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***  VIRAL PROTEIN 17-DEC-21 7WBQ  ***

elNémo ID: 220221231311117641

Job options:

ID        	=	 220221231311117641
JOBID     	=	 VIRAL PROTEIN 17-DEC-21 7WBQ
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    VIRAL PROTEIN                           17-DEC-21   7WBQ              
TITLE     CRYSTAL STRUCTURE OF THE RECEPTOR BINDING DOMAIN OF SARS-COV-2 DELTA  
TITLE    2 VARIANT SPIKE GLYCOPROTEIN IN COMPLEX WITH ITS RECEPTOR HUMAN ACE2   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME 2;                           
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: ACE-RELATED CARBOXYPEPTIDASE,ANGIOTENSIN-CONVERTING ENZYME  
COMPND   5 HOMOLOG;                                                             
COMPND   6 EC: 3.4.17.23,3.4.17.-;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SPIKE PROTEIN S1;                                          
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;              
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 266783;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE  10 2;                                                                   
SOURCE  11 ORGANISM_TAXID: 2697049;                                             
SOURCE  12 GENE: S, 2;                                                          
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    COMPLEX, VIRAL PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.QI,P.HAN                                                            
REVDAT   1   19-JAN-22 7WBQ    0                                                
JRNL        AUTH   P.HAN,L.LI,S.LIU,Q.WANG,D.ZHANG,Z.XU,P.HAN,X.LI,Q.PENG,C.SU, 
JRNL        AUTH 2 B.HUANG,D.LI,R.ZHANG,M.TIAN,L.FU,Y.GAO,X.ZHAO,K.LIU,J.QI,    
JRNL        AUTH 3 G.F.GAO,P.WANG                                               
JRNL        TITL   RECEPTOR BINDING AND COMPLEX STRUCTURES OF HUMAN ACE2 TO     
JRNL        TITL 2 SPIKE RBD FROM OMICRON AND DELTA SARS-COV-2.                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)                      2022              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        DOI    10.1016/J.CELL.2022.01.001                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19RC3_4028                                  
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38490                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1986                            
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 44.7000 -  8.0400    0.98     2652   144  0.1793 0.1924        
REMARK   3     2  8.0400 -  6.3900    1.00     2661   144  0.1897 0.1875        
REMARK   3     3  6.3900 -  5.5800    1.00     2636   144  0.1879 0.2281        
REMARK   3     4  5.5800 -  5.0700    1.00     2658   145  0.1742 0.2119        
REMARK   3     5  5.0700 -  4.7100    1.00     2633   143  0.1548 0.1777        
REMARK   3     6  4.7100 -  4.4300    1.00     2622   143  0.1571 0.2286        
REMARK   3     7  4.4300 -  4.2100    1.00     2654   146  0.1779 0.2000        
REMARK   3     8  4.2100 -  4.0300    1.00     2625   142  0.1875 0.2142        
REMARK   3     9  4.0300 -  3.8700    1.00     2637   144  0.2043 0.2488        
REMARK   3    10  3.8700 -  3.7400    1.00     2618   143  0.2254 0.2816        
REMARK   3    11  3.7400 -  3.6200    1.00     2618   143  0.2616 0.3103        
REMARK   3    12  3.6200 -  3.5200    0.99     2591   139  0.2993 0.3117        
REMARK   3    13  3.5200 -  3.4300    0.99     2598   141  0.3336 0.3821        
REMARK   3    14  3.4300 -  3.3400    0.87     2301   125  0.3704 0.4375        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.513            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.685           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 106.3                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 120.4                          
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      :  0.003          13398                                  
REMARK   3   ANGLE     :  0.629          18212                                  
REMARK   3   CHIRALITY :  0.044           1949                                  
REMARK   3   PLANARITY :  0.005           2344                                  
REMARK   3   DIHEDRAL  :  7.845           1842                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 22                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 19:109 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   17.286   42.262   56.751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1115 T22:   0.9350                                     
REMARK   3      T33:   0.9274 T12:   0.0232                                     
REMARK   3      T13:  -0.1068 T23:   0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2298 L22:   5.5823                                     
REMARK   3      L33:   0.6298 L12:   1.4314                                     
REMARK   3      L13:   1.1993 L23:   0.7815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2206 S12:   0.3407 S13:   0.0891                       
REMARK   3      S21:   0.2815 S22:   0.2974 S23:   0.7008                       
REMARK   3      S31:  -0.2329 S32:  -0.0843 S33:  -0.0759                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 110:172 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.422   22.263   53.820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8842 T22:   1.0343                                     
REMARK   3      T33:   0.7364 T12:  -0.0419                                     
REMARK   3      T13:   0.0960 T23:  -0.0739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4297 L22:   7.0029                                     
REMARK   3      L33:   4.9589 L12:   2.1396                                     
REMARK   3      L13:   1.8657 L23:   3.3679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7008 S12:  -0.8434 S13:  -0.0164                       
REMARK   3      S21:   1.6527 S22:  -0.7792 S23:   0.8224                       
REMARK   3      S31:   0.7774 S32:  -1.1545 S33:  -0.0283                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 173:318 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.269   19.812   40.094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7104 T22:   0.7357                                     
REMARK   3      T33:   0.6079 T12:   0.0632                                     
REMARK   3      T13:  -0.0194 T23:  -0.1531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6913 L22:   2.4967                                     
REMARK   3      L33:   2.9613 L12:   0.9263                                     
REMARK   3      L13:   1.2951 L23:   0.4498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:   0.4935 S13:  -0.3995                       
REMARK   3      S21:   0.0480 S22:   0.0595 S23:  -0.1496                       
REMARK   3      S31:   0.1103 S32:   0.2387 S33:  -0.0923                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 319:431 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   18.639   15.655   52.665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8177 T22:   0.9081                                     
REMARK   3      T33:   0.9715 T12:   0.2038                                     
REMARK   3      T13:  -0.2557 T23:  -0.1246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4601 L22:   7.0193                                     
REMARK   3      L33:   4.4013 L12:   1.6947                                     
REMARK   3      L13:   0.3409 L23:   0.8298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3045 S12:   0.3888 S13:  -0.8611                       
REMARK   3      S21:   0.4413 S22:  -0.0868 S23:  -0.1776                       
REMARK   3      S31:   0.8091 S32:   0.4611 S33:  -0.2085                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 432:614 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    3.910   20.165   35.113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7011 T22:   0.7572                                     
REMARK   3      T33:   0.6277 T12:   0.0144                                     
REMARK   3      T13:  -0.0360 T23:  -0.0974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8780 L22:   2.5642                                     
REMARK   3      L33:   2.9305 L12:   0.5608                                     
REMARK   3      L13:   0.8973 L23:   0.8582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0095 S12:   0.7597 S13:  -0.7915                       
REMARK   3      S21:  -0.1939 S22:   0.0555 S23:   0.0041                       
REMARK   3      S31:   0.0778 S32:   0.2933 S33:  -0.0390                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 333:364 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   53.049   36.759   76.079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0288 T22:   1.0909                                     
REMARK   3      T33:   1.0388 T12:   0.2107                                     
REMARK   3      T13:  -0.2914 T23:  -0.3108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8422 L22:   5.8925                                     
REMARK   3      L33:   7.4497 L12:  -0.8609                                     
REMARK   3      L13:   3.7721 L23:  -0.9731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3487 S12:  -0.4128 S13:   0.4052                       
REMARK   3      S21:   0.0943 S22:   0.2501 S23:  -0.9081                       
REMARK   3      S31:   0.2346 S32:   0.7996 S33:   0.0310                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 365:375 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   54.434   23.334   69.430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6265 T22:   1.4678                                     
REMARK   3      T33:   2.0125 T12:   0.1044                                     
REMARK   3      T13:  -0.3750 T23:   0.1781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0114 L22:   2.6284                                     
REMARK   3      L33:   7.0126 L12:  -4.4471                                     
REMARK   3      L13:   6.2724 L23:  -0.1541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3089 S12:  -0.5814 S13:  -2.9442                       
REMARK   3      S21:  -0.0320 S22:   0.1923 S23:  -0.4442                       
REMARK   3      S31:   1.6579 S32:   0.6744 S33:  -0.2658                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 376:459 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   47.022   36.786   64.059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9098 T22:   1.0360                                     
REMARK   3      T33:   0.8463 T12:  -0.0304                                     
REMARK   3      T13:  -0.1247 T23:  -0.1705                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4489 L22:   3.9260                                     
REMARK   3      L33:   4.5644 L12:  -2.4776                                     
REMARK   3      L13:  -0.9680 L23:   0.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1140 S12:   0.4596 S13:  -0.4191                       
REMARK   3      S21:  -0.3032 S22:   0.2709 S23:  -0.8762                       
REMARK   3      S31:   0.0443 S32:   0.8418 S33:  -0.3240                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 460:479 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   40.114   54.679   61.306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9446 T22:   1.0813                                     
REMARK   3      T33:   1.2044 T12:  -0.1508                                     
REMARK   3      T13:  -0.1071 T23:   0.2742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9465 L22:   3.8369                                     
REMARK   3      L33:   3.4346 L12:  -1.9320                                     
REMARK   3      L13:   2.4941 L23:  -0.1750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0619 S12:   0.4498 S13:   1.8739                       
REMARK   3      S21:  -0.8956 S22:   0.2912 S23:   0.1043                       
REMARK   3      S31:  -0.4110 S32:   0.0323 S33:   0.0304                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 480:527 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   42.158   41.084   66.304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9160 T22:   0.9704                                     
REMARK   3      T33:   0.5927 T12:   0.0649                                     
REMARK   3      T13:  -0.0736 T23:  -0.1392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3866 L22:   5.3425                                     
REMARK   3      L33:   1.7689 L12:  -1.9352                                     
REMARK   3      L13:   1.7300 L23:  -1.2730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2710 S12:  -0.1749 S13:   0.1587                       
REMARK   3      S21:  -0.0596 S22:   0.6193 S23:  -0.3343                       
REMARK   3      S31:  -0.0282 S32:   0.3287 S33:  -0.3041                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 19:82 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   48.667   46.324   15.522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2441 T22:   1.5891                                     
REMARK   3      T33:   0.9146 T12:   0.0087                                     
REMARK   3      T13:  -0.0540 T23:   0.2559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9539 L22:   5.7730                                     
REMARK   3      L33:   2.5994 L12:  -2.0897                                     
REMARK   3      L13:   0.0728 L23:   4.7566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1219 S12:  -1.1887 S13:  -0.1169                       
REMARK   3      S21:   1.7106 S22:   0.5007 S23:   0.1673                       
REMARK   3      S31:   1.2347 S32:   0.2583 S33:  -0.3452                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 83:129 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   37.582   58.116   18.862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4137 T22:   1.9771                                     
REMARK   3      T33:   1.0702 T12:   0.3108                                     
REMARK   3      T13:  -0.2086 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0935 L22:   1.0536                                     
REMARK   3      L33:   1.7338 L12:   0.5573                                     
REMARK   3      L13:   0.2155 L23:  -1.4611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0632 S12:  -1.4050 S13:   0.8610                       
REMARK   3      S21:   0.3842 S22:   0.1096 S23:   0.4018                       
REMARK   3      S31:   0.2905 S32:  -0.3324 S33:  -0.1277                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 130:193 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   17.212   54.551   -1.841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4034 T22:   1.3173                                     
REMARK   3      T33:   1.4568 T12:  -0.0065                                     
REMARK   3      T13:  -0.2779 T23:   0.5560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6252 L22:   1.7831                                     
REMARK   3      L33:   5.6293 L12:  -0.6478                                     
REMARK   3      L13:   1.0956 L23:   0.0393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2943 S12:  -0.6386 S13:  -0.9248                       
REMARK   3      S21:   0.0374 S22:   0.5625 S23:   0.7818                       
REMARK   3      S31:   0.6936 S32:  -1.2831 S33:  -0.7626                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 194:293 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   30.868   69.737   -7.905              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7738 T22:   0.8742                                     
REMARK   3      T33:   0.8352 T12:   0.0430                                     
REMARK   3      T13:  -0.0715 T23:   0.1383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5120 L22:   1.7577                                     
REMARK   3      L33:   3.9612 L12:  -1.1729                                     
REMARK   3      L13:   0.9315 L23:  -0.9744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2714 S12:  -0.6574 S13:   0.2638                       
REMARK   3      S21:   0.5510 S22:   0.5690 S23:   0.1032                       
REMARK   3      S31:  -0.0067 S32:  -0.8210 S33:  -0.3130                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 294:352 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   51.660   45.665  -12.428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7213 T22:   0.9790                                     
REMARK   3      T33:   0.8407 T12:   0.0491                                     
REMARK   3      T13:  -0.0746 T23:   0.0745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1417 L22:   5.5305                                     
REMARK   3      L33:   7.0612 L12:  -0.3599                                     
REMARK   3      L13:   1.2449 L23:   0.0399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5848 S12:  -0.7933 S13:  -0.6361                       
REMARK   3      S21:   0.0230 S22:  -0.1045 S23:  -0.0847                       
REMARK   3      S31:   0.7123 S32:  -0.2884 S33:  -0.4497                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 353:431 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   50.190   56.075  -10.659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7318 T22:   0.7888                                     
REMARK   3      T33:   0.6699 T12:  -0.0007                                     
REMARK   3      T13:  -0.1994 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4372 L22:   2.7486                                     
REMARK   3      L33:   1.9154 L12:  -0.5039                                     
REMARK   3      L13:  -1.1664 L23:   1.3625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:  -0.3679 S13:   0.1129                       
REMARK   3      S21:   0.0648 S22:   0.3257 S23:   0.0706                       
REMARK   3      S31:   0.1165 S32:  -0.3990 S33:  -0.2956                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 432:558 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   34.003   67.788   -5.675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9004 T22:   0.8873                                     
REMARK   3      T33:   0.8187 T12:   0.1136                                     
REMARK   3      T13:  -0.1194 T23:   0.1404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3170 L22:   2.8234                                     
REMARK   3      L33:   2.8326 L12:  -0.3971                                     
REMARK   3      L13:   0.0834 L23:  -0.0249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0657 S12:  -0.7950 S13:   0.0916                       
REMARK   3      S21:   0.3852 S22:   0.4418 S23:   0.2725                       
REMARK   3      S31:  -0.1605 S32:  -0.5159 S33:  -0.4323                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 559:614 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   37.250   74.932  -10.553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7600 T22:   0.7639                                     
REMARK   3      T33:   0.7444 T12:   0.0832                                     
REMARK   3      T13:  -0.0526 T23:  -0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4571 L22:   3.3705                                     
REMARK   3      L33:   4.5335 L12:  -1.5936                                     
REMARK   3      L13:   3.0715 L23:  -1.3171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5603 S12:  -0.9473 S13:   0.9689                       
REMARK   3      S21:   0.4807 S22:   0.3316 S23:  -0.1096                       
REMARK   3      S31:  -0.4319 S32:  -0.5432 S33:   0.3000                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 333:364 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   84.872   32.226   14.481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0207 T22:   1.4445                                     
REMARK   3      T33:   1.1117 T12:   0.1780                                     
REMARK   3      T13:  -0.1471 T23:   0.2324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6816 L22:   4.7538                                     
REMARK   3      L33:   5.6159 L12:  -0.1084                                     
REMARK   3      L13:  -0.5832 L23:   0.7152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3755 S12:  -0.2510 S13:  -0.7369                       
REMARK   3      S21:   0.0553 S22:  -0.0654 S23:  -0.8837                       
REMARK   3      S31:   0.8709 S32:   0.4574 S33:  -0.0701                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 365:459 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   79.183   43.290   11.663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1147 T22:   1.2142                                     
REMARK   3      T33:   0.8965 T12:   0.0682                                     
REMARK   3      T13:  -0.2377 T23:   0.1974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7510 L22:   2.8481                                     
REMARK   3      L33:   3.6011 L12:   0.5402                                     
REMARK   3      L13:   0.2310 L23:   0.3572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1506 S12:  -0.8037 S13:  -0.1422                       
REMARK   3      S21:  -0.2967 S22:   0.0622 S23:  -0.0575                       
REMARK   3      S31:  -0.0468 S32:   0.3602 S33:   0.1093                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 460:506 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   65.072   45.930   24.573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0867 T22:   1.7286                                     
REMARK   3      T33:   0.8196 T12:   0.0609                                     
REMARK   3      T13:  -0.1052 T23:   0.1203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9807 L22:   2.5986                                     
REMARK   3      L33:   0.8808 L12:  -1.7405                                     
REMARK   3      L13:  -0.6005 L23:  -0.7172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0456 S12:  -1.6814 S13:  -0.0998                       
REMARK   3      S21:   0.7981 S22:   0.2411 S23:   0.0144                       
REMARK   3      S31:  -0.4535 S32:  -0.0648 S33:  -0.1152                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 507:526 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   90.691   39.423   14.213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0414 T22:   1.5413                                     
REMARK   3      T33:   0.8785 T12:  -0.0571                                     
REMARK   3      T13:  -0.0948 T23:   0.0969                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3274 L22:   6.8793                                     
REMARK   3      L33:   5.7762 L12:   0.9957                                     
REMARK   3      L13:   2.3779 L23:   1.1683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1666 S12:   0.3049 S13:  -0.7815                       
REMARK   3      S21:   0.2397 S22:   0.2748 S23:  -0.7816                       
REMARK   3      S31:  -0.4012 S32:   1.1683 S33:  -0.5381                       
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 7WBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300026403.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL02U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 X 9M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38716                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.16200                            
REMARK 200  R SYM                      (I) : 0.16200                            
REMARK 200   FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.30700                            
REMARK 200  R SYM FOR SHELL            (I) : 1.30700                            
REMARK 200   FOR SHELL         : 1.100                              
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: 6LZG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5,10%W/V PEG 5000          
REMARK 280  MME,12% V/V 1-PROPANOL, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       71.82700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG B   319                                                      
REMARK 465     VAL B   320                                                      
REMARK 465     GLN B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     THR B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     ILE B   326                                                      
REMARK 465     VAL B   327                                                      
REMARK 465     ARG B   328                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     PRO B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ILE B   332                                                      
REMARK 465     LYS B   528                                                      
REMARK 465     LYS B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     THR B   531                                                      
REMARK 465     ASN B   532                                                      
REMARK 465     LEU B   533                                                      
REMARK 465     VAL B   534                                                      
REMARK 465     LYS B   535                                                      
REMARK 465     ASN B   536                                                      
REMARK 465     LYS B   537                                                      
REMARK 465     CYS B   538                                                      
REMARK 465     VAL B   539                                                      
REMARK 465     ASN B   540                                                      
REMARK 465     PHE B   541                                                      
REMARK 465     ARG D   319                                                      
REMARK 465     VAL D   320                                                      
REMARK 465     GLN D   321                                                      
REMARK 465     PRO D   322                                                      
REMARK 465     THR D   323                                                      
REMARK 465     GLU D   324                                                      
REMARK 465     SER D   325                                                      
REMARK 465     ILE D   326                                                      
REMARK 465     VAL D   327                                                      
REMARK 465     ARG D   328                                                      
REMARK 465     PHE D   329                                                      
REMARK 465     PRO D   330                                                      
REMARK 465     ASN D   331                                                      
REMARK 465     ILE D   332                                                      
REMARK 465     PRO D   527                                                      
REMARK 465     LYS D   528                                                      
REMARK 465     LYS D   529                                                      
REMARK 465     SER D   530                                                      
REMARK 465     THR D   531                                                      
REMARK 465     ASN D   532                                                      
REMARK 465     LEU D   533                                                      
REMARK 465     VAL D   534                                                      
REMARK 465     LYS D   535                                                      
REMARK 465     ASN D   536                                                      
REMARK 465     LYS D   537                                                      
REMARK 465     CYS D   538                                                      
REMARK 465     VAL D   539                                                      
REMARK 465     ASN D   540                                                      
REMARK 465     PHE D   541                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG C 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 187    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP C   198     N    ASP C   201              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  53       77.66   -151.11                                   
REMARK 500    ASN A 137       83.17   -151.94                                   
REMARK 500    LEU A 156       45.09   -141.06                                   
REMARK 500    ARG A 273      -73.29    -83.53                                   
REMARK 500    ASN A 338     -127.56     57.65                                   
REMARK 500    MET A 360      117.39   -160.09                                   
REMARK 500    GLN A 472       19.14   -140.64                                   
REMARK 500    ASP A 494     -168.35    -73.65                                   
REMARK 500    CYS A 498       58.13   -147.74                                   
REMARK 500    SER A 547       79.98   -152.81                                   
REMARK 500    ALA B 352       51.07   -107.80                                   
REMARK 500    PHE B 377       84.19   -155.43                                   
REMARK 500    ASN B 422      -51.88   -135.24                                   
REMARK 500    ASP B 428       37.40    -98.07                                   
REMARK 500    SER B 477       20.12   -146.76                                   
REMARK 500    ALA B 522       72.22     58.55                                   
REMARK 500    ASN C  53      100.70   -162.94                                   
REMARK 500    ASP C 136       -4.94     85.37                                   
REMARK 500    ASN C 194       39.35    -82.99                                   
REMARK 500    ASN C 338     -128.24     52.65                                   
REMARK 500    GLN C 340      109.28    -48.70                                   
REMARK 500    MET C 360      118.34   -166.62                                   
REMARK 500    GLU C 495       47.93    -79.03                                   
REMARK 500    CYS C 498       53.87   -144.28                                   
REMARK 500    ASN C 601       60.44   -107.36                                   
REMARK 500    ALA D 352       70.21   -107.06                                   
REMARK 500    ASN D 370       42.46   -109.12                                   
REMARK 500    PHE D 377       79.48   -154.69                                   
REMARK 500    ASN D 422      -50.40   -133.60                                   
REMARK 500    ASP D 428       47.07    -95.07                                   
REMARK 500    CYS D 525      -74.76   -106.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 374   NE2                                                    
REMARK 620 2 HIS A 378   NE2 110.3                                              
REMARK 620 3 GLU A 402   OE2  89.4  98.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 374   NE2                                                    
REMARK 620 2 HIS C 378   NE2  94.4                                              
REMARK 620 3 GLU C 402   OE2  91.9 106.2                                        
REMARK 620 N                    1     2                                         
DBREF  7WBQ A   19   614  UNP    Q9BYF1   ACE2_HUMAN      19    614             
DBREF  7WBQ B  319   541  UNP    P0DTC2   SPIKE_SARS2    319    541             
DBREF  7WBQ C   19   614  UNP    Q9BYF1   ACE2_HUMAN      19    614             
DBREF  7WBQ D  319   541  UNP    P0DTC2   SPIKE_SARS2    319    541             
SEQADV 7WBQ ARG B  452  UNP  P0DTC2    LEU   452 VARIANT                        
SEQADV 7WBQ LYS B  478  UNP  P0DTC2    THR   478 ENGINEERED MUTATION            
SEQADV 7WBQ ARG D  452  UNP  P0DTC2    LEU   452 VARIANT                        
SEQADV 7WBQ LYS D  478  UNP  P0DTC2    THR   478 ENGINEERED MUTATION            
SEQRES   1 A  596  SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS          
SEQRES   2 A  596  PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER          
SEQRES   3 A  596  LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU          
SEQRES   4 A  596  ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER          
SEQRES   5 A  596  ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR          
SEQRES   6 A  596  PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN          
SEQRES   7 A  596  LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER          
SEQRES   8 A  596  GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR          
SEQRES   9 A  596  MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO          
SEQRES  10 A  596  ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU          
SEQRES  11 A  596  ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG          
SEQRES  12 A  596  LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS          
SEQRES  13 A  596  GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS          
SEQRES  14 A  596  ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY          
SEQRES  15 A  596  ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP          
SEQRES  16 A  596  GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL          
SEQRES  17 A  596  GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS          
SEQRES  18 A  596  LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR          
SEQRES  19 A  596  PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS          
SEQRES  20 A  596  LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU          
SEQRES  21 A  596  TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE          
SEQRES  22 A  596  ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA          
SEQRES  23 A  596  GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER          
SEQRES  24 A  596  VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN          
SEQRES  25 A  596  SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL          
SEQRES  26 A  596  CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE          
SEQRES  27 A  596  ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE          
SEQRES  28 A  596  LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP          
SEQRES  29 A  596  MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY          
SEQRES  30 A  596  ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET          
SEQRES  31 A  596  SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE          
SEQRES  32 A  596  GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR          
SEQRES  33 A  596  GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL          
SEQRES  34 A  596  GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG          
SEQRES  35 A  596  TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP          
SEQRES  36 A  596  MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY          
SEQRES  37 A  596  VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP          
SEQRES  38 A  596  PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE          
SEQRES  39 A  596  ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE          
SEQRES  40 A  596  GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO          
SEQRES  41 A  596  LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY          
SEQRES  42 A  596  GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU          
SEQRES  43 A  596  PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS          
SEQRES  44 A  596  ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO          
SEQRES  45 A  596  LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE          
SEQRES  46 A  596  VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA                  
SEQRES   1 B  223  ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN          
SEQRES   2 B  223  ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA          
SEQRES   3 B  223  THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG          
SEQRES   4 B  223  ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN          
SEQRES   5 B  223  SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER          
SEQRES   6 B  223  PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR          
SEQRES   7 B  223  ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN          
SEQRES   8 B  223  ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN          
SEQRES   9 B  223  TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA          
SEQRES  10 B  223  TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN          
SEQRES  11 B  223  TYR ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU          
SEQRES  12 B  223  LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN          
SEQRES  13 B  223  ALA GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN          
SEQRES  14 B  223  CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR          
SEQRES  15 B  223  ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU          
SEQRES  16 B  223  SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY          
SEQRES  17 B  223  PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL          
SEQRES  18 B  223  ASN PHE                                                      
SEQRES   1 C  596  SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS          
SEQRES   2 C  596  PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER          
SEQRES   3 C  596  LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU          
SEQRES   4 C  596  ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER          
SEQRES   5 C  596  ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR          
SEQRES   6 C  596  PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN          
SEQRES   7 C  596  LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER          
SEQRES   8 C  596  GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR          
SEQRES   9 C  596  MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO          
SEQRES  10 C  596  ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU          
SEQRES  11 C  596  ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG          
SEQRES  12 C  596  LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS          
SEQRES  13 C  596  GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS          
SEQRES  14 C  596  ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY          
SEQRES  15 C  596  ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP          
SEQRES  16 C  596  GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL          
SEQRES  17 C  596  GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS          
SEQRES  18 C  596  LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR          
SEQRES  19 C  596  PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS          
SEQRES  20 C  596  LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU          
SEQRES  21 C  596  TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE          
SEQRES  22 C  596  ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA          
SEQRES  23 C  596  GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER          
SEQRES  24 C  596  VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN          
SEQRES  25 C  596  SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL          
SEQRES  26 C  596  CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE          
SEQRES  27 C  596  ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE          
SEQRES  28 C  596  LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP          
SEQRES  29 C  596  MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY          
SEQRES  30 C  596  ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET          
SEQRES  31 C  596  SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE          
SEQRES  32 C  596  GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR          
SEQRES  33 C  596  GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL          
SEQRES  34 C  596  GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG          
SEQRES  35 C  596  TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP          
SEQRES  36 C  596  MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY          
SEQRES  37 C  596  VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP          
SEQRES  38 C  596  PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE          
SEQRES  39 C  596  ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE          
SEQRES  40 C  596  GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO          
SEQRES  41 C  596  LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY          
SEQRES  42 C  596  GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU          
SEQRES  43 C  596  PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS          
SEQRES  44 C  596  ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO          
SEQRES  45 C  596  LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE          
SEQRES  46 C  596  VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA                  
SEQRES   1 D  223  ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN          
SEQRES   2 D  223  ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA          
SEQRES   3 D  223  THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG          
SEQRES   4 D  223  ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN          
SEQRES   5 D  223  SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER          
SEQRES   6 D  223  PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR          
SEQRES   7 D  223  ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN          
SEQRES   8 D  223  ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN          
SEQRES   9 D  223  TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA          
SEQRES  10 D  223  TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN          
SEQRES  11 D  223  TYR ASN TYR ARG TYR ARG LEU PHE ARG LYS SER ASN LEU          
SEQRES  12 D  223  LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN          
SEQRES  13 D  223  ALA GLY SER LYS PRO CYS ASN GLY VAL GLU GLY PHE ASN          
SEQRES  14 D  223  CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR          
SEQRES  15 D  223  ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU          
SEQRES  16 D  223  SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY          
SEQRES  17 D  223  PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL          
SEQRES  18 D  223  ASN PHE                                                      
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    FUL  F   2      10                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  A 701      14                                                       
HET     ZN  A 702       1                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    NAG  A 705      14                                                       
HET    NAG  C 701      14                                                       
HET     ZN  C 702       1                                                       
HET    NAG  C 703      14                                                       
HET    NAG  C 704      14                                                       
HET    NAG  C 705      14                                                       
HET    NAG  C 706      14                                                       
HET    NAG  D 601      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUL BETA-L-FUCOPYRANOSE                                              
HETNAM      ZN ZINC ION                                                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-                
HETSYN   2 FUL  FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE                        
FORMUL   5  NAG    15(C8 H15 N O6)                                              
FORMUL   6  FUL    C6 H12 O5                                                    
FORMUL   9   ZN    2(ZN 2+)                                                     
HELIX    1 AA1 THR A   20  ASN A   53  1                                  34    
HELIX    2 AA2 THR A   55  GLN A   81  1                                  27    
HELIX    3 AA3 MET A   82  TYR A   83  5                                   2    
HELIX    4 AA4 PRO A   84  ILE A   88  5                                   5    
HELIX    5 AA5 ASN A   90  GLN A  101  1                                  12    
HELIX    6 AA6 ASN A  103  LEU A  108  5                                   6    
HELIX    7 AA7 SER A  109  GLY A  130  1                                  22    
HELIX    8 AA8 PRO A  146  SER A  155  1                                  10    
HELIX    9 AA9 ASP A  157  VAL A  172  1                                  16    
HELIX   10 AB1 VAL A  172  ASN A  194  1                                  23    
HELIX   11 AB2 ASP A  198  GLY A  205  1                                   8    
HELIX   12 AB3 ASP A  206  GLU A  208  5                                   3    
HELIX   13 AB4 GLY A  220  ASN A  250  1                                  31    
HELIX   14 AB5 HIS A  265  LEU A  267  5                                   3    
HELIX   15 AB6 TRP A  275  ASN A  277  5                                   3    
HELIX   16 AB7 LEU A  278  VAL A  283  1                                   6    
HELIX   17 AB8 VAL A  293  GLN A  300  1                                   8    
HELIX   18 AB9 ASP A  303  SER A  317  1                                  15    
HELIX   19 AC1 THR A  324  SER A  331  1                                   8    
HELIX   20 AC2 THR A  365  TYR A  385  1                                  21    
HELIX   21 AC3 PRO A  389  ARG A  393  5                                   5    
HELIX   22 AC4 GLY A  399  THR A  414  1                                  16    
HELIX   23 AC5 THR A  414  ILE A  421  1                                   8    
HELIX   24 AC6 ASP A  431  GLY A  466  1                                  36    
HELIX   25 AC7 PRO A  469  ASP A  471  5                                   3    
HELIX   26 AC8 GLN A  472  ILE A  484  1                                  13    
HELIX   27 AC9 CYS A  498  SER A  502  5                                   5    
HELIX   28 AD1 LEU A  503  ASN A  508  1                                   6    
HELIX   29 AD2 ILE A  513  ALA A  533  1                                  21    
HELIX   30 AD3 PRO A  538  CYS A  542  5                                   5    
HELIX   31 AD4 SER A  547  ARG A  559  1                                  13    
HELIX   32 AD5 PRO A  565  GLY A  575  1                                  11    
HELIX   33 AD6 VAL A  581  LYS A  596  1                                  16    
HELIX   34 AD7 PRO B  337  ASN B  343  1                                   7    
HELIX   35 AD8 SER B  349  TRP B  353  5                                   5    
HELIX   36 AD9 ASP B  364  ASN B  370  1                                   7    
HELIX   37 AE1 LYS B  386  LEU B  390  5                                   5    
HELIX   38 AE2 ASP B  405  ILE B  410  5                                   6    
HELIX   39 AE3 GLY B  416  ASN B  422  1                                   7    
HELIX   40 AE4 SER B  438  SER B  443  1                                   6    
HELIX   41 AE5 GLY B  502  TYR B  505  5                                   4    
HELIX   42 AE6 THR C   20  ASN C   53  1                                  34    
HELIX   43 AE7 THR C   55  GLN C   81  1                                  27    
HELIX   44 AE8 MET C   82  TYR C   83  5                                   2    
HELIX   45 AE9 PRO C   84  ILE C   88  5                                   5    
HELIX   46 AF1 ASN C   90  GLN C  102  1                                  13    
HELIX   47 AF2 ASN C  103  LEU C  108  5                                   6    
HELIX   48 AF3 SER C  109  GLY C  130  1                                  22    
HELIX   49 AF4 PRO C  146  SER C  155  1                                  10    
HELIX   50 AF5 ASP C  157  ASN C  194  1                                  38    
HELIX   51 AF6 ASP C  198  ARG C  204  1                                   7    
HELIX   52 AF7 GLY C  205  GLU C  208  5                                   4    
HELIX   53 AF8 SER C  218  TYR C  252  1                                  35    
HELIX   54 AF9 HIS C  265  LEU C  267  5                                   3    
HELIX   55 AG1 TRP C  275  ASN C  277  5                                   3    
HELIX   56 AG2 LEU C  278  VAL C  283  1                                   6    
HELIX   57 AG3 VAL C  293  GLN C  300  1                                   8    
HELIX   58 AG4 ASP C  303  VAL C  318  1                                  16    
HELIX   59 AG5 THR C  324  SER C  331  1                                   8    
HELIX   60 AG6 THR C  365  TYR C  385  1                                  21    
HELIX   61 AG7 PRO C  389  ARG C  393  5                                   5    
HELIX   62 AG8 GLY C  399  ALA C  413  1                                  15    
HELIX   63 AG9 THR C  414  ILE C  421  1                                   8    
HELIX   64 AH1 ASP C  431  GLY C  466  1                                  36    
HELIX   65 AH2 PRO C  469  ASP C  471  5                                   3    
HELIX   66 AH3 GLN C  472  ILE C  484  1                                  13    
HELIX   67 AH4 CYS C  498  SER C  502  5                                   5    
HELIX   68 AH5 LEU C  503  ASN C  508  1                                   6    
HELIX   69 AH6 ILE C  513  ALA C  533  1                                  21    
HELIX   70 AH7 PRO C  538  CYS C  542  5                                   5    
HELIX   71 AH8 SER C  547  ARG C  559  1                                  13    
HELIX   72 AH9 PRO C  565  GLY C  575  1                                  11    
HELIX   73 AI1 VAL C  581  ASN C  599  1                                  19    
HELIX   74 AI2 LYS C  600  SER C  602  5                                   3    
HELIX   75 AI3 PRO D  337  ASN D  343  1                                   7    
HELIX   76 AI4 ASP D  364  ASN D  370  1                                   7    
HELIX   77 AI5 ASP D  405  ILE D  410  5                                   6    
HELIX   78 AI6 GLY D  416  ASN D  422  1                                   7    
HELIX   79 AI7 SER D  438  SER D  443  1                                   6    
HELIX   80 AI8 GLY D  502  TYR D  505  5                                   4    
SHEET    1 AA1 2 LYS A 131  ASN A 134  0                                        
SHEET    2 AA1 2 ASN A 137  LEU A 143 -1  O  LEU A 142   N  VAL A 132           
SHEET    1 AA2 2 LEU A 262  PRO A 263  0                                        
SHEET    2 AA2 2 VAL A 487  VAL A 488  1  O  VAL A 488   N  LEU A 262           
SHEET    1 AA3 2 THR A 347  GLY A 352  0                                        
SHEET    2 AA3 2 ASP A 355  LEU A 359 -1  O  ARG A 357   N  TRP A 349           
SHEET    1 AA4 5 ASN B 354  ILE B 358  0                                        
SHEET    2 AA4 5 ASN B 394  ARG B 403 -1  O  VAL B 395   N  ILE B 358           
SHEET    3 AA4 5 PRO B 507  GLU B 516 -1  O  TYR B 508   N  ILE B 402           
SHEET    4 AA4 5 GLY B 431  ASN B 437 -1  N  TRP B 436   O  ARG B 509           
SHEET    5 AA4 5 THR B 376  TYR B 380 -1  N  TYR B 380   O  GLY B 431           
SHEET    1 AA5 2 ARG B 452  ARG B 454  0                                        
SHEET    2 AA5 2 LEU B 492  SER B 494 -1  O  GLN B 493   N  TYR B 453           
SHEET    1 AA6 2 TYR B 473  GLN B 474  0                                        
