8.041  1.00 61.29           C  
ANISOU 3072  CA  LYS B  72     7172   7463   8653  -1524   -371   -831       C  
ATOM   3073  C   LYS B  72      -7.489   0.900   7.959  1.00 51.73           C  
ANISOU 3073  C   LYS B  72     6168   6080   7405  -1520   -398   -831       C  
ATOM   3074  O   LYS B  72      -7.198   0.251   8.968  1.00 51.12           O  
ANISOU 3074  O   LYS B  72     6183   5888   7352  -1602   -324   -760       O  
ATOM   3075  CB  LYS B  72      -9.956   1.271   8.084  1.00 70.48           C  
ANISOU 3075  CB  LYS B  72     8199   8639   9942  -1709   -389   -882       C  
ATOM   3076  CG  LYS B  72     -11.116   2.243   8.161  1.00 79.00           C  
ANISOU 3076  CG  LYS B  72     9045   9891  11081  -1710   -370   -902       C  
ATOM   3077  CD  LYS B  72     -12.448   1.522   8.087  1.00 98.06           C  
ANISOU 3077  CD  LYS B  72    11304  12326  13629  -1898   -398   -971       C  
ATOM   3078  CE  LYS B  72     -13.603   2.508   8.104  1.00 97.71           C  
ANISOU 3078  CE  LYS B  72    11004  12462  13660  -1879   -391  -1010       C  
ATOM   3079  NZ  LYS B  72     -14.922   1.823   8.016  1.00 98.29           N  
ANISOU 3079  NZ  LYS B  72    10897  12572  13875  -2068   -419  -1090       N  
ATOM   3080  N   LEU B  73      -6.873   0.713   6.792  1.00 41.18           N  
ANISOU 3080  N   LEU B  73     4909   4725   6010  -1426   -503   -912       N  
ATOM   3081  CA  LEU B  73      -5.806  -0.264   6.625  1.00 41.16           C  
ANISOU 3081  CA  LEU B  73     5090   4566   5985  -1400   -535   -939       C  
ATOM   3082  C   LEU B  73      -4.424   0.380   6.572  1.00 39.50           C  
ANISOU 3082  C   LEU B  73     4974   4368   5665  -1225   -501   -908       C  
ATOM   3083  O   LEU B  73      -3.482  -0.235   6.061  1.00 55.08           O  
ANISOU 3083  O   LEU B  73     7069   6253   7605  -1159   -546   -968       O  
ATOM   3084  CB  LEU B  73      -6.046  -1.103   5.368  1.00 42.48           C  
ANISOU 3084  CB  LEU B  73     5282   4692   6167  -1429   -668  -1079       C  
ATOM   3085  CG  LEU B  73      -7.138  -2.173   5.448  1.00 44.92           C  
ANISOU 3085  CG  LEU B  73     5549   4917   6603  -1624   -716  -1126       C  
ATOM   3086  CD1 LEU B  73      -7.273  -2.912   4.123  1.00 47.18           C  
ANISOU 3086  CD1 LEU B  73     5869   5170   6889  -1634   -860  -1282       C  
ATOM   3087  CD2 LEU B  73      -6.848  -3.149   6.577  1.00 44.96           C  
ANISOU 3087  CD2 LEU B  73     5671   4734   6678  -1731   -653  -1048       C  
ATOM   3088  N   GLU B  74      -4.281   1.597   7.091  1.00 38.21           N  
ANISOU 3088  N   GLU B  74     4751   4313   5455  -1150   -422   -825       N  
ATOM   3089  CA  GLU B  74      -3.008   2.311   7.104  1.00 36.72           C  
ANISOU 3089  CA  GLU B  74     4634   4146   5171  -1000   -384   -789       C  
ATOM   3090  C   GLU B  74      -2.688   2.823   8.500  1.00 35.80           C  
ANISOU 3090  C   GLU B  74     4526   4019   5056   -994   -272   -673       C  
ATOM   3091  O   GLU B  74      -2.273   3.971   8.684  1.00 37.40           O  
ANISOU 3091  O   GLU B  74     4699   4309   5201   -899   -224   -626       O  
ATOM   3092  CB  GLU B  74      -3.015   3.454   6.093  1.00 36.14           C  
ANISOU 3092  CB  GLU B  74     4495   4222   5015   -895   -421   -816       C  
ATOM   3093  CG  GLU B  74      -3.025   2.988   4.651  1.00 37.45           C  
ANISOU 3093  CG  GLU B  74     4690   4405   5133   -877   -531   -933       C  
ATOM   3094  CD  GLU B  74      -3.185   4.131   3.672  1.00 39.27           C  
ANISOU 3094  CD  GLU B  74     4864   4786   5271   -794   -578   -940       C  
ATOM   3095  OE1 GLU B  74      -3.812   5.144   4.045  1.00 39.73           O  
ANISOU 3095  OE1 GLU B  74     4818   4928   5348   -782   -555   -872       O  
ATOM   3096  OE2 GLU B  74      -2.687   4.016   2.531  1.00 41.30           O  
ANISOU 3096  OE2 GLU B  74     5185   5075   5432   -739   -639  -1015       O  
ATOM   3097  N   ARG B  75      -2.865   1.966   9.509  1.00 36.47           N  
ANISOU 3097  N   ARG B  75     4664   3992   5202  -1104   -234   -623       N  
ATOM   3098  CA  ARG B  75      -2.635   2.385  10.887  1.00 35.87           C  
ANISOU 3098  CA  ARG B  75     4606   3911   5111  -1116   -130   -513       C  
ATOM   3099  C   ARG B  75      -1.145   2.491  11.191  1.00 34.81           C  
ANISOU 3099  C   ARG B  75     4594   3716   4914   -993   -123   -480       C  
ATOM   3100  O   ARG B  75      -0.723   3.357  11.966  1.00 33.84           O  
ANISOU 3100  O   ARG B  75     4466   3646   4745   -938    -53   -412       O  
ATOM   3101  CB  ARG B  75      -3.312   1.409  11.848  1.00 37.20           C  
ANISOU 3101  CB  ARG B  75     4807   3983   5346  -1288    -93   -460       C  
ATOM   3102  CG  ARG B  75      -3.356   1.896  13.281  1.00 42.01           C  
ANISOU 3102  CG  ARG B  75     5419   4620   5923  -1328     25   -351       C  
ATOM   3103  CD  ARG B  75      -4.279   3.095  13.415  1.00 62.24           C  
ANISOU 3103  CD  ARG B  75     7804   7359   8485  -1326     97   -357       C  
ATOM   3104  NE  ARG B  75      -4.435   3.526  14.801  1.00 78.13           N  
ANISOU 3104  NE  ARG B  75     9812   9410  10463  -1377    221   -272       N  
ATOM   3105  CZ  ARG B  75      -5.330   3.020  15.645  1.00 88.22           C  
ANISOU 3105  CZ  ARG B  75    11061  10686  11773  -1547    301   -232       C  
ATOM   3106  NH1 ARG B  75      -5.404   3.475  16.888  1.00 94.06           N  
ANISOU 3106  NH1 ARG B  75    11806  11477  12457  -1586    421   -163       N  
ATOM   3107  NH2 ARG B  75      -6.149   2.055  15.246  1.00 67.74           N  
ANISOU 3107  NH2 ARG B  75     8435   8042   9261  -1689    266   -266       N  
ATOM   3108  N   ARG B  76      -0.333   1.610  10.600  1.00 39.03           N  
ANISOU 3108  N   ARG B  76     5233   4141   5455   -946   -197   -539       N  
ATOM   3109  CA  ARG B  76       1.112   1.697  10.789  1.00 34.30           C  
ANISOU 3109  CA  ARG B  76     4726   3495   4812   -819   -198   -528       C  
ATOM   3110  C   ARG B  76       1.672   2.990  10.207  1.00 33.00           C  
ANISOU 3110  C   ARG B  76     4495   3473   4569   -694   -172   -546       C  
ATOM   3111  O   ARG B  76       2.517   3.646  10.829  1.00 36.21           O  
ANISOU 3111  O   ARG B  76     4921   3900   4936   -619   -126   -493       O  
ATOM   3112  CB  ARG B  76       1.802   0.490  10.156  1.00 35.16           C  
ANISOU 3112  CB  ARG B  76     4939   3465   4957   -784   -285   -616       C  
ATOM   3113  CG  ARG B  76       1.558  -0.823  10.884  1.00 47.16           C  
ANISOU 3113  CG  ARG B  76     6564   4797   6558   -892   -322   -579       C  
ATOM   3114  CD  ARG B  76       2.064  -1.999  10.074  1.00 37.63           C  
ANISOU 3114  CD  ARG B  76     5446   3448   5404   -854   -423   -693       C  
ATOM   3115  NE  ARG B  76       1.423  -2.048   8.767  1.00 38.08           N  
ANISOU 3115  NE  ARG B  76     5433   3578   5458   -874   -465   -815       N  
ATOM   3116  CZ  ARG B  76       1.982  -2.563   7.679  1.00 38.62           C  
ANISOU 3116  CZ  ARG B  76     5538   3613   5524   -793   -533   -954       C  
ATOM   3117  NH1 ARG B  76       3.204  -3.072   7.737  1.00 38.79           N  
ANISOU 3117  NH1 ARG B  76     5648   3529   5560   -679   -561   -996       N  
ATOM   3118  NH2 ARG B  76       1.320  -2.557   6.533  1.00 39.14           N  
ANISOU 3118  NH2 ARG B  76     5545   3759   5569   -822   -575  -1059       N  
ATOM   3119  N   MET B  77       1.214   3.373   9.014  1.00 33.07           N  
ANISOU 3119  N   MET B  77     4434   3579   4553   -676   -207   -618       N  
ATOM   3120  CA  MET B  77       1.709   4.597   8.396  1.00 32.08           C  
ANISOU 3120  CA  MET B  77     4262   3580   4346   -572   -187   -622       C  
ATOM   3121  C   MET B  77       1.191   5.828   9.128  1.00 31.32           C  
ANISOU 3121  C   MET B  77     4083   3574   4242   -577   -121   -535       C  
ATOM   3122  O   MET B  77       1.906   6.830   9.257  1.00 35.98           O  
ANISOU 3122  O   MET B  77     4669   4220   4781   -495    -81   -499       O  
ATOM   3123  CB  MET B  77       1.312   4.641   6.921  1.00 39.93           C  
ANISOU 3123  CB  MET B  77     5222   4650   5299   -560   -254   -712       C  
ATOM   3124  CG  MET B  77       2.107   5.641   6.103  1.00 49.06           C  
ANISOU 3124  CG  MET B  77     6376   5912   6353   -456   -242   -722       C  
ATOM   3125  SD  MET B  77       1.394   5.944   4.476  1.00 63.06           S  
ANISOU 3125  SD  MET B  77     8111   7800   8050   -457   -325   -795       S  
ATOM   3126  CE  MET B  77       1.378   4.288   3.796  1.00 86.03           C  
ANISOU 3126  CE  MET B  77    11088  10612  10986   -502   -400   -932       C  
ATOM   3127  N   GLU B  78      -0.053   5.776   9.604  1.00 31.89           N  
ANISOU 3127  N   GLU B  78     4084   3663   4372   -674   -107   -510       N  
ATOM   3128  CA  GLU B  78      -0.575   6.861  10.424  1.00 31.41           C  
ANISOU 3128  CA  GLU B  78     3940   3679   4315   -676    -36   -445       C  
ATOM   3129  C   GLU B  78       0.251   7.032  11.691  1.00 35.73           C  
ANISOU 3129  C   GLU B  78     4556   4180   4841   -655     37   -373       C  
ATOM   3130  O   GLU B  78       0.596   8.158  12.074  1.00 32.14           O  
ANISOU 3130  O   GLU B  78     4075   3785   4351   -589     83   -337       O  
ATOM   3131  CB  GLU B  78      -2.036   6.594  10.773  1.00 32.46           C  
ANISOU 3131  CB  GLU B  78     3973   3838   4521   -794    -22   -448       C  
ATOM   3132  CG  GLU B  78      -2.680   7.715  11.554  1.00 36.42           C  
ANISOU 3132  CG  GLU B  78     4369   4432   5037   -789     55   -407       C  
ATOM   3133  CD  GLU B  78      -4.103   7.405  11.951  1.00 46.06           C  
ANISOU 3133  CD  GLU B  78     5472   5691   6339   -912     85   -423       C  
ATOM   3134  OE1 GLU B  78      -4.580   7.999  12.939  1.00 61.53           O  
ANISOU 3134  OE1 GLU B  78     7362   7705   8313   -935    178   -392       O  
ATOM   3135  OE2 GLU B  78      -4.743   6.570  11.280  1.00 55.66           O  
ANISOU 3135  OE2 GLU B  78     6657   6887   7603   -989     20   -475       O  
ATOM   3136  N   ASN B  79       0.586   5.922  12.350  1.00 31.23           N  
ANISOU 3136  N   ASN B  79     4081   3494   4290   -712     37   -352       N  
ATOM   3137  CA  ASN B  79       1.376   5.997  13.570  1.00 30.80           C  
ANISOU 3137  CA  ASN B  79     4105   3392   4206   -695     85   -280       C  
ATOM   3138  C   ASN B  79       2.813   6.413  13.290  1.00 29.86           C  
ANISOU 3138  C   ASN B  79     4037   3268   4042   -565     64   -293       C  
ATOM   3139  O   ASN B  79       3.457   7.012  14.156  1.00 36.06           O  
ANISOU 3139  O   ASN B  79     4847   4063   4793   -524    103   -243       O  
ATOM   3140  CB  ASN B  79       1.333   4.658  14.301  1.00 31.85           C  
ANISOU 3140  CB  ASN B  79     4342   3389   4370   -792     71   -243       C  
ATOM   3141  CG  ASN B  79      -0.001   4.406  14.966  1.00 32.86           C  
ANISOU 3141  CG  ASN B  79     4420   3535   4530   -942    129   -205       C  
ATOM   3142  OD1 ASN B  79      -0.709   5.343  15.336  1.00 35.02           O  
ANISOU 3142  OD1 ASN B  79     4588   3924   4792   -959    203   -193       O  
ATOM   3143  ND2 ASN B  79      -0.354   3.136  15.125  1.00 34.12           N  
ANISOU 3143  ND2 ASN B  79     4651   3578   4736  -1056     99   -192       N  
ATOM   3144  N   LEU B  80       3.333   6.108  12.098  1.00 29.88           N  
ANISOU 3144  N   LEU B  80     4050   3262   4040   -505      5   -367       N  
ATOM   3145  CA  LEU B  80       4.662   6.583  11.730  1.00 29.16           C  
ANISOU 3145  CA  LEU B  80     3980   3191   3906   -391      0   -390       C  
ATOM   3146  C   LEU B  80       4.660   8.090  11.500  1.00 28.28           C  
ANISOU 3146  C   LEU B  80     3794   3202   3749   -343     44   -368       C  
ATOM   3147  O   LEU B  80       5.564   8.795  11.961  1.00 29.40           O  
ANISOU 3147  O   LEU B  80     3945   3362   3864   -285     75   -340       O  
ATOM   3148  CB  LEU B  80       5.158   5.846  10.485  1.00 29.66           C  
ANISOU 3148  CB  LEU B  80     4070   3230   3969   -348    -59   -489       C  
ATOM   3149  CG  LEU B  80       6.511   6.272   9.912  1.00 29.21           C  
ANISOU 3149  CG  LEU B  80     4017   3215   3867   -240    -50   -535       C  
ATOM   3150  CD1 LEU B  80       7.615   6.082  10.937  1.00 29.01           C  
ANISOU 3150  CD1 LEU B  80     4040   3118   3864   -188    -45   -504       C  
ATOM   3151  CD2 LEU B  80       6.824   5.500   8.640  1.00 29.99           C  
ANISOU 3151  CD2 LEU B  80     4135   3305   3954   -209    -96   -651       C  
ATOM   3152  N   ASN B  81       3.654   8.594  10.782  1.00 28.43           N  
ANISOU 3152  N   ASN B  81     3740   3297   3764   -368     35   -382       N  
ATOM   3153  CA  ASN B  81       3.497  10.036  10.607  1.00 37.99           C  
ANISOU 3153  CA  ASN B  81     4886   4602   4944   -326     62   -351       C  
ATOM   3154  C   ASN B  81       3.390  10.738  11.958  1.00 27.40           C  
ANISOU 3154  C   ASN B  81     3528   3263   3618   -333    126   -289       C  
ATOM   3155  O   ASN B  81       4.057  11.752  12.207  1.00 27.72           O  
ANISOU 3155  O   ASN B  81     3569   3333   3632   -276    155   -262       O  
ATOM   3156  CB  ASN B  81       2.261  10.301   9.743  1.00 28.39           C  
ANISOU 3156  CB  ASN B  81     3595   3451   3740   -354     20   -374       C  
ATOM   3157  CG  ASN B  81       2.165  11.734   9.271  1.00 28.04           C  
ANISOU 3157  CG  ASN B  81     3503   3487   3663   -295     18   -345       C  
ATOM   3158  OD1 ASN B  81       2.972  12.188   8.462  1.00 28.52           O  
ANISOU 3158  OD1 ASN B  81     3600   3577   3660   -243      4   -348       O  
ATOM   3159  ND2 ASN B  81       1.156  12.448   9.754  1.00 36.82           N  
ANISOU 3159  ND2 ASN B  81     4534   4634   4822   -306     31   -320       N  
ATOM   3160  N   LYS B  82       2.627  10.211  12.879  1.00 40.43           N  
ANISOU 3160  N   LYS B  82     5169   4885   5307   -412    153   -269       N  
ATOM   3161  CA  LYS B  82       2.525  10.792  14.191  1.00 31.21           C  
ANISOU 3161  CA  LYS B  82     3998   3724   4137   -432    223   -220       C  
ATOM   3162  C   LYS B  82       3.836  10.773  14.970  1.00 31.42           C  
ANISOU 3162  C   LYS B  82     4114   3701   4125   -385    231   -191       C  
ATOM   3163  O   LYS B  82       4.150  11.672  15.681  1.00 28.04           O  
ANISOU 3163  O   LYS B  82     3679   3304   3672   -348    271   -167       O  
ATOM   3164  CB  LYS B  82       1.501  10.017  14.963  1.00 30.00           C  
ATOM   3165  CG  LYS B  82       0.955  10.766  16.134  1.00 30.00           C  
ATOM   3166  CD  LYS B  82      -0.026   9.934  16.897  1.00 30.00           C  
ATOM   3167  CE  LYS B  82      -0.367  10.603  18.209  1.00 30.00           C  
ATOM   3168  NZ  LYS B  82      -0.566   9.621  19.302  1.00 30.00           N  
ATOM   3169  N   LYS B  83       4.583   9.705  14.837  1.00 27.45           N  
ANISOU 3169  N   LYS B  83     3691   3116   3623   -382    185   -201       N  
ATOM   3170  CA  LYS B  83       5.858   9.543  15.464  1.00 27.17           C  
ANISOU 3170  CA  LYS B  83     3730   3030   3564   -330    173   -180       C  
ATOM   3171  C   LYS B  83       6.820  10.558  14.940  1.00 26.39           C  
ANISOU 3171  C   LYS B  83     3597   2987   3442   -240    176   -202       C  
ATOM   3172  O   LYS B  83       7.613  11.053  15.649  1.00 27.45           O  
ANISOU 3172  O   LYS B  83     3748   3125   3556   -206    192   -178       O  
ATOM   3173  CB  LYS B  83       6.371   8.142  15.173  1.00 27.80           C  
ANISOU 3173  CB  LYS B  83     3891   3001   3670   -327    106   -202       C  
ATOM   3174  CG  LYS B  83       7.705   7.787  15.751  1.00 27.75           C  
ANISOU 3174  CG  LYS B  83     3951   2937   3655   -258     71   -190       C  
ATOM   3175  CD  LYS B  83       7.810   6.315  15.903  1.00 28.70           C  
ANISOU 3175  CD  LYS B  83     4163   2923   3817   -259     -5   -200       C  
ATOM   3176  CE  LYS B  83       8.822   5.666  14.992  1.00 30.30           C  
ANISOU 3176  CE  LYS B  83     4345   3110   4059   -223    -45   -295       C  
ATOM   3177  NZ  LYS B  83       8.444   4.308  14.564  1.00 30.09           N  
ANISOU 3177  NZ  LYS B  83     4411   2932   4088   -212   -128   -318       N  
ATOM   3178  N   VAL B  84       6.784  10.823  13.661  1.00 26.26           N  
ANISOU 3178  N   VAL B  84     3536   3018   3423   -210    161   -246       N  
ATOM   3179  CA  VAL B  84       7.668  11.840  13.094  1.00 25.73           C  
ANISOU 3179  CA  VAL B  84     3440   3008   3328   -147    173   -258       C  
ATOM   3180  C   VAL B  84       7.302  13.220  13.630  1.00 25.29           C  
ANISOU 3180  C   VAL B  84     3344   3000   3264   -145    215   -215       C  
ATOM   3181  O   VAL B  84       8.153  13.955  14.150  1.00 24.92           O  
ANISOU 3181  O   VAL B  84     3303   2958   3207   -113    234   -200       O  
ATOM   3182  CB  VAL B  84       7.610  11.804  11.557  1.00 25.95           C  
ANISOU 3182  CB  VAL B  84     3445   3082   3331   -132    151   -306       C  
ATOM   3183  CG1 VAL B  84       8.359  12.986  10.970  1.00 25.59           C  
ANISOU 3183  CG1 VAL B  84     3376   3103   3246    -92    177   -298       C  
ATOM   3184  CG2 VAL B  84       8.178  10.498  11.036  1.00 26.49           C  
ANISOU 3184  CG2 VAL B  84     3555   3102   3409   -117    114   -372       C  
ATOM   3185  N   ASP B  85       6.021  13.588  13.510  1.00 25.47           N  
ANISOU 3185  N   ASP B  85     3320   3056   3303   -177    225   -204       N  
ATOM   3186  CA  ASP B  85       5.586  14.908  13.961  1.00 25.26           C  
ANISOU 3186  CA  ASP B  85     3249   3066   3284   -162    258   -179       C  
ATOM   3187  C   ASP B  85       5.892  15.115  15.442  1.00 25.13           C  
ANISOU 3187  C   ASP B  85     3260   3026   3262   -170    300   -159       C  
ATOM   3188  O   ASP B  85       6.508  16.119  15.830  1.00 24.80           O  
ANISOU 3188  O   ASP B  85     3221   2991   3212   -135    316   -152       O  
ATOM   3189  CB  ASP B  85       4.093  15.090  13.683  1.00 25.75           C  
ANISOU 3189  CB  ASP B  85     3239   3163   3380   -189    254   -186       C  
ATOM   3190  CG  ASP B  85       3.784  15.204  12.202  1.00 28.57           C  
ANISOU 3190  CG  ASP B  85     3571   3554   3730   -170    196   -200       C  
ATOM   3191  OD1 ASP B  85       4.705  15.514  11.418  1.00 30.68           O  
ANISOU 3191  OD1 ASP B  85     3874   3829   3954   -136    178   -196       O  
ATOM   3192  OD2 ASP B  85       2.616  14.989  11.818  1.00 35.13           O  
ANISOU 3192  OD2 ASP B  85     4344   4411   4592   -196    168   -217       O  
ATOM   3193  N   ASP B  86       5.480  14.161  16.283  1.00 25.53           N  
ANISOU 3193  N   ASP B  86     3343   3048   3311   -225    316   -150       N  
ATOM   3194  CA  ASP B  86       5.712  14.280  17.718  1.00 25.64           C  
ANISOU 3194  CA  ASP B  86     3399   3048   3294   -243    353   -127       C  
ATOM   3195  C   ASP B  86       7.198  14.336  18.039  1.00 33.63           C  
ANISOU 3195  C   ASP B  86     4471   4026   4282   -195    321   -121       C  
ATOM   3196  O   ASP B  86       7.619  15.091  18.921  1.00 25.17           O  
ANISOU 3196  O   ASP B  86     3414   2965   3185   -179    340   -116       O  
ATOM   3197  CB  ASP B  86       5.048  13.117  18.456  1.00 26.37           C  
ANISOU 3197  CB  ASP B  86     3535   3110   3376   -327    371   -103       C  
ATOM   3198  CG  ASP B  86       3.550  13.290  18.586  1.00 40.56           C  
ANISOU 3198  CG  ASP B  86     5252   4961   5197   -388    429   -114       C  
ATOM   3199  OD1 ASP B  86       3.047  14.390  18.272  1.00 29.28           O  
ANISOU 3199  OD1 ASP B  86     3738   3590   3797   -347    450   -144       O  
ATOM   3200  OD2 ASP B  86       2.875  12.331  19.017  1.00 36.10           O  
ANISOU 3200  OD2 ASP B  86     4707   4378   4631   -477    452    -95       O  
ATOM   3201  N   GLY B  87       8.009  13.543  17.334  1.00 25.23           N  
ANISOU 3201  N   GLY B  87     3434   2925   3228   -169    269   -135       N  
ATOM   3202  CA  GLY B  87       9.439  13.550  17.596  1.00 25.08           C  
ANISOU 3202  CA  GLY B  87     3447   2882   3202   -118    233   -143       C  
ATOM   3203  C   GLY B  87      10.075  14.897  17.311  1.00 24.61           C  
ANISOU 3203  C   GLY B  87     3338   2869   3143    -78    251   -157       C  
ATOM   3204  O   GLY B  87      10.817  15.437  18.140  1.00 24.56           O  
ANISOU 3204  O   GLY B  87     3346   2860   3125    -61    247   -155       O  
ATOM   3205  N   PHE B  88       9.785  15.464  16.135  1.00 24.40           N  
ANISOU 3205  N   PHE B  88     3260   2882   3128    -70    266   -169       N  
ATOM   3206  CA  PHE B  88      10.344  16.771  15.799  1.00 24.14           C  
ANISOU 3206  CA  PHE B  88     3194   2881   3097    -48    282   -169       C  
ATOM   3207  C   PHE B  88       9.868  17.843  16.776  1.00 24.08           C  
ANISOU 3207  C   PHE B  88     3183   2874   3093    -54    310   -154       C  
ATOM   3208  O   PHE B  88      10.651  18.711  17.189  1.00 32.02           O  
ANISOU 3208  O   PHE B  88     4189   3876   4103    -41    312   -159       O  
ATOM   3209  CB  PHE B  88       9.985  17.145  14.360  1.00 24.16           C  
ANISOU 3209  CB  PHE B  88     3165   2921   3096    -47    284   -168       C  
ATOM   3210  CG  PHE B  88      10.774  16.398  13.323  1.00 24.35           C  
ANISOU 3210  CG  PHE B  88     3189   2961   3102    -35    271   -202       C  
ATOM   3211  CD1 PHE B  88      12.072  15.988  13.582  1.00 24.44           C  
ANISOU 3211  CD1 PHE B  88     3202   2963   3122    -11    265   -235       C  
ATOM   3212  CD2 PHE B  88      10.221  16.105  12.088  1.00 31.71           C  
ANISOU 3212  CD2 PHE B  88     4115   3924   4009    -44    261   -213       C  
ATOM   3213  CE1 PHE B  88      12.802  15.299  12.628  1.00 28.89           C  
ANISOU 3213  CE1 PHE B  88     3752   3550   3676      9    262   -286       C  
ATOM   3214  CE2 PHE B  88      10.947  15.415  11.130  1.00 27.92           C  
ANISOU 3214  CE2 PHE B  88     3636   3468   3502    -32    258   -261       C  
ATOM   3215  CZ  PHE B  88      12.236  15.011  11.402  1.00 25.61           C  
ANISOU 3215  CZ  PHE B  88     3336   3168   3225     -4    265   -302       C  
ATOM   3216  N   ILE B  89       8.593  17.788  17.173  1.00 24.27           N  
ANISOU 3216  N   ILE B  89     3197   2904   3120    -77    333   -147       N  
ATOM   3217  CA  ILE B  89       8.077  18.753  18.144  1.00 24.42           C  
ANISOU 3217  CA  ILE B  89     3207   2930   3143    -77    368   -154       C  
ATOM   3218  C   ILE B  89       8.827  18.633  19.470  1.00 24.53           C  
ANISOU 3218  C   ILE B  89     3276   2928   3118    -84    370   -159       C  
ATOM   3219  O   ILE B  89       9.201  19.639  20.086  1.00 37.17           O  
ANISOU 3219  O   ILE B  89     4880   4527   4717    -68    378   -178       O  
ATOM   3220  CB  ILE B  89       6.561  18.566  18.334  1.00 24.84           C  
ANISOU 3220  CB  ILE B  89     3220   3008   3209   -103    403   -161       C  
ATOM   3221  CG1 ILE B  89       5.805  19.037  17.089  1.00 24.90           C  
ANISOU 3221  CG1 ILE B  89     3165   3033   3261    -80    383   -161       C  
ATOM   3222  CG2 ILE B  89       6.082  19.319  19.557  1.00 25.77           C  
ANISOU 3222  CG2 ILE B  89     3331   3141   3318   -104    455   -187       C  
ATOM   3223  CD1 ILE B  89       4.318  18.788  17.154  1.00 25.46           C  
ANISOU 3223  CD1 ILE B  89     3171   3137   3364   -104    406   -179       C  
ATOM   3224  N   ASP B  90       9.054  17.399  19.929  1.00 24.72           N  
ANISOU 3224  N   ASP B  90     3352   2933   3109   -108    350   -143       N  
ATOM   3225  CA  ASP B  90       9.777  17.196  21.183  1.00 25.02           C  
ANISOU 3225  CA  ASP B  90     3456   2953   3098   -113    330   -138       C  
ATOM   3226  C   ASP B  90      11.188  17.759  21.105  1.00 24.80           C  
ANISOU 3226  C   ASP B  90     3422   2916   3086    -70    284   -158       C  
ATOM   3227  O   ASP B  90      11.659  18.418  22.042  1.00 38.32           O  
ANISOU 3227  O   ASP B  90     5157   4632   4773    -66    276   -174       O  
ATOM   3228  CB  ASP B  90       9.829  15.709  21.535  1.00 25.44           C  
ANISOU 3228  CB  ASP B  90     3578   2967   3121   -141    296   -103       C  
ATOM   3229  CG  ASP B  90       8.477  15.150  21.909  1.00 36.90           C  
ANISOU 3229  CG  ASP B  90     5044   4429   4547   -211    350    -79       C  
ATOM   3230  OD1 ASP B  90       7.582  15.944  22.262  1.00 36.89           O  
ANISOU 3230  OD1 ASP B  90     5002   4478   4538   -231    419    -98       O  
ATOM   3231  OD2 ASP B  90       8.310  13.915  21.856  1.00 50.64           O  
ANISOU 3231  OD2 ASP B  90     6833   6124   6283   -247    324    -46       O  
ATOM   3232  N   ILE B  91      11.883  17.500  19.998  1.00 26.83           N  
ANISOU 3232  N   ILE B  91     3643   3168   3384    -44    256   -165       N  
ATOM   3233  CA  ILE B  91      13.252  17.982  19.868  1.00 24.52           C  
ANISOU 3233  CA  ILE B  91     3323   2878   3115    -15    223   -191       C  
ATOM   3234  C   ILE B  91      13.292  19.506  19.854  1.00 24.40           C  
ANISOU 3234  C   ILE B  91     3275   2878   3119    -22    254   -204       C  
ATOM   3235  O   ILE B  91      14.130  20.120  20.525  1.00 24.62           O  
ANISOU 3235  O   ILE B  91     3304   2902   3150    -19    230   -227       O  
ATOM   3236  CB  ILE B  91      13.906  17.369  18.619  1.00 24.46           C  
ANISOU 3236  CB  ILE B  91     3274   2878   3142      8    209   -209       C  
ATOM   3237  CG1 ILE B  91      14.132  15.870  18.830  1.00 28.56           C  
ANISOU 3237  CG1 ILE B  91     3835   3357   3659     29    156   -211       C  
ATOM   3238  CG2 ILE B  91      15.212  18.073  18.296  1.00 24.58           C  
ANISOU 3238  CG2 ILE B  91     3233   2917   3189     22    201   -241       C  
ATOM   3239  CD1 ILE B  91      14.620  15.142  17.601  1.00 38.92           C  
ANISOU 3239  CD1 ILE B  91     5108   4676   5004     59    147   -248       C  
ATOM   3240  N   TRP B  92      12.377  20.145  19.120  1.00 27.43           N  
ANISOU 3240  N   TRP B  92     3633   3270   3520    -30    294   -191       N  
ATOM   3241  CA  TRP B  92      12.398  21.604  19.055  1.00 32.66           C  
ANISOU 3241  CA  TRP B  92     4276   3922   4211    -33    311   -198       C  
ATOM   3242  C   TRP B  92      12.014  22.231  20.392  1.00 24.58           C  
ANISOU 3242  C   TRP B  92     3282   2885   3172    -33    321   -226       C  
ATOM   3243  O   TRP B  92      12.558  23.276  20.774  1.00 24.82           O  
ANISOU 3243  O   TRP B  92     3313   2894   3224    -34    311   -252       O  
ATOM   3244  CB  TRP B  92      11.482  22.091  17.933  1.00 24.22           C  
ANISOU 3244  CB  TRP B  92     3182   2855   3166    -30    331   -171       C  
ATOM   3245  CG  TRP B  92      12.113  21.944  16.585  1.00 24.52           C  
ANISOU 3245  CG  TRP B  92     3200   2912   3206    -39    325   -149       C  
ATOM   3246  CD1 TRP B  92      11.695  21.143  15.565  1.00 27.99           C  
ANISOU 3246  CD1 TRP B  92     3631   3379   3625    -39    324   -136       C  
ATOM   3247  CD2 TRP B  92      13.298  22.600  16.122  1.00 38.28           C  
ANISOU 3247  CD2 TRP B  92     4926   4656   4961    -60    327   -147       C  
ATOM   3248  NE1 TRP B  92      12.538  21.270  14.491  1.00 30.86           N  
ANISOU 3248  NE1 TRP B  92     3980   3768   3977    -54    331   -128       N  
ATOM   3249  CE2 TRP B  92      13.532  22.157  14.807  1.00 30.78           C  
ANISOU 3249  CE2 TRP B  92     3961   3745   3988    -72    338   -131       C  
ATOM   3250  CE3 TRP B  92      14.181  23.524  16.690  1.00 24.65           C  
ANISOU 3250  CE3 TRP B  92     3195   2906   3264    -80    323   -163       C  
ATOM   3251  CZ2 TRP B  92      14.612  22.604  14.049  1.00 33.29           C  
ANISOU 3251  CZ2 TRP B  92     4256   4089   4305   -107    360   -127       C  
ATOM   3252  CZ3 TRP B  92      15.251  23.966  15.939  1.00 31.67           C  
ANISOU 3252  CZ3 TRP B  92     4056   3811   4167   -118    336   -156       C  
ATOM   3253  CH2 TRP B  92      15.458  23.507  14.631  1.00 29.95           C  
ANISOU 3253  CH2 TRP B  92     3820   3642   3919   -134    362   -136       C  
ATOM   3254  N   THR B  93      11.086  21.604  21.118  1.00 24.72           N  
ANISOU 3254  N   THR B  93     3325   2918   3148    -39    344   -227       N  
ATOM   3255  CA  THR B  93      10.745  22.067  22.460  1.00 25.20           C  
ANISOU 3255  CA  THR B  93     3420   2985   3170    -45    366   -264       C  
ATOM   3256  C   THR B  93      11.959  22.008  23.381  1.00 25.46           C  
ANISOU 3256  C   THR B  93     3499   3011   3162    -50    316   -282       C  
ATOM   3257  O   THR B  93      12.306  22.995  24.045  1.00 25.82           O  
ANISOU 3257  O   THR B  93     3556   3047   3208    -47    308   -328       O  
ATOM   3258  CB  THR B  93       9.599  21.221  23.019  1.00 25.50           C  
ANISOU 3258  CB  THR B  93     3476   3055   3157    -71    413   -254       C  
ATOM   3259  OG1 THR B  93       8.463  21.324  22.153  1.00 31.26           O  
ANISOU 3259  OG1 THR B  93     4144   3796   3936    -65    448   -249       O  
ATOM   3260  CG2 THR B  93       9.214  21.680  24.413  1.00 26.21           C  
ANISOU 3260  CG2 THR B  93     3604   3169   3184    -85    453   -300       C  
ATOM   3261  N   TYR B  94      12.624  20.851  23.417  1.00 25.41           N  
ANISOU 3261  N   TYR B  94     3520   3005   3130    -52    269   -253       N  
ATOM   3262  CA  TYR B  94      13.835  20.691  24.215  1.00 25.80           C  
ANISOU 3262  CA  TYR B  94     3604   3048   3151    -44    197   -268       C  
ATOM   3263  C   TYR B  94      14.875  21.753  23.866  1.00 25.79           C  
ANISOU 3263  C   TYR B  94     3548   3037   3214    -36    170   -307       C  
ATOM   3264  O   TYR B  94      15.441  22.403  24.755  1.00 31.25           O  
ANISOU 3264  O   TYR B  94     4259   3726   3887    -42    135   -349       O  
ATOM   3265  CB  TYR B  94      14.390  19.280  24.004  1.00 25.84           C  
ANISOU 3265  CB  TYR B  94     3629   3039   3150    -29    139   -233       C  
ATOM   3266  CG  TYR B  94      15.754  19.036  24.602  1.00 26.36           C  
ANISOU 3266  CG  TYR B  94     3707   3094   3212     -3     42   -251       C  
ATOM   3267  CD1 TYR B  94      15.893  18.635  25.924  1.00 27.10           C  
ANISOU 3267  CD1 TYR B  94     3893   3184   3221     -9    -15   -239       C  
ATOM   3268  CD2 TYR B  94      16.904  19.192  23.840  1.00 27.53           C  
ANISOU 3268  CD2 TYR B  94     3773   3245   3440     24      5   -282       C  
ATOM   3269  CE1 TYR B  94      17.139  18.408  26.473  1.00 27.74           C  
ANISOU 3269  CE1 TYR B  94     3982   3256   3302     24   -126   -257       C  
ATOM   3270  CE2 TYR B  94      18.154  18.970  24.380  1.00 26.92           C  
ANISOU 3270  CE2 TYR B  94     3685   3167   3376     54    -91   -311       C  
ATOM   3271  CZ  TYR B  94      18.265  18.577  25.695  1.00 28.34           C  
ANISOU 3271  CZ  TYR B  94     3955   3334   3478     59   -167   -298       C  
ATOM   3272  OH  TYR B  94      19.509  18.356  26.234  1.00 30.34           O  
ANISOU 3272  OH  TYR B  94     4194   3585   3748     97   -284   -328       O  
ATOM   3273  N   ASN B  95      15.126  21.948  22.567  1.00 25.37           N  
ANISOU 3273  N   ASN B  95     3430   2981   3230    -33    188   -294       N  
ATOM   3274  CA  ASN B  95      16.109  22.933  22.120  1.00 25.53           C  
ANISOU 3274  CA  ASN B  95     3395   2993   3311    -47    176   -320       C  
ATOM   3275  C   ASN B  95      15.769  24.327  22.625  1.00 25.82           C  
ANISOU 3275  C   ASN B  95     3449   3000   3363    -65    193   -351       C  
ATOM   3276  O   ASN B  95      16.628  25.031  23.172  1.00 51.98           O  
ANISOU 3276  O   ASN B  95     6756   6299   6697    -83    155   -394       O  
ATOM   3277  CB  ASN B  95      16.187  22.940  20.593  1.00 25.20           C  
ANISOU 3277  CB  ASN B  95     3299   2961   3315    -56    212   -290       C  
ATOM   3278  CG  ASN B  95      16.889  21.724  20.036  1.00 28.78           C  
ANISOU 3278  CG  ASN B  95     3719   3444   3771    -35    190   -291       C  
ATOM   3279  OD1 ASN B  95      17.323  20.842  20.778  1.00 30.19           O  
ANISOU 3279  OD1 ASN B  95     3917   3623   3931     -7    135   -306       O  
ATOM   3280  ND2 ASN B  95      17.001  21.667  18.715  1.00 32.64           N  
ANISOU 3280  ND2 ASN B  95     4164   3956   4281    -45    228   -276       N  
ATOM   3281  N   ALA B  96      14.517  24.750  22.433  1.00 31.75           N  
ANISOU 3281  N   ALA B  96     4215   3735   4114    -57    244   -339       N  
ATOM   3282  CA  ALA B  96      14.120  26.097  22.830  1.00 26.11           C  
ANISOU 3282  CA  ALA B  96     3514   2977   3432    -58    258   -379       C  
ATOM   3283  C   ALA B  96      14.273  26.297  24.334  1.00 29.84           C  
ANISOU 3283  C   ALA B  96     4034   3455   3848    -58    237   -445       C  
ATOM   3284  O   ALA B  96      14.924  27.251  24.784  1.00 33.55           O  
ANISOU 3284  O   ALA B  96     4510   3890   4348    -74    204   -497       O  
ATOM   3285  CB  ALA B  96      12.682  26.366  22.391  1.00 26.02           C  
ANISOU 3285  CB  ALA B  96     3496   2953   3437    -31    307   -364       C  
ATOM   3286  N   GLU B  97      13.690  25.396  25.129  1.00 26.75           N  
ANISOU 3286  N   GLU B  97     3685   3109   3370    -50    252   -445       N  
ATOM   3287  CA  GLU B  97      13.713  25.580  26.577  1.00 27.51           C  
ANISOU 3287  CA  GLU B  97     3843   3224   3384    -56    240   -505       C  
ATOM   3288  C   GLU B  97      15.135  25.544  27.126  1.00 27.89           C  
ANISOU 3288  C   GLU B  97     3907   3272   3417    -70    149   -528       C  
ATOM   3289  O   GLU B  97      15.523  26.406  27.928  1.00 47.68           O  
ANISOU 3289  O   GLU B  97     6439   5764   5912    -80    118   -600       O  
ATOM   3290  CB  GLU B  97      12.841  24.521  27.249  1.00 27.66           C  
ANISOU 3290  CB  GLU B  97     3913   3297   3299    -64    281   -481       C  
ATOM   3291  CG  GLU B  97      11.370  24.646  26.886  1.00 33.58           C  
ANISOU 3291  CG  GLU B  97     4629   4060   4069    -54    373   -482       C  
ATOM   3292  CD  GLU B  97      10.472  23.762  27.722  1.00 43.93           C  
ANISOU 3292  CD  GLU B  97     5987   5432   5273    -84    432   -471       C  
ATOM   3293  OE1 GLU B  97      10.993  22.873  28.424  1.00 54.63           O  
ANISOU 3293  OE1 GLU B  97     7416   6807   6534   -113    392   -436       O  
ATOM   3294  OE2 GLU B  97       9.242  23.962  27.679  1.00 47.36           O  
ANISOU 3294  OE2 GLU B  97     6382   5894   5719    -82    515   -497       O  
ATOM   3295  N   LEU B  98      15.934  24.571  26.685  1.00 27.56           N  
ANISOU 3295  N   LEU B  98     3844   3244   3385    -67     98   -478       N  
ATOM   3296  CA  LEU B  98      17.302  24.457  27.178  1.00 28.08           C  
ANISOU 3296  CA  LEU B  98     3904   3316   3451    -70     -1   -505       C  
ATOM   3297  C   LEU B  98      18.132  25.674  26.782  1.00 28.83           C  
ANISOU 3297  C   LEU B  98     3932   3378   3643    -96    -19   -554       C  
ATOM   3298  O   LEU B  98      18.873  26.232  27.606  1.00 42.02           O  
ANISOU 3298  O   LEU B  98     5613   5044   5307   -112    -86   -617       O  
ATOM   3299  CB  LEU B  98      17.932  23.172  26.646  1.00 30.37           C  
ANISOU 3299  CB  LEU B  98     4164   3619   3755    -46    -48   -454       C  
ATOM   3300  CG  LEU B  98      19.291  22.817  27.235  1.00 46.42           C  
ANISOU 3300  CG  LEU B  98     6185   5664   5790    -31   -168   -482       C  
ATOM   3301  CD1 LEU B  98      19.153  22.473  28.710  1.00 35.82           C  
ANISOU 3301  CD1 LEU B  98     4954   4334   4320    -28   -232   -488       C  
ATOM   3302  CD2 LEU B  98      19.911  21.669  26.462  1.00 47.47           C  
ANISOU 3302  CD2 LEU B  98     6262   5800   5973      8   -205   -449       C  
ATOM   3303  N   LEU B  99      18.019  26.096  25.520  1.00 27.81           N  
ANISOU 3303  N   LEU B  99     3741   3223   3601   -108     35   -523       N  
ATOM   3304  CA  LEU B  99      18.728  27.285  25.059  1.00 28.19           C  
ANISOU 3304  CA  LEU B  99     3738   3230   3743   -153     29   -552       C  
ATOM   3305  C   LEU B  99      18.385  28.498  25.915  1.00 39.44           C  
ANISOU 3305  C   LEU B  99     5214   4604   5168   -166     23   -621       C  
ATOM   3306  O   LEU B  99      19.275  29.244  26.341  1.00 39.68           O  
ANISOU 3306  O   LEU B  99     5229   4609   5238   -205    -32   -680       O  
ATOM   3307  CB  LEU B  99      18.393  27.550  23.591  1.00 27.68           C  
ANISOU 3307  CB  LEU B  99     3631   3144   3742   -168     96   -490       C  
ATOM   3308  CG  LEU B  99      19.025  28.788  22.954  1.00 35.86           C  
ANISOU 3308  CG  LEU B  99     4630   4127   4870   -232    102   -493       C  
ATOM   3309  CD1 LEU B  99      20.539  28.668  22.947  1.00 34.26           C  
ANISOU 3309  CD1 LEU B  99     4348   3960   4709   -277     57   -525       C  
ATOM   3310  CD2 LEU B  99      18.495  29.004  21.546  1.00 27.85           C  
ANISOU 3310  CD2 LEU B  99     3604   3092   3886   -246    165   -415       C  
ATOM   3311  N   VAL B 100      17.092  28.701  26.191  1.00 28.73           N  
ANISOU 3311  N   VAL B 100     3911   3234   3773   -134     78   -627       N  
ATOM   3312  CA  VAL B 100      16.686  29.866  26.974  1.00 29.53           C  
ANISOU 3312  CA  VAL B 100     4057   3282   3880   -133     80   -711       C  
ATOM   3313  C   VAL B 100      17.248  29.789  28.390  1.00 32.27           C  
ANISOU 3313  C   VAL B 100     4454   3665   4141   -141     16   -792       C  
ATOM   3314  O   VAL B 100      17.745  30.786  28.926  1.00 40.88           O  
ANISOU 3314  O   VAL B 100     5559   4710   5265   -167    -28   -874       O  
ATOM   3315  CB  VAL B 100      15.154  30.012  26.968  1.00 29.40           C  
ANISOU 3315  CB  VAL B 100     4066   3258   3845    -86    159   -715       C  
ATOM   3316  CG1 VAL B 100      14.708  30.993  28.037  1.00 30.43           C  
ANISOU 3316  CG1 VAL B 100     4246   3356   3959    -70    164   -830       C  
ATOM   3317  CG2 VAL B 100      14.685  30.489  25.605  1.00 28.98           C  
ANISOU 3317  CG2 VAL B 100     3971   3146   3894    -78    192   -652       C  
ATOM   3318  N   LEU B 101      17.192  28.610  29.015  1.00 30.22           N  
ANISOU 3318  N   LEU B 101     4232   3482   3769   -124      0   -767       N  
ATOM   3319  CA  LEU B 101      17.796  28.444  30.338  1.00 31.97           C  
ANISOU 3319  CA  LEU B 101     4516   3743   3890   -133    -80   -827       C  
ATOM   3320  C   LEU B 101      19.264  28.862  30.336  1.00 34.68           C  
ANISOU 3320  C   LEU B 101     4805   4066   4305   -167   -185   -865       C  
ATOM   3321  O   LEU B 101      19.671  29.811  31.032  1.00 46.27           O  
ANISOU 3321  O   LEU B 101     6293   5506   5779   -193   -233   -960       O  
ATOM   3322  CB  LEU B 101      17.672  26.988  30.789  1.00 31.01           C  
ANISOU 3322  CB  LEU B 101     4444   3689   3648   -116   -100   -761       C  
ATOM   3323  CG  LEU B 101      16.527  26.556  31.698  1.00 31.99           C  
ANISOU 3323  CG  LEU B 101     4666   3864   3627   -111    -35   -763       C  
ATOM   3324  CD1 LEU B 101      16.784  25.148  32.205  1.00 34.52           C  
ANISOU 3324  CD1 LEU B 101     5052   4230   3834   -111    -93   -687       C  
ATOM   3325  CD2 LEU B 101      16.383  27.511  32.852  1.00 41.36           C  
ANISOU 3325  CD2 LEU B 101     5917   5061   4738   -124    -37   -879       C  
ATOM   3326  N   LEU B 102      20.074  28.161  29.538  1.00 31.20           N  
ANISOU 3326  N   LEU B 102     4287   3642   3926   -168   -218   -803       N  
ATOM   3327  CA  LEU B 102      21.519  28.344  29.595  1.00 31.89           C  
ANISOU 3327  CA  LEU B 102     4301   3734   4080   -198   -319   -843       C  
ATOM   3328  C   LEU B 102      21.915  29.771  29.232  1.00 33.38           C  
ANISOU 3328  C   LEU B 102     4442   3856   4386   -261   -309   -900       C  
ATOM   3329  O   LEU B 102      22.731  30.396  29.923  1.00 54.14           O  
ANISOU 3329  O   LEU B 102     7061   6474   7034   -299   -394   -984       O  
ATOM   3330  CB  LEU B 102      22.201  27.330  28.677  1.00 31.36           C  
ANISOU 3330  CB  LEU B 102     4143   3703   4070   -180   -333   -778       C  
ATOM   3331  CG  LEU B 102      21.829  25.872  28.969  1.00 33.46           C  
ANISOU 3331  CG  LEU B 102     4465   4010   4237   -119   -354   -716       C  
ATOM   3332  CD1 LEU B 102      22.510  24.924  27.996  1.00 30.64           C  
ANISOU 3332  CD1 LEU B 102     4012   3675   3954    -91   -368   -672       C  
ATOM   3333  CD2 LEU B 102      22.160  25.502  30.407  1.00 32.03           C  
ANISOU 3333  CD2 LEU B 102     4370   3858   3943   -101   -471   -751       C  
ATOM   3334  N   GLU B 103      21.330  30.317  28.164  1.00 31.77           N  
ANISOU 3334  N   GLU B 103     4215   3597   4258   -277   -214   -853       N  
ATOM   3335  CA  GLU B 103      21.712  31.663  27.755  1.00 38.92           C  
ANISOU 3335  CA  GLU B 103     5090   4418   5278   -346   -209   -888       C  
ATOM   3336  C   GLU B 103      21.152  32.738  28.679  1.00 33.22           C  
ANISOU 3336  C   GLU B 103     4455   3627   4542   -346   -222   -982       C  
ATOM   3337  O   GLU B 103      21.696  33.848  28.711  1.00 41.56           O  
ANISOU 3337  O   GLU B 103     5499   4605   5688   -409   -256  -1039       O  
ATOM   3338  CB  GLU B 103      21.293  31.913  26.309  1.00 32.21           C  
ANISOU 3338  CB  GLU B 103     4207   3526   4505   -365   -119   -797       C  
ATOM   3339  CG  GLU B 103      22.130  31.123  25.317  1.00 34.05           C  
ANISOU 3339  CG  GLU B 103     4340   3825   4774   -389   -105   -734       C  
ATOM   3340  CD  GLU B 103      23.624  31.245  25.586  1.00 40.12           C  
ANISOU 3340  CD  GLU B 103     5017   4626   5603   -450   -180   -793       C  
ATOM   3341  OE1 GLU B 103      24.125  32.385  25.694  1.00 48.36           O  
ANISOU 3341  OE1 GLU B 103     6046   5604   6725   -530   -202   -840       O  
ATOM   3342  OE2 GLU B 103      24.298  30.199  25.698  1.00 40.43           O  
ANISOU 3342  OE2 GLU B 103     4992   4749   5621   -417   -223   -798       O  
ATOM   3343  N   ASN B 104      20.089  32.443  29.431  1.00 33.06           N  
ANISOU 3343  N   ASN B 104     4518   3632   4411   -282   -191  -1006       N  
ATOM   3344  CA  ASN B 104      19.690  33.340  30.513  1.00 34.12           C  
ANISOU 3344  CA  ASN B 104     4730   3725   4508   -275   -208  -1126       C  
ATOM   3345  C   ASN B 104      20.782  33.418  31.570  1.00 35.23           C  
ANISOU 3345  C   ASN B 104     4883   3899   4605   -312   -325  -1216       C  
ATOM   3346  O   ASN B 104      21.206  34.515  31.974  1.00 40.77           O  
ANISOU 3346  O   ASN B 104     5596   4529   5366   -356   -376  -1316       O  
ATOM   3347  CB  ASN B 104      18.374  32.876  31.137  1.00 33.90           C  
ANISOU 3347  CB  ASN B 104     4777   3749   4356   -207   -137  -1139       C  
ATOM   3348  CG  ASN B 104      17.166  33.299  30.332  1.00 33.39           C  
ANISOU 3348  CG  ASN B 104     4703   3625   4359   -167    -38  -1106       C  
ATOM   3349  OD1 ASN B 104      17.267  34.126  29.426  1.00 33.39           O  
ANISOU 3349  OD1 ASN B 104     4669   3526   4492   -187    -34  -1081       O  
ATOM   3350  ND2 ASN B 104      16.009  32.738  30.663  1.00 33.12           N  
ANISOU 3350  ND2 ASN B 104     4701   3651   4233   -114     38  -1102       N  
ATOM   3351  N   GLU B 105      21.262  32.254  32.022  1.00 35.08           N  
ANISOU 3351  N   GLU B 105     4862   3980   4486   -294   -383  -1183       N  
ATOM   3352  CA  GLU B 105      22.361  32.247  32.983  1.00 36.26           C  
ANISOU 3352  CA  GLU B 105     5014   4167   4595   -321   -518  -1262       C  
ATOM   3353  C   GLU B 105      23.562  33.021  32.450  1.00 36.86           C  
ANISOU 3353  C   GLU B 105     4983   4189   4832   -398   -579  -1296       C  
ATOM   3354  O   GLU B 105      24.134  33.867  33.151  1.00 45.34           O  
ANISOU 3354  O   GLU B 105     6070   5231   5928   -445   -662  -1407       O  
ATOM   3355  CB  GLU B 105      22.755  30.812  33.324  1.00 36.04           C  
ANISOU 3355  CB  GLU B 105     4991   4238   4463   -282   -584  -1197       C  
ATOM   3356  CG  GLU B 105      23.839  30.708  34.377  1.00 37.42           C  
ANISOU 3356  CG  GLU B 105     5177   4458   4582   -296   -747  -1272       C  
ATOM   3357  CD  GLU B 105      23.299  30.870  35.785  1.00 57.26           C  
ANISOU 3357  CD  GLU B 105     7838   7005   6912   -284   -778  -1350       C  
ATOM   3358  OE1 GLU B 105      22.206  30.337  36.069  1.00 47.50           O  
ANISOU 3358  OE1 GLU B 105     6697   5804   5548   -248   -690  -1305       O  
ATOM   3359  OE2 GLU B 105      23.963  31.535  36.608  1.00 49.03           O  
ANISOU 3359  OE2 GLU B 105     6816   5962   5851   -318   -887  -1464       O  
ATOM   3360  N   ARG B 106      23.948  32.759  31.197  1.00 36.06           N  
ANISOU 3360  N   ARG B 106     4777   4083   4843   -420   -534  -1206       N  
ATOM   3361  CA  ARG B 106      25.114  33.435  30.638  1.00 36.79           C  
ANISOU 3361  CA  ARG B 106     4755   4140   5085   -511   -573  -1231       C  
ATOM   3362  C   ARG B 106      24.880  34.928  30.450  1.00 37.48           C  
ANISOU 3362  C   ARG B 106     4873   4098   5271   -581   -541  -1281       C  
ATOM   3363  O   ARG B 106      25.842  35.702  30.441  1.00 40.85           O  
ANISOU 3363  O   ARG B 106     5236   4480   5803   -674   -599  -1339       O  
ATOM   3364  CB  ARG B 106      25.516  32.792  29.313  1.00 35.95           C  
ANISOU 3364  CB  ARG B 106     4533   4069   5056   -523   -511  -1127       C  
ATOM   3365  CG  ARG B 106      26.390  31.563  29.476  1.00 35.99           C  
ANISOU 3365  CG  ARG B 106     4457   4183   5036   -482   -590  -1118       C  
ATOM   3366  CD  ARG B 106      27.014  31.139  28.163  1.00 53.56           C  
ANISOU 3366  CD  ARG B 106     6544   6445   7361   -509   -529  -1055       C  
ATOM   3367  NE  ARG B 106      27.936  32.136  27.629  1.00 41.94           N  
ANISOU 3367  NE  ARG B 106     4964   4942   6028   -629   -520  -1091       N  
ATOM   3368  CZ  ARG B 106      29.187  32.297  28.045  1.00 39.30           C  
ANISOU 3368  CZ  ARG B 106     4518   4648   5767   -681   -620  -1176       C  
ATOM   3369  NH1 ARG B 106      29.668  31.535  29.015  1.00 38.45           N  
ANISOU 3369  NH1 ARG B 106     4398   4608   5604   -610   -753  -1232       N  
ATOM   3370  NH2 ARG B 106      29.954  33.223  27.493  1.00 43.55           N  
ANISOU 3370  NH2 ARG B 106     4956   5155   6436   -809   -593  -1202       N  
ATOM   3371  N   THR B 107      23.626  35.354  30.293  1.00 37.92           N  
ANISOU 3371  N   THR B 107     5019   4085   5305   -538   -455  -1262       N  
ATOM   3372  CA  THR B 107      23.351  36.782  30.187  1.00 37.85           C  
ANISOU 3372  CA  THR B 107     5054   3931   5395   -586   -441  -1316       C  