SHEET    2 AA6 2 CYS B 488  TYR B 489 -1  O  TYR B 489   N  TYR B 473           
SHEET    1 AA7 2 VAL C 132  CYS C 133  0                                        
SHEET    2 AA7 2 CYS C 141  LEU C 142 -1  O  LEU C 142   N  VAL C 132           
SHEET    1 AA8 2 LEU C 262  PRO C 263  0                                        
SHEET    2 AA8 2 VAL C 487  VAL C 488  1  O  VAL C 488   N  LEU C 262           
SHEET    1 AA9 2 THR C 347  GLY C 352  0                                        
SHEET    2 AA9 2 ASP C 355  LEU C 359 -1  O  ARG C 357   N  TRP C 349           
SHEET    1 AB1 5 ASN D 354  ILE D 358  0                                        
SHEET    2 AB1 5 ASN D 394  ARG D 403 -1  O  VAL D 395   N  ILE D 358           
SHEET    3 AB1 5 PRO D 507  GLU D 516 -1  O  TYR D 508   N  ILE D 402           
SHEET    4 AB1 5 GLY D 431  ASN D 437 -1  N  ILE D 434   O  VAL D 511           
SHEET    5 AB1 5 THR D 376  TYR D 380 -1  N  TYR D 380   O  GLY D 431           
SHEET    1 AB2 2 ARG D 452  ARG D 454  0                                        
SHEET    2 AB2 2 LEU D 492  SER D 494 -1  O  GLN D 493   N  TYR D 453           
SHEET    1 AB3 2 TYR D 473  GLN D 474  0                                        
SHEET    2 AB3 2 CYS D 488  TYR D 489 -1  O  TYR D 489   N  TYR D 473           
SSBOND   1 CYS A  133    CYS A  141                          1555   1555  2.03  
SSBOND   2 CYS A  344    CYS A  361                          1555   1555  2.03  
SSBOND   3 CYS A  530    CYS A  542                          1555   1555  2.03  
SSBOND   4 CYS B  336    CYS B  361                          1555   1555  2.03  
SSBOND   5 CYS B  379    CYS B  432                          1555   1555  2.03  
SSBOND   6 CYS B  391    CYS B  525                          1555   1555  2.03  
SSBOND   7 CYS B  480    CYS B  488                          1555   1555  2.03  
SSBOND   8 CYS C  133    CYS C  141                          1555   1555  2.03  
SSBOND   9 CYS C  344    CYS C  361                          1555   1555  2.03  
SSBOND  10 CYS C  530    CYS C  542                          1555   1555  2.03  
SSBOND  11 CYS D  336    CYS D  361                          1555   1555  2.03  
SSBOND  12 CYS D  379    CYS D  432                          1555   1555  2.03  
SSBOND  13 CYS D  391    CYS D  525                          1555   1555  2.03  
SSBOND  14 CYS D  480    CYS D  488                          1555   1555  2.03  
LINK         ND2 ASN A  53                 C1  NAG A 703     1555   1555  1.43  
LINK         ND2 ASN A  90                 C1  NAG E   1     1555   1555  1.46  
LINK         ND2 ASN A 103                 C1  NAG A 705     1555   1555  1.44  
LINK         ND2 ASN A 322                 C1  NAG A 701     1555   1555  1.45  
LINK         ND2 ASN A 546                 C1  NAG A 704     1555   1555  1.46  
LINK         ND2 ASN B 343                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN C  53                 C1  NAG C 701     1555   1555  1.44  
LINK         ND2 ASN C  90                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN C 103                 C1  NAG C 704     1555   1555  1.44  
LINK         ND2 ASN C 322                 C1  NAG C 706     1555   1555  1.45  
LINK         ND2 ASN C 432                 C1  NAG C 705     1555   1555  1.44  
LINK         ND2 ASN C 546                 C1  NAG C 703     1555   1555  1.45  
LINK         ND2 ASN D 343                 C1  NAG D 601     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.46  
LINK         O6  NAG F   1                 C1  FUL F   2     1555   1555  1.44  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.45  
LINK         NE2 HIS A 374                ZN    ZN A 702     1555   1555  2.09  
LINK         NE2 HIS A 378                ZN    ZN A 702     1555   1555  2.09  
LINK         OE2 GLU A 402                ZN    ZN A 702     1555   1555  2.09  
LINK         NE2 HIS C 374                ZN    ZN C 702     1555   1555  2.10  
LINK         NE2 HIS C 378                ZN    ZN C 702     1555   1555  2.11  
LINK         OE2 GLU C 402                ZN    ZN C 702     1555   1555  2.09  
CISPEP   1 GLU A  145    PRO A  146          0         4.50                     
CISPEP   2 GLU C  145    PRO C  146          0         5.86                     
CRYST1   89.773  143.654  106.414  90.00  95.29  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011139  0.000000  0.001031        0.00000                         
SCALE2      0.000000  0.006961  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009437        0.00000                         
ATOM      1  N   SER A  19      33.472  58.470  46.809  1.00122.89           N  
ANISOU    1  N   SER A  19    17410  15709  13572  -2992  -1788   1564       N  
ATOM      2  CA  SER A  19      32.316  59.068  47.466  1.00108.72           C  
ANISOU    2  CA  SER A  19    15699  13692  11916  -2734  -2103   1758       C  
ATOM      3  C   SER A  19      31.047  58.879  46.640  1.00135.72           C  
ANISOU    3  C   SER A  19    19249  17241  15076  -2826  -2230   1962       C  
ATOM      4  O   SER A  19      30.042  59.546  46.879  1.00144.07           O  
ANISOU    4  O   SER A  19    20371  18117  16252  -2696  -2506   2180       O  
ATOM      5  CB  SER A  19      32.555  60.559  47.723  1.00110.34           C  
ANISOU    5  CB  SER A  19    15941  13641  12341  -2759  -2317   2006       C  
ATOM      6  OG  SER A  19      33.092  61.201  46.578  1.00119.60           O  
ANISOU    6  OG  SER A  19    17184  14930  13327  -3164  -2269   2230       O  
ATOM      7  N   THR A  20      31.099  57.970  45.668  1.00133.28           N  
ANISOU    7  N   THR A  20    18971  17231  14440  -3053  -2038   1873       N  
ATOM      8  CA  THR A  20      29.941  57.717  44.826  1.00117.15           C  
ANISOU    8  CA  THR A  20    17063  15314  12136  -3161  -2182   2051       C  
ATOM      9  C   THR A  20      28.799  57.131  45.651  1.00123.85           C  
ANISOU    9  C   THR A  20    17849  16042  13167  -2794  -2312   1966       C  
ATOM     10  O   THR A  20      29.000  56.564  46.729  1.00121.05           O  
ANISOU   10  O   THR A  20    17366  15597  13029  -2502  -2206   1709       O  
ATOM     11  CB  THR A  20      30.291  56.760  43.684  1.00117.08           C  
ANISOU   11  CB  THR A  20    17103  15652  11728  -3468  -1925   1910       C  
ATOM     12  OG1 THR A  20      30.134  55.406  44.126  1.00125.01           O  
ANISOU   12  OG1 THR A  20    17977  16745  12776  -3250  -1769   1573       O  
ATOM     13  CG2 THR A  20      31.725  56.972  43.233  1.00123.17           C  
ANISOU   13  CG2 THR A  20    17842  16546  12411  -3756  -1634   1811       C  
ATOM     14  N   ILE A  21      27.581  57.282  45.126  1.00127.55           N  
ANISOU   14  N   ILE A  21    18415  16495  13555  -2825  -2556   2194       N  
ATOM     15  CA  ILE A  21      26.415  56.709  45.791  1.00117.16           C  
ANISOU   15  CA  ILE A  21    17022  15070  12423  -2511  -2658   2122       C  
ATOM     16  C   ILE A  21      26.523  55.190  45.838  1.00115.44           C  
ANISOU   16  C   ILE A  21    16722  15058  12081  -2444  -2409   1801       C  
ATOM     17  O   ILE A  21      26.087  54.552  46.805  1.00122.72           O  
ANISOU   17  O   ILE A  21    17537  15881  13210  -2138  -2365   1627       O  
ATOM     18  CB  ILE A  21      25.122  57.168  45.095  1.00114.54           C  
ANISOU   18  CB  ILE A  21    16783  14665  12070  -2590  -2992   2432       C  
ATOM     19  CG1 ILE A  21      25.148  58.682  44.872  1.00119.03           C  
ANISOU   19  CG1 ILE A  21    17440  15032  12751  -2718  -3260   2768       C  
ATOM     20  CG2 ILE A  21      23.912  56.766  45.916  1.00119.72           C  
ANISOU   20  CG2 ILE A  21    17318  15147  13023  -2245  -3088   2362       C  
ATOM     21  CD1 ILE A  21      25.044  59.491  46.148  1.00126.01           C  
ANISOU   21  CD1 ILE A  21    18211  15591  14076  -2398  -3343   2751       C  
ATOM     22  N   GLU A  22      27.106  54.587  44.798  1.00107.27           N  
ANISOU   22  N   GLU A  22    15741  14307  10710  -2739  -2236   1712       N  
ATOM     23  CA  GLU A  22      27.385  53.154  44.824  1.00115.30           C  
ANISOU   23  CA  GLU A  22    16655  15508  11646  -2689  -1987   1370       C  
ATOM     24  C   GLU A  22      28.276  52.788  46.004  1.00113.32           C  
ANISOU   24  C   GLU A  22    16244  15149  11662  -2451  -1802   1093       C  
ATOM     25  O   GLU A  22      27.926  51.929  46.822  1.00108.83           O  
ANISOU   25  O   GLU A  22    15577  14515  11258  -2185  -1767    909       O  
ATOM     26  CB  GLU A  22      28.048  52.712  43.520  1.00117.71           C  
ANISOU   26  CB  GLU A  22    17041  16123  11561  -3071  -1791   1283       C  
ATOM     27  CG  GLU A  22      28.584  51.290  43.605  1.00119.06           C  
ANISOU   27  CG  GLU A  22    17062  16456  11719  -3019  -1505    877       C  
ATOM     28  CD  GLU A  22      29.108  50.765  42.287  1.00126.92           C  
ANISOU   28  CD  GLU A  22    18134  17765  12325  -3393  -1286    742       C  
ATOM     29  OE1 GLU A  22      28.360  50.796  41.288  1.00129.84           O  
ANISOU   29  OE1 GLU A  22    18689  18268  12374  -3604  -1423    914       O  
ATOM     30  OE2 GLU A  22      30.270  50.308  42.255  1.00126.67           O1-
ANISOU   30  OE2 GLU A  22    17975  17835  12318  -3479   -978    448       O1-
ATOM     31  N   GLU A  23      29.452  53.423  46.092  1.00117.86           N  
ANISOU   31  N   GLU A  23    16798  15694  12289  -2561  -1696   1068       N  
ATOM     32  CA  GLU A  23      30.396  53.122  47.166  1.00109.42           C  
ANISOU   32  CA  GLU A  23    15584  14499  11490  -2361  -1567    810       C  
ATOM     33  C   GLU A  23      29.745  53.247  48.535  1.00105.13           C  
ANISOU   33  C   GLU A  23    15032  13692  11223  -1986  -1729    824       C  
ATOM     34  O   GLU A  23      29.951  52.396  49.408  1.00108.46           O  
ANISOU   34  O   GLU A  23    15368  14050  11792  -1772  -1656    588       O  
ATOM     35  CB  GLU A  23      31.608  54.051  47.077  1.00107.48           C  
ANISOU   35  CB  GLU A  23    15320  14201  11316  -2530  -1499    847       C  
ATOM     36  CG  GLU A  23      32.405  53.939  45.796  1.00121.40           C  
ANISOU   36  CG  GLU A  23    17087  16224  12815  -2925  -1264    799       C  
ATOM     37  CD  GLU A  23      33.466  55.013  45.693  1.00127.47           C  
ANISOU   37  CD  GLU A  23    17841  16914  13678  -3108  -1212    896       C  
ATOM     38  OE1 GLU A  23      33.606  55.803  46.651  1.00119.10           O  
ANISOU   38  OE1 GLU A  23    16760  15588  12907  -2906  -1383    981       O  
ATOM     39  OE2 GLU A  23      34.145  55.081  44.648  1.00141.67           O1-
ANISOU   39  OE2 GLU A  23    19657  18914  15258  -3465   -992    884       O1-
ATOM     40  N   GLN A  24      28.960  54.309  48.742  1.00 94.70           N  
ANISOU   40  N   GLN A  24    13803  12201   9978  -1914  -1950   1094       N  
ATOM     41  CA  GLN A  24      28.206  54.449  49.984  1.00 98.24           C  
ANISOU   41  CA  GLN A  24    14253  12408  10666  -1577  -2068   1093       C  
ATOM     42  C   GLN A  24      27.326  53.232  50.234  1.00 99.25           C  
ANISOU   42  C   GLN A  24    14339  12597  10775  -1417  -2011    963       C  
ATOM     43  O   GLN A  24      27.267  52.719  51.357  1.00101.13           O  
ANISOU   43  O   GLN A  24    14552  12712  11161  -1169  -1963    802       O  
ATOM     44  CB  GLN A  24      27.348  55.713  49.936  1.00 91.87           C  
ANISOU   44  CB  GLN A  24    13521  11425   9961  -1556  -2307   1389       C  
ATOM     45  CG  GLN A  24      28.120  57.016  49.927  1.00 96.48           C  
ANISOU   45  CG  GLN A  24    14144  11877  10637  -1662  -2403   1533       C  
ATOM     46  CD  GLN A  24      27.246  58.182  49.520  1.00103.48           C  
ANISOU   46  CD  GLN A  24    15095  12620  11603  -1716  -2668   1855       C  
ATOM     47  OE1 GLN A  24      26.023  58.127  49.649  1.00105.72           O  
ANISOU   47  OE1 GLN A  24    15369  12818  11980  -1577  -2791   1930       O  
ATOM     48  NE2 GLN A  24      27.865  59.237  49.004  1.00117.78           N  
ANISOU   48  NE2 GLN A  24    16956  14386  13408  -1930  -2767   2049       N  
ATOM     49  N   ALA A  25      26.636  52.757  49.192  1.00 91.43           N  
ANISOU   49  N   ALA A  25    13355  11788   9597  -1572  -2029   1038       N  
ATOM     50  CA  ALA A  25      25.745  51.611  49.342  1.00 93.47           C  
ANISOU   50  CA  ALA A  25    13557  12096   9861  -1438  -1992    930       C  
ATOM     51  C   ALA A  25      26.525  50.326  49.592  1.00 89.06           C  
ANISOU   51  C   ALA A  25    12910  11652   9277  -1407  -1788    620       C  
ATOM     52  O   ALA A  25      26.094  49.483  50.386  1.00 96.48           O  
ANISOU   52  O   ALA A  25    13800  12520  10337  -1195  -1747    493       O  
ATOM     53  CB  ALA A  25      24.859  51.469  48.104  1.00 95.41           C  
ANISOU   53  CB  ALA A  25    13839  12492   9921  -1629  -2107   1088       C  
ATOM     54  N   LYS A  26      27.657  50.146  48.903  1.00 86.24           N  
ANISOU   54  N   LYS A  26    12522  11460   8785  -1628  -1654    494       N  
ATOM     55  CA  LYS A  26      28.581  49.067  49.243  1.00 86.40           C  
ANISOU   55  CA  LYS A  26    12422  11530   8878  -1588  -1480    178       C  
ATOM     56  C   LYS A  26      28.877  49.064  50.738  1.00103.22           C  
ANISOU   56  C   LYS A  26    14540  13411  11267  -1307  -1519     92       C  
ATOM     57  O   LYS A  26      28.691  48.055  51.426  1.00103.93           O  
ANISOU   57  O   LYS A  26    14584  13447  11458  -1136  -1493    -63       O  
ATOM     58  CB  LYS A  26      29.883  49.215  48.450  1.00 88.98           C  
ANISOU   58  CB  LYS A  26    12695  12003   9110  -1856  -1319     58       C  
ATOM     59  CG  LYS A  26      29.808  48.856  46.978  1.00 92.25           C  
ANISOU   59  CG  LYS A  26    13131  12704   9215  -2165  -1207     40       C  
ATOM     60  CD  LYS A  26      31.211  48.801  46.390  1.00 95.26           C  
ANISOU   60  CD  LYS A  26    13421  13217   9558  -2408   -966   -166       C  
ATOM     61  CE  LYS A  26      31.273  47.941  45.141  1.00116.49           C  
ANISOU   61  CE  LYS A  26    16094  16197  11971  -2670   -773   -346       C  
ATOM     62  NZ  LYS A  26      32.680  47.613  44.778  1.00120.82           N  
ANISOU   62  NZ  LYS A  26    16484  16844  12580  -2854   -478   -653       N  
ATOM     63  N   THR A  27      29.339  50.207  51.250  1.00111.02           N  
ANISOU   63  N   THR A  27    15590  14236  12355  -1272  -1599    200       N  
ATOM     64  CA  THR A  27      29.593  50.352  52.680  1.00 93.67           C  
ANISOU   64  CA  THR A  27    13435  11789  10364  -1020  -1668    134       C  
ATOM     65  C   THR A  27      28.326  50.104  53.491  1.00 97.86           C  
ANISOU   65  C   THR A  27    14045  12206  10932   -788  -1725    201       C  
ATOM     66  O   THR A  27      28.342  49.350  54.471  1.00 91.21           O  
ANISOU   66  O   THR A  27    13223  11259  10174   -611  -1707     64       O  
ATOM     67  CB  THR A  27      30.149  51.746  52.966  1.00 88.58           C  
ANISOU   67  CB  THR A  27    12856  10990   9811  -1037  -1768    260       C  
ATOM     68  OG1 THR A  27      31.467  51.858  52.416  1.00 89.91           O  
ANISOU   68  OG1 THR A  27    12927  11231  10005  -1237  -1685    156       O  
ATOM     69  CG2 THR A  27      30.206  51.999  54.459  1.00 93.21           C  
ANISOU   69  CG2 THR A  27    13537  11309  10569   -774  -1869    208       C  
ATOM     70  N   PHE A  28      27.218  50.743  53.100  1.00102.03           N  
ANISOU   70  N   PHE A  28    14616  12735  11417   -796  -1797    416       N  
ATOM     71  CA  PHE A  28      25.933  50.475  53.740  1.00102.25           C  
ANISOU   71  CA  PHE A  28    14674  12662  11516   -599  -1810    466       C  
ATOM     72  C   PHE A  28      25.644  48.982  53.785  1.00 97.15           C  
ANISOU   72  C   PHE A  28    13958  12116  10838   -555  -1707    311       C  
ATOM     73  O   PHE A  28      25.361  48.419  54.848  1.00 97.95           O  
ANISOU   73  O   PHE A  28    14102  12094  11021   -368  -1662    227       O  
ATOM     74  CB  PHE A  28      24.810  51.204  52.998  1.00102.36           C  
ANISOU   74  CB  PHE A  28    14681  12683  11529   -662  -1920    701       C  
ATOM     75  CG  PHE A  28      23.439  50.652  53.286  1.00 99.68           C  
ANISOU   75  CG  PHE A  28    14299  12292  11281   -516  -1904    727       C  
ATOM     76  CD1 PHE A  28      22.750  51.035  54.423  1.00 98.02           C  
ANISOU   76  CD1 PHE A  28    14130  11863  11251   -292  -1882    735       C  
ATOM     77  CD2 PHE A  28      22.845  49.742  52.423  1.00 96.24           C  
ANISOU   77  CD2 PHE A  28    13781  12023  10763   -612  -1896    725       C  
ATOM     78  CE1 PHE A  28      21.494  50.524  54.694  1.00 91.46           C  
ANISOU   78  CE1 PHE A  28    13236  10977  10539   -171  -1828    747       C  
ATOM     79  CE2 PHE A  28      21.592  49.226  52.692  1.00 93.19           C  
ANISOU   79  CE2 PHE A  28    13329  11570  10507   -482  -1883    748       C  
ATOM     80  CZ  PHE A  28      20.915  49.619  53.827  1.00 92.80           C  
ANISOU   80  CZ  PHE A  28    13300  11300  10661   -264  -1837    762       C  
ATOM     81  N   LEU A  29      25.713  48.326  52.625  1.00 94.20           N  
ANISOU   81  N   LEU A  29    13493  11962  10336   -741  -1670    271       N  
ATOM     82  CA  LEU A  29      25.452  46.894  52.553  1.00 96.08           C  
ANISOU   82  CA  LEU A  29    13646  12294  10569   -714  -1590    113       C  
ATOM     83  C   LEU A  29      26.450  46.100  53.381  1.00 88.60           C  
ANISOU   83  C   LEU A  29    12675  11275   9714   -627  -1529   -112       C  
ATOM     84  O   LEU A  29      26.106  45.044  53.925  1.00 78.96           O  
ANISOU   84  O   LEU A  29    11427  10012   8563   -511  -1498   -209       O  
ATOM     85  CB  LEU A  29      25.492  46.439  51.096  1.00 93.85           C  
ANISOU   85  CB  LEU A  29    13286  12261  10112   -953  -1564     80       C  
ATOM     86  CG  LEU A  29      24.181  46.506  50.316  1.00 82.52           C  
ANISOU   86  CG  LEU A  29    11854  10892   8607  -1010  -1662    255       C  
ATOM     87  CD1 LEU A  29      24.324  45.714  49.042  1.00 94.72           C  
ANISOU   87  CD1 LEU A  29    13347  12684   9956  -1232  -1623    146       C  
ATOM     88  CD2 LEU A  29      23.022  45.977  51.145  1.00 82.15           C  
ANISOU   88  CD2 LEU A  29    11772  10701   8742   -784  -1673    282       C  
ATOM     89  N   ASP A  30      27.688  46.588  53.485  1.00 99.73           N  
ANISOU   89  N   ASP A  30    14088  12650  11153   -688  -1533   -189       N  
ATOM     90  CA  ASP A  30      28.705  45.882  54.258  1.00 99.79           C  
ANISOU   90  CA  ASP A  30    14061  12552  11302   -612  -1530   -402       C  
ATOM     91  C   ASP A  30      28.323  45.816  55.731  1.00 89.62           C  
ANISOU   91  C   ASP A  30    12923  11032  10098   -377  -1602   -369       C  
ATOM     92  O   ASP A  30      28.417  44.758  56.364  1.00 83.25           O  
ANISOU   92  O   ASP A  30    12112  10152   9367   -287  -1613   -491       O  
ATOM     93  CB  ASP A  30      30.059  46.567  54.078  1.00 95.42           C  
ANISOU   93  CB  ASP A  30    13467  11977  10813   -726  -1538   -475       C  
ATOM     94  CG  ASP A  30      31.219  45.617  54.261  1.00104.63           C  
ANISOU   94  CG  ASP A  30    14493  13106  12157   -740  -1518   -748       C  
ATOM     95  OD1 ASP A  30      30.971  44.414  54.484  1.00102.51           O  
ANISOU   95  OD1 ASP A  30    14168  12835  11948   -668  -1513   -872       O  
ATOM     96  OD2 ASP A  30      32.379  46.074  54.181  1.00107.37           O1-
ANISOU   96  OD2 ASP A  30    14768  13405  12624   -825  -1519   -839       O1-
ATOM     97  N   LYS A  31      27.886  46.946  56.291  1.00 87.91           N  
ANISOU   97  N   LYS A  31    12850  10689   9863   -287  -1652   -208       N  
ATOM     98  CA  LYS A  31      27.401  46.965  57.668  1.00 94.24           C  
ANISOU   98  CA  LYS A  31    13828  11284  10693    -84  -1678   -183       C  
ATOM     99  C   LYS A  31      26.183  46.065  57.834  1.00 91.75           C  
ANISOU   99  C   LYS A  31    13505  10999  10356     -8  -1587   -151       C  
ATOM    100  O   LYS A  31      26.081  45.313  58.810  1.00103.99           O  
ANISOU  100  O   LYS A  31    15156  12434  11921    102  -1576   -210       O  
ATOM    101  CB  LYS A  31      27.075  48.403  58.079  1.00 99.90           C  
ANISOU  101  CB  LYS A  31    14672  11874  11410    -18  -1721    -42       C  
ATOM    102  CG  LYS A  31      26.084  48.532  59.230  1.00100.10           C  
ANISOU  102  CG  LYS A  31    14866  11737  11430    167  -1670      4       C  
ATOM    103  CD  LYS A  31      26.698  48.204  60.580  1.00 83.73           C  
ANISOU  103  CD  LYS A  31    12997   9482   9336    280  -1721   -110       C  
ATOM    104  CE  LYS A  31      25.763  48.627  61.705  1.00105.25           C  
ANISOU  104  CE  LYS A  31    15929  12048  12013    434  -1635    -69       C  
ATOM    105  NZ  LYS A  31      26.331  48.359  63.055  1.00130.84           N  
ANISOU  105  NZ  LYS A  31    19436  15107  15168    521  -1701   -165       N  
ATOM    106  N   PHE A  32      25.247  46.129  56.881  1.00 86.46           N  
ANISOU  106  N   PHE A  32    12724  10469   9658    -78  -1538    -46       N  
ATOM    107  CA  PHE A  32      24.020  45.341  56.971  1.00 92.74           C  
ANISOU  107  CA  PHE A  32    13478  11278  10482    -11  -1457     -8       C  
ATOM    108  C   PHE A  32      24.315  43.853  57.111  1.00 95.81           C  
ANISOU  108  C   PHE A  32    13808  11701  10895    -12  -1433   -157       C  
ATOM    109  O   PHE A  32      23.745  43.177  57.973  1.00102.84           O  
ANISOU  109  O   PHE A  32    14766  12486  11823     98  -1378   -156       O  
ATOM    110  CB  PHE A  32      23.139  45.599  55.744  1.00 98.33           C  
ANISOU  110  CB  PHE A  32    14054  12128  11180   -116  -1472    113       C  
ATOM    111  CG  PHE A  32      21.998  44.625  55.600  1.00 89.03           C  
ANISOU  111  CG  PHE A  32    12779  10982  10069    -79  -1414    126       C  
ATOM    112  CD1 PHE A  32      20.782  44.857  56.226  1.00 90.58           C  
ANISOU  112  CD1 PHE A  32    12990  11041  10386     52  -1347    228       C  
ATOM    113  CD2 PHE A  32      22.138  43.481  54.830  1.00 86.74           C  
ANISOU  113  CD2 PHE A  32    12363  10846   9750   -179  -1416     18       C  
ATOM    114  CE1 PHE A  32      19.737  43.956  56.095  1.00 91.35           C  
ANISOU  114  CE1 PHE A  32    12972  11149  10587     80  -1290    240       C  
ATOM    115  CE2 PHE A  32      21.100  42.581  54.694  1.00 89.01           C  
ANISOU  115  CE2 PHE A  32    12550  11145  10125   -146  -1382     28       C  
ATOM    116  CZ  PHE A  32      19.897  42.818  55.326  1.00 89.32           C  
ANISOU  116  CZ  PHE A  32    12599  11042  10298    -18  -1323    150       C  
ATOM    117  N   ASN A  33      25.207  43.326  56.266  1.00 93.45           N  
ANISOU  117  N   ASN A  33    13378  11540  10589   -146  -1465   -292       N  
ATOM    118  CA  ASN A  33      25.432  41.882  56.217  1.00 96.57           C  
ANISOU  118  CA  ASN A  33    13668  11967  11058   -158  -1458   -452       C  
ATOM    119  C   ASN A  33      25.876  41.335  57.570  1.00 98.89           C  
ANISOU  119  C   ASN A  33    14091  12051  11431    -31  -1512   -511       C  
ATOM    120  O   ASN A  33      25.346  40.324  58.046  1.00100.86           O  
ANISOU  120  O   ASN A  33    14348  12239  11735     31  -1497   -519       O  
ATOM    121  CB  ASN A  33      26.465  41.546  55.142  1.00 96.33           C  
ANISOU  121  CB  ASN A  33    13470  12097  11032   -327  -1460   -633       C  
ATOM    122  CG  ASN A  33      25.989  41.895  53.750  1.00 90.42           C  
ANISOU  122  CG  ASN A  33    12636  11572  10148   -490  -1413   -576       C  
ATOM    123  OD1 ASN A  33      24.822  41.693  53.415  1.00118.96           O  
ANISOU  123  OD1 ASN A  33    16232  15237  13729   -478  -1408   -469       O  
ATOM    124  ND2 ASN A  33      26.893  42.411  52.926  1.00 92.40           N  
ANISOU  124  ND2 ASN A  33    12838  11947  10321   -658  -1386   -644       N  
ATOM    125  N   HIS A  34      26.851  41.991  58.204  1.00 93.93           N  
ANISOU  125  N   HIS A  34    13581  11297  10812     -2  -1598   -542       N  
ATOM    126  CA  HIS A  34      27.395  41.469  59.454  1.00102.71           C  
ANISOU  126  CA  HIS A  34    14846  12193  11984     94  -1710   -597       C  
ATOM    127  C   HIS A  34      26.362  41.513  60.575  1.00 94.33           C  
ANISOU  127  C   HIS A  34    14019  11001  10821    219  -1649   -454       C  
ATOM    128  O   HIS A  34      26.225  40.546  61.335  1.00 95.80           O  
ANISOU  128  O   HIS A  34    14299  11074  11028    264  -1682   -463       O  
ATOM    129  CB  HIS A  34      28.655  42.242  59.840  1.00103.85           C  
ANISOU  129  CB  HIS A  34    15064  12217  12176     91  -1847   -662       C  
ATOM    130  CG  HIS A  34      29.774  42.092  58.857  1.00119.43           C  
ANISOU  130  CG  HIS A  34    16794  14290  14292    -42  -1874   -835       C  
ATOM    131  ND1 HIS A  34      29.990  42.987  57.832  1.00128.03           N  
ANISOU  131  ND1 HIS A  34    17771  15542  15331   -164  -1789   -817       N  
ATOM    132  CD2 HIS A  34      30.728  41.139  58.731  1.00116.70           C  
ANISOU  132  CD2 HIS A  34    16287  13898  14156    -85  -1961  -1038       C  
ATOM    133  CE1 HIS A  34      31.036  42.599  57.124  1.00126.21           C  
ANISOU  133  CE1 HIS A  34    17331  15377  15246   -285  -1783  -1011       C  
ATOM    134  NE2 HIS A  34      31.502  41.480  57.649  1.00123.77           N  
ANISOU  134  NE2 HIS A  34    16969  14938  15122   -231  -1886  -1164       N  
ATOM    135  N   GLU A  35      25.622  42.619  60.693  1.00 84.37           N  
ANISOU  135  N   GLU A  35    12850   9742   9464    264  -1551   -325       N  
ATOM    136  CA  GLU A  35      24.551  42.675  61.683  1.00 87.78           C  
ANISOU  136  CA  GLU A  35    13472  10063   9817    369  -1426   -221       C  
ATOM    137  C   GLU A  35      23.422  41.703  61.355  1.00 86.01           C  
ANISOU  137  C   GLU A  35    13116   9916   9649    362  -1294   -175       C  
ATOM    138  O   GLU A  35      22.809  41.139  62.269  1.00 88.74           O  
ANISOU  138  O   GLU A  35    13602  10153   9960    419  -1201   -130       O  
ATOM    139  CB  GLU A  35      24.005  44.102  61.793  1.00 83.70           C  
ANISOU  139  CB  GLU A  35    13030   9517   9256    422  -1346   -129       C  
ATOM    140  CG  GLU A  35      22.954  44.273  62.883  1.00 90.52           C  
ANISOU  140  CG  GLU A  35    14088  10250  10055    527  -1172    -66       C  
ATOM    141  CD  GLU A  35      23.329  45.324  63.904  1.00119.41           C  
ANISOU  141  CD  GLU A  35    18017  13745  13609    602  -1197    -86       C  
ATOM    142  OE1 GLU A  35      24.281  46.088  63.647  1.00129.94           O  
ANISOU  142  OE1 GLU A  35    19348  15067  14958    580  -1359   -120       O  
ATOM    143  OE2 GLU A  35      22.670  45.386  64.965  1.00135.92           O1-
ANISOU  143  OE2 GLU A  35    20326  15716  15602    674  -1042    -76       O1-
ATOM    144  N   ALA A  36      23.143  41.484  60.067  1.00 94.25           N  
ANISOU  144  N   ALA A  36    13901  11138  10769    280  -1286   -184       N  
ATOM    145  CA  ALA A  36      22.013  40.643  59.683  1.00 86.20           C  
ANISOU  145  CA  ALA A  36    12738  10181   9833    274  -1186   -140       C  
ATOM    146  C   ALA A  36      22.242  39.181  60.049  1.00100.26           C  
ANISOU  146  C   ALA A  36    14506  11913  11676    267  -1224   -217       C  
ATOM    147  O   ALA A  36      21.313  38.501  60.498  1.00103.59           O  
ANISOU  147  O   ALA A  36    14939  12274  12148    304  -1119   -150       O  
ATOM    148  CB  ALA A  36      21.741  40.773  58.184  1.00 87.57           C  
ANISOU  148  CB  ALA A  36    12675  10551  10046    170  -1216   -140       C  
ATOM    149  N   GLU A  37      23.466  38.679  59.856  1.00111.49           N  
ANISOU  149  N   GLU A  37    15885  13341  13134    214  -1377   -359       N  
ATOM    150  CA  GLU A  37      23.734  37.261  60.084  1.00105.48           C  
ANISOU  150  CA  GLU A  37    15070  12514  12493    201  -1458   -445       C  
ATOM    151  C   GLU A  37      23.436  36.860  61.524  1.00 95.37           C  
ANISOU  151  C   GLU A  37    14051  11024  11162    274  -1448   -342       C  
ATOM    152  O   GLU A  37      22.803  35.827  61.773  1.00 95.78           O  
ANISOU  152  O   GLU A  37    14078  11024  11289    273  -1411   -300       O  
ATOM    153  CB  GLU A  37      25.184  36.929  59.731  1.00 95.66           C  
ANISOU  153  CB  GLU A  37    13725  11268  11353    142  -1632   -638       C  
ATOM    154  CG  GLU A  37      25.395  36.541  58.282  1.00 91.60           C  
ANISOU  154  CG  GLU A  37    12916  10959  10929     33  -1615   -795       C  
ATOM    155  CD  GLU A  37      26.811  36.082  58.007  1.00111.45           C  
ANISOU  155  CD  GLU A  37    15295  13444  13605    -27  -1744  -1027       C  
ATOM    156  OE1 GLU A  37      27.699  36.945  57.845  1.00122.15           O  
ANISOU  156  OE1 GLU A  37    16660  14817  14933    -64  -1767  -1082       O  
ATOM    157  OE2 GLU A  37      27.034  34.854  57.953  1.00111.33           O1-
ANISOU  157  OE2 GLU A  37    15144  13372  13786    -37  -1825  -1163       O1-
ATOM    158  N   ASP A  38      23.889  37.665  62.488  1.00 86.51           N  
ANISOU  158  N   ASP A  38    13199   9772   9898    323  -1484   -300       N  
ATOM    159  CA  ASP A  38      23.649  37.342  63.892  1.00106.30           C  
ANISOU  159  CA  ASP A  38    16020  12083  12286    364  -1473   -202       C  
ATOM    160  C   ASP A  38      22.161  37.372  64.218  1.00 98.00           C  
ANISOU  160  C   ASP A  38    15017  11044  11174    393  -1194    -67       C  
ATOM    161  O   ASP A  38      21.633  36.449  64.851  1.00 99.91           O  
ANISOU  161  O   ASP A  38    15354  11194  11415    376  -1133      8       O  
ATOM    162  CB  ASP A  38      24.414  38.309  64.795  1.00 98.80           C  
ANISOU  162  CB  ASP A  38    15368  11000  11173    403  -1573   -202       C  
ATOM    163  CG  ASP A  38      24.104  38.097  66.261  1.00102.48           C  
ANISOU  163  CG  ASP A  38    16224  11277  11438    423  -1542    -98       C  
ATOM    164  OD1 ASP A  38      24.283  36.958  66.745  1.00104.67           O  
ANISOU  164  OD1 ASP A  38    16586  11437  11746    381  -1668    -69       O  
ATOM    165  OD2 ASP A  38      23.668  39.060  66.926  1.00104.12           O1-
ANISOU  165  OD2 ASP A  38    16660  11444  11455    468  -1389    -49       O1-
ATOM    166  N   LEU A  39      21.465  38.433  63.795  1.00 84.19           N  
ANISOU  166  N   LEU A  39    13191   9390   9408    428  -1026    -32       N  
ATOM    167  CA  LEU A  39      20.040  38.550  64.090  1.00 85.25           C  
ANISOU  167  CA  LEU A  39    13324   9510   9556    462   -750     70       C  
ATOM    168  C   LEU A  39      19.244  37.421  63.448  1.00 93.87           C  
ANISOU  168  C   LEU A  39    14160  10667  10841    422   -696     97       C  
ATOM    169  O   LEU A  39      18.285  36.914  64.043  1.00 89.79           O  
ANISOU  169  O   LEU A  39    13689  10073  10356    425   -502    181       O  
ATOM    170  CB  LEU A  39      19.517  39.908  63.624  1.00 85.43           C  
ANISOU  170  CB  LEU A  39    13256   9596   9606    509   -642     87       C  
ATOM    171  CG  LEU A  39      19.740  41.056  64.610  1.00 95.16           C  
ANISOU  171  CG  LEU A  39    14777  10710  10668    572   -579     82       C  
ATOM    172  CD1 LEU A  39      20.065  42.342  63.873  1.00104.45           C  
ANISOU  172  CD1 LEU A  39    15844  11953  11889    592   -669     60       C  
ATOM    173  CD2 LEU A  39      18.527  41.239  65.512  1.00 96.89           C  
ANISOU  173  CD2 LEU A  39    15122  10829  10865    619   -263    133       C  
ATOM    174  N   PHE A  40      19.624  37.017  62.232  1.00 82.86           N  
ANISOU  174  N   PHE A  40    12496   9410   9577    373   -854     15       N  
ATOM    175  CA  PHE A  40      18.988  35.863  61.606  1.00 86.93           C  
ANISOU  175  CA  PHE A  40    12774   9974  10281    332   -849     12       C  
ATOM    176  C   PHE A  40      19.247  34.590  62.401  1.00 91.14           C  
ANISOU  176  C   PHE A  40    13419  10371  10841    308   -909     23       C  
ATOM    177  O   PHE A  40      18.343  33.764  62.577  1.00 93.52           O  
ANISOU  177  O   PHE A  40    13651  10620  11262    294   -800     98       O  
ATOM    178  CB  PHE A  40      19.482  35.698  60.167  1.00 92.75           C  
ANISOU  178  CB  PHE A  40    13247  10890  11106    268  -1011   -113       C  
ATOM    179  CG  PHE A  40      18.820  34.570  59.428  1.00 94.33           C  
ANISOU  179  CG  PHE A  40    13199  11144  11497    224  -1027   -143       C  
ATOM    180  CD1 PHE A  40      17.443  34.428  59.447  1.00 86.56           C  
ANISOU  180  CD1 PHE A  40    12120  10128  10642    248   -876    -29       C  
ATOM    181  CD2 PHE A  40      19.575  33.640  58.732  1.00 91.80           C  
ANISOU  181  CD2 PHE A  40    12726  10889  11265    160  -1192   -305       C  
ATOM    182  CE1 PHE A  40      16.831  33.386  58.779  1.00 88.29           C  
ANISOU  182  CE1 PHE A  40    12108  10378  11061    209   -916    -58       C  
ATOM    183  CE2 PHE A  40      18.968  32.595  58.061  1.00 86.71           C  
ANISOU  183  CE2 PHE A  40    11859  10283  10804    122  -1221   -353       C  
ATOM    184  CZ  PHE A  40      17.595  32.469  58.085  1.00 90.60           C  
ANISOU  184  CZ  PHE A  40    12271  10741  11410    147  -1096   -220       C  
ATOM    185  N   TYR A  41      20.479  34.412  62.887  1.00100.83           N  
ANISOU  185  N   TYR A  41    14808  11514  11988    296  -1106    -43       N  
ATOM    186  CA  TYR A  41      20.806  33.230  63.679  1.00101.62           C  
ANISOU  186  CA  TYR A  41    15038  11446  12128    263  -1228    -14       C  
ATOM    187  C   TYR A  41      19.906  33.117  64.903  1.00104.75           C  
ANISOU  187  C   TYR A  41    15709  11705  12388    262  -1021    165       C  
ATOM    188  O   TYR A  41      19.317  32.060  65.157  1.00119.87           O  
ANISOU  188  O   TYR A  41    17595  13542  14409    218   -978    247       O  
ATOM    189  CB  TYR A  41      22.275  33.269  64.102  1.00 87.56           C  
ANISOU  189  CB  TYR A  41    13412   9557  10301    257  -1502   -103       C  
ATOM    190  CG  TYR A  41      22.850  31.904  64.399  1.00 88.02           C  
ANISOU  190  CG  TYR A  41    13458   9456  10530    212  -1744   -133       C  
ATOM    191  CD1 TYR A  41      22.654  31.304  65.637  1.00 94.36           C  
ANISOU  191  CD1 TYR A  41    14565  10050  11236    182  -1784     26       C  
ATOM    192  CD2 TYR A  41      23.593  31.220  63.449  1.00 87.42           C  
ANISOU  192  CD2 TYR A  41    13072   9424  10718    187  -1934   -326       C  
ATOM    193  CE1 TYR A  41      23.175  30.055  65.916  1.00 89.71           C  
ANISOU  193  CE1 TYR A  41    13968   9283  10834    133  -2051     22       C  
ATOM    194  CE2 TYR A  41      24.122  29.974  63.719  1.00 93.26           C  
ANISOU  194  CE2 TYR A  41    13770   9985  11678    153  -2178   -369       C  
ATOM    195  CZ  TYR A  41      23.910  29.396  64.953  1.00 96.07           C  
ANISOU  195  CZ  TYR A  41    14426  10116  11959    129  -2259   -182       C  
ATOM    196  OH  TYR A  41      24.437  28.153  65.216  1.00 90.55           O  
ANISOU  196  OH  TYR A  41    13685   9209  11510     88  -2547   -204       O  
ATOM    197  N   GLN A  42      19.797  34.201  65.679  1.00 89.70           N  
ANISOU  197  N   GLN A  42    14074   9761  10246    300   -878    219       N  
ATOM    198  CA  GLN A  42      18.957  34.189  66.873  1.00103.01           C  
ANISOU  198  CA  GLN A  42    16051  11328  11761    281   -624    360       C  
ATOM    199  C   GLN A  42      17.534  33.754  66.552  1.00107.82           C  
ANISOU  199  C   GLN A  42    16431  11979  12555    269   -342    433       C  
ATOM    200  O   GLN A  42      16.921  32.994  67.312  1.00109.62           O  
ANISOU  200  O   GLN A  42    16794  12097  12760    205   -193    551       O  
ATOM    201  CB  GLN A  42      18.958  35.573  67.525  1.00106.83           C  
ANISOU  201  CB  GLN A  42    16792  11795  12002    334   -475    350       C  
ATOM    202  CG  GLN A  42      20.336  36.068  67.925  1.00 94.49           C  
ANISOU  202  CG  GLN A  42    15470  10163  10270    347   -762    281       C  
ATOM    203  CD  GLN A  42      20.893  35.330  69.128  1.00108.38           C  
ANISOU  203  CD  GLN A  42    17620  11724  11835    275   -926    360       C  
ATOM    204  OE1 GLN A  42      20.166  34.631  69.835  1.00113.27           O  
ANISOU  204  OE1 GLN A  42    18408  12263  12367    206   -759    486       O  
ATOM    205  NE2 GLN A  42      22.192  35.475  69.360  1.00112.56           N  
ANISOU  205  NE2 GLN A  42    18298  12160  12311    278  -1269    297       N  
ATOM    206  N   SER A  43      16.993  34.220  65.426  1.00101.31           N  
ANISOU  206  N   SER A  43    15264  11300  11928    316   -282    374       N  
ATOM    207  CA  SER A  43      15.668  33.777  65.005  1.00106.76           C  
ANISOU  207  CA  SER A  43    15689  12011  12862    308    -75    432       C  
ATOM    208  C   SER A  43      15.680  32.305  64.611  1.00105.06           C  
ANISOU  208  C   SER A  43    15299  11775  12845    245   -228    442       C  
ATOM    209  O   SER A  43      14.834  31.526  65.066  1.00111.95           O  
ANISOU  209  O   SER A  43    16159  12552  13824    198    -62    548       O  
ATOM    210  CB  SER A  43      15.171  34.641  63.847  1.00107.57           C  
ANISOU  210  CB  SER A  43    15488  12252  13131    363    -59    374       C  
ATOM    211  OG  SER A  43      14.077  34.021  63.196  1.00113.61           O  
ANISOU  211  OG  SER A  43    15943  13032  14190    348     20    408       O  
ATOM    212  N   SER A  44      16.637  31.907  63.768  1.00 92.58           N  
ANISOU  212  N   SER A  44    13571  10272  11333    236   -533    320       N  
ATOM    213  CA  SER A  44      16.710  30.521  63.309  1.00 95.66           C  
ANISOU  213  CA  SER A  44    13763  10634  11948    184   -702    287       C  
ATOM    214  C   SER A  44      16.851  29.553  64.477  1.00104.77           C  
ANISOU  214  C   SER A  44    15163  11585  13058    123   -731    408       C  
ATOM    215  O   SER A  44      16.118  28.562  64.569  1.00109.48           O  
ANISOU  215  O   SER A  44    15656  12102  13841     74   -670    493       O  
ATOM    216  CB  SER A  44      17.875  30.356  62.331  1.00 92.38           C  
ANISOU  216  CB  SER A  44    13184  10323  11593    180   -996     92       C  
ATOM    217  OG  SER A  44      17.802  31.305  61.281  1.00103.60           O  
ANISOU  217  OG  SER A  44    14437  11933  12994    205   -972      6       O  
ATOM    218  N   LEU A  45      17.790  29.830  65.385  1.00116.10           N  
ANISOU  218  N   LEU A  45    16938  12920  14253    114   -846    429       N  
ATOM    219  CA  LEU A  45      18.025  28.939  66.517  1.00108.10           C  
ANISOU  219  CA  LEU A  45    16215  11695  13162     33   -937    566       C  
ATOM    220  C   LEU A  45      16.785  28.819  67.399  1.00108.73           C  
ANISOU  220  C   LEU A  45    16468  11697  13146    -26   -581    761       C  
ATOM    221  O   LEU A  45      16.388  27.712  67.784  1.00112.31           O  
ANISOU  221  O   LEU A  45    16943  12022  13710   -114   -583    888       O  
ATOM    222  CB  LEU A  45      19.221  29.438  67.327  1.00 92.45           C  
ANISOU  222  CB  LEU A  45    14595   9613  10920     34  -1147    555       C  
ATOM    223  CG  LEU A  45      19.701  28.507  68.438  1.00113.18           C  
ANISOU  223  CG  LEU A  45    17551  11992  13460    -64  -1363    696       C  
ATOM    224  CD1 LEU A  45      19.918  27.098  67.900  1.00109.61           C  
ANISOU  224  CD1 LEU A  45    16822  11453  13371   -104  -1624    666       C  
ATOM    225  CD2 LEU A  45      20.962  29.054  69.095  1.00136.95           C  
ANISOU  225  CD2 LEU A  45    20882  14893  16259    -55  -1643    659       C  
ATOM    226  N   ALA A  46      16.156  29.951  67.726  1.00 96.46           N  
ANISOU  226  N   ALA A  46    15028  10210  11413     14   -260    778       N  
ATOM    227  CA  ALA A  46      14.942  29.921  68.538  1.00 99.87           C  
ANISOU  227  CA  ALA A  46    15594  10573  11780    -48    147    924       C  
ATOM    228  C   ALA A  46      13.808  29.208  67.809  1.00112.64           C  
ANISOU  228  C   ALA A  46    16805  12216  13776    -58    293    953       C  
ATOM    229  O   ALA A  46      13.166  28.309  68.364  1.00115.78           O  
ANISOU  229  O   ALA A  46    17254  12493  14245   -160    438   1098       O  
ATOM    230  CB  ALA A  46      14.529  31.343  68.920  1.00 99.46           C  
ANISOU  230  CB  ALA A  46    15682  10580  11529     14    457    879       C  
ATOM    231  N   SER A  47      13.544  29.602  66.559  1.00115.35           N  
ANISOU  231  N   SER A  47    16755  12706  14368     33    243    825       N  
ATOM    232  CA  SER A  47      12.557  28.899  65.748  1.00109.57           C  
ANISOU  232  CA  SER A  47    15623  11988  14020     26    298    833       C  
ATOM    233  C   SER A  47      12.920  27.434  65.551  1.00107.26           C  
ANISOU  233  C   SER A  47    15236  11613  13906    -44     31    858       C  
ATOM    234  O   SER A  47      12.032  26.615  65.290  1.00116.78           O  
ANISOU  234  O   SER A  47    16202  12761  15408    -84    109    918       O  
ATOM    235  CB  SER A  47      12.396  29.588  64.392  1.00108.92           C  
ANISOU  235  CB  SER A  47    15193  12074  14119    119    199    690       C  
ATOM    236  OG  SER A  47      12.094  30.964  64.556  1.00111.11           O  
ANISOU  236  OG  SER A  47    15543  12401  14275    185    403    671       O  
ATOM    237  N   TRP A  48      14.201  27.086  65.671  1.00 97.65           N  
ANISOU  237  N   TRP A  48    14179  10364  12558    -57   -297    805       N  
ATOM    238  CA  TRP A  48      14.577  25.680  65.655  1.00 97.35           C  
ANISOU  238  CA  TRP A  48    14077  10197  12715   -126   -561    831       C  
ATOM    239  C   TRP A  48      14.227  24.998  66.972  1.00106.73           C  
ANISOU  239  C   TRP A  48    15582  11176  13794   -250   -435   1069       C  
ATOM    240  O   TRP A  48      13.973  23.789  66.990  1.00110.60           O  
ANISOU  240  O   TRP A  48    15962  11535  14525   -326   -538   1153       O  
ATOM    241  CB  TRP A  48      16.072  25.534  65.350  1.00 97.66           C  
ANISOU  241  CB  TRP A  48    14148  10238  12720    -99   -960    676       C  
ATOM    242  CG  TRP A  48      16.660  24.265  65.863  1.00 94.46           C  
ANISOU  242  CG  TRP A  48    13836   9618  12437   -180  -1245    742       C  
ATOM    243  CD1 TRP A  48      17.136  24.020  67.120  1.00101.76           C  
ANISOU  243  CD1 TRP A  48    15172  10344  13148   -262  -1342    912       C  
ATOM    244  CD2 TRP A  48      16.798  23.042  65.136  1.00 93.59           C  
ANISOU  244  CD2 TRP A  48    13405   9446  12709   -196  -1496    644       C  
ATOM    245  NE1 TRP A  48      17.572  22.721  67.213  1.00 96.54           N  
ANISOU  245  NE1 TRP A  48    14456   9486  12737   -328  -1662    945       N  
ATOM    246  CE2 TRP A  48      17.378  22.101  66.006  1.00 93.91           C  
ANISOU  246  CE2 TRP A  48    13660   9233  12789   -282  -1752    768       C  
ATOM    247  CE3 TRP A  48      16.495  22.655  63.828  1.00 94.83           C  
ANISOU  247  CE3 TRP A  48    13127   9727  13176   -153  -1549    456       C  
ATOM    248  CZ2 TRP A  48      17.657  20.797  65.611  1.00 99.96           C  
ANISOU  248  CZ2 TRP A  48    14185   9854  13940   -312  -2051    702       C  
ATOM    249  CZ3 TRP A  48      16.774  21.361  63.437  1.00 96.08           C  
ANISOU  249  CZ3 TRP A  48    13062   9760  13684   -185  -1822    369       C  
ATOM    250  CH2 TRP A  48      17.350  20.447  64.325  1.00 98.81           C  
ANISOU  250  CH2 TRP A  48    13595   9842  14108   -257  -2068    488       C  
ATOM    251  N   ASN A  49      14.201  25.751  68.075  1.00114.65           N  
ANISOU  251  N   ASN A  49    16992  12142  14427   -285   -213   1178       N  
ATOM    252  CA  ASN A  49      13.830  25.167  69.361  1.00112.54           C  
ANISOU  252  CA  ASN A  49    17087  11690  13983   -437    -53   1416       C  
ATOM    253  C   ASN A  49      12.353  24.797  69.394  1.00118.01           C  
ANISOU  253  C   ASN A  49    17584  12359  14894   -499    348   1529       C  
ATOM    254  O   ASN A  49      11.996  23.679  69.786  1.00124.46           O  
ANISOU  254  O   ASN A  49    18426  13021  15842   -627    342   1697       O  
ATOM    255  CB  ASN A  49      14.171  26.123  70.504  1.00122.47           C  
ANISOU  255  CB  ASN A  49    18855  12927  14751   -470    101   1472       C  
ATOM    256  CG  ASN A  49      15.644  26.107  70.857  1.00111.02           C  
ANISOU  256  CG  ASN A  49    17697  11393  13095   -470   -346   1443       C  
ATOM    257  OD1 ASN A  49      16.462  25.553  70.125  1.00105.24           O  
ANISOU  257  OD1 ASN A  49    16731  10644  12613   -421   -746   1336       O  
ATOM    258  ND2 ASN A  49      15.987  26.706  71.991  1.00103.72           N  
ANISOU  258  ND2 ASN A  49    17279  10398  11730   -531   -283   1523       N  
ATOM    259  N   TYR A  50      11.475  25.723  68.994  1.00120.34           N  
ANISOU  259  N   TYR A  50    17671  12784  15268   -416    687   1442       N  
ATOM    260  CA  TYR A  50      10.049  25.411  68.971  1.00125.41           C  
ANISOU  260  CA  TYR A  50    18068  13383  16199   -465   1064   1526       C  
ATOM    261  C   TYR A  50       9.762  24.209  68.081  1.00129.07           C  
ANISOU  261  C   TYR A  50    18123  13798  17118   -474    831   1528       C  
ATOM    262  O   TYR A  50       8.931  23.359  68.422  1.00137.02           O  
ANISOU  262  O   TYR A  50    19055  14673  18334   -587   1011   1680       O  
ATOM    263  CB  TYR A  50       9.232  26.612  68.495  1.00125.45           C  
ANISOU  263  CB  TYR A  50    17836  13511  16320   -349   1369   1399       C  
ATOM    264  CG  TYR A  50       7.820  26.212  68.129  1.00137.39           C  
ANISOU  264  CG  TYR A  50    18952  14967  18283   -370   1647   1440       C  
ATOM    265  CD1 TYR A  50       6.925  25.797  69.104  1.00138.71           C  
ANISOU  265  CD1 TYR A  50    19241  14995  18469   -513   2071   1600       C  
ATOM    266  CD2 TYR A  50       7.393  26.211  66.807  1.00143.74           C  
ANISOU  266  CD2 TYR A  50    19270  15845  19499   -265   1476   1321       C  
ATOM    267  CE1 TYR A  50       5.639  25.410  68.776  1.00140.14           C  
ANISOU  267  CE1 TYR A  50    19027  15101  19120   -536   2326   1633       C  
ATOM    268  CE2 TYR A  50       6.105  25.828  66.471  1.00147.03           C  
ANISOU  268  CE2 TYR A  50    19313  16180  20372   -284   1685   1357       C  
ATOM    269  CZ  TYR A  50       5.233  25.429  67.463  1.00143.06           C  
ANISOU  269  CZ  TYR A  50    18898  15527  19933   -413   2114   1510       C  
ATOM    270  OH  TYR A  50       3.951  25.045  67.146  1.00149.67           O  
ANISOU  270  OH  TYR A  50    19332  16260  21276   -435   2331   1541       O  
ATOM    271  N   ASN A  51      10.445  24.117  66.939  1.00112.34           N  
ANISOU  271  N   ASN A  51    15742  11784  15160   -368    442   1350       N  
ATOM    272  CA  ASN A  51      10.194  23.013  66.020  1.00115.71           C  
ANISOU  272  CA  ASN A  51    15777  12173  16016   -370    209   1306       C  
ATOM    273  C   ASN A  51      10.702  21.693  66.580  1.00113.72           C  
ANISOU  273  C   ASN A  51    15672  11727  15810   -488    -30   1437       C  
ATOM    274  O   ASN A  51      10.170  20.627  66.244  1.00116.40           O  
ANISOU  274  O   ASN A  51    15749  11959  16517   -539   -104   1483       O  
ATOM    275  CB  ASN A  51      10.843  23.302  64.666  1.00109.35           C  
ANISOU  275  CB  ASN A  51    14695  11541  15312   -247   -117   1056       C  
ATOM    276  CG  ASN A  51       9.997  24.215  63.796  1.00124.90           C  
ANISOU  276  CG  ASN A  51    16378  13656  17421   -156     47    958       C  
ATOM    277  OD1 ASN A  51       9.284  25.085  64.297  1.00133.95           O  
ANISOU  277  OD1 ASN A  51    17605  14806  18484   -143    390   1030       O  
ATOM    278  ND2 ASN A  51      10.080  24.025  62.483  1.00124.63           N  
ANISOU  278  ND2 ASN A  51    16016  13731  17606   -101   -211    786       N  
ATOM    279  N   THR A  52      11.723  21.736  67.427  1.00115.62           N  
ANISOU  279  N   THR A  52    16324  11897  15711   -537   -186   1501       N  
ATOM    280  CA  THR A  52      12.265  20.515  68.009  1.00112.87           C  
ANISOU  280  CA  THR A  52    16143  11328  15416   -658   -472   1645       C  
ATOM    281  C   THR A  52      11.723  20.237  69.395  1.00114.75           C  
ANISOU  281  C   THR A  52    16782  11396  15420   -840   -194   1948       C  
ATOM    282  O   THR A  52      11.849  19.113  69.882  1.00111.52           O  
ANISOU  282  O   THR A  52    16483  10775  15114   -975   -383   2128       O  
ATOM    283  CB  THR A  52      13.778  20.616  68.136  1.00103.16           C  
ANISOU  283  CB  THR A  52    15130  10069  13995   -621   -886   1548       C  
ATOM    284  OG1 THR A  52      14.093  21.907  68.661  1.00103.90           O  
ANISOU  284  OG1 THR A  52    15545  10274  13659   -581   -713   1530       O  
ATOM    285  CG2 THR A  52      14.444  20.424  66.777  1.00110.19           C  
ANISOU  285  CG2 THR A  52    15606  11069  15193   -493  -1218   1253       C  
ATOM    286  N   ASN A  53      11.147  21.246  70.038  1.00120.42           N  
ANISOU  286  N   ASN A  53    17732  12197  15825   -858    250   2002       N  
ATOM    287  CA  ASN A  53      10.773  21.142  71.436  1.00123.90           C  
ANISOU  287  CA  ASN A  53    18647  12503  15927  -1052    550   2261       C  
ATOM    288  C   ASN A  53       9.578  22.048  71.687  1.00125.91           C  
ANISOU  288  C   ASN A  53    18865  12862  16114  -1051   1164   2249       C  
ATOM    289  O   ASN A  53       9.730  23.148  72.222  1.00129.18           O  
ANISOU  289  O   ASN A  53    19573  13364  16147  -1023   1383   2192       O  
ATOM    290  CB  ASN A  53      11.985  21.501  72.292  1.00128.53           C  
ANISOU  290  CB  ASN A  53    19771  13036  16030  -1092    296   2305       C  
ATOM    291  CG  ASN A  53      11.724  21.445  73.781  1.00136.07           C  
ANISOU  291  CG  ASN A  53    21311  13858  16532  -1316    568   2569       C  
ATOM    292  OD1 ASN A  53      10.980  20.600  74.279  1.00140.14           O  
ANISOU  292  OD1 ASN A  53    21887  14236  17123  -1498    765   2794       O  
ATOM    293  ND2 ASN A  53      12.370  22.350  74.507  1.00145.27           N  
ANISOU  293  ND2 ASN A  53    22935  15058  17205  -1318    573   2543       N  
ATOM    294  N   ILE A  54       8.387  21.602  71.285  1.00129.79           N  
ANISOU  294  N   ILE A  54    18971  13325  17018  -1075   1434   2284       N  
ATOM    295  CA  ILE A  54       7.211  22.466  71.365  1.00129.88           C  
ANISOU  295  CA  ILE A  54    18836  13414  17100  -1050   1997   2229       C  
ATOM    296  C   ILE A  54       6.902  22.766  72.825  1.00130.70           C  
ANISOU  296  C   ILE A  54    19460  13448  16752  -1237   2463   2391       C  