ATOM   3373  C   THR B 107      23.547  37.474  31.531  1.00 39.29           C  
ANISOU 3373  C   THR B 107     5304   4084   5541   -596   -532  -1475       C  
ATOM   3374  O   THR B 107      24.199  38.527  31.613  1.00 40.57           O  
ANISOU 3374  O   THR B 107     5454   4149   5813   -683   -588  -1548       O  
ATOM   3375  CB  THR B 107      21.936  37.011  29.661  1.00 37.08           C  
ANISOU 3375  CB  THR B 107     5024   3770   5295   -517   -339  -1261       C  
ATOM   3376  OG1 THR B 107      21.828  36.482  28.335  1.00 35.95           O  
ANISOU 3376  OG1 THR B 107     4823   3647   5190   -522   -266  -1118       O  
ATOM   3377  CG2 THR B 107      21.618  38.497  29.626  1.00 38.21           C  
ANISOU 3377  CG2 THR B 107     5225   3744   5550   -549   -343  -1325       C  
ATOM   3378  N   LEU B 108      22.999  36.891  32.603  1.00 42.52           N  
ANISOU 3378  N   LEU B 108     5790   4576   5789   -518   -547  -1531       N  
ATOM   3379  CA  LEU B 108      23.232  37.467  33.926  1.00 40.79           C  
ANISOU 3379  CA  LEU B 108     5643   4351   5506   -529   -638  -1691       C  
ATOM   3380  C   LEU B 108      24.719  37.476  34.269  1.00 41.83           C  
ANISOU 3380  C   LEU B 108     5698   4516   5678   -610   -775  -1742       C  
ATOM   3381  O   LEU B 108      25.238  38.466  34.807  1.00 43.34           O  
ANISOU 3381  O   LEU B 108     5905   4635   5927   -674   -856  -1867       O  
ATOM   3382  CB  LEU B 108      22.430  36.706  34.979  1.00 40.70           C  
ANISOU 3382  CB  LEU B 108     5730   4448   5287   -443   -621  -1725       C  
ATOM   3383  CG  LEU B 108      20.912  36.810  34.819  1.00 40.09           C  
ANISOU 3383  CG  LEU B 108     5714   4345   5171   -367   -485  -1712       C  
ATOM   3384  CD1 LEU B 108      20.202  36.065  35.933  1.00 40.31           C  
ANISOU 3384  CD1 LEU B 108     5836   4496   4984   -308   -459  -1752       C  
ATOM   3385  CD2 LEU B 108      20.474  38.263  34.786  1.00 41.09           C  
ANISOU 3385  CD2 LEU B 108     5876   4322   5415   -372   -465  -1821       C  
ATOM   3386  N   ASP B 109      25.427  36.391  33.943  1.00 41.17           N  
ANISOU 3386  N   ASP B 109     5525   4538   5579   -606   -809  -1655       N  
ATOM   3387  CA  ASP B 109      26.875  36.376  34.133  1.00 42.24           C  
ANISOU 3387  CA  ASP B 109     5554   4711   5782   -678   -940  -1703       C  
ATOM   3388  C   ASP B 109      27.548  37.477  33.321  1.00 45.99           C  
ANISOU 3388  C   ASP B 109     5937   5077   6458   -799   -928  -1717       C  
ATOM   3389  O   ASP B 109      28.526  38.084  33.774  1.00 44.48           O  
ANISOU 3389  O   ASP B 109     5694   4867   6340   -885  -1038  -1820       O  
ATOM   3390  CB  ASP B 109      27.444  35.011  33.752  1.00 43.36           C  
ANISOU 3390  CB  ASP B 109     5601   4973   5900   -636   -965  -1605       C  
ATOM   3391  CG  ASP B 109      26.998  33.912  34.689  1.00 48.46           C  
ANISOU 3391  CG  ASP B 109     6347   5718   6349   -536  -1013  -1590       C  
ATOM   3392  OD1 ASP B 109      26.601  34.224  35.831  1.00 61.66           O  
ANISOU 3392  OD1 ASP B 109     8142   7394   7891   -520  -1060  -1680       O  
ATOM   3393  OD2 ASP B 109      27.050  32.733  34.286  1.00 46.49           O  
ANISOU 3393  OD2 ASP B 109     6058   5538   6068   -479  -1002  -1489       O  
ATOM   3394  N   PHE B 110      27.036  37.747  32.120  1.00 42.00           N  
ANISOU 3394  N   PHE B 110     5416   4499   6043   -817   -800  -1612       N  
ATOM   3395  CA  PHE B 110      27.604  38.801  31.287  1.00 42.81           C  
ANISOU 3395  CA  PHE B 110     5452   4488   6324   -947   -777  -1601       C  
ATOM   3396  C   PHE B 110      27.469  40.164  31.958  1.00 44.33           C  
ANISOU 3396  C   PHE B 110     5736   4536   6573  -1000   -831  -1730       C  
ATOM   3397  O   PHE B 110      28.420  40.955  31.980  1.00 49.31           O  
ANISOU 3397  O   PHE B 110     6306   5103   7327  -1126   -898  -1795       O  
ATOM   3398  CB  PHE B 110      26.929  38.789  29.915  1.00 41.59           C  
ANISOU 3398  CB  PHE B 110     5297   4284   6220   -943   -636  -1452       C  
ATOM   3399  CG  PHE B 110      27.377  39.893  29.004  1.00 42.53           C  
ANISOU 3399  CG  PHE B 110     5381   4274   6504  -1083   -601  -1415       C  
ATOM   3400  CD1 PHE B 110      28.687  39.959  28.563  1.00 43.45           C  
ANISOU 3400  CD1 PHE B 110     5354   4431   6724  -1213   -624  -1412       C  
ATOM   3401  CD2 PHE B 110      26.477  40.853  28.569  1.00 42.66           C  
ANISOU 3401  CD2 PHE B 110     5507   4129   6575  -1086   -547  -1380       C  
ATOM   3402  CE1 PHE B 110      29.096  40.971  27.717  1.00 44.51           C  
ANISOU 3402  CE1 PHE B 110     5464   4447   7000  -1363   -581  -1366       C  
ATOM   3403  CE2 PHE B 110      26.879  41.865  27.722  1.00 43.72           C  
ANISOU 3403  CE2 PHE B 110     5630   4128   6853  -1223   -522  -1328       C  
ATOM   3404  CZ  PHE B 110      28.191  41.925  27.296  1.00 44.65           C  
ANISOU 3404  CZ  PHE B 110     5614   4289   7060  -1372   -533  -1315       C  
ATOM   3405  N   HIS B 111      26.291  40.453  32.520  1.00 44.14           N  
ANISOU 3405  N   HIS B 111     5851   4457   6465   -907   -801  -1779       N  
ATOM   3406  CA  HIS B 111      26.116  41.715  33.237  1.00 45.75           C  
ANISOU 3406  CA  HIS B 111     6148   4520   6716   -939   -855  -1926       C  
ATOM   3407  C   HIS B 111      27.058  41.800  34.432  1.00 47.27           C  
ANISOU 3407  C   HIS B 111     6327   4770   6864   -984  -1004  -2080       C  
ATOM   3408  O   HIS B 111      27.694  42.838  34.668  1.00 52.42           O  
ANISOU 3408  O   HIS B 111     6974   5312   7631  -1090  -1082  -2185       O  
ATOM   3409  CB  HIS B 111      24.668  41.871  33.695  1.00 45.39           C  
ANISOU 3409  CB  HIS B 111     6235   4436   6574   -813   -789  -1971       C  
ATOM   3410  CG  HIS B 111      23.695  42.070  32.577  1.00 44.36           C  
ANISOU 3410  CG  HIS B 111     6124   4215   6515   -770   -670  -1847       C  
ATOM   3411  ND1 HIS B 111      23.699  43.191  31.775  1.00 45.11           N  
ANISOU 3411  ND1 HIS B 111     6233   4123   6784   -841   -658  -1815       N  
ATOM   3412  CD2 HIS B 111      22.675  41.296  32.137  1.00 42.80           C  
ANISOU 3412  CD2 HIS B 111     5939   4085   6239   -666   -569  -1746       C  
ATOM   3413  CE1 HIS B 111      22.728  43.096  30.886  1.00 44.06           C  
ANISOU 3413  CE1 HIS B 111     6123   3950   6669   -774   -563  -1698       C  
ATOM   3414  NE2 HIS B 111      22.091  41.957  31.084  1.00 42.63           N  
ANISOU 3414  NE2 HIS B 111     5934   3924   6340   -668   -507  -1660       N  
ATOM   3415  N   ASP B 112      27.149  40.713  35.206  1.00 46.84           N  
ANISOU 3415  N   ASP B 112     6276   4883   6640   -908  -1054  -2094       N  
ATOM   3416  CA  ASP B 112      28.065  40.680  36.343  1.00 48.37           C  
ANISOU 3416  CA  ASP B 112     6460   5147   6771   -942  -1215  -2229       C  
ATOM   3417  C   ASP B 112      29.491  41.005  35.908  1.00 49.40           C  
ANISOU 3417  C   ASP B 112     6433   5264   7074  -1079  -1302  -2240       C  
ATOM   3418  O   ASP B 112      30.197  41.781  36.569  1.00 52.75           O  
ANISOU 3418  O   ASP B 112     6851   5640   7553  -1164  -1423  -2384       O  
ATOM   3419  CB  ASP B 112      27.998  39.305  37.010  1.00 47.68           C  
ANISOU 3419  CB  ASP B 112     6394   5239   6483   -842  -1257  -2193       C  
ATOM   3420  CG  ASP B 112      28.522  39.315  38.429  1.00 49.39           C  
ANISOU 3420  CG  ASP B 112     6670   5526   6569   -843  -1422  -2343       C  
ATOM   3421  OD1 ASP B 112      28.485  40.381  39.076  1.00 50.91           O  
ANISOU 3421  OD1 ASP B 112     6936   5632   6776   -887  -1471  -2498       O  
ATOM   3422  OD2 ASP B 112      28.963  38.247  38.903  1.00 49.34           O  
ANISOU 3422  OD2 ASP B 112     6647   5657   6443   -796  -1511  -2308       O  
ATOM   3423  N   SER B 113      29.921  40.440  34.779  1.00 48.37           N  
ANISOU 3423  N   SER B 113     6169   5176   7033  -1108  -1235  -2099       N  
ATOM   3424  CA  SER B 113      31.257  40.725  34.268  1.00 49.45           C  
ANISOU 3424  CA  SER B 113     6134   5316   7340  -1248  -1289  -2108       C  
ATOM   3425  C   SER B 113      31.401  42.188  33.875  1.00 50.76           C  
ANISOU 3425  C   SER B 113     6313   5296   7677  -1391  -1268  -2152       C  
ATOM   3426  O   SER B 113      32.453  42.797  34.101  1.00 52.54           O  
ANISOU 3426  O   SER B 113     6449   5495   8020  -1522  -1367  -2247       O  
ATOM   3427  CB  SER B 113      31.568  39.826  33.074  1.00 48.14           C  
ANISOU 3427  CB  SER B 113     5830   5240   7222  -1244  -1193  -1953       C  
ATOM   3428  OG  SER B 113      32.699  40.308  32.373  1.00 49.29           O  
ANISOU 3428  OG  SER B 113     5810   5370   7549  -1399  -1195  -1954       O  
ATOM   3429  N   ASN B 114      30.358  42.770  33.277  1.00 50.05           N  
ANISOU 3429  N   ASN B 114     6334   5069   7613  -1370  -1149  -2083       N  
ATOM   3430  CA  ASN B 114      30.442  44.175  32.887  1.00 51.45           C  
ANISOU 3430  CA  ASN B 114     6548   5042   7958  -1502  -1139  -2112       C  
ATOM   3431  C   ASN B 114      30.600  45.079  34.105  1.00 53.38           C  
ANISOU 3431  C   ASN B 114     6876   5196   8209  -1533  -1272  -2315       C  
ATOM   3432  O   ASN B 114      31.397  46.027  34.086  1.00 55.23           O  
ANISOU 3432  O   ASN B 114     7068   5318   8597  -1689  -1339  -2387       O  
ATOM   3433  CB  ASN B 114      29.212  44.569  32.071  1.00 50.43           C  
ANISOU 3433  CB  ASN B 114     6534   4780   7846  -1445  -1008  -2000       C  
ATOM   3434  CG  ASN B 114      29.211  43.948  30.691  1.00 49.01           C  
ANISOU 3434  CG  ASN B 114     6271   4658   7693  -1462   -883  -1803       C  
ATOM   3435  OD1 ASN B 114      30.262  43.581  30.163  1.00 52.72           O  
ANISOU 3435  OD1 ASN B 114     6590   5219   8224  -1564   -879  -1755       O  
ATOM   3436  ND2 ASN B 114      28.032  43.833  30.094  1.00 47.68           N  
ANISOU 3436  ND2 ASN B 114     6195   4443   7481  -1363   -781  -1698       N  
ATOM   3437  N   VAL B 115      29.862  44.793  35.179  1.00 55.46           N  
ANISOU 3437  N   VAL B 115     7259   5511   8302  -1395  -1310  -2415       N  
ATOM   3438  CA  VAL B 115      29.978  45.603  36.389  1.00 55.10           C  
ANISOU 3438  CA  VAL B 115     7303   5396   8236  -1415  -1436  -2626       C  
ATOM   3439  C   VAL B 115      31.361  45.441  37.012  1.00 56.56           C  
ANISOU 3439  C   VAL B 115     7370   5682   8439  -1514  -1597  -2726       C  
ATOM   3440  O   VAL B 115      32.020  46.428  37.363  1.00 58.63           O  
ANISOU 3440  O   VAL B 115     7622   5834   8820  -1640  -1699  -2859       O  
ATOM   3441  CB  VAL B 115      28.862  45.246  37.385  1.00 54.62           C  
ANISOU 3441  CB  VAL B 115     7395   5398   7962  -1249  -1420  -2708       C  
ATOM   3442  CG1 VAL B 115      29.052  46.005  38.687  1.00 56.81           C  
ANISOU 3442  CG1 VAL B 115     7765   5631   8190  -1269  -1553  -2942       C  
ATOM   3443  CG2 VAL B 115      27.506  45.558  36.784  1.00 53.55           C  
ANISOU 3443  CG2 VAL B 115     7356   5150   7842  -1157  -1272  -2637       C  
ATOM   3444  N   LYS B 116      31.822  44.192  37.155  1.00 55.68           N  
ANISOU 3444  N   LYS B 116     7163   5773   8218  -1456  -1634  -2667       N  
ATOM   3445  CA  LYS B 116      33.158  43.957  37.700  1.00 57.15           C  
ANISOU 3445  CA  LYS B 116     7215   6066   8432  -1533  -1802  -2757       C  
ATOM   3446  C   LYS B 116      34.223  44.697  36.898  1.00 58.40           C  
ANISOU 3446  C   LYS B 116     7212   6141   8837  -1726  -1811  -2750       C  
ATOM   3447  O   LYS B 116      35.112  45.341  37.470  1.00 60.54           O  
ANISOU 3447  O   LYS B 116     7427   6382   9195  -1843  -1953  -2897       O  
ATOM   3448  CB  LYS B 116      33.451  42.454  37.730  1.00 55.92           C  
ANISOU 3448  CB  LYS B 116     6972   6120   8154  -1429  -1827  -2663       C  
ATOM   3449  CG  LYS B 116      34.850  42.072  38.210  1.00 57.44           C  
ANISOU 3449  CG  LYS B 116     7002   6436   8388  -1485  -2012  -2743       C  
ATOM   3450  CD  LYS B 116      35.062  42.408  39.679  1.00 64.35           C  
ANISOU 3450  CD  LYS B 116     7976   7331   9143  -1476  -2204  -2933       C  
ATOM   3451  CE  LYS B 116      36.442  41.975  40.153  1.00 60.97           C  
ANISOU 3451  CE  LYS B 116     7378   7032   8755  -1519  -2409  -3010       C  
ATOM   3452  NZ  LYS B 116      36.636  40.500  40.083  1.00 81.35           N  
ANISOU 3452  NZ  LYS B 116     9889   9784  11236  -1390  -2439  -2895       N  
ATOM   3453  N   ASN B 117      34.128  44.642  35.568  1.00 61.99           N  
ANISOU 3453  N   ASN B 117     7593   6557   9402  -1773  -1656  -2583       N  
ATOM   3454  CA  ASN B 117      35.128  45.286  34.725  1.00 63.87           C  
ANISOU 3454  CA  ASN B 117     7675   6731   9861  -1973  -1638  -2557       C  
ATOM   3455  C   ASN B 117      35.068  46.802  34.846  1.00 60.38           C  
ANISOU 3455  C   ASN B 117     7330   6056   9555  -2110  -1665  -2650       C  
ATOM   3456  O   ASN B 117      36.108  47.469  34.817  1.00 62.40           O  
ANISOU 3456  O   ASN B 117     7473   6264   9973  -2294  -1739  -2724       O  
ATOM   3457  CB  ASN B 117      34.941  44.862  33.269  1.00 56.96           C  
ANISOU 3457  CB  ASN B 117     6729   5876   9039  -1988  -1454  -2351       C  
ATOM   3458  CG  ASN B 117      35.329  43.419  33.026  1.00 55.66           C  
ANISOU 3458  CG  ASN B 117     6421   5933   8794  -1892  -1439  -2277       C  
ATOM   3459  OD1 ASN B 117      36.073  42.822  33.804  1.00 60.72           O  
ANISOU 3459  OD1 ASN B 117     6965   6711   9394  -1857  -1580  -2373       O  
ATOM   3460  ND2 ASN B 117      34.831  42.853  31.933  1.00 56.74           N  
ANISOU 3460  ND2 ASN B 117     6547   6102   8911  -1845  -1280  -2109       N  
ATOM   3461  N   LEU B 118      33.865  47.367  34.967  1.00 59.88           N  
ANISOU 3461  N   LEU B 118     7469   5840   9442  -2027  -1609  -2653       N  
ATOM   3462  CA  LEU B 118      33.751  48.813  35.138  1.00 61.80           C  
ANISOU 3462  CA  LEU B 118     7822   5839   9820  -2137  -1650  -2755       C  
ATOM   3463  C   LEU B 118      34.386  49.254  36.452  1.00 63.94           C  
ANISOU 3463  C   LEU B 118     8101   6113  10081  -2182  -1840  -2991       C  
ATOM   3464  O   LEU B 118      35.160  50.222  36.495  1.00 66.16           O  
ANISOU 3464  O   LEU B 118     8355   6297  10487  -2343  -1891  -3032       O  
ATOM   3465  CB  LEU B 118      32.281  49.229  35.076  1.00 60.90           C  
ANISOU 3465  CB  LEU B 118     7913   5576   9650  -2001  -1561  -2730       C  
ATOM   3466  CG  LEU B 118      31.979  50.719  35.230  1.00 62.88           C  
ANISOU 3466  CG  LEU B 118     8302   5544  10043  -2078  -1602  -2836       C  
ATOM   3467  CD1 LEU B 118      32.627  51.520  34.115  1.00 65.22           C  
ANISOU 3467  CD1 LEU B 118     8538   5677  10566  -2292  -1562  -2720       C  
ATOM   3468  CD2 LEU B 118      30.482  50.954  35.254  1.00 61.95           C  
ANISOU 3468  CD2 LEU B 118     8365   5316   9857  -1902  -1522  -2828       C  
ATOM   3469  N   TYR B 119      34.072  48.541  37.537  1.00 63.45           N  
ANISOU 3469  N   TYR B 119     8099   6200   9810  -2026  -1918  -3089       N  
ATOM   3470  CA  TYR B 119      34.682  48.834  38.831  1.00 65.53           C  
ANISOU 3470  CA  TYR B 119     8384   6518   9995  -2044  -2086  -3271       C  
ATOM   3471  C   TYR B 119      36.202  48.755  38.753  1.00 67.56           C  
ANISOU 3471  C   TYR B 119     8434   6879  10357  -2194  -2181  -3268       C  
ATOM   3472  O   TYR B 119      36.908  49.622  39.282  1.00 74.01           O  
ANISOU 3472  O   TYR B 119     9251   7645  11227  -2305  -2270  -3361       O  
ATOM   3473  CB  TYR B 119      34.142  47.870  39.887  1.00 64.65           C  
ANISOU 3473  CB  TYR B 119     8360   6576   9628  -1862  -2153  -3352       C  
ATOM   3474  CG  TYR B 119      34.764  48.028  41.256  1.00 66.80           C  
ANISOU 3474  CG  TYR B 119     8669   6945   9769  -1864  -2318  -3504       C  
ATOM   3475  CD1 TYR B 119      34.312  48.999  42.137  1.00 70.53           C  
ANISOU 3475  CD1 TYR B 119     9315   7314  10170  -1850  -2339  -3642       C  
ATOM   3476  CD2 TYR B 119      35.794  47.194  41.674  1.00 67.30           C  
ANISOU 3476  CD2 TYR B 119     8593   7201   9775  -1873  -2455  -3511       C  
ATOM   3477  CE1 TYR B 119      34.873  49.145  43.392  1.00 75.21           C  
ANISOU 3477  CE1 TYR B 119     9948   7999  10632  -1859  -2488  -3783       C  
ATOM   3478  CE2 TYR B 119      36.362  47.333  42.927  1.00 69.42           C  
ANISOU 3478  CE2 TYR B 119     8902   7557   9917  -1874  -2616  -3642       C  
ATOM   3479  CZ  TYR B 119      35.898  48.310  43.782  1.00 76.99           C  
ANISOU 3479  CZ  TYR B 119    10040   8414  10797  -1874  -2629  -3777       C  
ATOM   3480  OH  TYR B 119      36.456  48.455  45.031  1.00 73.31           O  
ANISOU 3480  OH  TYR B 119     9619   8038  10196  -1883  -2787  -3910       O  
ATOM   3481  N   GLU B 120      36.725  47.719  38.089  1.00 65.75           N  
ANISOU 3481  N   GLU B 120     8019   6799  10164  -2197  -2161  -3170       N  
ATOM   3482  CA  GLU B 120      38.174  47.600  37.956  1.00 67.27           C  
ANISOU 3482  CA  GLU B 120     7987   7105  10467  -2328  -2238  -3168       C  
ATOM   3483  C   GLU B 120      38.758  48.730  37.117  1.00 68.85           C  
ANISOU 3483  C   GLU B 120     8123   7155  10883  -2544  -2161  -3112       C  
ATOM   3484  O   GLU B 120      39.898  49.148  37.350  1.00 78.89           O  
ANISOU 3484  O   GLU B 120     9271   8466  12240  -2679  -2245  -3165       O  
ATOM   3485  CB  GLU B 120      38.542  46.244  37.353  1.00 65.63           C  
ANISOU 3485  CB  GLU B 120     7590   7087  10260  -2269  -2215  -3077       C  
ATOM   3486  CG  GLU B 120      38.182  45.056  38.227  1.00 64.50           C  
ANISOU 3486  CG  GLU B 120     7505   7111   9890  -2064  -2312  -3107       C  
ATOM   3487  CD  GLU B 120      38.909  45.062  39.559  1.00 93.00           C  
ANISOU 3487  CD  GLU B 120    11115  10818  13402  -2048  -2526  -3253       C  
ATOM   3488  OE1 GLU B 120      40.046  45.578  39.624  1.00 90.90           O  
ANISOU 3488  OE1 GLU B 120    10709  10569  13261  -2182  -2597  -3296       O  
ATOM   3489  OE2 GLU B 120      38.339  44.550  40.544  1.00 91.89           O  
ANISOU 3489  OE2 GLU B 120    11125  10745  13043  -1902  -2611  -3310       O  
ATOM   3490  N   LYS B 121      38.000  49.232  36.140  1.00 67.89           N  
ANISOU 3490  N   LYS B 121     8087   6862  10846  -2584  -2005  -3000       N  
ATOM   3491  CA  LYS B 121      38.462  50.378  35.362  1.00 69.60           C  
ANISOU 3491  CA  LYS B 121     8286   6914  11245  -2794  -1934  -2930       C  
ATOM   3492  C   LYS B 121      38.602  51.613  36.241  1.00 75.88           C  
ANISOU 3492  C   LYS B 121     9215   7563  12053  -2862  -2035  -3061       C  
ATOM   3493  O   LYS B 121      39.653  52.267  36.256  1.00 74.51           O  
ANISOU 3493  O   LYS B 121     8947   7375  11991  -3043  -2086  -3088       O  
ATOM   3494  CB  LYS B 121      37.498  50.658  34.209  1.00 68.14           C  
ANISOU 3494  CB  LYS B 121     8205   6562  11123  -2799  -1764  -2773       C  
ATOM   3495  CG  LYS B 121      37.538  49.651  33.080  1.00 72.49           C  
ANISOU 3495  CG  LYS B 121     8606   7235  11703  -2796  -1635  -2624       C  
ATOM   3496  CD  LYS B 121      36.484  49.988  32.033  1.00 91.12           C  
ANISOU 3496  CD  LYS B 121    11106   9425  14091  -2782  -1478  -2460       C  
ATOM   3497  CE  LYS B 121      36.331  48.881  31.002  1.00101.79           C  
ANISOU 3497  CE  LYS B 121    12364  10948  15362  -2708  -1323  -2268       C  
ATOM   3498  NZ  LYS B 121      35.185  49.146  30.086  1.00 96.14           N  
ANISOU 3498  NZ  LYS B 121    11814  10092  14621  -2652  -1183  -2097       N  
ATOM   3499  N   VAL B 122      37.540  51.952  36.979  1.00 74.14           N  
ANISOU 3499  N   VAL B 122     9212   7237  11719  -2721  -2060  -3149       N  
ATOM   3500  CA  VAL B 122      37.579  53.139  37.831  1.00 74.27           C  
ANISOU 3500  CA  VAL B 122     9369   7108  11741  -2772  -2147  -3288       C  
ATOM   3501  C   VAL B 122      38.678  53.010  38.879  1.00 76.20           C  
ANISOU 3501  C   VAL B 122     9510   7509  11935  -2818  -2315  -3430       C  
ATOM   3502  O   VAL B 122      39.413  53.968  39.152  1.00 78.86           O  
ANISOU 3502  O   VAL B 122     9839   7760  12365  -2974  -2383  -3501       O  
ATOM   3503  CB  VAL B 122      36.200  53.379  38.475  1.00 73.52           C  
ANISOU 3503  CB  VAL B 122     9508   6911  11515  -2584  -2130  -3371       C  
ATOM   3504  CG1 VAL B 122      36.270  54.513  39.487  1.00 76.56           C  
ANISOU 3504  CG1 VAL B 122    10029   7175  11886  -2619  -2226  -3542       C  
ATOM   3505  CG2 VAL B 122      35.169  53.686  37.402  1.00 72.10           C  
ANISOU 3505  CG2 VAL B 122     9428   6550  11415  -2550  -1978  -3229       C  
ATOM   3506  N   LYS B 123      38.813  51.824  39.475  1.00 75.06           N  
ANISOU 3506  N   LYS B 123     9289   7588  11641  -2686  -2391  -3470       N  
ATOM   3507  CA  LYS B 123      39.883  51.590  40.441  1.00 76.92           C  
ANISOU 3507  CA  LYS B 123     9419   7986  11822  -2717  -2564  -3589       C  
ATOM   3508  C   LYS B 123      41.252  51.815  39.810  1.00 78.60           C  
ANISOU 3508  C   LYS B 123     9400   8238  12226  -2922  -2579  -3540       C  
ATOM   3509  O   LYS B 123      42.102  52.521  40.370  1.00 81.32           O  
ANISOU 3509  O   LYS B 123     9708   8566  12625  -3047  -2690  -3642       O  
ATOM   3510  CB  LYS B 123      39.769  50.172  40.998  1.00 85.32           C  
ANISOU 3510  CB  LYS B 123    10439   9278  12698  -2535  -2635  -3599       C  
ATOM   3511  CG  LYS B 123      40.905  49.754  41.908  1.00 77.12           C  
ANISOU 3511  CG  LYS B 123     9276   8423  11603  -2548  -2825  -3694       C  
ATOM   3512  CD  LYS B 123      40.755  48.298  42.304  1.00 75.44           C  
ANISOU 3512  CD  LYS B 123     9031   8420  11213  -2365  -2889  -3669       C  
ATOM   3513  CE  LYS B 123      41.821  47.874  43.295  1.00 77.46           C  
ANISOU 3513  CE  LYS B 123     9187   8849  11394  -2355  -3098  -3759       C  
ATOM   3514  NZ  LYS B 123      41.612  46.472  43.751  1.00 80.59           N  
ANISOU 3514  NZ  LYS B 123     9589   9431  11599  -2169  -3175  -3724       N  
ATOM   3515  N   SER B 124      41.476  51.228  38.631  1.00 77.14           N  
ANISOU 3515  N   SER B 124     9055   8112  12144  -2963  -2461  -3388       N  
ATOM   3516  CA  SER B 124      42.736  51.419  37.922  1.00 81.10           C  
ANISOU 3516  CA  SER B 124     9326   8665  12824  -3163  -2443  -3331       C  
ATOM   3517  C   SER B 124      42.975  52.877  37.553  1.00 93.61           C  
ANISOU 3517  C   SER B 124    10977  10031  14557  -3380  -2399  -3321       C  
ATOM   3518  O   SER B 124      44.126  53.269  37.333  1.00 87.01           O  
ANISOU 3518  O   SER B 124     9977   9231  13851  -3567  -2427  -3324       O  
ATOM   3519  CB  SER B 124      42.763  50.557  36.661  1.00 79.02           C  
ANISOU 3519  CB  SER B 124     8904   8495  12625  -3160  -2291  -3167       C  
ATOM   3520  OG  SER B 124      41.752  50.964  35.756  1.00 87.69           O  
ANISOU 3520  OG  SER B 124    10148   9415  13756  -3171  -2126  -3044       O  
ATOM   3521  N   GLN B 125      41.917  53.684  37.469  1.00 97.85           N  
ANISOU 3521  N   GLN B 125    11752  10343  15083  -3357  -2333  -3307       N  
ATOM   3522  CA  GLN B 125      42.101  55.111  37.230  1.00 91.92           C  
ANISOU 3522  CA  GLN B 125    11097   9365  14465  -3551  -2313  -3307       C  
ATOM   3523  C   GLN B 125      42.498  55.844  38.504  1.00 91.13           C  
ANISOU 3523  C   GLN B 125    11070   9226  14329  -3581  -2480  -3504       C  
ATOM   3524  O   GLN B 125      43.439  56.645  38.501  1.00 93.75           O  
ANISOU 3524  O   GLN B 125    11333   9504  14783  -3787  -2529  -3537       O  
ATOM   3525  CB  GLN B 125      40.826  55.720  36.652  1.00 95.43           C  
ANISOU 3525  CB  GLN B 125    11769   9571  14919  -3501  -2189  -3219       C  
ATOM   3526  CG  GLN B 125      40.671  55.528  35.166  1.00104.97           C  
ANISOU 3526  CG  GLN B 125    12920  10742  16221  -3578  -2017  -3002       C  
ATOM   3527  CD  GLN B 125      39.918  56.669  34.527  1.00 95.81           C  
ANISOU 3527  CD  GLN B 125    11970   9292  15141  -3646  -1928  -2912       C  
ATOM   3528  OE1 GLN B 125      40.479  57.431  33.742  1.00100.78           O  
ANISOU 3528  OE1 GLN B 125    12580   9810  15901  -3867  -1870  -2810       O  
ATOM   3529  NE2 GLN B 125      38.642  56.803  34.869  1.00 88.95           N  
ANISOU 3529  NE2 GLN B 125    11307   8299  14190  -3455  -1918  -2950       N  
ATOM   3530  N   LEU B 126      41.788  55.584  39.604  1.00 88.10           N  
ANISOU 3530  N   LEU B 126    10829   8874  13772  -3386  -2565  -3636       N  
ATOM   3531  CA  LEU B 126      41.993  56.371  40.814  1.00 87.68           C  
ANISOU 3531  CA  LEU B 126    10884   8762  13668  -3407  -2708  -3827       C  
ATOM   3532  C   LEU B 126      43.307  56.018  41.499  1.00 89.59           C  
ANISOU 3532  C   LEU B 126    10934   9202  13903  -3481  -2870  -3923       C  
ATOM   3533  O   LEU B 126      44.001  56.907  42.007  1.00 94.22           O  
ANISOU 3533  O   LEU B 126    11523   9721  14556  -3626  -2969  -4033       O  
ATOM   3534  CB  LEU B 126      40.817  56.176  41.770  1.00 86.54           C  
ANISOU 3534  CB  LEU B 126    10950   8610  13320  -3179  -2734  -3937       C  
ATOM   3535  CG  LEU B 126      39.449  56.588  41.222  1.00 84.96           C  
ANISOU 3535  CG  LEU B 126    10944   8211  13127  -3083  -2588  -3868       C  
ATOM   3536  CD1 LEU B 126      38.390  56.509  42.309  1.00 84.51           C  
ANISOU 3536  CD1 LEU B 126    11082   8160  12867  -2875  -2618  -4009       C  
ATOM   3537  CD2 LEU B 126      39.504  57.983  40.615  1.00 86.99           C  
ANISOU 3537  CD2 LEU B 126    11285   8196  13571  -3257  -2535  -3835       C  
ATOM   3538  N   LYS B 127      43.664  54.738  41.525  1.00107.89           N  
ANISOU 3538  N   LYS B 127    13087  11759  16147  -3380  -2905  -3884       N  
ATOM   3539  CA  LYS B 127      44.889  54.267  42.203  1.00100.24           C  
ANISOU 3539  CA  LYS B 127    11927  10994  15164  -3415  -3073  -3971       C  
ATOM   3540  C   LYS B 127      44.766  54.647  43.683  1.00 99.43           C  
ANISOU 3540  C   LYS B 127    11983  10890  14905  -3348  -3238  -4165       C  
ATOM   3541  O   LYS B 127      43.692  54.471  44.278  1.00101.28           O  
ANISOU 3541  O   LYS B 127    12420  11101  14961  -3177  -3229  -4213       O  
ATOM   3542  CB  LYS B 127      46.123  54.805  41.500  1.00 96.14           C  
ANISOU 3542  CB  LYS B 127    11199  10466  14865  -3661  -3061  -3927       C  
ATOM   3543  CG  LYS B 127      46.196  54.479  40.018  1.00 95.53           C  
ANISOU 3543  CG  LYS B 127    10981  10392  14923  -3737  -2877  -3733       C  
ATOM   3544  CD  LYS B 127      47.382  55.168  39.362  1.00100.31           C  
ANISOU 3544  CD  LYS B 127    11403  10975  15733  -4007  -2853  -3694       C  
ATOM   3545  CE  LYS B 127      47.387  54.950  37.858  1.00105.38           C  
ANISOU 3545  CE  LYS B 127    11936  11613  16493  -4098  -2651  -3495       C  
ATOM   3546  NZ  LYS B 127      48.496  55.692  37.199  1.00110.00           N  
ANISOU 3546  NZ  LYS B 127    12361  12171  17264  -4379  -2612  -3447       N  
ATOM   3547  N   ASN B 128      45.820  55.179  44.304  1.00103.98           N  
ANISOU 3547  N   ASN B 128    12475  11496  15537  -3483  -3385  -4282       N  
ATOM   3548  CA  ASN B 128      45.819  55.464  45.733  1.00102.87           C  
ANISOU 3548  CA  ASN B 128    12467  11381  15236  -3427  -3554  -4470       C  
ATOM   3549  C   ASN B 128      45.365  56.884  46.060  1.00 98.68           C  
ANISOU 3549  C   ASN B 128    12147  10605  14741  -3519  -3538  -4579       C  
ATOM   3550  O   ASN B 128      45.583  57.349  47.185  1.00101.07           O  
ANISOU 3550  O   ASN B 128    12538  10912  14953  -3529  -3681  -4751       O  
ATOM   3551  CB  ASN B 128      47.208  55.210  46.324  1.00 99.30           C  
ANISOU 3551  CB  ASN B 128    11812  11105  14812  -3507  -3745  -4551       C  
ATOM   3552  CG  ASN B 128      48.250  56.173  45.801  1.00102.05           C  
ANISOU 3552  CG  ASN B 128    12013  11361  15400  -3769  -3749  -4558       C  
ATOM   3553  OD1 ASN B 128      48.134  56.690  44.691  1.00101.54           O  
ANISOU 3553  OD1 ASN B 128    11926  11152  15501  -3896  -3590  -4443       O  
ATOM   3554  ND2 ASN B 128      49.280  56.419  46.602  1.00109.87           N  
ANISOU 3554  ND2 ASN B 128    12906  12435  16405  -3860  -3933  -4690       N  
ATOM   3555  N   ASN B 129      44.742  57.582  45.113  1.00 97.86           N  
ANISOU 3555  N   ASN B 129    12130  10287  14766  -3583  -3373  -4485       N  
ATOM   3556  CA  ASN B 129      44.156  58.887  45.392  1.00 99.55           C  
ANISOU 3556  CA  ASN B 129    12563  10249  15011  -3635  -3349  -4582       C  
ATOM   3557  C   ASN B 129      42.780  58.785  46.035  1.00 98.05           C  
ANISOU 3557  C   ASN B 129    12613  10016  14625  -3413  -3308  -4653       C  
ATOM   3558  O   ASN B 129      42.126  59.815  46.233  1.00 99.23           O  
ANISOU 3558  O   ASN B 129    12953   9952  14796  -3419  -3271  -4734       O  
ATOM   3559  CB  ASN B 129      44.069  59.714  44.107  1.00 99.62           C  
ANISOU 3559  CB  ASN B 129    12578  10033  15240  -3797  -3199  -4443       C  
ATOM   3560  CG  ASN B 129      45.429  60.152  43.607  1.00107.31           C  
ANISOU 3560  CG  ASN B 129    13352  11013  16409  -4060  -3238  -4407       C  
ATOM   3561  OD1 ASN B 129      46.458  59.650  44.058  1.00110.97           O  
ANISOU 3561  OD1 ASN B 129    13628  11674  16860  -4103  -3365  -4463       O  
ATOM   3562  ND2 ASN B 129      45.443  61.095  42.672  1.00103.05           N  
ANISOU 3562  ND2 ASN B 129    12852  10255  16047  -4239  -3130  -4311       N  
ATOM   3563  N   ALA B 130      42.333  57.575  46.358  1.00 95.67           N  
ANISOU 3563  N   ALA B 130    12304   9911  14136  -3221  -3311  -4625       N  
ATOM   3564  CA  ALA B 130      41.053  57.347  47.009  1.00 94.31           C  
ANISOU 3564  CA  ALA B 130    12343   9737  13753  -3012  -3267  -4689       C  
ATOM   3565  C   ALA B 130      41.090  55.964  47.636  1.00 92.83           C  
ANISOU 3565  C   ALA B 130    12102   9821  13346  -2859  -3342  -4683       C  
ATOM   3566  O   ALA B 130      41.798  55.074  47.156  1.00 91.77           O  
ANISOU 3566  O   ALA B 130    11771   9841  13257  -2877  -3371  -4573       O  
ATOM   3567  CB  ALA B 130      39.885  57.463  46.024  1.00 92.45           C  
ANISOU 3567  CB  ALA B 130    12203   9343  13581  -2933  -3072  -4562       C  
ATOM   3568  N   LYS B 131      40.333  55.789  48.712  1.00 92.95           N  
ANISOU 3568  N   LYS B 131    12298   9897  13121  -2711  -3373  -4801       N  
ATOM   3569  CA  LYS B 131      40.313  54.513  49.406  1.00 91.86           C  
ANISOU 3569  CA  LYS B 131    12149  10010  12745  -2570  -3452  -4794       C  
ATOM   3570  C   LYS B 131      39.059  53.729  49.041  1.00100.00           C  
ANISOU 3570  C   LYS B 131    13271  11069  13654  -2392  -3301  -4692       C  
ATOM   3571  O   LYS B 131      38.013  54.300  48.716  1.00 89.10           O  
ANISOU 3571  O   LYS B 131    12027   9526  12301  -2342  -3157  -4696       O  
ATOM   3572  CB  LYS B 131      40.403  54.699  50.923  1.00 96.74           C  
ANISOU 3572  CB  LYS B 131    12902  10716  13138  -2539  -3597  -4984       C  
ATOM   3573  CG  LYS B 131      39.081  54.886  51.642  1.00 98.33           C  
ANISOU 3573  CG  LYS B 131    13353  10883  13125  -2398  -3509  -5081       C  
ATOM   3574  CD  LYS B 131      39.304  54.867  53.145  1.00103.83           C  
ANISOU 3574  CD  LYS B 131    14165  11717  13571  -2376  -3661  -5252       C  
ATOM   3575  CE  LYS B 131      38.003  54.975  53.914  1.00105.49           C  
ANISOU 3575  CE  LYS B 131    14615  11923  13541  -2239  -3561  -5355       C  
ATOM   3576  NZ  LYS B 131      38.236  54.928  55.383  1.00109.21           N  
ANISOU 3576  NZ  LYS B 131    15206  12542  13748  -2231  -3704  -5516       N  
ATOM   3577  N   GLU B 132      39.185  52.403  49.088  1.00 98.81           N  
ANISOU 3577  N   GLU B 132    13042  11127  13374  -2294  -3340  -4601       N  
ATOM   3578  CA  GLU B 132      38.115  51.501  48.667  1.00 97.54           C  
ANISOU 3578  CA  GLU B 132    12941  11016  13105  -2136  -3206  -4488       C  
ATOM   3579  C   GLU B 132      37.240  51.149  49.865  1.00104.71           C  
ANISOU 3579  C   GLU B 132    14058  12027  13699  -1993  -3216  -4586       C  
ATOM   3580  O   GLU B 132      37.420  50.129  50.534  1.00110.44           O  
ANISOU 3580  O   GLU B 132    14790  12954  14216  -1915  -3313  -4569       O  
ATOM   3581  CB  GLU B 132      38.695  50.249  48.022  1.00 98.92           C  
ANISOU 3581  CB  GLU B 132    12922  11347  13314  -2108  -3236  -4332       C  
ATOM   3582  CG  GLU B 132      39.000  50.383  46.545  1.00 98.87           C  
ANISOU 3582  CG  GLU B 132    12744  11238  13585  -2204  -3128  -4192       C  
ATOM   3583  CD  GLU B 132      39.365  49.056  45.913  1.00107.44           C  
ANISOU 3583  CD  GLU B 132    13656  12484  14681  -2145  -3132  -4047       C  
ATOM   3584  OE1 GLU B 132      40.141  48.296  46.530  1.00108.04           O  
ANISOU 3584  OE1 GLU B 132    13646  12740  14663  -2113  -3289  -4063       O  
ATOM   3585  OE2 GLU B 132      38.863  48.765  44.808  1.00113.65           O  
ANISOU 3585  OE2 GLU B 132    14398  13216  15569  -2124  -2984  -3918       O  
ATOM   3586  N   ILE B 133      36.264  52.020  50.134  1.00113.11           N  
ANISOU 3586  N   ILE B 133    15301  12950  14728  -1959  -3110  -4687       N  
ATOM   3587  CA  ILE B 133      35.203  51.637  51.049  1.00115.64           C  
ANISOU 3587  CA  ILE B 133    15814  13365  14757  -1815  -3057  -4758       C  
ATOM   3588  C   ILE B 133      34.389  50.517  50.404  1.00116.89           C  
ANISOU 3588  C   ILE B 133    15963  13604  14846  -1687  -2932  -4602       C  
ATOM   3589  O   ILE B 133      34.405  50.318  49.182  1.00128.43           O  
ANISOU 3589  O   ILE B 133    17300  14993  16507  -1702  -2854  -4461       O  
ATOM   3590  CB  ILE B 133      34.304  52.828  51.418  1.00122.59           C  
ANISOU 3590  CB  ILE B 133    16869  14074  15635  -1796  -2955  -4908       C  
ATOM   3591  CG1 ILE B 133      33.897  53.603  50.164  1.00124.98           C  
ANISOU 3591  CG1 ILE B 133    17130  14136  16222  -1827  -2820  -4835       C  
ATOM   3592  CG2 ILE B 133      34.997  53.732  52.424  1.00119.89           C  
ANISOU 3592  CG2 ILE B 133    16584  13705  15263  -1897  -3096  -5093       C  
ATOM   3593  CD1 ILE B 133      33.082  54.845  50.457  1.00125.99           C  
ANISOU 3593  CD1 ILE B 133    17416  14070  16385  -1803  -2736  -4979       C  
ATOM   3594  N   GLY B 134      33.671  49.775  51.241  1.00118.59           N  
ANISOU 3594  N   GLY B 134    16316  13976  14767  -1568  -2910  -4626       N  
ATOM   3595  CA  GLY B 134      32.886  48.652  50.766  1.00122.25           C  
ANISOU 3595  CA  GLY B 134    16787  14533  15132  -1448  -2802  -4487       C  
ATOM   3596  C   GLY B 134      31.782  49.042  49.803  1.00113.82           C  
ANISOU 3596  C   GLY B 134    15740  13302  14203  -1392  -2597  -4441       C  
ATOM   3597  O   GLY B 134      31.609  50.224  49.485  1.00117.80           O  
ANISOU 3597  O   GLY B 134    16262  13609  14888  -1441  -2541  -4511       O  
ATOM   3598  N   ASN B 135      31.039  48.046  49.321  1.00 93.85           N  
ANISOU 3598  N   ASN B 135    13212  10852  11595  -1287  -2493  -4318       N  
ATOM   3599  CA  ASN B 135      29.882  48.240  48.449  1.00 85.36           C  
ANISOU 3599  CA  ASN B 135    12161   9653  10620  -1212  -2298  -4267       C  
ATOM   3600  C   ASN B 135      30.257  48.857  47.105  1.00 74.76           C  
ANISOU 3600  C   ASN B 135    10678   8113   9614  -1297  -2266  -4178       C  
ATOM   3601  O   ASN B 135      29.395  49.400  46.407  1.00 70.21           O  
ANISOU 3601  O   ASN B 135    10132   7381   9165  -1257  -2125  -4157       O  
ATOM   3602  CB  ASN B 135      28.805  49.084  49.140  1.00 99.33           C  
ANISOU 3602  CB  ASN B 135    14099  11352  12290  -1146  -2185  -4421       C  
ATOM   3603  CG  ASN B 135      27.405  48.563  48.888  1.00 97.89           C  
ANISOU 3603  CG  ASN B 135    13983  11205  12003  -1007  -1999  -4377       C  
ATOM   3604  OD1 ASN B 135      27.093  48.085  47.798  1.00 95.64           O  
ANISOU 3604  OD1 ASN B 135    13611  10882  11844   -974  -1920  -4237       O  
ATOM   3605  ND2 ASN B 135      26.552  48.647  49.904  1.00 96.96           N  
ANISOU 3605  ND2 ASN B 135    14017  11170  11654   -931  -1922  -4501       N  
ATOM   3606  N   GLY B 136      31.530  48.787  46.725  1.00 83.01           N  
ANISOU 3606  N   GLY B 136    11570   9166  10804  -1416  -2391  -4120       N  
ATOM   3607  CA  GLY B 136      31.948  49.265  45.422  1.00 80.74           C  
ANISOU 3607  CA  GLY B 136    11145   8717  10816  -1517  -2349  -4016       C  
ATOM   3608  C   GLY B 136      32.040  50.767  45.273  1.00 80.96           C  
ANISOU 3608  C   GLY B 136    11212   8518  11032  -1615  -2333  -4094       C  
ATOM   3609  O   GLY B 136      31.899  51.279  44.158  1.00 77.31           O  
ANISOU 3609  O   GLY B 136    10701   7884  10789  -1668  -2245  -3999       O  
ATOM   3610  N   CYS B 137      32.275  51.493  46.361  1.00 77.94           N  
ANISOU 3610  N   CYS B 137    10923   8124  10566  -1645  -2419  -4261       N  
ATOM   3611  CA  CYS B 137      32.431  52.938  46.319  1.00 90.07           C  
ANISOU 3611  CA  CYS B 137    12507   9441  12275  -1744  -2424  -4350       C  
ATOM   3612  C   CYS B 137      33.881  53.321  46.582  1.00 79.34           C  
ANISOU 3612  C   CYS B 137    11040   8096  11008  -1913  -2585  -4393       C  
ATOM   3613  O   CYS B 137      34.666  52.544  47.133  1.00 84.70           O  
ANISOU 3613  O   CYS B 137    11641   8970  11571  -1928  -2709  -4401       O  
ATOM   3614  CB  CYS B 137      31.522  53.627  47.342  1.00 85.07           C  
ANISOU 3614  CB  CYS B 137    12068   8758  11495  -1650  -2388  -4529       C  
ATOM   3615  SG  CYS B 137      29.752  53.433  47.050  1.00 90.55           S  
ANISOU 3615  SG  CYS B 137    12881   9411  12115  -1454  -2185  -4505       S  
ATOM   3616  N   PHE B 138      34.229  54.539  46.178  1.00 81.04           N  
ANISOU 3616  N   PHE B 138    11253   8100  11438  -2042  -2586  -4419       N  
ATOM   3617  CA  PHE B 138      35.553  55.100  46.407  1.00 86.64           C  
ANISOU 3617  CA  PHE B 138    11868   8795  12257  -2221  -2726  -4475       C  
ATOM   3618  C   PHE B 138      35.414  56.395  47.190  1.00 87.06           C  
ANISOU 3618  C   PHE B 138    12070   8691  12317  -2260  -2766  -4659       C  
ATOM   3619  O   PHE B 138      34.647  57.281  46.798  1.00 86.75           O  
ANISOU 3619  O   PHE B 138    12139   8436  12384  -2240  -2667  -4670       O  
ATOM   3620  CB  PHE B 138      36.285  55.366  45.088  1.00 91.95           C  
ANISOU 3620  CB  PHE B 138    12379   9360  13199  -2382  -2691  -4320       C  
ATOM   3621  CG  PHE B 138      36.541  54.134  44.272  1.00 80.50           C  
ANISOU 3621  CG  PHE B 138    10762   8063  11762  -2359  -2653  -4148       C  
ATOM   3622  CD1 PHE B 138      37.670  53.361  44.492  1.00 80.82           C  
ANISOU 3622  CD1 PHE B 138    10629   8302  11776  -2413  -2773  -4135       C  
ATOM   3623  CD2 PHE B 138      35.663  53.757  43.270  1.00 84.92           C  
ANISOU 3623  CD2 PHE B 138    11334   8566  12366  -2280  -2500  -4004       C  
ATOM   3624  CE1 PHE B 138      37.911  52.230  43.735  1.00 78.58           C  
ANISOU 3624  CE1 PHE B 138    10187   8157  11515  -2383  -2738  -3987       C  
ATOM   3625  CE2 PHE B 138      35.898  52.627  42.510  1.00 75.63           C  
ANISOU 3625  CE2 PHE B 138    10004   7527  11203  -2261  -2463  -3856       C  
ATOM   3626  CZ  PHE B 138      37.024  51.863  42.743  1.00 75.98           C  
ANISOU 3626  CZ  PHE B 138     9876   7768  11224  -2311  -2579  -3850       C  
ATOM   3627  N   GLU B 139      36.153  56.505  48.290  1.00102.44           N  
ANISOU 3627  N   GLU B 139    14025  10742  14154  -2312  -2918  -4805       N  
ATOM   3628  CA  GLU B 139      36.187  57.726  49.084  1.00 93.03           C  
ANISOU 3628  CA  GLU B 139    12963   9412  12973  -2369  -2976  -4995       C  
ATOM   3629  C   GLU B 139      37.414  58.531  48.679  1.00 94.11           C  
ANISOU 3629  C   GLU B 139    12983   9434  13342  -2591  -3068  -4990       C  
ATOM   3630  O   GLU B 139      38.549  58.088  48.888  1.00 94.87           O  
ANISOU 3630  O   GLU B 139    12930   9679  13437  -2687  -3196  -4983       O  
ATOM   3631  CB  GLU B 139      36.207  57.415  50.579  1.00101.19           C  
ANISOU 3631  CB  GLU B 139    14094  10626  13728  -2300  -3086  -5167       C  
ATOM   3632  CG  GLU B 139      35.706  58.562  51.444  1.00112.50           C  
ANISOU 3632  CG  GLU B 139    15714  11920  15112  -2287  -3089  -5377       C  
ATOM   3633  CD  GLU B 139      35.707  58.223  52.921  1.00123.17           C  
ANISOU 3633  CD  GLU B 139    17171  13462  16164  -2228  -3187  -5543       C  
ATOM   3634  OE1 GLU B 139      36.789  57.907  53.458  1.00123.99           O  
ANISOU 3634  OE1 GLU B 139    17192  13708  16212  -2318  -3353  -5574       O  
ATOM   3635  OE2 GLU B 139      34.624  58.267  53.542  1.00127.72           O  
ANISOU 3635  OE2 GLU B 139    17913  14054  16561  -2091  -3096  -5641       O  
ATOM   3636  N   PHE B 140      37.182  59.706  48.100  1.00 95.24           N  
ANISOU 3636  N   PHE B 140    13191   9313  13685  -2670  -3002  -4991       N  
ATOM   3637  CA  PHE B 140      38.268  60.516  47.569  1.00101.51           C  
ANISOU 3637  CA  PHE B 140    13882   9975  14711  -2898  -3061  -4964       C  
ATOM   3638  C   PHE B 140      39.129  61.090  48.688  1.00113.44           C  
ANISOU 3638  C   PHE B 140    15408  11517  16178  -3004  -3232  -5160       C  
ATOM   3639  O   PHE B 140      38.624  61.520  49.729  1.00109.88           O  
ANISOU 3639  O   PHE B 140    15121  11044  15586  -2923  -3270  -5343       O  
ATOM   3640  CB  PHE B 140      37.713  61.655  46.715  1.00106.85           C  
ANISOU 3640  CB  PHE B 140    14658  10345  15593  -2951  -2950  -4911       C  
ATOM   3641  CG  PHE B 140      37.192  61.215  45.380  1.00 98.70           C  
ANISOU 3641  CG  PHE B 140    13575   9264  14663  -2914  -2801  -4687       C  
ATOM   3642  CD1 PHE B 140      38.060  60.992  44.325  1.00103.21           C  
ANISOU 3642  CD1 PHE B 140    13971   9849  15393  -3079  -2781  -4513       C  
ATOM   3643  CD2 PHE B 140      35.835  61.033  45.175  1.00 96.18           C  
ANISOU 3643  CD2 PHE B 140    13379   8890  14276  -2718  -2677  -4653       C  
ATOM   3644  CE1 PHE B 140      37.585  60.589  43.093  1.00100.32           C  
ANISOU 3644  CE1 PHE B 140    13566   9442  15110  -3052  -2643  -4307       C  
ATOM   3645  CE2 PHE B 140      35.355  60.632  43.944  1.00 93.53           C  
ANISOU 3645  CE2 PHE B 140    12998   8507  14031  -2686  -2548  -4447       C  
ATOM   3646  CZ  PHE B 140      36.231  60.410  42.902  1.00 94.87           C  
ANISOU 3646  CZ  PHE B 140    13005   8689  14351  -2855  -2532  -4273       C  
ATOM   3647  N   TYR B 141      40.440  61.096  48.461  1.00114.65           N  
ANISOU 3647  N   TYR B 141    15383  11726  16453  -3191  -3333  -5126       N  
ATOM   3648  CA  TYR B 141      41.395  61.736  49.353  1.00114.14           C  
ANISOU 3648  CA  TYR B 141    15306  11669  16393  -3329  -3501  -5298       C  
ATOM   3649  C   TYR B 141      41.681  63.181  48.966  1.00117.00           C  
ANISOU 3649  C   TYR B 141    15722  11751  16983  -3516  -3492  -5339       C  
ATOM   3650  O   TYR B 141      42.583  63.797  49.542  1.00123.45           O  
ANISOU 3650  O   TYR B 141    16507  12551  17846  -3668  -3629  -5469       O  
ATOM   3651  CB  TYR B 141      42.706  60.945  49.383  1.00115.45           C  
ANISOU 3651  CB  TYR B 141    15236  12062  16570  -3427  -3628  -5250       C  
ATOM   3652  CG  TYR B 141      42.701  59.766  50.327  1.00116.63           C  
ANISOU 3652  CG  TYR B 141    15368  12487  16457  -3269  -3725  -5297       C  
ATOM   3653  CD1 TYR B 141      41.869  59.743  51.438  1.00119.14           C  
ANISOU 3653  CD1 TYR B 141    15890  12846  16534  -3116  -3746  -5443       C  
ATOM   3654  CD2 TYR B 141      43.536  58.678  50.111  1.00118.72           C  
ANISOU 3654  CD2 TYR B 141    15419  12974  16714  -3275  -3795  -5194       C  
ATOM   3655  CE1 TYR B 141      41.866  58.667  52.305  1.00124.39           C  
ANISOU 3655  CE1 TYR B 141    16559  13762  16943  -2986  -3835  -5472       C  
ATOM   3656  CE2 TYR B 141      43.539  57.598  50.971  1.00119.77           C  
ANISOU 3656  CE2 TYR B 141    15551  13348  16607  -3130  -3895  -5225       C  
ATOM   3657  CZ  TYR B 141      42.704  57.597  52.066  1.00123.57           C  
ANISOU 3657  CZ  TYR B 141    16251  13863  16838  -2993  -3915  -5358       C  
ATOM   3658  OH  TYR B 141      42.706  56.522  52.925  1.00122.65           O  
ANISOU 3658  OH  TYR B 141    16151  13986  16466  -2862  -4014  -5374       O  
ATOM   3659  N   HIS B 142      40.943  63.733  48.005  1.00110.87           N  
ANISOU 3659  N   HIS B 142    15027  10750  16347  -3512  -3343  -5230       N  
ATOM   3660  CA  HIS B 142      41.179  65.089  47.535  1.00109.95           C  
ANISOU 3660  CA  HIS B 142    14974  10350  16452  -3693  -3328  -5243       C  
ATOM   3661  C   HIS B 142      39.857  65.686  47.069  1.00115.00           C  
ANISOU 3661  C   HIS B 142    15806  10752  17138  -3568  -3186  -5208       C  
ATOM   3662  O   HIS B 142      38.806  65.042  47.125  1.00106.51           O  
ANISOU 3662  O   HIS B 142    14799   9746  15926  -3349  -3100  -5181       O  
ATOM   3663  CB  HIS B 142      42.227  65.108  46.418  1.00110.12           C  
ANISOU 3663  CB  HIS B 142    14802  10359  16680  -3925  -3307  -5066       C  
ATOM   3664  CG  HIS B 142      41.811  64.364  45.187  1.00110.80           C  
ANISOU 3664  CG  HIS B 142    14810  10477  16811  -3871  -3153  -4827       C  
ATOM   3665  ND1 HIS B 142      40.970  64.904  44.239  1.00108.25           N  
ANISOU 3665  ND1 HIS B 142    14606   9924  16599  -3854  -3009  -4702       N  
ATOM   3666  CD2 HIS B 142      42.118  63.119  44.751  1.00112.37           C  
ANISOU 3666  CD2 HIS B 142    14827  10910  16957  -3828  -3127  -4694       C  
ATOM   3667  CE1 HIS B 142      40.778  64.026  43.271  1.00105.21           C  
ANISOU 3667  CE1 HIS B 142    14119   9636  16222  -3810  -2899  -4501       C  
ATOM   3668  NE2 HIS B 142      41.463  62.934  43.557  1.00101.68           N  
ANISOU 3668  NE2 HIS B 142    13486   9468  15679  -3794  -2964  -4496       N  
ATOM   3669  N   LYS B 143      39.919  66.931  46.605  1.00125.79           N  
ANISOU 3669  N   LYS B 143    17259  11834  18702  -3709  -3164  -5208       N  
ATOM   3670  CA  LYS B 143      38.739  67.609  46.091  1.00129.49           C  
ANISOU 3670  CA  LYS B 143    17905  12049  19247  -3600  -3044  -5167       C  
ATOM   3671  C   LYS B 143      38.455  67.172  44.661  1.00122.23           C  