ATOM    297  O   ILE A  54       6.657  21.853  73.623  1.00135.74           O  
ANISOU  297  O   ILE A  54    20336  13928  17311  -1453   2573   2632       O  
ATOM    298  CB  ILE A  54       6.016  21.815  70.656  1.00136.90           C  
ANISOU  298  CB  ILE A  54    19187  14244  18584  -1051   2146   2241       C  
ATOM    299  CG1 ILE A  54       6.345  21.571  69.179  1.00134.12           C  
ANISOU  299  CG1 ILE A  54    18365  13975  18619   -875   1675   2054       C  
ATOM    300  CG2 ILE A  54       4.730  22.668  70.828  1.00138.72           C  
ANISOU  300  CG2 ILE A  54    19240  14504  18965  -1038   2749   2187       C  
ATOM    301  CD1 ILE A  54       5.276  20.831  68.423  1.00138.35           C  
ANISOU  301  CD1 ILE A  54    18384  14433  19749   -876   1716   2059       C  
ATOM    302  N   THR A  55       6.936  24.048  73.180  1.00125.45           N  
ANISOU  302  N   THR A  55    18994  12898  15775  -1167   2731   2258       N  
ATOM    303  CA  THR A  55       6.593  24.538  74.505  1.00131.24           C  
ANISOU  303  CA  THR A  55    20214  13595  16055  -1329   3234   2341       C  
ATOM    304  C   THR A  55       5.922  25.885  74.318  1.00136.03           C  
ANISOU  304  C   THR A  55    20624  14320  16739  -1188   3654   2112       C  
ATOM    305  O   THR A  55       6.293  26.627  73.409  1.00139.07           O  
ANISOU  305  O   THR A  55    20742  14826  17272   -973   3397   1917       O  
ATOM    306  CB  THR A  55       7.824  24.724  75.403  1.00137.18           C  
ANISOU  306  CB  THR A  55    21618  14327  16177  -1406   2965   2411       C  
ATOM    307  OG1 THR A  55       8.432  25.986  75.093  1.00128.45           O  
ANISOU  307  OG1 THR A  55    20533  13365  14905  -1210   2854   2178       O  
ATOM    308  CG2 THR A  55       8.844  23.609  75.209  1.00141.64           C  
ANISOU  308  CG2 THR A  55    22263  14781  16772  -1447   2325   2553       C  
ATOM    309  N   GLU A  56       4.941  26.214  75.168  1.00152.55           N  
ANISOU  309  N   GLU A  56    22844  16369  18748  -1318   4302   2127       N  
ATOM    310  CA  GLU A  56       4.420  27.579  75.115  1.00151.71           C  
ANISOU  310  CA  GLU A  56    22599  16348  18695  -1182   4683   1884       C  
ATOM    311  C   GLU A  56       5.535  28.575  75.367  1.00149.34           C  
ANISOU  311  C   GLU A  56    22689  16147  17904  -1080   4438   1760       C  
ATOM    312  O   GLU A  56       5.475  29.711  74.885  1.00152.26           O  
ANISOU  312  O   GLU A  56    22850  16604  18398   -893   4473   1542       O  
ATOM    313  CB  GLU A  56       3.289  27.788  76.120  1.00152.03           C  
ANISOU  313  CB  GLU A  56    22767  16315  18683  -1355   5457   1886       C  
ATOM    314  CG  GLU A  56       2.113  28.564  75.553  1.00155.42           C  
ANISOU  314  CG  GLU A  56    22624  16742  19686  -1214   5859   1669       C  
ATOM    315  CD  GLU A  56       2.388  30.049  75.489  1.00159.27           C  
ANISOU  315  CD  GLU A  56    23154  17324  20038  -1029   5900   1410       C  
ATOM    316  OE1 GLU A  56       3.115  30.548  76.372  1.00157.60           O  
ANISOU  316  OE1 GLU A  56    23513  17156  19212  -1089   5942   1385       O  
ATOM    317  OE2 GLU A  56       1.905  30.712  74.549  1.00157.23           O1-
ANISOU  317  OE2 GLU A  56    22371  17082  20289   -828   5849   1240       O1-
ATOM    318  N   GLU A  57       6.559  28.166  76.119  1.00143.49           N  
ANISOU  318  N   GLU A  57    22513  15373  16634  -1206   4158   1904       N  
ATOM    319  CA  GLU A  57       7.703  29.039  76.336  1.00141.09           C  
ANISOU  319  CA  GLU A  57    22570  15139  15899  -1111   3856   1793       C  
ATOM    320  C   GLU A  57       8.374  29.379  75.015  1.00134.27           C  
ANISOU  320  C   GLU A  57    21288  14378  15350   -866   3336   1652       C  
ATOM    321  O   GLU A  57       8.625  30.550  74.713  1.00141.81           O  
ANISOU  321  O   GLU A  57    22183  15427  16273   -705   3317   1457       O  
ATOM    322  CB  GLU A  57       8.714  28.382  77.278  1.00157.48           C  
ANISOU  322  CB  GLU A  57    25282  17121  17434  -1294   3542   1995       C  
ATOM    323  CG  GLU A  57       9.999  29.188  77.390  1.00164.30           C  
ANISOU  323  CG  GLU A  57    26465  18030  17932  -1182   3126   1882       C  
ATOM    324  CD  GLU A  57      10.921  28.715  78.493  1.00169.60           C  
ANISOU  324  CD  GLU A  57    27827  18575  18036  -1375   2848   2069       C  
ATOM    325  OE1 GLU A  57      10.460  28.031  79.430  1.00172.20           O  
ANISOU  325  OE1 GLU A  57    28524  18800  18105  -1626   3115   2275       O  
ATOM    326  OE2 GLU A  57      12.137  28.979  78.381  1.00155.39           O1-
ANISOU  326  OE2 GLU A  57    26193  16767  16081  -1285   2324   2022       O1-
ATOM    327  N   ASN A  58       8.657  28.360  74.201  1.00128.39           N  
ANISOU  327  N   ASN A  58    20250  13614  14920   -847   2922   1741       N  
ATOM    328  CA  ASN A  58       9.379  28.604  72.960  1.00133.03           C  
ANISOU  328  CA  ASN A  58    20488  14307  15751   -649   2436   1601       C  
ATOM    329  C   ASN A  58       8.488  29.181  71.869  1.00133.71           C  
ANISOU  329  C   ASN A  58    19999  14485  16321   -493   2590   1448       C  
ATOM    330  O   ASN A  58       8.987  29.900  70.998  1.00128.60           O  
ANISOU  330  O   ASN A  58    19152  13952  15759   -332   2321   1298       O  
ATOM    331  CB  ASN A  58      10.054  27.323  72.474  1.00134.36           C  
ANISOU  331  CB  ASN A  58    20555  14415  16080   -687   1937   1709       C  
ATOM    332  CG  ASN A  58      11.064  26.777  73.470  1.00126.14           C  
ANISOU  332  CG  ASN A  58    20066  13250  14613   -829   1665   1863       C  
ATOM    333  OD1 ASN A  58      11.485  27.473  74.394  1.00132.52           O  
ANISOU  333  OD1 ASN A  58    21349  14045  14956   -874   1754   1863       O  
ATOM    334  ND2 ASN A  58      11.483  25.541  73.260  1.00119.17           N  
ANISOU  334  ND2 ASN A  58    19117  12257  13904   -897   1291   1985       N  
ATOM    335  N   VAL A  59       7.185  28.887  71.887  1.00149.52           N  
ANISOU  335  N   VAL A  59    21729  16426  18658   -548   3001   1489       N  
ATOM    336  CA  VAL A  59       6.273  29.593  70.990  1.00146.69           C  
ANISOU  336  CA  VAL A  59    20860  16115  18760   -404   3159   1340       C  
ATOM    337  C   VAL A  59       6.444  31.095  71.160  1.00144.99           C  
ANISOU  337  C   VAL A  59    20765  15971  18355   -286   3295   1168       C  
ATOM    338  O   VAL A  59       6.407  31.859  70.188  1.00148.41           O  
ANISOU  338  O   VAL A  59    20870  16481  19040   -127   3122   1036       O  
ATOM    339  CB  VAL A  59       4.816  29.165  71.242  1.00149.67           C  
ANISOU  339  CB  VAL A  59    20974  16374  19521   -496   3654   1400       C  
ATOM    340  CG1 VAL A  59       3.875  29.903  70.303  1.00151.40           C  
ANISOU  340  CG1 VAL A  59    20645  16603  20277   -343   3756   1247       C  
ATOM    341  CG2 VAL A  59       4.666  27.676  71.065  1.00150.36           C  
ANISOU  341  CG2 VAL A  59    20937  16375  19819   -615   3492   1578       C  
ATOM    342  N   GLN A  60       6.651  31.538  72.401  1.00144.14           N  
ANISOU  342  N   GLN A  60    21150  15829  17786   -375   3588   1170       N  
ATOM    343  CA  GLN A  60       6.889  32.949  72.672  1.00147.81           C  
ANISOU  343  CA  GLN A  60    21774  16342  18044   -270   3706    995       C  
ATOM    344  C   GLN A  60       8.328  33.355  72.374  1.00144.56           C  
ANISOU  344  C   GLN A  60    21579  16021  17326   -182   3180    956       C  
ATOM    345  O   GLN A  60       8.567  34.491  71.951  1.00146.45           O  
ANISOU  345  O   GLN A  60    21722  16324  17600    -38   3094    806       O  
ATOM    346  CB  GLN A  60       6.535  33.267  74.127  1.00153.94           C  
ANISOU  346  CB  GLN A  60    23014  17046  18432   -411   4241    982       C  
ATOM    347  CG  GLN A  60       5.112  32.881  74.535  1.00162.57           C  
ANISOU  347  CG  GLN A  60    23910  18040  19820   -527   4845   1006       C  
ATOM    348  CD  GLN A  60       4.064  33.876  74.062  1.00163.43           C  
ANISOU  348  CD  GLN A  60    23542  18122  20431   -384   5176    799       C  
ATOM    349  OE1 GLN A  60       4.049  34.280  72.899  1.00164.12           O  
ANISOU  349  OE1 GLN A  60    23190  18250  20917   -207   4850    728       O  
ATOM    350  NE2 GLN A  60       3.179  34.275  74.969  1.00156.00           N  
ANISOU  350  NE2 GLN A  60    22691  17100  19482   -472   5825    696       N  
ATOM    351  N   ASN A  61       9.292  32.455  72.587  1.00145.53           N  
ANISOU  351  N   ASN A  61    21976  16131  17188   -269   2819   1087       N  
ATOM    352  CA  ASN A  61      10.676  32.768  72.240  1.00146.44           C  
ANISOU  352  CA  ASN A  61    22234  16311  17095   -186   2310   1036       C  
ATOM    353  C   ASN A  61      10.856  32.859  70.731  1.00144.43           C  
ANISOU  353  C   ASN A  61    21476  16169  17234    -44   1970    951       C  
ATOM    354  O   ASN A  61      11.539  33.762  70.235  1.00144.67           O  
ANISOU  354  O   ASN A  61    21475  16284  17212     70   1747    834       O  
ATOM    355  CB  ASN A  61      11.622  31.720  72.825  1.00141.48           C  
ANISOU  355  CB  ASN A  61    21978  15600  16177   -317   1986   1189       C  
ATOM    356  CG  ASN A  61      11.883  31.931  74.299  1.00154.19           C  
ANISOU  356  CG  ASN A  61    24219  17116  17250   -452   2168   1254       C  
ATOM    357  OD1 ASN A  61      11.811  33.054  74.798  1.00151.63           O  
ANISOU  357  OD1 ASN A  61    24099  16815  16698   -409   2406   1130       O  
ATOM    358  ND2 ASN A  61      12.214  30.855  75.002  1.00161.32           N  
ANISOU  358  ND2 ASN A  61    25453  17899  17940   -624   2029   1448       N  
ATOM    359  N   MET A  62      10.261  31.923  69.989  1.00135.98           N  
ANISOU  359  N   MET A  62    20027  15096  16544    -63   1923   1011       N  
ATOM    360  CA  MET A  62      10.305  31.974  68.530  1.00121.70           C  
ANISOU  360  CA  MET A  62    17757  13395  15087     48   1628    925       C  
ATOM    361  C   MET A  62       9.754  33.296  68.010  1.00118.64           C  
ANISOU  361  C   MET A  62    17144  13069  14865    171   1773    803       C  
ATOM    362  O   MET A  62      10.348  33.928  67.128  1.00120.97           O  
ANISOU  362  O   MET A  62    17307  13472  15184    262   1482    714       O  
ATOM    363  CB  MET A  62       9.518  30.795  67.957  1.00125.50           C  
ANISOU  363  CB  MET A  62    17886  13836  15964     -3   1624   1002       C  
ATOM    364  CG  MET A  62       9.513  30.686  66.447  1.00115.99           C  
ANISOU  364  CG  MET A  62    16238  12738  15097     82   1307    913       C  
ATOM    365  SD  MET A  62       8.408  29.362  65.925  1.00131.69           S  
ANISOU  365  SD  MET A  62    17826  14640  17569     19   1348    994       S  
ATOM    366  CE  MET A  62       8.692  29.330  64.158  1.00131.35           C  
ANISOU  366  CE  MET A  62    17378  14746  17784    106    903    856       C  
ATOM    367  N   ASN A  63       8.622  33.739  68.563  1.00126.74           N  
ANISOU  367  N   ASN A  63    18121  14012  16023    165   2228    795       N  
ATOM    368  CA  ASN A  63       7.982  34.956  68.075  1.00132.21           C  
ANISOU  368  CA  ASN A  63    18551  14715  16968    284   2355    678       C  
ATOM    369  C   ASN A  63       8.807  36.195  68.404  1.00129.97           C  
ANISOU  369  C   ASN A  63    18548  14475  16361    356   2286    577       C  
ATOM    370  O   ASN A  63       8.885  37.125  67.592  1.00132.16           O  
ANISOU  370  O   ASN A  63    18616  14804  16792    462   2112    499       O  
ATOM    371  CB  ASN A  63       6.574  35.077  68.659  1.00130.78           C  
ANISOU  371  CB  ASN A  63    18224  14402  17065    256   2886    665       C  
ATOM    372  CG  ASN A  63       5.639  33.993  68.156  1.00129.48           C  
ANISOU  372  CG  ASN A  63    17685  14176  17335    202   2934    753       C  
ATOM    373  OD1 ASN A  63       5.743  33.549  67.013  1.00130.00           O  
ANISOU  373  OD1 ASN A  63    17454  14303  17639    240   2560    774       O  
ATOM    374  ND2 ASN A  63       4.722  33.556  69.013  1.00134.00           N  
ANISOU  374  ND2 ASN A  63    18278  14625  18009    101   3406    798       N  
ATOM    375  N   ASN A  64       9.427  36.229  69.587  1.00126.07           N  
ANISOU  375  N   ASN A  64    18540  13945  15417    290   2397    587       N  
ATOM    376  CA  ASN A  64      10.202  37.404  69.978  1.00122.54           C  
ANISOU  376  CA  ASN A  64    18374  13515  14669    357   2329    482       C  
ATOM    377  C   ASN A  64      11.420  37.590  69.084  1.00121.48           C  
ANISOU  377  C   ASN A  64    18195  13492  14470    418   1810    467       C  
ATOM    378  O   ASN A  64      11.762  38.721  68.721  1.00124.41           O  
ANISOU  378  O   ASN A  64    18525  13900  14846    512   1697    376       O  
ATOM    379  CB  ASN A  64      10.624  37.298  71.444  1.00121.30           C  
ANISOU  379  CB  ASN A  64    18783  13285  14020    254   2516    502       C  
ATOM    380  CG  ASN A  64       9.452  37.414  72.396  1.00129.37           C  
ANISOU  380  CG  ASN A  64    19894  14209  15051    184   3110    469       C  
ATOM    381  OD1 ASN A  64       8.438  38.031  72.073  1.00133.69           O  
ANISOU  381  OD1 ASN A  64    20098  14724  15974    259   3393    369       O  
ATOM    382  ND2 ASN A  64       9.589  36.830  73.581  1.00143.96           N  
ANISOU  382  ND2 ASN A  64    22209  15995  16494     29   3301    548       N  
ATOM    383  N   ALA A  65      12.087  36.496  68.715  1.00117.96           N  
ANISOU  383  N   ALA A  65    17743  13090  13987    358   1502    547       N  
ATOM    384  CA  ALA A  65      13.224  36.608  67.810  1.00113.43           C  
ANISOU  384  CA  ALA A  65    17085  12622  13391    401   1055    505       C  
ATOM    385  C   ALA A  65      12.773  36.968  66.399  1.00123.27           C  
ANISOU  385  C   ALA A  65    17876  13972  14990    468    939    466       C  
ATOM    386  O   ALA A  65      13.421  37.775  65.722  1.00122.43           O  
ANISOU  386  O   ALA A  65    17709  13949  14860    520    714    403       O  
ATOM    387  CB  ALA A  65      14.023  35.307  67.808  1.00105.81           C  
ANISOU  387  CB  ALA A  65    16206  11650  12347    318    775    569       C  
ATOM    388  N   GLY A  66      11.665  36.386  65.939  1.00126.81           N  
ANISOU  388  N   GLY A  66    18011  14404  15768    453   1075    510       N  
ATOM    389  CA  GLY A  66      11.178  36.700  64.605  1.00115.11           C  
ANISOU  389  CA  GLY A  66    16125  12998  14612    500    925    486       C  
ATOM    390  C   GLY A  66      10.645  38.116  64.498  1.00118.35           C  
ANISOU  390  C   GLY A  66    16445  13374  15148    587   1048    438       C  
ATOM    391  O   GLY A  66      10.772  38.761  63.453  1.00123.16           O  
ANISOU  391  O   GLY A  66    16861  14060  15875    622    809    420       O  
ATOM    392  N   ASP A  67      10.040  38.619  65.577  1.00126.69           N  
ANISOU  392  N   ASP A  67    17647  14306  16184    611   1420    412       N  
ATOM    393  CA  ASP A  67       9.530  39.986  65.563  1.00134.03           C  
ANISOU  393  CA  ASP A  67    18480  15167  17278    702   1546    339       C  
ATOM    394  C   ASP A  67      10.666  41.001  65.514  1.00128.23           C  
ANISOU  394  C   ASP A  67    17960  14491  16268    745   1313    287       C  
ATOM    395  O   ASP A  67      10.544  42.046  64.865  1.00127.43           O  
ANISOU  395  O   ASP A  67    17689  14384  16344    810   1187    261       O  
ATOM    396  CB  ASP A  67       8.641  40.231  66.781  1.00134.64           C  
ANISOU  396  CB  ASP A  67    18666  15093  17399    707   2047    280       C  
ATOM    397  CG  ASP A  67       7.286  39.562  66.658  1.00147.26           C  
ANISOU  397  CG  ASP A  67    19930  16598  19424    681   2308    314       C  
ATOM    398  OD1 ASP A  67       6.961  39.067  65.557  1.00151.80           O  
ANISOU  398  OD1 ASP A  67    20166  17211  20299    680   2061    378       O  
ATOM    399  OD2 ASP A  67       6.541  39.540  67.659  1.00148.83           O1-
ANISOU  399  OD2 ASP A  67    20207  16680  19661    652   2769    267       O1-
ATOM    400  N   LYS A  68      11.777  40.712  66.195  1.00121.73           N  
ANISOU  400  N   LYS A  68    17508  13705  15039    704   1229    281       N  
ATOM    401  CA  LYS A  68      12.936  41.596  66.128  1.00124.34           C  
ANISOU  401  CA  LYS A  68    18026  14080  15136    738    981    232       C  
ATOM    402  C   LYS A  68      13.611  41.523  64.765  1.00113.98           C  
ANISOU  402  C   LYS A  68    16498  12912  13896    718    591    263       C  
ATOM    403  O   LYS A  68      14.186  42.515  64.302  1.00113.93           O  
ANISOU  403  O   LYS A  68    16487  12942  13860    748    406    238       O  
ATOM    404  CB  LYS A  68      13.929  41.236  67.232  1.00121.64           C  
ANISOU  404  CB  LYS A  68    18129  13708  14382    692    960    217       C  
ATOM    405  CG  LYS A  68      13.392  41.456  68.633  1.00128.70           C  
ANISOU  405  CG  LYS A  68    19328  14471  15102    686   1347    174       C  
ATOM    406  CD  LYS A  68      14.419  41.077  69.685  1.00129.32           C  
ANISOU  406  CD  LYS A  68    19888  14506  14740    620   1251    182       C  
ATOM    407  CE  LYS A  68      13.874  41.303  71.087  1.00123.96           C  
ANISOU  407  CE  LYS A  68    19570  13710  13820    583   1653    133       C  
ATOM    408  NZ  LYS A  68      14.851  40.911  72.140  1.00105.53           N  
ANISOU  408  NZ  LYS A  68    17755  11315  11026    498   1515    163       N  
ATOM    409  N   TRP A  69      13.551  40.361  64.114  1.00111.81           N  
ANISOU  409  N   TRP A  69    16053  12718  13713    655    474    311       N  
ATOM    410  CA  TRP A  69      14.116  40.208  62.780  1.00109.38           C  
ANISOU  410  CA  TRP A  69    15543  12560  13458    614    148    314       C  
ATOM    411  C   TRP A  69      13.190  40.780  61.714  1.00103.79           C  
ANISOU  411  C   TRP A  69    14509  11872  13053    631     97    352       C  
ATOM    412  O   TRP A  69      13.667  41.316  60.707  1.00 98.90           O  
ANISOU  412  O   TRP A  69    13800  11357  12419    600   -151    358       O  
ATOM    413  CB  TRP A  69      14.405  38.725  62.525  1.00108.08           C  
ANISOU  413  CB  TRP A  69    15324  12455  13286    540     41    318       C  
ATOM    414  CG  TRP A  69      14.687  38.343  61.105  1.00 94.51           C  
ANISOU  414  CG  TRP A  69    13357  10890  11664    482   -223    293       C  
ATOM    415  CD1 TRP A  69      13.920  37.549  60.306  1.00 99.09           C  
ANISOU  415  CD1 TRP A  69    13668  11509  12473    445   -263    312       C  
ATOM    416  CD2 TRP A  69      15.842  38.695  60.332  1.00 93.02           C  
ANISOU  416  CD2 TRP A  69    13180  10834  11332    437   -472    228       C  
ATOM    417  NE1 TRP A  69      14.513  37.401  59.076  1.00 99.18           N  
ANISOU  417  NE1 TRP A  69    13548  11679  12456    377   -520    254       N  
ATOM    418  CE2 TRP A  69      15.695  38.094  59.066  1.00 93.69           C  
ANISOU  418  CE2 TRP A  69    13016  11048  11532    364   -629    201       C  
ATOM    419  CE3 TRP A  69      16.978  39.468  60.584  1.00 94.80           C  
ANISOU  419  CE3 TRP A  69    13596  11073  11350    442   -567    182       C  
ATOM    420  CZ2 TRP A  69      16.641  38.242  58.056  1.00 95.57           C  
ANISOU  420  CZ2 TRP A  69    13210  11446  11659    283   -838    123       C  
ATOM    421  CZ3 TRP A  69      17.917  39.614  59.579  1.00 95.34           C  
ANISOU  421  CZ3 TRP A  69    13587  11286  11352    368   -780    116       C  
ATOM    422  CH2 TRP A  69      17.743  39.004  58.330  1.00 93.30           C  
ANISOU  422  CH2 TRP A  69    13094  11170  11184    283   -893     84       C  
ATOM    423  N   SER A  70      11.875  40.685  61.923  1.00115.03           N  
ANISOU  423  N   SER A  70    15759  13183  14762    667    321    383       N  
ATOM    424  CA  SER A  70      10.931  41.351  61.032  1.00121.42           C  
ANISOU  424  CA  SER A  70    16264  13954  15915    694    247    423       C  
ATOM    425  C   SER A  70      11.051  42.865  61.140  1.00118.43           C  
ANISOU  425  C   SER A  70    15942  13507  15547    759    226    407       C  
ATOM    426  O   SER A  70      10.947  43.578  60.135  1.00124.11           O  
ANISOU  426  O   SER A  70    16500  14250  16408    746    -18    460       O  
ATOM    427  CB  SER A  70       9.502  40.909  61.352  1.00137.59           C  
ANISOU  427  CB  SER A  70    18089  15857  18332    724    511    440       C  
ATOM    428  OG  SER A  70       9.244  39.601  60.871  1.00139.57           O  
ANISOU  428  OG  SER A  70    18192  16163  18675    658    438    474       O  
ATOM    429  N   ALA A  71      11.268  43.376  62.355  1.00113.59           N  
ANISOU  429  N   ALA A  71    15578  12800  14782    818    465    337       N  
ATOM    430  CA  ALA A  71      11.379  44.813  62.570  1.00117.31           C  
ANISOU  430  CA  ALA A  71    16109  13180  15285    889    459    297       C  
ATOM    431  C   ALA A  71      12.751  45.362  62.202  1.00106.43           C  
ANISOU  431  C   ALA A  71    14912  11913  13613    855    169    305       C  
ATOM    432  O   ALA A  71      12.881  46.572  61.992  1.00110.78           O  
ANISOU  432  O   ALA A  71    15449  12406  14238    892     59    308       O  
ATOM    433  CB  ALA A  71      11.061  45.154  64.026  1.00122.19           C  
ANISOU  433  CB  ALA A  71    16937  13650  15841    958    843    187       C  
ATOM    434  N   PHE A  72      13.774  44.509  62.132  1.00 96.63           N  
ANISOU  434  N   PHE A  72    13822  10811  12082    782     43    304       N  
ATOM    435  CA  PHE A  72      15.081  44.954  61.664  1.00101.01           C  
ANISOU  435  CA  PHE A  72    14492  11470  12417    734   -225    301       C  
ATOM    436  C   PHE A  72      15.099  45.098  60.148  1.00100.76           C  
ANISOU  436  C   PHE A  72    14225  11567  12492    649   -492    382       C  
ATOM    437  O   PHE A  72      15.696  46.040  59.616  1.00106.00           O  
ANISOU  437  O   PHE A  72    14907  12263  13104    616   -676    414       O  
ATOM    438  CB  PHE A  72      16.162  43.976  62.132  1.00103.85           C  
ANISOU  438  CB  PHE A  72    15063  11900  12495    686   -270    249       C  
ATOM    439  CG  PHE A  72      17.477  44.124  61.416  1.00 94.37           C  
ANISOU  439  CG  PHE A  72    13887  10824  11144    612   -543    230       C  
ATOM    440  CD1 PHE A  72      18.335  45.168  61.720  1.00 96.65           C  
ANISOU  440  CD1 PHE A  72    14339  11067  11315    633   -634    200       C  
ATOM    441  CD2 PHE A  72      17.865  43.203  60.455  1.00 90.54           C  
ANISOU  441  CD2 PHE A  72    13255  10493  10652    514   -690    221       C  
ATOM    442  CE1 PHE A  72      19.547  45.299  61.069  1.00 97.36           C  
ANISOU  442  CE1 PHE A  72    14428  11261  11303    552   -854    176       C  
ATOM    443  CE2 PHE A  72      19.074  43.329  59.800  1.00 88.47           C  
ANISOU  443  CE2 PHE A  72    12999  10345  10272    431   -888    175       C  
ATOM    444  CZ  PHE A  72      19.917  44.377  60.107  1.00 87.03           C  
ANISOU  444  CZ  PHE A  72    12963  10113   9990    447   -962    158       C  
ATOM    445  N   LEU A  73      14.439  44.178  59.441  1.00 88.59           N  
ANISOU  445  N   LEU A  73    12478  10094  11089    598   -521    419       N  
ATOM    446  CA  LEU A  73      14.402  44.250  57.985  1.00 84.86           C  
ANISOU  446  CA  LEU A  73    11821   9747  10674    495   -782    491       C  
ATOM    447  C   LEU A  73      13.547  45.418  57.510  1.00 94.63           C  
ANISOU  447  C   LEU A  73    12912  10871  12174    521   -877    592       C  
ATOM    448  O   LEU A  73      13.875  46.066  56.509  1.00 88.35           O  
ANISOU  448  O   LEU A  73    12086  10148  11333    428  -1128    674       O  
ATOM    449  CB  LEU A  73      13.887  42.930  57.412  1.00 85.73           C  
ANISOU  449  CB  LEU A  73    11764   9938  10870    438   -804    486       C  
ATOM    450  CG  LEU A  73      14.966  41.872  57.174  1.00 84.28           C  
ANISOU  450  CG  LEU A  73    11659   9917  10445    353   -875    394       C  
ATOM    451  CD1 LEU A  73      14.358  40.584  56.646  1.00 85.51           C  
ANISOU  451  CD1 LEU A  73    11635  10124  10730    309   -898    374       C  
ATOM    452  CD2 LEU A  73      16.027  42.402  56.221  1.00 83.26           C  
ANISOU  452  CD2 LEU A  73    11576   9948  10112    238  -1087    382       C  
ATOM    453  N   LYS A  74      12.448  45.703  58.214  1.00117.56           N  
ANISOU  453  N   LYS A  74    15718  13580  15368    636   -679    585       N  
ATOM    454  CA  LYS A  74      11.649  46.878  57.883  1.00116.00           C  
ANISOU  454  CA  LYS A  74    15360  13222  15494    680   -777    659       C  
ATOM    455  C   LYS A  74      12.418  48.163  58.159  1.00114.89           C  
ANISOU  455  C   LYS A  74    15385  13032  15236    704   -848    658       C  
ATOM    456  O   LYS A  74      12.244  49.157  57.445  1.00111.64           O  
ANISOU  456  O   LYS A  74    14880  12554  14984    675  -1085    763       O  
ATOM    457  CB  LYS A  74      10.335  46.856  58.667  1.00115.60           C  
ANISOU  457  CB  LYS A  74    15140  12955  15828    801   -496    605       C  
ATOM    458  CG  LYS A  74       9.277  47.821  58.150  1.00133.98           C  
ANISOU  458  CG  LYS A  74    17198  15082  18628    844   -638    675       C  
ATOM    459  CD  LYS A  74       8.102  47.927  59.113  1.00129.71           C  
ANISOU  459  CD  LYS A  74    16489  14303  18490    975   -284    567       C  
ATOM    460  CE  LYS A  74       7.505  49.326  59.106  1.00118.46           C  
ANISOU  460  CE  LYS A  74    14900  12633  17476   1061   -360    562       C  
ATOM    461  NZ  LYS A  74       6.478  49.506  60.171  1.00125.63           N  
ANISOU  461  NZ  LYS A  74    15659  13308  18766   1189     58    398       N  
ATOM    462  N   GLU A  75      13.273  48.156  59.185  1.00110.76           N  
ANISOU  462  N   GLU A  75    15116  12522  14445    750   -676    550       N  
ATOM    463  CA  GLU A  75      14.128  49.306  59.454  1.00108.10           C  
ANISOU  463  CA  GLU A  75    14949  12142  13984    768   -766    538       C  
ATOM    464  C   GLU A  75      15.201  49.455  58.383  1.00106.32           C  
ANISOU  464  C   GLU A  75    14766  12093  13539    622  -1062    627       C  
ATOM    465  O   GLU A  75      15.564  50.576  58.008  1.00100.88           O  
ANISOU  465  O   GLU A  75    14093  11357  12878    592  -1243    700       O  
ATOM    466  CB  GLU A  75      14.774  49.169  60.831  1.00117.12           C  
ANISOU  466  CB  GLU A  75    16372  13243  14885    844   -538    395       C  
ATOM    467  CG  GLU A  75      15.610  50.370  61.251  1.00134.19           C  
ANISOU  467  CG  GLU A  75    18713  15324  16949    879   -624    358       C  
ATOM    468  CD  GLU A  75      16.269  50.180  62.605  1.00141.74           C  
ANISOU  468  CD  GLU A  75    19982  16232  17640    940   -446    216       C  
ATOM    469  OE1 GLU A  75      16.618  49.027  62.939  1.00124.76           O  
ANISOU  469  OE1 GLU A  75    17947  14176  15279    903   -374    186       O  
ATOM    470  OE2 GLU A  75      16.448  51.180  63.331  1.00135.53           O1-
ANISOU  470  OE2 GLU A  75    19338  15301  16858   1019   -405    136       O1-
ATOM    471  N   GLN A  76      15.724  48.334  57.884  1.00105.89           N  
ANISOU  471  N   GLN A  76    14724  12235  13276    521  -1103    614       N  
ATOM    472  CA  GLN A  76      16.797  48.387  56.898  1.00101.55           C  
ANISOU  472  CA  GLN A  76    14214  11866  12502    364  -1319    657       C  
ATOM    473  C   GLN A  76      16.259  48.598  55.490  1.00108.96           C  
ANISOU  473  C   GLN A  76    14989  12879  13533    232  -1550    806       C  
ATOM    474  O   GLN A  76      16.933  49.221  54.662  1.00103.45           O  
ANISOU  474  O   GLN A  76    14336  12270  12701     94  -1740    890       O  
ATOM    475  CB  GLN A  76      17.627  47.106  56.959  1.00 95.64           C  
ANISOU  475  CB  GLN A  76    13534  11279  11524    309  -1260    543       C  
ATOM    476  CG  GLN A  76      18.429  46.943  58.241  1.00107.23           C  
ANISOU  476  CG  GLN A  76    15212  12674  12855    399  -1126    420       C  
ATOM    477  CD  GLN A  76      19.543  47.958  58.386  1.00114.56           C  
ANISOU  477  CD  GLN A  76    16280  13576  13671    378  -1232    409       C  
ATOM    478  OE1 GLN A  76      20.435  48.042  57.544  1.00115.21           O  
ANISOU  478  OE1 GLN A  76    16338  13792  13644    246  -1372    419       O  
ATOM    479  NE2 GLN A  76      19.504  48.728  59.468  1.00110.02           N  
ANISOU  479  NE2 GLN A  76    15854  12823  13126    501  -1152    376       N  
ATOM    480  N   SER A  77      15.060  48.080  55.203  1.00109.33           N  
ANISOU  480  N   SER A  77    14857  12880  13802    258  -1547    844       N  
ATOM    481  CA  SER A  77      14.417  48.348  53.922  1.00 99.79           C  
ANISOU  481  CA  SER A  77    13509  11694  12710    137  -1816    999       C  
ATOM    482  C   SER A  77      14.241  49.843  53.701  1.00107.35           C  
ANISOU  482  C   SER A  77    14462  12496  13831    133  -2006   1143       C  
ATOM    483  O   SER A  77      14.457  50.348  52.593  1.00113.49           O  
ANISOU  483  O   SER A  77    15262  13345  14515    -36  -2281   1294       O  
ATOM    484  CB  SER A  77      13.061  47.640  53.859  1.00111.35           C  
ANISOU  484  CB  SER A  77    14760  13065  14481    201  -1785   1006       C  
ATOM    485  OG  SER A  77      12.395  47.914  52.640  1.00141.25           O  
ANISOU  485  OG  SER A  77    18424  16843  18403     84  -2099   1162       O  
ATOM    486  N   THR A  78      13.855  50.568  54.754  1.00108.03           N  
ANISOU  486  N   THR A  78    14531  12358  14157    306  -1861   1094       N  
ATOM    487  CA  THR A  78      13.652  52.008  54.644  1.00110.24           C  
ANISOU  487  CA  THR A  78    14781  12446  14659    324  -2043   1208       C  
ATOM    488  C   THR A  78      14.953  52.723  54.296  1.00103.80           C  
ANISOU  488  C   THR A  78    14156  11735  13550    199  -2184   1272       C  
ATOM    489  O   THR A  78      14.998  53.538  53.367  1.00112.67           O  
ANISOU  489  O   THR A  78    15271  12836  14701     64  -2477   1459       O  
ATOM    490  CB  THR A  78      13.077  52.554  55.951  1.00102.06           C  
ANISOU  490  CB  THR A  78    13700  11158  13919    540  -1801   1079       C  
ATOM    491  OG1 THR A  78      11.833  51.903  56.245  1.00104.77           O  
ANISOU  491  OG1 THR A  78    13841  11395  14572    638  -1637   1018       O  
ATOM    492  CG2 THR A  78      12.851  54.051  55.841  1.00103.47           C  
ANISOU  492  CG2 THR A  78    13819  11108  14387    571  -2005   1174       C  
ATOM    493  N   LEU A  79      16.025  52.428  55.037  1.00108.49           N  
ANISOU  493  N   LEU A  79    14922  12425  13872    231  -1992   1128       N  
ATOM    494  CA  LEU A  79      17.310  53.076  54.789  1.00114.42           C  
ANISOU  494  CA  LEU A  79    15828  13256  14389    118  -2100   1166       C  
ATOM    495  C   LEU A  79      17.856  52.752  53.404  1.00110.37           C  
ANISOU  495  C   LEU A  79    15332  12980  13622   -133  -2278   1281       C  
ATOM    496  O   LEU A  79      18.507  53.600  52.783  1.00113.80           O  
ANISOU  496  O   LEU A  79    15838  13441  13960   -281  -2449   1409       O  
ATOM    497  CB  LEU A  79      18.319  52.658  55.860  1.00104.87           C  
ANISOU  497  CB  LEU A  79    14783  12087  12978    202  -1883    972       C  
ATOM    498  CG  LEU A  79      17.980  53.059  57.296  1.00 98.08           C  
ANISOU  498  CG  LEU A  79    13988  11006  12270    419  -1696    842       C  
ATOM    499  CD1 LEU A  79      18.913  52.365  58.273  1.00106.75           C  
ANISOU  499  CD1 LEU A  79    15277  12159  13125    472  -1525    668       C  
ATOM    500  CD2 LEU A  79      18.028  54.573  57.469  1.00 94.11           C  
ANISOU  500  CD2 LEU A  79    13502  10302  11954    462  -1829    904       C  
ATOM    501  N   ALA A  80      17.604  51.538  52.907  1.00 99.43           N  
ANISOU  501  N   ALA A  80    13891  11766  12121   -195  -2229   1231       N  
ATOM    502  CA  ALA A  80      18.154  51.128  51.617  1.00 99.10           C  
ANISOU  502  CA  ALA A  80    13887  11968  11797   -444  -2353   1289       C  
ATOM    503  C   ALA A  80      17.622  51.991  50.479  1.00108.01           C  
ANISOU  503  C   ALA A  80    15004  13062  12973   -611  -2665   1541       C  
ATOM    504  O   ALA A  80      18.357  52.308  49.536  1.00104.57           O  
ANISOU  504  O   ALA A  80    14679  12779  12275   -847  -2784   1640       O  
ATOM    505  CB  ALA A  80      17.837  49.655  51.358  1.00 94.36           C  
ANISOU  505  CB  ALA A  80    13214  11522  11115   -457  -2254   1165       C  
ATOM    506  N   GLN A  81      16.346  52.378  50.546  1.00116.65           N  
ANISOU  506  N   GLN A  81    15967  13943  14413   -507  -2804   1650       N  
ATOM    507  CA  GLN A  81      15.746  53.168  49.477  1.00120.35           C  
ANISOU  507  CA  GLN A  81    16420  14331  14975   -664  -3167   1909       C  
ATOM    508  C   GLN A  81      16.398  54.537  49.326  1.00115.83           C  
ANISOU  508  C   GLN A  81    15959  13670  14380   -759  -3327   2071       C  
ATOM    509  O   GLN A  81      16.257  55.163  48.270  1.00124.65           O  
ANISOU  509  O   GLN A  81    17139  14780  15444   -970  -3644   2314       O  
ATOM    510  CB  GLN A  81      14.243  53.320  49.725  1.00121.87           C  
ANISOU  510  CB  GLN A  81    16400  14255  15649   -500  -3285   1962       C  
ATOM    511  CG  GLN A  81      13.488  52.000  49.693  1.00119.36           C  
ANISOU  511  CG  GLN A  81    15954  14007  15392   -442  -3180   1845       C  
ATOM    512  CD  GLN A  81      12.055  52.132  50.163  1.00132.35           C  
ANISOU  512  CD  GLN A  81    17349  15359  17580   -252  -3214   1851       C  
ATOM    513  OE1 GLN A  81      11.536  53.239  50.311  1.00146.78           O  
ANISOU  513  OE1 GLN A  81    19086  16924  19759   -185  -3378   1960       O  
ATOM    514  NE2 GLN A  81      11.407  51.000  50.410  1.00125.20           N  
ANISOU  514  NE2 GLN A  81    16308  14478  16783   -164  -3051   1724       N  
ATOM    515  N   MET A  82      17.115  55.012  50.349  1.00107.87           N  
ANISOU  515  N   MET A  82    14995  12586  13406   -622  -3137   1953       N  
ATOM    516  CA  MET A  82      17.830  56.278  50.236  1.00110.29           C  
ANISOU  516  CA  MET A  82    15400  12805  13700   -714  -3281   2093       C  
ATOM    517  C   MET A  82      18.950  56.219  49.204  1.00109.60           C  
ANISOU  517  C   MET A  82    15476  12980  13186  -1020  -3326   2182       C  
ATOM    518  O   MET A  82      19.444  57.270  48.781  1.00110.25           O  
ANISOU  518  O   MET A  82    15646  13006  13238  -1172  -3501   2369       O  
ATOM    519  CB  MET A  82      18.394  56.685  51.599  1.00104.33           C  
ANISOU  519  CB  MET A  82    14666  11915  13060   -498  -3064   1911       C  
ATOM    520  CG  MET A  82      17.336  56.911  52.669  1.00115.72           C  
ANISOU  520  CG  MET A  82    15972  13086  14909   -216  -2978   1805       C  
ATOM    521  SD  MET A  82      17.921  57.952  54.021  1.00117.99           S  
ANISOU  521  SD  MET A  82    16331  13148  15354    -22  -2861   1667       S  
ATOM    522  CE  MET A  82      16.472  57.992  55.073  1.00123.59           C  
ANISOU  522  CE  MET A  82    16867  13582  16509    264  -2701   1516       C  
ATOM    523  N   TYR A  83      19.369  55.016  48.798  1.00104.49           N  
ANISOU  523  N   TYR A  83    14865  12610  12228  -1121  -3156   2043       N  
ATOM    524  CA  TYR A  83      20.346  54.838  47.733  1.00104.31           C  
ANISOU  524  CA  TYR A  83    14980  12854  11798  -1431  -3149   2086       C  
ATOM    525  C   TYR A  83      19.603  54.458  46.457  1.00117.62           C  
ANISOU  525  C   TYR A  83    16707  14660  13322  -1645  -3366   2240       C  
ATOM    526  O   TYR A  83      19.239  53.285  46.284  1.00117.91           O  
ANISOU  526  O   TYR A  83    16691  14834  13275  -1621  -3270   2090       O  
ATOM    527  CB  TYR A  83      21.371  53.761  48.104  1.00112.18           C  
ANISOU  527  CB  TYR A  83    15976  14061  12585  -1410  -2820   1792       C  
ATOM    528  CG  TYR A  83      22.025  53.950  49.459  1.00109.90           C  
ANISOU  528  CG  TYR A  83    15661  13636  12461  -1180  -2638   1620       C  
ATOM    529  CD1 TYR A  83      23.185  54.704  49.593  1.00104.06           C  
ANISOU  529  CD1 TYR A  83    14990  12881  11667  -1262  -2607   1628       C  
ATOM    530  CD2 TYR A  83      21.495  53.358  50.599  1.00107.23           C  
ANISOU  530  CD2 TYR A  83    15243  13179  12321   -898  -2502   1452       C  
ATOM    531  CE1 TYR A  83      23.788  54.876  50.828  1.00100.23           C  
ANISOU  531  CE1 TYR A  83    14500  12254  11329  -1057  -2486   1468       C  
ATOM    532  CE2 TYR A  83      22.093  53.524  51.837  1.00109.34           C  
ANISOU  532  CE2 TYR A  83    15537  13319  12689   -710  -2363   1301       C  
ATOM    533  CZ  TYR A  83      23.239  54.283  51.945  1.00107.56           C  
ANISOU  533  CZ  TYR A  83    15386  13071  12412   -785  -2374   1306       C  
ATOM    534  OH  TYR A  83      23.839  54.451  53.174  1.00114.42           O  
ANISOU  534  OH  TYR A  83    16299  13796  13380   -603  -2278   1153       O  
ATOM    535  N   PRO A  84      19.348  55.396  45.543  1.00110.82           N  
ANISOU  535  N   PRO A  84    15953  13739  12415  -1864  -3685   2541       N  
ATOM    536  CA  PRO A  84      18.500  55.090  44.380  1.00105.99           C  
ANISOU  536  CA  PRO A  84    15406  13193  11674  -2060  -3964   2709       C  
ATOM    537  C   PRO A  84      19.232  54.238  43.352  1.00114.51           C  
ANISOU  537  C   PRO A  84    16648  14634  12227  -2358  -3829   2619       C  
ATOM    538  O   PRO A  84      20.330  54.582  42.910  1.00115.68           O  
ANISOU  538  O   PRO A  84    16945  14944  12064  -2592  -3713   2642       O  
ATOM    539  CB  PRO A  84      18.155  56.475  43.824  1.00119.32           C  
ANISOU  539  CB  PRO A  84    17186  14671  13478  -2213  -4368   3076       C  
ATOM    540  CG  PRO A  84      19.307  57.330  44.236  1.00102.39           C  
ANISOU  540  CG  PRO A  84    15107  12512  11286  -2250  -4226   3089       C  
ATOM    541  CD  PRO A  84      19.747  56.814  45.580  1.00108.98           C  
ANISOU  541  CD  PRO A  84    15789  13333  12285  -1936  -3851   2758       C  
ATOM    542  N   LEU A  85      18.581  53.141  42.941  1.00106.17           N  
ANISOU  542  N   LEU A  85    15555  13692  11093  -2359  -3844   2509       N  
ATOM    543  CA  LEU A  85      19.208  52.126  42.093  1.00102.19           C  
ANISOU  543  CA  LEU A  85    15170  13528  10130  -2595  -3665   2333       C  
ATOM    544  C   LEU A  85      19.800  52.697  40.811  1.00117.14           C  
ANISOU  544  C   LEU A  85    17346  15603  11561  -3019  -3783   2531       C  
ATOM    545  O   LEU A  85      20.751  52.127  40.261  1.00112.35           O  
ANISOU  545  O   LEU A  85    16844  15287  10559  -3236  -3516   2349       O  
ATOM    546  CB  LEU A  85      18.187  51.046  41.732  1.00102.47           C  
ANISOU  546  CB  LEU A  85    15135  13599  10200  -2546  -3779   2247       C  
ATOM    547  CG  LEU A  85      17.665  50.123  42.830  1.00101.94           C  
ANISOU  547  CG  LEU A  85    14808  13426  10497  -2189  -3593   2008       C  
ATOM    548  CD1 LEU A  85      16.875  48.981  42.213  1.00114.62           C  
ANISOU  548  CD1 LEU A  85    16376  15124  12052  -2226  -3694   1913       C  
ATOM    549  CD2 LEU A  85      18.814  49.587  43.664  1.00113.04           C  
ANISOU  549  CD2 LEU A  85    16150  14950  11852  -2072  -3176   1715       C  
ATOM    550  N   GLN A  86      19.247  53.806  40.312  1.00138.85           N  
ANISOU  550  N   GLN A  86    20220  18176  14360  -3156  -4178   2898       N  
ATOM    551  CA  GLN A  86      19.671  54.347  39.022  1.00137.92           C  
ANISOU  551  CA  GLN A  86    20419  18218  13767  -3599  -4338   3138       C  
ATOM    552  C   GLN A  86      21.161  54.653  38.995  1.00136.45           C  
ANISOU  552  C   GLN A  86    20322  18222  13300  -3783  -3978   3048       C  
ATOM    553  O   GLN A  86      21.804  54.539  37.944  1.00144.49           O  
ANISOU  553  O   GLN A  86    21582  19507  13811  -4166  -3880   3067       O  
ATOM    554  CB  GLN A  86      18.874  55.613  38.716  1.00132.32           C  
ANISOU  554  CB  GLN A  86    19798  17213  13264  -3673  -4851   3570       C  
ATOM    555  CG  GLN A  86      17.397  55.370  38.499  1.00159.30           C  
ANISOU  555  CG  GLN A  86    23142  20431  16954  -3564  -5269   3691       C  
ATOM    556  CD  GLN A  86      16.632  56.655  38.271  1.00188.25           C  
ANISOU  556  CD  GLN A  86    26852  23751  20921  -3614  -5803   4104       C  
ATOM    557  OE1 GLN A  86      17.056  57.728  38.703  1.00172.04           O  
ANISOU  557  OE1 GLN A  86    24781  21533  19053  -3586  -5823   4251       O  
ATOM    558  NE2 GLN A  86      15.493  56.555  37.596  1.00188.93           N  
ANISOU  558  NE2 GLN A  86    26984  23701  21100  -3686  -6267   4291       N  
ATOM    559  N   GLU A  87      21.722  55.027  40.136  1.00138.50           N  
ANISOU  559  N   GLU A  87    20393  18344  13886  -3525  -3771   2937       N  
ATOM    560  CA  GLU A  87      23.099  55.476  40.234  1.00141.60           C  
ANISOU  560  CA  GLU A  87    20827  18841  14134  -3666  -3481   2876       C  
ATOM    561  C   GLU A  87      24.069  54.345  40.559  1.00142.27           C  
ANISOU  561  C   GLU A  87    20789  19159  14108  -3606  -3010   2448       C  
ATOM    562  O   GLU A  87      25.284  54.568  40.553  1.00146.45           O  
ANISOU  562  O   GLU A  87    21327  19794  14522  -3746  -2737   2349       O  
ATOM    563  CB  GLU A  87      23.167  56.586  41.285  1.00149.93           C  
ANISOU  563  CB  GLU A  87    21755  19580  15633  -3425  -3577   3001       C  
ATOM    564  CG  GLU A  87      22.387  57.826  40.838  1.00151.89           C  
ANISOU  564  CG  GLU A  87    22125  19585  16003  -3539  -4052   3435       C  
ATOM    565  CD  GLU A  87      22.258  58.890  41.911  1.00164.46           C  
ANISOU  565  CD  GLU A  87    23564  20826  18099  -3263  -4180   3528       C  
ATOM    566  OE1 GLU A  87      22.577  58.604  43.082  1.00170.49           O  
ANISOU  566  OE1 GLU A  87    24136  21522  19120  -2947  -3925   3255       O  
ATOM    567  OE2 GLU A  87      21.812  60.010  41.581  1.00144.91           O1-
ANISOU  567  OE2 GLU A  87    21167  18126  15766  -3367  -4558   3874       O1-
ATOM    568  N   ILE A  88      23.562  53.141  40.820  1.00137.39           N  
ANISOU  568  N   ILE A  88    20042  18603  13556  -3412  -2924   2194       N  
ATOM    569  CA  ILE A  88      24.390  51.963  41.059  1.00137.59           C  
ANISOU  569  CA  ILE A  88    19942  18828  13509  -3360  -2529   1785       C  
ATOM    570  C   ILE A  88      24.623  51.228  39.746  1.00120.96           C  
ANISOU  570  C   ILE A  88    17998  17044  10918  -3713  -2414   1671       C  
ATOM    571  O   ILE A  88      23.679  50.943  38.999  1.00121.11           O  
ANISOU  571  O   ILE A  88    18143  17111  10763  -3819  -2657   1786       O  
ATOM    572  CB  ILE A  88      23.752  51.030  42.107  1.00135.04           C  
ANISOU  572  CB  ILE A  88    19392  18381  13536  -2964  -2493   1569       C  
ATOM    573  CG1 ILE A  88      23.638  51.700  43.487  1.00123.63           C  
ANISOU  573  CG1 ILE A  88    17811  16638  12527  -2626  -2536   1624       C  
ATOM    574  CG2 ILE A  88      24.509  49.712  42.193  1.00136.94           C  
ANISOU  574  CG2 ILE A  88    19513  18818  13699  -2942  -2151   1163       C  
ATOM    575  CD1 ILE A  88      22.487  52.631  43.667  1.00120.79           C  
ANISOU  575  CD1 ILE A  88    17470  16020  12406  -2517  -2884   1935       C  
ATOM    576  N   GLN A  89      25.886  50.903  39.477  1.00128.84           N  
ANISOU  576  N   GLN A  89    18984  18250  11719  -3895  -2042   1421       N  
ATOM    577  CA  GLN A  89      26.306  50.251  38.243  1.00131.80           C  
ANISOU  577  CA  GLN A  89    19514  18948  11616  -4260  -1844   1254       C  
ATOM    578  C   GLN A  89      26.831  48.837  38.449  1.00135.39           C  
ANISOU  578  C   GLN A  89    19762  19551  12130  -4150  -1504    771       C  
ATOM    579  O   GLN A  89      26.567  47.966  37.619  1.00139.23           O  
ANISOU  579  O   GLN A  89    20330  20241  12330  -4310  -1457    603       O  
ATOM    580  CB  GLN A  89      27.369  51.108  37.548  1.00131.12           C  
ANISOU  580  CB  GLN A  89    19598  18996  11225  -4644  -1657   1361       C  
ATOM    581  CG  GLN A  89      26.890  52.529  37.269  1.00140.32           C  
ANISOU  581  CG  GLN A  89    20984  20002  12330  -4789  -2022   1863       C  
ATOM    582  CD  GLN A  89      27.975  53.427  36.708  1.00173.43           C  
ANISOU  582  CD  GLN A  89    25328  24294  16274  -5158  -1830   1993       C  
ATOM    583  OE1 GLN A  89      29.142  53.042  36.636  1.00186.74           O  
ANISOU  583  OE1 GLN A  89    26914  26149  17891  -5279  -1393   1690       O  
ATOM    584  NE2 GLN A  89      27.594  54.637  36.313  1.00173.44           N  
ANISOU  584  NE2 GLN A  89    25553  24169  16178  -5344  -2162   2448       N  
ATOM    585  N   ASN A  90      27.576  48.584  39.527  1.00144.42           N  
ANISOU  585  N   ASN A  90    20644  20580  13648  -3889  -1292    540       N  
ATOM    586  CA  ASN A  90      27.933  47.217  39.901  1.00138.99           C  
ANISOU  586  CA  ASN A  90    19728  19955  13126  -3723  -1055    108       C  
ATOM    587  C   ASN A  90      26.662  46.394  40.069  1.00132.78           C  
ANISOU  587  C   ASN A  90    18907  19109  12436  -3508  -1284    106       C  
ATOM    588  O   ASN A  90      25.833  46.683  40.939  1.00136.15           O  
ANISOU  588  O   ASN A  90    19275  19299  13158  -3220  -1522    297       O  
ATOM    589  CB  ASN A  90      28.762  47.222  41.194  1.00133.24           C  
ANISOU  589  CB  ASN A  90    18752  19033  12839  -3439   -915    -53       C  
ATOM    590  CG  ASN A  90      29.374  45.848  41.534  1.00136.02           C  
ANISOU  590  CG  ASN A  90    18860  19433  13389  -3312   -668   -510       C  
ATOM    591  OD1 ASN A  90      28.745  44.816  41.320  1.00138.82           O  
ANISOU  591  OD1 ASN A  90    19177  19856  13714  -3251   -702   -661       O  
ATOM    592  ND2 ASN A  90      30.597  45.844  42.093  1.00131.42           N  
ANISOU  592  ND2 ASN A  90    18096  18783  13055  -3266   -450   -726       N  
ATOM    593  N   LEU A  91      26.512  45.369  39.226  1.00117.15           N  
ANISOU  593  N   LEU A  91    16957  17340  10217  -3660  -1198   -128       N  
ATOM    594  CA  LEU A  91      25.263  44.617  39.173  1.00111.83           C  
ANISOU  594  CA  LEU A  91    16270  16621   9598  -3515  -1441   -110       C  
ATOM    595  C   LEU A  91      25.023  43.812  40.443  1.00110.46           C  
ANISOU  595  C   LEU A  91    15820  16249   9900  -3110  -1427   -275       C  
ATOM    596  O   LEU A  91      23.868  43.614  40.835  1.00103.15           O  
ANISOU  596  O   LEU A  91    14856  15171   9165  -2904  -1671   -133       O  
ATOM    597  CB  LEU A  91      25.260  43.689  37.957  1.00118.45           C  
ANISOU  597  CB  LEU A  91    17212  17732  10060  -3787  -1344   -359       C  
ATOM    598  CG  LEU A  91      25.298  44.316  36.561  1.00132.28           C  
ANISOU  598  CG  LEU A  91    19311  19706  11243  -4234  -1390   -193       C  
ATOM    599  CD1 LEU A  91      25.343  43.230  35.496  1.00115.02           C  
ANISOU  599  CD1 LEU A  91    17213  17787   8704  -4471  -1251   -524       C  
ATOM    600  CD2 LEU A  91      24.103  45.231  36.342  1.00110.32           C  
ANISOU  600  CD2 LEU A  91    16739  16780   8399  -4254  -1857    286       C  
ATOM    601  N   THR A  92      26.087  43.330  41.091  1.00118.07           N  
ANISOU  601  N   THR A  92    16590  17196  11076  -3002  -1154   -570       N  
ATOM    602  CA  THR A  92      25.901  42.544  42.303  1.00102.89           C  
ANISOU  602  CA  THR A  92    14444  15077   9574  -2646  -1162   -707       C  
ATOM    603  C   THR A  92      25.557  43.426  43.496  1.00108.47           C  
ANISOU  603  C   THR A  92    15145  15517  10553  -2387  -1310   -434       C  
ATOM    604  O   THR A  92      24.918  42.957  44.444  1.00109.84           O  
ANISOU  604  O   THR A  92    15213  15510  11011  -2106  -1396   -426       O  
ATOM    605  CB  THR A  92      27.145  41.695  42.591  1.00 99.95           C  
ANISOU  605  CB  THR A  92    13868  14742   9368  -2624   -876  -1112       C  
ATOM    606  OG1 THR A  92      26.789  40.605  43.447  1.00116.65           O  
ANISOU  606  OG1 THR A  92    15800  16707  11814  -2343   -923  -1268       O  
ATOM    607  CG2 THR A  92      28.232  42.514  43.270  1.00110.47           C  
ANISOU  607  CG2 THR A  92    15155  15964  10856  -2589   -761  -1091       C  
ATOM    608  N   VAL A  93      25.959  44.699  43.462  1.00109.79           N  
ANISOU  608  N   VAL A  93    15429  15652  10635  -2489  -1334   -216       N  
ATOM    609  CA  VAL A  93      25.476  45.654  44.452  1.00104.30           C  
ANISOU  609  CA  VAL A  93    14756  14705  10169  -2268  -1506     56       C  
ATOM    610  C   VAL A  93      24.001  45.951  44.221  1.00111.01           C  
ANISOU  610  C   VAL A  93    15687  15475  11018  -2221  -1785    331       C  
ATOM    611  O   VAL A  93      23.211  46.015  45.171  1.00107.46           O  
ANISOU  611  O   VAL A  93    15166  14810  10853  -1950  -1892    427       O  
ATOM    612  CB  VAL A  93      26.322  46.941  44.414  1.00 91.20           C  
ANISOU  612  CB  VAL A  93    13188  13019   8444  -2403  -1474    206       C  
ATOM    613  CG1 VAL A  93      25.706  48.008  45.307  1.00 89.89           C  
ANISOU  613  CG1 VAL A  93    13061  12591   8501  -2194  -1680    489       C  
ATOM    614  CG2 VAL A  93      27.757  46.653  44.831  1.00 90.93           C  
ANISOU  614  CG2 VAL A  93    13024  13000   8524  -2403  -1218    -75       C  
ATOM    615  N   LYS A  94      23.602  46.118  42.956  1.00118.38           N  
ANISOU  615  N   LYS A  94    16769  16568  11640  -2493  -1910    453       N  
ATOM    616  CA  LYS A  94      22.221  46.484  42.659  1.00107.39           C  
ANISOU  616  CA  LYS A  94    15448  15070  10286  -2469  -2233    732       C  
ATOM    617  C   LYS A  94      21.250  45.370  43.033  1.00105.16           C  
ANISOU  617  C   LYS A  94    15013  14716  10228  -2253  -2286    613       C  
ATOM    618  O   LYS A  94      20.140  45.647  43.497  1.00109.84           O  
ANISOU  618  O   LYS A  94    15548  15100  11086  -2071  -2486    798       O  
ATOM    619  CB  LYS A  94      22.067  46.849  41.181  1.00107.86           C  
ANISOU  619  CB  LYS A  94    15739  15312   9930  -2840  -2394    891       C  
ATOM    620  CG  LYS A  94      20.727  47.513  40.872  1.00112.82           C  
ANISOU  620  CG  LYS A  94    16452  15772  10643  -2835  -2804   1239       C  
ATOM    621  CD  LYS A  94      20.465  47.666  39.380  1.00123.11           C  
ANISOU  621  CD  LYS A  94    18017  17249  11509  -3211  -3021   1390       C  