ANISOU 3671  C   LYS B 143    16917  11094  18430  -3607  -2902  -4898       C  
ATOM   3672  O   LYS B 143      39.371  66.999  43.852  1.00123.63           O  
ANISOU 3672  O   LYS B 143    16944  11308  18721  -3801  -2892  -4748       O  
ATOM   3673  CB  LYS B 143      38.920  69.126  46.150  1.00140.91           C  
ANISOU 3673  CB  LYS B 143    19483  13191  20868  -3746  -3085  -5268       C  
ATOM   3674  CG  LYS B 143      38.774  69.714  47.544  1.00148.04           C  
ANISOU 3674  CG  LYS B 143    20516  14069  21665  -3680  -3195  -5552       C  
ATOM   3675  CD  LYS B 143      37.388  69.440  48.112  1.00150.28           C  
ANISOU 3675  CD  LYS B 143    20939  14381  21778  -3388  -3127  -5646       C  
ATOM   3676  CE  LYS B 143      36.299  70.045  47.237  1.00153.10           C  
ANISOU 3676  CE  LYS B 143    21422  14475  22274  -3288  -2996  -5543       C  
ATOM   3677  NZ  LYS B 143      34.936  69.677  47.711  1.00157.94           N  
ANISOU 3677  NZ  LYS B 143    22141  15144  22726  -3000  -2916  -5621       N  
ATOM   3678  N   CYS B 144      37.171  66.999  44.352  1.00111.48           N  
ANISOU 3678  N   CYS B 144    15665   9666  17025  -3396  -2791  -4843       N  
ATOM   3679  CA  CYS B 144      36.736  66.507  43.045  1.00106.69           C  
ANISOU 3679  CA  CYS B 144    15011   9037  16488  -3368  -2656  -4594       C  
ATOM   3680  C   CYS B 144      35.419  67.194  42.700  1.00117.03           C  
ANISOU 3680  C   CYS B 144    16509  10101  17858  -3211  -2566  -4578       C  
ATOM   3681  O   CYS B 144      34.351  66.751  43.133  1.00109.37           O  
ANISOU 3681  O   CYS B 144    15607   9199  16752  -2971  -2522  -4641       O  
ATOM   3682  CB  CYS B 144      36.590  64.989  43.058  1.00107.60           C  
ANISOU 3682  CB  CYS B 144    14996   9454  16434  -3233  -2624  -4520       C  
ATOM   3683  SG  CYS B 144      36.153  64.235  41.473  1.00105.46           S  
ANISOU 3683  SG  CYS B 144    14646   9191  16232  -3207  -2466  -4221       S  
ATOM   3684  N   ASN B 145      35.496  68.272  41.925  1.00130.76           N  
ANISOU 3684  N   ASN B 145    18328  11557  19799  -3347  -2539  -4493       N  
ATOM   3685  CA  ASN B 145      34.303  68.980  41.481  1.00130.34           C  
ANISOU 3685  CA  ASN B 145    18444  11249  19829  -3203  -2464  -4457       C  
ATOM   3686  C   ASN B 145      33.665  68.214  40.321  1.00123.98           C  
ANISOU 3686  C   ASN B 145    17595  10486  19027  -3113  -2340  -4214       C  
ATOM   3687  O   ASN B 145      34.067  67.097  39.986  1.00115.75           O  
ANISOU 3687  O   ASN B 145    16398   9679  17903  -3139  -2308  -4100       O  
ATOM   3688  CB  ASN B 145      34.647  70.419  41.103  1.00132.58           C  
ANISOU 3688  CB  ASN B 145    18840  11207  20326  -3384  -2492  -4453       C  
ATOM   3689  CG  ASN B 145      35.726  70.502  40.041  1.00136.22           C  
ANISOU 3689  CG  ASN B 145    19199  11637  20921  -3671  -2465  -4249       C  
ATOM   3690  OD1 ASN B 145      36.690  69.737  40.060  1.00132.83           O  
ANISOU 3690  OD1 ASN B 145    18594  11442  20434  -3801  -2487  -4214       O  
ATOM   3691  ND2 ASN B 145      35.570  71.434  39.108  1.00142.87           N  
ANISOU 3691  ND2 ASN B 145    20148  12193  21941  -3771  -2413  -4113       N  
ATOM   3692  N   ASP B 146      32.650  68.816  39.694  1.00122.95           N  
ANISOU 3692  N   ASP B 146    17599  10124  18993  -2999  -2273  -4135       N  
ATOM   3693  CA  ASP B 146      31.983  68.164  38.572  1.00104.74           C  
ANISOU 3693  CA  ASP B 146    15266   7839  16693  -2909  -2162  -3904       C  
ATOM   3694  C   ASP B 146      32.944  67.910  37.420  1.00102.76           C  
ANISOU 3694  C   ASP B 146    14902   7613  16529  -3154  -2117  -3670       C  
ATOM   3695  O   ASP B 146      32.805  66.912  36.704  1.00109.41           O  
ANISOU 3695  O   ASP B 146    15647   8611  17314  -3118  -2039  -3503       O  
ATOM   3696  CB  ASP B 146      30.798  69.009  38.105  1.00108.40           C  
ANISOU 3696  CB  ASP B 146    15898   8024  17264  -2758  -2122  -3864       C  
ATOM   3697  CG  ASP B 146      29.747  69.181  39.184  1.00115.27           C  
ANISOU 3697  CG  ASP B 146    16861   8893  18044  -2498  -2145  -4093       C  
ATOM   3698  OD1 ASP B 146      30.015  68.793  40.341  1.00110.59           O  
ANISOU 3698  OD1 ASP B 146    16225   8489  17304  -2463  -2196  -4292       O  
ATOM   3699  OD2 ASP B 146      28.659  69.712  38.879  1.00119.10           O  
ANISOU 3699  OD2 ASP B 146    17459   9193  18601  -2330  -2111  -4076       O  
ATOM   3700  N   GLU B 147      33.924  68.794  37.228  1.00109.16           N  
ANISOU 3700  N   GLU B 147    15722   8279  17474  -3410  -2157  -3660       N  
ATOM   3701  CA  GLU B 147      34.953  68.568  36.218  1.00112.30           C  
ANISOU 3701  CA  GLU B 147    15998   8729  17943  -3670  -2104  -3460       C  
ATOM   3702  C   GLU B 147      35.711  67.272  36.489  1.00104.58           C  
ANISOU 3702  C   GLU B 147    14804   8100  16833  -3704  -2117  -3465       C  
ATOM   3703  O   GLU B 147      35.912  66.454  35.583  1.00101.39           O  
ANISOU 3703  O   GLU B 147    14282   7830  16412  -3753  -2032  -3275       O  
ATOM   3704  CB  GLU B 147      35.907  69.763  36.186  1.00123.26           C  
ANISOU 3704  CB  GLU B 147    17429   9919  19485  -3944  -2152  -3493       C  
ATOM   3705  CG  GLU B 147      37.227  69.517  35.478  1.00121.41           C  
ANISOU 3705  CG  GLU B 147    17032   9799  19301  -4247  -2115  -3354       C  
ATOM   3706  CD  GLU B 147      38.178  70.692  35.614  1.00139.56           C  
ANISOU 3706  CD  GLU B 147    19368  11918  21742  -4520  -2169  -3422       C  
ATOM   3707  OE1 GLU B 147      37.722  71.782  36.021  1.00139.27           O  
ANISOU 3707  OE1 GLU B 147    19510  11617  21789  -4477  -2221  -3534       O  
ATOM   3708  OE2 GLU B 147      39.381  70.526  35.322  1.00146.98           O  
ANISOU 3708  OE2 GLU B 147    20153  12981  22712  -4778  -2161  -3368       O  
ATOM   3709  N   CYS B 148      36.125  67.063  37.740  1.00102.05           N  
ANISOU 3709  N   CYS B 148    14429   7930  16416  -3671  -2226  -3684       N  
ATOM   3710  CA  CYS B 148      36.877  65.861  38.086  1.00101.52           C  
ANISOU 3710  CA  CYS B 148    14157   8189  16228  -3691  -2260  -3702       C  
ATOM   3711  C   CYS B 148      35.994  64.619  38.042  1.00110.02           C  
ANISOU 3711  C   CYS B 148    15195   9454  17154  -3446  -2199  -3652       C  
ATOM   3712  O   CYS B 148      36.431  63.557  37.581  1.00100.38           O  
ANISOU 3712  O   CYS B 148    13807   8448  15886  -3474  -2162  -3536       O  
ATOM   3713  CB  CYS B 148      37.510  66.025  39.467  1.00105.15           C  
ANISOU 3713  CB  CYS B 148    14590   8746  16616  -3712  -2405  -3950       C  
ATOM   3714  SG  CYS B 148      37.813  64.474  40.333  1.00101.35           S  
ANISOU 3714  SG  CYS B 148    13934   8657  15919  -3578  -2469  -4036       S  
ATOM   3715  N   MET B 149      34.755  64.729  38.529  1.00110.34           N  
ANISOU 3715  N   MET B 149    15381   9421  17120  -3204  -2187  -3743       N  
ATOM   3716  CA  MET B 149      33.827  63.604  38.460  1.00 95.85           C  
ANISOU 3716  CA  MET B 149    13523   7749  15147  -2975  -2119  -3695       C  
ATOM   3717  C   MET B 149      33.616  63.162  37.018  1.00 95.78           C  
ANISOU 3717  C   MET B 149    13465   7719  15210  -3008  -2001  -3432       C  
ATOM   3718  O   MET B 149      33.765  61.978  36.687  1.00 99.79           O  
ANISOU 3718  O   MET B 149    13834   8445  15637  -2979  -1961  -3339       O  
ATOM   3719  CB  MET B 149      32.495  63.983  39.107  1.00 98.11           C  
ANISOU 3719  CB  MET B 149    13979   7929  15368  -2730  -2108  -3831       C  
ATOM   3720  CG  MET B 149      32.561  64.198  40.611  1.00104.20           C  
ANISOU 3720  CG  MET B 149    14799   8774  16018  -2662  -2207  -4099       C  
ATOM   3721  SD  MET B 149      32.918  62.682  41.518  1.00 89.98           S  
ANISOU 3721  SD  MET B 149    12857   7358  13972  -2580  -2252  -4181       S  
ATOM   3722  CE  MET B 149      32.580  63.200  43.198  1.00 92.36           C  
ANISOU 3722  CE  MET B 149    13291   7677  14124  -2465  -2340  -4488       C  
ATOM   3723  N   GLU B 150      33.275  64.107  36.139  1.00 89.55           N  
ANISOU 3723  N   GLU B 150    12793   6664  14568  -3071  -1948  -3308       N  
ATOM   3724  CA  GLU B 150      33.125  63.780  34.727  1.00 87.97           C  
ANISOU 3724  CA  GLU B 150    12562   6433  14430  -3126  -1838  -3049       C  
ATOM   3725  C   GLU B 150      34.436  63.320  34.105  1.00 87.93           C  
ANISOU 3725  C   GLU B 150    12375   6575  14459  -3376  -1815  -2926       C  
ATOM   3726  O   GLU B 150      34.411  62.620  33.088  1.00 92.11           O  
ANISOU 3726  O   GLU B 150    12826   7188  14984  -3402  -1720  -2732       O  
ATOM   3727  CB  GLU B 150      32.571  64.980  33.956  1.00 89.87           C  
ANISOU 3727  CB  GLU B 150    12978   6349  14818  -3156  -1800  -2941       C  
ATOM   3728  CG  GLU B 150      31.206  65.451  34.433  1.00 91.71           C  
ANISOU 3728  CG  GLU B 150    13376   6430  15038  -2894  -1816  -3048       C  
ATOM   3729  CD  GLU B 150      30.155  64.359  34.394  1.00103.95           C  
ANISOU 3729  CD  GLU B 150    14896   8141  16459  -2645  -1760  -3019       C  
ATOM   3730  OE1 GLU B 150      30.197  63.515  33.473  1.00109.38           O  
ANISOU 3730  OE1 GLU B 150    15495   8941  17123  -2672  -1684  -2829       O  
ATOM   3731  OE2 GLU B 150      29.286  64.343  35.291  1.00108.75           O  
ANISOU 3731  OE2 GLU B 150    15567   8768  16985  -2426  -1785  -3193       O  
ATOM   3732  N   SER B 151      35.578  63.697  34.687  1.00 95.00           N  
ANISOU 3732  N   SER B 151    13195   7511  15388  -3560  -1897  -3039       N  
ATOM   3733  CA  SER B 151      36.846  63.140  34.227  1.00 96.03           C  
ANISOU 3733  CA  SER B 151    13118   7829  15540  -3777  -1882  -2951       C  
ATOM   3734  C   SER B 151      36.970  61.669  34.601  1.00 99.39           C  
ANISOU 3734  C   SER B 151    13368   8571  15826  -3647  -1897  -2982       C  
ATOM   3735  O   SER B 151      37.557  60.885  33.846  1.00 95.42           O  
ANISOU 3735  O   SER B 151    12696   8232  15328  -3740  -1834  -2844       O  
ATOM   3736  CB  SER B 151      38.020  63.929  34.805  1.00 94.69           C  
ANISOU 3736  CB  SER B 151    12904   7627  15446  -4000  -1979  -3075       C  
ATOM   3737  OG  SER B 151      38.264  63.566  36.152  1.00 96.87           O  
ANISOU 3737  OG  SER B 151    13126   8063  15618  -3898  -2107  -3298       O  
ATOM   3738  N   VAL B 152      36.431  61.279  35.757  1.00100.57           N  
ANISOU 3738  N   VAL B 152    13556   8811  15843  -3435  -1975  -3164       N  
ATOM   3739  CA  VAL B 152      36.454  59.872  36.144  1.00 87.22           C  
ANISOU 3739  CA  VAL B 152    11723   7407  14008  -3298  -1989  -3194       C  
ATOM   3740  C   VAL B 152      35.469  59.072  35.301  1.00 80.74           C  
ANISOU 3740  C   VAL B 152    10917   6615  13144  -3146  -1869  -3036       C  
ATOM   3741  O   VAL B 152      35.743  57.927  34.923  1.00 78.64           O  
ANISOU 3741  O   VAL B 152    10494   6559  12827  -3128  -1831  -2954       O  
ATOM   3742  CB  VAL B 152      36.158  59.724  37.648  1.00 84.14           C  
ANISOU 3742  CB  VAL B 152    11392   7108  13468  -3131  -2102  -3430       C  
ATOM   3743  CG1 VAL B 152      36.137  58.255  38.045  1.00 81.57           C  
ANISOU 3743  CG1 VAL B 152    10941   7071  12980  -2986  -2118  -3449       C  
ATOM   3744  CG2 VAL B 152      37.184  60.487  38.466  1.00 87.33           C  
ANISOU 3744  CG2 VAL B 152    11776   7492  13914  -3289  -2229  -3585       C  
ATOM   3745  N   LYS B 153      34.313  59.662  34.988  1.00 90.46           N  
ANISOU 3745  N   LYS B 153    12332   7637  14400  -3032  -1813  -2995       N  
ATOM   3746  CA  LYS B 153      33.280  58.928  34.264  1.00 84.54           C  
ANISOU 3746  CA  LYS B 153    11607   6910  13605  -2870  -1711  -2859       C  
ATOM   3747  C   LYS B 153      33.752  58.528  32.870  1.00 86.00           C  
ANISOU 3747  C   LYS B 153    11681   7128  13867  -3022  -1610  -2622       C  
ATOM   3748  O   LYS B 153      33.706  57.348  32.504  1.00 99.80           O  
ANISOU 3748  O   LYS B 153    13305   9068  15547  -2960  -1558  -2546       O  
ATOM   3749  CB  LYS B 153      32.003  59.762  34.185  1.00 85.24           C  
ANISOU 3749  CB  LYS B 153    11906   6756  13726  -2723  -1682  -2863       C  
ATOM   3750  CG  LYS B 153      31.302  59.931  35.518  1.00 83.61           C  
ANISOU 3750  CG  LYS B 153    11799   6558  13411  -2528  -1749  -3095       C  
ATOM   3751  CD  LYS B 153      30.037  60.752  35.370  1.00 82.77           C  
ANISOU 3751  CD  LYS B 153    11876   6218  13354  -2375  -1714  -3100       C  
ATOM   3752  CE  LYS B 153      29.322  60.899  36.698  1.00 83.30           C  
ANISOU 3752  CE  LYS B 153    12030   6316  13304  -2182  -1760  -3340       C  
ATOM   3753  NZ  LYS B 153      28.126  61.771  36.567  1.00 84.86           N  
ANISOU 3753  NZ  LYS B 153    12387   6286  13570  -2030  -1729  -3360       N  
ATOM   3754  N   ASN B 154      34.214  59.494  32.078  1.00 95.87           N  
ANISOU 3754  N   ASN B 154    12976   8198  15253  -3227  -1575  -2504       N  
ATOM   3755  CA  ASN B 154      34.639  59.210  30.712  1.00 98.31           C  
ANISOU 3755  CA  ASN B 154    13198   8534  15620  -3387  -1462  -2272       C  
ATOM   3756  C   ASN B 154      36.037  58.604  30.632  1.00 99.99           C  
ANISOU 3756  C   ASN B 154    13172   8977  15840  -3575  -1464  -2267       C  
ATOM   3757  O   ASN B 154      36.598  58.527  29.535  1.00106.26           O  
ANISOU 3757  O   ASN B 154    13884   9802  16690  -3755  -1366  -2090       O  
ATOM   3758  CB  ASN B 154      34.567  60.480  29.857  1.00106.82           C  
ANISOU 3758  CB  ASN B 154    14431   9334  16823  -3541  -1411  -2137       C  
ATOM   3759  CG  ASN B 154      35.431  61.605  30.395  1.00127.55           C  
ANISOU 3759  CG  ASN B 154    17087  11837  19540  -3731  -1487  -2250       C  
ATOM   3760  OD1 ASN B 154      36.217  61.418  31.323  1.00138.87           O  
ANISOU 3760  OD1 ASN B 154    18406  13412  20947  -3774  -1578  -2415       O  
ATOM   3761  ND2 ASN B 154      35.290  62.788  29.806  1.00138.17           N  
ANISOU 3761  ND2 ASN B 154    18589  12914  20995  -3845  -1453  -2161       N  
ATOM   3762  N   GLY B 155      36.610  58.183  31.757  1.00 78.81           N  
ANISOU 3762  N   GLY B 155    10379   6465  13100  -3534  -1573  -2455       N  
ATOM   3763  CA  GLY B 155      37.893  57.509  31.750  1.00 79.08           C  
ANISOU 3763  CA  GLY B 155    10166   6738  13142  -3671  -1590  -2464       C  
ATOM   3764  C   GLY B 155      39.060  58.387  31.351  1.00 88.55           C  
ANISOU 3764  C   GLY B 155    11302   7875  14466  -3965  -1589  -2420       C  
ATOM   3765  O   GLY B 155      39.893  57.985  30.534  1.00 91.83           O  
ANISOU 3765  O   GLY B 155    11540   8425  14926  -4125  -1513  -2298       O  
ATOM   3766  N   THR B 156      39.139  59.586  31.926  1.00 89.58           N  
ANISOU 3766  N   THR B 156    11573   7808  14655  -4043  -1667  -2524       N  
ATOM   3767  CA  THR B 156      40.231  60.517  31.652  1.00 97.49           C  
ANISOU 3767  CA  THR B 156    12534   8732  15777  -4335  -1677  -2501       C  
ATOM   3768  C   THR B 156      40.719  61.162  32.944  1.00 90.40           C  
ANISOU 3768  C   THR B 156    11659   7799  14891  -4360  -1835  -2729       C  
ATOM   3769  O   THR B 156      41.009  62.362  32.988  1.00 93.34           O  
ANISOU 3769  O   THR B 156    12139   7966  15359  -4527  -1861  -2758       O  
ATOM   3770  CB  THR B 156      39.811  61.590  30.646  1.00101.62           C  
ANISOU 3770  CB  THR B 156    13248   8975  16388  -4469  -1573  -2339       C  
ATOM   3771  OG1 THR B 156      38.586  62.199  31.073  1.00102.53           O  
ANISOU 3771  OG1 THR B 156    13603   8863  16490  -4276  -1603  -2406       O  
ATOM   3772  CG2 THR B 156      39.622  60.991  29.256  1.00 96.91           C  
ANISOU 3772  CG2 THR B 156    12602   8440  15777  -4511  -1413  -2095       C  
ATOM   3773  N   TYR B 157      40.821  60.374  34.012  1.00 90.77           N  
ANISOU 3773  N   TYR B 157    11611   8043  14835  -4198  -1943  -2894       N  
ATOM   3774  CA  TYR B 157      41.255  60.906  35.297  1.00 91.54           C  
ANISOU 3774  CA  TYR B 157    11734   8128  14919  -4207  -2100  -3116       C  
ATOM   3775  C   TYR B 157      42.756  61.163  35.294  1.00 99.70           C  
ANISOU 3775  C   TYR B 157    12577   9255  16050  -4467  -2158  -3138       C  
ATOM   3776  O   TYR B 157      43.534  60.409  34.703  1.00101.39           O  
ANISOU 3776  O   TYR B 157    12566   9669  16288  -4552  -2114  -3041       O  
ATOM   3777  CB  TYR B 157      40.888  59.943  36.428  1.00 89.68           C  
ANISOU 3777  CB  TYR B 157    11469   8086  14518  -3956  -2196  -3272       C  
ATOM   3778  CG  TYR B 157      41.405  60.356  37.792  1.00100.17           C  
ANISOU 3778  CG  TYR B 157    12810   9444  15804  -3963  -2365  -3501       C  
ATOM   3779  CD1 TYR B 157      40.778  61.358  38.523  1.00100.76           C  
ANISOU 3779  CD1 TYR B 157    13105   9312  15866  -3910  -2418  -3639       C  
ATOM   3780  CD2 TYR B 157      42.515  59.736  38.353  1.00110.73           C  
ANISOU 3780  CD2 TYR B 157    13939  11018  17114  -4014  -2475  -3582       C  
ATOM   3781  CE1 TYR B 157      41.247  61.735  39.771  1.00104.44           C  
ANISOU 3781  CE1 TYR B 157    13588   9810  16283  -3921  -2570  -3852       C  
ATOM   3782  CE2 TYR B 157      42.991  60.107  39.601  1.00114.58           C  
ANISOU 3782  CE2 TYR B 157    14444  11536  17553  -4022  -2637  -3787       C  
ATOM   3783  CZ  TYR B 157      42.353  61.106  40.305  1.00112.55           C  
ANISOU 3783  CZ  TYR B 157    14414  11074  17274  -3981  -2682  -3922       C  
ATOM   3784  OH  TYR B 157      42.821  61.478  41.545  1.00121.66           O  
ANISOU 3784  OH  TYR B 157    15591  12262  18371  -3994  -2841  -4130       O  
ATOM   3785  N   ASP B 158      43.161  62.236  35.968  1.00109.83           N  
ANISOU 3785  N   ASP B 158    13942  10396  17392  -4589  -2258  -3274       N  
ATOM   3786  CA  ASP B 158      44.558  62.647  36.035  1.00115.82           C  
ANISOU 3786  CA  ASP B 158    14538  11215  18255  -4850  -2326  -3311       C  
ATOM   3787  C   ASP B 158      45.105  62.279  37.411  1.00121.16           C  
ANISOU 3787  C   ASP B 158    15117  12065  18852  -4765  -2507  -3532       C  
ATOM   3788  O   ASP B 158      44.711  62.870  38.422  1.00108.58           O  
ANISOU 3788  O   ASP B 158    13686  10360  17209  -4684  -2608  -3706       O  
ATOM   3789  CB  ASP B 158      44.692  64.144  35.769  1.00111.14           C  
ANISOU 3789  CB  ASP B 158    14107  10330  17792  -5075  -2312  -3301       C  
ATOM   3790  CG  ASP B 158      46.096  64.542  35.371  1.00111.12           C  
ANISOU 3790  CG  ASP B 158    13926  10379  17914  -5395  -2325  -3259       C  
ATOM   3791  OD1 ASP B 158      47.059  63.963  35.915  1.00111.41           O  
ANISOU 3791  OD1 ASP B 158    13738  10651  17943  -5423  -2427  -3351       O  
ATOM   3792  OD2 ASP B 158      46.237  65.431  34.507  1.00108.76           O  
ANISOU 3792  OD2 ASP B 158    13714   9889  17721  -5620  -2233  -3132       O  
ATOM   3793  N   TYR B 159      46.016  61.310  37.446  1.00129.51           N  
ANISOU 3793  N   TYR B 159    15913  13400  19897  -4779  -2547  -3528       N  
ATOM   3794  CA  TYR B 159      46.558  60.825  38.710  1.00129.44           C  
ANISOU 3794  CA  TYR B 159    15802  13579  19799  -4684  -2724  -3722       C  
ATOM   3795  C   TYR B 159      47.575  61.794  39.315  1.00133.85           C  
ANISOU 3795  C   TYR B 159    16324  14078  20453  -4900  -2856  -3857       C  
ATOM   3796  O   TYR B 159      47.434  62.150  40.492  1.00146.98           O  
ANISOU 3796  O   TYR B 159    18101  15706  22039  -4824  -2994  -4048       O  
ATOM   3797  CB  TYR B 159      47.170  59.431  38.533  1.00124.78           C  
ANISOU 3797  CB  TYR B 159    14943  13298  19170  -4605  -2729  -3672       C  
ATOM   3798  CG  TYR B 159      48.028  58.987  39.695  1.00128.89           C  
ANISOU 3798  CG  TYR B 159    15320  14021  19632  -4561  -2923  -3848       C  
ATOM   3799  CD1 TYR B 159      47.455  58.590  40.896  1.00125.84           C  
ANISOU 3799  CD1 TYR B 159    15055  13693  19066  -4338  -3045  -3996       C  
ATOM   3800  CD2 TYR B 159      49.412  58.962  39.590  1.00133.47           C  
ANISOU 3800  CD2 TYR B 159    15643  14739  20329  -4743  -2985  -3862       C  
ATOM   3801  CE1 TYR B 159      48.239  58.183  41.961  1.00127.39           C  
ANISOU 3801  CE1 TYR B 159    15136  14074  19194  -4299  -3231  -4145       C  
ATOM   3802  CE2 TYR B 159      50.204  58.557  40.650  1.00132.66           C  
ANISOU 3802  CE2 TYR B 159    15410  14820  20177  -4696  -3175  -4019       C  
ATOM   3803  CZ  TYR B 159      49.612  58.169  41.833  1.00128.84           C  
ANISOU 3803  CZ  TYR B 159    15065  14384  19506  -4474  -3302  -4157       C  
ATOM   3804  OH  TYR B 159      50.396  57.765  42.889  1.00127.63           O  
ANISOU 3804  OH  TYR B 159    14795  14411  19288  -4428  -3499  -4303       O  
ATOM   3805  N   PRO B 160      48.606  62.246  38.583  1.00129.33           N  
ANISOU 3805  N   PRO B 160    15599  13499  20040  -5175  -2820  -3772       N  
ATOM   3806  CA  PRO B 160      49.579  63.159  39.208  1.00133.57           C  
ANISOU 3806  CA  PRO B 160    16098  13984  20669  -5386  -2955  -3911       C  
ATOM   3807  C   PRO B 160      48.998  64.508  39.595  1.00129.72           C  
ANISOU 3807  C   PRO B 160    15894  13187  20208  -5448  -2978  -4002       C  
ATOM   3808  O   PRO B 160      49.569  65.178  40.464  1.00138.58           O  
ANISOU 3808  O   PRO B 160    17029  14266  21359  -5547  -3122  -4174       O  
ATOM   3809  CB  PRO B 160      50.666  63.315  38.133  1.00134.38           C  
ANISOU 3809  CB  PRO B 160    15984  14139  20936  -5669  -2872  -3761       C  
ATOM   3810  CG  PRO B 160      50.492  62.146  37.235  1.00133.43           C  
ANISOU 3810  CG  PRO B 160    15716  14200  20783  -5558  -2738  -3591       C  
ATOM   3811  CD  PRO B 160      49.022  61.892  37.213  1.00122.61           C  
ANISOU 3811  CD  PRO B 160    14582  12718  19286  -5313  -2663  -3555       C  
ATOM   3812  N   LYS B 161      47.886  64.927  38.989  1.00129.87           N  
ANISOU 3812  N   LYS B 161    16136  12986  20223  -5386  -2846  -3899       N  
ATOM   3813  CA  LYS B 161      47.297  66.224  39.302  1.00125.13           C  
ANISOU 3813  CA  LYS B 161    15804  12076  19665  -5427  -2860  -3986       C  
ATOM   3814  C   LYS B 161      46.748  66.298  40.723  1.00124.95           C  
ANISOU 3814  C   LYS B 161    15917  12045  19512  -5215  -3000  -4221       C  
ATOM   3815  O   LYS B 161      46.398  67.393  41.176  1.00145.98           O  
ANISOU 3815  O   LYS B 161    18782  14470  22214  -5248  -3039  -4338       O  
ATOM   3816  CB  LYS B 161      46.190  66.547  38.295  1.00117.64           C  
ANISOU 3816  CB  LYS B 161    15049  10909  18741  -5376  -2687  -3813       C  
ATOM   3817  CG  LYS B 161      45.833  68.023  38.204  1.00117.71           C  
ANISOU 3817  CG  LYS B 161    15299  10567  18858  -5500  -2669  -3844       C  
ATOM   3818  CD  LYS B 161      44.641  68.252  37.291  1.00113.97           C  
ANISOU 3818  CD  LYS B 161    15019   9888  18397  -5397  -2513  -3682       C  
ATOM   3819  CE  LYS B 161      44.222  69.714  37.291  1.00125.04           C  
ANISOU 3819  CE  LYS B 161    16667  10928  19912  -5481  -2506  -3730       C  
ATOM   3820  NZ  LYS B 161      43.006  69.943  36.462  1.00117.55           N  
ANISOU 3820  NZ  LYS B 161    15909   9774  18982  -5348  -2371  -3581       N  
ATOM   3821  N   TYR B 162      46.671  65.173  41.439  1.00112.44           N  
ANISOU 3821  N   TYR B 162    14236  10714  17772  -5003  -3074  -4296       N  
ATOM   3822  CA  TYR B 162      46.193  65.187  42.816  1.00112.76           C  
ANISOU 3822  CA  TYR B 162    14407  10776  17661  -4814  -3204  -4515       C  
ATOM   3823  C   TYR B 162      47.055  64.345  43.750  1.00113.17           C  
ANISOU 3823  C   TYR B 162    14271  11118  17610  -4771  -3366  -4636       C  
ATOM   3824  O   TYR B 162      46.635  64.088  44.887  1.00112.98           O  
ANISOU 3824  O   TYR B 162    14343  11168  17416  -4590  -3468  -4797       O  
ATOM   3825  CB  TYR B 162      44.742  64.699  42.891  1.00111.26           C  
ANISOU 3825  CB  TYR B 162    14388  10560  17327  -4525  -3119  -4493       C  
ATOM   3826  CG  TYR B 162      43.777  65.489  42.037  1.00111.31           C  
ANISOU 3826  CG  TYR B 162    14588  10279  17426  -4524  -2972  -4381       C  
ATOM   3827  CD1 TYR B 162      43.226  66.678  42.496  1.00111.28           C  
ANISOU 3827  CD1 TYR B 162    14809  10014  17460  -4521  -2996  -4508       C  
ATOM   3828  CD2 TYR B 162      43.411  65.042  40.775  1.00113.95           C  
ANISOU 3828  CD2 TYR B 162    14883  10605  17810  -4519  -2814  -4152       C  
ATOM   3829  CE1 TYR B 162      42.341  67.402  41.719  1.00112.86           C  
ANISOU 3829  CE1 TYR B 162    15185   9944  17752  -4504  -2873  -4405       C  
ATOM   3830  CE2 TYR B 162      42.526  65.759  39.990  1.00110.92           C  
ANISOU 3830  CE2 TYR B 162    14681   9957  17506  -4512  -2691  -4043       C  
ATOM   3831  CZ  TYR B 162      41.994  66.938  40.468  1.00114.49           C  
ANISOU 3831  CZ  TYR B 162    15351  10146  18002  -4500  -2724  -4168       C  
ATOM   3832  OH  TYR B 162      41.113  67.656  39.691  1.00108.59           O  
ANISOU 3832  OH  TYR B 162    14783   9130  17344  -4477  -2612  -4059       O  
ATOM   3833  N   SER B 163      48.239  63.907  43.316  1.00134.10           N  
ANISOU 3833  N   SER B 163    16660  13941  20353  -4928  -3392  -4563       N  
ATOM   3834  CA  SER B 163      49.058  63.040  44.157  1.00139.65           C  
ANISOU 3834  CA  SER B 163    17172  14924  20965  -4867  -3551  -4667       C  
ATOM   3835  C   SER B 163      49.571  63.778  45.387  1.00147.55           C  
ANISOU 3835  C   SER B 163    18230  15891  21939  -4939  -3741  -4896       C  
ATOM   3836  O   SER B 163      49.651  63.198  46.476  1.00159.62           O  
ANISOU 3836  O   SER B 163    19751  17593  23306  -4792  -3885  -5032       O  
ATOM   3837  CB  SER B 163      50.222  62.471  43.347  1.00141.31           C  
ANISOU 3837  CB  SER B 163    17073  15315  21305  -5020  -3528  -4541       C  
ATOM   3838  OG  SER B 163      51.060  63.508  42.870  1.00160.42           O  
ANISOU 3838  OG  SER B 163    19433  17602  23918  -5322  -3520  -4524       O  
ATOM   3839  N   GLU B 164      49.929  65.055  45.234  1.00129.80           N  
ANISOU 3839  N   GLU B 164    16051  13424  19844  -5171  -3747  -4940       N  
ATOM   3840  CA  GLU B 164      50.363  65.844  46.383  1.00131.79           C  
ANISOU 3840  CA  GLU B 164    16375  13620  20078  -5247  -3923  -5167       C  
ATOM   3841  C   GLU B 164      49.235  65.981  47.398  1.00123.90           C  
ANISOU 3841  C   GLU B 164    15639  12548  18889  -5017  -3961  -5320       C  
ATOM   3842  O   GLU B 164      49.416  65.710  48.591  1.00124.94           O  
ANISOU 3842  O   GLU B 164    15784  12819  18869  -4922  -4120  -5493       O  
ATOM   3843  CB  GLU B 164      50.841  67.222  45.923  1.00143.75           C  
ANISOU 3843  CB  GLU B 164    17938  14880  21800  -5542  -3901  -5171       C  
ATOM   3844  CG  GLU B 164      51.453  67.246  44.530  1.00147.94           C  
ANISOU 3844  CG  GLU B 164    18298  15398  22515  -5761  -3767  -4953       C  
ATOM   3845  CD  GLU B 164      52.796  66.549  44.465  1.00146.85           C  
ANISOU 3845  CD  GLU B 164    17829  15533  22435  -5877  -3851  -4932       C  
ATOM   3846  OE1 GLU B 164      53.497  66.505  45.497  1.00139.68           O  
ANISOU 3846  OE1 GLU B 164    16837  14750  21486  -5886  -4041  -5109       O  
ATOM   3847  OE2 GLU B 164      53.149  66.043  43.379  1.00146.76           O  
ANISOU 3847  OE2 GLU B 164    17639  15613  22509  -5954  -3728  -4741       O  
ATOM   3848  N   GLU B 165      48.055  66.390  46.929  1.00122.26           N  
ANISOU 3848  N   GLU B 165    15642  12130  18682  -4923  -3813  -5256       N  
ATOM   3849  CA  GLU B 165      46.909  66.586  47.811  1.00121.75           C  
ANISOU 3849  CA  GLU B 165    15825  11984  18449  -4705  -3824  -5399       C  
ATOM   3850  C   GLU B 165      46.536  65.294  48.529  1.00131.57           C  
ANISOU 3850  C   GLU B 165    17039  13501  19451  -4454  -3871  -5429       C  
ATOM   3851  O   GLU B 165      46.317  65.285  49.747  1.00138.07           O  
ANISOU 3851  O   GLU B 165    17972  14391  20098  -4342  -3986  -5616       O  
ATOM   3852  CB  GLU B 165      45.733  67.115  46.992  1.00120.19           C  
ANISOU 3852  CB  GLU B 165    15816  11532  18318  -4638  -3643  -5290       C  
ATOM   3853  CG  GLU B 165      44.625  67.764  47.789  1.00120.84           C  
ANISOU 3853  CG  GLU B 165    16165  11450  18300  -4473  -3645  -5456       C  
ATOM   3854  CD  GLU B 165      43.637  68.480  46.893  1.00120.10           C  
ANISOU 3854  CD  GLU B 165    16237  11070  18326  -4445  -3484  -5348       C  
ATOM   3855  OE1 GLU B 165      43.938  68.635  45.690  1.00119.67           O  
ANISOU 3855  OE1 GLU B 165    16107  10924  18439  -4597  -3386  -5153       O  
ATOM   3856  OE2 GLU B 165      42.563  68.885  47.384  1.00120.10           O  
ANISOU 3856  OE2 GLU B 165    16442  10941  18248  -4270  -3455  -5456       O  
ATOM   3857  N   SER B 166      46.469  64.186  47.786  1.00118.21           N  
ANISOU 3857  N   SER B 166    15206  11971  17740  -4370  -3784  -5246       N  
ATOM   3858  CA  SER B 166      46.080  62.915  48.388  1.00113.44           C  
ANISOU 3858  CA  SER B 166    14581  11613  16906  -4135  -3820  -5256       C  
ATOM   3859  C   SER B 166      47.141  62.411  49.359  1.00120.48           C  
ANISOU 3859  C   SER B 166    15329  12741  17706  -4160  -4025  -5375       C  
ATOM   3860  O   SER B 166      46.810  61.860  50.415  1.00115.06           O  
ANISOU 3860  O   SER B 166    14727  12199  16792  -3993  -4117  -5484       O  
ATOM   3861  CB  SER B 166      45.810  61.882  47.296  1.00120.93           C  
ANISOU 3861  CB  SER B 166    15407  12664  17879  -4054  -3679  -5031       C  
ATOM   3862  OG  SER B 166      44.767  62.314  46.438  1.00109.74           O  
ANISOU 3862  OG  SER B 166    14133  11034  16529  -4014  -3500  -4921       O  
ATOM   3863  N   LYS B 167      48.421  62.590  49.024  1.00143.91           N  
ANISOU 3863  N   LYS B 167    18081  15755  20844  -4372  -4098  -5353       N  
ATOM   3864  CA  LYS B 167      49.482  62.169  49.933  1.00148.56           C  
ANISOU 3864  CA  LYS B 167    18520  16559  21365  -4401  -4307  -5469       C  
ATOM   3865  C   LYS B 167      49.492  63.008  51.204  1.00149.51           C  
ANISOU 3865  C   LYS B 167    18811  16609  21388  -4426  -4457  -5706       C  
ATOM   3866  O   LYS B 167      49.854  62.507  52.275  1.00150.48           O  
ANISOU 3866  O   LYS B 167    18915  16919  21341  -4348  -4627  -5826       O  
ATOM   3867  CB  LYS B 167      50.838  62.241  49.232  1.00148.61           C  
ANISOU 3867  CB  LYS B 167    18244  16625  21597  -4630  -4340  -5397       C  
ATOM   3868  CG  LYS B 167      51.951  61.495  49.955  1.00147.89           C  
ANISOU 3868  CG  LYS B 167    17941  16801  21451  -4622  -4542  -5471       C  
ATOM   3869  CD  LYS B 167      53.196  61.383  49.088  1.00149.24           C  
ANISOU 3869  CD  LYS B 167    17801  17055  21850  -4818  -4537  -5372       C  
ATOM   3870  CE  LYS B 167      54.253  60.508  49.745  1.00153.22           C  
ANISOU 3870  CE  LYS B 167    18075  17836  22305  -4773  -4735  -5434       C  
ATOM   3871  NZ  LYS B 167      55.442  60.313  48.868  1.00154.52           N  
ANISOU 3871  NZ  LYS B 167    17914  18102  22694  -4943  -4715  -5338       N  
ATOM   3872  N   LEU B 168      49.092  64.278  51.111  1.00150.12           N  
ANISOU 3872  N   LEU B 168    19061  16413  21564  -4532  -4399  -5777       N  
ATOM   3873  CA  LEU B 168      48.970  65.099  52.312  1.00162.04           C  
ANISOU 3873  CA  LEU B 168    20754  17839  22973  -4540  -4525  -6013       C  
ATOM   3874  C   LEU B 168      47.784  64.654  53.159  1.00151.71           C  
ANISOU 3874  C   LEU B 168    19664  16589  21391  -4278  -4505  -6095       C  
ATOM   3875  O   LEU B 168      47.893  64.523  54.384  1.00154.24           O  
ANISOU 3875  O   LEU B 168    20056  17033  21517  -4214  -4654  -6265       O  
ATOM   3876  CB  LEU B 168      48.832  66.574  51.932  1.00167.52           C  
ANISOU 3876  CB  LEU B 168    21579  18211  23860  -4716  -4462  -6064       C  
ATOM   3877  CG  LEU B 168      50.055  67.261  51.323  1.00168.34           C  
ANISOU 3877  CG  LEU B 168    21508  18235  24219  -5018  -4504  -6030       C  
ATOM   3878  CD1 LEU B 168      49.739  68.716  51.014  1.00168.82           C  
ANISOU 3878  CD1 LEU B 168    21747  17954  24441  -5170  -4437  -6080       C  
ATOM   3879  CD2 LEU B 168      51.251  67.154  52.253  1.00170.64           C  
ANISOU 3879  CD2 LEU B 168    21651  18707  24476  -5119  -4731  -6181       C  
ATOM   3880  N   ASN B 169      46.636  64.414  52.518  1.00139.35           N  
ANISOU 3880  N   ASN B 169    18205  14940  19800  -4131  -4319  -5973       N  
ATOM   3881  CA  ASN B 169      45.438  64.055  53.272  1.00133.97           C  
ANISOU 3881  CA  ASN B 169    17732  14303  18866  -3893  -4276  -6050       C  
ATOM   3882  C   ASN B 169      45.539  62.661  53.875  1.00128.41           C  
ANISOU 3882  C   ASN B 169    16955  13910  17925  -3738  -4357  -6023       C  
ATOM   3883  O   ASN B 169      44.909  62.385  54.904  1.00125.14           O  
ANISOU 3883  O   ASN B 169    16703  13589  17256  -3587  -4394  -6141       O  
ATOM   3884  CB  ASN B 169      44.203  64.159  52.381  1.00127.96           C  
ANISOU 3884  CB  ASN B 169    17087  13374  18157  -3780  -4059  -5923       C  
ATOM   3885  CG  ASN B 169      43.863  65.593  52.034  1.00130.90           C  
ANISOU 3885  CG  ASN B 169    17601  13422  18714  -3886  -3991  -5982       C  
ATOM   3886  OD1 ASN B 169      43.079  66.241  52.727  1.00133.98           O  
ANISOU 3886  OD1 ASN B 169    18199  13691  19015  -3797  -3981  -6141       O  
ATOM   3887  ND2 ASN B 169      44.453  66.098  50.957  1.00128.96           N  
ANISOU 3887  ND2 ASN B 169    17244  13032  18724  -4080  -3943  -5853       N  
ATOM   3888  N   ARG B 170      46.318  61.772  53.260  1.00131.95           N  
ANISOU 3888  N   ARG B 170    17167  14521  18448  -3772  -4382  -5869       N  
ATOM   3889  CA  ARG B 170      46.495  60.445  53.832  1.00127.79           C  
ANISOU 3889  CA  ARG B 170    16567  14280  17708  -3627  -4477  -5839       C  
ATOM   3890  C   ARG B 170      47.302  60.475  55.120  1.00134.78           C  
ANISOU 3890  C   ARG B 170    17447  15307  18454  -3667  -4710  -6017       C  
ATOM   3891  O   ARG B 170      47.365  59.451  55.810  1.00134.78           O  
ANISOU 3891  O   ARG B 170    17438  15536  18236  -3537  -4809  -6015       O  
ATOM   3892  CB  ARG B 170      47.161  59.517  52.815  1.00124.92           C  
ANISOU 3892  CB  ARG B 170    15940  14043  17479  -3650  -4448  -5638       C  
ATOM   3893  CG  ARG B 170      46.511  58.147  52.724  1.00122.11           C  
ANISOU 3893  CG  ARG B 170    15587  13865  16944  -3433  -4389  -5511       C  
ATOM   3894  CD  ARG B 170      47.230  57.245  51.738  1.00116.36           C  
ANISOU 3894  CD  ARG B 170    14590  13262  16359  -3455  -4367  -5329       C  
ATOM   3895  NE  ARG B 170      47.457  57.908  50.458  1.00118.40           N  
ANISOU 3895  NE  ARG B 170    14741  13348  16897  -3619  -4228  -5224       N  
ATOM   3896  CZ  ARG B 170      48.644  58.008  49.872  1.00122.83           C  
ANISOU 3896  CZ  ARG B 170    15058  13944  17667  -3793  -4270  -5176       C  
ATOM   3897  NH1 ARG B 170      49.712  57.471  50.443  1.00124.89           N  
ANISOU 3897  NH1 ARG B 170    15144  14405  17903  -3810  -4454  -5229       N  
ATOM   3898  NH2 ARG B 170      48.760  58.632  48.708  1.00115.19           N  
ANISOU 3898  NH2 ARG B 170    14021  12816  16929  -3951  -4127  -5070       N  
ATOM   3899  N   GLU B 171      47.907  61.615  55.448  1.00138.11           N  
ANISOU 3899  N   GLU B 171    17883  15597  18995  -3847  -4801  -6165       N  
ATOM   3900  CA  GLU B 171      48.670  61.827  56.675  1.00132.89           C  
ANISOU 3900  CA  GLU B 171    17230  15043  18218  -3907  -5027  -6356       C  
ATOM   3901  C   GLU B 171      49.608  60.664  56.984  1.00136.66           C  
ANISOU 3901  C   GLU B 171    17504  15804  18615  -3868  -5193  -6299       C  
ATOM   3902  O   GLU B 171      50.243  60.115  56.082  1.00135.94           O  
ANISOU 3902  O   GLU B 171    17177  15780  18694  -3911  -5169  -6143       O  
ATOM   3903  CB  GLU B 171      47.723  62.075  57.856  1.00129.02           C  
ANISOU 3903  CB  GLU B 171    17026  14546  17451  -3778  -5041  -6529       C  
ATOM   3904  CG  GLU B 171      47.253  60.816  58.568  1.00131.38           C  
ANISOU 3904  CG  GLU B 171    17391  15093  17435  -3570  -5076  -6495       C  
ATOM   3905  CD  GLU B 171      45.769  60.837  58.872  1.00132.93           C  
ANISOU 3905  CD  GLU B 171    17847  15231  17430  -3401  -4915  -6529       C  
ATOM   3906  OE1 GLU B 171      45.198  61.942  58.987  1.00126.17           O  
ANISOU 3906  OE1 GLU B 171    17153  14164  16624  -3438  -4838  -6656       O  
ATOM   3907  OE2 GLU B 171      45.170  59.746  58.987  1.00124.16           O  
ANISOU 3907  OE2 GLU B 171    16776  14283  16116  -3232  -4863  -6429       O  
TER    3908      GLU B 171                                                      
HETATM 3909  C1  NAG A 401       0.066  42.482  14.764  1.00 52.49           C  
ANISOU 3909  C1  NAG A 401     6909   4514   8521   1280   -844   -289       C  
HETATM 3910  C2  NAG A 401      -0.759  43.379  15.676  1.00 57.67           C  
ANISOU 3910  C2  NAG A 401     7487   5058   9368   1454   -876   -484       C  
HETATM 3911  C3  NAG A 401      -0.201  44.800  15.664  1.00 57.42           C  
ANISOU 3911  C3  NAG A 401     7617   4748   9454   1470   -985   -452       C  
HETATM 3912  C4  NAG A 401       1.294  44.794  15.965  1.00 58.38           C  
ANISOU 3912  C4  NAG A 401     7864   4856   9461   1277   -893   -393       C  
HETATM 3913  C5  NAG A 401       2.026  43.786  15.077  1.00 57.94           C  
ANISOU 3913  C5  NAG A 401     7852   4950   9212   1109   -843   -207       C  
HETATM 3914  C6  NAG A 401       3.476  43.599  15.460  1.00 58.09           C  
ANISOU 3914  C6  NAG A 401     7950   5002   9121    924   -734   -176       C  
HETATM 3915  C7  NAG A 401      -2.644  43.745  14.114  1.00 59.43           C  
ANISOU 3915  C7  NAG A 401     7626   5197   9760   1694  -1155   -396       C  
HETATM 3916  C8  NAG A 401      -4.130  43.651  13.944  1.00 51.74           C  
ANISOU 3916  C8  NAG A 401     6472   4273   8914   1878  -1241   -493       C  
HETATM 3917  N2  NAG A 401      -2.168  43.368  15.309  1.00 60.56           N  
ANISOU 3917  N2  NAG A 401     7718   5445   9848   1625   -971   -537       N  
HETATM 3918  O3  NAG A 401      -0.887  45.587  16.630  1.00 56.43           O  
ANISOU 3918  O3  NAG A 401     7416   4523   9503   1632   -997   -665       O  
HETATM 3919  O4  NAG A 401       1.819  46.092  15.712  1.00 67.04           O  
ANISOU 3919  O4  NAG A 401     9125   5682  10665   1266  -1012   -324       O  
HETATM 3920  O5  NAG A 401       1.411  42.494  15.180  1.00 57.95           O  
ANISOU 3920  O5  NAG A 401     7702   5195   9121   1124   -751   -259       O  
HETATM 3921  O6  NAG A 401       3.609  43.372  16.856  1.00 56.58           O  
ANISOU 3921  O6  NAG A 401     7676   4893   8928    933   -613   -369       O  
HETATM 3922  O7  NAG A 401      -1.914  44.148  13.211  1.00 65.97           O  
ANISOU 3922  O7  NAG A 401     8634   5899  10532   1607  -1249   -201       O  
HETATM 3923  C1  NAG A 402       2.525  46.599  16.859  1.00 66.29           C  
ANISOU 3923  C1  NAG A 402     9060   5520  10606   1222   -936   -464       C  
HETATM 3924  C2  NAG A 402       3.546  47.610  16.354  1.00 72.79           C  
ANISOU 3924  C2  NAG A 402    10081   6107  11469   1105  -1027   -321       C  
HETATM 3925  C3  NAG A 402       4.326  48.204  17.522  1.00 75.81           C  
ANISOU 3925  C3  NAG A 402    10501   6404  11899   1051   -967   -471       C  
HETATM 3926  C4  NAG A 402       3.371  48.768  18.565  1.00 82.60           C  
ANISOU 3926  C4  NAG A 402    11274   7196  12915   1249   -981   -721       C  
HETATM 3927  C5  NAG A 402       2.354  47.706  18.974  1.00 69.84           C  
ANISOU 3927  C5  NAG A 402     9462   5838  11237   1356   -878   -843       C  
HETATM 3928  C6  NAG A 402       1.295  48.229  19.918  1.00 64.79           C  
ANISOU 3928  C6  NAG A 402     8713   5156  10748   1558   -879  -1096       C  
HETATM 3929  C7  NAG A 402       4.464  47.315  14.095  1.00 86.44           C  
ANISOU 3929  C7  NAG A 402    12003   7823  13016    880  -1112    109       C  
HETATM 3930  C8  NAG A 402       5.462  46.583  13.251  1.00 86.49           C  
ANISOU 3930  C8  NAG A 402    12067   7966  12831    677  -1038    292       C  
HETATM 3931  N2  NAG A 402       4.449  46.996  15.394  1.00 83.40           N  
ANISOU 3931  N2  NAG A 402    11501   7543  12646    918   -994   -106       N  
HETATM 3932  O3  NAG A 402       5.190  49.227  17.039  1.00 78.49           O  
ANISOU 3932  O3  NAG A 402    11020   6501  12301    941  -1062   -342       O  
HETATM 3933  O4  NAG A 402       4.101  49.184  19.714  1.00 83.19           O  
ANISOU 3933  O4  NAG A 402    11378   7227  13003   1191   -913   -879       O  
HETATM 3934  O5  NAG A 402       1.668  47.217  17.812  1.00 72.98           O  
ANISOU 3934  O5  NAG A 402     9824   6293  11612   1400   -950   -689       O  
HETATM 3935  O6  NAG A 402       0.320  48.997  19.227  1.00 74.46           O  
ANISOU 3935  O6  NAG A 402     9937   6199  12154   1734  -1047  -1074       O  
HETATM 3936  O7  NAG A 402       3.707  48.157  13.624  1.00 81.30           O  
ANISOU 3936  O7  NAG A 402    11413   6980  12500   1008  -1274    150       O  
HETATM 3937  C1  BMA A 403       4.162  50.626  19.763  1.00 81.78           C  
ANISOU 3937  C1  BMA A 403    11325   6731  13017   1246  -1050   -916       C  
HETATM 3938  C2  BMA A 403       4.315  51.045  21.224  1.00 76.39           C  
ANISOU 3938  C2  BMA A 403    10613   6029  12384   1285   -981  -1184       C  
HETATM 3939  C3  BMA A 403       4.679  52.542  21.423  1.00 80.30           C  
ANISOU 3939  C3  BMA A 403    11259   6183  13070   1299  -1112  -1240       C  
HETATM 3940  C4  BMA A 403       5.455  53.183  20.227  1.00 83.44           C  
ANISOU 3940  C4  BMA A 403    11841   6354  13508   1155  -1242   -969       C  
HETATM 3941  C5  BMA A 403       5.120  52.560  18.847  1.00 93.91           C  
ANISOU 3941  C5  BMA A 403    13167   7763  14749   1137  -1282   -714       C  
HETATM 3942  C6  BMA A 403       6.122  52.962  17.772  1.00 95.66           C  
ANISOU 3942  C6  BMA A 403    13568   7838  14939    936  -1353   -444       C  
HETATM 3943  O2  BMA A 403       5.350  50.301  21.852  1.00 69.07           O  
ANISOU 3943  O2  BMA A 403     9670   5291  11282   1111   -843  -1203       O  
HETATM 3944  O3  BMA A 403       5.517  52.674  22.579  1.00 92.79           O  
ANISOU 3944  O3  BMA A 403    12856   7791  14608   1203  -1027  -1406       O  
HETATM 3945  O4  BMA A 403       5.225  54.590  20.177  1.00 75.55           O  
ANISOU 3945  O4  BMA A 403    10944   5106  12655   1219  -1362   -982       O  
HETATM 3946  O5  BMA A 403       5.175  51.144  18.961  1.00 89.39           O  
ANISOU 3946  O5  BMA A 403    12457   7531  13977   1080  -1125   -709       O  
HETATM 3947  O6  BMA A 403       7.303  52.189  17.964  1.00 99.50           O  
ANISOU 3947  O6  BMA A 403    14033   8525  15249    721  -1207   -401       O  
HETATM 3948  C1  MAN A 404       4.820  53.102  23.780  1.00 84.80           C  
ANISOU 3948  C1  MAN A 404    11771   6783  13668   1364   -990  -1697       C  
HETATM 3949  C2  MAN A 404       4.067  51.882  24.455  1.00 86.69           C  
ANISOU 3949  C2  MAN A 404    11820   7344  13773   1448   -830  -1839       C  
HETATM 3950  C3  MAN A 404       2.855  52.324  25.252  1.00103.59           C  
ANISOU 3950  C3  MAN A 404    13851   9513  15996   1656   -801  -2082       C  
HETATM 3951  C4  MAN A 404       3.112  53.709  25.795  1.00104.07           C  
ANISOU 3951  C4  MAN A 404    14016   9378  16149   1666   -866  -2181       C  
HETATM 3952  C5  MAN A 404       3.112  54.697  24.625  1.00100.16           C  
ANISOU 3952  C5  MAN A 404    13643   8616  15798   1674  -1044  -1976       C  
HETATM 3953  C6  MAN A 404       3.421  56.121  25.068  1.00 95.19           C  
ANISOU 3953  C6  MAN A 404    13130   7762  15274   1672  -1120  -2057       C  
HETATM 3954  O2  MAN A 404       4.918  51.210  25.391  1.00 91.29           O  
ANISOU 3954  O2  MAN A 404    12387   8126  14175   1305   -694  -1917       O  
HETATM 3955  O3  MAN A 404       2.534  51.401  26.302  1.00 99.32           O  
ANISOU 3955  O3  MAN A 404    13176   9237  15325   1682   -630  -2277       O  
HETATM 3956  O4  MAN A 404       2.092  54.068  26.707  1.00108.64           O  
ANISOU 3956  O4  MAN A 404    14486  10036  16758   1831   -806  -2417       O  
HETATM 3957  O5  MAN A 404       4.080  54.301  23.575  1.00 92.62           O  
ANISOU 3957  O5  MAN A 404    12796   7595  14800   1496  -1098  -1712       O  
HETATM 3958  O6  MAN A 404       3.611  56.912  23.912  1.00 90.53           O  
ANISOU 3958  O6  MAN A 404    12675   6933  14791   1636  -1276  -1831       O  
HETATM 3959  C1  NAG A 405       6.275  50.432  37.662  1.00123.08           C  
ANISOU 3959  C1  NAG A 405    16418  13401  16948   1157    128  -3826       C  
HETATM 3960  C2  NAG A 405       4.792  50.174  37.437  1.00129.92           C  
ANISOU 3960  C2  NAG A 405    17142  14369  17851   1308    241  -3850       C  
HETATM 3961  C3  NAG A 405       4.345  50.798  36.119  1.00130.30           C  
ANISOU 3961  C3  NAG A 405    17152  14189  18167   1403    133  -3718       C  
HETATM 3962  C4  NAG A 405       4.743  52.268  36.049  1.00133.86           C  
ANISOU 3962  C4  NAG A 405    17709  14359  18793   1424    -10  -3756       C  
HETATM 3963  C5  NAG A 405       6.221  52.456  36.397  1.00129.12           C  
ANISOU 3963  C5  NAG A 405    17246  13683  18129   1254    -92  -3743       C  
HETATM 3964  C6  NAG A 405       6.614  53.909  36.533  1.00130.94           C  
ANISOU 3964  C6  NAG A 405    17584  13658  18510   1257   -214  -3810       C  
HETATM 3965  C7  NAG A 405       3.512  48.210  38.165  1.00134.39           C  
ANISOU 3965  C7  NAG A 405    17534  15422  18105   1320    535  -3894       C  
HETATM 3966  C8  NAG A 405       3.359  46.722  38.059  1.00127.45           C  
ANISOU 3966  C8  NAG A 405    16589  14779  17058   1249    653  -3799       C  
HETATM 3967  N2  NAG A 405       4.505  48.749  37.451  1.00135.05           N  
ANISOU 3967  N2  NAG A 405    17710  15273  18330   1267    370  -3790       N  
HETATM 3968  O3  NAG A 405       2.932  50.676  35.997  1.00128.92           O  
ANISOU 3968  O3  NAG A 405    16835  14109  18040   1553    223  -3766       O  
HETATM 3969  O4  NAG A 405       4.522  52.745  34.726  1.00142.29           O  
ANISOU 3969  O4  NAG A 405    18771  15209  20084   1479   -128  -3587       O  
HETATM 3970  O5  NAG A 405       6.522  51.830  37.653  1.00129.32           O  