ATOM    622  CE  LYS A  94      21.470  48.587  38.709  1.00132.70           C  
ANISOU  622  CE  LYS A  94    19458  18606  12355  -3543  -2937   1516       C  
ATOM    623  NZ  LYS A  94      20.944  49.083  37.404  1.00115.75           N  
ANISOU  623  NZ  LYS A  94    17618  16535   9826  -3896  -3268   1801       N  
ATOM    624  N   LEU A  95      21.642  44.107  42.835  1.00102.79           N  
ANISOU  624  N   LEU A  95    14628  14569   9860  -2274  -2105    298       N  
ATOM    625  CA  LEU A  95      20.771  42.993  43.202  1.00 95.01           C  
ANISOU  625  CA  LEU A  95    13486  13506   9107  -2078  -2152    183       C  
ATOM    626  C   LEU A  95      20.440  43.022  44.689  1.00 92.45           C  
ANISOU  626  C   LEU A  95    13015  12925   9185  -1739  -2107    220       C  
ATOM    627  O   LEU A  95      19.267  43.021  45.080  1.00 99.26           O  
ANISOU  627  O   LEU A  95    13808  13615  10291  -1577  -2256    364       O  
ATOM    628  CB  LEU A  95      21.419  41.659  42.828  1.00 91.48           C  
ANISOU  628  CB  LEU A  95    12955  13244   8560  -2150  -1952   -188       C  
ATOM    629  CG  LEU A  95      21.494  41.267  41.354  1.00 94.59           C  
ANISOU  629  CG  LEU A  95    13481  13897   8561  -2470  -1979   -301       C  
ATOM    630  CD1 LEU A  95      22.085  39.874  41.217  1.00 94.55           C  
ANISOU  630  CD1 LEU A  95    13332  14019   8574  -2475  -1763   -716       C  
ATOM    631  CD2 LEU A  95      20.116  41.328  40.720  1.00103.75           C  
ANISOU  631  CD2 LEU A  95    14726  15010   9683  -2515  -2318    -81       C  
ATOM    632  N   GLN A  96      21.472  43.041  45.536  1.00102.39           N  
ANISOU  632  N   GLN A  96    14232  14149  10524  -1639  -1900     83       N  
ATOM    633  CA  GLN A  96      21.252  43.061  46.979  1.00 93.61           C  
ANISOU  633  CA  GLN A  96    13036  12802   9729  -1344  -1848    107       C  
ATOM    634  C   GLN A  96      20.460  44.295  47.393  1.00 97.32           C  
ANISOU  634  C   GLN A  96    13563  13082  10331  -1248  -1998    400       C  
ATOM    635  O   GLN A  96      19.500  44.200  48.166  1.00101.97           O  
ANISOU  635  O   GLN A  96    14075  13486  11182  -1041  -2029    473       O  
ATOM    636  CB  GLN A  96      22.592  43.016  47.709  1.00106.27           C  
ANISOU  636  CB  GLN A  96    14625  14391  11362  -1293  -1660    -71       C  
ATOM    637  CG  GLN A  96      23.514  41.884  47.294  1.00107.38           C  
ANISOU  637  CG  GLN A  96    14674  14690  11435  -1394  -1511   -391       C  
ATOM    638  CD  GLN A  96      24.898  42.022  47.902  1.00112.29           C  
ANISOU  638  CD  GLN A  96    15267  15271  12126  -1372  -1369   -549       C  
ATOM    639  OE1 GLN A  96      25.046  42.131  49.120  1.00 94.96           O  
ANISOU  639  OE1 GLN A  96    13068  12878  10133  -1165  -1371   -526       O  
ATOM    640  NE2 GLN A  96      25.921  42.021  47.053  1.00100.81           N  
ANISOU  640  NE2 GLN A  96    13798  13996  10508  -1596  -1244   -716       N  
ATOM    641  N   LEU A  97      20.859  45.465  46.887  1.00 97.35           N  
ANISOU  641  N   LEU A  97    13691  13117  10178  -1404  -2080    563       N  
ATOM    642  CA  LEU A  97      20.129  46.698  47.166  1.00 98.65           C  
ANISOU  642  CA  LEU A  97    13898  13086  10499  -1330  -2256    838       C  
ATOM    643  C   LEU A  97      18.664  46.576  46.770  1.00112.50           C  
ANISOU  643  C   LEU A  97    15589  14750  12404  -1299  -2473    987       C  
ATOM    644  O   LEU A  97      17.766  46.966  47.525  1.00116.99           O  
ANISOU  644  O   LEU A  97    16073  15089  13291  -1097  -2528   1091       O  
ATOM    645  CB  LEU A  97      20.784  47.867  46.428  1.00 96.96           C  
ANISOU  645  CB  LEU A  97    13834  12940  10068  -1561  -2350   1004       C  
ATOM    646  CG  LEU A  97      21.374  48.994  47.274  1.00 94.52           C  
ANISOU  646  CG  LEU A  97    13560  12466   9885  -1462  -2317   1084       C  
ATOM    647  CD1 LEU A  97      21.652  50.208  46.407  1.00103.66           C  
ANISOU  647  CD1 LEU A  97    14858  13652  10877  -1704  -2486   1326       C  
ATOM    648  CD2 LEU A  97      20.426  49.355  48.403  1.00101.37           C  
ANISOU  648  CD2 LEU A  97    14349  13060  11109  -1171  -2365   1157       C  
ATOM    649  N   GLN A  98      18.406  46.029  45.581  1.00115.96           N  
ANISOU  649  N   GLN A  98    16065  15359  12634  -1504  -2597    981       N  
ATOM    650  CA  GLN A  98      17.035  45.901  45.101  1.00119.32           C  
ANISOU  650  CA  GLN A  98    16431  15686  13218  -1495  -2858   1124       C  
ATOM    651  C   GLN A  98      16.255  44.884  45.926  1.00121.55           C  
ANISOU  651  C   GLN A  98    16512  15848  13824  -1249  -2753    991       C  
ATOM    652  O   GLN A  98      15.068  45.087  46.209  1.00125.18           O  
ANISOU  652  O   GLN A  98    16851  16096  14617  -1115  -2891   1121       O  
ATOM    653  CB  GLN A  98      17.045  45.517  43.623  1.00119.61           C  
ANISOU  653  CB  GLN A  98    16599  15946  12901  -1796  -3025   1129       C  
ATOM    654  CG  GLN A  98      15.690  45.450  42.955  1.00117.18           C  
ANISOU  654  CG  GLN A  98    16262  15532  12730  -1832  -3373   1297       C  
ATOM    655  CD  GLN A  98      15.807  45.106  41.484  1.00132.45           C  
ANISOU  655  CD  GLN A  98    18390  17700  14236  -2160  -3548   1292       C  
ATOM    656  OE1 GLN A  98      16.886  45.208  40.898  1.00127.19           O  
ANISOU  656  OE1 GLN A  98    17903  17267  13156  -2391  -3408   1214       O  
ATOM    657  NE2 GLN A  98      14.699  44.699  40.877  1.00150.09           N  
ANISOU  657  NE2 GLN A  98    20593  19865  16570  -2192  -3848   1366       N  
ATOM    658  N   ALA A  99      16.907  43.790  46.328  1.00119.73           N  
ANISOU  658  N   ALA A  99    16230  15728  13532  -1194  -2510    733       N  
ATOM    659  CA  ALA A  99      16.248  42.783  47.153  1.00117.67           C  
ANISOU  659  CA  ALA A  99    15797  15349  13562   -981  -2398    620       C  
ATOM    660  C   ALA A  99      15.841  43.328  48.514  1.00100.88           C  
ANISOU  660  C   ALA A  99    13611  12978  11742   -735  -2280    698       C  
ATOM    661  O   ALA A  99      14.949  42.762  49.156  1.00102.21           O  
ANISOU  661  O   ALA A  99    13639  13000  12197   -573  -2217    682       O  
ATOM    662  CB  ALA A  99      17.160  41.569  47.336  1.00109.71           C  
ANISOU  662  CB  ALA A  99    14760  14486  12437   -984  -2190    339       C  
ATOM    663  N   LEU A 100      16.471  44.409  48.968  1.00 96.11           N  
ANISOU  663  N   LEU A 100    13114  12321  11083   -714  -2236    770       N  
ATOM    664  CA  LEU A 100      16.155  45.019  50.250  1.00102.92           C  
ANISOU  664  CA  LEU A 100    13954  12956  12196   -496  -2116    817       C  
ATOM    665  C   LEU A 100      15.245  46.234  50.119  1.00109.03           C  
ANISOU  665  C   LEU A 100    14691  13541  13195   -466  -2301   1035       C  
ATOM    666  O   LEU A 100      14.771  46.745  51.139  1.00111.96           O  
ANISOU  666  O   LEU A 100    15013  13701  13824   -281  -2194   1055       O  
ATOM    667  CB  LEU A 100      17.452  45.414  50.970  1.00106.75           C  
ANISOU  667  CB  LEU A 100    14574  13464  12521   -467  -1961    728       C  
ATOM    668  CG  LEU A 100      17.425  45.574  52.489  1.00 92.02           C  
ANISOU  668  CG  LEU A 100    12735  11408  10820   -243  -1770    676       C  
ATOM    669  CD1 LEU A 100      17.131  44.236  53.148  1.00 92.61           C  
ANISOU  669  CD1 LEU A 100    12745  11468  10976   -139  -1606    539       C  
ATOM    670  CD2 LEU A 100      18.745  46.143  52.983  1.00 90.43           C  
ANISOU  670  CD2 LEU A 100    12683  11222  10456   -250  -1710    614       C  
ATOM    671  N   GLN A 101      14.982  46.696  48.895  1.00126.82           N  
ANISOU  671  N   GLN A 101    16971  15851  15363   -653  -2583   1192       N  
ATOM    672  CA  GLN A 101      14.164  47.876  48.637  1.00123.76           C  
ANISOU  672  CA  GLN A 101    16545  15262  15216   -652  -2835   1419       C  
ATOM    673  C   GLN A 101      12.718  47.522  48.301  1.00123.87           C  
ANISOU  673  C   GLN A 101    16368  15127  15569   -605  -3018   1495       C  
ATOM    674  O   GLN A 101      12.055  48.261  47.565  1.00142.11           O  
ANISOU  674  O   GLN A 101    18655  17317  18022   -692  -3349   1697       O  
ATOM    675  CB  GLN A 101      14.776  48.701  47.505  1.00114.54           C  
ANISOU  675  CB  GLN A 101    15554  14215  13752   -911  -3082   1588       C  
ATOM    676  CG  GLN A 101      15.923  49.599  47.924  1.00119.31           C  
ANISOU  676  CG  GLN A 101    16296  14837  14200   -931  -2973   1595       C  
ATOM    677  CD  GLN A 101      16.351  50.540  46.816  1.00116.91           C  
ANISOU  677  CD  GLN A 101    16155  14605  13658  -1200  -3231   1811       C  
ATOM    678  OE1 GLN A 101      15.743  50.575  45.745  1.00117.04           O  
ANISOU  678  OE1 GLN A 101    16209  14648  13614  -1375  -3518   1972       O  
ATOM    679  NE2 GLN A 101      17.411  51.301  47.062  1.00112.85           N  
ANISOU  679  NE2 GLN A 101    15754  14117  13005  -1250  -3144   1825       N  
ATOM    680  N   GLN A 102      12.216  46.408  48.825  1.00126.61           N  
ANISOU  680  N   GLN A 102    16573  15457  16075   -476  -2832   1346       N  
ATOM    681  CA  GLN A 102      10.878  45.929  48.495  1.00138.70           C  
ANISOU  681  CA  GLN A 102    17895  16847  17956   -437  -2992   1394       C  
ATOM    682  C   GLN A 102       9.874  46.580  49.439  1.00144.23           C  
ANISOU  682  C   GLN A 102    18398  17229  19174   -222  -2911   1438       C  
ATOM    683  O   GLN A 102       9.827  46.251  50.630  1.00133.32           O  
ANISOU  683  O   GLN A 102    16958  15776  17921    -46  -2562   1302       O  
ATOM    684  CB  GLN A 102      10.814  44.407  48.583  1.00126.91           C  
ANISOU  684  CB  GLN A 102    16327  15476  16417   -414  -2828   1214       C  
ATOM    685  CG  GLN A 102      11.792  43.699  47.662  1.00136.69           C  
ANISOU  685  CG  GLN A 102    17731  17020  17186   -619  -2879   1115       C  
ATOM    686  CD  GLN A 102      11.485  43.921  46.192  1.00162.53           C  
ANISOU  686  CD  GLN A 102    21077  20370  20308   -848  -3268   1250       C  
ATOM    687  OE1 GLN A 102      10.327  44.076  45.802  1.00156.11           O  
ANISOU  687  OE1 GLN A 102    20132  19378  19805   -838  -3535   1383       O  
ATOM    688  NE2 GLN A 102      12.526  43.937  45.367  1.00158.86           N  
ANISOU  688  NE2 GLN A 102    20828  20162  19368  -1070  -3303   1212       N  
ATOM    689  N   ASN A 103       9.074  47.508  48.904  1.00150.70           N  
ANISOU  689  N   ASN A 103    19120  17843  20294   -249  -3235   1622       N  
ATOM    690  CA  ASN A 103       8.034  48.148  49.702  1.00141.04           C  
ANISOU  690  CA  ASN A 103    17659  16287  19642    -51  -3170   1638       C  
ATOM    691  C   ASN A 103       7.038  47.124  50.226  1.00137.42           C  
ANISOU  691  C   ASN A 103    16949  15719  19545     83  -2966   1516       C  
ATOM    692  O   ASN A 103       6.684  47.131  51.410  1.00136.39           O  
ANISOU  692  O   ASN A 103    16704  15443  19677    266  -2609   1396       O  
ATOM    693  CB  ASN A 103       7.310  49.206  48.874  1.00143.58           C  
ANISOU  693  CB  ASN A 103    17890  16384  20279   -123  -3632   1862       C  
ATOM    694  CG  ASN A 103       8.256  50.162  48.187  1.00155.75           C  
ANISOU  694  CG  ASN A 103    19696  18038  21443   -305  -3878   2025       C  
ATOM    695  OD1 ASN A 103       9.469  50.119  48.392  1.00162.90           O  
ANISOU  695  OD1 ASN A 103    20828  19177  21889   -362  -3673   1953       O  
ATOM    696  ND2 ASN A 103       7.696  51.042  47.373  1.00165.43           N  
ANISOU  696  ND2 ASN A 103    20887  19076  22894   -406  -4335   2254       N  
ATOM    697  N   GLY A 104       6.565  46.242  49.349  1.00124.14           N  
ANISOU  697  N   GLY A 104    15189  14101  17879    -19  -3184   1542       N  
ATOM    698  CA  GLY A 104       5.623  45.223  49.774  1.00115.56           C  
ANISOU  698  CA  GLY A 104    13849  12904  17156     91  -3011   1438       C  
ATOM    699  C   GLY A 104       4.281  45.831  50.124  1.00127.49           C  
ANISOU  699  C   GLY A 104    15032  14042  19368    230  -3055   1485       C  
ATOM    700  O   GLY A 104       3.834  46.813  49.519  1.00139.19           O  
ANISOU  700  O   GLY A 104    16442  15339  21104    193  -3426   1639       O  
ATOM    701  N   SER A 105       3.625  45.239  51.124  1.00122.95           N  
ANISOU  701  N   SER A 105    14247  13337  19132    384  -2670   1348       N  
ATOM    702  CA  SER A 105       2.347  45.758  51.598  1.00140.61           C  
ANISOU  702  CA  SER A 105    16131  15207  22086    527  -2609   1338       C  
ATOM    703  C   SER A 105       2.471  47.156  52.194  1.00147.82           C  
ANISOU  703  C   SER A 105    17065  15955  23146    622  -2526   1340       C  
ATOM    704  O   SER A 105       1.456  47.846  52.341  1.00141.70           O  
ANISOU  704  O   SER A 105    15989  14848  23005    720  -2589   1346       O  
ATOM    705  CB  SER A 105       1.750  44.800  52.631  1.00131.71           C  
ANISOU  705  CB  SER A 105    14817  14010  21215    644  -2124   1177       C  
ATOM    706  OG  SER A 105       0.517  45.284  53.131  1.00131.42           O  
ANISOU  706  OG  SER A 105    14414  13616  21902    775  -1997   1133       O  
ATOM    707  N   SER A 106       3.689  47.586  52.538  1.00150.85           N  
ANISOU  707  N   SER A 106    17776  16541  22999    598  -2397   1320       N  
ATOM    708  CA  SER A 106       3.880  48.907  53.131  1.00143.28           C  
ANISOU  708  CA  SER A 106    16854  15427  22160    689  -2323   1306       C  
ATOM    709  C   SER A 106       3.513  50.023  52.163  1.00150.34           C  
ANISOU  709  C   SER A 106    17651  16124  23349    625  -2852   1500       C  
ATOM    710  O   SER A 106       3.107  51.108  52.596  1.00158.03           O  
ANISOU  710  O   SER A 106    18482  16823  24737    734  -2848   1482       O  
ATOM    711  CB  SER A 106       5.328  49.069  53.594  1.00140.45           C  
ANISOU  711  CB  SER A 106    16873  15328  21163    657  -2136   1257       C  
ATOM    712  OG  SER A 106       5.757  47.937  54.331  1.00152.27           O  
ANISOU  712  OG  SER A 106    18494  17015  22348    682  -1748   1113       O  
ATOM    713  N   VAL A 107       3.640  49.781  50.857  1.00141.37           N  
ANISOU  713  N   VAL A 107    16600  15107  22007    439  -3320   1682       N  
ATOM    714  CA  VAL A 107       3.271  50.768  49.852  1.00130.60           C  
ANISOU  714  CA  VAL A 107    15185  13550  20887    340  -3885   1908       C  
ATOM    715  C   VAL A 107       1.807  51.172  49.949  1.00128.94           C  
ANISOU  715  C   VAL A 107    14545  12906  21543    470  -4036   1911       C  
ATOM    716  O   VAL A 107       1.395  52.157  49.327  1.00132.44           O  
ANISOU  716  O   VAL A 107    14896  13096  22329    426  -4502   2087       O  
ATOM    717  CB  VAL A 107       3.586  50.227  48.438  1.00132.76           C  
ANISOU  717  CB  VAL A 107    15655  14047  20739     92  -4329   2084       C  
ATOM    718  CG1 VAL A 107       2.463  49.311  47.945  1.00128.77           C  
ANISOU  718  CG1 VAL A 107    14890  13422  20614     88  -4515   2083       C  
ATOM    719  CG2 VAL A 107       3.847  51.373  47.469  1.00141.79           C  
ANISOU  719  CG2 VAL A 107    16960  15122  21791    -80  -4857   2346       C  
ATOM    720  N   LEU A 108       1.016  50.437  50.720  1.00129.73           N  
ANISOU  720  N   LEU A 108    14369  12895  22029    618  -3656   1723       N  
ATOM    721  CA  LEU A 108      -0.404  50.686  50.905  1.00139.68           C  
ANISOU  721  CA  LEU A 108    15166  13735  24171    750  -3713   1677       C  
ATOM    722  C   LEU A 108      -0.635  51.514  52.164  1.00138.94           C  
ANISOU  722  C   LEU A 108    14910  13415  24465    949  -3272   1481       C  
ATOM    723  O   LEU A 108       0.208  51.566  53.063  1.00143.96           O  
ANISOU  723  O   LEU A 108    15792  14246  24661   1000  -2829   1347       O  
ATOM    724  CB  LEU A 108      -1.159  49.360  51.006  1.00136.74           C  
ANISOU  724  CB  LEU A 108    14569  13369  24019    777  -3518   1575       C  
ATOM    725  CG  LEU A 108      -1.657  48.769  49.688  1.00132.16           C  
ANISOU  725  CG  LEU A 108    13920  12770  23525    629  -4088   1749       C  
ATOM    726  CD1 LEU A 108      -2.526  47.551  49.946  1.00129.82           C  
ANISOU  726  CD1 LEU A 108    13330  12407  23590    688  -3861   1623       C  
ATOM    727  CD2 LEU A 108      -2.416  49.816  48.885  1.00139.28           C  
ANISOU  727  CD2 LEU A 108    14615  13301  25004    600  -4710   1935       C  
ATOM    728  N   SER A 109      -1.792  52.169  52.217  1.00136.19           N  
ANISOU  728  N   SER A 109    14143  12636  24969   1058  -3410   1452       N  
ATOM    729  CA  SER A 109      -2.196  52.844  53.440  1.00137.02           C  
ANISOU  729  CA  SER A 109    14031  12495  25536   1254  -2931   1206       C  
ATOM    730  C   SER A 109      -2.264  51.839  54.584  1.00143.36           C  
ANISOU  730  C   SER A 109    14833  13451  26188   1336  -2205    959       C  
ATOM    731  O   SER A 109      -2.595  50.666  54.386  1.00141.75           O  
ANISOU  731  O   SER A 109    14560  13356  25942   1286  -2134    968       O  
ATOM    732  CB  SER A 109      -3.551  53.525  53.255  1.00149.58           C  
ANISOU  732  CB  SER A 109    15095  13570  28170   1355  -3188   1183       C  
ATOM    733  OG  SER A 109      -4.614  52.623  53.512  1.00147.01           O  
ANISOU  733  OG  SER A 109    14398  13100  28360   1418  -2933   1049       O  
ATOM    734  N   GLU A 110      -1.923  52.304  55.790  1.00168.01           N  
ANISOU  734  N   GLU A 110    21500  15278  27057   2011   -492  -3839       N  
ATOM    735  CA  GLU A 110      -1.960  51.425  56.957  1.00166.34           C  
ANISOU  735  CA  GLU A 110    21204  15703  26295   1978   -302  -4313       C  
ATOM    736  C   GLU A 110      -3.331  50.781  57.109  1.00157.71           C  
ANISOU  736  C   GLU A 110    19945  14972  25007   2303   -146  -4447       C  
ATOM    737  O   GLU A 110      -3.437  49.572  57.336  1.00147.90           O  
ANISOU  737  O   GLU A 110    18670  14355  23172   2237    -12  -4379       O  
ATOM    738  CB  GLU A 110      -1.589  52.197  58.222  1.00164.44           C  
ANISOU  738  CB  GLU A 110    20999  15269  26211   1888   -280  -5026       C  
ATOM    739  CG  GLU A 110      -0.175  52.741  58.247  1.00169.27           C  
ANISOU  739  CG  GLU A 110    21731  15601  26985   1518   -423  -4996       C  
ATOM    740  CD  GLU A 110       0.210  53.256  59.617  1.00190.07           C  
ANISOU  740  CD  GLU A 110    24395  18202  29622   1409   -412  -5753       C  
ATOM    741  OE1 GLU A 110      -0.400  52.807  60.611  1.00189.35           O  
ANISOU  741  OE1 GLU A 110    24272  18535  29136   1526   -259  -6232       O  
ATOM    742  OE2 GLU A 110       1.112  54.115  59.701  1.00198.61           O1-
ANISOU  742  OE2 GLU A 110    25539  18843  31080   1175   -546  -5883       O1-
ATOM    743  N   ASP A 111      -4.394  51.576  56.961  1.00143.23           N  
ANISOU  743  N   ASP A 111    17988  12720  23711   2654   -181  -4644       N  
ATOM    744  CA  ASP A 111      -5.750  51.045  57.071  1.00138.06           C  
ANISOU  744  CA  ASP A 111    17096  12392  22969   2965    -24  -4837       C  
ATOM    745  C   ASP A 111      -5.985  49.906  56.083  1.00138.41           C  
ANISOU  745  C   ASP A 111    17108  12851  22631   2965    -42  -4203       C  
ATOM    746  O   ASP A 111      -6.605  48.892  56.427  1.00128.73           O  
ANISOU  746  O   ASP A 111    15750  12196  20967   2989    167  -4320       O  
ATOM    747  CB  ASP A 111      -6.764  52.165  56.844  1.00129.80           C  
ANISOU  747  CB  ASP A 111    15880  10733  22706   3382   -157  -5099       C  
ATOM    748  CG  ASP A 111      -6.665  53.258  57.887  1.00160.50           C  
ANISOU  748  CG  ASP A 111    19761  14254  26969   3401   -112  -5813       C  
ATOM    749  OD1 ASP A 111      -5.706  53.230  58.688  1.00165.67           O  
ANISOU  749  OD1 ASP A 111    20575  15034  27339   3089    -20  -6089       O  
ATOM    750  OD2 ASP A 111      -7.541  54.149  57.901  1.00169.27           O1-
ANISOU  750  OD2 ASP A 111    20717  15092  28505   3653   -192  -5982       O1-
ATOM    751  N   LYS A 112      -5.494  50.056  54.851  1.00136.96           N  
ANISOU  751  N   LYS A 112    17059  12391  22588   2902   -276  -3541       N  
ATOM    752  CA  LYS A 112      -5.648  49.010  53.845  1.00122.69           C  
ANISOU  752  CA  LYS A 112    15233  10971  20411   2884   -305  -2962       C  
ATOM    753  C   LYS A 112      -4.701  47.842  54.099  1.00126.87           C  
ANISOU  753  C   LYS A 112    15842  12076  20286   2542   -172  -2834       C  
ATOM    754  O   LYS A 112      -5.125  46.681  54.097  1.00124.03           O  
ANISOU  754  O   LYS A 112    15390  12242  19494   2557    -55  -2763       O  
ATOM    755  CB  LYS A 112      -5.420  49.592  52.449  1.00124.18           C  
ANISOU  755  CB  LYS A 112    15579  10697  20907   2887   -587  -2320       C  
ATOM    756  CG  LYS A 112      -6.485  50.585  52.028  1.00126.59           C  
ANISOU  756  CG  LYS A 112    15820  10422  21857   3288   -830  -2339       C  
ATOM    757  CD  LYS A 112      -6.254  51.081  50.613  1.00129.01           C  
ANISOU  757  CD  LYS A 112    16374  10292  22353   3241  -1149  -1610       C  
ATOM    758  CE  LYS A 112      -7.447  51.881  50.117  1.00134.25           C  
ANISOU  758  CE  LYS A 112    16972  10414  23624   3704  -1490  -1572       C  
ATOM    759  NZ  LYS A 112      -7.267  52.330  48.709  1.00127.74           N  
ANISOU  759  NZ  LYS A 112    16470   9169  22897   3633  -1852   -790       N  
ATOM    760  N   SER A 113      -3.414  48.132  54.317  1.00138.74           N  
ANISOU  760  N   SER A 113    17501  13460  21754   2235   -214  -2823       N  
ATOM    761  CA  SER A 113      -2.461  47.075  54.641  1.00133.96           C  
ANISOU  761  CA  SER A 113    16936  13352  20609   1952   -156  -2775       C  
ATOM    762  C   SER A 113      -2.868  46.321  55.900  1.00116.02           C  
ANISOU  762  C   SER A 113    14635  11534  17912   1970      2  -3231       C  
ATOM    763  O   SER A 113      -2.490  45.157  56.076  1.00 99.25           O  
ANISOU  763  O   SER A 113    12543   9873  15294   1828     18  -3121       O  
ATOM    764  CB  SER A 113      -1.057  47.664  54.798  1.00135.99           C  
ANISOU  764  CB  SER A 113    17299  13369  21002   1639   -247  -2816       C  
ATOM    765  OG  SER A 113      -0.884  48.249  56.077  1.00132.61           O  
ANISOU  765  OG  SER A 113    16909  12819  20659   1604   -226  -3406       O  
ATOM    766  N   LYS A 114      -3.639  46.962  56.782  1.00111.68           N  
ANISOU  766  N   LYS A 114    14038  10850  17543   2126    118  -3754       N  
ATOM    767  CA  LYS A 114      -4.186  46.263  57.938  1.00117.85           C  
ANISOU  767  CA  LYS A 114    14816  12099  17864   2100    328  -4181       C  
ATOM    768  C   LYS A 114      -5.408  45.429  57.575  1.00114.74           C  
ANISOU  768  C   LYS A 114    14256  12036  17304   2273    484  -4050       C  
ATOM    769  O   LYS A 114      -5.668  44.411  58.225  1.00116.75           O  
ANISOU  769  O   LYS A 114    14557  12778  17025   2142    644  -4155       O  
ATOM    770  CB  LYS A 114      -4.532  47.261  59.046  1.00121.15           C  
ANISOU  770  CB  LYS A 114    15221  12306  18503   2159    451  -4877       C  
ATOM    771  CG  LYS A 114      -3.341  47.646  59.918  1.00134.00           C  
ANISOU  771  CG  LYS A 114    17046  13866  20001   1891    346  -5168       C  
ATOM    772  CD  LYS A 114      -3.495  49.037  60.521  1.00144.70           C  
ANISOU  772  CD  LYS A 114    18369  14749  21860   1987    371  -5756       C  
ATOM    773  CE  LYS A 114      -4.779  49.169  61.322  1.00137.29           C  
ANISOU  773  CE  LYS A 114    17285  13985  20892   2170    671  -6360       C  
ATOM    774  NZ  LYS A 114      -4.925  50.539  61.891  1.00121.19           N  
ANISOU  774  NZ  LYS A 114    15185  11458  19406   2294    685  -7004       N  
ATOM    775  N   ARG A 115      -6.168  45.831  56.550  1.00121.44           N  
ANISOU  775  N   ARG A 115    14928  12618  18597   2547    414  -3814       N  
ATOM    776  CA  ARG A 115      -7.282  44.999  56.103  1.00120.07           C  
ANISOU  776  CA  ARG A 115    14559  12768  18295   2702    521  -3679       C  
ATOM    777  C   ARG A 115      -6.793  43.794  55.312  1.00113.23           C  
ANISOU  777  C   ARG A 115    13775  12230  17018   2547    430  -3116       C  
ATOM    778  O   ARG A 115      -7.242  42.666  55.547  1.00107.48           O  
ANISOU  778  O   ARG A 115    13008  11953  15875   2470    572  -3108       O  
ATOM    779  CB  ARG A 115      -8.273  45.802  55.264  1.00112.69           C  
ANISOU  779  CB  ARG A 115    13396  11442  17981   3075    397  -3629       C  
ATOM    780  CG  ARG A 115      -9.428  44.929  54.799  1.00 98.85           C  
ANISOU  780  CG  ARG A 115    11391  10047  16120   3230    482  -3533       C  
ATOM    781  CD  ARG A 115     -10.563  44.896  55.806  1.00113.51           C  
ANISOU  781  CD  ARG A 115    12976  12143  18008   3327    804  -4196       C  
ATOM    782  NE  ARG A 115     -11.222  43.593  55.822  1.00124.49           N  
ANISOU  782  NE  ARG A 115    14240  14097  18962   3213   1010  -4134       N  
ATOM    783  CZ  ARG A 115     -12.373  43.316  55.226  1.00132.09           C  
ANISOU  783  CZ  ARG A 115    14865  15168  20154   3439   1016  -4133       C  
ATOM    784  NH1 ARG A 115     -13.031  44.231  54.532  1.00133.20           N  
ANISOU  784  NH1 ARG A 115    14759  14893  20957   3835    778  -4169       N  
ATOM    785  NH2 ARG A 115     -12.879  42.091  55.331  1.00113.06           N  
ANISOU  785  NH2 ARG A 115    12367  13270  17322   3261   1228  -4095       N  
ATOM    786  N   LEU A 116      -5.888  44.016  54.352  1.00107.97           N  
ANISOU  786  N   LEU A 116    13215  11334  16472   2479    209  -2663       N  
ATOM    787  CA  LEU A 116      -5.347  42.907  53.569  1.00 97.30           C  
ANISOU  787  CA  LEU A 116    11911  10295  14763   2333    136  -2203       C  
ATOM    788  C   LEU A 116      -4.815  41.806  54.475  1.00106.66           C  
ANISOU  788  C   LEU A 116    13203  11902  15420   2105    213  -2343       C  
ATOM    789  O   LEU A 116      -5.072  40.619  54.242  1.00 99.69           O  
ANISOU  789  O   LEU A 116    12295  11375  14207   2068    240  -2163       O  
ATOM    790  CB  LEU A 116      -4.248  43.419  52.634  1.00 92.10           C  
ANISOU  790  CB  LEU A 116    11360   9357  14278   2200    -42  -1823       C  
ATOM    791  CG  LEU A 116      -3.479  42.393  51.797  1.00 98.91           C  
ANISOU  791  CG  LEU A 116    12240  10527  14814   2021    -97  -1430       C  
ATOM    792  CD1 LEU A 116      -4.421  41.581  50.921  1.00 89.60           C  
ANISOU  792  CD1 LEU A 116    10947   9602  13495   2176    -99  -1160       C  
ATOM    793  CD2 LEU A 116      -2.427  43.088  50.948  1.00105.80           C  
ANISOU  793  CD2 LEU A 116    13195  11120  15884   1835   -193  -1140       C  
ATOM    794  N   ASN A 117      -4.099  42.185  55.536  1.00123.46           N  
ANISOU  794  N   ASN A 117    15471  13969  17469   1951    213  -2672       N  
ATOM    795  CA  ASN A 117      -3.608  41.199  56.491  1.00120.77           C  
ANISOU  795  CA  ASN A 117    15290  13987  16608   1741    209  -2802       C  
ATOM    796  C   ASN A 117      -4.747  40.543  57.262  1.00115.54           C  
ANISOU  796  C   ASN A 117    14636  13650  15612   1744    439  -3030       C  
ATOM    797  O   ASN A 117      -4.632  39.378  57.656  1.00110.66           O  
ANISOU  797  O   ASN A 117    14160  13360  14524   1582    422  -2935       O  
ATOM    798  CB  ASN A 117      -2.617  41.852  57.455  1.00109.91           C  
ANISOU  798  CB  ASN A 117    14070  12465  15227   1580    111  -3128       C  
ATOM    799  CG  ASN A 117      -1.318  42.247  56.777  1.00123.92           C  
ANISOU  799  CG  ASN A 117    15821  14003  17258   1479   -102  -2913       C  
ATOM    800  OD1 ASN A 117      -0.943  41.680  55.751  1.00122.71           O  
ANISOU  800  OD1 ASN A 117    15586  13928  17112   1464   -179  -2521       O  
ATOM    801  ND2 ASN A 117      -0.629  43.230  57.345  1.00136.67           N  
ANISOU  801  ND2 ASN A 117    17491  15345  19092   1381   -173  -3209       N  
ATOM    802  N   THR A 118      -5.845  41.267  57.491  1.00105.70           N  
ANISOU  802  N   THR A 118    13234  12306  14622   1909    652  -3347       N  
ATOM    803  CA  THR A 118      -7.006  40.659  58.134  1.00 99.95           C  
ANISOU  803  CA  THR A 118    12444  11924  13609   1875    942  -3599       C  
ATOM    804  C   THR A 118      -7.652  39.626  57.220  1.00 99.89           C  
ANISOU  804  C   THR A 118    12291  12135  13527   1933    951  -3222       C  
ATOM    805  O   THR A 118      -7.969  38.511  57.650  1.00 96.50           O  
ANISOU  805  O   THR A 118    11957  12064  12646   1740   1071  -3188       O  
ATOM    806  CB  THR A 118      -8.020  41.735  58.525  1.00 95.12           C  
ANISOU  806  CB  THR A 118    11604  11149  13390   2070   1172  -4113       C  
ATOM    807  OG1 THR A 118      -7.396  42.691  59.392  1.00116.39           O  
ANISOU  807  OG1 THR A 118    14440  13627  16157   2005   1158  -4511       O  
ATOM    808  CG2 THR A 118      -9.211  41.109  59.235  1.00 89.38           C  
ANISOU  808  CG2 THR A 118    10762  10838  12362   1975   1545  -4448       C  
ATOM    809  N   ILE A 119      -7.853  39.987  55.949  1.00107.06           N  
ANISOU  809  N   ILE A 119    12998  12818  14861   2174    806  -2927       N  
ATOM    810  CA  ILE A 119      -8.443  39.063  54.983  1.00 93.51           C  
ANISOU  810  CA  ILE A 119    11134  11303  13093   2239    774  -2587       C  
ATOM    811  C   ILE A 119      -7.582  37.815  54.849  1.00 98.35           C  
ANISOU  811  C   ILE A 119    11952  12149  13268   2015    646  -2259       C  
ATOM    812  O   ILE A 119      -8.072  36.685  54.961  1.00 99.58           O  
ANISOU  812  O   ILE A 119    12113  12606  13118   1900    734  -2195       O  
ATOM    813  CB  ILE A 119      -8.625  39.759  53.624  1.00 91.76           C  
ANISOU  813  CB  ILE A 119    10742  10778  13345   2511    568  -2295       C  
ATOM    814  CG1 ILE A 119      -9.650  40.886  53.729  1.00100.54           C  
ANISOU  814  CG1 ILE A 119    11616  11622  14962   2795    628  -2632       C  
ATOM    815  CG2 ILE A 119      -9.030  38.753  52.560  1.00 93.93           C  
ANISOU  815  CG2 ILE A 119    10905  11285  13499   2546    484  -1928       C  
ATOM    816  CD1 ILE A 119      -9.670  41.775  52.518  1.00105.59           C  
ANISOU  816  CD1 ILE A 119    12200  11845  16074   3047    337  -2316       C  
ATOM    817  N   LEU A 120      -6.283  38.009  54.598  1.00102.43           N  
ANISOU  817  N   LEU A 120    12617  12506  13794   1946    429  -2074       N  
ATOM    818  CA  LEU A 120      -5.355  36.891  54.463  1.00 92.07           C  
ANISOU  818  CA  LEU A 120    11449  11372  12163   1778    260  -1830       C  
ATOM    819  C   LEU A 120      -5.446  35.950  55.657  1.00100.21           C  
ANISOU  819  C   LEU A 120    12698  12655  12723   1569    317  -1984       C  
ATOM    820  O   LEU A 120      -5.525  34.726  55.497  1.00 97.72           O  
ANISOU  820  O   LEU A 120    12440  12536  12150   1480    258  -1790       O  
ATOM    821  CB  LEU A 120      -3.928  37.422  54.309  1.00 82.71           C  
ANISOU  821  CB  LEU A 120    10340   9980  11105   1712     59  -1769       C  
ATOM    822  CG  LEU A 120      -3.582  38.173  53.022  1.00 90.00           C  
ANISOU  822  CG  LEU A 120    11127  10673  12396   1807    -12  -1516       C  
ATOM    823  CD1 LEU A 120      -2.204  38.804  53.131  1.00 90.80           C  
ANISOU  823  CD1 LEU A 120    11291  10576  12631   1664   -138  -1560       C  
ATOM    824  CD2 LEU A 120      -3.652  37.244  51.823  1.00 95.81           C  
ANISOU  824  CD2 LEU A 120    11758  11604  13041   1834    -70  -1176       C  
ATOM    825  N   ASN A 121      -5.446  36.511  56.868  1.00111.59           N  
ANISOU  825  N   ASN A 121    14292  14077  14029   1466    422  -2332       N  
ATOM    826  CA  ASN A 121      -5.539  35.686  58.067  1.00109.59           C  
ANISOU  826  CA  ASN A 121    14328  14070  13241   1210    473  -2457       C  
ATOM    827  C   ASN A 121      -6.917  35.049  58.192  1.00109.13           C  
ANISOU  827  C   ASN A 121    14191  14265  13010   1139    782  -2506       C  
ATOM    828  O   ASN A 121      -7.040  33.913  58.664  1.00109.49           O  
ANISOU  828  O   ASN A 121    14464  14517  12619    905    780  -2384       O  
ATOM    829  CB  ASN A 121      -5.215  36.524  59.303  1.00105.72           C  
ANISOU  829  CB  ASN A 121    14030  13531  12606   1094    524  -2858       C  
ATOM    830  CG  ASN A 121      -3.723  36.691  59.520  1.00118.66           C  
ANISOU  830  CG  ASN A 121    15839  15016  14231   1041    158  -2815       C  
ATOM    831  OD1 ASN A 121      -2.957  35.732  59.423  1.00125.15           O  
ANISOU  831  OD1 ASN A 121    16800  15897  14853    964   -134  -2557       O  
ATOM    832  ND2 ASN A 121      -3.302  37.917  59.810  1.00127.93           N  
ANISOU  832  ND2 ASN A 121    16971  15968  15667   1089    152  -3103       N  
ATOM    833  N   THR A 122      -7.964  35.764  57.775  1.00101.59           N  
ANISOU  833  N   THR A 122    12906  13274  12420   1330   1028  -2690       N  
ATOM    834  CA  THR A 122      -9.306  35.193  57.804  1.00 95.58           C  
ANISOU  834  CA  THR A 122    11968  12768  11580   1269   1332  -2788       C  
ATOM    835  C   THR A 122      -9.407  33.998  56.865  1.00 96.26           C  
ANISOU  835  C   THR A 122    12004  12953  11616   1260   1187  -2374       C  
ATOM    836  O   THR A 122      -9.962  32.953  57.224  1.00 96.32           O  
ANISOU  836  O   THR A 122    12104  13198  11294   1019   1328  -2333       O  
ATOM    837  CB  THR A 122     -10.340  36.254  57.429  1.00 84.70           C  
ANISOU  837  CB  THR A 122    10174  11285  10722   1551   1531  -3095       C  
ATOM    838  OG1 THR A 122     -10.202  37.385  58.298  1.00104.86           O  
ANISOU  838  OG1 THR A 122    12767  13703  13372   1575   1651  -3532       O  
ATOM    839  CG2 THR A 122     -11.746  35.690  57.555  1.00 86.85           C  
ANISOU  839  CG2 THR A 122    10191  11858  10950   1468   1871  -3296       C  
ATOM    840  N   MET A 123      -8.868  34.137  55.653  1.00100.10           N  
ANISOU  840  N   MET A 123    12359  13259  12414   1489    917  -2077       N  
ATOM    841  CA  MET A 123      -8.912  33.046  54.685  1.00 98.06           C  
ANISOU  841  CA  MET A 123    12035  13098  12124   1496    771  -1738       C  
ATOM    842  C   MET A 123      -8.089  31.857  55.164  1.00 98.78           C  
ANISOU  842  C   MET A 123    12465  13260  11807   1253    590  -1556       C  
ATOM    843  O   MET A 123      -8.531  30.705  55.077  1.00 95.32           O  
ANISOU  843  O   MET A 123    12070  12966  11181   1110    604  -1424       O  
ATOM    844  CB  MET A 123      -8.420  33.547  53.326  1.00 98.14           C  
ANISOU  844  CB  MET A 123    11872  12928  12490   1750    544  -1495       C  
ATOM    845  CG  MET A 123      -9.337  34.596  52.702  1.00 88.86           C  
ANISOU  845  CG  MET A 123    10394  11634  11736   2015    621  -1590       C  
ATOM    846  SD  MET A 123      -9.021  34.918  50.956  1.00 87.69           S  
ANISOU  846  SD  MET A 123    10109  11339  11868   2238    348  -1205       S  
ATOM    847  CE  MET A 123      -7.298  35.399  51.000  1.00 80.01           C  
ANISOU  847  CE  MET A 123     9383  10160  10858   2133    188  -1078       C  
ATOM    848  N   SER A 124      -6.884  32.120  55.681  1.00100.12           N  
ANISOU  848  N   SER A 124    12872  13298  11872   1207    382  -1558       N  
ATOM    849  CA  SER A 124      -6.060  31.047  56.230  1.00100.82           C  
ANISOU  849  CA  SER A 124    13291  13404  11612   1015    122  -1410       C  
ATOM    850  C   SER A 124      -6.781  30.325  57.360  1.00 99.32           C  
ANISOU  850  C   SER A 124    13392  13386  10959    705    293  -1475       C  
ATOM    851  O   SER A 124      -6.645  29.106  57.516  1.00100.77           O  
ANISOU  851  O   SER A 124    13812  13592  10886    536    120  -1261       O  
ATOM    852  CB  SER A 124      -4.727  31.611  56.721  1.00112.84           C  
ANISOU  852  CB  SER A 124    14975  14767  13133   1025   -140  -1485       C  
ATOM    853  OG  SER A 124      -3.952  30.612  57.359  1.00126.75           O  
ANISOU  853  OG  SER A 124    17064  16520  14577    870   -464  -1371       O  
ATOM    854  N   THR A 125      -7.560  31.061  58.154  1.00101.85           N  
ANISOU  854  N   THR A 125    13706  13819  11171    606    643  -1784       N  
ATOM    855  CA  THR A 125      -8.300  30.436  59.242  1.00109.19           C  
ANISOU  855  CA  THR A 125    14915  14968  11605    235    896  -1878       C  
ATOM    856  C   THR A 125      -9.445  29.575  58.723  1.00111.97           C  
ANISOU  856  C   THR A 125    15075  15477  11990    135   1124  -1778       C  
ATOM    857  O   THR A 125      -9.748  28.532  59.309  1.00117.10           O  
ANISOU  857  O   THR A 125    16032  16238  12225   -217   1177  -1646       O  
ATOM    858  CB  THR A 125      -8.829  31.510  60.195  1.00108.26           C  
ANISOU  858  CB  THR A 125    14780  14972  11384    150   1265  -2333       C  
ATOM    859  OG1 THR A 125      -7.732  32.280  60.702  1.00117.78           O  
ANISOU  859  OG1 THR A 125    16176  16019  12556    217   1024  -2445       O  
ATOM    860  CG2 THR A 125      -9.575  30.879  61.361  1.00 97.73           C  
ANISOU  860  CG2 THR A 125    13759  13924   9451   -313   1592  -2456       C  
ATOM    861  N   ILE A 126     -10.077  29.978  57.620  1.00105.54           N  
ANISOU  861  N   ILE A 126    13781  14657  11663    421   1226  -1822       N  
ATOM    862  CA  ILE A 126     -11.259  29.265  57.142  1.00101.51           C  
ANISOU  862  CA  ILE A 126    13020  14318  11229    333   1449  -1807       C  
ATOM    863  C   ILE A 126     -10.867  27.923  56.532  1.00 98.52           C  
ANISOU  863  C   ILE A 126    12791  13871  10772    260   1146  -1422       C  
ATOM    864  O   ILE A 126     -11.496  26.895  56.803  1.00 95.89           O  
ANISOU  864  O   ILE A 126    12576  13650  10208    -50   1273  -1344       O  
ATOM    865  CB  ILE A 126     -12.042  30.139  56.147  1.00 92.89           C  
ANISOU  865  CB  ILE A 126    11378  13225  10691    692   1562  -1980       C  
ATOM    866  CG1 ILE A 126     -12.665  31.331  56.876  1.00 99.83           C  
ANISOU  866  CG1 ILE A 126    12078  14164  11689    738   1900  -2446       C  
ATOM    867  CG2 ILE A 126     -13.120  29.322  55.455  1.00 88.09           C  
ANISOU  867  CG2 ILE A 126    10472  12781  10217    643   1678  -1940       C  
ATOM    868  CD1 ILE A 126     -13.432  32.267  55.972  1.00108.51           C  
ANISOU  868  CD1 ILE A 126    12653  15188  13387   1133   1930  -2629       C  
ATOM    869  N   TYR A 127      -9.829  27.914  55.693  1.00 93.06           N  
ANISOU  869  N   TYR A 127    12082  12988  10290    523    759  -1208       N  
ATOM    870  CA  TYR A 127      -9.334  26.665  55.120  1.00 87.51           C  
ANISOU  870  CA  TYR A 127    11500  12194   9557    491    444   -918       C  
ATOM    871  C   TYR A 127      -8.866  25.702  56.207  1.00 96.81           C  
ANISOU  871  C   TYR A 127    13200  13294  10289    160    278   -770       C  
ATOM    872  O   TYR A 127      -9.366  24.577  56.321  1.00 93.83           O  
ANISOU  872  O   TYR A 127    12978  12926   9746    -94    288   -628       O  
ATOM    873  CB  TYR A 127      -8.200  26.969  54.138  1.00 83.10           C  
ANISOU  873  CB  TYR A 127    10808  11481   9287    809    112   -807       C  
ATOM    874  CG  TYR A 127      -7.623  25.768  53.419  1.00 77.78           C  
ANISOU  874  CG  TYR A 127    10170  10719   8665    838   -210   -605       C  
ATOM    875  CD1 TYR A 127      -8.191  25.293  52.246  1.00 77.63           C  
ANISOU  875  CD1 TYR A 127     9856  10782   8857    941   -190   -557       C  
ATOM    876  CD2 TYR A 127      -6.479  25.136  53.895  1.00 98.96           C  
ANISOU  876  CD2 TYR A 127    13159  13223  11218    788   -571   -504       C  
ATOM    877  CE1 TYR A 127      -7.653  24.206  51.584  1.00 82.52           C  
ANISOU  877  CE1 TYR A 127    10490  11319   9546    974   -473   -444       C  
ATOM    878  CE2 TYR A 127      -5.935  24.049  53.236  1.00 89.45           C  
ANISOU  878  CE2 TYR A 127    11946  11906  10137    853   -884   -390       C  
ATOM    879  CZ  TYR A 127      -6.528  23.589  52.080  1.00 75.60           C  
ANISOU  879  CZ  TYR A 127     9895  10244   8585    939   -809   -376       C  
ATOM    880  OH  TYR A 127      -6.001  22.510  51.408  1.00 75.62           O  
ANISOU  880  OH  TYR A 127     9866  10137   8729   1008  -1103   -331       O  
ATOM    881  N   SER A 128      -7.903  26.138  57.024  1.00116.65           N  
ANISOU  881  N   SER A 128    16012  15705  12605    145     87   -792       N  
ATOM    882  CA  SER A 128      -7.268  25.248  57.991  1.00114.95           C  
ANISOU  882  CA  SER A 128    16339  15363  11974   -117   -220   -606       C  
ATOM    883  C   SER A 128      -8.207  24.813  59.110  1.00119.62           C  
ANISOU  883  C   SER A 128    17287  16111  12053   -588     92   -606       C  
ATOM    884  O   SER A 128      -7.949  23.788  59.750  1.00131.62           O  
ANISOU  884  O   SER A 128    19297  17504  13208   -872   -162   -352       O  
ATOM    885  CB  SER A 128      -6.027  25.924  58.577  1.00118.63           C  
ANISOU  885  CB  SER A 128    16995  15707  12370     -3   -527   -676       C  
ATOM    886  OG  SER A 128      -6.371  27.114  59.265  1.00122.25           O  
ANISOU  886  OG  SER A 128    17429  16316  12704    -57   -194   -964       O  
ATOM    887  N   THR A 129      -9.282  25.560  59.368  1.00112.36           N  
ANISOU  887  N   THR A 129    16138  15453  11101   -693    628   -895       N  
ATOM    888  CA  THR A 129     -10.280  25.164  60.354  1.00107.84           C  
ANISOU  888  CA  THR A 129    15822  15101  10050  -1194   1038   -963       C  
ATOM    889  C   THR A 129     -11.599  24.735  59.727  1.00114.82           C  
ANISOU  889  C   THR A 129    16314  16157  11156  -1301   1428  -1037       C  
ATOM    890  O   THR A 129     -12.542  24.419  60.462  1.00112.61           O  
ANISOU  890  O   THR A 129    16154  16101  10530  -1756   1856  -1145       O  
ATOM    891  CB  THR A 129     -10.540  26.302  61.351  1.00123.10           C  
ANISOU  891  CB  THR A 129    17791  17257  11726  -1310   1411  -1354       C  
ATOM    892  OG1 THR A 129     -11.243  27.368  60.699  1.00105.03           O  
ANISOU  892  OG1 THR A 129    14876  15087   9944   -995   1749  -1720       O  
ATOM    893  CG2 THR A 129      -9.230  26.831  61.919  1.00141.96           C  
ANISOU  893  CG2 THR A 129    20509  19481  13947  -1180   1005  -1335       C  
ATOM    894  N   GLY A 130     -11.690  24.707  58.399  1.00123.73           N  
ANISOU  894  N   GLY A 130    16977  17208  12827   -930   1297  -1000       N  
ATOM    895  CA  GLY A 130     -12.948  24.405  57.741  1.00120.04           C  
ANISOU  895  CA  GLY A 130    16072  16915  12622   -984   1619  -1121       C  
ATOM    896  C   GLY A 130     -13.347  22.961  57.950  1.00115.60           C  
ANISOU  896  C   GLY A 130    15803  16316  11804  -1427   1618   -872       C  
ATOM    897  O   GLY A 130     -12.584  22.042  57.605  1.00117.10           O  
ANISOU  897  O   GLY A 130    16265  16231  11998  -1390   1163   -541       O  
ATOM    898  N   LYS A 131     -14.535  22.738  58.503  1.00119.01           N  
ANISOU  898  N   LYS A 131    16167  17005  12045  -1860   2124  -1055       N  
ATOM    899  CA  LYS A 131     -15.023  21.403  58.808  1.00128.05           C  
ANISOU  899  CA  LYS A 131    17622  18113  12919  -2387   2197   -824       C  
ATOM    900  C   LYS A 131     -16.352  21.143  58.112  1.00134.01           C  
ANISOU  900  C   LYS A 131    17795  19084  14039  -2477   2563  -1057       C  
ATOM    901  O   LYS A 131     -17.158  22.056  57.908  1.00138.57           O  
ANISOU  901  O   LYS A 131    17807  19940  14902  -2306   2931  -1478       O  
ATOM    902  CB  LYS A 131     -15.162  21.204  60.324  1.00142.04           C  
ANISOU  902  CB  LYS A 131    19986  20006  13976  -3008   2490   -784       C  
ATOM    903  CG  LYS A 131     -16.106  22.162  61.029  1.00146.36           C  
ANISOU  903  CG  LYS A 131    20246  20987  14379  -3211   3169  -1289       C  
ATOM    904  CD  LYS A 131     -16.405  21.670  62.439  1.00155.13           C  
ANISOU  904  CD  LYS A 131    21974  22268  14701  -3973   3525  -1222       C  
ATOM    905  CE  LYS A 131     -15.267  21.993  63.399  1.00158.31           C  
ANISOU  905  CE  LYS A 131    23046  22550  14556  -4000   3203  -1044       C  
ATOM    906  NZ  LYS A 131     -15.288  23.403  63.872  1.00164.25           N  
ANISOU  906  NZ  LYS A 131    23544  23572  15293  -3793   3511  -1551       N  
ATOM    907  N   VAL A 132     -16.561  19.883  57.738  1.00142.83           N  
ANISOU  907  N   VAL A 132    19041  20039  15190  -2729   2416   -803       N  
ATOM    908  CA  VAL A 132     -17.767  19.433  57.052  1.00142.72           C  
ANISOU  908  CA  VAL A 132    18505  20194  15526  -2864   2691   -999       C  
ATOM    909  C   VAL A 132     -18.393  18.319  57.879  1.00151.25           C  
ANISOU  909  C   VAL A 132    19983  21281  16204  -3638   2987   -850       C  
ATOM    910  O   VAL A 132     -17.698  17.385  58.295  1.00160.27           O  
ANISOU  910  O   VAL A 132    21796  22083  17017  -3904   2651   -414       O  
ATOM    911  CB  VAL A 132     -17.461  18.952  55.621  1.00121.20           C  
ANISOU  911  CB  VAL A 132    15500  17257  13294  -2431   2216   -873       C  
ATOM    912  CG1 VAL A 132     -18.550  18.013  55.117  1.00120.47           C  
ANISOU  912  CG1 VAL A 132    15106  17238  13432  -2746   2391   -958       C  
ATOM    913  CG2 VAL A 132     -17.301  20.141  54.687  1.00116.72           C  
ANISOU  913  CG2 VAL A 132    14399  16801  13150  -1771   2092  -1098       C  
ATOM    914  N   CYS A 133     -19.697  18.417  58.113  1.00145.01           N  
ANISOU  914  N   CYS A 133    18777  20858  15462  -4009   3600  -1218       N  
ATOM    915  CA  CYS A 133     -20.399  17.494  58.989  1.00150.81           C  
ANISOU  915  CA  CYS A 133    19861  21670  15768  -4849   4018  -1129       C  
ATOM    916  C   CYS A 133     -21.382  16.640  58.196  1.00155.72           C  
ANISOU  916  C   CYS A 133    20032  22317  16818  -5061   4136  -1231       C  
ATOM    917  O   CYS A 133     -21.860  17.037  57.130  1.00149.71           O  
ANISOU  917  O   CYS A 133    18534  21690  16659  -4594   4082  -1546       O  
ATOM    918  CB  CYS A 133     -21.127  18.250  60.106  1.00153.28           C  
ANISOU  918  CB  CYS A 133    20088  22447  15705  -5262   4744  -1538       C  
ATOM    919  SG  CYS A 133     -20.012  19.173  61.206  1.00181.93           S  
ANISOU  919  SG  CYS A 133    24330  26063  18733  -5136   4630  -1449       S  
ATOM    920  N   ASN A 134     -21.675  15.461  58.738  1.00180.63           N  
ANISOU  920  N   ASN A 134    23667  25322  19641  -5792   4268   -947       N  
ATOM    921  CA  ASN A 134     -22.505  14.489  58.041  1.00186.18           C  
ANISOU  921  CA  ASN A 134    24044  25968  20730  -6071   4327   -994       C  
ATOM    922  C   ASN A 134     -23.911  15.038  57.811  1.00186.97           C  
ANISOU  922  C   ASN A 134    23232  26602  21205  -6171   4960  -1640       C  
ATOM    923  O   ASN A 134     -24.465  15.719  58.682  1.00184.76           O  
ANISOU  923  O   ASN A 134    22815  26729  20658  -6469   5569  -1982       O  
ATOM    924  CB  ASN A 134     -22.592  13.192  58.846  1.00194.89           C  
ANISOU  924  CB  ASN A 134    25905  26791  21354  -6943   4413   -558       C  
ATOM    925  CG  ASN A 134     -23.094  12.022  58.022  1.00197.95           C  
ANISOU  925  CG  ASN A 134    26112  26921  22180  -7154   4248   -485       C  
ATOM    926  OD1 ASN A 134     -22.526  11.687  56.983  1.00193.88           O  
ANISOU  926  OD1 ASN A 134    25486  26078  22102  -6608   3640   -371       O  
ATOM    927  ND2 ASN A 134     -24.171  11.396  58.483  1.00195.44           N  
ANISOU  927  ND2 ASN A 134    25746  26767  21745  -7980   4816   -590       N  
ATOM    928  N   PRO A 135     -24.514  14.766  56.655  1.00185.62           N  
ANISOU  928  N   PRO A 135    22403  26456  21668  -5919   4819  -1866       N  
ATOM    929  CA  PRO A 135     -25.954  14.999  56.515  1.00188.66           C  
ANISOU  929  CA  PRO A 135    21947  27311  22426  -6160   5400  -2468       C  
ATOM    930  C   PRO A 135     -26.715  14.035  57.405  1.00195.39           C  
ANISOU  930  C   PRO A 135    23071  28244  22923  -7199   5977  -2431       C  
ATOM    931  O   PRO A 135     -26.352  12.862  57.527  1.00195.69           O  
ANISOU  931  O   PRO A 135    23759  27869  22727  -7641   5741  -1934       O  
ATOM    932  CB  PRO A 135     -26.222  14.722  55.031  1.00174.55           C  
ANISOU  932  CB  PRO A 135    19560  25433  21328  -5667   4945  -2595       C  
ATOM    933  CG  PRO A 135     -25.098  13.850  54.597  1.00172.72           C  
ANISOU  933  CG  PRO A 135    19992  24654  20981  -5517   4283  -2017       C  
ATOM    934  CD  PRO A 135     -23.911  14.267  55.409  1.00173.70           C  
ANISOU  934  CD  PRO A 135    20850  24581  20569  -5390   4115  -1639       C  
ATOM    935  N   ASP A 136     -27.764  14.549  58.045  1.00212.21           N  
ANISOU  935  N   ASP A 136    24708  30900  25024  -7605   6743  -2976       N  
ATOM    936  CA  ASP A 136     -28.626  13.812  58.964  1.00216.79           C  
ANISOU  936  CA  ASP A 136    25513  31585  25272  -8489   7276  -3025       C  
ATOM    937  C   ASP A 136     -27.908  13.417  60.247  1.00205.39           C  
ANISOU  937  C   ASP A 136    25183  29925  22929  -9050   7335  -2483       C  
ATOM    938  O   ASP A 136     -28.463  12.657  61.049  1.00199.89           O  
ANISOU  938  O   ASP A 136    24880  29195  21876  -9754   7615  -2378       O  
ATOM    939  CB  ASP A 136     -29.223  12.565  58.300  1.00214.58           C  
ANISOU  939  CB  ASP A 136    25075  31104  25351  -8893   7189  -2935       C  
ATOM    940  CG  ASP A 136     -29.979  12.893  57.030  1.00218.64           C  
ANISOU  940  CG  ASP A 136    24508  31830  26735  -8336   7047  -3476       C  
ATOM    941  OD1 ASP A 136     -30.282  14.084  56.814  1.00224.48           O  
ANISOU  941  OD1 ASP A 136    24614  32885  27794  -7700   7081  -3960       O  
ATOM    942  OD2 ASP A 136     -30.255  11.965  56.241  1.00221.58           O1-
ANISOU  942  OD2 ASP A 136    24699  32010  27481  -8507   6830  -3409       O1-
ATOM    943  N   ASN A 137     -26.687  13.901  60.462  1.00187.04           N  
ANISOU  943  N   ASN A 137    23395  27447  20223  -8748   7037  -2133       N  
ATOM    944  CA  ASN A 137     -25.973  13.702  61.725  1.00194.83           C  
ANISOU  944  CA  ASN A 137    25424  28250  20351  -9159   6993  -1664       C  
ATOM    945  C   ASN A 137     -25.023  14.871  61.920  1.00197.41           C  
ANISOU  945  C   ASN A 137    25868  28670  20468  -8577   6824  -1697       C  
ATOM    946  O   ASN A 137     -23.833  14.794  61.589  1.00195.72           O  