ANISOU 3970  O5  NAG A 405    17287  13941  17906   1186     10  -3884       O  
HETATM 3971  O6  NAG A 405       8.025  54.076  36.503  1.00128.93           O  
ANISOU 3971  O6  NAG A 405    17441  13303  18246   1084   -314  -3743       O  
HETATM 3972  O7  NAG A 405       2.770  48.892  38.865  1.00130.79           O  
ANISOU 3972  O7  NAG A 405    17050  14985  17659   1414    590  -4058       O  
HETATM 3973  C1  NAG A 406       3.528  53.787  34.726  1.00150.80           C  
ANISOU 3973  C1  NAG A 406    19812  16165  21320   1644   -158  -3684       C  
HETATM 3974  C2  NAG A 406       3.456  54.414  33.343  1.00153.02           C  
ANISOU 3974  C2  NAG A 406    20126  16188  21826   1684   -313  -3489       C  
HETATM 3975  C3  NAG A 406       2.468  55.576  33.345  1.00158.16           C  
ANISOU 3975  C3  NAG A 406    20750  16692  22654   1860   -368  -3592       C  
HETATM 3976  C4  NAG A 406       1.116  55.136  33.899  1.00160.00           C  
ANISOU 3976  C4  NAG A 406    20808  17150  22835   2009   -228  -3750       C  
HETATM 3977  C5  NAG A 406       1.285  54.405  35.232  1.00155.34           C  
ANISOU 3977  C5  NAG A 406    20191  16829  22002   1940    -56  -3923       C  
HETATM 3978  C6  NAG A 406       0.002  53.784  35.734  1.00153.34           C  
ANISOU 3978  C6  NAG A 406    19761  16831  21670   2049    106  -4049       C  
HETATM 3979  C7  NAG A 406       5.228  54.631  31.660  1.00145.23           C  
ANISOU 3979  C7  NAG A 406    19329  14887  20965   1454   -527  -3113       C  
HETATM 3980  C8  NAG A 406       6.599  55.161  31.364  1.00139.09           C  
ANISOU 3980  C8  NAG A 406    18699  13919  20228   1275   -634  -3001       C  
HETATM 3981  N2  NAG A 406       4.766  54.857  32.895  1.00150.50           N  
ANISOU 3981  N2  NAG A 406    19957  15668  21557   1529   -437  -3355       N  
HETATM 3982  O3  NAG A 406       2.345  56.048  32.007  1.00154.13           O  
ANISOU 3982  O3  NAG A 406    20272  15960  22330   1896   -516  -3388       O  
HETATM 3983  O4  NAG A 406       0.284  56.266  34.148  1.00167.53           O  
ANISOU 3983  O4  NAG A 406    21734  17979  23939   2168   -270  -3895       O  
HETATM 3984  O5  NAG A 406       2.240  53.340  35.110  1.00150.10           O  
ANISOU 3984  O5  NAG A 406    19572  16278  21182   1775    -26  -3797       O  
HETATM 3985  O6  NAG A 406       0.240  52.922  36.839  1.00151.23           O  
ANISOU 3985  O6  NAG A 406    19486  16826  21146   1954    267  -4156       O  
HETATM 3986  O7  NAG A 406       4.569  54.026  30.820  1.00145.78           O  
ANISOU 3986  O7  NAG A 406    19316  15010  21065   1520   -519  -2990       O  
HETATM 3987  C1  BMA A 407      -0.368  56.756  32.962  1.00167.50           C  
ANISOU 3987  C1  BMA A 407    21698  17799  24147   2283   -402  -3759       C  
HETATM 3988  C2  BMA A 407      -1.839  57.101  33.265  1.00167.99           C  
ANISOU 3988  C2  BMA A 407    21599  17931  24300   2487   -355  -3930       C  
HETATM 3989  C3  BMA A 407      -2.468  57.853  32.080  1.00165.02           C  
ANISOU 3989  C3  BMA A 407    21212  17327  24160   2618   -530  -3802       C  
HETATM 3990  C4  BMA A 407      -1.555  58.983  31.580  1.00171.13           C  
ANISOU 3990  C4  BMA A 407    22190  17768  25063   2560   -711  -3690       C  
HETATM 3991  C5  BMA A 407      -0.183  58.403  31.235  1.00169.93           C  
ANISOU 3991  C5  BMA A 407    22170  17600  24794   2343   -722  -3504       C  
HETATM 3992  C6  BMA A 407       0.795  59.447  30.720  1.00168.19           C  
ANISOU 3992  C6  BMA A 407    22149  17067  24688   2249   -885  -3376       C  
HETATM 3993  O2  BMA A 407      -1.933  57.956  34.394  1.00169.51           O  
ANISOU 3993  O2  BMA A 407    21819  18094  24493   2540   -316  -4172       O  
HETATM 3994  O3  BMA A 407      -3.753  58.371  32.403  1.00159.80           O  
ANISOU 3994  O3  BMA A 407    20409  16695  23612   2813   -512  -3981       O  
HETATM 3995  O4  BMA A 407      -2.116  59.591  30.431  1.00170.92           O  
ANISOU 3995  O4  BMA A 407    22168  17541  25232   2668   -877  -3544       O  
HETATM 3996  O5  BMA A 407       0.357  57.850  32.434  1.00170.07           O  
ANISOU 3996  O5  BMA A 407    22187  17814  24616   2243   -573  -3661       O  
HETATM 3997  O6  BMA A 407       1.257  60.213  31.827  1.00167.52           O  
ANISOU 3997  O6  BMA A 407    22142  16920  24588   2221   -863  -3577       O  
HETATM 3998  C1  NAG A 408     -26.654  16.672   3.164  1.00 69.78           C  
ANISOU 3998  C1  NAG A 408     4239  10519  11756     59  -2120  -1956       C  
HETATM 3999  C2  NAG A 408     -27.540  15.522   2.675  1.00 76.89           C  
ANISOU 3999  C2  NAG A 408     5026  11495  12693   -127  -2176  -2027       C  
HETATM 4000  C3  NAG A 408     -28.900  15.561   3.364  1.00 86.65           C  
ANISOU 4000  C3  NAG A 408     5966  12840  14118   -157  -2053  -2136       C  
HETATM 4001  C4  NAG A 408     -28.722  15.571   4.875  1.00 87.76           C  
ANISOU 4001  C4  NAG A 408     6040  13003  14301   -239  -1712  -2161       C  
HETATM 4002  C5  NAG A 408     -27.839  16.748   5.274  1.00 78.24           C  
ANISOU 4002  C5  NAG A 408     4956  11719  13051    -38  -1677  -2100       C  
HETATM 4003  C6  NAG A 408     -27.543  16.789   6.754  1.00 79.60           C  
ANISOU 4003  C6  NAG A 408     5099  11912  13235   -114  -1343  -2120       C  
HETATM 4004  C7  NAG A 408     -26.856  14.964   0.384  1.00 84.98           C  
ANISOU 4004  C7  NAG A 408     6368  12450  13472   -113  -2625  -1939       C  
HETATM 4005  C8  NAG A 408     -27.174  15.107  -1.073  1.00 90.30           C  
ANISOU 4005  C8  NAG A 408     7124  13127  14061    -21  -2951  -1913       C  
HETATM 4006  N2  NAG A 408     -27.700  15.563   1.230  1.00 83.64           N  
ANISOU 4006  N2  NAG A 408     5969  12335  13475    -46  -2498  -1997       N  
HETATM 4007  O3  NAG A 408     -29.660  14.426   2.967  1.00100.66           O  
ANISOU 4007  O3  NAG A 408     7641  14678  15927   -352  -2091  -2196       O  
HETATM 4008  O4  NAG A 408     -29.984  15.665   5.527  1.00108.35           O  
ANISOU 4008  O4  NAG A 408     8378  15719  17069   -260  -1593  -2266       O  
HETATM 4009  O5  NAG A 408     -26.575  16.648   4.601  1.00 69.57           O  
ANISOU 4009  O5  NAG A 408     4126  10519  11790    -20  -1799  -1993       O  
HETATM 4010  O6  NAG A 408     -26.512  17.721   7.051  1.00 90.03           O  
ANISOU 4010  O6  NAG A 408     6573  13143  14489     45  -1318  -2054       O  
HETATM 4011  O7  NAG A 408     -25.877  14.339   0.778  1.00 84.97           O  
ANISOU 4011  O7  NAG A 408     6573  12378  13333   -242  -2444  -1874       O  
HETATM 4012  C1  NAG A 409     -30.303  14.374   6.082  1.00117.02           C  
ANISOU 4012  C1  NAG A 409     9411  16875  18176   -546  -1398  -2300       C  
HETATM 4013  C2  NAG A 409     -31.304  14.524   7.225  1.00119.35           C  
ANISOU 4013  C2  NAG A 409     9464  17282  18603   -593  -1162  -2393       C  
HETATM 4014  C3  NAG A 409     -31.643  13.157   7.812  1.00124.04           C  
ANISOU 4014  C3  NAG A 409    10009  17926  19195   -906   -959  -2407       C  
HETATM 4015  C4  NAG A 409     -32.108  12.207   6.716  1.00130.61           C  
ANISOU 4015  C4  NAG A 409    10821  18759  20045  -1029  -1167  -2419       C  
HETATM 4016  C5  NAG A 409     -31.078  12.155   5.591  1.00126.33           C  
ANISOU 4016  C5  NAG A 409    10528  18103  19370   -958  -1404  -2339       C  
HETATM 4017  C6  NAG A 409     -31.533  11.328   4.411  1.00132.34           C  
ANISOU 4017  C6  NAG A 409    11286  18864  20132  -1050  -1638  -2362       C  
HETATM 4018  C7  NAG A 409     -30.936  16.738   8.220  1.00111.28           C  
ANISOU 4018  C7  NAG A 409     8431  16228  17623   -213  -1058  -2414       C  
HETATM 4019  C8  NAG A 409     -30.344  17.497   9.368  1.00100.68           C  
ANISOU 4019  C8  NAG A 409     7147  14863  16244   -134   -834  -2410       C  
HETATM 4020  N2  NAG A 409     -30.790  15.409   8.258  1.00117.18           N  
ANISOU 4020  N2  NAG A 409     9227  16990  18306   -479   -969  -2384       N  
HETATM 4021  O3  NAG A 409     -32.661  13.301   8.795  1.00127.62           O  
ANISOU 4021  O3  NAG A 409    10228  18498  19764   -950   -755  -2497       O  
HETATM 4022  O4  NAG A 409     -32.288  10.901   7.251  1.00133.85           O  
ANISOU 4022  O4  NAG A 409    11227  19184  20445  -1330   -985  -2414       O  
HETATM 4023  O5  NAG A 409     -30.829  13.479   5.097  1.00126.25           O  
ANISOU 4023  O5  NAG A 409    10551  18063  19355   -664  -1581  -2320       O  
HETATM 4024  O6  NAG A 409     -31.425   9.936   4.678  1.00134.34           O  
ANISOU 4024  O6  NAG A 409    11601  19092  20352  -1340  -1509  -2352       O  
HETATM 4025  O7  NAG A 409     -31.519  17.301   7.299  1.00106.80           O  
ANISOU 4025  O7  NAG A 409     7786  15659  17135    -46  -1313  -2440       O  
HETATM 4026  C1  NAG A 410       8.247  33.835  42.038  1.00 87.23           C  
ANISOU 4026  C1  NAG A 410    12123  11406   9614    -17    904  -2349       C  
HETATM 4027  C2  NAG A 410       7.008  33.030  42.405  1.00 97.57           C  
ANISOU 4027  C2  NAG A 410    13409  12881  10784    -54   1097  -2333       C  
HETATM 4028  C3  NAG A 410       5.826  33.963  42.643  1.00 96.60           C  
ANISOU 4028  C3  NAG A 410    13190  12789  10725     26   1252  -2553       C  
HETATM 4029  C4  NAG A 410       6.185  35.020  43.680  1.00102.13           C  
ANISOU 4029  C4  NAG A 410    13978  13488  11338     53   1227  -2783       C  
HETATM 4030  C5  NAG A 410       7.477  35.736  43.286  1.00 98.37           C  
ANISOU 4030  C5  NAG A 410    13545  12830  11002     78   1015  -2773       C  
HETATM 4031  C6  NAG A 410       7.970  36.697  44.344  1.00100.10           C  
ANISOU 4031  C6  NAG A 410    13867  13042  11124     87    965  -2992       C  
HETATM 4032  C7  NAG A 410       6.583  30.746  41.617  1.00 92.58           C  
ANISOU 4032  C7  NAG A 410    12755  12342  10080   -168   1153  -1977       C  
HETATM 4033  C8  NAG A 410       6.255  29.883  40.436  1.00 73.44           C  
ANISOU 4033  C8  NAG A 410    10235   9877   7792   -175   1158  -1795       C  
HETATM 4034  N2  NAG A 410       6.693  32.056  41.373  1.00 94.61           N  
ANISOU 4034  N2  NAG A 410    12951  12492  10503    -73   1113  -2131       N  
HETATM 4035  O3  NAG A 410       4.707  33.201  43.084  1.00 82.55           O  
ANISOU 4035  O3  NAG A 410    11379  11186   8800    -27   1444  -2551       O  
HETATM 4036  O4  NAG A 410       5.135  35.975  43.778  1.00122.66           O  
ANISOU 4036  O4  NAG A 410    16474  16087  14043    151   1355  -3003       O  
HETATM 4037  O5  NAG A 410       8.528  34.781  43.072  1.00 93.31           O  
ANISOU 4037  O5  NAG A 410    12976  12185  10291     -4    883  -2559       O  
HETATM 4038  O6  NAG A 410       9.386  36.811  44.328  1.00100.33           O  
ANISOU 4038  O6  NAG A 410    13980  12978  11164     45    762  -2929       O  
HETATM 4039  O7  NAG A 410       6.737  30.279  42.742  1.00104.10           O  
ANISOU 4039  O7  NAG A 410    14350  13919  11286   -248   1178  -1984       O  
HETATM 4040  C1  NAG A 411       4.438  35.807  45.027  1.00143.40           C  
ANISOU 4040  C1  NAG A 411    19152  18917  16416    107   1528  -3152       C  
HETATM 4041  C2  NAG A 411       3.302  36.820  45.107  1.00149.06           C  
ANISOU 4041  C2  NAG A 411    19735  19636  17264    227   1669  -3406       C  
HETATM 4042  C3  NAG A 411       2.560  36.673  46.430  1.00152.49           C  
ANISOU 4042  C3  NAG A 411    20212  20291  17437    180   1854  -3546       C  
HETATM 4043  C4  NAG A 411       2.094  35.235  46.617  1.00156.90           C  
ANISOU 4043  C4  NAG A 411    20785  21039  17790     43   1986  -3369       C  
HETATM 4044  C5  NAG A 411       3.267  34.269  46.458  1.00153.56           C  
ANISOU 4044  C5  NAG A 411    20513  20586  17247    -70   1830  -3127       C  
HETATM 4045  C6  NAG A 411       2.844  32.818  46.487  1.00148.19           C  
ANISOU 4045  C6  NAG A 411    19853  20045  16405   -202   1930  -2916       C  
HETATM 4046  C7  NAG A 411       3.179  39.090  44.184  1.00154.88           C  
ANISOU 4046  C7  NAG A 411    20334  20038  18474    474   1542  -3670       C  
HETATM 4047  C8  NAG A 411       3.823  40.442  44.127  1.00156.89           C  
ANISOU 4047  C8  NAG A 411    20632  20081  18899    561   1395  -3821       C  
HETATM 4048  N2  NAG A 411       3.795  38.178  44.944  1.00152.21           N  
ANISOU 4048  N2  NAG A 411    20137  19843  17852    335   1542  -3568       N  
HETATM 4049  O3  NAG A 411       1.443  37.554  46.446  1.00150.35           O  
ANISOU 4049  O3  NAG A 411    19788  20002  17334    308   1952  -3703       O  
HETATM 4050  O4  NAG A 411       1.526  35.074  47.912  1.00159.68           O  
ANISOU 4050  O4  NAG A 411    21196  21574  17899    -13   2117  -3423       O  
HETATM 4051  O5  NAG A 411       3.916  34.485  45.196  1.00150.16           O  
ANISOU 4051  O5  NAG A 411    20017  19941  17095     -1   1649  -2995       O  
HETATM 4052  O6  NAG A 411       3.785  32.014  47.186  1.00144.46           O  
ANISOU 4052  O6  NAG A 411    19589  19626  15674   -321   1830  -2771       O  
HETATM 4053  O7  NAG A 411       2.147  38.835  43.570  1.00153.97           O  
ANISOU 4053  O7  NAG A 411    20066  19958  18479    524   1648  -3640       O  
HETATM 4054  C1  NAG A 412     -24.892  23.442   6.927  1.00132.86           C  
ANISOU 4054  C1  NAG A 412    12386  18144  19951   1077  -1689  -1866       C  
HETATM 4055  C2  NAG A 412     -26.271  23.838   6.406  1.00146.60           C  
ANISOU 4055  C2  NAG A 412    13910  19938  21854   1193  -1869  -1956       C  
HETATM 4056  C3  NAG A 412     -26.883  24.915   7.298  1.00154.70           C  
ANISOU 4056  C3  NAG A 412    14804  20954  23021   1349  -1760  -2058       C  
HETATM 4057  C4  NAG A 412     -26.881  24.467   8.754  1.00152.89           C  
ANISOU 4057  C4  NAG A 412    14469  20821  22800   1200  -1401  -2157       C  
HETATM 4058  C5  NAG A 412     -25.481  24.029   9.174  1.00146.75           C  
ANISOU 4058  C5  NAG A 412    13896  19996  21867   1086  -1254  -2065       C  
HETATM 4059  C6  NAG A 412     -25.437  23.446  10.567  1.00150.44           C  
ANISOU 4059  C6  NAG A 412    14291  20563  22308    908   -902  -2142       C  
HETATM 4060  C7  NAG A 412     -26.298  23.472   3.978  1.00153.57           C  
ANISOU 4060  C7  NAG A 412    14971  20770  22610   1231  -2381  -1805       C  
HETATM 4061  C8  NAG A 412     -26.202  24.115   2.627  1.00156.10           C  
ANISOU 4061  C8  NAG A 412    15460  20994  22857   1387  -2718  -1686       C  
HETATM 4062  N2  NAG A 412     -26.199  24.296   5.027  1.00151.49           N  
ANISOU 4062  N2  NAG A 412    14666  20468  22427   1330  -2206  -1849       N  
HETATM 4063  O3  NAG A 412     -28.215  25.181   6.875  1.00158.61           O  
ANISOU 4063  O3  NAG A 412    15099  21506  23660   1435  -1901  -2146       O  
HETATM 4064  O4  NAG A 412     -27.306  25.536   9.591  1.00154.33           O  
ANISOU 4064  O4  NAG A 412    14564  20985  23089   1354  -1302  -2253       O  
HETATM 4065  O5  NAG A 412     -24.997  23.012   8.284  1.00134.40           O  
ANISOU 4065  O5  NAG A 412    12458  18429  20179    940  -1364  -1964       O  
HETATM 4066  O6  NAG A 412     -24.590  24.204  11.420  1.00150.47           O  
ANISOU 4066  O6  NAG A 412    14418  20489  22263    991   -758  -2130       O  
HETATM 4067  O7  NAG A 412     -26.454  22.263   4.114  1.00152.56           O  
ANISOU 4067  O7  NAG A 412    14763  20744  22459   1018  -2270  -1855       O  
HETATM 4068  C2  EZ7 B 201      15.330  41.053  18.622  1.00 39.08           C  
ANISOU 4068  C2  EZ7 B 201     5595   3172   6082   -396    -87   -192       C  
HETATM 4069  C3  EZ7 B 201      14.049  41.132  19.140  1.00 46.42           C  
ANISOU 4069  C3  EZ7 B 201     6528   4069   7039   -241   -113   -272       C  
HETATM 4070  C4  EZ7 B 201      13.884  41.748  20.380  1.00 42.85           C  
ANISOU 4070  C4  EZ7 B 201     6087   3542   6653   -186   -140   -431       C  
HETATM 4071  C11 EZ7 B 201      14.940  42.233  21.038  1.00 45.62           C  
ANISOU 4071  C11 EZ7 B 201     6451   3847   7036   -283   -153   -500       C  
HETATM 4072  C12 EZ7 B 201      16.168  42.144  20.521  1.00 43.00           C  
ANISOU 4072  C12 EZ7 B 201     6108   3544   6688   -435   -136   -417       C  
HETATM 4073  C16 EZ7 B 201      18.321  43.708  23.451  1.00 45.25           C  
ANISOU 4073  C16 EZ7 B 201     6404   3685   7104   -598   -241   -790       C  
HETATM 4074  C18 EZ7 B 201      16.217  44.382  24.402  1.00 42.69           C  
ANISOU 4074  C18 EZ7 B 201     6158   3233   6827   -337   -272   -962       C  
HETATM 4075  C19 EZ7 B 201      16.896  45.022  25.446  1.00 42.79           C  
ANISOU 4075  C19 EZ7 B 201     6196   3184   6880   -389   -319  -1112       C  
HETATM 4076  C60 EZ7 B 201      10.918  39.769  17.742  1.00 35.75           C  
ANISOU 4076  C60 EZ7 B 201     5109   2858   5614     46   -120   -168       C  
HETATM 4077  C58 EZ7 B 201      11.818  40.384  18.811  1.00 41.15           C  
ANISOU 4077  C58 EZ7 B 201     5814   3478   6343    -13   -114   -274       C  
HETATM 4078  O59 EZ7 B 201      11.371  40.622  19.932  1.00 52.09           O  
ANISOU 4078  O59 EZ7 B 201     7179   4847   7765     67   -112   -422       O  
HETATM 4079  N7  EZ7 B 201      13.075  40.608  18.380  1.00 46.04           N  
ANISOU 4079  N7  EZ7 B 201     6468   4074   6952   -159   -109   -197       N  
HETATM 4080  C1  EZ7 B 201      16.387  41.574  19.345  1.00 38.68           C  
ANISOU 4080  C1  EZ7 B 201     5543   3075   6080   -493    -97   -268       C  
HETATM 4081  O13 EZ7 B 201      17.019  42.696  21.364  1.00 45.83           O  
ANISOU 4081  O13 EZ7 B 201     6471   3849   7095   -509   -164   -518       O  
HETATM 4082  N10 EZ7 B 201      15.060  42.854  22.213  1.00 49.95           N  
ANISOU 4082  N10 EZ7 B 201     7018   4324   7636   -263   -184   -657       N  
HETATM 4083  C9  EZ7 B 201      16.353  43.120  22.370  1.00 46.91           C  
ANISOU 4083  C9  EZ7 B 201     6633   3924   7268   -405   -196   -661       C  
HETATM 4084  C17 EZ7 B 201      16.934  43.730  23.399  1.00 43.14           C  
ANISOU 4084  C17 EZ7 B 201     6172   3382   6836   -444   -236   -799       C  
HETATM 4085  C15 EZ7 B 201      18.977  44.332  24.502  1.00 42.03           C  
ANISOU 4085  C15 EZ7 B 201     6009   3216   6744   -648   -295   -937       C  
HETATM 4086  N14 EZ7 B 201      18.238  44.971  25.495  1.00 43.87           N  
ANISOU 4086  N14 EZ7 B 201     6301   3354   7013   -542   -335  -1097       N  
HETATM 4087  C23 EZ7 B 201      16.211  45.664  26.485  1.00 44.93           C  
ANISOU 4087  C23 EZ7 B 201     6511   3372   7187   -283   -348  -1296       C  
HETATM 4088  O24 EZ7 B 201      15.454  44.980  27.169  1.00 46.09           O  
ANISOU 4088  O24 EZ7 B 201     6623   3658   7231   -170   -296  -1384       O  
HETATM 4089  N27 EZ7 B 201      16.452  46.961  26.792  1.00 45.77           N  
ANISOU 4089  N27 EZ7 B 201     6697   3262   7430   -315   -427  -1387       N  
HETATM 4090  C28 EZ7 B 201      15.756  47.594  27.932  1.00 47.04           C  
ANISOU 4090  C28 EZ7 B 201     6901   3351   7623   -197   -452  -1607       C  
HETATM 4091  C29 EZ7 B 201      16.725  48.460  28.743  1.00 48.69           C  
ANISOU 4091  C29 EZ7 B 201     7161   3444   7895   -300   -529  -1749       C  
HETATM 4092  C26 EZ7 B 201      17.364  47.828  26.007  1.00 50.75           C  
ANISOU 4092  C26 EZ7 B 201     7379   3714   8189   -472   -488  -1279       C  
HETATM 4093  C25 EZ7 B 201      18.213  48.727  26.909  1.00 52.06           C  
ANISOU 4093  C25 EZ7 B 201     7588   3759   8434   -566   -562  -1434       C  
HETATM 4094  N30 EZ7 B 201      17.421  49.459  27.912  1.00 54.08           N  
ANISOU 4094  N30 EZ7 B 201     7905   3901   8741   -433   -603  -1644       N  
HETATM 4095  C40 EZ7 B 201      18.329  50.279  28.750  1.00 56.55           C  
ANISOU 4095  C40 EZ7 B 201     8261   4103   9123   -538   -682  -1797       C  
HETATM 4096  C52 EZ7 B 201      18.966  51.433  27.980  1.00 59.42           C  
ANISOU 4096  C52 EZ7 B 201     8702   4203   9672   -684   -761  -1704       C  
HETATM 4097  N56 EZ7 B 201      18.497  52.023  26.906  1.00 58.42           N  
ANISOU 4097  N56 EZ7 B 201     8645   3890   9660   -676   -783  -1552       N  
HETATM 4098  N53 EZ7 B 201      20.096  52.031  28.288  1.00 64.32           N  
ANISOU 4098  N53 EZ7 B 201     9337   4736  10366   -852   -824  -1758       N  
HETATM 4099  N54 EZ7 B 201      20.236  52.815  27.514  1.00 58.96           N  
ANISOU 4099  N54 EZ7 B 201     8726   3855   9820   -933   -865  -1650       N  
HETATM 4100  N55 EZ7 B 201      19.283  52.825  26.673  1.00 61.85           N  
ANISOU 4100  N55 EZ7 B 201     9134   4157  10210   -827   -844  -1520       N  
HETATM 4101  C57 EZ7 B 201      19.246  53.773  25.555  1.00 60.23           C  
ANISOU 4101  C57 EZ7 B 201     9038   3689  10158   -904   -899  -1348       C  
HETATM 4102  C44 EZ7 B 201      17.703  50.800  29.881  1.00 65.92           C  
ANISOU 4102  C44 EZ7 B 201     9495   5232  10319   -416   -710  -2031       C  
HETATM 4103  C43 EZ7 B 201      18.176  50.432  31.134  1.00 65.47           C  
ANISOU 4103  C43 EZ7 B 201     9411   5325  10138   -432   -712  -2207       C  
HETATM 4104  C42 EZ7 B 201      17.569  50.933  32.276  1.00 71.37           C  
ANISOU 4104  C42 EZ7 B 201    10211   6033  10872   -317   -728  -2451       C  
HETATM 4105  C41 EZ7 B 201      16.495  51.809  32.168  1.00 74.97           C  
ANISOU 4105  C41 EZ7 B 201    10731   6295  11460   -178   -742  -2530       C  
HETATM 4106  C46 EZ7 B 201      16.023  52.187  30.916  1.00 77.20           C  
ANISOU 4106  C46 EZ7 B 201    11034   6414  11884   -152   -756  -2350       C  
HETATM 4107  C45 EZ7 B 201      16.631  51.685  29.770  1.00 75.16           C  
ANISOU 4107  C45 EZ7 B 201    10740   6199  11619   -278   -741  -2095       C  
HETATM 4108  O   HOH A 501     -10.224  25.387 -18.619  1.00100.08           O  
ANISOU 4108  O   HOH A 501    10029  14647  13348   1023  -6706  -1139       O  
HETATM 4109  O   HOH A 502      -4.055   4.786  -1.294  1.00 40.02           O  
ANISOU 4109  O   HOH A 502     4990   5216   5001   -694   -976  -1198       O  
HETATM 4110  O   HOH A 503     -11.416  31.919  -6.038  1.00 58.66           O  
ANISOU 4110  O   HOH A 503     7517   7055   7715   1401  -3439    911       O  
HETATM 4111  O   HOH A 504     -25.821  20.516  -8.942  1.00 79.64           O  
ANISOU 4111  O   HOH A 504     7143  11471  11646   1048  -4756  -1109       O  
HETATM 4112  O   HOH A 505      19.150  35.859  28.195  1.00 41.02           O  
ANISOU 4112  O   HOH A 505     5566   4306   5712   -338   -126  -1061       O  
HETATM 4113  O   HOH A 506       2.869  36.415  11.793  1.00 42.78           O  
ANISOU 4113  O   HOH A 506     5707   4136   6410    623   -478    188       O  
HETATM 4114  O   HOH A 507       6.181  24.315  13.655  1.00 31.10           O  
ANISOU 4114  O   HOH A 507     3942   3715   4160     73    229    -50       O  
HETATM 4115  O   HOH A 508      -5.469   6.744  -0.242  1.00 39.28           O  
ANISOU 4115  O   HOH A 508     4670   5225   5030   -664   -969  -1014       O  
HETATM 4116  O   HOH A 509     -14.447   5.358   0.640  1.00 51.88           O  
ANISOU 4116  O   HOH A 509     5073   7088   7550  -1229  -1417  -1350       O  
HETATM 4117  O   HOH A 510      -2.380  29.404  22.861  1.00 35.83           O  
ANISOU 4117  O   HOH A 510     3860   4454   5299    529    707   -991       O  
HETATM 4118  O   HOH A 511      -4.318  12.861   2.777  1.00 42.42           O  
ANISOU 4118  O   HOH A 511     4950   5697   5470   -298   -661   -517       O  
HETATM 4119  O   HOH A 512      -1.210  36.554  16.838  1.00 60.78           O  