ANISOU  946  O   ASN A 137    26119  28012  20234  -8072   6095  -1236       O  
ATOM    947  CB  ASN A 137     -25.216  12.372  61.742  1.00192.65           C  
ANISOU  947  CB  ASN A 137    26080  27368  19750  -9592   6513   -868       C  
ATOM    948  CG  ASN A 137     -24.611  12.059  63.105  1.00205.19           C  
ANISOU  948  CG  ASN A 137    28752  28739  20471 -10026   6382   -385       C  
ATOM    949  OD1 ASN A 137     -24.863  12.757  64.087  1.00191.36           O  
ANISOU  949  OD1 ASN A 137    27041  27341  18327 -10125   6740   -675       O  
ATOM    950  ND2 ASN A 137     -23.809  11.002  63.166  1.00211.65           N  
ANISOU  950  ND2 ASN A 137    30441  28944  21030 -10261   5808    335       N  
ATOM    951  N   PRO A 138     -25.524  15.993  62.447  1.00208.08           N  
ANISOU  951  N   PRO A 138    26772  30434  21853  -8351   7202  -2278       N  
ATOM    952  CA  PRO A 138     -24.651  17.163  62.645  1.00209.84           C  
ANISOU  952  CA  PRO A 138    27078  30726  21927  -7784   7040  -2362       C  
ATOM    953  C   PRO A 138     -23.446  16.876  63.521  1.00210.44           C  
ANISOU  953  C   PRO A 138    28257  30504  21195  -8014   6693  -1750       C  
ATOM    954  O   PRO A 138     -22.417  17.550  63.391  1.00206.84           O  
ANISOU  954  O   PRO A 138    27980  29904  20705  -7438   6268  -1631       O  
ATOM    955  CB  PRO A 138     -25.593  18.185  63.298  1.00214.26           C  
ANISOU  955  CB  PRO A 138    27069  31711  22629  -7714   7537  -3082       C  
ATOM    956  CG  PRO A 138     -26.954  17.789  62.820  1.00214.10           C  
ANISOU  956  CG  PRO A 138    26311  31876  23161  -7902   7856  -3489       C  
ATOM    957  CD  PRO A 138     -26.926  16.286  62.793  1.00208.36           C  
ANISOU  957  CD  PRO A 138    26146  30866  22157  -8556   7758  -2932       C  
ATOM    958  N   GLN A 139     -23.549  15.886  64.409  1.00212.36           N  
ANISOU  958  N   GLN A 139    29232  30571  20886  -8733   6709  -1359       N  
ATOM    959  CA  GLN A 139     -22.442  15.539  65.293  1.00215.55           C  
ANISOU  959  CA  GLN A 139    30709  30642  20549  -8936   6262   -756       C  
ATOM    960  C   GLN A 139     -21.244  15.021  64.506  1.00210.92           C  
ANISOU  960  C   GLN A 139    30573  29537  20030  -8597   5525   -147       C  
ATOM    961  O   GLN A 139     -20.101  15.429  64.746  1.00197.09           O  
ANISOU  961  O   GLN A 139    29256  27565  18064  -8166   4986     88       O  
ATOM    962  CB  GLN A 139     -22.916  14.504  66.311  1.00214.62           C  
ANISOU  962  CB  GLN A 139    31225  30412  19909  -9770   6397   -470       C  
ATOM    963  CG  GLN A 139     -21.814  13.803  67.069  1.00213.36           C  
ANISOU  963  CG  GLN A 139    32208  29771  19090 -10000   5771    264       C  
ATOM    964  CD  GLN A 139     -22.170  12.364  67.381  1.00221.25           C  
ANISOU  964  CD  GLN A 139    33777  30416  19871 -10696   5667    732       C  
ATOM    965  OE1 GLN A 139     -23.214  11.865  66.955  1.00229.74           O  
ANISOU  965  OE1 GLN A 139    34387  31606  21299 -11013   6073    517       O  
ATOM    966  NE2 GLN A 139     -21.301  11.685  68.116  1.00219.79           N  
ANISOU  966  NE2 GLN A 139    34587  29776  19146 -10910   5078   1360       N  
ATOM    967  N   GLU A 140     -21.486  14.110  63.565  1.00202.85           N  
ANISOU  967  N   GLU A 140    29331  28191  19551  -8543   5255     33       N  
ATOM    968  CA  GLU A 140     -20.410  13.544  62.759  1.00193.17           C  
ANISOU  968  CA  GLU A 140    28357  26344  18696  -7959   4330    489       C  
ATOM    969  C   GLU A 140     -19.839  14.613  61.838  1.00185.69           C  
ANISOU  969  C   GLU A 140    26760  25458  18336  -6940   4000    173       C  
ATOM    970  O   GLU A 140     -20.573  15.206  61.042  1.00183.65           O  
ANISOU  970  O   GLU A 140    25616  25514  18648  -6599   4297   -326       O  
ATOM    971  CB  GLU A 140     -20.927  12.363  61.945  1.00187.25           C  
ANISOU  971  CB  GLU A 140    27445  25286  18417  -8167   4198    641       C  
ATOM    972  CG  GLU A 140     -19.903  11.784  60.986  1.00195.17           C  
ANISOU  972  CG  GLU A 140    28569  25687  19900  -7525   3294    978       C  
ATOM    973  CD  GLU A 140     -20.486  10.709  60.091  1.00202.51           C  
ANISOU  973  CD  GLU A 140    29228  26354  21363  -7681   3194   1006       C  
ATOM    974  OE1 GLU A 140     -21.482  10.073  60.495  1.00197.94           O  
ANISOU  974  OE1 GLU A 140    28718  25874  20615  -8483   3700   1004       O  
ATOM    975  OE2 GLU A 140     -19.943  10.497  58.986  1.00197.91           O1-
ANISOU  975  OE2 GLU A 140    28361  25478  21359  -7033   2627   1003       O1-
ATOM    976  N   CYS A 141     -18.535  14.860  61.944  1.00174.46           N  
ANISOU  976  N   CYS A 141    25779  23726  16783  -6473   3368    463       N  
ATOM    977  CA  CYS A 141     -17.882  15.894  61.157  1.00170.17           C  
ANISOU  977  CA  CYS A 141    24716  23220  16721  -5584   3063    212       C  
ATOM    978  C   CYS A 141     -16.496  15.427  60.739  1.00162.89           C  
ANISOU  978  C   CYS A 141    24198  21753  15940  -5118   2193    638       C  
ATOM    979  O   CYS A 141     -15.873  14.596  61.406  1.00173.28           O  
ANISOU  979  O   CYS A 141    26304  22690  16843  -5436   1800   1108       O  
ATOM    980  CB  CYS A 141     -17.778  17.216  61.930  1.00180.78           C  
ANISOU  980  CB  CYS A 141    26000  24945  17743  -5478   3400   -123       C  
ATOM    981  SG  CYS A 141     -19.358  17.820  62.578  1.00210.92           S  
ANISOU  981  SG  CYS A 141    29326  29432  21381  -6035   4461   -736       S  
ATOM    982  N   LEU A 142     -16.021  15.977  59.624  1.00134.23           N  
ANISOU  982  N   LEU A 142    20012  18084  12903  -4366   1887    454       N  
ATOM    983  CA  LEU A 142     -14.740  15.596  59.044  1.00130.41           C  
ANISOU  983  CA  LEU A 142    19730  17148  12670  -3870   1124    730       C  
ATOM    984  C   LEU A 142     -14.022  16.837  58.546  1.00126.99           C  
ANISOU  984  C   LEU A 142    18889  16852  12510  -3184    982    482       C  
ATOM    985  O   LEU A 142     -14.623  17.676  57.868  1.00125.86           O  
ANISOU  985  O   LEU A 142    18080  17027  12716  -2897   1309    117       O  
ATOM    986  CB  LEU A 142     -14.926  14.600  57.892  1.00120.71           C  
ANISOU  986  CB  LEU A 142    18234  15659  11970  -3741    858    790       C  
ATOM    987  CG  LEU A 142     -15.565  13.260  58.253  1.00123.47           C  
ANISOU  987  CG  LEU A 142    18994  15763  12154  -4413    917   1061       C  
ATOM    988  CD1 LEU A 142     -15.873  12.454  57.007  1.00122.18           C  
ANISOU  988  CD1 LEU A 142    18420  15413  12589  -4239    722    984       C  
ATOM    989  CD2 LEU A 142     -14.660  12.474  59.192  1.00140.12           C  
ANISOU  989  CD2 LEU A 142    22035  17383  13822  -4685    404   1572       C  
ATOM    990  N   LEU A 143     -12.743  16.949  58.881  1.00134.92           N  
ANISOU  990  N   LEU A 143    20294  17595  13375  -2935    468    684       N  
ATOM    991  CA  LEU A 143     -11.915  18.029  58.372  1.00128.59           C  
ANISOU  991  CA  LEU A 143    19144  16857  12857  -2322    280    486       C  
ATOM    992  C   LEU A 143     -11.308  17.592  57.044  1.00113.99           C  
ANISOU  992  C   LEU A 143    16967  14772  11573  -1840   -163    512       C  
ATOM    993  O   LEU A 143     -11.466  16.445  56.617  1.00115.91           O  
ANISOU  993  O   LEU A 143    17293  14774  11975  -1964   -366    669       O  
ATOM    994  CB  LEU A 143     -10.817  18.377  59.385  1.00127.56           C  
ANISOU  994  CB  LEU A 143    19554  16590  12325  -2309    -54    630       C  
ATOM    995  CG  LEU A 143     -11.230  18.417  60.862  1.00120.06           C  
ANISOU  995  CG  LEU A 143    19175  15792  10649  -2907    245    710       C  
ATOM    996  CD1 LEU A 143     -10.132  19.016  61.727  1.00147.32           C  
ANISOU  996  CD1 LEU A 143    23044  19178  13754  -2795    -98    755       C  
ATOM    997  CD2 LEU A 143     -12.523  19.165  61.073  1.00129.73           C  
ANISOU  997  CD2 LEU A 143    20011  17501  11781  -3156   1037    331       C  
ATOM    998  N   LEU A 144     -10.613  18.513  56.375  1.00109.96           N  
ANISOU  998  N   LEU A 144    16084  14331  11362  -1318   -294    335       N  
ATOM    999  CA  LEU A 144      -9.892  18.113  55.171  1.00114.32           C  
ANISOU  999  CA  LEU A 144    16368  14694  12374   -899   -701    334       C  
ATOM   1000  C   LEU A 144      -8.913  16.997  55.495  1.00125.72           C  
ANISOU 1000  C   LEU A 144    18294  15692  13783   -933  -1292    595       C  
ATOM   1001  O   LEU A 144      -8.821  15.999  54.774  1.00128.08           O  
ANISOU 1001  O   LEU A 144    18529  15759  14376   -863  -1561    640       O  
ATOM   1002  CB  LEU A 144      -9.152  19.305  54.561  1.00112.54           C  
ANISOU 1002  CB  LEU A 144    15771  14600  12390   -420   -747    143       C  
ATOM   1003  CG  LEU A 144      -8.510  19.022  53.198  1.00 95.11           C  
ANISOU 1003  CG  LEU A 144    13208  12307  10620    -27  -1042     75       C  
ATOM   1004  CD1 LEU A 144      -9.528  19.104  52.069  1.00 94.99           C  
ANISOU 1004  CD1 LEU A 144    12703  12536  10854     52   -759    -74       C  
ATOM   1005  CD2 LEU A 144      -7.355  19.970  52.945  1.00103.47           C  
ANISOU 1005  CD2 LEU A 144    14121  13379  11812    330  -1211    -26       C  
ATOM   1006  N   GLU A 145      -8.183  17.150  56.595  1.00127.73           N  
ANISOU 1006  N   GLU A 145    19036  15804  13691  -1032  -1534    745       N  
ATOM   1007  CA  GLU A 145      -7.342  16.111  57.138  1.00118.00           C  
ANISOU 1007  CA  GLU A 145    18350  14114  12370  -1107  -2148   1026       C  
ATOM   1008  C   GLU A 145      -7.866  15.722  58.512  1.00118.01           C  
ANISOU 1008  C   GLU A 145    19039  14056  11745  -1697  -2052   1317       C  
ATOM   1009  O   GLU A 145      -8.108  16.606  59.347  1.00120.02           O  
ANISOU 1009  O   GLU A 145    19425  14603  11574  -1887  -1714   1249       O  
ATOM   1010  CB  GLU A 145      -5.886  16.573  57.243  1.00111.88           C  
ANISOU 1010  CB  GLU A 145    17588  13197  11726   -702  -2641    960       C  
ATOM   1011  CG  GLU A 145      -4.898  15.446  57.485  1.00122.62           C  
ANISOU 1011  CG  GLU A 145    19347  14032  13213   -614  -3402   1169       C  
ATOM   1012  CD  GLU A 145      -4.522  14.709  56.215  1.00125.21           C  
ANISOU 1012  CD  GLU A 145    19256  14156  14163   -258  -3670   1011       C  
ATOM   1013  OE1 GLU A 145      -4.786  15.240  55.118  1.00123.54           O  
ANISOU 1013  OE1 GLU A 145    18440  14252  14247    -29  -3308    734       O  
ATOM   1014  OE2 GLU A 145      -3.952  13.603  56.311  1.00133.40           O1-
ANISOU 1014  OE2 GLU A 145    20582  14713  15391   -205  -4266   1151       O1-
ATOM   1015  N   PRO A 146      -8.056  14.426  58.793  1.00124.01           N  
ANISOU 1015  N   PRO A 146    20270  14438  12411  -2028  -2329   1636       N  
ATOM   1016  CA  PRO A 146      -7.709  13.322  57.906  1.00127.11           C  
ANISOU 1016  CA  PRO A 146    20557  14417  13321  -1807  -2787   1687       C  
ATOM   1017  C   PRO A 146      -8.858  12.769  57.067  1.00139.21           C  
ANISOU 1017  C   PRO A 146    21740  16042  15112  -1989  -2395   1592       C  
ATOM   1018  O   PRO A 146      -8.601  12.142  56.047  1.00149.86           O  
ANISOU 1018  O   PRO A 146    22787  17180  16974  -1693  -2669   1475       O  
ATOM   1019  CB  PRO A 146      -7.252  12.256  58.888  1.00123.50           C  
ANISOU 1019  CB  PRO A 146    20930  13418  12575  -2110  -3379   2128       C  
ATOM   1020  CG  PRO A 146      -8.183  12.461  60.060  1.00135.17           C  
ANISOU 1020  CG  PRO A 146    22903  15139  13317  -2785  -2889   2344       C  
ATOM   1021  CD  PRO A 146      -8.542  13.937  60.094  1.00135.21           C  
ANISOU 1021  CD  PRO A 146    22439  15767  13166  -2681  -2256   1983       C  
ATOM   1022  N   GLY A 147     -10.100  12.975  57.507  1.00139.15           N  
ANISOU 1022  N   GLY A 147    21756  16354  14761  -2484  -1769   1599       N  
ATOM   1023  CA  GLY A 147     -11.257  12.348  56.895  1.00138.58           C  
ANISOU 1023  CA  GLY A 147    21411  16348  14896  -2760  -1419   1524       C  
ATOM   1024  C   GLY A 147     -11.510  12.598  55.420  1.00122.73           C  
ANISOU 1024  C   GLY A 147    18613  14556  13461  -2314  -1298   1156       C  
ATOM   1025  O   GLY A 147     -11.521  11.656  54.623  1.00126.37           O  
ANISOU 1025  O   GLY A 147    18957  14749  14308  -2238  -1560   1135       O  
ATOM   1026  N   LEU A 148     -11.716  13.859  55.039  1.00118.83           N  
ANISOU 1026  N   LEU A 148    17601  14530  13021  -2026   -929    860       N  
ATOM   1027  CA  LEU A 148     -12.101  14.159  53.663  1.00111.43           C  
ANISOU 1027  CA  LEU A 148    15961  13838  12538  -1665   -794    547       C  
ATOM   1028  C   LEU A 148     -11.003  13.741  52.694  1.00110.96           C  
ANISOU 1028  C   LEU A 148    15770  13518  12872  -1187  -1328    492       C  
ATOM   1029  O   LEU A 148     -11.272  13.134  51.650  1.00117.10           O  
ANISOU 1029  O   LEU A 148    16231  14264  13997  -1076  -1409    344       O  
ATOM   1030  CB  LEU A 148     -12.408  15.648  53.533  1.00104.81           C  
ANISOU 1030  CB  LEU A 148    14689  13464  11671  -1432   -391    298       C  
ATOM   1031  CG  LEU A 148     -13.688  16.145  54.208  1.00110.01           C  
ANISOU 1031  CG  LEU A 148    15242  14468  12087  -1828    219    178       C  
ATOM   1032  CD1 LEU A 148     -13.962  17.586  53.843  1.00105.39           C  
ANISOU 1032  CD1 LEU A 148    14146  14261  11637  -1480    512   -117       C  
ATOM   1033  CD2 LEU A 148     -14.864  15.288  53.808  1.00111.59           C  
ANISOU 1033  CD2 LEU A 148    15229  14720  12451  -2168    444    107       C  
ATOM   1034  N   ASN A 149      -9.748  14.023  53.048  1.00109.79           N  
ANISOU 1034  N   ASN A 149    15848  13191  12676   -921  -1700    569       N  
ATOM   1035  CA  ASN A 149      -8.640  13.649  52.178  1.00111.76           C  
ANISOU 1035  CA  ASN A 149    15922  13222  13320   -477  -2175    444       C  
ATOM   1036  C   ASN A 149      -8.567  12.136  52.004  1.00113.70           C  
ANISOU 1036  C   ASN A 149    16406  12994  13802   -596  -2580    535       C  
ATOM   1037  O   ASN A 149      -8.208  11.649  50.927  1.00111.80           O  
ANISOU 1037  O   ASN A 149    15838  12671  13970   -302  -2798    303       O  
ATOM   1038  CB  ASN A 149      -7.324  14.208  52.716  1.00110.19           C  
ANISOU 1038  CB  ASN A 149    15903  12911  13052   -214  -2503    478       C  
ATOM   1039  CG  ASN A 149      -7.006  15.587  52.152  1.00107.06           C  
ANISOU 1039  CG  ASN A 149    15044  12914  12719    120  -2247    246       C  
ATOM   1040  OD1 ASN A 149      -7.362  15.896  51.016  1.00 91.00           O  
ANISOU 1040  OD1 ASN A 149    12530  11141  10904    303  -2029     41       O  
ATOM   1041  ND2 ASN A 149      -6.314  16.408  52.933  1.00101.91           N  
ANISOU 1041  ND2 ASN A 149    14566  12286  11867    183  -2307    287       N  
ATOM   1042  N   GLU A 150      -8.928  11.374  53.041  1.00117.91           N  
ANISOU 1042  N   GLU A 150    17522  13204  14072  -1055  -2677    861       N  
ATOM   1043  CA  GLU A 150      -8.981   9.923  52.897  1.00127.81           C  
ANISOU 1043  CA  GLU A 150    19043  13943  15577  -1220  -3059    976       C  
ATOM   1044  C   GLU A 150      -9.989   9.532  51.829  1.00130.52           C  
ANISOU 1044  C   GLU A 150    18920  14466  16205  -1296  -2757    734       C  
ATOM   1045  O   GLU A 150      -9.666   8.808  50.881  1.00126.99           O  
ANISOU 1045  O   GLU A 150    18241  13807  16203  -1043  -3061    518       O  
ATOM   1046  CB  GLU A 150      -9.351   9.263  54.225  1.00126.89           C  
ANISOU 1046  CB  GLU A 150    19690  13478  15045  -1806  -3141   1429       C  
ATOM   1047  CG  GLU A 150      -9.122   7.760  54.230  1.00145.49           C  
ANISOU 1047  CG  GLU A 150    22460  15136  17683  -1938  -3708   1625       C  
ATOM   1048  CD  GLU A 150     -10.337   6.984  53.774  1.00160.05           C  
ANISOU 1048  CD  GLU A 150    24190  16948  19672  -2353  -3399   1592       C  
ATOM   1049  OE1 GLU A 150     -11.464   7.489  53.954  1.00161.21           O  
ANISOU 1049  OE1 GLU A 150    24173  17554  19526  -2737  -2746   1567       O  
ATOM   1050  OE2 GLU A 150     -10.166   5.879  53.219  1.00158.16           O1-
ANISOU 1050  OE2 GLU A 150    23984  16225  19884  -2284  -3812   1542       O1-
ATOM   1051  N   ILE A 151     -11.226  10.013  51.975  1.00126.99           N  
ANISOU 1051  N   ILE A 151    18304  14426  15522  -1642  -2164    717       N  
ATOM   1052  CA  ILE A 151     -12.294   9.646  51.050  1.00115.89           C  
ANISOU 1052  CA  ILE A 151    16450  13209  14374  -1761  -1890    481       C  
ATOM   1053  C   ILE A 151     -11.862   9.914  49.614  1.00116.20           C  
ANISOU 1053  C   ILE A 151    15901  13454  14796  -1206  -2021    106       C  
ATOM   1054  O   ILE A 151     -11.872   9.020  48.762  1.00122.45           O  
ANISOU 1054  O   ILE A 151    16533  14050  15943  -1127  -2255    -76       O  
ATOM   1055  CB  ILE A 151     -13.587  10.400  51.395  1.00116.01           C  
ANISOU 1055  CB  ILE A 151    16236  13719  14123  -2106  -1229    426       C  
ATOM   1056  CG1 ILE A 151     -14.040  10.074  52.821  1.00123.71           C  
ANISOU 1056  CG1 ILE A 151    17812  14539  14654  -2746  -1030    765       C  
ATOM   1057  CG2 ILE A 151     -14.661  10.061  50.392  1.00121.26           C  
ANISOU 1057  CG2 ILE A 151    16376  14597  15100  -2184  -1009    141       C  
ATOM   1058  CD1 ILE A 151     -15.312  10.767  53.219  1.00120.26           C  
ANISOU 1058  CD1 ILE A 151    17106  14604  13982  -3116   -337    628       C  
ATOM   1059  N   MET A 152     -11.444  11.150  49.335  1.00107.47           N  
ANISOU 1059  N   MET A 152    14497  12734  13604   -838  -1875    -18       N  
ATOM   1060  CA  MET A 152     -11.070  11.505  47.971  1.00104.05           C  
ANISOU 1060  CA  MET A 152    13544  12554  13435   -381  -1940   -342       C  
ATOM   1061  C   MET A 152      -9.894  10.674  47.470  1.00115.31           C  
ANISOU 1061  C   MET A 152    15029  13610  15173    -92  -2453   -470       C  
ATOM   1062  O   MET A 152      -9.851  10.295  46.293  1.00110.13           O  
ANISOU 1062  O   MET A 152    14016  13040  14787    111  -2542   -777       O  
ATOM   1063  CB  MET A 152     -10.743  12.995  47.889  1.00 98.10           C  
ANISOU 1063  CB  MET A 152    12561  12201  12512    -96  -1716   -385       C  
ATOM   1064  CG  MET A 152     -11.857  13.896  48.383  1.00 98.82           C  
ANISOU 1064  CG  MET A 152    12542  12636  12368   -312  -1234   -334       C  
ATOM   1065  SD  MET A 152     -13.297  13.790  47.306  1.00113.33           S  
ANISOU 1065  SD  MET A 152    13843  14818  14400   -382   -973   -584       S  
ATOM   1066  CE  MET A 152     -12.572  14.260  45.738  1.00118.56           C  
ANISOU 1066  CE  MET A 152    14101  15705  15240    146  -1180   -814       C  
ATOM   1067  N   ALA A 153      -8.937  10.372  48.346  1.00123.56           N  
ANISOU 1067  N   ALA A 153    16506  14249  16194    -64  -2814   -277       N  
ATOM   1068  CA  ALA A 153      -7.689   9.754  47.921  1.00125.74           C  
ANISOU 1068  CA  ALA A 153    16759  14192  16824    291  -3322   -466       C  
ATOM   1069  C   ALA A 153      -7.691   8.234  48.013  1.00130.61           C  
ANISOU 1069  C   ALA A 153    17668  14208  17751    148  -3753   -438       C  
ATOM   1070  O   ALA A 153      -6.761   7.602  47.506  1.00137.15           O  
ANISOU 1070  O   ALA A 153    18390  14743  18979    471  -4183   -699       O  
ATOM   1071  CB  ALA A 153      -6.513  10.305  48.739  1.00116.19           C  
ANISOU 1071  CB  ALA A 153    15784  12853  15509    486  -3576   -337       C  
ATOM   1072  N   ASN A 154      -8.695   7.631  48.630  1.00120.89           N  
ANISOU 1072  N   ASN A 154    16786  12770  16378   -336  -3646   -161       N  
ATOM   1073  CA  ASN A 154      -8.721   6.176  48.766  1.00123.49           C  
ANISOU 1073  CA  ASN A 154    17460  12447  17015   -523  -4078    -85       C  
ATOM   1074  C   ASN A 154     -10.073   5.531  48.491  1.00122.13           C  
ANISOU 1074  C   ASN A 154    17242  12281  16879   -974  -3792    -86       C  
ATOM   1075  O   ASN A 154     -10.094   4.380  48.045  1.00117.64           O  
ANISOU 1075  O   ASN A 154    16715  11269  16715  -1008  -4116   -224       O  
ATOM   1076  CB  ASN A 154      -8.259   5.777  50.175  1.00131.22           C  
ANISOU 1076  CB  ASN A 154    19184  12881  17793   -751  -4468    394       C  
ATOM   1077  CG  ASN A 154      -6.945   5.026  50.166  1.00142.72           C  
ANISOU 1077  CG  ASN A 154    20806  13735  19687   -355  -5224    305       C  
ATOM   1078  OD1 ASN A 154      -6.347   4.800  49.116  1.00150.16           O  
ANISOU 1078  OD1 ASN A 154    21272  14687  21096     85  -5408   -164       O  
ATOM   1079  ND2 ASN A 154      -6.480   4.640  51.349  1.00141.91           N  
ANISOU 1079  ND2 ASN A 154    21378  13112  19428   -510  -5682    734       N  
ATOM   1080  N   SER A 155     -11.189   6.220  48.715  1.00120.03           N  
ANISOU 1080  N   SER A 155    16850  12492  16266  -1310  -3213     10       N  
ATOM   1081  CA  SER A 155     -12.522   5.658  48.522  1.00115.29           C  
ANISOU 1081  CA  SER A 155    16152  11938  15715  -1780  -2909    -22       C  
ATOM   1082  C   SER A 155     -12.823   5.420  47.043  1.00108.73           C  
ANISOU 1082  C   SER A 155    14707  11339  15265  -1521  -2900   -512       C  
ATOM   1083  O   SER A 155     -12.146   5.930  46.146  1.00121.43           O  
ANISOU 1083  O   SER A 155    15927  13224  16988  -1012  -2988   -819       O  
ATOM   1084  CB  SER A 155     -13.591   6.578  49.122  1.00123.68           C  
ANISOU 1084  CB  SER A 155    17127  13516  16351  -2146  -2277    108       C  
ATOM   1085  OG  SER A 155     -14.907   6.177  48.771  1.00114.72           O  
ANISOU 1085  OG  SER A 155    15720  12542  15326  -2546  -1940    -36       O  
ATOM   1086  N   LEU A 156     -13.882   4.645  46.798  1.00111.18           N  
ANISOU 1086  N   LEU A 156    14941  11560  15742  -1925  -2772   -592       N  
ATOM   1087  CA  LEU A 156     -14.261   4.211  45.457  1.00110.28           C  
ANISOU 1087  CA  LEU A 156    14313  11599  15988  -1765  -2822  -1063       C  
ATOM   1088  C   LEU A 156     -15.775   4.224  45.290  1.00106.18           C  
ANISOU 1088  C   LEU A 156    13485  11419  15439  -2205  -2384  -1158       C  
ATOM   1089  O   LEU A 156     -16.369   3.273  44.771  1.00105.91           O  
ANISOU 1089  O   LEU A 156    13331  11186  15725  -2437  -2476  -1373       O  
ATOM   1090  CB  LEU A 156     -13.714   2.816  45.156  1.00103.12           C  
ANISOU 1090  CB  LEU A 156    13631  10005  15547  -1731  -3358  -1196       C  
ATOM   1091  CG  LEU A 156     -12.205   2.611  45.039  1.00113.60           C  
ANISOU 1091  CG  LEU A 156    15100  10974  17088  -1216  -3874  -1289       C  
ATOM   1092  CD1 LEU A 156     -11.906   1.150  44.742  1.00103.33           C  
ANISOU 1092  CD1 LEU A 156    13979   8950  16332  -1228  -4392  -1478       C  
ATOM   1093  CD2 LEU A 156     -11.632   3.504  43.948  1.00111.70           C  
ANISOU 1093  CD2 LEU A 156    14292  11332  16816   -663  -3772  -1703       C  
ATOM   1094  N   ASP A 157     -16.429   5.291  45.742  1.00124.01           N  
ANISOU 1094  N   ASP A 157    15581  14179  17358  -2328  -1914  -1043       N  
ATOM   1095  CA  ASP A 157     -17.866   5.447  45.556  1.00120.86           C  
ANISOU 1095  CA  ASP A 157    14770  14175  16977  -2683  -1489  -1212       C  
ATOM   1096  C   ASP A 157     -18.123   6.819  44.954  1.00116.90           C  
ANISOU 1096  C   ASP A 157    13723  14361  16333  -2282  -1241  -1418       C  
ATOM   1097  O   ASP A 157     -17.758   7.839  45.550  1.00126.52           O  
ANISOU 1097  O   ASP A 157    15042  15774  17255  -2122  -1071  -1228       O  
ATOM   1098  CB  ASP A 157     -18.628   5.276  46.874  1.00127.16           C  
ANISOU 1098  CB  ASP A 157    15922  14850  17543  -3363  -1115   -888       C  
ATOM   1099  CG  ASP A 157     -20.131   5.456  46.710  1.00131.19           C  
ANISOU 1099  CG  ASP A 157    15915  15802  18130  -3744   -638  -1140       C  
ATOM   1100  OD1 ASP A 157     -20.622   5.439  45.560  1.00144.33           O  
ANISOU 1100  OD1 ASP A 157    17009  17744  20086  -3527   -705  -1541       O  
ATOM   1101  OD2 ASP A 157     -20.825   5.613  47.736  1.00131.45           O1-
ANISOU 1101  OD2 ASP A 157    16097  15924  17924  -4272   -198   -965       O1-
ATOM   1102  N   TYR A 158     -18.748   6.834  43.775  1.00115.85           N  
ANISOU 1102  N   TYR A 158    13039  14565  16414  -2125  -1262  -1804       N  
ATOM   1103  CA  TYR A 158     -19.042   8.086  43.084  1.00109.69           C  
ANISOU 1103  CA  TYR A 158    11763  14391  15525  -1736  -1120  -1982       C  
ATOM   1104  C   TYR A 158     -19.874   9.015  43.961  1.00111.30           C  
ANISOU 1104  C   TYR A 158    11841  14897  15550  -1947   -659  -1867       C  
ATOM   1105  O   TYR A 158     -19.529  10.188  44.147  1.00115.00           O  
ANISOU 1105  O   TYR A 158    12274  15614  15809  -1636   -549  -1769       O  
ATOM   1106  CB  TYR A 158     -19.763   7.785  41.767  1.00108.16           C  
ANISOU 1106  CB  TYR A 158    11045  14476  15576  -1641  -1256  -2401       C  
ATOM   1107  CG  TYR A 158     -20.011   8.978  40.863  1.00115.07           C  
ANISOU 1107  CG  TYR A 158    11455  15924  16341  -1206  -1246  -2569       C  
ATOM   1108  CD1 TYR A 158     -21.057   9.861  41.109  1.00119.58           C  
ANISOU 1108  CD1 TYR A 158    11662  16872  16901  -1262   -955  -2607       C  
ATOM   1109  CD2 TYR A 158     -19.219   9.200  39.745  1.00111.39           C  
ANISOU 1109  CD2 TYR A 158    10916  15614  15793   -755  -1542  -2707       C  
ATOM   1110  CE1 TYR A 158     -21.289  10.944  40.278  1.00113.62           C  
ANISOU 1110  CE1 TYR A 158    10526  16565  16079   -845  -1032  -2725       C  
ATOM   1111  CE2 TYR A 158     -19.446  10.277  38.907  1.00104.86           C  
ANISOU 1111  CE2 TYR A 158     9749  15274  14820   -402  -1572  -2796       C  
ATOM   1112  CZ  TYR A 158     -20.480  11.146  39.178  1.00101.59           C  
ANISOU 1112  CZ  TYR A 158     9018  15160  14421   -432  -1354  -2780       C  
ATOM   1113  OH  TYR A 158     -20.703  12.219  38.345  1.00 99.42           O  
ANISOU 1113  OH  TYR A 158     8448  15296  14030    -59  -1465  -2832       O  
ATOM   1114  N   ASN A 159     -20.974   8.501  44.516  1.00112.23           N  
ANISOU 1114  N   ASN A 159    11877  14994  15770  -2499   -366  -1914       N  
ATOM   1115  CA  ASN A 159     -21.864   9.340  45.312  1.00114.36           C  
ANISOU 1115  CA  ASN A 159    11935  15602  15914  -2729    125  -1920       C  
ATOM   1116  C   ASN A 159     -21.204   9.776  46.615  1.00122.13           C  
ANISOU 1116  C   ASN A 159    13462  16423  16520  -2850    316  -1552       C  
ATOM   1117  O   ASN A 159     -21.392  10.916  47.058  1.00121.78           O  
ANISOU 1117  O   ASN A 159    13260  16701  16309  -2715    602  -1570       O  
ATOM   1118  CB  ASN A 159     -23.171   8.600  45.589  1.00118.07           C  
ANISOU 1118  CB  ASN A 159    12163  16104  16593  -3360    434  -2108       C  
ATOM   1119  CG  ASN A 159     -24.057   8.512  44.364  1.00113.21           C  
ANISOU 1119  CG  ASN A 159    10859  15806  16350  -3212    305  -2554       C  
ATOM   1120  OD1 ASN A 159     -24.121   9.443  43.560  1.00114.48           O  
ANISOU 1120  OD1 ASN A 159    10601  16346  16551  -2688    170  -2738       O  
ATOM   1121  ND2 ASN A 159     -24.743   7.386  44.209  1.00134.41           N  
ANISOU 1121  ND2 ASN A 159    13448  18317  19306  -3688    311  -2719       N  
ATOM   1122  N   GLU A 160     -20.435   8.885  47.248  1.00118.22           N  
ANISOU 1122  N   GLU A 160    13612  15410  15896  -3095    122  -1231       N  
ATOM   1123  CA  GLU A 160     -19.698   9.268  48.451  1.00117.10           C  
ANISOU 1123  CA  GLU A 160    14037  15100  15356  -3180    201   -868       C  
ATOM   1124  C   GLU A 160     -18.669  10.346  48.145  1.00113.20           C  
ANISOU 1124  C   GLU A 160    13505  14754  14751  -2531      5   -844       C  
ATOM   1125  O   GLU A 160     -18.602  11.370  48.836  1.00111.16           O  
ANISOU 1125  O   GLU A 160    13287  14718  14230  -2470    263   -774       O  
ATOM   1126  CB  GLU A 160     -19.009   8.053  49.071  1.00120.76           C  
ANISOU 1126  CB  GLU A 160    15216  14919  15746  -3504   -113   -514       C  
ATOM   1127  CG  GLU A 160     -18.281   8.384  50.365  1.00120.25           C  
ANISOU 1127  CG  GLU A 160    15788  14675  15228  -3634    -90   -121       C  
ATOM   1128  CD  GLU A 160     -17.444   7.234  50.883  1.00123.53           C  
ANISOU 1128  CD  GLU A 160    16935  14396  15604  -3832   -562    254       C  
ATOM   1129  OE1 GLU A 160     -17.113   6.331  50.087  1.00121.37           O  
ANISOU 1129  OE1 GLU A 160    16633  13763  15720  -3666   -987    163       O  
ATOM   1130  OE2 GLU A 160     -17.115   7.235  52.088  1.00131.49           O1-
ANISOU 1130  OE2 GLU A 160    18557  15208  16196  -4145   -536    624       O1-
ATOM   1131  N   ARG A 161     -17.841  10.121  47.121  1.00118.81           N  
ANISOU 1131  N   ARG A 161    14141  15343  15660  -2072   -434   -927       N  
ATOM   1132  CA  ARG A 161     -16.826  11.104  46.755  1.00114.67           C  
ANISOU 1132  CA  ARG A 161    13568  14959  15041  -1509   -601   -916       C  
ATOM   1133  C   ARG A 161     -17.443  12.453  46.418  1.00118.04           C  
ANISOU 1133  C   ARG A 161    13510  15907  15434  -1264   -312  -1088       C  
ATOM   1134  O   ARG A 161     -16.940  13.495  46.853  1.00124.51           O  
ANISOU 1134  O   ARG A 161    14413  16836  16059  -1047   -223   -983       O  
ATOM   1135  CB  ARG A 161     -16.001  10.608  45.571  1.00103.44           C  
ANISOU 1135  CB  ARG A 161    12043  13411  13848  -1119  -1037  -1074       C  
ATOM   1136  CG  ARG A 161     -14.897   9.649  45.924  1.00104.21           C  
ANISOU 1136  CG  ARG A 161    12627  12962  14008  -1123  -1431   -916       C  
ATOM   1137  CD  ARG A 161     -13.829   9.770  44.869  1.00 97.83           C  
ANISOU 1137  CD  ARG A 161    11634  12196  13340   -606  -1748  -1125       C  
ATOM   1138  NE  ARG A 161     -12.872   8.675  44.867  1.00115.38           N  
ANISOU 1138  NE  ARG A 161    14151  13900  15788   -538  -2188  -1142       N  
ATOM   1139  CZ  ARG A 161     -11.737   8.691  44.182  1.00134.41           C  
ANISOU 1139  CZ  ARG A 161    16453  16282  18333   -119  -2466  -1343       C  
ATOM   1140  NH1 ARG A 161     -11.363   9.756  43.491  1.00134.77           N  
ANISOU 1140  NH1 ARG A 161    16178  16780  18247    218  -2332  -1478       N  
ATOM   1141  NH2 ARG A 161     -10.954   7.617  44.198  1.00147.97           N  
ANISOU 1141  NH2 ARG A 161    18389  17491  20342    -50  -2888  -1424       N  
ATOM   1142  N   LEU A 162     -18.520  12.454  45.625  1.00114.65           N  
ANISOU 1142  N   LEU A 162    12566  15771  15224  -1278   -212  -1366       N  
ATOM   1143  CA  LEU A 162     -19.201  13.700  45.292  1.00109.43           C  
ANISOU 1143  CA  LEU A 162    11428  15552  14598  -1026    -11  -1538       C  
ATOM   1144  C   LEU A 162     -19.556  14.494  46.540  1.00112.87           C  
ANISOU 1144  C   LEU A 162    11948  16087  14849  -1222    403  -1466       C  
ATOM   1145  O   LEU A 162     -19.484  15.727  46.533  1.00109.44           O  
ANISOU 1145  O   LEU A 162    11343  15864  14377   -897    485  -1501       O  
ATOM   1146  CB  LEU A 162     -20.460  13.402  44.470  1.00101.82           C  
ANISOU 1146  CB  LEU A 162     9913  14848  13926  -1110     16  -1862       C  
ATOM   1147  CG  LEU A 162     -21.355  14.591  44.116  1.00102.84           C  
ANISOU 1147  CG  LEU A 162     9492  15400  14184   -855    155  -2081       C  
ATOM   1148  CD1 LEU A 162     -20.534  15.747  43.569  1.00100.42           C  
ANISOU 1148  CD1 LEU A 162     9213  15188  13753   -306    -53  -1962       C  
ATOM   1149  CD2 LEU A 162     -22.445  14.191  43.131  1.00110.35           C  
ANISOU 1149  CD2 LEU A 162     9898  16584  15445   -874     34  -2414       C  
ATOM   1150  N   TRP A 163     -19.920  13.807  47.623  1.00107.55           N  
ANISOU 1150  N   TRP A 163    11568  15252  14045  -1773    666  -1369       N  
ATOM   1151  CA  TRP A 163     -20.191  14.483  48.886  1.00109.80           C  
ANISOU 1151  CA  TRP A 163    11997  15652  14072  -2024   1094  -1326       C  
ATOM   1152  C   TRP A 163     -18.962  15.235  49.390  1.00112.04           C  
ANISOU 1152  C   TRP A 163    12686  15807  14076  -1730    957  -1089       C  
ATOM   1153  O   TRP A 163     -19.010  16.451  49.609  1.00105.19           O  
ANISOU 1153  O   TRP A 163    11635  15166  13165  -1486   1135  -1193       O  
ATOM   1154  CB  TRP A 163     -20.667  13.472  49.931  1.00118.66           C  
ANISOU 1154  CB  TRP A 163    13482  16596  15007  -2746   1373  -1203       C  
ATOM   1155  CG  TRP A 163     -21.069  14.142  51.191  1.00127.04           C  
ANISOU 1155  CG  TRP A 163    14654  17861  15755  -3070   1879  -1229       C  
ATOM   1156  CD1 TRP A 163     -22.099  15.020  51.357  1.00126.44           C  
ANISOU 1156  CD1 TRP A 163    14029  18214  15797  -3088   2330  -1603       C  
ATOM   1157  CD2 TRP A 163     -20.401  14.060  52.454  1.00129.87           C  
ANISOU 1157  CD2 TRP A 163    15705  18016  15624  -3382   1961   -911       C  
ATOM   1158  NE1 TRP A 163     -22.138  15.461  52.657  1.00132.39           N  
ANISOU 1158  NE1 TRP A 163    15079  19069  16156  -3427   2749  -1576       N  
ATOM   1159  CE2 TRP A 163     -21.103  14.888  53.350  1.00134.67           C  
ANISOU 1159  CE2 TRP A 163    16157  18984  16026  -3626   2525  -1132       C  
ATOM   1160  CE3 TRP A 163     -19.288  13.353  52.919  1.00121.78           C  
ANISOU 1160  CE3 TRP A 163    15410  16536  14325  -3472   1580   -486       C  
ATOM   1161  CZ2 TRP A 163     -20.726  15.033  54.683  1.00143.75           C  
ANISOU 1161  CZ2 TRP A 163    17893  20091  16634  -3993   2744   -931       C  
ATOM   1162  CZ3 TRP A 163     -18.918  13.496  54.245  1.00123.75           C  
ANISOU 1162  CZ3 TRP A 163    16251  16713  14057  -3815   1737   -248       C  
ATOM   1163  CH2 TRP A 163     -19.636  14.328  55.111  1.00145.76           C  
ANISOU 1163  CH2 TRP A 163    18905  19902  16576  -4091   2328   -464       C  
ATOM   1164  N   ALA A 164     -17.847  14.523  49.595  1.00117.28           N  
ANISOU 1164  N   ALA A 164    13888  16083  14591  -1744    615   -798       N  
ATOM   1165  CA  ALA A 164     -16.643  15.167  50.119  1.00114.59           C  
ANISOU 1165  CA  ALA A 164    13918  15612  14010  -1493    452   -600       C  
ATOM   1166  C   ALA A 164     -16.147  16.267  49.188  1.00107.68           C  
ANISOU 1166  C   ALA A 164    12690  14929  13293   -900    306   -722       C  
ATOM   1167  O   ALA A 164     -15.762  17.351  49.644  1.00110.25           O  
ANISOU 1167  O   ALA A 164    13060  15348  13482   -718    408   -707       O  
ATOM   1168  CB  ALA A 164     -15.545  14.126  50.344  1.00116.37           C  
ANISOU 1168  CB  ALA A 164    14693  15366  14158  -1552     18   -322       C  
ATOM   1169  N   TRP A 165     -16.152  16.006  47.881  1.00107.35           N  
ANISOU 1169  N   TRP A 165    12325  14944  13517   -626     65   -845       N  
ATOM   1170  CA  TRP A 165     -15.709  17.005  46.914  1.00 98.58           C  
ANISOU 1170  CA  TRP A 165    10931  14022  12503   -129    -76   -920       C  
ATOM   1171  C   TRP A 165     -16.613  18.233  46.937  1.00 98.53           C  
ANISOU 1171  C   TRP A 165    10545  14328  12564     -6    207  -1074       C  
ATOM   1172  O   TRP A 165     -16.133  19.373  46.963  1.00 94.79           O  
ANISOU 1172  O   TRP A 165    10062  13906  12046    281    210  -1036       O  
ATOM   1173  CB  TRP A 165     -15.675  16.383  45.517  1.00 95.19           C  
ANISOU 1173  CB  TRP A 165    10256  13638  12274     55   -362  -1045       C  
ATOM   1174  CG  TRP A 165     -15.101  17.269  44.455  1.00 96.14           C  
ANISOU 1174  CG  TRP A 165    10178  13940  12409    495   -528  -1076       C  
ATOM   1175  CD1 TRP A 165     -13.814  17.279  44.001  1.00 94.27           C  
ANISOU 1175  CD1 TRP A 165    10102  13602  12114    720   -762  -1016       C  
ATOM   1176  CD2 TRP A 165     -15.796  18.276  43.711  1.00 99.57           C  
ANISOU 1176  CD2 TRP A 165    10229  14682  12921    733   -481  -1173       C  
ATOM   1177  NE1 TRP A 165     -13.666  18.228  43.019  1.00 94.95           N  
ANISOU 1177  NE1 TRP A 165     9962  13933  12180   1024   -812  -1044       N  
ATOM   1178  CE2 TRP A 165     -14.869  18.855  42.824  1.00101.55           C  
ANISOU 1178  CE2 TRP A 165    10496  14994  13093   1052   -681  -1109       C  
ATOM   1179  CE3 TRP A 165     -17.114  18.744  43.709  1.00 87.53           C  
ANISOU 1179  CE3 TRP A 165     8338  13374  11544    705   -310  -1322       C  
ATOM   1180  CZ2 TRP A 165     -15.216  19.877  41.946  1.00100.08           C  
ANISOU 1180  CZ2 TRP A 165    10058  15045  12924   1320   -744  -1115       C  
ATOM   1181  CZ3 TRP A 165     -17.456  19.759  42.838  1.00 81.01           C  
ANISOU 1181  CZ3 TRP A 165     7214  12765  10800   1038   -422  -1365       C  
ATOM   1182  CH2 TRP A 165     -16.511  20.315  41.967  1.00 77.97           C  
ANISOU 1182  CH2 TRP A 165     6937  12402  10285   1331   -652  -1226       C  
ATOM   1183  N   GLU A 166     -17.931  18.018  46.934  1.00105.30           N  
ANISOU 1183  N   GLU A 166    11061  15371  13576   -221    434  -1278       N  
ATOM   1184  CA  GLU A 166     -18.869  19.134  46.842  1.00 97.24           C  
ANISOU 1184  CA  GLU A 166     9584  14634  12728    -47    641  -1501       C  
ATOM   1185  C   GLU A 166     -18.956  19.901  48.157  1.00103.75           C  
ANISOU 1185  C   GLU A 166    10548  15478  13396   -192   1008  -1533       C  
ATOM   1186  O   GLU A 166     -18.901  21.137  48.168  1.00102.79           O  
ANISOU 1186  O   GLU A 166    10276  15433  13347    123   1044  -1605       O  
ATOM   1187  CB  GLU A 166     -20.250  18.619  46.430  1.00 90.83           C  
ANISOU 1187  CB  GLU A 166     8292  14031  12187   -232    752  -1781       C  
ATOM   1188  CG  GLU A 166     -21.391  19.609  46.601  1.00107.15           C  
ANISOU 1188  CG  GLU A 166     9839  16372  14501   -130   1009  -2093       C  
ATOM   1189  CD  GLU A 166     -21.314  20.777  45.638  1.00106.50           C  
ANISOU 1189  CD  GLU A 166     9482  16378  14603    442    710  -2114       C  
ATOM   1190  OE1 GLU A 166     -20.538  20.706  44.662  1.00 99.09           O  
ANISOU 1190  OE1 GLU A 166     8699  15366  13584    703    332  -1912       O  
ATOM   1191  OE2 GLU A 166     -22.041  21.768  45.857  1.00102.78           O1-
ANISOU 1191  OE2 GLU A 166     8645  16044  14363    618    854  -2346       O1-
ATOM   1192  N   SER A 167     -19.099  19.185  49.276  1.00105.73           N  
ANISOU 1192  N   SER A 167    11110  15649  13414   -690   1278  -1485       N  
ATOM   1193  CA  SER A 167     -19.313  19.852  50.558  1.00106.41           C  
ANISOU 1193  CA  SER A 167    11319  15822  13289   -904   1684  -1579       C  
ATOM   1194  C   SER A 167     -18.122  20.719  50.943  1.00107.48           C  
ANISOU 1194  C   SER A 167    11802  15812  13225   -624   1537  -1407       C  
ATOM   1195  O   SER A 167     -18.293  21.792  51.534  1.00107.31           O  
ANISOU 1195  O   SER A 167    11683  15906  13184   -533   1778  -1584       O  
ATOM   1196  CB  SER A 167     -19.600  18.819  51.648  1.00112.96           C  
ANISOU 1196  CB  SER A 167    12527  16587  13804  -1562   1970  -1492       C  
ATOM   1197  OG  SER A 167     -20.747  18.049  51.332  1.00111.31           O  
ANISOU 1197  OG  SER A 167    11965  16516  13810  -1879   2154  -1683       O  
ATOM   1198  N   TRP A 168     -16.906  20.272  50.619  1.00103.78           N  
ANISOU 1198  N   TRP A 168    11704  15083  12643   -487   1142  -1113       N  
ATOM   1199  CA  TRP A 168     -15.730  21.096  50.882  1.00104.32           C  
ANISOU 1199  CA  TRP A 168    12038  15021  12578   -216    975   -983       C  
ATOM   1200  C   TRP A 168     -15.799  22.416  50.124  1.00104.65           C  
ANISOU 1200  C   TRP A 168    11690  15184  12889    247    937  -1119       C  
ATOM   1201  O   TRP A 168     -15.434  23.467  50.660  1.00117.64           O  
ANISOU 1201  O   TRP A 168    13406  16809  14482    382   1024  -1165       O  
ATOM   1202  CB  TRP A 168     -14.456  20.341  50.510  1.00101.78           C  
ANISOU 1202  CB  TRP A 168    12060  14424  12188   -122    543   -722       C  
ATOM   1203  CG  TRP A 168     -13.219  21.160  50.702  1.00 97.98           C  
ANISOU 1203  CG  TRP A 168    11781  13824  11622    145    361   -628       C  
ATOM   1204  CD1 TRP A 168     -12.423  21.679  49.725  1.00 92.35           C  
ANISOU 1204  CD1 TRP A 168    10917  13090  11081    528    116   -602       C  
ATOM   1205  CD2 TRP A 168     -12.636  21.561  51.948  1.00101.53           C  
ANISOU 1205  CD2 TRP A 168    12616  14178  11781      8    420   -568       C  
ATOM   1206  NE1 TRP A 168     -11.381  22.377  50.283  1.00101.26           N  
ANISOU 1206  NE1 TRP A 168    12278  14101  12095    633     30   -541       N  
ATOM   1207  CE2 TRP A 168     -11.488  22.319  51.647  1.00104.62           C  
ANISOU 1207  CE2 TRP A 168    13032  14476  12242    340    187   -526       C  
ATOM   1208  CE3 TRP A 168     -12.970  21.350  53.290  1.00105.09           C  
ANISOU 1208  CE3 TRP A 168    13411  14634  11883   -400    654   -554       C  
ATOM   1209  CZ2 TRP A 168     -10.674  22.868  52.634  1.00 99.22           C  
ANISOU 1209  CZ2 TRP A 168    12668  13689  11342    310    143   -495       C  
ATOM   1210  CZ3 TRP A 168     -12.159  21.896  54.269  1.00102.86           C  
ANISOU 1210  CZ3 TRP A 168    13490  14268  11326   -427    602   -506       C  
ATOM   1211  CH2 TRP A 168     -11.026  22.647  53.936  1.00101.23           C  
ANISOU 1211  CH2 TRP A 168    13265  13954  11246    -57    331   -489       C  
ATOM   1212  N   ARG A 169     -16.264  22.382  48.876  1.00 87.61           N  
ANISOU 1212  N   ARG A 169     9147  13129  11011    483    776  -1177       N  
ATOM   1213  CA  ARG A 169     -16.330  23.591  48.067  1.00 89.54           C  
ANISOU 1213  CA  ARG A 169     9087  13443  11492    911    662  -1236       C  
ATOM   1214  C   ARG A 169     -17.558  24.439  48.362  1.00 97.46           C  
ANISOU 1214  C   ARG A 169     9678  14613  12739    974    928  -1541       C  
ATOM   1215  O   ARG A 169     -17.615  25.591  47.916  1.00 99.29           O  
ANISOU 1215  O   ARG A 169     9712  14826  13187   1334    822  -1586       O  
ATOM   1216  CB  ARG A 169     -16.307  23.230  46.582  1.00 80.13           C  
ANISOU 1216  CB  ARG A 169     7698  12308  10438   1129    334  -1162       C  
ATOM   1217  CG  ARG A 169     -14.939  22.828  46.076  1.00 72.64           C  
ANISOU 1217  CG  ARG A 169     7059  11214   9326   1207     58   -937       C  
ATOM   1218  CD  ARG A 169     -15.048  21.956  44.843  1.00 86.00           C  
ANISOU 1218  CD  ARG A 169     8601  12999  11075   1250   -181   -946       C  
ATOM   1219  NE  ARG A 169     -13.737  21.608  44.309  1.00 89.30           N  
ANISOU 1219  NE  ARG A 169     9246  13314  11371   1337   -409   -819       N  
ATOM   1220  CZ  ARG A 169     -12.943  20.678  44.820  1.00 90.67           C  
ANISOU 1220  CZ  ARG A 169     9706  13293  11453   1172   -479   -774       C  
ATOM   1221  NH1 ARG A 169     -13.298  19.973  45.882  1.00 86.01           N  
ANISOU 1221  NH1 ARG A 169     9299  12567  10813    874   -357   -770       N  
ATOM   1222  NH2 ARG A 169     -11.767  20.444  44.247  1.00106.43           N  
ANISOU 1222  NH2 ARG A 169    11808  15221  13409   1297   -687   -740       N  
ATOM   1223  N   SER A 170     -18.533  23.909  49.096  1.00113.88           N  
ANISOU 1223  N   SER A 170    11617  16840  14812    624   1268  -1766       N  
ATOM   1224  CA  SER A 170     -19.769  24.629  49.375  1.00121.19           C  
ANISOU 1224  CA  SER A 170    12053  17962  16033    673   1554  -2158       C  
ATOM   1225  C   SER A 170     -19.775  25.319  50.730  1.00132.74           C  
ANISOU 1225  C   SER A 170    13646  19445  17345    512   1949  -2360       C  
ATOM   1226  O   SER A 170     -20.397  26.375  50.870  1.00140.72           O  
ANISOU 1226  O   SER A 170    14284  20528  18656    744   2087  -2687       O  
ATOM   1227  CB  SER A 170     -20.965  23.676  49.297  1.00111.02           C  
ANISOU 1227  CB  SER A 170    10413  16890  14879    352   1751  -2386       C  
ATOM   1228  OG  SER A 170     -20.915  22.716  50.338  1.00137.73           O  
ANISOU 1228  OG  SER A 170    14152  20274  17906   -214   2068  -2331       O  
ATOM   1229  N   GLU A 171     -19.106  24.749  51.732  1.00133.22           N  
ANISOU 1229  N   GLU A 171    14232  19434  16952    127   2103  -2194       N  
ATOM   1230  CA  GLU A 171     -19.070  25.342  53.061  1.00136.99           C  
ANISOU 1230  CA  GLU A 171    14897  19966  17186    -79   2476  -2392       C  
ATOM   1231  C   GLU A 171     -17.756  26.043  53.368  1.00122.52           C  
ANISOU 1231  C   GLU A 171    13490  17901  15160    128   2254  -2185       C  
ATOM   1232  O   GLU A 171     -17.728  26.918  54.240  1.00127.82           O  
ANISOU 1232  O   GLU A 171    14210  18604  15753    120   2491  -2421       O  
ATOM   1233  CB  GLU A 171     -19.342  24.269  54.121  1.00142.03           C  
ANISOU 1233  CB  GLU A 171    15868  20716  17380   -732   2826  -2370       C  
ATOM   1234  CG  GLU A 171     -20.768  23.744  54.086  1.00162.55           C  
ANISOU 1234  CG  GLU A 171    17993  23594  20173  -1040   3199  -2691       C  
ATOM   1235  CD  GLU A 171     -20.889  22.326  54.602  1.00172.58           C  
ANISOU 1235  CD  GLU A 171    19648  24862  21062  -1678   3353  -2477       C  
ATOM   1236  OE1 GLU A 171     -20.200  21.985  55.587  1.00191.39           O  
ANISOU 1236  OE1 GLU A 171    22665  27136  22918  -2026   3410  -2236       O  
ATOM   1237  OE2 GLU A 171     -21.675  21.551  54.019  1.00150.82           O1-
ANISOU 1237  OE2 GLU A 171    16575  22190  18538  -1840   3384  -2542       O1-
ATOM   1238  N   VAL A 172     -16.681  25.687  52.673  1.00101.07           N  
ANISOU 1238  N   VAL A 172    11044  14970  12389    301   1821  -1805       N  
ATOM   1239  CA  VAL A 172     -15.400  26.361  52.818  1.00106.93           C  
ANISOU 1239  CA  VAL A 172    12107  15498  13022    510   1585  -1634       C  
ATOM   1240  C   VAL A 172     -15.147  27.334  51.674  1.00102.02           C  
ANISOU 1240  C   VAL A 172    11209  14771  12783   1001   1315  -1592       C  
ATOM   1241  O   VAL A 172     -14.640  28.433  51.894  1.00104.90           O  
ANISOU 1241  O   VAL A 172    11626  15007  13225   1202   1285  -1645       O  
ATOM   1242  CB  VAL A 172     -14.265  25.321  52.930  1.00110.22           C  
ANISOU 1242  CB  VAL A 172    13015  15741  13123    339   1295  -1281       C  
ATOM   1243  CG1 VAL A 172     -12.914  26.005  53.081  1.00105.76           C  
ANISOU 1243  CG1 VAL A 172    12718  14978  12490    543   1044  -1156       C  
ATOM   1244  CG2 VAL A 172     -14.532  24.391  54.100  1.00120.73           C  
ANISOU 1244  CG2 VAL A 172    14708  17121  14041   -178   1512  -1257       C  
ATOM   1245  N   GLY A 173     -15.515  26.956  50.449  1.00101.34           N  
ANISOU 1245  N   GLY A 173    12401  13929  12176    897   1111  -1963       N  
ATOM   1246  CA  GLY A 173     -15.282  27.838  49.317  1.00106.49           C  
ANISOU 1246  CA  GLY A 173    13063  14406  12994   1081    922  -1954       C  
ATOM   1247  C   GLY A 173     -16.155  29.078  49.344  1.00102.25           C  
ANISOU 1247  C   GLY A 173    12368  13872  12611   1314    934  -2136       C  
ATOM   1248  O   GLY A 173     -15.706  30.172  48.989  1.00 97.46           O  
ANISOU 1248  O   GLY A 173    11857  13078  12096   1475    801  -2161       O  
ATOM   1249  N   LYS A 174     -17.411  28.929  49.771  1.00107.84           N  
ANISOU 1249  N   LYS A 174    12825  14789  13362   1336   1088  -2268       N  
ATOM   1250  CA  LYS A 174     -18.345  30.050  49.726  1.00100.85           C  
ANISOU 1250  CA  LYS A 174    11741  13912  12665   1588   1089  -2463       C  
ATOM   1251  C   LYS A 174     -17.995  31.111  50.763  1.00114.05           C  
ANISOU 1251  C   LYS A 174    13529  15514  14290   1718   1169  -2657       C  
ATOM   1252  O   LYS A 174     -18.168  32.310  50.512  1.00112.03           O  
ANISOU 1252  O   LYS A 174    13249  15101  14217   1960   1062  -2780       O  
ATOM   1253  CB  LYS A 174     -19.772  29.542  49.922  1.00101.33           C  
ANISOU 1253  CB  LYS A 174    11466  14250  12786   1566   1246  -2566       C  
ATOM   1254  CG  LYS A 174     -20.288  28.726  48.748  1.00103.07           C  
ANISOU 1254  CG  LYS A 174    11535  14514  13111   1484   1123  -2414       C  
ATOM   1255  CD  LYS A 174     -21.785  28.492  48.837  1.00115.47           C  
ANISOU 1255  CD  LYS A 174    12729  16344  14799   1505   1244  -2539       C  
ATOM   1256  CE  LYS A 174     -22.274  27.686  47.645  1.00118.38           C  
ANISOU 1256  CE  LYS A 174    12959  16750  15270   1411   1095  -2393       C  
ATOM   1257  NZ  LYS A 174     -23.747  27.473  47.676  1.00107.84           N  
ANISOU 1257  NZ  LYS A 174    11229  15677  14070   1423   1192  -2511       N  
ATOM   1258  N   GLN A 175     -17.507  30.692  51.936  1.00116.70           N  
ANISOU 1258  N   GLN A 175    14000  15957  14384   1556   1338  -2688       N  
ATOM   1259  CA  GLN A 175     -16.994  31.655  52.906  1.00109.30           C  
ANISOU 1259  CA  GLN A 175    13219  14944  13367   1651   1391  -2869       C  
ATOM   1260  C   GLN A 175     -15.854  32.472  52.314  1.00106.76           C  
ANISOU 1260  C   GLN A 175    13143  14295  13126   1737   1154  -2782       C  
ATOM   1261  O   GLN A 175     -15.749  33.680  52.559  1.00107.43           O  
ANISOU 1261  O   GLN A 175    13287  14221  13311   1924   1100  -2952       O  
ATOM   1262  CB  GLN A 175     -16.516  30.938  54.169  1.00106.97           C  
ANISOU 1262  CB  GLN A 175    13063  14822  12759   1419   1574  -2861       C  
ATOM   1263  CG  GLN A 175     -17.587  30.202  54.947  1.00115.61           C  
ANISOU 1263  CG  GLN A 175    13937  16264  13726   1292   1834  -2946       C  
ATOM   1264  CD  GLN A 175     -17.049  29.624  56.242  1.00118.03           C  
ANISOU 1264  CD  GLN A 175    14419  16730  13698   1058   1991  -2920       C  
ATOM   1265  OE1 GLN A 175     -16.319  30.291  56.976  1.00115.17           O  
ANISOU 1265  OE1 GLN A 175    14256  16297  13208   1095   1989  -3028       O  
ATOM   1266  NE2 GLN A 175     -17.403  28.377  56.527  1.00124.81           N  
ANISOU 1266  NE2 GLN A 175    15213  17799  14410    802   2108  -2766       N  
ATOM   1267  N   LEU A 176     -14.993  31.829  51.524  1.00 91.04           N  
ANISOU 1267  N   LEU A 176    11289  12200  11100   1598   1010  -2526       N  
ATOM   1268  CA  LEU A 176     -13.819  32.477  50.959  1.00 89.73           C  
ANISOU 1268  CA  LEU A 176    11348  11768  10977   1626    804  -2414       C  
ATOM   1269  C   LEU A 176     -14.138  33.358  49.760  1.00 87.39           C  
ANISOU 1269  C   LEU A 176    10985  11289  10932   1813    603  -2379       C  
ATOM   1270  O   LEU A 176     -13.286  34.162  49.364  1.00 88.92           O  
ANISOU 1270  O   LEU A 176    11354  11251  11182   1853    434  -2312       O  