ANISOU 4119  O   HOH A 512     7398   6581   9113   1063   -237   -587       O  
HETATM 4120  O   HOH A 513      10.267  26.744  29.671  1.00 41.10           O  
ANISOU 4120  O   HOH A 513     5663   5061   4893    -42    476   -731       O  
HETATM 4121  O   HOH A 514     -10.868   5.659   1.846  1.00 62.54           O  
ANISOU 4121  O   HOH A 514     6920   8225   8618  -1060  -1071  -1127       O  
HETATM 4122  O   HOH A 515      -0.834  40.187   5.813  1.00 46.49           O  
ANISOU 4122  O   HOH A 515     6586   4009   7069   1041  -1516    830       O  
HETATM 4123  O   HOH A 516     -15.374  29.574   0.376  1.00 63.15           O  
ANISOU 4123  O   HOH A 516     6477   7969   9548   1593  -2714   -179       O  
HETATM 4124  O   HOH A 517     -31.261   5.920 -11.885  1.00 89.40           O  
ANISOU 4124  O   HOH A 517     7508  13339  13120  -1191  -4770  -2555       O  
HETATM 4125  O   HOH A 518       7.612  34.523  12.679  1.00 51.27           O  
ANISOU 4125  O   HOH A 518     6885   5454   7142    168   -104    224       O  
HETATM 4126  O   HOH A 519      11.832  31.136  31.005  1.00 51.20           O  
ANISOU 4126  O   HOH A 519     6992   6130   6333     16    347  -1078       O  
HETATM 4127  O   HOH A 520       0.426  46.500  12.583  1.00 51.21           O  
ANISOU 4127  O   HOH A 520     7254   3505   8700   1398  -1402     88       O  
HETATM 4128  O   HOH A 521      -3.020   8.480 -11.293  1.00 52.60           O  
ANISOU 4128  O   HOH A 521     7267   7740   4981   -466  -1613  -1282       O  
HETATM 4129  O   HOH A 522     -27.525  20.282 -16.786  1.00 90.86           O  
ANISOU 4129  O   HOH A 522     9388  13188  11946   1079  -6177   -823       O  
HETATM 4130  O   HOH A 523      -8.090   2.158  -1.754  1.00 56.01           O  
ANISOU 4130  O   HOH A 523     6716   7172   7394  -1083  -1315  -1474       O  
HETATM 4131  O   HOH A 524       7.274  25.470  30.341  1.00 56.37           O  
ANISOU 4131  O   HOH A 524     7550   7167   6703    -87    722   -741       O  
HETATM 4132  O   HOH A 525     -22.032  24.393   2.111  1.00 61.26           O  
ANISOU 4132  O   HOH A 525     4452   8637  10187   1288  -2579  -1198       O  
HETATM 4133  O   HOH A 526       3.702  32.914  26.723  1.00 43.51           O  
ANISOU 4133  O   HOH A 526     5476   5054   5999    452    637  -1148       O  
HETATM 4134  O   HOH A 527     -16.257  37.019   5.649  1.00 64.42           O  
ANISOU 4134  O   HOH A 527     6318   7248  10912   2593  -2624   -576       O  
HETATM 4135  O   HOH A 528     -15.593   9.544   1.370  1.00 48.43           O  
ANISOU 4135  O   HOH A 528     4267   6905   7229   -813  -1445  -1189       O  
HETATM 4136  O   HOH B 301      -3.891   5.854  15.161  1.00 47.75           O  
ANISOU 4136  O   HOH B 301     5868   5746   6528  -1161    298   -262       O  
HETATM 4137  O   HOH B 302      12.256  32.978  13.220  1.00 69.95           O  
ANISOU 4137  O   HOH B 302     9230   8045   9304   -187    154    205       O  
HETATM 4138  O   HOH B 303      -5.957   4.375  10.372  1.00 44.94           O  
ANISOU 4138  O   HOH B 303     5284   5427   6363  -1212    -95   -575       O  
HETATM 4139  O   HOH B 304       1.179  15.422   9.520  1.00 27.69           O  
ANISOU 4139  O   HOH B 304     3321   3552   3649   -172     27   -240       O  
HETATM 4140  O   HOH B 305      34.562  54.739  32.563  1.00 71.23           O  
ANISOU 4140  O   HOH B 305     9319   5974  11772  -2891  -1540  -2537       O  
HETATM 4141  O   HOH B 306      -1.909  13.853  10.407  1.00 48.67           O  
ANISOU 4141  O   HOH B 306     5759   6249   6483   -327     25   -330       O  
HETATM 4142  O   HOH B 307      21.398  31.859  38.263  1.00 41.09           O  
ANISOU 4142  O   HOH B 307     6093   5011   4507   -273   -692  -1559       O  
HETATM 4143  O   HOH B 308      -6.491   9.258   9.306  1.00 49.24           O  
ANISOU 4143  O   HOH B 308     5513   6357   6838   -791   -136   -567       O  
HETATM 4144  O   HOH B 309       0.184   1.183   7.283  1.00 35.75           O  
ANISOU 4144  O   HOH B 309     4817   3790   4978   -801   -377   -818       O  
HETATM 4145  O   HOH B 310       0.506  16.845   4.653  1.00 54.46           O  
ANISOU 4145  O   HOH B 310     6784   7095   6814    -84   -295   -196       O  
HETATM 4146  O   HOH B 311       3.192   7.182  17.224  1.00 41.66           O  
ANISOU 4146  O   HOH B 311     5646   4743   5442   -640    223    -82       O  
HETATM 4147  O   HOH B 312      13.423  27.430  29.943  1.00 48.04           O  
ANISOU 4147  O   HOH B 312     6593   5853   5807    -66    245   -747       O  
HETATM 4148  O   HOH B 313       7.922  10.466  18.689  1.00 33.97           O  
ANISOU 4148  O   HOH B 313     4728   3855   4325   -266    194    -73       O  
HETATM 4149  O   HOH B 314      22.127  60.905  34.374  1.00 84.55           O  
ANISOU 4149  O   HOH B 314    12543   6052  13529  -1096  -1417  -3061       O  
HETATM 4150  O   HOH B 315      23.399  55.723  46.683  1.00 77.15           O  
ANISOU 4150  O   HOH B 315    11610   7220  10482   -782  -1522  -4754       O  
HETATM 4151  O   HOH B 316     -10.111  11.074   5.148  1.00 51.96           O  
ANISOU 4151  O   HOH B 316     5401   7022   7318   -618   -688   -765       O  
HETATM 4152  O   HOH B 317      -1.110  11.106  11.625  1.00 52.23           O  
ANISOU 4152  O   HOH B 317     6361   6562   6922   -498    106   -334       O  
HETATM 4153  O   HOH B 318      24.152  44.257  17.452  1.00 44.64           O  
ANISOU 4153  O   HOH B 318     6156   3710   7097  -1631     23    -42       O  
HETATM 4154  O   HOH B 319       4.078   9.291  18.750  1.00 45.69           O  
ANISOU 4154  O   HOH B 319     6142   5370   5850   -541    312    -39       O  
HETATM 4155  O   HOH B 320      -9.431   0.664   2.624  1.00 69.11           O  
ANISOU 4155  O   HOH B 320     8166   8538   9556  -1460   -967  -1283       O  
HETATM 4156  O   HOH B 321     -11.062   2.969   4.308  1.00 66.02           O  
ANISOU 4156  O   HOH B 321     7394   8395   9293  -1437   -804  -1120       O  
HETATM 4157  O   HOH B 322      17.426  55.606  28.528  1.00 68.04           O  
ANISOU 4157  O   HOH B 322    10166   4375  11310   -492  -1044  -2024       O  
HETATM 4158  O   HOH B 323       1.012  16.733  16.113  1.00 44.84           O  
ANISOU 4158  O   HOH B 323     5449   5678   5910   -228    399   -221       O  
HETATM 4159  O   HOH B 324      36.155  43.755  45.999  1.00 77.35           O  
ANISOU 4159  O   HOH B 324    10118   9183  10090  -1454  -2979  -3674       O  
CONECT   29 3615                                                                
CONECT   84 3959                                                                
CONECT  175 4026                                                                
CONECT  318 2165                                                                
CONECT  407 4054                                                                
CONECT  413  499                                                                
CONECT  499  413                                                                
CONECT  668 3998                                                                
CONECT  685 1049                                                                
CONECT 1049  685                                                                
CONECT 2165  318                                                                
CONECT 2193 2370                                                                
CONECT 2250 3909                                                                
CONECT 2370 2193                                                                
CONECT 3615   29                                                                
CONECT 3683 3714                                                                
CONECT 3714 3683                                                                
CONECT 3909 2250 3910 3920                                                      
CONECT 3910 3909 3911 3917                                                      
CONECT 3911 3910 3912 3918                                                      
CONECT 3912 3911 3913 3919                                                      
CONECT 3913 3912 3914 3920                                                      
CONECT 3914 3913 3921                                                           
CONECT 3915 3916 3917 3922                                                      
CONECT 3916 3915                                                                
CONECT 3917 3910 3915                                                           
CONECT 3918 3911                                                                
CONECT 3919 3912 3923                                                           
CONECT 3920 3909 3913                                                           
CONECT 3921 3914                                                                
CONECT 3922 3915                                                                
CONECT 3923 3919 3924 3934                                                      
CONECT 3924 3923 3925 3931                                                      
CONECT 3925 3924 3926 3932                                                      
CONECT 3926 3925 3927 3933                                                      
CONECT 3927 3926 3928 3934                                                      
CONECT 3928 3927 3935                                                           
CONECT 3929 3930 3931 3936                                                      
CONECT 3930 3929                                                                
CONECT 3931 3924 3929                                                           
CONECT 3932 3925                                                                
CONECT 3933 3926 3937                                                           
CONECT 3934 3923 3927                                                           
CONECT 3935 3928                                                                
CONECT 3936 3929                                                                
CONECT 3937 3933 3938 3946                                                      
CONECT 3938 3937 3939 3943                                                      
CONECT 3939 3938 3940 3944                                                      
CONECT 3940 3939 3941 3945                                                      
CONECT 3941 3940 3942 3946                                                      
CONECT 3942 3941 3947                                                           
CONECT 3943 3938                                                                
CONECT 3944 3939 3948                                                           
CONECT 3945 3940                                                                
CONECT 3946 3937 3941                                                           
CONECT 3947 3942                                                                
CONECT 3948 3944 3949 3957                                                      
CONECT 3949 3948 3950 3954                                                      
CONECT 3950 3949 3951 3955                                                      
CONECT 3951 3950 3952 3956                                                      
CONECT 3952 3951 3953 3957                                                      
CONECT 3953 3952 3958                                                           
CONECT 3954 3949                                                                
CONECT 3955 3950                                                                
CONECT 3956 3951                                                                
CONECT 3957 3948 3952                                                           
CONECT 3958 3953                                                                
CONECT 3959   84 3960 3970                                                      
CONECT 3960 3959 3961 3967                                                      
CONECT 3961 3960 3962 3968                                                      
CONECT 3962 3961 3963 3969                                                      
CONECT 3963 3962 3964 3970                                                      
CONECT 3964 3963 3971                                                           
CONECT 3965 3966 3967 3972                                                      
CONECT 3966 3965                                                                
CONECT 3967 3960 3965                                                           
CONECT 3968 3961                                                                
CONECT 3969 3962 3973                                                           
CONECT 3970 3959 3963                                                           
CONECT 3971 3964                                                                
CONECT 3972 3965                                                                
CONECT 3973 3969 3974 3984                                                      
CONECT 3974 3973 3975 3981                                                      
CONECT 3975 3974 3976 3982                                                      
CONECT 3976 3975 3977 3983                                                      
CONECT 3977 3976 3978 3984                                                      
CONECT 3978 3977 3985                                                           
CONECT 3979 3980 3981 3986                                                      
CONECT 3980 3979                                                                
CONECT 3981 3974 3979                                                           
CONECT 3982 3975                                                                
CONECT 3983 3976 3987                                                           
CONECT 3984 3973 3977                                                           
CONECT 3985 3978                                                                
CONECT 3986 3979                                                                
CONECT 3987 3983 3988 3996                                                      
CONECT 3988 3987 3989 3993                                                      
CONECT 3989 3988 3990 3994                                                      
CONECT 3990 3989 3991 3995                                                      
CONECT 3991 3990 3992 3996                                                      
CONECT 3992 3991 3997                                                           
CONECT 3993 3988                                                                
CONECT 3994 3989                                                                
CONECT 3995 3990                                                                
CONECT 3996 3987 3991                                                           
CONECT 3997 3992                                                                
CONECT 3998  668 3999 4009                                                      
CONECT 3999 3998 4000 4006                                                      
CONECT 4000 3999 4001 4007                                                      
CONECT 4001 4000 4002 4008                                                      
CONECT 4002 4001 4003 4009                                                      
CONECT 4003 4002 4010                                                           
CONECT 4004 4005 4006 4011                                                      
CONECT 4005 4004                                                                
CONECT 4006 3999 4004                                                           
CONECT 4007 4000                                                                
CONECT 4008 4001 4012                                                           
CONECT 4009 3998 4002                                                           
CONECT 4010 4003                                                                
CONECT 4011 4004                                                                
CONECT 4012 4008 4013 4023                                                      
CONECT 4013 4012 4014 4020                                                      
CONECT 4014 4013 4015 4021                                                      
CONECT 4015 4014 4016 4022                                                      
CONECT 4016 4015 4017 4023                                                      
CONECT 4017 4016 4024                                                           
CONECT 4018 4019 4020 4025                                                      
CONECT 4019 4018                                                                
CONECT 4020 4013 4018                                                           
CONECT 4021 4014                                                                
CONECT 4022 4015                                                                
CONECT 4023 4012 4016                                                           
CONECT 4024 4017                                                                
CONECT 4025 4018                                                                
CONECT 4026  175 4027 4037                                                      
CONECT 4027 4026 4028 4034                                                      
CONECT 4028 4027 4029 4035                                                      
CONECT 4029 4028 4030 4036                                                      
CONECT 4030 4029 4031 4037                                                      
CONECT 4031 4030 4038                                                           
CONECT 4032 4033 4034 4039                                                      
CONECT 4033 4032                                                                
CONECT 4034 4027 4032                                                           
CONECT 4035 4028                                                                
CONECT 4036 4029 4040                                                           
CONECT 4037 4026 4030                                                           
CONECT 4038 4031                                                                
CONECT 4039 4032                                                                
CONECT 4040 4036 4041 4051                                                      
CONECT 4041 4040 4042 4048                                                      
CONECT 4042 4041 4043 4049                                                      
CONECT 4043 4042 4044 4050                                                      
CONECT 4044 4043 4045 4051                                                      
CONECT 4045 4044 4052                                                           
CONECT 4046 4047 4048 4053                                                      
CONECT 4047 4046                                                                
CONECT 4048 4041 4046                                                           
CONECT 4049 4042                                                                
CONECT 4050 4043                                                                
CONECT 4051 4040 4044                                                           
CONECT 4052 4045                                                                
CONECT 4053 4046                                                                
CONECT 4054  407 4055 4065                                                      
CONECT 4055 4054 4056 4062                                                      
CONECT 4056 4055 4057 4063                                                      
CONECT 4057 4056 4058 4064                                                      
CONECT 4058 4057 4059 4065                                                      
CONECT 4059 4058 4066                                                           
CONECT 4060 4061 4062 4067                                                      
CONECT 4061 4060                                                                
CONECT 4062 4055 4060                                                           
CONECT 4063 4056                                                                
CONECT 4064 4057                                                                
CONECT 4065 4054 4058                                                           
CONECT 4066 4059                                                                
CONECT 4067 4060                                                                
CONECT 4068 4069 4080                                                           
CONECT 4069 4068 4070 4079                                                      
CONECT 4070 4069 4071                                                           
CONECT 4071 4070 4072 4082                                                      
CONECT 4072 4071 4080 4081                                                      
CONECT 4073 4084 4085                                                           
CONECT 4074 4075 4084                                                           
CONECT 4075 4074 4086 4087                                                      
CONECT 4076 4077                                                                
CONECT 4077 4076 4078 4079                                                      
CONECT 4078 4077                                                                
CONECT 4079 4069 4077                                                           
CONECT 4080 4068 4072                                                           
CONECT 4081 4072 4083                                                           
CONECT 4082 4071 4083                                                           
CONECT 4083 4081 4082 4084                                                      
CONECT 4084 4073 4074 4083                                                      
CONECT 4085 4073 4086                                                           
CONECT 4086 4075 4085                                                           
CONECT 4087 4075 4088 4089                                                      
CONECT 4088 4087                                                                
CONECT 4089 4087 4090 4092                                                      
CONECT 4090 4089 4091                                                           
CONECT 4091 4090 4094                                                           
CONECT 4092 4089 4093                                                           
CONECT 4093 4092 4094                                                           
CONECT 4094 4091 4093 4095                                                      
CONECT 4095 4094 4096 4102                                                      
CONECT 4096 4095 4097 4098                                                      
CONECT 4097 4096 4100                                                           
CONECT 4098 4096 4099                                                           
CONECT 4099 4098 4100                                                           
CONECT 4100 4097 4099 4101                                                      
CONECT 4101 4100                                                                
CONECT 4102 4095 4103 4107                                                      
CONECT 4103 4102 4104                                                           
CONECT 4104 4103 4105                                                           
CONECT 4105 4104 4106                                                           
CONECT 4106 4105 4107                                                           
CONECT 4107 4102 4106                                                           
MASTER      368    0   13    9   35    0   11    6 4157    2  216   40          
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.