ATOM   1271  CB  LEU A 176     -12.793  31.418  50.548  1.00 83.26           C  
ANISOU 1271  CB  LEU A 176    10669  10942  10024   1413    741  -2174       C  
ATOM   1272  CG  LEU A 176     -12.285  30.516  51.673  1.00 87.38           C  
ANISOU 1272  CG  LEU A 176    11300  11598  10305   1216    880  -2153       C  
ATOM   1273  CD1 LEU A 176     -11.585  29.287  51.111  1.00 78.01           C  
ANISOU 1273  CD1 LEU A 176    10178  10412   9052   1039    811  -1930       C  
ATOM   1274  CD2 LEU A 176     -11.371  31.288  52.609  1.00 99.44           C  
ANISOU 1274  CD2 LEU A 176    13034  13028  11722   1221    872  -2243       C  
ATOM   1275  N   ARG A 177     -15.331  33.232  49.177  1.00 92.84           N  
ANISOU 1275  N   ARG A 177    11426  12078  11772   1914    603  -2409       N  
ATOM   1276  CA  ARG A 177     -15.624  33.953  47.939  1.00 94.61           C  
ANISOU 1276  CA  ARG A 177    11593  12136  12219   2070    377  -2327       C  
ATOM   1277  C   ARG A 177     -15.621  35.469  48.110  1.00 91.15           C  
ANISOU 1277  C   ARG A 177    11219  11454  11960   2297    262  -2464       C  
ATOM   1278  O   ARG A 177     -14.908  36.145  47.349  1.00 87.70           O  
ANISOU 1278  O   ARG A 177    10945  10779  11598   2316     45  -2315       O  
ATOM   1279  CB  ARG A 177     -16.946  33.453  47.347  1.00 88.31           C  
ANISOU 1279  CB  ARG A 177    10496  11517  11542   2125    391  -2338       C  
ATOM   1280  CG  ARG A 177     -17.379  34.216  46.109  1.00 98.47           C  
ANISOU 1280  CG  ARG A 177    11706  12652  13058   2298    138  -2254       C  
ATOM   1281  CD  ARG A 177     -16.276  34.240  45.060  1.00 98.97           C  
ANISOU 1281  CD  ARG A 177    11992  12554  13057   2185    -65  -1996       C  
ATOM   1282  NE  ARG A 177     -16.619  35.112  43.944  1.00118.43           N  
ANISOU 1282  NE  ARG A 177    14422  14859  15716   2337   -325  -1893       N  
ATOM   1283  CZ  ARG A 177     -17.071  34.686  42.773  1.00116.08           C  
ANISOU 1283  CZ  ARG A 177    14014  14644  15448   2307   -462  -1743       C  
ATOM   1284  NH1 ARG A 177     -17.212  33.396  42.514  1.00113.42           N  
ANISOU 1284  NH1 ARG A 177    13591  14529  14973   2132   -367  -1694       N  
ATOM   1285  NH2 ARG A 177     -17.390  35.576  41.837  1.00107.22           N  
ANISOU 1285  NH2 ARG A 177    12874  13368  14496   2449   -717  -1639       N  
ATOM   1286  N   PRO A 178     -16.366  36.070  49.047  1.00 94.66           N  
ANISOU 1286  N   PRO A 178    11546  11936  12485   2468    388  -2744       N  
ATOM   1287  CA  PRO A 178     -16.287  37.535  49.177  1.00 97.88           C  
ANISOU 1287  CA  PRO A 178    12040  12056  13092   2694    248  -2888       C  
ATOM   1288  C   PRO A 178     -14.920  38.014  49.622  1.00 98.99           C  
ANISOU 1288  C   PRO A 178    12501  11996  13116   2589    190  -2851       C  
ATOM   1289  O   PRO A 178     -14.486  39.098  49.211  1.00105.81           O  
ANISOU 1289  O   PRO A 178    13508  12551  14144   2690    -25  -2815       O  
ATOM   1290  CB  PRO A 178     -17.365  37.856  50.220  1.00106.84           C  
ANISOU 1290  CB  PRO A 178    12959  13340  14294   2879    449  -3242       C  
ATOM   1291  CG  PRO A 178     -17.490  36.614  51.014  1.00104.73           C  
ANISOU 1291  CG  PRO A 178    12619  13423  13750   2662    729  -3266       C  
ATOM   1292  CD  PRO A 178     -17.286  35.491  50.044  1.00 96.23           C  
ANISOU 1292  CD  PRO A 178    11532  12434  12596   2459    662  -2956       C  
ATOM   1293  N   LEU A 179     -14.226  37.229  50.448  1.00101.19           N  
ANISOU 1293  N   LEU A 179    12894  12435  13120   2378    360  -2846       N  
ATOM   1294  CA  LEU A 179     -12.881  37.598  50.877  1.00 97.06           C  
ANISOU 1294  CA  LEU A 179    12656  11748  12475   2258    296  -2802       C  
ATOM   1295  C   LEU A 179     -11.913  37.605  49.701  1.00 95.05           C  
ANISOU 1295  C   LEU A 179    12544  11323  12246   2142     77  -2494       C  
ATOM   1296  O   LEU A 179     -11.125  38.543  49.537  1.00 90.87           O  
ANISOU 1296  O   LEU A 179    12200  10534  11793   2150    -91  -2452       O  
ATOM   1297  CB  LEU A 179     -12.401  36.638  51.965  1.00 88.65           C  
ANISOU 1297  CB  LEU A 179    11661  10917  11107   2053    505  -2834       C  
ATOM   1298  CG  LEU A 179     -13.207  36.640  53.263  1.00 89.67           C  
ANISOU 1298  CG  LEU A 179    11679  11254  11136   2116    746  -3137       C  
ATOM   1299  CD1 LEU A 179     -12.925  35.380  54.059  1.00 98.63           C  
ANISOU 1299  CD1 LEU A 179    12844  12667  11962   1871    935  -3068       C  
ATOM   1300  CD2 LEU A 179     -12.894  37.882  54.086  1.00 94.91           C  
ANISOU 1300  CD2 LEU A 179    12488  11737  11838   2243    717  -3396       C  
ATOM   1301  N   TYR A 180     -11.958  36.559  48.868  1.00 85.21           N  
ANISOU 1301  N   TYR A 180    11213  10231  10933   2020     78  -2286       N  
ATOM   1302  CA  TYR A 180     -11.045  36.488  47.732  1.00 77.73           C  
ANISOU 1302  CA  TYR A 180    10381   9177   9975   1899   -102  -2014       C  
ATOM   1303  C   TYR A 180     -11.263  37.638  46.759  1.00 86.14           C  
ANISOU 1303  C   TYR A 180    11462   9999  11268   2039   -338  -1931       C  
ATOM   1304  O   TYR A 180     -10.321  38.055  46.077  1.00 89.69           O  
ANISOU 1304  O   TYR A 180    12068  10296  11713   1941   -500  -1740       O  
ATOM   1305  CB  TYR A 180     -11.190  35.154  47.001  1.00 74.63           C  
ANISOU 1305  CB  TYR A 180     9876   9001   9478   1768    -54  -1854       C  
ATOM   1306  CG  TYR A 180      -9.939  34.770  46.244  1.00 73.89           C  
ANISOU 1306  CG  TYR A 180     9922   8880   9273   1588   -152  -1630       C  
ATOM   1307  CD1 TYR A 180      -8.872  34.162  46.889  1.00 77.01           C  
ANISOU 1307  CD1 TYR A 180    10441   9328   9492   1427    -72  -1608       C  
ATOM   1308  CD2 TYR A 180      -9.811  35.057  44.892  1.00 77.61           C  
ANISOU 1308  CD2 TYR A 180    10395   9283   9811   1580   -330  -1445       C  
ATOM   1309  CE1 TYR A 180      -7.722  33.823  46.201  1.00 75.00           C  
ANISOU 1309  CE1 TYR A 180    10279   9066   9153   1281   -153  -1432       C  
ATOM   1310  CE2 TYR A 180      -8.665  34.726  44.197  1.00 80.79           C  
ANISOU 1310  CE2 TYR A 180    10902   9698  10096   1413   -395  -1265       C  
ATOM   1311  CZ  TYR A 180      -7.624  34.110  44.856  1.00 76.78           C  
ANISOU 1311  CZ  TYR A 180    10489   9247   9436   1272   -300  -1271       C  
ATOM   1312  OH  TYR A 180      -6.481  33.780  44.165  1.00 79.08           O  
ANISOU 1312  OH  TYR A 180    10850   9570   9626   1122   -357  -1117       O  
ATOM   1313  N   GLU A 181     -12.488  38.160  46.676  1.00 96.67           N  
ANISOU 1313  N   GLU A 181    12628  11296  12805   2262   -368  -2062       N  
ATOM   1314  CA  GLU A 181     -12.735  39.309  45.810  1.00104.06           C  
ANISOU 1314  CA  GLU A 181    13589  11965  13982   2412   -627  -1975       C  
ATOM   1315  C   GLU A 181     -12.033  40.554  46.336  1.00110.28           C  
ANISOU 1315  C   GLU A 181    14594  12439  14869   2461   -739  -2052       C  
ATOM   1316  O   GLU A 181     -11.435  41.311  45.561  1.00110.26           O  
ANISOU 1316  O   GLU A 181    14743  12196  14955   2419   -969  -1853       O  
ATOM   1317  CB  GLU A 181     -14.236  39.559  45.673  1.00101.96           C  
ANISOU 1317  CB  GLU A 181    13069  11734  13939   2664   -644  -2120       C  
ATOM   1318  CG  GLU A 181     -14.987  38.459  44.949  1.00105.86           C  
ANISOU 1318  CG  GLU A 181    13343  12503  14376   2612   -594  -2017       C  
ATOM   1319  CD  GLU A 181     -16.477  38.721  44.880  1.00115.50           C  
ANISOU 1319  CD  GLU A 181    14279  13777  15828   2861   -612  -2175       C  
ATOM   1320  OE1 GLU A 181     -16.952  39.648  45.570  1.00125.41           O  
ANISOU 1320  OE1 GLU A 181    15489  14889  17272   3087   -610  -2412       O  
ATOM   1321  OE2 GLU A 181     -17.173  38.003  44.132  1.00108.80           O1-
ANISOU 1321  OE2 GLU A 181    13242  13117  14982   2835   -633  -2079       O1-
ATOM   1322  N   GLU A 182     -12.097  40.784  47.649  1.00110.33           N  
ANISOU 1322  N   GLU A 182    14621  12449  14850   2531   -582  -2340       N  
ATOM   1323  CA  GLU A 182     -11.402  41.923  48.237  1.00102.87           C  
ANISOU 1323  CA  GLU A 182    13891  11206  13988   2563   -685  -2449       C  
ATOM   1324  C   GLU A 182      -9.896  41.695  48.273  1.00 92.11           C  
ANISOU 1324  C   GLU A 182    12753   9824  12422   2286   -709  -2269       C  
ATOM   1325  O   GLU A 182      -9.121  42.654  48.166  1.00 89.40           O  
ANISOU 1325  O   GLU A 182    12605   9194  12169   2243   -890  -2207       O  
ATOM   1326  CB  GLU A 182     -11.939  42.187  49.642  1.00100.73           C  
ANISOU 1326  CB  GLU A 182    13568  10987  13718   2714   -498  -2842       C  
ATOM   1327  CG  GLU A 182     -11.674  43.585  50.165  1.00109.44           C  
ANISOU 1327  CG  GLU A 182    14841  11732  15010   2851   -641  -3039       C  
ATOM   1328  CD  GLU A 182     -12.272  43.803  51.539  1.00114.03           C  
ANISOU 1328  CD  GLU A 182    15350  12410  15565   3010   -434  -3468       C  
ATOM   1329  OE1 GLU A 182     -13.014  42.914  52.009  1.00114.86           O  
ANISOU 1329  OE1 GLU A 182    15249  12867  15525   3022   -183  -3589       O  
ATOM   1330  OE2 GLU A 182     -12.008  44.861  52.147  1.00120.84           O1-
ANISOU 1330  OE2 GLU A 182    16363  13005  16548   3111   -520  -3689       O1-
ATOM   1331  N   TYR A 183      -9.470  40.439  48.426  1.00 82.87           N  
ANISOU 1331  N   TYR A 183    11550   8944  10994   2097   -540  -2185       N  
ATOM   1332  CA  TYR A 183      -8.053  40.101  48.341  1.00 85.04           C  
ANISOU 1332  CA  TYR A 183    11991   9232  11090   1847   -568  -2002       C  
ATOM   1333  C   TYR A 183      -7.477  40.439  46.970  1.00 89.21           C  
ANISOU 1333  C   TYR A 183    12583   9627  11684   1748   -781  -1699       C  
ATOM   1334  O   TYR A 183      -6.315  40.846  46.870  1.00 90.66           O  
ANISOU 1334  O   TYR A 183    12932   9689  11827   1587   -881  -1578       O  
ATOM   1335  CB  TYR A 183      -7.880  38.613  48.682  1.00 89.13           C  
ANISOU 1335  CB  TYR A 183    12428  10076  11360   1703   -365  -1974       C  
ATOM   1336  CG  TYR A 183      -6.676  37.905  48.094  1.00 89.43           C  
ANISOU 1336  CG  TYR A 183    12539  10194  11246   1476   -402  -1733       C  
ATOM   1337  CD1 TYR A 183      -5.454  37.895  48.755  1.00 88.21           C  
ANISOU 1337  CD1 TYR A 183    12534  10021  10962   1323   -400  -1728       C  
ATOM   1338  CD2 TYR A 183      -6.779  37.200  46.901  1.00 98.62           C  
ANISOU 1338  CD2 TYR A 183    13604  11476  12392   1419   -434  -1533       C  
ATOM   1339  CE1 TYR A 183      -4.361  37.229  48.225  1.00 92.69           C  
ANISOU 1339  CE1 TYR A 183    13130  10679  11411   1136   -427  -1532       C  
ATOM   1340  CE2 TYR A 183      -5.694  36.535  46.365  1.00 98.73           C  
ANISOU 1340  CE2 TYR A 183    13660  11582  12270   1231   -451  -1354       C  
ATOM   1341  CZ  TYR A 183      -4.487  36.550  47.031  1.00 89.84           C  
ANISOU 1341  CZ  TYR A 183    12662  10433  11039   1098   -444  -1356       C  
ATOM   1342  OH  TYR A 183      -3.401  35.889  46.507  1.00 85.26           O  
ANISOU 1342  OH  TYR A 183    12093   9958  10345    930   -458  -1200       O  
ATOM   1343  N   VAL A 184      -8.278  40.305  45.910  1.00 94.57           N  
ANISOU 1343  N   VAL A 184    13131  10343  12458   1828   -856  -1572       N  
ATOM   1344  CA  VAL A 184      -7.803  40.654  44.574  1.00 88.33           C  
ANISOU 1344  CA  VAL A 184    12405   9457  11701   1723  -1060  -1275       C  
ATOM   1345  C   VAL A 184      -7.719  42.167  44.397  1.00 88.90           C  
ANISOU 1345  C   VAL A 184    12623   9154  12001   1800  -1301  -1236       C  
ATOM   1346  O   VAL A 184      -6.815  42.669  43.716  1.00 91.78           O  
ANISOU 1346  O   VAL A 184    13131   9388  12352   1630  -1459  -1002       O  
ATOM   1347  CB  VAL A 184      -8.706  39.999  43.510  1.00 79.72           C  
ANISOU 1347  CB  VAL A 184    11134   8542  10614   1774  -1080  -1156       C  
ATOM   1348  CG1 VAL A 184      -8.402  40.549  42.123  1.00 97.47           C  
ANISOU 1348  CG1 VAL A 184    13453  10682  12899   1688  -1316   -857       C  
ATOM   1349  CG2 VAL A 184      -8.528  38.489  43.530  1.00 78.89           C  
ANISOU 1349  CG2 VAL A 184    10927   8767  10282   1642   -880  -1151       C  
ATOM   1350  N   VAL A 185      -8.644  42.919  45.001  1.00 95.37           N  
ANISOU 1350  N   VAL A 185    13405   9790  13040   2051  -1334  -1466       N  
ATOM   1351  CA  VAL A 185      -8.604  44.378  44.901  1.00101.00           C  
ANISOU 1351  CA  VAL A 185    14269  10096  14012   2148  -1584  -1455       C  
ATOM   1352  C   VAL A 185      -7.329  44.920  45.533  1.00109.37           C  
ANISOU 1352  C   VAL A 185    15555  10985  15015   1971  -1615  -1470       C  
ATOM   1353  O   VAL A 185      -6.567  45.665  44.904  1.00113.42           O  
ANISOU 1353  O   VAL A 185    16233  11272  15591   1823  -1826  -1239       O  
ATOM   1354  CB  VAL A 185      -9.852  45.000  45.553  1.00 99.36           C  
ANISOU 1354  CB  VAL A 185    13950   9741  14060   2483  -1587  -1768       C  
ATOM   1355  CG1 VAL A 185      -9.759  46.521  45.532  1.00102.35           C  
ANISOU 1355  CG1 VAL A 185    14504   9647  14737   2598  -1864  -1786       C  
ATOM   1356  CG2 VAL A 185     -11.115  44.526  44.856  1.00102.93           C  
ANISOU 1356  CG2 VAL A 185    14156  10359  14595   2652  -1587  -1736       C  
ATOM   1357  N   LEU A 186      -7.079  44.550  46.791  1.00 98.92           N  
ANISOU 1357  N   LEU A 186    14242   9782  13563   1963  -1413  -1734       N  
ATOM   1358  CA  LEU A 186      -5.966  45.132  47.533  1.00 95.90           C  
ANISOU 1358  CA  LEU A 186    14065   9230  13143   1819  -1456  -1799       C  
ATOM   1359  C   LEU A 186      -4.623  44.673  46.981  1.00 97.95           C  
ANISOU 1359  C   LEU A 186    14404   9608  13205   1501  -1476  -1510       C  
ATOM   1360  O   LEU A 186      -3.699  45.482  46.839  1.00104.08           O  
ANISOU 1360  O   LEU A 186    15352  10156  14040   1344  -1645  -1390       O  
ATOM   1361  CB  LEU A 186      -6.094  44.779  49.013  1.00 96.23           C  
ANISOU 1361  CB  LEU A 186    14089   9416  13059   1886  -1235  -2150       C  
ATOM   1362  CG  LEU A 186      -7.250  45.479  49.729  1.00 88.94           C  
ANISOU 1362  CG  LEU A 186    13107   8348  12337   2192  -1214  -2500       C  
ATOM   1363  CD1 LEU A 186      -7.426  44.933  51.134  1.00106.89           C  
ANISOU 1363  CD1 LEU A 186    15337  10866  14411   2223   -952  -2826       C  
ATOM   1364  CD2 LEU A 186      -7.029  46.982  49.755  1.00 98.93           C  
ANISOU 1364  CD2 LEU A 186    14561   9148  13880   2270  -1472  -2567       C  
ATOM   1365  N   LYS A 187      -4.495  43.381  46.669  1.00 85.48           N  
ANISOU 1365  N   LYS A 187    12693   8382  11404   1401  -1309  -1406       N  
ATOM   1366  CA  LYS A 187      -3.246  42.880  46.106  1.00 89.07           C  
ANISOU 1366  CA  LYS A 187    13185   8978  11681   1125  -1314  -1161       C  
ATOM   1367  C   LYS A 187      -2.904  43.584  44.800  1.00102.58           C  
ANISOU 1367  C   LYS A 187    14962  10533  13481   1007  -1531   -853       C  
ATOM   1368  O   LYS A 187      -1.729  43.853  44.521  1.00105.25           O  
ANISOU 1368  O   LYS A 187    15396  10839  13754    771  -1606   -683       O  
ATOM   1369  CB  LYS A 187      -3.332  41.368  45.893  1.00 83.80           C  
ANISOU 1369  CB  LYS A 187    12352   8685  10802   1082  -1118  -1124       C  
ATOM   1370  CG  LYS A 187      -3.142  40.553  47.159  1.00 83.94           C  
ANISOU 1370  CG  LYS A 187    12348   8881  10663   1076   -922  -1333       C  
ATOM   1371  CD  LYS A 187      -1.722  40.697  47.668  1.00 93.07           C  
ANISOU 1371  CD  LYS A 187    13630  10012  11720    874   -955  -1303       C  
ATOM   1372  CE  LYS A 187      -1.433  39.743  48.810  1.00 88.65           C  
ANISOU 1372  CE  LYS A 187    13048   9660  10974    842   -787  -1453       C  
ATOM   1373  NZ  LYS A 187      -0.015  39.854  49.252  1.00 89.03           N  
ANISOU 1373  NZ  LYS A 187    13198   9698  10933    645   -845  -1410       N  
ATOM   1374  N   ASN A 188      -3.916  43.896  43.987  1.00104.43           N  
ANISOU 1374  N   ASN A 188    15138  10682  13857   1156  -1641   -768       N  
ATOM   1375  CA  ASN A 188      -3.662  44.638  42.757  1.00105.36           C  
ANISOU 1375  CA  ASN A 188    15340  10640  14051   1037  -1873   -452       C  
ATOM   1376  C   ASN A 188      -3.302  46.092  43.042  1.00114.00           C  
ANISOU 1376  C   ASN A 188    16640  11308  15367   1016  -2099   -438       C  
ATOM   1377  O   ASN A 188      -2.521  46.689  42.294  1.00126.26           O  
ANISOU 1377  O   ASN A 188    18313  12740  16921    792  -2268   -157       O  
ATOM   1378  CB  ASN A 188      -4.872  44.559  41.828  1.00112.11           C  
ANISOU 1378  CB  ASN A 188    16078  11524  14996   1206  -1957   -356       C  
ATOM   1379  CG  ASN A 188      -4.822  43.354  40.911  1.00108.20           C  
ANISOU 1379  CG  ASN A 188    15441  11411  14261   1089  -1840   -200       C  
ATOM   1380  OD1 ASN A 188      -3.755  42.786  40.673  1.00104.54           O  
ANISOU 1380  OD1 ASN A 188    14988  11146  13585    856  -1748    -92       O  
ATOM   1381  ND2 ASN A 188      -5.976  42.959  40.387  1.00111.85           N  
ANISOU 1381  ND2 ASN A 188    15758  11978  14764   1255  -1848   -207       N  
ATOM   1382  N   GLU A 189      -3.855  46.679  44.108  1.00114.17           N  
ANISOU 1382  N   GLU A 189    16706  11099  15574   1234  -2107   -742       N  
ATOM   1383  CA  GLU A 189      -3.459  48.034  44.482  1.00117.82           C  
ANISOU 1383  CA  GLU A 189    17379  11131  16258   1214  -2325   -774       C  
ATOM   1384  C   GLU A 189      -2.014  48.072  44.963  1.00117.65           C  
ANISOU 1384  C   GLU A 189    17478  11131  16091    922  -2295   -742       C  
ATOM   1385  O   GLU A 189      -1.261  48.987  44.610  1.00111.00           O  
ANISOU 1385  O   GLU A 189    16802  10026  15347    728  -2504   -550       O  
ATOM   1386  CB  GLU A 189      -4.386  48.594  45.560  1.00111.32           C  
ANISOU 1386  CB  GLU A 189    16558  10086  15652   1531  -2317  -1166       C  
ATOM   1387  CG  GLU A 189      -5.798  48.889  45.094  1.00135.60           C  
ANISOU 1387  CG  GLU A 189    19519  13042  18961   1840  -2415  -1207       C  
ATOM   1388  CD  GLU A 189      -6.603  49.643  46.135  1.00144.48           C  
ANISOU 1388  CD  GLU A 189    20652  13905  20339   2154  -2432  -1612       C  
ATOM   1389  OE1 GLU A 189      -6.010  50.092  47.140  1.00132.38           O  
ANISOU 1389  OE1 GLU A 189    19260  12230  18810   2110  -2409  -1838       O  
ATOM   1390  OE2 GLU A 189      -7.829  49.788  45.947  1.00142.59           O1-
ANISOU 1390  OE2 GLU A 189    20268  13614  20294   2446  -2471  -1722       O1-
ATOM   1391  N   MET A 190      -1.610  47.088  45.772  1.00114.97           N  
ANISOU 1391  N   MET A 190    17055  11102  15525    878  -2052   -915       N  
ATOM   1392  CA  MET A 190      -0.242  47.054  46.281  1.00117.73           C  
ANISOU 1392  CA  MET A 190    17493  11503  15738    615  -2030   -898       C  
ATOM   1393  C   MET A 190       0.770  46.871  45.154  1.00116.25           C  
ANISOU 1393  C   MET A 190    17292  11449  15427    310  -2086   -528       C  
ATOM   1394  O   MET A 190       1.855  47.464  45.183  1.00130.81           O  
ANISOU 1394  O   MET A 190    19250  13172  17282     66  -2199   -416       O  
ATOM   1395  CB  MET A 190      -0.106  45.942  47.324  1.00109.59           C  
ANISOU 1395  CB  MET A 190    16362  10792  14486    648  -1775  -1132       C  
ATOM   1396  CG  MET A 190       1.323  45.529  47.631  1.00107.76           C  
ANISOU 1396  CG  MET A 190    16150  10726  14067    373  -1732  -1060       C  
ATOM   1397  SD  MET A 190       1.847  44.081  46.693  1.00120.25           S  
ANISOU 1397  SD  MET A 190    17536  12749  15405    225  -1575   -818       S  
ATOM   1398  CE  MET A 190       3.622  44.296  46.731  1.00113.74           C  
ANISOU 1398  CE  MET A 190    16762  11959  14495   -117  -1650   -672       C  
ATOM   1399  N   ALA A 191       0.431  46.062  44.145  1.00 95.40           N  
ANISOU 1399  N   ALA A 191    14506   9076  12665    310  -2006   -346       N  
ATOM   1400  CA  ALA A 191       1.362  45.806  43.048  1.00106.51           C  
ANISOU 1400  CA  ALA A 191    15877  10673  13918     26  -2025    -25       C  
ATOM   1401  C   ALA A 191       1.439  46.982  42.080  1.00109.31           C  
ANISOU 1401  C   ALA A 191    16369  10747  14417   -108  -2287    271       C  
ATOM   1402  O   ALA A 191       2.518  47.291  41.562  1.00111.05           O  
ANISOU 1402  O   ALA A 191    16636  10996  14561   -413  -2354    506       O  
ATOM   1403  CB  ALA A 191       0.962  44.531  42.305  1.00105.06           C  
ANISOU 1403  CB  ALA A 191    15501  10874  13543     71  -1854     38       C  
ATOM   1404  N   ARG A 192       0.308  47.644  41.817  1.00114.07           N  
ANISOU 1404  N   ARG A 192    17029  11081  15232    107  -2444    274       N  
ATOM   1405  CA  ARG A 192       0.321  48.812  40.942  1.00113.89           C  
ANISOU 1405  CA  ARG A 192    17161  10739  15372     -9  -2733    573       C  
ATOM   1406  C   ARG A 192       1.088  49.966  41.572  1.00115.36           C  
ANISOU 1406  C   ARG A 192    17552  10543  15736   -155  -2909    555       C  
ATOM   1407  O   ARG A 192       1.835  50.672  40.884  1.00125.27           O  
ANISOU 1407  O   ARG A 192    18926  11664  17007   -445  -3085    867       O  
ATOM   1408  CB  ARG A 192      -1.111  49.229  40.608  1.00122.40           C  
ANISOU 1408  CB  ARG A 192    18239  11599  16671    296  -2882    554       C  
ATOM   1409  CG  ARG A 192      -1.732  48.394  39.511  1.00115.23           C  
ANISOU 1409  CG  ARG A 192    17171  11014  15597    331  -2821    727       C  
ATOM   1410  CD  ARG A 192      -3.242  48.356  39.608  1.00102.78           C  
ANISOU 1410  CD  ARG A 192    15498   9350  14203    703  -2857    555       C  
ATOM   1411  NE  ARG A 192      -3.798  47.355  38.705  1.00118.58           N  
ANISOU 1411  NE  ARG A 192    17322  11718  16014    728  -2760    665       N  
ATOM   1412  CZ  ARG A 192      -5.060  46.951  38.718  1.00130.35           C  
ANISOU 1412  CZ  ARG A 192    18661  13274  17590   1013  -2727    514       C  
ATOM   1413  NH1 ARG A 192      -5.939  47.456  39.568  1.00133.82           N  
ANISOU 1413  NH1 ARG A 192    19086  13460  18301   1316  -2768    240       N  
ATOM   1414  NH2 ARG A 192      -5.448  46.010  37.862  1.00120.11           N  
ANISOU 1414  NH2 ARG A 192    17213  12322  16100    990  -2647    621       N  
ATOM   1415  N   ALA A 193       0.917  50.171  42.880  1.00113.60           N  
ANISOU 1415  N   ALA A 193    17375  10150  15636     24  -2864    191       N  
ATOM   1416  CA  ALA A 193       1.698  51.185  43.579  1.00120.52           C  
ANISOU 1416  CA  ALA A 193    18444  10683  16664   -122  -3020    125       C  
ATOM   1417  C   ALA A 193       3.183  50.847  43.550  1.00119.51           C  
ANISOU 1417  C   ALA A 193    18295  10797  16318   -498  -2940    270       C  
ATOM   1418  O   ALA A 193       4.028  51.740  43.421  1.00128.31           O  
ANISOU 1418  O   ALA A 193    19556  11674  17524   -768  -3126    440       O  
ATOM   1419  CB  ALA A 193       1.204  51.329  45.017  1.00113.64           C  
ANISOU 1419  CB  ALA A 193    17608   9660  15911    149  -2953   -336       C  
ATOM   1420  N   ASN A 194       3.520  49.563  43.655  1.00113.32           N  
ANISOU 1420  N   ASN A 194    17318  10480  15260   -523  -2673    210       N  
ATOM   1421  CA  ASN A 194       4.901  49.113  43.546  1.00117.39           C  
ANISOU 1421  CA  ASN A 194    17760  11275  15570   -848  -2583    340       C  
ATOM   1422  C   ASN A 194       5.395  49.084  42.105  1.00118.09           C  
ANISOU 1422  C   ASN A 194    17792  11539  15536  -1119  -2622    743       C  
ATOM   1423  O   ASN A 194       6.460  48.510  41.839  1.00119.07           O  
ANISOU 1423  O   ASN A 194    17792  11989  15460  -1365  -2502    849       O  
ATOM   1424  CB  ASN A 194       5.050  47.728  44.181  1.00114.55           C  
ANISOU 1424  CB  ASN A 194    17213  11325  14987   -750  -2306    123       C  
ATOM   1425  CG  ASN A 194       5.721  47.780  45.535  1.00124.49           C  
ANISOU 1425  CG  ASN A 194    18522  12540  16240   -783  -2280   -136       C  
ATOM   1426  OD1 ASN A 194       6.880  48.177  45.655  1.00149.47           O  
ANISOU 1426  OD1 ASN A 194    21723  15678  19392  -1058  -2360    -48       O  
ATOM   1427  ND2 ASN A 194       4.989  47.387  46.568  1.00117.88           N  
ANISOU 1427  ND2 ASN A 194    17680  11709  15400   -517  -2171   -455       N  
ATOM   1428  N   HIS A 195       4.626  49.669  41.182  1.00119.72           N  
ANISOU 1428  N   HIS A 195    18080  11556  15854  -1070  -2788    960       N  
ATOM   1429  CA  HIS A 195       5.017  49.871  39.785  1.00122.79           C  
ANISOU 1429  CA  HIS A 195    18464  12062  16129  -1351  -2872   1374       C  
ATOM   1430  C   HIS A 195       5.073  48.549  39.020  1.00122.65           C  
ANISOU 1430  C   HIS A 195    18218  12580  15805  -1369  -2628   1434       C  
ATOM   1431  O   HIS A 195       5.929  48.344  38.158  1.00117.79           O  
ANISOU 1431  O   HIS A 195    17524  12243  14986  -1670  -2577   1680       O  
ATOM   1432  CB  HIS A 195       6.338  50.635  39.689  1.00121.05           C  
ANISOU 1432  CB  HIS A 195    18334  11748  15913  -1758  -2988   1586       C  
ATOM   1433  CG  HIS A 195       6.313  51.943  40.416  1.00126.05           C  
ANISOU 1433  CG  HIS A 195    19207  11827  16859  -1758  -3248   1519       C  
ATOM   1434  ND1 HIS A 195       7.066  52.177  41.545  1.00141.17           N  
ANISOU 1434  ND1 HIS A 195    21166  13631  18842  -1832  -3242   1291       N  
ATOM   1435  CD2 HIS A 195       5.612  53.078  40.189  1.00124.03           C  
ANISOU 1435  CD2 HIS A 195    19163  11082  16880  -1679  -3537   1633       C  
ATOM   1436  CE1 HIS A 195       6.835  53.403  41.979  1.00150.50           C  
ANISOU 1436  CE1 HIS A 195    22581  14280  20321  -1807  -3506   1250       C  
ATOM   1437  NE2 HIS A 195       5.957  53.972  41.173  1.00140.18           N  
ANISOU 1437  NE2 HIS A 195    21380  12722  19161  -1706  -3692   1455       N  
ATOM   1438  N   TYR A 196       4.145  47.654  39.342  1.00119.07           N  
ANISOU 1438  N   TYR A 196    17651  12270  15321  -1050  -2476   1193       N  
ATOM   1439  CA  TYR A 196       3.879  46.438  38.591  1.00114.84           C  
ANISOU 1439  CA  TYR A 196    16922  12165  14547  -1003  -2285   1220       C  
ATOM   1440  C   TYR A 196       2.489  46.548  37.974  1.00109.56           C  
ANISOU 1440  C   TYR A 196    16273  11392  13964   -772  -2390   1277       C  
ATOM   1441  O   TYR A 196       1.637  47.296  38.459  1.00112.49           O  
ANISOU 1441  O   TYR A 196    16757  11393  14590   -555  -2545   1180       O  
ATOM   1442  CB  TYR A 196       3.963  45.201  39.495  1.00115.65           C  
ANISOU 1442  CB  TYR A 196    16866  12530  14545   -844  -2029    899       C  
ATOM   1443  CG  TYR A 196       5.372  44.776  39.860  1.00113.78           C  
ANISOU 1443  CG  TYR A 196    16545  12517  14171  -1071  -1906    869       C  
ATOM   1444  CD1 TYR A 196       6.106  43.929  39.038  1.00116.76           C  
ANISOU 1444  CD1 TYR A 196    16748  13302  14312  -1245  -1759    981       C  
ATOM   1445  CD2 TYR A 196       5.964  45.215  41.039  1.00119.47           C  
ANISOU 1445  CD2 TYR A 196    17344  13048  15000  -1103  -1942    707       C  
ATOM   1446  CE1 TYR A 196       7.396  43.539  39.377  1.00119.08           C  
ANISOU 1446  CE1 TYR A 196    16933  13806  14508  -1430  -1655    939       C  
ATOM   1447  CE2 TYR A 196       7.248  44.831  41.384  1.00126.71           C  
ANISOU 1447  CE2 TYR A 196    18165  14174  15807  -1304  -1853    682       C  
ATOM   1448  CZ  TYR A 196       7.960  43.995  40.553  1.00122.47           C  
ANISOU 1448  CZ  TYR A 196    17437  14036  15060  -1459  -1710    800       C  
ATOM   1449  OH  TYR A 196       9.237  43.617  40.902  1.00123.45           O  
ANISOU 1449  OH  TYR A 196    17436  14371  15100  -1638  -1630    761       O  
ATOM   1450  N   GLU A 197       2.261  45.802  36.889  1.00110.56           N  
ANISOU 1450  N   GLU A 197    16277  11852  13879   -813  -2312   1420       N  
ATOM   1451  CA  GLU A 197       0.974  45.879  36.199  1.00123.90           C  
ANISOU 1451  CA  GLU A 197    17969  13477  15631   -619  -2432   1501       C  
ATOM   1452  C   GLU A 197      -0.162  45.417  37.104  1.00117.20           C  
ANISOU 1452  C   GLU A 197    17045  12552  14936   -243  -2350   1164       C  
ATOM   1453  O   GLU A 197      -1.070  46.188  37.434  1.00118.89           O  
ANISOU 1453  O   GLU A 197    17342  12424  15408    -26  -2518   1104       O  
ATOM   1454  CB  GLU A 197       1.000  45.046  34.918  1.00124.02           C  
ANISOU 1454  CB  GLU A 197    17857  13913  15353   -747  -2344   1677       C  
ATOM   1455  CG  GLU A 197       2.146  45.351  33.981  1.00130.46           C  
ANISOU 1455  CG  GLU A 197    18706  14906  15955  -1139  -2370   1991       C  
ATOM   1456  CD  GLU A 197       2.207  44.376  32.826  1.00133.25           C  
ANISOU 1456  CD  GLU A 197    18910  15735  15984  -1247  -2233   2083       C  
ATOM   1457  OE1 GLU A 197       1.399  43.423  32.809  1.00115.92           O  
ANISOU 1457  OE1 GLU A 197    16591  13708  13747  -1018  -2122   1890       O  
ATOM   1458  OE2 GLU A 197       3.059  44.562  31.933  1.00139.31           O1-
ANISOU 1458  OE2 GLU A 197    19682  16716  16534  -1571  -2233   2338       O1-
ATOM   1459  N   ASP A 198      -0.134  44.149  37.498  1.00111.47           N  
ANISOU 1459  N   ASP A 198    16152  12144  14056   -166  -2094    943       N  
ATOM   1460  CA  ASP A 198      -1.099  43.590  38.430  1.00106.10           C  
ANISOU 1460  CA  ASP A 198    15386  11448  13479    140  -1977    628       C  
ATOM   1461  C   ASP A 198      -0.364  42.620  39.344  1.00113.50           C  
ANISOU 1461  C   ASP A 198    16239  12602  14284    105  -1737    409       C  
ATOM   1462  O   ASP A 198       0.826  42.350  39.163  1.00116.14           O  
ANISOU 1462  O   ASP A 198    16558  13107  14464   -126  -1669    496       O  
ATOM   1463  CB  ASP A 198      -2.260  42.910  37.691  1.00109.29           C  
ANISOU 1463  CB  ASP A 198    15656  12030  13840    301  -1960    636       C  
ATOM   1464  CG  ASP A 198      -1.788  41.972  36.597  1.00108.60           C  
ANISOU 1464  CG  ASP A 198    15463  12331  13467    114  -1860    786       C  
ATOM   1465  OD1 ASP A 198      -1.341  40.852  36.921  1.00108.65           O  
ANISOU 1465  OD1 ASP A 198    15354  12604  13323     89  -1641    630       O  
ATOM   1466  OD2 ASP A 198      -1.863  42.358  35.411  1.00110.95           O1-
ANISOU 1466  OD2 ASP A 198    15799  12668  13691     -8  -2009   1055       O1-
ATOM   1467  N   TYR A 199      -1.082  42.102  40.345  1.00109.51           N  
ANISOU 1467  N   TYR A 199    15670  12097  13843    334  -1613    128       N  
ATOM   1468  CA  TYR A 199      -0.452  41.220  41.324  1.00102.41           C  
ANISOU 1468  CA  TYR A 199    14713  11368  12829    311  -1416    -68       C  
ATOM   1469  C   TYR A 199       0.195  40.012  40.660  1.00 93.16           C  
ANISOU 1469  C   TYR A 199    13407  10558  11431    173  -1274      6       C  
ATOM   1470  O   TYR A 199       1.206  39.499  41.154  1.00 96.51           O  
ANISOU 1470  O   TYR A 199    13804  11111  11756     60  -1174    -52       O  
ATOM   1471  CB  TYR A 199      -1.477  40.774  42.367  1.00 98.93           C  
ANISOU 1471  CB  TYR A 199    14216  10914  12459    562  -1300   -347       C  
ATOM   1472  CG  TYR A 199      -0.876  40.075  43.565  1.00 93.53           C  
ANISOU 1472  CG  TYR A 199    13519  10342  11675    538  -1139   -539       C  
ATOM   1473  CD1 TYR A 199       0.263  40.571  44.187  1.00 89.93           C  
ANISOU 1473  CD1 TYR A 199    13172   9791  11208    390  -1181   -548       C  
ATOM   1474  CD2 TYR A 199      -1.451  38.922  44.080  1.00 94.48           C  
ANISOU 1474  CD2 TYR A 199    13522  10662  11713    650   -963   -697       C  
ATOM   1475  CE1 TYR A 199       0.814  39.935  45.284  1.00 93.38           C  
ANISOU 1475  CE1 TYR A 199    13601  10337  11545    367  -1062   -707       C  
ATOM   1476  CE2 TYR A 199      -0.910  38.281  45.176  1.00 85.52           C  
ANISOU 1476  CE2 TYR A 199    12391   9623  10478    618   -842   -840       C  
ATOM   1477  CZ  TYR A 199       0.224  38.788  45.772  1.00 85.46           C  
ANISOU 1477  CZ  TYR A 199    12492   9526  10452    483   -896   -844       C  
ATOM   1478  OH  TYR A 199       0.763  38.150  46.866  1.00 92.42           O  
ANISOU 1478  OH  TYR A 199    13381  10509  11225    449   -801   -972       O  
ATOM   1479  N   GLY A 200      -0.360  39.552  39.537  1.00 89.41           N  
ANISOU 1479  N   GLY A 200    12844  10250  10878    184  -1277    120       N  
ATOM   1480  CA  GLY A 200       0.266  38.462  38.807  1.00 89.94           C  
ANISOU 1480  CA  GLY A 200    12786  10653  10733     55  -1153    168       C  
ATOM   1481  C   GLY A 200       1.595  38.857  38.193  1.00 91.09           C  
ANISOU 1481  C   GLY A 200    12960  10886  10765   -214  -1187    356       C  
ATOM   1482  O   GLY A 200       2.564  38.094  38.246  1.00 91.14           O  
ANISOU 1482  O   GLY A 200    12872  11114  10644   -320  -1059    306       O  
ATOM   1483  N   ASP A 201       1.659  40.049  37.591  1.00 96.51           N  
ANISOU 1483  N   ASP A 201    13765  11401  11504   -332  -1366    580       N  
ATOM   1484  CA  ASP A 201       2.930  40.559  37.084  1.00 97.31           C  
ANISOU 1484  CA  ASP A 201    13896  11571  11506   -624  -1403    777       C  
ATOM   1485  C   ASP A 201       3.961  40.659  38.200  1.00103.86           C  
ANISOU 1485  C   ASP A 201    14742  12333  12387   -696  -1351    654       C  
ATOM   1486  O   ASP A 201       5.144  40.364  37.995  1.00108.01           O  
ANISOU 1486  O   ASP A 201    15182  13072  12785   -897  -1272    700       O  
ATOM   1487  CB  ASP A 201       2.725  41.922  36.426  1.00103.21           C  
ANISOU 1487  CB  ASP A 201    14804  12072  12340   -739  -1638   1051       C  
ATOM   1488  CG  ASP A 201       4.009  42.494  35.860  1.00106.03           C  
ANISOU 1488  CG  ASP A 201    15192  12511  12585  -1084  -1679   1288       C  
ATOM   1489  OD1 ASP A 201       4.676  41.792  35.071  1.00113.04           O  
ANISOU 1489  OD1 ASP A 201    15943  13772  13235  -1248  -1545   1350       O  
ATOM   1490  OD2 ASP A 201       4.357  43.641  36.213  1.00102.67           O1-
ANISOU 1490  OD2 ASP A 201    14919  11780  12310  -1196  -1840   1398       O1-
ATOM   1491  N   TYR A 202       3.523  41.081  39.389  1.00113.19           N  
ANISOU 1491  N   TYR A 202    16023  13234  13751   -533  -1398    485       N  
ATOM   1492  CA  TYR A 202       4.390  41.103  40.562  1.00104.07           C  
ANISOU 1492  CA  TYR A 202    14890  12022  12632   -580  -1357    337       C  
ATOM   1493  C   TYR A 202       4.988  39.726  40.832  1.00101.80           C  
ANISOU 1493  C   TYR A 202    14430  12053  12194   -573  -1164    201       C  
ATOM   1494  O   TYR A 202       6.207  39.582  40.983  1.00109.78           O  
ANISOU 1494  O   TYR A 202    15379  13191  13139   -744  -1131    218       O  
ATOM   1495  CB  TYR A 202       3.587  41.608  41.763  1.00107.46           C  
ANISOU 1495  CB  TYR A 202    15440  12149  13242   -367  -1411    133       C  
ATOM   1496  CG  TYR A 202       4.309  41.586  43.089  1.00122.20           C  
ANISOU 1496  CG  TYR A 202    17344  13964  15124   -389  -1376    -52       C  
ATOM   1497  CD1 TYR A 202       5.179  42.607  43.446  1.00127.97           C  
ANISOU 1497  CD1 TYR A 202    18194  14496  15933   -569  -1510      0       C  
ATOM   1498  CD2 TYR A 202       4.093  40.559  43.999  1.00112.70           C  
ANISOU 1498  CD2 TYR A 202    16067  12902  13853   -244  -1225   -271       C  
ATOM   1499  CE1 TYR A 202       5.831  42.594  44.663  1.00128.25           C  
ANISOU 1499  CE1 TYR A 202    18265  14494  15969   -596  -1497   -175       C  
ATOM   1500  CE2 TYR A 202       4.738  40.539  45.218  1.00115.75           C  
ANISOU 1500  CE2 TYR A 202    16498  13252  14228   -272  -1212   -425       C  
ATOM   1501  CZ  TYR A 202       5.605  41.559  45.545  1.00132.81           C  
ANISOU 1501  CZ  TYR A 202    18770  15232  16459   -444  -1350   -385       C  
ATOM   1502  OH  TYR A 202       6.251  41.545  46.759  1.00143.04           O  
ANISOU 1502  OH  TYR A 202    20111  16505  17731   -480  -1355   -544       O  
ATOM   1503  N   TRP A 203       4.138  38.695  40.877  1.00 83.31           N  
ANISOU 1503  N   TRP A 203    12003   9837   9812   -376  -1050     68       N  
ATOM   1504  CA  TRP A 203       4.623  37.337  41.109  1.00 81.04           C  
ANISOU 1504  CA  TRP A 203    11567   9813   9413   -352   -892    -57       C  
ATOM   1505  C   TRP A 203       5.578  36.876  40.018  1.00 81.38           C  
ANISOU 1505  C   TRP A 203    11471  10142   9306   -530   -834     59       C  
ATOM   1506  O   TRP A 203       6.522  36.130  40.297  1.00 81.12           O  
ANISOU 1506  O   TRP A 203    11322  10283   9215   -577   -749    -20       O  
ATOM   1507  CB  TRP A 203       3.455  36.359  41.198  1.00 80.20           C  
ANISOU 1507  CB  TRP A 203    11403   9770   9301   -138   -799   -189       C  
ATOM   1508  CG  TRP A 203       2.796  36.311  42.526  1.00 76.51           C  
ANISOU 1508  CG  TRP A 203    11003   9144   8923     25   -776   -369       C  
ATOM   1509  CD1 TRP A 203       3.203  36.930  43.670  1.00 76.02           C  
ANISOU 1509  CD1 TRP A 203    11047   8914   8922     11   -821   -451       C  
ATOM   1510  CD2 TRP A 203       1.626  35.564  42.865  1.00 74.86           C  
ANISOU 1510  CD2 TRP A 203    10752   8962   8731    209   -693   -498       C  
ATOM   1511  NE1 TRP A 203       2.342  36.631  44.699  1.00 76.02           N  
ANISOU 1511  NE1 TRP A 203    11079   8850   8956    178   -761   -628       N  
ATOM   1512  CE2 TRP A 203       1.366  35.792  44.229  1.00 74.17           C  
ANISOU 1512  CE2 TRP A 203    10747   8735   8699    296   -677   -652       C  
ATOM   1513  CE3 TRP A 203       0.766  34.732  42.143  1.00 74.41           C  
ANISOU 1513  CE3 TRP A 203    10592   9043   8639    293   -633   -503       C  
ATOM   1514  CZ2 TRP A 203       0.283  35.215  44.888  1.00 70.87           C  
ANISOU 1514  CZ2 TRP A 203    10300   8331   8294    452   -585   -795       C  
ATOM   1515  CZ3 TRP A 203      -0.308  34.163  42.796  1.00 70.05           C  
ANISOU 1515  CZ3 TRP A 203    10010   8480   8124    447   -558   -642       C  
ATOM   1516  CH2 TRP A 203      -0.542  34.407  44.155  1.00 69.93           C  
ANISOU 1516  CH2 TRP A 203    10069   8344   8158    521   -526   -780       C  
ATOM   1517  N   ARG A 204       5.343  37.287  38.771  1.00 88.40           N  
ANISOU 1517  N   ARG A 204    12361  11099  10126   -626   -880    240       N  
ATOM   1518  CA  ARG A 204       6.232  36.889  37.689  1.00 90.36           C  
ANISOU 1518  CA  ARG A 204    12471  11662  10200   -810   -806    338       C  
ATOM   1519  C   ARG A 204       7.599  37.553  37.785  1.00 90.30           C  
ANISOU 1519  C   ARG A 204    12447  11685  10178  -1056   -835    442       C  
ATOM   1520  O   ARG A 204       8.521  37.132  37.079  1.00 98.41           O  
ANISOU 1520  O   ARG A 204    13317  13013  11062  -1210   -741    477       O  
ATOM   1521  CB  ARG A 204       5.580  37.198  36.337  1.00102.45           C  
ANISOU 1521  CB  ARG A 204    14025  13276  11626   -870   -859    520       C  
ATOM   1522  CG  ARG A 204       4.346  36.351  36.060  1.00 88.38           C  
ANISOU 1522  CG  ARG A 204    12206  11546   9829   -656   -818    408       C  
ATOM   1523  CD  ARG A 204       3.826  36.529  34.641  1.00 88.79           C  
ANISOU 1523  CD  ARG A 204    12259  11742   9736   -736   -874    584       C  
ATOM   1524  NE  ARG A 204       3.211  37.832  34.411  1.00 91.02           N  
ANISOU 1524  NE  ARG A 204    12706  11764  10114   -768  -1075    800       N  
ATOM   1525  CZ  ARG A 204       1.942  38.119  34.671  1.00 97.70           C  
ANISOU 1525  CZ  ARG A 204    13627  12382  11112   -566  -1181    775       C  
ATOM   1526  NH1 ARG A 204       1.130  37.228  35.217  1.00 89.85           N  
ANISOU 1526  NH1 ARG A 204    12561  11397  10183   -341  -1094    553       N  
ATOM   1527  NH2 ARG A 204       1.476  39.329  34.375  1.00 95.52           N  
ANISOU 1527  NH2 ARG A 204    13494  11860  10938   -595  -1386    980       N  
ATOM   1528  N   GLY A 205       7.757  38.555  38.655  1.00 93.09           N  
ANISOU 1528  N   GLY A 205    12944  11747  10678  -1097   -959    470       N  
ATOM   1529  CA  GLY A 205       9.030  39.233  38.824  1.00103.11           C  
ANISOU 1529  CA  GLY A 205    14201  13021  11955  -1347  -1008    566       C  
ATOM   1530  C   GLY A 205      10.162  38.346  39.304  1.00 99.45           C  
ANISOU 1530  C   GLY A 205    13547  12796  11444  -1377   -890    420       C  
ATOM   1531  O   GLY A 205      11.330  38.685  39.087  1.00109.02           O  
ANISOU 1531  O   GLY A 205    14665  14142  12617  -1614   -891    512       O  
ATOM   1532  N   ASP A 206       9.849  37.215  39.945  1.00 92.14           N  
ANISOU 1532  N   ASP A 206    12554  11925  10529  -1149   -798    206       N  
ATOM   1533  CA  ASP A 206      10.894  36.315  40.424  1.00 91.21           C  
ANISOU 1533  CA  ASP A 206    12256  12008  10392  -1147   -717     70       C  
ATOM   1534  C   ASP A 206      11.756  35.766  39.293  1.00 92.64           C  
ANISOU 1534  C   ASP A 206    12205  12558  10435  -1279   -598    108       C  
ATOM   1535  O   ASP A 206      12.875  35.306  39.546  1.00101.35           O  
ANISOU 1535  O   ASP A 206    13129  13839  11540  -1335   -554     31       O  
ATOM   1536  CB  ASP A 206      10.276  35.156  41.207  1.00 88.42           C  
ANISOU 1536  CB  ASP A 206    11893  11630  10074   -882   -658   -134       C  
ATOM   1537  CG  ASP A 206      11.319  34.299  41.898  1.00100.72           C  
ANISOU 1537  CG  ASP A 206    13297  13322  11649   -860   -626   -262       C  
ATOM   1538  OD1 ASP A 206      11.753  34.666  43.011  1.00117.00           O  
ANISOU 1538  OD1 ASP A 206    15428  15244  13784   -884   -716   -300       O  
ATOM   1539  OD2 ASP A 206      11.714  33.263  41.322  1.00 91.65           O1-
ANISOU 1539  OD2 ASP A 206    11959  12417  10447   -813   -525   -335       O1-
ATOM   1540  N   TYR A 207      11.267  35.801  38.058  1.00 82.47           N  
ANISOU 1540  N   TYR A 207    10907  11405   9024  -1328   -550    214       N  
ATOM   1541  CA  TYR A 207      12.027  35.319  36.916  1.00 82.83           C  
ANISOU 1541  CA  TYR A 207    10735  11835   8901  -1463   -420    233       C  
ATOM   1542  C   TYR A 207      12.639  36.448  36.102  1.00 85.18           C  
ANISOU 1542  C   TYR A 207    11038  12227   9099  -1789   -457    486       C  
ATOM   1543  O   TYR A 207      13.323  36.179  35.111  1.00 88.57           O  
ANISOU 1543  O   TYR A 207    11280  13014   9356  -1946   -336    519       O  
ATOM   1544  CB  TYR A 207      11.135  34.453  36.022  1.00 79.82           C  
ANISOU 1544  CB  TYR A 207    10322  11604   8403  -1318   -330    162       C  
ATOM   1545  CG  TYR A 207      10.561  33.251  36.738  1.00 77.96           C  
ANISOU 1545  CG  TYR A 207    10067  11291   8262  -1028   -290    -74       C  
ATOM   1546  CD1 TYR A 207       9.403  33.360  37.495  1.00 76.52           C  
ANISOU 1546  CD1 TYR A 207    10070  10809   8196   -855   -372    -97       C  
ATOM   1547  CD2 TYR A 207      11.189  32.015  36.674  1.00 77.70           C  
ANISOU 1547  CD2 TYR A 207     9827  11484   8212   -933   -175   -273       C  
ATOM   1548  CE1 TYR A 207       8.877  32.271  38.156  1.00 74.05           C  
ANISOU 1548  CE1 TYR A 207     9744  10436   7957   -630   -334   -284       C  
ATOM   1549  CE2 TYR A 207      10.670  30.918  37.334  1.00 75.23           C  
ANISOU 1549  CE2 TYR A 207     9517  11070   7998   -690   -162   -460       C  
ATOM   1550  CZ  TYR A 207       9.515  31.053  38.073  1.00 73.18           C  
ANISOU 1550  CZ  TYR A 207     9450  10524   7830   -557   -239   -450       C  
ATOM   1551  OH  TYR A 207       8.994  29.965  38.732  1.00 70.90           O  
ANISOU 1551  OH  TYR A 207     9166  10147   7626   -352   -224   -609       O  
ATOM   1552  N   GLU A 208      12.421  37.698  36.501  1.00 85.84           N  
ANISOU 1552  N   GLU A 208    11330  11999   9286  -1903   -621    660       N  
ATOM   1553  CA  GLU A 208      12.919  38.831  35.738  1.00 87.82           C  
ANISOU 1553  CA  GLU A 208    11621  12286   9458  -2235   -688    939       C  
ATOM   1554  C   GLU A 208      14.432  38.962  35.882  1.00 89.56           C  
ANISOU 1554  C   GLU A 208    11645  12720   9664  -2480   -637    951       C  
ATOM   1555  O   GLU A 208      15.009  38.668  36.932  1.00 90.75           O  
ANISOU 1555  O   GLU A 208    11725  12811   9945  -2400   -646    785       O  
ATOM   1556  CB  GLU A 208      12.231  40.119  36.191  1.00 88.20           C  
ANISOU 1556  CB  GLU A 208    11961  11884   9669  -2264   -907   1101       C  
ATOM   1557  CG  GLU A 208      12.583  41.346  35.368  1.00 92.67           C  
ANISOU 1557  CG  GLU A 208    12618  12417  10176  -2611  -1020   1433       C  
ATOM   1558  CD  GLU A 208      11.709  42.539  35.698  1.00108.65           C  
ANISOU 1558  CD  GLU A 208    14942  13957  12385  -2583  -1257   1577       C  
ATOM   1559  OE1 GLU A 208      11.027  42.511  36.745  1.00111.63           O  
ANISOU 1559  OE1 GLU A 208    15434  14033  12946  -2317  -1321   1388       O  
ATOM   1560  OE2 GLU A 208      11.700  43.504  34.905  1.00118.94           O1-
ANISOU 1560  OE2 GLU A 208    16362  15180  13647  -2828  -1384   1878       O1-
ATOM   1561  N   VAL A 209      15.074  39.396  34.798  1.00 81.21           N  
ANISOU 1561  N   VAL A 209    10489  11936   8432  -2792   -583   1155       N  
ATOM   1562  CA  VAL A 209      16.516  39.621  34.752  1.00 82.83           C  
ANISOU 1562  CA  VAL A 209    10476  12394   8602  -3078   -522   1200       C  
ATOM   1563  C   VAL A 209      16.770  40.862  33.909  1.00 85.30           C  
ANISOU 1563  C   VAL A 209    10884  12715   8809  -3477   -603   1558       C  
ATOM   1564  O   VAL A 209      16.246  40.975  32.795  1.00110.25           O  
ANISOU 1564  O   VAL A 209    14102  16012  11777  -3564   -573   1726       O  
ATOM   1565  CB  VAL A 209      17.273  38.414  34.160  1.00 82.76           C  
ANISOU 1565  CB  VAL A 209    10116  12895   8433  -3041   -282   1005       C  
ATOM   1566  CG1 VAL A 209      18.742  38.752  33.988  1.00 84.71           C  
ANISOU 1566  CG1 VAL A 209    10108  13442   8635  -3366   -212   1073       C  
ATOM   1567  CG2 VAL A 209      17.100  37.170  35.024  1.00 81.58           C  
ANISOU 1567  CG2 VAL A 209     9877  12705   8413  -2661   -231    672       C  
ATOM   1568  N   ASN A 210      17.574  41.790  34.427  1.00100.69           N  
ANISOU 1568  N   ASN A 210    12857  14519  10880  -3736   -720   1685       N  
ATOM   1569  CA  ASN A 210      17.896  43.015  33.711  1.00102.54           C  
ANISOU 1569  CA  ASN A 210    13194  14725  11042  -4154   -821   2049       C  
ATOM   1570  C   ASN A 210      19.391  43.299  33.789  1.00103.84           C  
ANISOU 1570  C   ASN A 210    13112  15147  11195  -4502   -764   2101       C  
ATOM   1571  O   ASN A 210      20.079  42.856  34.713  1.00115.65           O  
ANISOU 1571  O   ASN A 210    14440  16674  12826  -4400   -737   1871       O  
ATOM   1572  CB  ASN A 210      17.116  44.216  34.263  1.00114.45           C  
ANISOU 1572  CB  ASN A 210    15076  15642  12769  -4155  -1106   2217       C  
ATOM   1573  CG  ASN A 210      15.630  44.123  33.982  1.00122.30           C  
ANISOU 1573  CG  ASN A 210    16297  16407  13766  -3870  -1177   2227       C  
ATOM   1574  OD1 ASN A 210      15.192  44.237  32.836  1.00117.24           O  
ANISOU 1574  OD1 ASN A 210    15699  15912  12934  -3976  -1164   2437       O  
ATOM   1575  ND2 ASN A 210      14.845  43.915  35.031  1.00116.34           N  
ANISOU 1575  ND2 ASN A 210    15678  15311  13216  -3516  -1256   1999       N  
ATOM   1576  N   GLY A 211      19.886  44.036  32.794  1.00120.11           N  
ANISOU 1576  N   GLY A 211    15144  17408  13083  -4927   -751   2419       N  
ATOM   1577  CA  GLY A 211      21.247  44.533  32.785  1.00123.51           C  
ANISOU 1577  CA  GLY A 211    15363  18061  13505  -5334   -721   2536       C  
ATOM   1578  C   GLY A 211      22.333  43.522  32.493  1.00125.23           C  
ANISOU 1578  C   GLY A 211    15125  18880  13576  -5360   -441   2321       C  
ATOM   1579  O   GLY A 211      23.507  43.814  32.750  1.00128.66           O  
ANISOU 1579  O   GLY A 211    15336  19488  14062  -5634   -420   2343       O  
ATOM   1580  N   VAL A 212      21.994  42.346  31.970  1.00123.74           N  
ANISOU 1580  N   VAL A 212    14780  19012  13223  -5081   -233   2098       N  
ATOM   1581  CA  VAL A 212      22.971  41.306  31.652  1.00127.08           C  
ANISOU 1581  CA  VAL A 212    14759  20001  13524  -5053     35   1847       C  
ATOM   1582  C   VAL A 212      22.738  40.916  30.197  1.00131.70           C  
ANISOU 1582  C   VAL A 212    15251  21038  13752  -5149    246   1910       C  
ATOM   1583  O   VAL A 212      21.803  40.168  29.891  1.00126.11           O  
ANISOU 1583  O   VAL A 212    14635  20315  12965  -4834    296   1763       O  
ATOM   1584  CB  VAL A 212      22.857  40.087  32.577  1.00121.34           C  
ANISOU 1584  CB  VAL A 212    13915  19209  12979  -4570     72   1437       C  
ATOM   1585  CG1 VAL A 212      24.084  39.194  32.439  1.00127.13           C  
ANISOU 1585  CG1 VAL A 212    14170  20462  13672  -4565    293   1185       C  
ATOM   1586  CG2 VAL A 212      22.670  40.523  34.025  1.00120.44           C  
ANISOU 1586  CG2 VAL A 212    14017  18567  13179  -4431   -176   1399       C  
ATOM   1587  N   ASP A 213      23.587  41.417  29.298  1.00145.75           N  
ANISOU 1587  N   ASP A 213    16843  23235  15301  -5599    372   2126       N  
ATOM   1588  CA  ASP A 213      23.403  41.192  27.869  1.00154.39           C  
ANISOU 1588  CA  ASP A 213    17869  24789  16005  -5760    566   2226       C  
ATOM   1589  C   ASP A 213      23.418  39.704  27.541  1.00141.95           C  
ANISOU 1589  C   ASP A 213    16008  23612  14315  -5404    821   1799       C  
ATOM   1590  O   ASP A 213      24.353  38.983  27.901  1.00140.16           O  
ANISOU 1590  O   ASP A 213    15415  23661  14179  -5296    973   1500       O  
ATOM   1591  CB  ASP A 213      24.493  41.914  27.077  1.00171.63           C  
ANISOU 1591  CB  ASP A 213    19840  27416  17956  -6329    688   2500       C  
ATOM   1592  CG  ASP A 213      24.194  43.388  26.881  1.00175.42           C  
ANISOU 1592  CG  ASP A 213    20674  27549  18430  -6737    441   3008       C  
ATOM   1593  OD1 ASP A 213      24.271  44.150  27.869  1.00181.04           O  
ANISOU 1593  OD1 ASP A 213    21561  27770  19458  -6778    198   3111       O  
ATOM   1594  OD2 ASP A 213      23.883  43.785  25.739  1.00160.76           O1-
ANISOU 1594  OD2 ASP A 213    18928  25904  16249  -7019    476   3304       O1-
ATOM   1595  N   GLY A 214      22.373  39.248  26.850  1.00131.74           N  
ANISOU 1595  N   GLY A 214    14883  22335  12838  -5218    850   1767       N  
ATOM   1596  CA  GLY A 214      22.250  37.862  26.461  1.00137.75           C  
ANISOU 1596  CA  GLY A 214    15424  23428  13487  -4886   1066   1368       C  
ATOM   1597  C   GLY A 214      21.634  36.953  27.502  1.00132.42           C  
ANISOU 1597  C   GLY A 214    14820  22370  13122  -4363    975   1041       C  
ATOM   1598  O   GLY A 214      21.328  35.796  27.185  1.00133.83           O  
ANISOU 1598  O   GLY A 214    14882  22733  13234  -4063   1112    723       O  
ATOM   1599  N   TYR A 215      21.439  37.435  28.731  1.00115.73           N  
ANISOU 1599  N   TYR A 215    12902  19732  11338  -4257    745   1105       N  
ATOM   1600  CA  TYR A 215      20.877  36.616  29.797  1.00112.04           C  
ANISOU 1600  CA  TYR A 215    12511  18909  11151  -3796    654    823       C  
ATOM   1601  C   TYR A 215      19.679  37.268  30.477  1.00113.86           C  
ANISOU 1601  C   TYR A 215    13166  18543  11554  -3674    395    996       C  
ATOM   1602  O   TYR A 215      19.245  36.784  31.528  1.00117.97           O  
ANISOU 1602  O   TYR A 215    13774  18732  12316  -3345    298    808       O  
ATOM   1603  CB  TYR A 215      21.954  36.282  30.836  1.00114.47           C  
ANISOU 1603  CB  TYR A 215    12563  19221  11710  -3712    655    620       C  
ATOM   1604  CG  TYR A 215      22.999  35.319  30.324  1.00115.27           C  
ANISOU 1604  CG  TYR A 215    12210  19873  11715  -3680    909    334       C  
ATOM   1605  CD1 TYR A 215      22.828  33.948  30.455  1.00110.42           C  
ANISOU 1605  CD1 TYR A 215    11454  19325  11177  -3274    998    -41       C  
ATOM   1606  CD2 TYR A 215      24.148  35.778  29.693  1.00130.93           C  
ANISOU 1606  CD2 TYR A 215    13899  22309  13538  -4057   1059    432       C  
ATOM   1607  CE1 TYR A 215      23.775  33.060  29.985  1.00110.98           C  
ANISOU 1607  CE1 TYR A 215    11101  19877  11188  -3211   1220   -336       C  
ATOM   1608  CE2 TYR A 215      25.101  34.897  29.217  1.00134.99           C  
ANISOU 1608  CE2 TYR A 215    13968  23350  13973  -4008   1304    137       C  
ATOM   1609  CZ  TYR A 215      24.909  33.539  29.366  1.00128.52           C  
ANISOU 1609  CZ  TYR A 215    13015  22567  13251  -3568   1380   -259       C  
ATOM   1610  OH  TYR A 215      25.855  32.659  28.894  1.00135.26           O  
ANISOU 1610  OH  TYR A 215    13416  23922  14054  -3489   1613   -584       O  
ATOM   1611  N   ASP A 216      19.128  38.338  29.907  1.00105.26           N  
ANISOU 1611  N   ASP A 216    12333  17314  10345  -3926    276   1346       N  
ATOM   1612  CA  ASP A 216      17.943  38.960  30.474  1.00101.38           C  
ANISOU 1612  CA  ASP A 216    12224  16269  10028  -3786     32   1486       C  
ATOM   1613  C   ASP A 216      16.741  38.023  30.373  1.00 99.15           C  
ANISOU 1613  C   ASP A 216    12038  15903   9733  -3403     51   1286       C  
ATOM   1614  O   ASP A 216      16.771  36.985  29.705  1.00 98.65           O  
ANISOU 1614  O   ASP A 216    11784  16201   9498  -3287    238   1079       O  
ATOM   1615  CB  ASP A 216      17.631  40.282  29.772  1.00101.96           C  
ANISOU 1615  CB  ASP A 216    12537  16219   9984  -4135   -115   1913       C  
ATOM   1616  CG  ASP A 216      18.671  41.348  30.043  1.00108.07           C  
ANISOU 1616  CG  ASP A 216    13282  16950  10831  -4522   -193   2141       C  
ATOM   1617  OD1 ASP A 216      19.096  41.481  31.208  1.00125.16           O  
ANISOU 1617  OD1 ASP A 216    15433  18860  13260  -4442   -279   2022       O  
ATOM   1618  OD2 ASP A 216      19.055  42.063  29.093  1.00114.08           O1-
ANISOU 1618  OD2 ASP A 216    14040  17930  11375  -4924   -177   2451       O1-
ATOM   1619  N   TYR A 217      15.665  38.408  31.056  1.00 92.38           N  
ANISOU 1619  N   TYR A 217    11473  14558   9068  -3210   -146   1337       N  
ATOM   1620  CA  TYR A 217      14.410  37.669  31.009  1.00 91.40           C  
ANISOU 1620  CA  TYR A 217    11462  14311   8955  -2877   -158   1188       C  
ATOM   1621  C   TYR A 217      13.293  38.623  31.397  1.00 91.62           C  
ANISOU 1621  C   TYR A 217    11823  13851   9138  -2818   -398   1384       C  
ATOM   1622  O   TYR A 217      13.394  39.313  32.415  1.00 97.11           O  
ANISOU 1622  O   TYR A 217    12643  14190  10064  -2813   -538   1420       O  
ATOM   1623  CB  TYR A 217      14.438  36.458  31.950  1.00 90.09           C  
ANISOU 1623  CB  TYR A 217    11168  14104   8959  -2529    -80    823       C  
ATOM   1624  CG  TYR A 217      13.420  35.386  31.621  1.00 88.12           C  
ANISOU 1624  CG  TYR A 217    10931  13894   8656  -2239    -20    628       C  
ATOM   1625  CD1 TYR A 217      12.128  35.446  32.126  1.00 86.51           C  
ANISOU 1625  CD1 TYR A 217    10958  13322   8592  -2015   -155    628       C  
ATOM   1626  CD2 TYR A 217      13.757  34.307  30.814  1.00 88.02           C  
ANISOU 1626  CD2 TYR A 217    10688  14292   8463  -2192    172    425       C  
ATOM   1627  CE1 TYR A 217      11.196  34.466  31.829  1.00 87.94           C  
ANISOU 1627  CE1 TYR A 217    11138  13543   8733  -1776   -107    457       C  
ATOM   1628  CE2 TYR A 217      12.833  33.321  30.512  1.00100.96           C  
ANISOU 1628  CE2 TYR A 217    12345  15949  10065  -1943    211    238       C  
ATOM   1629  CZ  TYR A 217      11.554  33.406  31.022  1.00 96.56           C  
ANISOU 1629  CZ  TYR A 217    12018  15020   9649  -1747     67    267       C  
ATOM   1630  OH  TYR A 217      10.629  32.430  30.727  1.00 86.08           O  
ANISOU 1630  OH  TYR A 217    10700  13714   8294  -1525     98     89       O  
ATOM   1631  N   SER A 218      12.245  38.671  30.584  1.00112.73           N  
ANISOU 1631  N   SER A 218    14630  16514  11689  -2771   -452   1496       N  
ATOM   1632  CA  SER A 218      11.110  39.538  30.857  1.00107.95           C  
ANISOU 1632  CA  SER A 218    14313  15460  11241  -2684   -686   1667       C  
ATOM   1633  C   SER A 218      10.119  38.843  31.780  1.00101.24           C  
ANISOU 1633  C   SER A 218    13519  14353  10595  -2283   -705   1401       C  
ATOM   1634  O   SER A 218       9.999  37.615  31.783  1.00105.64           O  
ANISOU 1634  O   SER A 218    13927  15113  11100  -2086   -554   1142       O  
ATOM   1635  CB  SER A 218      10.412  39.941  29.556  1.00113.26           C  
ANISOU 1635  CB  SER A 218    15097  16239  11697  -2818   -766   1931       C  
ATOM   1636  OG  SER A 218       9.053  40.272  29.787  1.00106.19           O  
ANISOU 1636  OG  SER A 218    14415  14969  10964  -2591   -956   1974       O  
ATOM   1637  N   ARG A 219       9.412  39.647  32.578  1.00 97.70           N  
ANISOU 1637  N   ARG A 219    13286  13451  10383  -2172   -894   1460       N  
ATOM   1638  CA  ARG A 219       8.332  39.103  33.396  1.00102.52           C  
ANISOU 1638  CA  ARG A 219    13957  13829  11166  -1816   -915   1237       C  
ATOM   1639  C   ARG A 219       7.277  38.429  32.527  1.00109.50           C  
ANISOU 1639  C   ARG A 219    14823  14862  11921  -1673   -887   1210       C  
ATOM   1640  O   ARG A 219       6.785  37.346  32.863  1.00109.86           O  
ANISOU 1640  O   ARG A 219    14783  14966  11993  -1433   -785    962       O  
ATOM   1641  CB  ARG A 219       7.697  40.209  34.238  1.00107.39           C  
ANISOU 1641  CB  ARG A 219    14803  13962  12037  -1736  -1123   1310       C  
ATOM   1642  CG  ARG A 219       8.580  40.746  35.347  1.00 98.51           C  
ANISOU 1642  CG  ARG A 219    13712  12647  11071  -1817  -1160   1258       C  
ATOM   1643  CD  ARG A 219       7.769  41.582  36.316  1.00 98.87           C  
ANISOU 1643  CD  ARG A 219    13970  12223  11373  -1650  -1336   1218       C  
ATOM   1644  NE  ARG A 219       7.182  42.745  35.661  1.00108.60           N  
ANISOU 1644  NE  ARG A 219    15387  13209  12668  -1741  -1544   1486       N  
ATOM   1645  CZ  ARG A 219       7.704  43.964  35.684  1.00118.28           C  
ANISOU 1645  CZ  ARG A 219    16754  14197  13991  -1971  -1714   1692       C  
ATOM   1646  NH1 ARG A 219       8.833  44.220  36.326  1.00111.66           N  
ANISOU 1646  NH1 ARG A 219    15887  13348  13192  -2148  -1696   1656       N  
ATOM   1647  NH2 ARG A 219       7.077  44.950  35.049  1.00139.14           N  
ANISOU 1647  NH2 ARG A 219    19572  16592  16704  -2029  -1927   1946       N  
ATOM   1648  N   GLY A 220       6.924  39.051  31.401  1.00 97.95           N  
ANISOU 1648  N   GLY A 220    13442  13460  10314  -1834   -990   1475       N  
ATOM   1649  CA  GLY A 220       5.938  38.460  30.515  1.00102.37           C  
ANISOU 1649  CA  GLY A 220    13985  14179  10732  -1723   -988   1462       C  
ATOM   1650  C   GLY A 220       6.420  37.203  29.818  1.00 97.07           C  
ANISOU 1650  C   GLY A 220    13100  13969   9812  -1747   -767   1281       C  
ATOM   1651  O   GLY A 220       5.623  36.299  29.552  1.00111.05           O  
ANISOU 1651  O   GLY A 220    14820  15836  11539  -1559   -722   1114       O  
ATOM   1652  N   GLN A 221       7.723  37.121  29.521  1.00 93.63           N  
ANISOU 1652  N   GLN A 221    12526  13825   9224  -1974   -628   1291       N  
ATOM   1653  CA  GLN A 221       8.269  35.967  28.809  1.00 98.35           C  
ANISOU 1653  CA  GLN A 221    12902  14879   9588  -1995   -411   1092       C  
ATOM   1654  C   GLN A 221       7.981  34.649  29.520  1.00 96.80           C  
ANISOU 1654  C   GLN A 221    12595  14657   9528  -1680   -302    728       C  
ATOM   1655  O   GLN A 221       7.990  33.595  28.874  1.00103.75           O  
ANISOU 1655  O   GLN A 221    13334  15838  10250  -1620   -168    532       O  
ATOM   1656  CB  GLN A 221       9.780  36.143  28.614  1.00 94.43           C  
ANISOU 1656  CB  GLN A 221    12242  14670   8968  -2264   -275   1129       C  
ATOM   1657  CG  GLN A 221      10.442  35.082  27.736  1.00 94.33           C  
ANISOU 1657  CG  GLN A 221    11979  15172   8691  -2312    -42    924       C  
ATOM   1658  CD  GLN A 221      10.304  35.377  26.257  1.00134.72           C  
ANISOU 1658  CD  GLN A 221    17112  20630  13445  -2561    -28   1125       C  
ATOM   1659  OE1 GLN A 221      10.100  36.523  25.858  1.00146.62           O  
ANISOU 1659  OE1 GLN A 221    18792  22032  14884  -2787   -184   1482       O  
ATOM   1660  NE2 GLN A 221      10.414  34.340  25.433  1.00134.28           N  
ANISOU 1660  NE2 GLN A 221    16885  20983  13153  -2525    148    896       N  
ATOM   1661  N   LEU A 222       7.717  34.681  30.829  1.00 95.30           N  
ANISOU 1661  N   LEU A 222    12476  14114   9620  -1488   -364    631       N  
ATOM   1662  CA  LEU A 222       7.348  33.459  31.535  1.00 97.11           C  
ANISOU 1662  CA  LEU A 222    12630  14291   9978  -1209   -285    329       C  
ATOM   1663  C   LEU A 222       6.063  32.862  30.968  1.00 93.47           C  
ANISOU 1663  C   LEU A 222    12205  13845   9463  -1057   -313    264       C  
ATOM   1664  O   LEU A 222       6.024  31.678  30.617  1.00 98.11           O  
ANISOU 1664  O   LEU A 222    12665  14636   9975   -958   -200     42       O  
ATOM   1665  CB  LEU A 222       7.209  33.735  33.033  1.00 83.11           C  
ANISOU 1665  CB  LEU A 222    10953  12147   8479  -1064   -359    278       C  
ATOM   1666  CG  LEU A 222       6.888  32.489  33.862  1.00 81.05           C  
ANISOU 1666  CG  LEU A 222    10626  11824   8344   -809   -287      1       C  
ATOM   1667  CD1 LEU A 222       8.083  31.547  33.903  1.00 80.29           C  
ANISOU 1667  CD1 LEU A 222    10325  11972   8211   -817   -146   -182       C  
ATOM   1668  CD2 LEU A 222       6.437  32.857  35.269  1.00 79.92           C  
ANISOU 1668  CD2 LEU A 222    10616  11323   8427   -673   -374    -23       C  
ATOM   1669  N   ILE A 223       5.005  33.676  30.853  1.00 82.33           N  
ANISOU 1669  N   ILE A 223    10961  12215   8104  -1035   -478    448       N  
ATOM   1670  CA  ILE A 223       3.737  33.201  30.292  1.00 89.59           C  
ANISOU 1670  CA  ILE A 223    11904  13154   8983   -904   -531    406       C  
ATOM   1671  C   ILE A 223       3.962  32.541  28.936  1.00 93.11           C  
ANISOU 1671  C   ILE A 223    12238  14009   9129  -1021   -441    363       C  
ATOM   1672  O   ILE A 223       3.480  31.434  28.675  1.00 87.85           O  
ANISOU 1672  O   ILE A 223    11490  13465   8424   -890   -376    146       O  
ATOM   1673  CB  ILE A 223       2.725  34.356  30.186  1.00 86.81           C  
ANISOU 1673  CB  ILE A 223    11726  12541   8716   -898   -746    652       C  
ATOM   1674  CG1 ILE A 223       2.610  35.109  31.512  1.00 83.39           C  
ANISOU 1674  CG1 ILE A 223    11401  11716   8566   -793   -825    667       C  
ATOM   1675  CG2 ILE A 223       1.372  33.826  29.758  1.00 88.20           C  
ANISOU 1675  CG2 ILE A 223    11898  12724   8890   -738   -811    586       C  
ATOM   1676  CD1 ILE A 223       1.481  36.117  31.530  1.00 84.04           C  
ANISOU 1676  CD1 ILE A 223    11633  11505   8793   -713  -1037    837       C  
ATOM   1677  N   GLU A 224       4.686  33.228  28.051  1.00 97.94           N  
ANISOU 1677  N   GLU A 224    12852  14844   9518  -1285   -439    570       N  
ATOM   1678  CA  GLU A 224       5.117  32.635  26.788  1.00 94.42           C  
ANISOU 1678  CA  GLU A 224    12284  14849   8744  -1429   -317    508       C  
ATOM   1679  C   GLU A 224       5.779  31.277  26.998  1.00105.06           C  
ANISOU 1679  C   GLU A 224    13430  16393  10094  -1308   -111    142       C  
ATOM   1680  O   GLU A 224       5.295  30.251  26.506  1.00109.00           O  
ANISOU 1680  O   GLU A 224    13862  17045  10510  -1195    -58    -76       O  
ATOM   1681  CB  GLU A 224       6.076  33.578  26.072  1.00 96.51           C  
ANISOU 1681  CB  GLU A 224    12553  15333   8784  -1760   -304    774       C  
ATOM   1682  CG  GLU A 224       6.687  32.974  24.826  1.00123.43           C  
ANISOU 1682  CG  GLU A 224    15808  19265  11824  -1931   -136    682       C  
ATOM   1683  CD  GLU A 224       7.644  33.923  24.122  1.00144.74           C  
ANISOU 1683  CD  GLU A 224    18500  22216  14276  -2297   -107    967       C  
ATOM   1684  OE1 GLU A 224       7.590  35.138  24.426  1.00137.08           O  
ANISOU 1684  OE1 GLU A 224    17695  20973  13416  -2427   -276   1290       O  
ATOM   1685  OE2 GLU A 224       8.401  33.467  23.229  1.00158.87           O1-
ANISOU 1685  OE2 GLU A 224    20125  24480  15759  -2462     78    868       O1-
ATOM   1686  N   ASP A 225       6.902  31.252  27.720  1.00101.71           N  
ANISOU 1686  N   ASP A 225    12907  15960   9780  -1328     -9     67       N  
ATOM   1687  CA  ASP A 225       7.688  30.027  27.808  1.00 91.88           C  
ANISOU 1687  CA  ASP A 225    11451  14926   8535  -1226    173   -263       C  
ATOM   1688  C   ASP A 225       6.984  28.958  28.633  1.00 88.16           C  
ANISOU 1688  C   ASP A 225    10984  14212   8300   -929    156   -513       C  
ATOM   1689  O   ASP A 225       7.197  27.763  28.403  1.00 86.36           O  
ANISOU 1689  O   ASP A 225    10617  14143   8053   -814    264   -800       O  
ATOM   1690  CB  ASP A 225       9.068  30.344  28.378  1.00 98.32           C  
ANISOU 1690  CB  ASP A 225    12145  15791   9421  -1330    256   -256       C  
ATOM   1691  CG  ASP A 225       9.935  31.114  27.399  1.00112.49           C  
ANISOU 1691  CG  ASP A 225    13868  17934  10939  -1654    327    -65       C  
ATOM   1692  OD1 ASP A 225       9.750  30.951  26.172  1.00108.34           O  
ANISOU 1692  OD1 ASP A 225    13310  17735  10118  -1770    386    -57       O  
ATOM   1693  OD2 ASP A 225      10.766  31.922  27.859  1.00115.77           O1-
ANISOU 1693  OD2 ASP A 225    14270  18297  11422  -1812    315     92       O1-
ATOM   1694  N   VAL A 226       6.149  29.359  29.594  1.00 86.20           N  
ANISOU 1694  N   VAL A 226    10892  13582   8277   -810     23   -415       N  
ATOM   1695  CA  VAL A 226       5.256  28.400  30.238  1.00 75.78           C  
ANISOU 1695  CA  VAL A 226     9594  12059   7140   -568     -1   -607       C  
ATOM   1696  C   VAL A 226       4.333  27.769  29.205  1.00 85.50           C  
ANISOU 1696  C   VAL A 226    10819  13447   8222   -538    -14   -695       C  
ATOM   1697  O   VAL A 226       4.246  26.541  29.090  1.00 82.10           O  
ANISOU 1697  O   VAL A 226    10296  13088   7811   -417     54   -957       O  
ATOM   1698  CB  VAL A 226       4.453  29.072  31.366  1.00 75.45           C  
ANISOU 1698  CB  VAL A 226     9712  11630   7326   -472   -129   -477       C  
ATOM   1699  CG1 VAL A 226       3.323  28.170  31.800  1.00 73.78           C  
ANISOU 1699  CG1 VAL A 226     9523  11262   7249   -272   -154   -632       C  
ATOM   1700  CG2 VAL A 226       5.353  29.356  32.553  1.00 96.55           C  
ANISOU 1700  CG2 VAL A 226    12382  14143  10161   -464   -111   -477       C  
ATOM   1701  N   GLU A 227       3.641  28.608  28.427  1.00107.08           N  
ANISOU 1701  N   GLU A 227    13653  16224  10809   -652   -121   -473       N  
ATOM   1702  CA  GLU A 227       2.692  28.112  27.433  1.00 93.57           C  
ANISOU 1702  CA  GLU A 227    11944  14663   8944   -638   -166   -531       C  
ATOM   1703  C   GLU A 227       3.395  27.348  26.322  1.00 90.37           C  
ANISOU 1703  C   GLU A 227    11401  14669   8267   -732    -28   -720       C  
ATOM   1704  O   GLU A 227       2.994  26.229  25.978  1.00 85.74           O  
ANISOU 1704  O   GLU A 227    10750  14170   7658   -627      7   -976       O  
ATOM   1705  CB  GLU A 227       1.888  29.274  26.847  1.00 97.97           C  
ANISOU 1705  CB  GLU A 227    12640  15179   9406   -747   -340   -219       C  
ATOM   1706  CG  GLU A 227       0.929  29.921  27.823  1.00 95.19           C  
ANISOU 1706  CG  GLU A 227    12408  14430   9331   -610   -487    -91       C  
ATOM   1707  CD  GLU A 227       0.155  31.091  27.228  1.00131.78           C  
ANISOU 1707  CD  GLU A 227    17169  18995  13906   -693   -688    213       C  
ATOM   1708  OE1 GLU A 227       0.471  31.528  26.096  1.00110.27           O  
ANISOU 1708  OE1 GLU A 227    14466  16522  10909   -896   -723    382       O  
ATOM   1709  OE2 GLU A 227      -0.780  31.570  27.905  1.00137.69           O1-
ANISOU 1709  OE2 GLU A 227    17993  19440  14884   -552   -815    283       O1-
ATOM   1710  N   HIS A 228       4.442  27.943  25.738  1.00 98.74           N  
ANISOU 1710  N   HIS A 228    12410  15993   9114   -939     53   -607       N  
ATOM   1711  CA  HIS A 228       5.128  27.306  24.617  1.00106.20           C  
ANISOU 1711  CA  HIS A 228    13207  17382   9762  -1045    205   -795       C  
ATOM   1712  C   HIS A 228       5.688  25.941  24.990  1.00106.74           C  
ANISOU 1712  C   HIS A 228    13108  17487   9961   -858    349  -1193       C  
ATOM   1713  O   HIS A 228       5.844  25.079  24.117  1.00108.04           O  
ANISOU 1713  O   HIS A 228    13161  17949   9940   -853    448  -1453       O  
ATOM   1714  CB  HIS A 228       6.250  28.201  24.091  1.00 98.65           C  
ANISOU 1714  CB  HIS A 228    12199  16706   8576  -1315    290   -600       C  
ATOM   1715  CG  HIS A 228       6.878  27.694  22.828  1.00124.62           C  
ANISOU 1715  CG  HIS A 228    15337  20512  11502  -1459    456   -770       C  
ATOM   1716  ND1 HIS A 228       7.854  26.721  22.825  1.00129.24           N  
ANISOU 1716  ND1 HIS A 228    15699  21317  12088  -1377    658  -1123       N  
ATOM   1717  CD2 HIS A 228       6.659  28.010  21.530  1.00130.94           C  
ANISOU 1717  CD2 HIS A 228    16172  21663  11916  -1673    449   -649       C  
ATOM   1718  CE1 HIS A 228       8.215  26.466  21.580  1.00133.35           C  
ANISOU 1718  CE1 HIS A 228    16114  22316  12238  -1530    788  -1239       C  
ATOM   1719  NE2 HIS A 228       7.505  27.235  20.775  1.00135.78           N  
ANISOU 1719  NE2 HIS A 228    16582  22723  12286  -1725    667   -948       N  
ATOM   1720  N   THR A 229       6.005  25.723  26.265  1.00111.10           N  
ANISOU 1720  N   THR A 229    13643  17740  10830   -703    350  -1253       N  
ATOM   1721  CA  THR A 229       6.474  24.412  26.697  1.00113.44           C  
ANISOU 1721  CA  THR A 229    13799  18009  11292   -508    442  -1604       C  
ATOM   1722  C   THR A 229       5.333  23.487  27.093  1.00104.68           C  
ANISOU 1722  C   THR A 229    12766  16635  10370   -311    349  -1753       C  
ATOM   1723  O   THR A 229       5.468  22.264  26.965  1.00106.01           O  
ANISOU 1723  O   THR A 229    12838  16842  10601   -178    404  -2067       O  
ATOM   1724  CB  THR A 229       7.457  24.548  27.862  1.00101.72           C  
ANISOU 1724  CB  THR A 229    12250  16357  10042   -450    474  -1594       C  
ATOM   1725  OG1 THR A 229       6.881  25.363  28.892  1.00 88.12           O  
ANISOU 1725  OG1 THR A 229    10701  14277   8505   -435    340  -1342       O  
ATOM   1726  CG2 THR A 229       8.766  25.171  27.386  1.00102.94           C  
ANISOU 1726  CG2 THR A 229    12259  16836  10019   -644    598  -1531       C  
ATOM   1727  N   PHE A 230       4.212  24.036  27.568  1.00 94.88           N  
ANISOU 1727  N   PHE A 230    11690  15127   9235   -292    207  -1543       N  
ATOM   1728  CA  PHE A 230       3.051  23.197  27.849  1.00 97.41           C  
ANISOU 1728  CA  PHE A 230    12066  15239   9707   -143    125  -1667       C  
ATOM   1729  C   PHE A 230       2.494  22.586  26.570  1.00103.17           C  
ANISOU 1729  C   PHE A 230    12765  16217  10219   -181    120  -1826       C  
ATOM   1730  O   PHE A 230       2.016  21.446  26.577  1.00110.08           O  
ANISOU 1730  O   PHE A 230    13613  17017  11196    -64    106  -2069       O  
ATOM   1731  CB  PHE A 230       1.972  24.003  28.570  1.00 95.48           C  
ANISOU 1731  CB  PHE A 230    11970  14704   9604   -122    -11  -1417       C  
ATOM   1732  CG  PHE A 230       0.732  23.210  28.879  1.00 85.56           C  
ANISOU 1732  CG  PHE A 230    10749  13259   8501      3    -88  -1522       C  
ATOM   1733  CD1 PHE A 230       0.751  22.213  29.842  1.00 84.33           C  
ANISOU 1733  CD1 PHE A 230    10571  12889   8581    142    -64  -1691       C  
ATOM   1734  CD2 PHE A 230      -0.449  23.455  28.200  1.00 89.94           C  
ANISOU 1734  CD2 PHE A 230    11353  13856   8965    -34   -196  -1438       C  
ATOM   1735  CE1 PHE A 230      -0.388  21.480  30.123  1.00 84.86           C  
ANISOU 1735  CE1 PHE A 230    10666  12792   8784    221   -132  -1770       C  
ATOM   1736  CE2 PHE A 230      -1.590  22.727  28.477  1.00 87.11           C  
ANISOU 1736  CE2 PHE A 230    11002  13344   8753     60   -265  -1535       C  
ATOM   1737  CZ  PHE A 230      -1.560  21.738  29.439  1.00 84.06           C  
ANISOU 1737  CZ  PHE A 230    10594  12750   8595    177   -224  -1700       C  
ATOM   1738  N   GLU A 231       2.543  23.334  25.462  1.00 99.83           N  
ANISOU 1738  N   GLU A 231    12354  16090   9487   -362    118  -1684       N  
ATOM   1739  CA  GLU A 231       2.076  22.807  24.183  1.00101.84           C  
ANISOU 1739  CA  GLU A 231    12584  16630   9482   -423    110  -1834       C  
ATOM   1740  C   GLU A 231       2.800  21.517  23.816  1.00106.63           C  
ANISOU 1740  C   GLU A 231    13042  17415  10058   -340    250  -2243       C  
ATOM   1741  O   GLU A 231       2.198  20.597  23.250  1.00108.04           O  
ANISOU 1741  O   GLU A 231    13208  17650  10190   -288    219  -2484       O  
ATOM   1742  CB  GLU A 231       2.255  23.855  23.082  1.00108.70           C  
ANISOU 1742  CB  GLU A 231    13488  17827   9987   -660     99  -1594       C  
ATOM   1743  CG  GLU A 231       1.199  24.957  23.062  1.00114.58           C  
ANISOU 1743  CG  GLU A 231    14391  18415  10729   -728   -100  -1231       C  
ATOM   1744  CD  GLU A 231      -0.133  24.481  22.506  1.00131.89           C  
ANISOU 1744  CD  GLU A 231    16627  20607  12879   -683   -243  -1295       C  
ATOM   1745  OE1 GLU A 231      -0.123  23.647  21.575  1.00117.25           O  
ANISOU 1745  OE1 GLU A 231    14708  19033  10807   -717   -195  -1542       O  
ATOM   1746  OE2 GLU A 231      -1.187  24.940  22.995  1.00140.64           O1-
ANISOU 1746  OE2 GLU A 231    17822  21444  14171   -614   -405  -1115       O1-
ATOM   1747  N   GLU A 232       4.093  21.424  24.137  1.00108.99           N  
ANISOU 1747  N   GLU A 232    13217  17793  10400   -320    393  -2343       N  
ATOM   1748  CA  GLU A 232       4.830  20.197  23.860  1.00108.53           C  
ANISOU 1748  CA  GLU A 232    12998  17876  10364   -203    518  -2756       C  
ATOM   1749  C   GLU A 232       4.513  19.076  24.840  1.00104.48           C  
ANISOU 1749  C   GLU A 232    12494  16977  10226     30    454  -2959       C  
ATOM   1750  O   GLU A 232       4.872  17.925  24.567  1.00102.51           O  
ANISOU 1750  O   GLU A 232    12139  16776  10035    152    508  -3323       O  
ATOM   1751  CB  GLU A 232       6.342  20.449  23.862  1.00101.19           C  
ANISOU 1751  CB  GLU A 232    11896  17179   9372   -248    689  -2808       C  
ATOM   1752  CG  GLU A 232       6.791  21.744  23.206  1.00115.95           C  
ANISOU 1752  CG  GLU A 232    13767  19365  10923   -514    747  -2515       C  
ATOM   1753  CD  GLU A 232       8.304  21.881  23.182  1.00131.30           C  
ANISOU 1753  CD  GLU A 232    15502  21575  12812   -571    931  -2602       C  
ATOM   1754  OE1 GLU A 232       8.965  21.024  22.559  1.00135.93           O  
ANISOU 1754  OE1 GLU A 232    15899  22450  13298   -512   1079  -2965       O  
ATOM   1755  OE2 GLU A 232       8.834  22.840  23.782  1.00129.92           O1-
ANISOU 1755  OE2 GLU A 232    15339  21322  12702   -674    925  -2325       O1-
ATOM   1756  N   ILE A 233       3.860  19.370  25.966  1.00 98.36           N  
ANISOU 1756  N   ILE A 233    11843  15824   9706     88    337  -2740       N  
ATOM   1757  CA  ILE A 233       3.486  18.299  26.885  1.00 95.39           C  
ANISOU 1757  CA  ILE A 233    11491  15093   9659    272    267  -2897       C  
ATOM   1758  C   ILE A 233       2.193  17.633  26.434  1.00107.59           C  
ANISOU 1758  C   ILE A 233    13110  16565  11203    284    163  -3000       C  
ATOM   1759  O   ILE A 233       2.031  16.417  26.596  1.00106.62           O  
ANISOU 1759  O   ILE A 233    12968  16282  11261    404    130  -3260       O  
ATOM   1760  CB  ILE A 233       3.352  18.825  28.324  1.00 79.73           C  
ANISOU 1760  CB  ILE A 233     9601  12769   7925    317    202  -2640       C  
ATOM   1761  CG1 ILE A 233       4.683  19.358  28.827  1.00 99.55           C  
ANISOU 1761  CG1 ILE A 233    12027  15335  10463    308    287  -2572       C  
ATOM   1762  CG2 ILE A 233       2.892  17.717  29.261  1.00 77.86           C  
ANISOU 1762  CG2 ILE A 233     9404  12183   7995    470    124  -2764       C  
ATOM   1763  CD1 ILE A 233       4.610  19.980  30.203  1.00112.41           C  
ANISOU 1763  CD1 ILE A 233    13756  16663  12293    332    221  -2326       C  
ATOM   1764  N   LYS A 234       1.273  18.410  25.851  1.00 94.52           N  
ANISOU 1764  N   LYS A 234    11537  15018   9357    155     92  -2796       N  
ATOM   1765  CA  LYS A 234      -0.072  17.941  25.498  1.00 80.16           C  
ANISOU 1765  CA  LYS A 234     9782  13125   7548    148    -34  -2842       C  
ATOM   1766  C   LYS A 234      -0.125  16.543  24.891  1.00 91.52           C  
ANISOU 1766  C   LYS A 234    11163  14609   9000    213    -33  -3236       C  
ATOM   1767  O   LYS A 234      -0.968  15.751  25.332  1.00103.27           O  
ANISOU 1767  O   LYS A 234    12693  15837  10706    276   -132  -3318       O  
ATOM   1768  CB  LYS A 234      -0.737  18.957  24.555  1.00 97.33           C  
ANISOU 1768  CB  LYS A 234    12010  15538   9431    -11   -103  -2620       C  
ATOM   1769  CG  LYS A 234      -1.177  20.246  25.236  1.00 97.50           C  
ANISOU 1769  CG  LYS A 234    12122  15400   9525    -48   -176  -2234       C  
ATOM   1770  CD  LYS A 234      -1.963  21.142  24.289  1.00107.43           C  
ANISOU 1770  CD  LYS A 234    13436  16845  10536   -183   -292  -2017       C  
ATOM   1771  CE  LYS A 234      -2.455  22.391  25.001  1.00104.07           C  
ANISOU 1771  CE  LYS A 234    13098  16210  10233   -187   -386  -1664       C  
ATOM   1772  NZ  LYS A 234      -3.248  23.271  24.100  1.00 94.74           N  
ANISOU 1772  NZ  LYS A 234    11974  15173   8849   -299   -537  -1434       N  
ATOM   1773  N   PRO A 235       0.714  16.166  23.915  1.00 95.59           N  
ANISOU 1773  N   PRO A 235    11580  15439   9300    198     74  -3501       N  
ATOM   1774  CA  PRO A 235       0.643  14.780  23.412  1.00 98.91           C  
ANISOU 1774  CA  PRO A 235    11953  15854   9775    285     62  -3918       C  
ATOM   1775  C   PRO A 235       0.869  13.733  24.490  1.00100.23           C  
ANISOU 1775  C   PRO A 235    12113  15622  10348    466     29  -4076       C  
ATOM   1776  O   PRO A 235       0.159  12.720  24.521  1.00100.26           O  
ANISOU 1776  O   PRO A 235    12157  15417  10519    516    -76  -4262       O  
ATOM   1777  CB  PRO A 235       1.738  14.740  22.337  1.00 90.36           C  
ANISOU 1777  CB  PRO A 235    10740  15201   8391    250    223  -4166       C  
ATOM   1778  CG  PRO A 235       1.929  16.156  21.935  1.00 98.35           C  
ANISOU 1778  CG  PRO A 235    11770  16500   9099     68    274  -3826       C  
ATOM   1779  CD  PRO A 235       1.722  16.953  23.179  1.00 93.99           C  
ANISOU 1779  CD  PRO A 235    11300  15624   8787     87    212  -3452       C  
ATOM   1780  N   LEU A 236       1.834  13.954  25.386  1.00 91.70           N  
ANISOU 1780  N   LEU A 236    10987  14423   9432    552     99  -3989       N  
ATOM   1781  CA  LEU A 236       2.083  12.984  26.448  1.00 98.31           C  
ANISOU 1781  CA  LEU A 236    11830  14876  10649    718     42  -4100       C  
ATOM   1782  C   LEU A 236       0.966  12.999  27.487  1.00 96.55           C  
ANISOU 1782  C   LEU A 236    11747  14292  10646    697    -90  -3845       C  
ATOM   1783  O   LEU A 236       0.571  11.944  27.997  1.00 98.98           O  
ANISOU 1783  O   LEU A 236    12099  14293  11215    772   -189  -3966       O  
ATOM   1784  CB  LEU A 236       3.436  13.260  27.102  1.00103.88           C  
ANISOU 1784  CB  LEU A 236    12436  15582  11450    808    135  -4066       C  
ATOM   1785  CG  LEU A 236       3.782  12.435  28.343  1.00 84.31           C  
ANISOU 1785  CG  LEU A 236     9975  12701   9360    973     52  -4101       C  
ATOM   1786  CD1 LEU A 236       3.739  10.944  28.031  1.00 91.06           C  
ANISOU 1786  CD1 LEU A 236    10803  13390  10404   1109    -21  -4485       C  
ATOM   1787  CD2 LEU A 236       5.141  12.840  28.893  1.00 88.46           C  
ANISOU 1787  CD2 LEU A 236    10383  13284   9944   1045    133  -4054       C  
ATOM   1788  N   TYR A 237       0.440  14.183  27.812  1.00 88.71           N  
ANISOU 1788  N   TYR A 237    10820  13331   9554    591    -96  -3497       N  
ATOM   1789  CA  TYR A 237      -0.671  14.254  28.757  1.00 84.21           C  
ANISOU 1789  CA  TYR A 237    10357  12470   9167    568   -198  -3276       C  
ATOM   1790  C   TYR A 237      -1.947  13.684  28.153  1.00 95.83           C  
ANISOU 1790  C   TYR A 237    11860  13927  10623    504   -300  -3372       C  
ATOM   1791  O   TYR A 237      -2.703  12.981  28.836  1.00 91.21           O  
ANISOU 1791  O   TYR A 237    11327  13063  10268    514   -388  -3366       O  
ATOM   1792  CB  TYR A 237      -0.895  15.697  29.206  1.00 71.59           C  
ANISOU 1792  CB  TYR A 237     8807  10916   7477    492   -178  -2921       C  
ATOM   1793  CG  TYR A 237      -2.056  15.855  30.161  1.00 70.86           C  
ANISOU 1793  CG  TYR A 237     8799  10572   7552    474   -259  -2717       C  
ATOM   1794  CD1 TYR A 237      -2.006  15.312  31.437  1.00 80.78           C  
ANISOU 1794  CD1 TYR A 237    10099  11529   9063    539   -278  -2680       C  
ATOM   1795  CD2 TYR A 237      -3.203  16.543  29.787  1.00 72.25           C  
ANISOU 1795  CD2 TYR A 237     8999  10826   7626    390   -318  -2562       C  
ATOM   1796  CE1 TYR A 237      -3.063  15.451  32.315  1.00 87.76           C  
ANISOU 1796  CE1 TYR A 237    11045  12227  10072    505   -326  -2506       C  
ATOM   1797  CE2 TYR A 237      -4.266  16.688  30.658  1.00 75.62           C  
ANISOU 1797  CE2 TYR A 237     9468  11055   8210    382   -373  -2404       C  
ATOM   1798  CZ  TYR A 237      -4.189  16.140  31.920  1.00 83.69           C  
ANISOU 1798  CZ  TYR A 237    10528  11810   9461    432   -362  -2382       C  
ATOM   1799  OH  TYR A 237      -5.242  16.279  32.793  1.00 83.79           O  
ANISOU 1799  OH  TYR A 237    10567  11666   9602    407   -392  -2234       O  
ATOM   1800  N   GLU A 238      -2.200  13.976  26.874  1.00103.04           N  
ANISOU 1800  N   GLU A 238    12742  15151  11258    418   -298  -3451       N  
ATOM   1801  CA  GLU A 238      -3.416  13.502  26.219  1.00 99.51           C  
ANISOU 1801  CA  GLU A 238    12314  14724  10770    343   -414  -3541       C  
ATOM   1802  C   GLU A 238      -3.508  11.982  26.253  1.00106.98           C  
ANISOU 1802  C   GLU A 238    13260  15457  11931    406   -477  -3863       C  
ATOM   1803  O   GLU A 238      -4.596  11.421  26.433  1.00119.36           O  
ANISOU 1803  O   GLU A 238    14864  16847  13642    355   -594  -3868       O  
ATOM   1804  CB  GLU A 238      -3.455  14.007  24.777  1.00107.27           C  
ANISOU 1804  CB  GLU A 238    13267  16111  11382    241   -405  -3599       C  
ATOM   1805  CG  GLU A 238      -4.303  15.248  24.565  1.00108.03           C  
ANISOU 1805  CG  GLU A 238    13398  16331  11318    132   -473  -3266       C  
ATOM   1806  CD  GLU A 238      -4.289  15.715  23.123  1.00124.45           C  
ANISOU 1806  CD  GLU A 238    15463  18816  13007     12   -485  -3297       C  
ATOM   1807  OE1 GLU A 238      -4.760  14.960  22.245  1.00127.63           O  
ANISOU 1807  OE1 GLU A 238    15850  19344  13298    -32   -555  -3542       O  
ATOM   1808  OE2 GLU A 238      -3.801  16.835  22.865  1.00119.77           O1-
ANISOU 1808  OE2 GLU A 238    14880  18417  12209    -52   -434  -3073       O1-
ATOM   1809  N   HIS A 239      -2.375  11.297  26.083  1.00 88.39           N  
ANISOU 1809  N   HIS A 239    10855  13110   9618    517   -408  -4138       N  
ATOM   1810  CA  HIS A 239      -2.380   9.838  26.118  1.00 99.14           C  
ANISOU 1810  CA  HIS A 239    12224  14225  11218    598   -488  -4460       C  
ATOM   1811  C   HIS A 239      -2.526   9.325  27.545  1.00 94.91           C  
ANISOU 1811  C   HIS A 239    11758  13253  11050    654   -559  -4313       C  
ATOM   1812  O   HIS A 239      -3.325   8.418  27.810  1.00 97.76           O  
ANISOU 1812  O   HIS A 239    12177  13349  11620    619   -685  -4377       O  
ATOM   1813  CB  HIS A 239      -1.107   9.295  25.471  1.00 99.30           C  
ANISOU 1813  CB  HIS A 239    12150  14396  11183    725   -396  -4824       C  
ATOM   1814  CG  HIS A 239      -1.143   9.306  23.974  1.00 96.82           C  
ANISOU 1814  CG  HIS A 239    11782  14478  10529    657   -354  -5084       C  
ATOM   1815  ND1 HIS A 239      -0.669  10.361  23.224  1.00122.07           N  
ANISOU 1815  ND1 HIS A 239    14919  18105  13358    577   -224  -4991       N  
ATOM   1816  CD2 HIS A 239      -1.603   8.391  23.088  1.00 90.07           C  
ANISOU 1816  CD2 HIS A 239    10931  13660   9630    639   -431  -5432       C  
ATOM   1817  CE1 HIS A 239      -0.831  10.094  21.940  1.00 93.04           C  
ANISOU 1817  CE1 HIS A 239    11213  14738   9402    510   -216  -5262       C  
ATOM   1818  NE2 HIS A 239      -1.397   8.906  21.831  1.00 90.33           N  
ANISOU 1818  NE2 HIS A 239    10906  14165   9248    553   -341  -5548       N  
ATOM   1819  N   LEU A 240      -1.751   9.887  28.478  1.00 95.96           N  
ANISOU 1819  N   LEU A 240    11888  13315  11257    722   -487  -4108       N  
ATOM   1820  CA  LEU A 240      -1.935   9.577  29.894  1.00103.78           C  
ANISOU 1820  CA  LEU A 240    12959  13936  12538    745   -553  -3909       C  
ATOM   1821  C   LEU A 240      -3.384   9.790  30.310  1.00 99.66           C  
ANISOU 1821  C   LEU A 240    12505  13314  12048    602   -623  -3679       C  
ATOM   1822  O   LEU A 240      -3.934   9.018  31.103  1.00105.02           O  
ANISOU 1822  O   LEU A 240    13250  13686  12967    571   -715  -3630       O  
ATOM   1823  CB  LEU A 240      -0.991  10.439  30.740  1.00105.78           C  
ANISOU 1823  CB  LEU A 240    13199  14209  12786    806   -463  -3689       C  
ATOM   1824  CG  LEU A 240      -0.733  10.127  32.223  1.00 79.88           C  
ANISOU 1824  CG  LEU A 240     9991  10592   9770    857   -518  -3514       C  
ATOM   1825  CD1 LEU A 240      -1.844  10.660  33.124  1.00 77.93           C  
ANISOU 1825  CD1 LEU A 240     9835  10232   9544    734   -540  -3196       C  
ATOM   1826  CD2 LEU A 240      -0.532   8.635  32.449  1.00 77.23           C  
ANISOU 1826  CD2 LEU A 240     9684   9940   9720    947   -643  -3732       C  
ATOM   1827  N   HIS A 241      -4.025  10.826  29.765  1.00 97.04           N  
ANISOU 1827  N   HIS A 241    12149  13242  11480    508   -586  -3534       N  
ATOM   1828  CA  HIS A 241      -5.408  11.121  30.122  1.00100.20           C  
ANISOU 1828  CA  HIS A 241    12574  13584  11914    390   -647  -3328       C  
ATOM   1829  C   HIS A 241      -6.358  10.064  29.568  1.00 89.04           C  
ANISOU 1829  C   HIS A 241    11158  12088  10584    308   -769  -3521       C  
ATOM   1830  O   HIS A 241      -7.241   9.576  30.282  1.00 83.46           O  
ANISOU 1830  O   HIS A 241    10479  11160  10070    229   -839  -3426       O  
ATOM   1831  CB  HIS A 241      -5.789  12.513  29.615  1.00 99.32           C  
ANISOU 1831  CB  HIS A 241    12428  13758  11551    336   -605  -3135       C  
ATOM   1832  CG  HIS A 241      -7.182  12.926  29.975  1.00 91.56           C  
ANISOU 1832  CG  HIS A 241    11438  12738  10614    246   -664  -2934       C  
ATOM   1833  ND1 HIS A 241      -8.293  12.475  29.295  1.00 83.34           N  
ANISOU 1833  ND1 HIS A 241    10355  11749   9562    153   -770  -3025       N  
ATOM   1834  CD2 HIS A 241      -7.643  13.749  30.945  1.00 91.06           C  
ANISOU 1834  CD2 HIS A 241    11384  12602  10612    240   -630  -2668       C  
ATOM   1835  CE1 HIS A 241      -9.378  13.002  29.833  1.00 86.29           C  
ANISOU 1835  CE1 HIS A 241    10695  12092  10000     97   -797  -2816       C  
ATOM   1836  NE2 HIS A 241      -9.011  13.780  30.836  1.00 80.97           N  
ANISOU 1836  NE2 HIS A 241    10052  11343   9368    155   -706  -2608       N  
ATOM   1837  N   ALA A 242      -6.194   9.700  28.292  1.00 96.69           N  
ANISOU 1837  N   ALA A 242    12091  13249  11400    308   -795  -3799       N  
ATOM   1838  CA  ALA A 242      -7.062   8.698  27.685  1.00105.34           C  
ANISOU 1838  CA  ALA A 242    13186  14275  12563    222   -927  -4016       C  
ATOM   1839  C   ALA A 242      -6.809   7.300  28.233  1.00107.13           C  
ANISOU 1839  C   ALA A 242    13471  14128  13105    265  -1006  -4201       C  
ATOM   1840  O   ALA A 242      -7.698   6.446  28.150  1.00104.65           O  
ANISOU 1840  O   ALA A 242    13180  13647  12938    161  -1135  -4295       O  
ATOM   1841  CB  ALA A 242      -6.890   8.696  26.166  1.00105.23           C  
ANISOU 1841  CB  ALA A 242    13127  14587  12267    210   -933  -4288       C  
ATOM   1842  N   TYR A 243      -5.617   7.046  28.777  1.00 99.23           N  
ANISOU 1842  N   TYR A 243    12494  12986  12225    411   -951  -4251       N  
ATOM   1843  CA  TYR A 243      -5.351   5.764  29.420  1.00 90.19           C  
ANISOU 1843  CA  TYR A 243    11418  11440  11413    464  -1056  -4377       C  
ATOM   1844  C   TYR A 243      -5.950   5.714  30.819  1.00 83.70           C  
ANISOU 1844  C   TYR A 243    10669  10333  10799    374  -1098  -4044       C  
ATOM   1845  O   TYR A 243      -6.503   4.686  31.223  1.00 82.84           O  
ANISOU 1845  O   TYR A 243    10627   9914  10934    292  -1229  -4068       O  
ATOM   1846  CB  TYR A 243      -3.846   5.500  29.473  1.00 96.25           C  
ANISOU 1846  CB  TYR A 243    12161  12165  12245    669  -1003  -4558       C  
ATOM   1847  CG  TYR A 243      -3.472   4.292  30.301  1.00 99.87           C  
ANISOU 1847  CG  TYR A 243    12698  12172  13075    750  -1134  -4627       C  
ATOM   1848  CD1 TYR A 243      -3.648   3.005  29.808  1.00108.41           C  
ANISOU 1848  CD1 TYR A 243    13817  13020  14355    767  -1281  -4951       C  
ATOM   1849  CD2 TYR A 243      -2.952   4.437  31.580  1.00 98.96           C  
ANISOU 1849  CD2 TYR A 243    12632  11852  13117    803  -1132  -4364       C  
ATOM   1850  CE1 TYR A 243      -3.312   1.897  30.565  1.00105.92           C  
ANISOU 1850  CE1 TYR A 243    13589  12252  14404    839  -1432  -4994       C  
ATOM   1851  CE2 TYR A 243      -2.615   3.336  32.344  1.00101.35           C  
ANISOU 1851  CE2 TYR A 243    13020  11732  13757    869  -1282  -4392       C  
ATOM   1852  CZ  TYR A 243      -2.797   2.069  31.832  1.00110.23           C  
ANISOU 1852  CZ  TYR A 243    14184  12604  15095    889  -1436  -4698       C  
ATOM   1853  OH  TYR A 243      -2.462   0.969  32.588  1.00124.99           O  
ANISOU 1853  OH  TYR A 243    16152  14015  17324    954  -1614  -4709       O  
ATOM   1854  N   VAL A 244      -5.848   6.811  31.572  1.00 85.64           N  
ANISOU 1854  N   VAL A 244    10907  10686  10947    375   -988  -3734       N  
ATOM   1855  CA  VAL A 244      -6.482   6.868  32.885  1.00 89.01           C  
ANISOU 1855  CA  VAL A 244    11394  10909  11516    274  -1002  -3423       C  
ATOM   1856  C   VAL A 244      -7.999   6.850  32.743  1.00 92.49           C  
ANISOU 1856  C   VAL A 244    11804  11389  11950     86  -1050  -3339       C  
ATOM   1857  O   VAL A 244      -8.700   6.175  33.508  1.00 89.91           O  
ANISOU 1857  O   VAL A 244    11524  10824  11814    -43  -1121  -3227       O  
ATOM   1858  CB  VAL A 244      -5.996   8.109  33.655  1.00 93.51           C  
ANISOU 1858  CB  VAL A 244    11960  11609  11962    328   -871  -3157       C  
ATOM   1859  CG1 VAL A 244      -6.870   8.358  34.873  1.00 91.92           C  
ANISOU 1859  CG1 VAL A 244    11799  11293  11834    203   -857  -2855       C  
ATOM   1860  CG2 VAL A 244      -4.543   7.937  34.066  1.00 92.54           C  
ANISOU 1860  CG2 VAL A 244    11864  11383  11913    490   -854  -3209       C  
ATOM   1861  N   ARG A 245      -8.528   7.582  31.759  1.00105.15           N  
ANISOU 1861  N   ARG A 245    13319  13302  13330     55  -1020  -3383       N  
ATOM   1862  CA  ARG A 245      -9.970   7.589  31.529  1.00103.01           C  
ANISOU 1862  CA  ARG A 245    12986  13098  13056   -112  -1082  -3322       C  
ATOM   1863  C   ARG A 245     -10.471   6.208  31.132  1.00 92.80           C  
ANISOU 1863  C   ARG A 245    11718  11599  11942   -218  -1236  -3545       C  
ATOM   1864  O   ARG A 245     -11.541   5.776  31.577  1.00 99.00           O  
ANISOU 1864  O   ARG A 245    12484  12263  12869   -387  -1302  -3442       O  
ATOM   1865  CB  ARG A 245     -10.325   8.611  30.452  1.00 95.07           C  
ANISOU 1865  CB  ARG A 245    11888  12458  11776   -106  -1058  -3335       C  
ATOM   1866  CG  ARG A 245     -11.785   8.589  30.040  1.00 87.78           C  
ANISOU 1866  CG  ARG A 245    10872  11630  10848   -261  -1152  -3309       C  
ATOM   1867  CD  ARG A 245     -12.067   9.681  29.034  1.00 96.98           C  
ANISOU 1867  CD  ARG A 245    11959  13147  11743   -241  -1153  -3280       C  
ATOM   1868  NE  ARG A 245     -11.154   9.590  27.902  1.00 91.96           N  
ANISOU 1868  NE  ARG A 245    11356  12676  10907   -167  -1155  -3517       N  
ATOM   1869  CZ  ARG A 245     -11.009  10.530  26.979  1.00 93.21           C  
ANISOU 1869  CZ  ARG A 245    11482  13149  10784   -143  -1141  -3492       C  
ATOM   1870  NH1 ARG A 245     -11.712  11.650  27.017  1.00 96.80           N  
ANISOU 1870  NH1 ARG A 245    11876  13756  11147   -165  -1150  -3242       N  
ATOM   1871  NH2 ARG A 245     -10.134  10.342  25.995  1.00 92.63           N  
ANISOU 1871  NH2 ARG A 245    11435  13243  10516    -96  -1122  -3724       N  
ATOM   1872  N   ALA A 246      -9.717   5.505  30.284  1.00 92.39           N  
ANISOU 1872  N   ALA A 246    11700  11514  11891   -127  -1292  -3866       N  
ATOM   1873  CA  ALA A 246     -10.080   4.135  29.942  1.00 99.20           C  
ANISOU 1873  CA  ALA A 246    12607  12127  12957   -211  -1455  -4111       C  
ATOM   1874  C   ALA A 246     -10.125   3.254  31.185  1.00104.26           C  
ANISOU 1874  C   ALA A 246    13348  12349  13917   -277  -1526  -3966       C  
ATOM   1875  O   ALA A 246     -11.048   2.447  31.349  1.00102.36           O  
ANISOU 1875  O   ALA A 246    13127  11909  13855   -462  -1650  -3959       O  
ATOM   1876  CB  ALA A 246      -9.096   3.570  28.917  1.00108.51           C  
ANISOU 1876  CB  ALA A 246    13806  13334  14089    -61  -1485  -4510       C  
ATOM   1877  N   LYS A 247      -9.150   3.411  32.084  1.00112.44           N  
ANISOU 1877  N   LYS A 247    14448  13253  15022   -148  -1459  -3829       N  
ATOM   1878  CA  LYS A 247      -9.083   2.550  33.258  1.00109.93           C  
ANISOU 1878  CA  LYS A 247    14244  12534  14989   -209  -1548  -3676       C  
ATOM   1879  C   LYS A 247     -10.082   2.961  34.335  1.00106.23           C  
ANISOU 1879  C   LYS A 247    13767  12070  14526   -406  -1495  -3303       C  
ATOM   1880  O   LYS A 247     -10.553   2.101  35.088  1.00112.15           O  
ANISOU 1880  O   LYS A 247    14596  12526  15492   -569  -1596  -3178       O  
ATOM   1881  CB  LYS A 247      -7.662   2.538  33.825  1.00101.12           C  
ANISOU 1881  CB  LYS A 247    13194  11285  13943      2  -1521  -3668       C  
ATOM   1882  CG  LYS A 247      -6.611   2.013  32.850  1.00109.86           C  
ANISOU 1882  CG  LYS A 247    14286  12373  15082    211  -1567  -4064       C  
ATOM   1883  CD  LYS A 247      -6.770   0.526  32.573  1.00122.12           C  
ANISOU 1883  CD  LYS A 247    15922  13549  16930    179  -1776  -4317       C  
ATOM   1884  CE  LYS A 247      -6.247  -0.322  33.718  1.00123.68           C  
ANISOU 1884  CE  LYS A 247    16251  13293  17449    213  -1912  -4175       C  
ATOM   1885  NZ  LYS A 247      -6.371  -1.777  33.422  1.00137.41           N  
ANISOU 1885  NZ  LYS A 247    18085  14618  19508    190  -2143  -4428       N  
ATOM   1886  N   LEU A 248     -10.414   4.252  34.435  1.00 88.04           N  
ANISOU 1886  N   LEU A 248    11367  10092  11992   -400  -1340  -3126       N  
ATOM   1887  CA  LEU A 248     -11.494   4.656  35.331  1.00 88.65           C  
ANISOU 1887  CA  LEU A 248    11398  10221  12064   -582  -1277  -2832       C  
ATOM   1888  C   LEU A 248     -12.843   4.161  34.834  1.00102.88           C  
ANISOU 1888  C   LEU A 248    13112  12047  13929   -796  -1365  -2888       C  
ATOM   1889  O   LEU A 248     -13.714   3.816  35.642  1.00108.69           O  
ANISOU 1889  O   LEU A 248    13834  12683  14778  -1002  -1373  -2696       O  
ATOM   1890  CB  LEU A 248     -11.535   6.178  35.489  1.00 85.12           C  
ANISOU 1890  CB  LEU A 248    10862  10100  11382   -498  -1106  -2671       C  
ATOM   1891  CG  LEU A 248     -10.460   6.893  36.305  1.00 93.08           C  
ANISOU 1891  CG  LEU A 248    11938  11111  12317   -347   -997  -2526       C  
ATOM   1892  CD1 LEU A 248     -10.833   8.358  36.473  1.00 87.19           C  
ANISOU 1892  CD1 LEU A 248    11100  10656  11372   -312   -853  -2365       C  
ATOM   1893  CD2 LEU A 248     -10.292   6.224  37.659  1.00 97.17           C  
ANISOU 1893  CD2 LEU A 248    12574  11346  12999   -432  -1024  -2335       C  
ATOM   1894  N   MET A 249     -13.032   4.125  33.513  1.00117.44           N  
ANISOU 1894  N   MET A 249    14890  14046  15687   -765  -1432  -3147       N  
ATOM   1895  CA  MET A 249     -14.303   3.692  32.945  1.00112.13           C  
ANISOU 1895  CA  MET A 249    14119  13422  15062   -967  -1536  -3220       C  
ATOM   1896  C   MET A 249     -14.609   2.240  33.294  1.00118.92           C  
ANISOU 1896  C   MET A 249    15073  13903  16210  -1152  -1694  -3268       C  
ATOM   1897  O   MET A 249     -15.780   1.867  33.425  1.00132.87           O  
ANISOU 1897  O   MET A 249    16760  15652  18072  -1392  -1755  -3192       O  
ATOM   1898  CB  MET A 249     -14.274   3.906  31.431  1.00112.36           C  
ANISOU 1898  CB  MET A 249    14086  13691  14914   -887  -1595  -3506       C  
ATOM   1899  CG  MET A 249     -15.623   3.892  30.746  1.00127.25           C  
ANISOU 1899  CG  MET A 249    15829  15752  16768  -1068  -1689  -3551       C  
ATOM   1900  SD  MET A 249     -15.417   4.178  28.979  1.00137.94           S  
ANISOU 1900  SD  MET A 249    17142  17412  17857   -968  -1766  -3876       S  
ATOM   1901  CE  MET A 249     -14.458   2.737  28.521  1.00130.94           C  
ANISOU 1901  CE  MET A 249    16419  16204  17126   -912  -1884  -4255       C  
ATOM   1902  N   ASN A 250     -13.575   1.413  33.464  1.00113.85           N  
ANISOU 1902  N   ASN A 250    14591  12944  15724  -1049  -1773  -3387       N  
ATOM   1903  CA  ASN A 250     -13.780   0.056  33.955  1.00116.80           C  
ANISOU 1903  CA  ASN A 250    15084  12894  16402  -1220  -1942  -3382       C  
ATOM   1904  C   ASN A 250     -14.205   0.026  35.419  1.00103.41           C  
ANISOU 1904  C   ASN A 250    13424  11068  14797  -1402  -1888  -2991       C  
ATOM   1905  O   ASN A 250     -14.793  -0.968  35.859  1.00105.44           O  
ANISOU 1905  O   ASN A 250    13744  11043  15276  -1642  -2018  -2906       O  
ATOM   1906  CB  ASN A 250     -12.503  -0.772  33.785  1.00121.34           C  
ANISOU 1906  CB  ASN A 250    15815  13148  17142  -1023  -2056  -3611       C  
ATOM   1907  CG  ASN A 250     -12.180  -1.066  32.333  1.00138.47           C  
ANISOU 1907  CG  ASN A 250    17957  15399  19256   -890  -2133  -4052       C  
ATOM   1908  OD1 ASN A 250     -13.048  -1.002  31.463  1.00132.22           O  
ANISOU 1908  OD1 ASN A 250    17068  14804  18364  -1010  -2170  -4191       O  
ATOM   1909  ND2 ASN A 250     -10.921  -1.398  32.066  1.00143.88           N  
ANISOU 1909  ND2 ASN A 250    18718  15950  20002   -644  -2160  -4285       N  
ATOM   1910  N   ALA A 251     -13.926   1.089  36.179  1.00107.88           N  
ANISOU 1910  N   ALA A 251    13958  11840  15191  -1310  -1702  -2754       N  
ATOM   1911  CA  ALA A 251     -14.139   1.094  37.622  1.00116.22           C  
ANISOU 1911  CA  ALA A 251    15068  12797  16292  -1458  -1634  -2402       C  
ATOM   1912  C   ALA A 251     -15.420   1.795  38.055  1.00117.03           C  
ANISOU 1912  C   ALA A 251    14998  13194  16274  -1654  -1491  -2194       C  
ATOM   1913  O   ALA A 251     -15.936   1.491  39.137  1.00103.52           O  
ANISOU 1913  O   ALA A 251    13310  11397  14626  -1875  -1459  -1933       O  
ATOM   1914  CB  ALA A 251     -12.945   1.747  38.330  1.00109.94           C  
ANISOU 1914  CB  ALA A 251    14362  12016  15395  -1237  -1531  -2283       C  
ATOM   1915  N   TYR A 252     -15.923   2.742  37.264  1.00129.26           N  
ANISOU 1915  N   TYR A 252    16368  15095  17648  -1575  -1405  -2296       N  
ATOM   1916  CA  TYR A 252     -17.281   3.262  37.418  1.00129.36           C  
ANISOU 1916  CA  TYR A 252    16173  15377  17600  -1752  -1315  -2173       C  
ATOM   1917  C   TYR A 252     -17.895   3.335  36.027  1.00123.87           C  
ANISOU 1917  C   TYR A 252    15337  14859  16870  -1745  -1412  -2416       C  
ATOM   1918  O   TYR A 252     -17.856   4.382  35.368  1.00125.04           O  
ANISOU 1918  O   TYR A 252    15384  15295  16832  -1568  -1348  -2486       O  
ATOM   1919  CB  TYR A 252     -17.311   4.635  38.094  1.00119.41           C  
ANISOU 1919  CB  TYR A 252    14821  14406  16144  -1635  -1099  -1993       C  
ATOM   1920  CG  TYR A 252     -16.245   4.901  39.136  1.00118.87           C  
ANISOU 1920  CG  TYR A 252    14918  14224  16024  -1517  -1008  -1835       C  
ATOM   1921  CD1 TYR A 252     -16.405   4.479  40.452  1.00127.78           C  
ANISOU 1921  CD1 TYR A 252    16122  15223  17207  -1702   -958  -1590       C  
ATOM   1922  CD2 TYR A 252     -15.091   5.599  38.812  1.00111.82           C  
ANISOU 1922  CD2 TYR A 252    14098  13376  15010  -1240   -973  -1922       C  
ATOM   1923  CE1 TYR A 252     -15.440   4.737  41.410  1.00125.35           C  
ANISOU 1923  CE1 TYR A 252    15966  14829  16832  -1601   -894  -1442       C  
ATOM   1924  CE2 TYR A 252     -14.119   5.857  39.762  1.00112.50           C  
ANISOU 1924  CE2 TYR A 252    14321  13370  15052  -1140   -906  -1782       C  
ATOM   1925  CZ  TYR A 252     -14.300   5.428  41.059  1.00124.32           C  
ANISOU 1925  CZ  TYR A 252    15898  14735  16602  -1314   -874  -1546       C  
ATOM   1926  OH  TYR A 252     -13.333   5.687  42.005  1.00136.74           O  
ANISOU 1926  OH  TYR A 252    17611  16229  18115  -1221   -827  -1406       O  
ATOM   1927  N   PRO A 253     -18.478   2.233  35.547  1.00113.12           N  
ANISOU 1927  N   PRO A 253    13974  13325  15681  -1948  -1585  -2543       N  
ATOM   1928  CA  PRO A 253     -18.899   2.198  34.136  1.00131.27           C  
ANISOU 1928  CA  PRO A 253    16171  15773  17931  -1931  -1710  -2816       C  
ATOM   1929  C   PRO A 253     -20.078   3.100  33.826  1.00129.11           C  
ANISOU 1929  C   PRO A 253    15637  15880  17538  -1989  -1652  -2752       C  
ATOM   1930  O   PRO A 253     -20.096   3.742  32.768  1.00120.82           O  
ANISOU 1930  O   PRO A 253    14508  15071  16326  -1849  -1687  -2905       O  
ATOM   1931  CB  PRO A 253     -19.241   0.718  33.916  1.00137.28           C  
ANISOU 1931  CB  PRO A 253    17014  16205  18942  -2164  -1919  -2947       C  
ATOM   1932  CG  PRO A 253     -19.617   0.218  35.273  1.00139.29           C  
ANISOU 1932  CG  PRO A 253    17307  16261  19357  -2399  -1874  -2648       C  
ATOM   1933  CD  PRO A 253     -18.748   0.965  36.245  1.00112.32           C  
ANISOU 1933  CD  PRO A 253    13978  12876  15823  -2213  -1693  -2442       C  
ATOM   1934  N   SER A 254     -21.069   3.169  34.715  1.00132.65           N  
ANISOU 1934  N   SER A 254    15942  16400  18060  -2195  -1568  -2528       N  
ATOM   1935  CA  SER A 254     -22.267   3.955  34.446  1.00124.06           C  
ANISOU 1935  CA  SER A 254    14569  15664  16903  -2248  -1527  -2484       C  
ATOM   1936  C   SER A 254     -22.036   5.456  34.560  1.00124.10           C  
ANISOU 1936  C   SER A 254    14493  15951  16708  -1985  -1365  -2394       C  
ATOM   1937  O   SER A 254     -22.945   6.226  34.229  1.00108.15           O  
ANISOU 1937  O   SER A 254    12237  14221  14635  -1970  -1353  -2376       O  
ATOM   1938  CB  SER A 254     -23.385   3.541  35.405  1.00125.79           C  
ANISOU 1938  CB  SER A 254    14631  15894  17268  -2555  -1466  -2288       C  
ATOM   1939  OG  SER A 254     -23.016   3.787  36.751  1.00130.86           O  
ANISOU 1939  OG  SER A 254    15350  16482  17887  -2553  -1275  -2051       O  
ATOM   1940  N   TYR A 255     -20.852   5.891  34.999  1.00115.70           N  
ANISOU 1940  N   TYR A 255    13613  14800  15549  -1779  -1260  -2342       N  
ATOM   1941  CA  TYR A 255     -20.646   7.277  35.397  1.00102.32           C  
ANISOU 1941  CA  TYR A 255    11859  13319  13698  -1570  -1095  -2217       C  
ATOM   1942  C   TYR A 255     -19.695   8.068  34.506  1.00 99.18           C  
ANISOU 1942  C   TYR A 255    11551  13011  13122  -1301  -1118  -2329       C  
ATOM   1943  O   TYR A 255     -19.724   9.301  34.556  1.00 97.65           O  
ANISOU 1943  O   TYR A 255    11279  13018  12806  -1140  -1028  -2245       O  
ATOM   1944  CB  TYR A 255     -20.118   7.337  36.840  1.00102.43           C  
ANISOU 1944  CB  TYR A 255    11991  13205  13724  -1575   -927  -2018       C  
ATOM   1945  CG  TYR A 255     -21.093   6.864  37.902  1.00103.77           C  
ANISOU 1945  CG  TYR A 255    12049  13373  14006  -1843   -845  -1850       C  
ATOM   1946  CD1 TYR A 255     -22.228   7.603  38.216  1.00103.15           C  
ANISOU 1946  CD1 TYR A 255    11704  13581  13908  -1889   -731  -1772       C  
ATOM   1947  CD2 TYR A 255     -20.869   5.684  38.602  1.00118.57           C  
ANISOU 1947  CD2 TYR A 255    14078  14963  16008  -2052   -883  -1764       C  
ATOM   1948  CE1 TYR A 255     -23.115   7.177  39.191  1.00108.42           C  
ANISOU 1948  CE1 TYR A 255    12245  14292  14656  -2151   -629  -1626       C  
ATOM   1949  CE2 TYR A 255     -21.750   5.250  39.577  1.00125.72           C  
ANISOU 1949  CE2 TYR A 255    14886  15890  16990  -2334   -801  -1584       C  
ATOM   1950  CZ  TYR A 255     -22.871   6.000  39.867  1.00119.15           C  
ANISOU 1950  CZ  TYR A 255    13772  15385  16113  -2389   -660  -1522       C  
ATOM   1951  OH  TYR A 255     -23.750   5.572  40.836  1.00123.80           O  
ANISOU 1951  OH  TYR A 255    14241  16040  16758  -2686   -553  -1352       O  
ATOM   1952  N   ILE A 256     -18.858   7.411  33.702  1.00112.94           N  
ANISOU 1952  N   ILE A 256    13451  14613  14847  -1252  -1234  -2519       N  
ATOM   1953  CA  ILE A 256     -17.798   8.083  32.956  1.00113.58           C  
ANISOU 1953  CA  ILE A 256    13629  14784  14743  -1021  -1228  -2616       C  
ATOM   1954  C   ILE A 256     -18.048   7.923  31.462  1.00115.03           C  
ANISOU 1954  C   ILE A 256    13763  15114  14828  -1026  -1388  -2839       C  
ATOM   1955  O   ILE A 256     -18.449   6.849  31.000  1.00116.60           O  
ANISOU 1955  O   ILE A 256    13964  15203  15135  -1178  -1526  -3002       O  
ATOM   1956  CB  ILE A 256     -16.407   7.536  33.344  1.00118.16           C  
ANISOU 1956  CB  ILE A 256    14428  15113  15356   -927  -1196  -2666       C  
ATOM   1957  CG1 ILE A 256     -16.041   7.974  34.763  1.00114.85           C  
ANISOU 1957  CG1 ILE A 256    14065  14610  14963   -891  -1039  -2429       C  
ATOM   1958  CG2 ILE A 256     -15.339   8.003  32.364  1.00113.46           C  
ANISOU 1958  CG2 ILE A 256    13905  14630  14573   -729  -1204  -2822       C  
ATOM   1959  CD1 ILE A 256     -15.043   7.064  35.442  1.00121.57           C  
ANISOU 1959  CD1 ILE A 256    15107  15149  15936   -887  -1054  -2430       C  
ATOM   1960  N   SER A 257     -17.801   9.017  30.696  1.00119.26           N  
ANISOU 1960  N   SER A 257    14266  15901  15147   -869  -1381  -2839       N  
ATOM   1961  CA  SER A 257     -17.941   9.063  29.240  1.00122.54           C  
ANISOU 1961  CA  SER A 257    14648  16514  15396   -863  -1527  -3022       C  
ATOM   1962  C   SER A 257     -16.621   8.698  28.570  1.00113.88           C  
ANISOU 1962  C   SER A 257    13724  15374  14173   -758  -1527  -3230       C  
ATOM   1963  O   SER A 257     -15.567   9.203  28.977  1.00120.68           O  
ANISOU 1963  O   SER A 257    14681  16203  14967   -611  -1399  -3158       O  
ATOM   1964  CB  SER A 257     -18.377  10.447  28.782  1.00127.94           C  
ANISOU 1964  CB  SER A 257    15213  17491  15909   -766  -1535  -2880       C  
ATOM   1965  OG  SER A 257     -18.287  10.574  27.373  1.00110.82           O  
ANISOU 1965  OG  SER A 257    13053  15531  13524   -753  -1671  -3030       O  
ATOM   1966  N   PRO A 258     -16.638   7.840  27.547  1.00108.58           N  
ANISOU 1966  N   PRO A 258    13080  14712  13462   -828  -1665  -3504       N  
ATOM   1967  CA  PRO A 258     -15.394   7.450  26.870  1.00106.20           C  
ANISOU 1967  CA  PRO A 258    12916  14398  13037   -719  -1652  -3750       C  
ATOM   1968  C   PRO A 258     -14.811   8.508  25.945  1.00107.52           C  
ANISOU 1968  C   PRO A 258    13084  14892  12875   -600  -1611  -3750       C  
ATOM   1969  O   PRO A 258     -13.741   8.275  25.373  1.00106.67           O  
ANISOU 1969  O   PRO A 258    13065  14828  12636   -511  -1570  -3953       O  
ATOM   1970  CB  PRO A 258     -15.816   6.205  26.072  1.00 98.13           C  
ANISOU 1970  CB  PRO A 258    11905  13295  12083   -853  -1825  -4062       C  
ATOM   1971  CG  PRO A 258     -17.274   6.388  25.841  1.00107.19           C  
ANISOU 1971  CG  PRO A 258    12896  14582  13249  -1018  -1949  -3967       C  
ATOM   1972  CD  PRO A 258     -17.798   7.067  27.073  1.00106.19           C  
ANISOU 1972  CD  PRO A 258    12680  14408  13258  -1023  -1838  -3625       C  
ATOM   1973  N   ILE A 259     -15.477   9.650  25.762  1.00108.98           N  
ANISOU 1973  N   ILE A 259    13169  15310  12928   -600  -1628  -3530       N  
ATOM   1974  CA  ILE A 259     -14.914  10.768  25.013  1.00102.51           C  
ANISOU 1974  CA  ILE A 259    12369  14774  11807   -504  -1595  -3456       C  
ATOM   1975  C   ILE A 259     -14.918  12.062  25.809  1.00 97.84           C  
ANISOU 1975  C   ILE A 259    11747  14201  11227   -410  -1494  -3127       C  
ATOM   1976  O   ILE A 259     -14.464  13.088  25.301  1.00 93.70           O  
ANISOU 1976  O   ILE A 259    11247  13877  10479   -342  -1474  -3015       O  
ATOM   1977  CB  ILE A 259     -15.639  10.983  23.668  1.00 96.21           C  
ANISOU 1977  CB  ILE A 259    11504  14277  10776   -592  -1771  -3533       C  
ATOM   1978  CG1 ILE A 259     -17.062  11.493  23.905  1.00101.98           C  
ANISOU 1978  CG1 ILE A 259    12074  15056  11616   -658  -1885  -3324       C  
ATOM   1979  CG2 ILE A 259     -15.643   9.705  22.842  1.00 96.02           C  
ANISOU 1979  CG2 ILE A 259    11515  14242  10724   -690  -1878  -3898       C  
ATOM   1980  CD1 ILE A 259     -17.748  11.984  22.650  1.00104.69           C  
ANISOU 1980  CD1 ILE A 259    12346  15714  11718   -719  -2078  -3321       C  
ATOM   1981  N   GLY A 260     -15.430  12.054  27.039  1.00109.47           N  
ANISOU 1981  N   GLY A 260    13172  15476  12948   -416  -1434  -2970       N  
ATOM   1982  CA  GLY A 260     -15.562  13.267  27.814  1.00125.50           C  
ANISOU 1982  CA  GLY A 260    15162  17521  15001   -326  -1347  -2694       C  
ATOM   1983  C   GLY A 260     -14.372  13.524  28.718  1.00103.05           C  
ANISOU 1983  C   GLY A 260    12439  14528  12187   -218  -1177  -2619       C  
ATOM   1984  O   GLY A 260     -13.393  12.778  28.751  1.00 92.44           O  
ANISOU 1984  O   GLY A 260    11200  13072  10852   -199  -1126  -2770       O  
ATOM   1985  N   CYS A 261     -14.467  14.622  29.460  1.00 88.06           N  
ANISOU 1985  N   CYS A 261    10518  12628  10313   -137  -1100  -2393       N  
ATOM   1986  CA  CYS A 261     -13.476  14.935  30.472  1.00 93.90           C  
ANISOU 1986  CA  CYS A 261    11360  13224  11096    -49   -950  -2302       C  
ATOM   1987  C   CYS A 261     -13.639  14.012  31.676  1.00 98.16           C  
ANISOU 1987  C   CYS A 261    11913  13523  11858   -106   -883  -2309       C  
ATOM   1988  O   CYS A 261     -14.638  13.304  31.828  1.00 91.99           O  
ANISOU 1988  O   CYS A 261    11047  12693  11210   -221   -938  -2345       O  
ATOM   1989  CB  CYS A 261     -13.581  16.399  30.892  1.00106.08           C  
ANISOU 1989  CB  CYS A 261    12881  14825  12601     47   -905  -2079       C  
ATOM   1990  SG  CYS A 261     -13.550  17.559  29.511  1.00130.55           S  
ANISOU 1990  SG  CYS A 261    15970  18182  15451     85  -1022  -2002       S  
ATOM   1991  N   LEU A 262     -12.640  14.021  32.530  1.00100.51           N  
ANISOU 1991  N   LEU A 262    12320  13679  12192    -42   -775  -2262       N  
ATOM   1992  CA  LEU A 262     -12.705  13.149  33.695  1.00 97.02           C  
ANISOU 1992  CA  LEU A 262    11918  13008  11938   -108   -727  -2239       C  
ATOM   1993  C   LEU A 262     -13.425  13.860  34.833  1.00 90.69           C  
ANISOU 1993  C   LEU A 262    11055  12203  11201   -117   -636  -2043       C  
ATOM   1994  O   LEU A 262     -13.102  15.014  35.131  1.00 90.89           O  
ANISOU 1994  O   LEU A 262    11094  12296  11145    -10   -567  -1929       O  
ATOM   1995  CB  LEU A 262     -11.309  12.740  34.138  1.00 79.33           C  
ANISOU 1995  CB  LEU A 262     9817  10610   9714    -36   -676  -2280       C  
ATOM   1996  CG  LEU A 262     -10.698  11.614  33.302  1.00 79.35           C  
ANISOU 1996  CG  LEU A 262     9867  10544   9737    -39   -760  -2522       C  
ATOM   1997  CD1 LEU A 262      -9.233  11.406  33.654  1.00 98.23           C  
ANISOU 1997  CD1 LEU A 262    12361  12820  12143     73   -712  -2569       C  
ATOM   1998  CD2 LEU A 262     -11.491  10.326  33.472  1.00102.16           C  
ANISOU 1998  CD2 LEU A 262    12750  13251  12817   -180   -852  -2604       C  
ATOM   1999  N   PRO A 263     -14.410  13.223  35.468  1.00 82.76           N  
ANISOU 1999  N   PRO A 263     9977  11131  10337   -250   -632  -2009       N  
ATOM   2000  CA  PRO A 263     -15.062  13.847  36.627  1.00 83.43           C  
ANISOU 2000  CA  PRO A 263     9991  11240  10468   -263   -515  -1850       C  
ATOM   2001  C   PRO A 263     -14.046  14.199  37.704  1.00 92.10           C  
ANISOU 2001  C   PRO A 263    11232  12228  11533   -189   -403  -1752       C  
ATOM   2002  O   PRO A 263     -13.191  13.386  38.066  1.00104.14           O  
ANISOU 2002  O   PRO A 263    12893  13580  13097   -215   -412  -1771       O  
ATOM   2003  CB  PRO A 263     -16.045  12.769  37.095  1.00 93.84           C  
ANISOU 2003  CB  PRO A 263    11231  12489  11934   -464   -528  -1848       C  
ATOM   2004  CG  PRO A 263     -16.369  12.029  35.836  1.00 87.04           C  
ANISOU 2004  CG  PRO A 263    10326  11649  11096   -531   -686  -2009       C  
ATOM   2005  CD  PRO A 263     -15.044  11.939  35.122  1.00 87.31           C  
ANISOU 2005  CD  PRO A 263    10516  11626  11033   -410   -732  -2123       C  
ATOM   2006  N   ALA A 264     -14.148  15.430  38.213  1.00 88.96           N  
ANISOU 2006  N   ALA A 264    10802  11923  11076    -89   -313  -1654       N  
ATOM   2007  CA  ALA A 264     -13.107  15.969  39.084  1.00 81.32           C  
ANISOU 2007  CA  ALA A 264     9972  10878  10050     -5   -226  -1577       C  
ATOM   2008  C   ALA A 264     -12.935  15.133  40.344  1.00 92.24           C  
ANISOU 2008  C   ALA A 264    11441  12114  11492   -116   -162  -1509       C  
ATOM   2009  O   ALA A 264     -11.805  14.835  40.748  1.00 98.48           O  
ANISOU 2009  O   ALA A 264    12379  12773  12265    -88   -167  -1490       O  
ATOM   2010  CB  ALA A 264     -13.424  17.419  39.446  1.00 79.85           C  
ANISOU 2010  CB  ALA A 264     9728  10800   9812    109   -154  -1504       C  
ATOM   2011  N   HIS A 265     -14.040  14.731  40.972  1.00 98.64           N  
ANISOU 2011  N   HIS A 265    12153  12956  12370   -255   -108  -1462       N  
ATOM   2012  CA  HIS A 265     -13.953  14.043  42.254  1.00 97.10           C  
ANISOU 2012  CA  HIS A 265    12046  12650  12198   -389    -41  -1356       C  
ATOM   2013  C   HIS A 265     -13.291  12.675  42.151  1.00100.20           C  
ANISOU 2013  C   HIS A 265    12574  12819  12679   -481   -156  -1369       C  
ATOM   2014  O   HIS A 265     -12.912  12.115  43.185  1.00102.07           O  
ANISOU 2014  O   HIS A 265    12932  12923  12927   -572   -138  -1257       O  
ATOM   2015  CB  HIS A 265     -15.351  13.918  42.878  1.00101.74           C  
ANISOU 2015  CB  HIS A 265    12472  13361  12824   -546     55  -1302       C  
ATOM   2016  CG  HIS A 265     -16.351  13.196  42.024  1.00103.58           C  
ANISOU 2016  CG  HIS A 265    12555  13632  13169   -668    -32  -1372       C  
ATOM   2017  ND1 HIS A 265     -16.671  13.594  40.743  1.00103.17           N  
ANISOU 2017  ND1 HIS A 265    12392  13679  13130   -568   -128  -1487       N  
ATOM   2018  CD2 HIS A 265     -17.151  12.137  42.297  1.00108.09           C  
ANISOU 2018  CD2 HIS A 265    13064  14167  13838   -900    -45  -1334       C  
ATOM   2019  CE1 HIS A 265     -17.591  12.785  40.248  1.00110.29           C  
ANISOU 2019  CE1 HIS A 265    13170  14602  14134   -724   -203  -1535       C  
ATOM   2020  NE2 HIS A 265     -17.902  11.894  41.172  1.00109.68           N  
ANISOU 2020  NE2 HIS A 265    13117  14437  14120   -931   -153  -1445       N  
ATOM   2021  N   LEU A 266     -13.110  12.147  40.940  1.00105.17           N  
ANISOU 2021  N   LEU A 266    13193  13400  13366   -451   -282  -1508       N  
ATOM   2022  CA  LEU A 266     -12.600  10.800  40.713  1.00103.53           C  
ANISOU 2022  CA  LEU A 266    13094  12964  13280   -522   -410  -1570       C  
ATOM   2023  C   LEU A 266     -11.098  10.760  40.465  1.00 99.20           C  
ANISOU 2023  C   LEU A 266    12679  12302  12712   -359   -464  -1640       C  
ATOM   2024  O   LEU A 266     -10.591   9.758  39.948  1.00 96.82           O  
ANISOU 2024  O   LEU A 266    12440  11831  12518   -355   -584  -1761       O  
ATOM   2025  CB  LEU A 266     -13.332  10.164  39.529  1.00 97.28           C  
ANISOU 2025  CB  LEU A 266    12202  12193  12568   -592   -520  -1724       C  
ATOM   2026  CG  LEU A 266     -14.489   9.207  39.812  1.00 96.83           C  
ANISOU 2026  CG  LEU A 266    12078  12070  12644   -834   -558  -1681       C  
ATOM   2027  CD1 LEU A 266     -15.513   9.832  40.722  1.00110.78           C  
ANISOU 2027  CD1 LEU A 266    13717  14011  14365   -935   -412  -1524       C  
ATOM   2028  CD2 LEU A 266     -15.142   8.793  38.502  1.00103.29           C  
ANISOU 2028  CD2 LEU A 266    12787  12944  13514   -878   -680  -1863       C  
ATOM   2029  N   LEU A 267     -10.366  11.804  40.842  1.00 89.81           N  
ANISOU 2029  N   LEU A 267    11525  11197  11401   -226   -382  -1580       N  
ATOM   2030  CA  LEU A 267      -8.972  11.927  40.439  1.00 93.38           C  
ANISOU 2030  CA  LEU A 267    12054  11604  11823    -71   -422  -1663       C  
ATOM   2031  C   LEU A 267      -7.971  11.758  41.580  1.00 97.61           C  
ANISOU 2031  C   LEU A 267    12722  11987  12378    -44   -424  -1550       C  
ATOM   2032  O   LEU A 267      -6.790  12.054  41.389  1.00 98.79           O  
ANISOU 2032  O   LEU A 267    12910  12133  12495     90   -440  -1601       O  
ATOM   2033  CB  LEU A 267      -8.766  13.271  39.739  1.00 87.20           C  
ANISOU 2033  CB  LEU A 267    11203  11040  10888     55   -361  -1696       C  
ATOM   2034  CG  LEU A 267      -9.622  13.451  38.483  1.00 73.92           C  
ANISOU 2034  CG  LEU A 267     9399   9518   9170     42   -396  -1802       C  
ATOM   2035  CD1 LEU A 267      -9.448  14.844  37.928  1.00 71.74           C  
ANISOU 2035  CD1 LEU A 267     9078   9435   8744    148   -353  -1777       C  
ATOM   2036  CD2 LEU A 267      -9.282  12.406  37.425  1.00 82.41           C  
ANISOU 2036  CD2 LEU A 267    10480  10536  10298     41   -504  -2000       C  
ATOM   2037  N   GLY A 268      -8.396  11.287  42.754  1.00 93.93           N  
ANISOU 2037  N   GLY A 268    12322  11413  11954   -180   -413  -1392       N  
ATOM   2038  CA  GLY A 268      -7.461  10.947  43.812  1.00 96.29           C  
ANISOU 2038  CA  GLY A 268    12762  11551  12274   -174   -457  -1273       C  
ATOM   2039  C   GLY A 268      -7.116  12.049  44.797  1.00 98.48           C  
ANISOU 2039  C   GLY A 268    13080  11943  12395   -139   -352  -1146       C  
ATOM   2040  O   GLY A 268      -6.537  11.750  45.846  1.00 92.14           O  
ANISOU 2040  O   GLY A 268    12398  11026  11586   -175   -391  -1016       O  
ATOM   2041  N   ASP A 269      -7.423  13.306  44.492  1.00106.28           N  
ANISOU 2041  N   ASP A 269    13981  13138  13260    -68   -239  -1182       N  
ATOM   2042  CA  ASP A 269      -7.260  14.406  45.437  1.00 84.45           C  
ANISOU 2042  CA  ASP A 269    11254  10477  10356    -43   -138  -1087       C  
ATOM   2043  C   ASP A 269      -8.595  15.132  45.543  1.00101.70           C  
ANISOU 2043  C   ASP A 269    13326  12836  12478    -94     -9  -1080       C  
ATOM   2044  O   ASP A 269      -9.421  15.064  44.631  1.00117.02           O  
ANISOU 2044  O   ASP A 269    15144  14846  14473   -102    -12  -1160       O  
ATOM   2045  CB  ASP A 269      -6.164  15.382  44.990  1.00 86.60           C  
ANISOU 2045  CB  ASP A 269    11534  10806  10566    118   -143  -1149       C  
ATOM   2046  CG  ASP A 269      -4.763  14.797  45.094  1.00111.41           C  
ANISOU 2046  CG  ASP A 269    14760  13807  13764    181   -254  -1156       C  
ATOM   2047  OD1 ASP A 269      -4.637  13.642  45.555  1.00122.34           O  
ANISOU 2047  OD1 ASP A 269    16214  15022  15248    115   -344  -1106       O  
ATOM   2048  OD2 ASP A 269      -3.791  15.470  44.678  1.00109.83           O1-
ANISOU 2048  OD2 ASP A 269    14544  13661  13523    293   -262  -1210       O1-
ATOM   2049  N   MET A 270      -8.797  15.838  46.658  1.00 92.27           N  
ANISOU 2049  N   MET A 270    12164  11722  11172   -122     98  -1000       N  
ATOM   2050  CA  MET A 270      -9.981  16.672  46.762  1.00 88.21           C  
ANISOU 2050  CA  MET A 270    11520  11385  10612   -125    227  -1030       C  
ATOM   2051  C   MET A 270     -10.026  17.733  45.673  1.00 89.27           C  
ANISOU 2051  C   MET A 270    11560  11601  10756     36    215  -1133       C  
ATOM   2052  O   MET A 270     -11.106  18.021  45.137  1.00 99.25           O  
ANISOU 2052  O   MET A 270    12674  12975  12061     44    246  -1184       O  
ATOM   2053  CB  MET A 270     -10.065  17.320  48.139  1.00 96.37           C  
ANISOU 2053  CB  MET A 270    12611  12499  11509   -159    348   -968       C  
ATOM   2054  CG  MET A 270     -10.952  18.504  48.183  1.00 85.75           C  
ANISOU 2054  CG  MET A 270    11134  11320  10125    -79    471  -1050       C  
ATOM   2055  SD  MET A 270     -12.613  18.054  48.620  1.00 90.14           S  
ANISOU 2055  SD  MET A 270    11512  12040  10695   -237    608  -1045       S  
ATOM   2056  CE  MET A 270     -12.318  17.134  50.119  1.00 94.22           C  
ANISOU 2056  CE  MET A 270    12189  12529  11081   -458    657   -887       C  
ATOM   2057  N   TRP A 271      -8.862  18.266  45.287  1.00 97.18           N  
ANISOU 2057  N   TRP A 271    12642  12554  11728    152    154  -1153       N  
ATOM   2058  CA  TRP A 271      -8.724  19.306  44.285  1.00 99.82           C  
ANISOU 2058  CA  TRP A 271    12920  12955  12051    280    127  -1213       C  
ATOM   2059  C   TRP A 271      -8.232  18.766  42.937  1.00102.56           C  
ANISOU 2059  C   TRP A 271    13244  13286  12439    305     22  -1276       C  
ATOM   2060  O   TRP A 271      -8.166  19.522  41.957  1.00107.75           O  
ANISOU 2060  O   TRP A 271    13854  14020  13066    382    -12  -1309       O  
ATOM   2061  CB  TRP A 271      -7.766  20.396  44.792  1.00100.99           C  
ANISOU 2061  CB  TRP A 271    13168  13084  12121    362    140  -1186       C  
ATOM   2062  CG  TRP A 271      -7.968  20.694  46.258  1.00 98.98           C  
ANISOU 2062  CG  TRP A 271    12976  12834  11800    321    235  -1146       C  
ATOM   2063  CD1 TRP A 271      -8.913  21.511  46.800  1.00 99.90           C  
ANISOU 2063  CD1 TRP A 271    13029  13037  11890    347    336  -1178       C  
ATOM   2064  CD2 TRP A 271      -7.168  20.215  47.359  1.00 97.84           C  
ANISOU 2064  CD2 TRP A 271    12966  12618  11592    252    230  -1079       C  
ATOM   2065  NE1 TRP A 271      -8.779  21.535  48.170  1.00105.60           N  
ANISOU 2065  NE1 TRP A 271    13841  13767  12515    285    415  -1149       N  
ATOM   2066  CE2 TRP A 271      -7.714  20.756  48.536  1.00116.52           C  
ANISOU 2066  CE2 TRP A 271    15354  15053  13864    219    342  -1072       C  
ATOM   2067  CE3 TRP A 271      -6.051  19.370  47.463  1.00103.29           C  
ANISOU 2067  CE3 TRP A 271    13751  13196  12297    223    133  -1030       C  
ATOM   2068  CZ2 TRP A 271      -7.188  20.487  49.802  1.00139.18           C  
ANISOU 2068  CZ2 TRP A 271    18357  17901  16626    135    357  -1002       C  
ATOM   2069  CZ3 TRP A 271      -5.526  19.102  48.732  1.00130.10           C  
ANISOU 2069  CZ3 TRP A 271    17272  16545  15615    153    128   -946       C  
ATOM   2070  CH2 TRP A 271      -6.100  19.661  49.878  1.00139.84           C  
ANISOU 2070  CH2 TRP A 271    18542  17864  16725     99    237   -924       C  
ATOM   2071  N   GLY A 272      -7.898  17.483  42.854  1.00 97.80           N  
ANISOU 2071  N   GLY A 272    12676  12586  11899    241    -37  -1299       N  
ATOM   2072  CA  GLY A 272      -7.545  16.882  41.590  1.00 83.90           C  
ANISOU 2072  CA  GLY A 272    10880  10823  10174    266   -124  -1404       C  
ATOM   2073  C   GLY A 272      -6.235  17.402  41.025  1.00 99.25           C  
ANISOU 2073  C   GLY A 272    12861  12796  12054    364   -152  -1442       C  
ATOM   2074  O   GLY A 272      -6.122  17.645  39.823  1.00101.43           O  
ANISOU 2074  O   GLY A 272    13079  13177  12284    402   -184  -1518       O  
ATOM   2075  N   ARG A 273      -5.247  17.552  41.907  1.00 95.30           N  
ANISOU 2075  N   ARG A 273    12451  12220  11540    388   -144  -1384       N  
ATOM   2076  CA  ARG A 273      -3.905  18.018  41.599  1.00 83.30           C  
ANISOU 2076  CA  ARG A 273    10953  10727   9971    462   -164  -1405       C  
ATOM   2077  C   ARG A 273      -3.018  16.884  41.093  1.00 82.17           C  
ANISOU 2077  C   ARG A 273    10797  10520   9904    494   -235  -1519       C  
ATOM   2078  O   ARG A 273      -2.644  16.835  39.911  1.00105.86           O  
ANISOU 2078  O   ARG A 273    13727  13623  12872    533   -248  -1636       O  
ATOM   2079  CB  ARG A 273      -3.286  18.632  42.837  1.00 85.22           C  
ANISOU 2079  CB  ARG A 273    11285  10916  10178    466   -140  -1303       C  
ATOM   2080  CG  ARG A 273      -1.987  19.317  42.639  1.00 92.50           C  
ANISOU 2080  CG  ARG A 273    12215  11880  11049    520   -157  -1305       C  
ATOM   2081  CD  ARG A 273      -1.640  20.079  43.899  1.00 86.61           C  
ANISOU 2081  CD  ARG A 273    11561  11090  10256    506   -139  -1207       C  
ATOM   2082  NE  ARG A 273      -0.297  20.639  43.897  1.00 85.97           N  
ANISOU 2082  NE  ARG A 273    11488  11031  10144    534   -172  -1200       N  
ATOM   2083  CZ  ARG A 273       0.343  20.953  45.011  1.00 88.74           C  
ANISOU 2083  CZ  ARG A 273    11920  11326  10472    519   -196  -1137       C  
ATOM   2084  NH1 ARG A 273      -0.188  20.705  46.197  1.00 77.07           N  
ANISOU 2084  NH1 ARG A 273    10531   9776   8977    477   -185  -1077       N  
ATOM   2085  NH2 ARG A 273       1.531  21.551  44.937  1.00 80.57           N  
ANISOU 2085  NH2 ARG A 273    10871  10329   9414    530   -230  -1132       N  
ATOM   2086  N   PHE A 274      -2.613  16.001  42.003  1.00 84.22           N  
ANISOU 2086  N   PHE A 274    11126  10615  10260    482   -286  -1488       N  
ATOM   2087  CA  PHE A 274      -1.788  14.842  41.684  1.00101.33           C  
ANISOU 2087  CA  PHE A 274    13284  12671  12547    536   -378  -1602       C  
ATOM   2088  C   PHE A 274      -2.707  13.650  41.441  1.00 96.54           C  
ANISOU 2088  C   PHE A 274    12680  11944  12058    473   -433  -1662       C  
ATOM   2089  O   PHE A 274      -3.646  13.425  42.211  1.00103.45           O  
ANISOU 2089  O   PHE A 274    13606  12746  12954    365   -423  -1544       O  
ATOM   2090  CB  PHE A 274      -0.812  14.522  42.826  1.00100.39           C  
ANISOU 2090  CB  PHE A 274    13243  12407  12492    563   -446  -1516       C  
ATOM   2091  CG  PHE A 274       0.016  15.697  43.261  1.00 94.85           C  
ANISOU 2091  CG  PHE A 274    12549  11808  11681    594   -405  -1443       C  
ATOM   2092  CD1 PHE A 274       1.063  16.149  42.482  1.00 99.42           C  
ANISOU 2092  CD1 PHE A 274    13038  12509  12228    673   -394  -1539       C  
ATOM   2093  CD2 PHE A 274      -0.279  16.371  44.439  1.00 89.10           C  
ANISOU 2093  CD2 PHE A 274    11913  11067  10872    530   -371  -1287       C  
ATOM   2094  CE1 PHE A 274       1.823  17.231  42.877  1.00 96.62           C  
ANISOU 2094  CE1 PHE A 274    12688  12239  11786    675   -368  -1464       C  
ATOM   2095  CE2 PHE A 274       0.480  17.462  44.840  1.00 76.55           C  
ANISOU 2095  CE2 PHE A 274    10340   9554   9191    549   -349  -1236       C  
ATOM   2096  CZ  PHE A 274       1.532  17.890  44.053  1.00 78.16           C  
ANISOU 2096  CZ  PHE A 274    10457   9857   9385    616   -354  -1316       C  
ATOM   2097  N   TRP A 275      -2.458  12.902  40.366  1.00 79.20           N  
ANISOU 2097  N   TRP A 275    10423   9741   9930    526   -486  -1854       N  
ATOM   2098  CA  TRP A 275      -3.223  11.698  40.070  1.00 93.58           C  
ANISOU 2098  CA  TRP A 275    12252  11418  11885    464   -564  -1939       C  
ATOM   2099  C   TRP A 275      -2.589  10.454  40.688  1.00 91.04           C  
ANISOU 2099  C   TRP A 275    12010  10817  11766    493   -697  -1953       C  
ATOM   2100  O   TRP A 275      -2.841   9.334  40.225  1.00 99.66           O  
ANISOU 2100  O   TRP A 275    13106  11752  13007    482   -795  -2086       O  
ATOM   2101  CB  TRP A 275      -3.368  11.527  38.555  1.00105.48           C  
ANISOU 2101  CB  TRP A 275    13663  13061  13354    500   -566  -2166       C  
ATOM   2102  CG  TRP A 275      -4.240  12.568  37.903  1.00 92.06           C  
ANISOU 2102  CG  TRP A 275    11898  11601  11481    448   -483  -2129       C  
ATOM   2103  CD1 TRP A 275      -4.815  13.656  38.500  1.00 93.03           C  
ANISOU 2103  CD1 TRP A 275    12028  11812  11509    403   -406  -1942       C  
ATOM   2104  CD2 TRP A 275      -4.610  12.627  36.523  1.00 80.16           C  
ANISOU 2104  CD2 TRP A 275    10308  10270   9879    445   -486  -2288       C  
ATOM   2105  NE1 TRP A 275      -5.531  14.378  37.576  1.00 81.68           N  
ANISOU 2105  NE1 TRP A 275    10513  10571   9951    384   -378  -1962       N  
ATOM   2106  CE2 TRP A 275      -5.421  13.768  36.354  1.00 93.47           C  
ANISOU 2106  CE2 TRP A 275    11956  12132  11427    398   -429  -2159       C  
ATOM   2107  CE3 TRP A 275      -4.341  11.822  35.413  1.00 85.41           C  
ANISOU 2107  CE3 TRP A 275    10930  10966  10558    480   -540  -2538       C  
ATOM   2108  CZ2 TRP A 275      -5.964  14.121  35.121  1.00111.44           C  
ANISOU 2108  CZ2 TRP A 275    14158  14610  13574    376   -443  -2239       C  
ATOM   2109  CZ3 TRP A 275      -4.880  12.173  34.190  1.00 84.91           C  
ANISOU 2109  CZ3 TRP A 275    10796  11127  10337    445   -534  -2635       C  
ATOM   2110  CH2 TRP A 275      -5.682  13.312  34.053  1.00 94.98           C  
ANISOU 2110  CH2 TRP A 275    12042  12574  11472    389   -494  -2470       C  
ATOM   2111  N   THR A 276      -1.758  10.641  41.717  1.00 95.21           N  
ANISOU 2111  N   THR A 276    12602  11267  12306    532   -722  -1818       N  
ATOM   2112  CA  THR A 276      -0.940   9.550  42.239  1.00107.87           C  
ANISOU 2112  CA  THR A 276    14270  12608  14108    596   -879  -1828       C  
ATOM   2113  C   THR A 276      -1.787   8.416  42.798  1.00106.72           C  
ANISOU 2113  C   THR A 276    14232  12202  14113    461   -989  -1730       C  
ATOM   2114  O   THR A 276      -1.525   7.241  42.515  1.00118.76           O  
ANISOU 2114  O   THR A 276    15781  13491  15851    509  -1137  -1850       O  
ATOM   2115  CB  THR A 276       0.009  10.070  43.321  1.00100.36           C  
ANISOU 2115  CB  THR A 276    13369  11648  13116    640   -898  -1666       C  
ATOM   2116  OG1 THR A 276       0.583  11.319  42.913  1.00 99.13           O  
ANISOU 2116  OG1 THR A 276    13121  11749  12793    707   -778  -1708       O  
ATOM   2117  CG2 THR A 276       1.108   9.055  43.584  1.00 85.99           C  
ANISOU 2117  CG2 THR A 276    11569   9593  11512    765  -1079  -1722       C  
ATOM   2118  N   ASN A 277      -2.798   8.741  43.601  1.00 92.12           N  
ANISOU 2118  N   ASN A 277    12445  10391  12166    285   -921  -1520       N  
ATOM   2119  CA  ASN A 277      -3.570   7.711  44.285  1.00 99.39           C  
ANISOU 2119  CA  ASN A 277    13472  11085  13208    113  -1017  -1378       C  
ATOM   2120  C   ASN A 277      -4.409   6.860  43.339  1.00108.41           C  
ANISOU 2120  C   ASN A 277    14571  12139  14480     45  -1068  -1534       C  
ATOM   2121  O   ASN A 277      -5.025   5.888  43.792  1.00121.09           O  
ANISOU 2121  O   ASN A 277    16264  13526  16220   -115  -1169  -1430       O  
ATOM   2122  CB  ASN A 277      -4.462   8.361  45.342  1.00 96.28           C  
ANISOU 2122  CB  ASN A 277    13121  10821  12640    -67   -895  -1138       C  
ATOM   2123  CG  ASN A 277      -3.662   9.077  46.409  1.00102.24           C  
ANISOU 2123  CG  ASN A 277    13948  11632  13267    -27   -871   -983       C  
ATOM   2124  OD1 ASN A 277      -2.915   8.455  47.165  1.00111.23           O  
ANISOU 2124  OD1 ASN A 277    15198  12576  14490    -18  -1016   -870       O  
ATOM   2125  ND2 ASN A 277      -3.808  10.395  46.471  1.00110.31           N  
ANISOU 2125  ND2 ASN A 277    14910  12910  14092      0   -708   -980       N  
ATOM   2126  N   LEU A 278      -4.445   7.194  42.049  1.00 98.54           N  
ANISOU 2126  N   LEU A 278    13198  11057  13186    143  -1010  -1773       N  
ATOM   2127  CA  LEU A 278      -5.150   6.406  41.046  1.00100.70           C  
ANISOU 2127  CA  LEU A 278    13428  11266  13568     90  -1072  -1963       C  
ATOM   2128  C   LEU A 278      -4.340   5.210  40.558  1.00103.52           C  
ANISOU 2128  C   LEU A 278    13821  11351  14159    213  -1248  -2176       C  
ATOM   2129  O   LEU A 278      -4.819   4.474  39.687  1.00114.64           O  
ANISOU 2129  O   LEU A 278    15205  12680  15673    182  -1319  -2376       O  
ATOM   2130  CB  LEU A 278      -5.521   7.298  39.857  1.00 95.39           C  
ANISOU 2130  CB  LEU A 278    12615  10910  12718    138   -948  -2126       C  
ATOM   2131  CG  LEU A 278      -6.554   8.394  40.127  1.00 94.33           C  
ANISOU 2131  CG  LEU A 278    12421  11020  12400     28   -803  -1961       C  
ATOM   2132  CD1 LEU A 278      -6.813   9.207  38.868  1.00 84.61           C  
ANISOU 2132  CD1 LEU A 278    11066  10068  11016     90   -730  -2114       C  
ATOM   2133  CD2 LEU A 278      -7.851   7.814  40.677  1.00105.98           C  
ANISOU 2133  CD2 LEU A 278    13912  12403  13952   -193   -823  -1829       C  
ATOM   2134  N   TYR A 279      -3.134   5.007  41.098  1.00 95.64           N  
ANISOU 2134  N   TYR A 279    12874  10209  13255    357  -1328  -2151       N  
ATOM   2135  CA  TYR A 279      -2.265   3.922  40.648  1.00101.90           C  
ANISOU 2135  CA  TYR A 279    13679  10742  14297    520  -1500  -2381       C  
ATOM   2136  C   TYR A 279      -2.922   2.561  40.840  1.00104.28           C  
ANISOU 2136  C   TYR A 279    14099  10670  14854    388  -1692  -2364       C  
ATOM   2137  O   TYR A 279      -2.872   1.705  39.948  1.00103.75           O  
ANISOU 2137  O   TYR A 279    14011  10448  14960    459  -1798  -2648       O  
ATOM   2138  CB  TYR A 279      -0.933   3.986  41.399  1.00102.63           C  
ANISOU 2138  CB  TYR A 279    13795  10741  14458    684  -1572  -2303       C  
ATOM   2139  CG  TYR A 279       0.089   2.954  40.971  1.00103.64           C  
ANISOU 2139  CG  TYR A 279    13900  10614  14863    900  -1750  -2559       C  
ATOM   2140  CD1 TYR A 279       0.786   3.087  39.777  1.00106.53           C  
ANISOU 2140  CD1 TYR A 279    14106  11159  15210   1098  -1681  -2914       C  
ATOM   2141  CD2 TYR A 279       0.363   1.850  41.770  1.00106.21           C  
ANISOU 2141  CD2 TYR A 279    14362  10523  15470    908  -1991  -2446       C  
ATOM   2142  CE1 TYR A 279       1.725   2.144  39.389  1.00105.88           C  
ANISOU 2142  CE1 TYR A 279    13979  10859  15393   1318  -1832  -3187       C  
ATOM   2143  CE2 TYR A 279       1.298   0.904  41.390  1.00107.43           C  
ANISOU 2143  CE2 TYR A 279    14486  10417  15916   1136  -2172  -2697       C  
ATOM   2144  CZ  TYR A 279       1.976   1.056  40.199  1.00106.08           C  
ANISOU 2144  CZ  TYR A 279    14133  10442  15731   1351  -2084  -3086       C  
ATOM   2145  OH  TYR A 279       2.907   0.118  39.816  1.00 96.68           O  
ANISOU 2145  OH  TYR A 279    12886   9008  14839   1599  -2252  -3377       O  
ATOM   2146  N   SER A 280      -3.535   2.342  42.009  1.00107.19           N  
ANISOU 2146  N   SER A 280    14595  10890  15242    180  -1740  -2034       N  
ATOM   2147  CA  SER A 280      -4.213   1.080  42.289  1.00110.87           C  
ANISOU 2147  CA  SER A 280    15187  10995  15943      2  -1926  -1959       C  
ATOM   2148  C   SER A 280      -5.173   0.694  41.177  1.00121.98           C  
ANISOU 2148  C   SER A 280    16526  12431  17389    -92  -1918  -2190       C  
ATOM   2149  O   SER A 280      -5.362  -0.496  40.893  1.00124.16           O  
ANISOU 2149  O   SER A 280    16877  12372  17927   -139  -2110  -2306       O  
ATOM   2150  CB  SER A 280      -4.963   1.180  43.621  1.00111.11           C  
ANISOU 2150  CB  SER A 280    15330  11003  15884   -268  -1902  -1553       C  
ATOM   2151  OG  SER A 280      -5.900   2.244  43.602  1.00113.22           O  
ANISOU 2151  OG  SER A 280    15493  11646  15878   -397  -1666  -1475       O  
ATOM   2152  N   LEU A 281      -5.771   1.682  40.522  1.00127.17           N  
ANISOU 2152  N   LEU A 281    17044  13473  17800   -117  -1718  -2265       N  
ATOM   2153  CA  LEU A 281      -6.733   1.425  39.463  1.00121.95           C  
ANISOU 2153  CA  LEU A 281    16306  12890  17141   -217  -1713  -2469       C  
ATOM   2154  C   LEU A 281      -6.079   1.410  38.094  1.00117.03           C  
ANISOU 2154  C   LEU A 281    15589  12373  16506      5  -1715  -2869       C  
ATOM   2155  O   LEU A 281      -6.594   0.770  37.173  1.00121.36           O  
ANISOU 2155  O   LEU A 281    16113  12863  17135    -43  -1794  -3111       O  
ATOM   2156  CB  LEU A 281      -7.829   2.489  39.505  1.00107.97           C  
ANISOU 2156  CB  LEU A 281    14429  11480  15116   -372  -1520  -2318       C  
ATOM   2157  CG  LEU A 281      -8.422   2.762  40.890  1.00124.41           C  
ANISOU 2157  CG  LEU A 281    16569  13565  17139   -573  -1454  -1942       C  
ATOM   2158  CD1 LEU A 281      -9.407   3.919  40.852  1.00121.40           C  
ANISOU 2158  CD1 LEU A 281    16047  13562  16518   -664  -1252  -1852       C  
ATOM   2159  CD2 LEU A 281      -9.097   1.515  41.426  1.00120.93           C  
ANISOU 2159  CD2 LEU A 281    16238  12792  16918   -819  -1614  -1809       C  
ATOM   2160  N   THR A 282      -4.943   2.090  37.944  1.00115.08           N  
ANISOU 2160  N   THR A 282    15283  12294  16149    233  -1628  -2949       N  
ATOM   2161  CA  THR A 282      -4.313   2.257  36.641  1.00114.13           C  
ANISOU 2161  CA  THR A 282    15047  12369  15947    424  -1580  -3313       C  
ATOM   2162  C   THR A 282      -3.028   1.457  36.493  1.00115.81           C  
ANISOU 2162  C   THR A 282    15273  12350  16381    661  -1703  -3553       C  
ATOM   2163  O   THR A 282      -2.311   1.652  35.508  1.00109.22           O  
ANISOU 2163  O   THR A 282    14322  11715  15460    839  -1636  -3859       O  
ATOM   2164  CB  THR A 282      -4.010   3.733  36.387  1.00106.80           C  
ANISOU 2164  CB  THR A 282    14006  11871  14702    491  -1367  -3252       C  
ATOM   2165  OG1 THR A 282      -3.188   4.228  37.450  1.00105.15           O  
ANISOU 2165  OG1 THR A 282    13832  11633  14487    567  -1333  -3027       O  
ATOM   2166  CG2 THR A 282      -5.297   4.555  36.296  1.00 94.15           C  
ANISOU 2166  CG2 THR A 282    12361  10515  12896    300  -1256  -3083       C  
ATOM   2167  N   VAL A 283      -2.722   0.568  37.437  1.00118.69           N  
ANISOU 2167  N   VAL A 283    15765  12309  17024    666  -1886  -3421       N  
ATOM   2168  CA  VAL A 283      -1.425  -0.126  37.412  1.00113.83           C  
ANISOU 2168  CA  VAL A 283    15144  11460  16648    926  -2021  -3629       C  
ATOM   2169  C   VAL A 283      -1.309  -0.932  36.124  1.00114.63           C  
ANISOU 2169  C   VAL A 283    15184  11495  16874   1050  -2089  -4101       C  
ATOM   2170  O   VAL A 283      -2.209  -1.738  35.811  1.00105.82           O  
ANISOU 2170  O   VAL A 283    14148  10167  15891    903  -2209  -4186       O  
ATOM   2171  CB  VAL A 283      -1.262  -1.030  38.649  1.00112.76           C  
ANISOU 2171  CB  VAL A 283    15179  10852  16810    886  -2253  -3375       C  
ATOM   2172  CG1 VAL A 283      -2.521  -1.857  38.895  1.00133.20           C  
ANISOU 2172  CG1 VAL A 283    17911  13160  19537    610  -2385  -3239       C  
ATOM   2173  CG2 VAL A 283      -0.027  -1.931  38.512  1.00104.96           C  
ANISOU 2173  CG2 VAL A 283    14180   9561  16141   1174  -2445  -3634       C  
ATOM   2174  N   PRO A 284      -0.244  -0.749  35.339  1.00110.17           N  
ANISOU 2174  N   PRO A 284    14472  11122  16264   1303  -2013  -4430       N  
ATOM   2175  CA  PRO A 284      -0.160  -1.448  34.046  1.00 98.08           C  
ANISOU 2175  CA  PRO A 284    12873   9593  14801   1417  -2048  -4922       C  
ATOM   2176  C   PRO A 284      -0.116  -2.960  34.175  1.00100.12           C  
ANISOU 2176  C   PRO A 284    13248   9303  15489   1485  -2330  -5104       C  
ATOM   2177  O   PRO A 284      -0.824  -3.662  33.445  1.00116.48           O  
ANISOU 2177  O   PRO A 284    15364  11254  17639   1401  -2416  -5350       O  
ATOM   2178  CB  PRO A 284       1.136  -0.884  33.447  1.00 98.91           C  
ANISOU 2178  CB  PRO A 284    12783  10027  14771   1676  -1894  -5178       C  
ATOM   2179  CG  PRO A 284       1.277   0.463  34.099  1.00106.35           C  
ANISOU 2179  CG  PRO A 284    13687  11279  15440   1598  -1718  -4799       C  
ATOM   2180  CD  PRO A 284       0.850   0.216  35.513  1.00109.97           C  
ANISOU 2180  CD  PRO A 284    14319  11390  16074   1465  -1862  -4381       C  
ATOM   2181  N   PHE A 285       0.706  -3.485  35.082  1.00108.01           N  
ANISOU 2181  N   PHE A 285    14304   9952  16782   1634  -2498  -4991       N  
ATOM   2182  CA  PHE A 285       0.830  -4.926  35.303  1.00118.20           C  
ANISOU 2182  CA  PHE A 285    15723  10661  18526   1716  -2805  -5129       C  
ATOM   2183  C   PHE A 285       0.669  -5.160  36.804  1.00133.25           C  
ANISOU 2183  C   PHE A 285    17812  12213  20604   1576  -2979  -4619       C  
ATOM   2184  O   PHE A 285       1.644  -5.095  37.556  1.00136.86           O  
ANISOU 2184  O   PHE A 285    18257  12570  21175   1746  -3052  -4480       O  
ATOM   2185  CB  PHE A 285       2.159  -5.445  34.767  1.00121.26           C  
ANISOU 2185  CB  PHE A 285    15972  10964  19137   2098  -2870  -5574       C  
ATOM   2186  CG  PHE A 285       2.426  -5.062  33.336  1.00120.66           C  
ANISOU 2186  CG  PHE A 285    15695  11335  18814   2226  -2651  -6057       C  
ATOM   2187  CD1 PHE A 285       1.919  -5.819  32.291  1.00125.70           C  
ANISOU 2187  CD1 PHE A 285    16352  11886  19523   2217  -2712  -6478       C  
ATOM   2188  CD2 PHE A 285       3.164  -3.929  33.037  1.00119.99           C  
ANISOU 2188  CD2 PHE A 285    15411  11771  18408   2327  -2387  -6080       C  
ATOM   2189  CE1 PHE A 285       2.161  -5.460  30.974  1.00128.47           C  
ANISOU 2189  CE1 PHE A 285    16518  12713  19582   2301  -2493  -6871       C  
ATOM   2190  CE2 PHE A 285       3.406  -3.564  31.728  1.00119.47           C  
ANISOU 2190  CE2 PHE A 285    15167  12145  18080   2411  -2181  -6492       C  
ATOM   2191  CZ  PHE A 285       2.905  -4.330  30.694  1.00127.52           C  
ANISOU 2191  CZ  PHE A 285    16208  13098  19147   2407  -2237  -6913       C  
ATOM   2192  N   GLY A 286      -0.565  -5.444  37.225  1.00136.50           N  
ANISOU 2192  N   GLY A 286    18386  12455  21022   1252  -3050  -4344       N  
ATOM   2193  CA  GLY A 286      -0.885  -5.413  38.642  1.00129.86           C  
ANISOU 2193  CA  GLY A 286    17707  11422  20214   1047  -3140  -3811       C  
ATOM   2194  C   GLY A 286      -0.167  -6.468  39.465  1.00130.28           C  
ANISOU 2194  C   GLY A 286    17904  10919  20678   1168  -3465  -3704       C  
ATOM   2195  O   GLY A 286       0.194  -6.223  40.619  1.00127.33           O  
ANISOU 2195  O   GLY A 286    17608  10483  20289   1135  -3520  -3318       O  
ATOM   2196  N   GLN A 287       0.043  -7.655  38.893  1.00132.33           N  
ANISOU 2196  N   GLN A 287    18209  10760  21311   1310  -3702  -4044       N  
ATOM   2197  CA  GLN A 287       0.600  -8.757  39.674  1.00146.10           C  
ANISOU 2197  CA  GLN A 287    20116  11900  23494   1407  -4063  -3920       C  
ATOM   2198  C   GLN A 287       2.042  -8.487  40.087  1.00148.28           C  
ANISOU 2198  C   GLN A 287    20284  12207  23850   1750  -4102  -3939       C  
ATOM   2199  O   GLN A 287       2.447  -8.832  41.203  1.00153.23           O  
ANISOU 2199  O   GLN A 287    21045  12515  24660   1749  -4329  -3588       O  
ATOM   2200  CB  GLN A 287       0.497 -10.064  38.889  1.00151.86           C  
ANISOU 2200  CB  GLN A 287    20912  12159  24628   1504  -4314  -4331       C  
ATOM   2201  CG  GLN A 287      -0.928 -10.456  38.545  1.00155.75           C  
ANISOU 2201  CG  GLN A 287    21523  12563  25092   1141  -4327  -4298       C  
ATOM   2202  CD  GLN A 287      -1.771 -10.697  39.783  1.00165.11           C  
ANISOU 2202  CD  GLN A 287    22931  13498  26304    752  -4458  -3702       C  
ATOM   2203  OE1 GLN A 287      -1.297 -11.260  40.770  1.00171.84           O  
ANISOU 2203  OE1 GLN A 287    23940  13941  27412    773  -4715  -3407       O  
ATOM   2204  NE2 GLN A 287      -3.027 -10.267  39.739  1.00174.57           N  
ANISOU 2204  NE2 GLN A 287    24135  14962  27231    390  -4284  -3517       N  
ATOM   2205  N   LYS A 288       2.830  -7.876  39.212  1.00135.46           N  
ANISOU 2205  N   LYS A 288    18412  10973  22082   2029  -3893  -4330       N  
ATOM   2206  CA  LYS A 288       4.225  -7.606  39.541  1.00134.66           C  
ANISOU 2206  CA  LYS A 288    18166  10935  22063   2353  -3921  -4378       C  
ATOM   2207  C   LYS A 288       4.314  -6.461  40.544  1.00139.46           C  
ANISOU 2207  C   LYS A 288    18776  11875  22338   2206  -3766  -3903       C  
ATOM   2208  O   LYS A 288       3.774  -5.377  40.292  1.00130.43           O  
ANISOU 2208  O   LYS A 288    17562  11214  20783   2034  -3460  -3826       O  
ATOM   2209  CB  LYS A 288       5.020  -7.283  38.279  1.00117.68           C  
ANISOU 2209  CB  LYS A 288    15732   9146  19836   2661  -3719  -4942       C  
ATOM   2210  CG  LYS A 288       5.311  -8.506  37.422  1.00119.95           C  
ANISOU 2210  CG  LYS A 288    15963   9172  20438   2863  -3868  -5380       C  
ATOM   2211  CD  LYS A 288       6.244  -8.179  36.269  1.00141.76           C  
ANISOU 2211  CD  LYS A 288    18406  12408  23050   3138  -3626  -5856       C  
ATOM   2212  CE  LYS A 288       6.673  -9.444  35.538  1.00149.45           C  
ANISOU 2212  CE  LYS A 288    19296  13195  24294   3325  -3756  -6205       C  
ATOM   2213  NZ  LYS A 288       7.474  -9.151  34.317  1.00153.46           N  
ANISOU 2213  NZ  LYS A 288    19495  14197  24617   3546  -3499  -6681       N  
ATOM   2214  N   PRO A 289       4.979  -6.654  41.678  1.00139.31           N  
ANISOU 2214  N   PRO A 289    18839  11608  22485   2271  -3982  -3588       N  
ATOM   2215  CA  PRO A 289       4.993  -5.628  42.723  1.00130.24           C  
ANISOU 2215  CA  PRO A 289    17725  10743  21017   2102  -3860  -3129       C  
ATOM   2216  C   PRO A 289       6.042  -4.557  42.451  1.00129.63           C  
ANISOU 2216  C   PRO A 289    17388  11136  20729   2325  -3640  -3286       C  
ATOM   2217  O   PRO A 289       6.926  -4.703  41.605  1.00132.54           O  
ANISOU 2217  O   PRO A 289    17543  11580  21237   2634  -3617  -3715       O  
ATOM   2218  CB  PRO A 289       5.337  -6.433  43.977  1.00117.46           C  
ANISOU 2218  CB  PRO A 289    16310   8627  19693   2091  -4232  -2760       C  
ATOM   2219  CG  PRO A 289       6.260  -7.490  43.460  1.00124.97           C  
ANISOU 2219  CG  PRO A 289    17181   9182  21120   2461  -4500  -3143       C  
ATOM   2220  CD  PRO A 289       5.750  -7.847  42.075  1.00117.11           C  
ANISOU 2220  CD  PRO A 289    16101   8223  20173   2507  -4375  -3636       C  
ATOM   2221  N   ASN A 290       5.926  -3.463  43.198  1.00133.76           N  
ANISOU 2221  N   ASN A 290    17930  11986  20908   2150  -3475  -2934       N  
ATOM   2222  CA  ASN A 290       6.903  -2.390  43.119  1.00134.93           C  
ANISOU 2222  CA  ASN A 290    17858  12556  20852   2310  -3290  -3007       C  
ATOM   2223  C   ASN A 290       8.130  -2.719  43.963  1.00136.72           C  
ANISOU 2223  C   ASN A 290    18054  12564  21328   2528  -3552  -2895       C  
ATOM   2224  O   ASN A 290       8.092  -3.555  44.871  1.00143.43           O  
ANISOU 2224  O   ASN A 290    19102  12976  22420   2489  -3862  -2628       O  
ATOM   2225  CB  ASN A 290       6.295  -1.063  43.575  1.00131.08           C  
ANISOU 2225  CB  ASN A 290    17406  12482  19916   2044  -3026  -2700       C  
ATOM   2226  CG  ASN A 290       5.914  -0.166  42.414  1.00142.87           C  
ANISOU 2226  CG  ASN A 290    18739  14433  21114   2010  -2691  -2956       C  
ATOM   2227  OD1 ASN A 290       6.588  -0.147  41.383  1.00149.70           O  
ANISOU 2227  OD1 ASN A 290    19396  15463  22021   2229  -2605  -3345       O  
ATOM   2228  ND2 ASN A 290       4.837   0.593  42.579  1.00126.79           N  
ANISOU 2228  ND2 ASN A 290    16789  12615  18769   1736  -2505  -2736       N  
ATOM   2229  N   ILE A 291       9.230  -2.042  43.650  1.00130.11           N  
ANISOU 2229  N   ILE A 291    16962  12048  20427   2749  -3432  -3090       N  
ATOM   2230  CA  ILE A 291      10.497  -2.249  44.344  1.00128.60           C  
ANISOU 2230  CA  ILE A 291    16679  11718  20466   2984  -3666  -3029       C  
ATOM   2231  C   ILE A 291      10.411  -1.546  45.695  1.00128.96           C  
ANISOU 2231  C   ILE A 291    16881  11842  20277   2762  -3704  -2519       C  
ATOM   2232  O   ILE A 291      10.410  -0.315  45.763  1.00125.20           O  
ANISOU 2232  O   ILE A 291    16331  11799  19440   2640  -3447  -2429       O  
ATOM   2233  CB  ILE A 291      11.678  -1.724  43.521  1.00124.09           C  
ANISOU 2233  CB  ILE A 291    15749  11510  19888   3266  -3502  -3419       C  
ATOM   2234  CG1 ILE A 291      11.870  -2.564  42.258  1.00129.44           C  
ANISOU 2234  CG1 ILE A 291    16268  12086  20826   3516  -3496  -3956       C  
ATOM   2235  CG2 ILE A 291      12.953  -1.739  44.348  1.00133.58           C  
ANISOU 2235  CG2 ILE A 291    16833  12638  21282   3472  -3726  -3306       C  
ATOM   2236  CD1 ILE A 291      13.073  -2.148  41.439  1.00133.27           C  
ANISOU 2236  CD1 ILE A 291    16378  12945  21315   3797  -3331  -4364       C  
ATOM   2237  N   ASP A 292      10.335  -2.325  46.773  1.00127.83           N  
ANISOU 2237  N   ASP A 292    16964  11273  20331   2700  -4036  -2185       N  
ATOM   2238  CA  ASP A 292      10.265  -1.786  48.131  1.00129.74           C  
ANISOU 2238  CA  ASP A 292    17379  11568  20348   2482  -4107  -1698       C  
ATOM   2239  C   ASP A 292      11.380  -2.417  48.961  1.00146.51           C  
ANISOU 2239  C   ASP A 292    19502  13382  22782   2691  -4497  -1560       C  
ATOM   2240  O   ASP A 292      11.272  -3.572  49.384  1.00160.50           O  
ANISOU 2240  O   ASP A 292    21453  14657  24872   2713  -4835  -1421       O  
ATOM   2241  CB  ASP A 292       8.899  -2.037  48.758  1.00131.75           C  
ANISOU 2241  CB  ASP A 292    17946  11664  20451   2116  -4116  -1342       C  
ATOM   2242  CG  ASP A 292       8.680  -1.221  50.017  1.00120.82           C  
ANISOU 2242  CG  ASP A 292    16712  10479  18716   1856  -4075   -898       C  
ATOM   2243  OD1 ASP A 292       8.628   0.024  49.917  1.00105.17           O  
ANISOU 2243  OD1 ASP A 292    14625   8947  16387   1782  -3776   -924       O  
ATOM   2244  OD2 ASP A 292       8.562  -1.823  51.104  1.00120.35           O1-
ANISOU 2244  OD2 ASP A 292    16883  10123  18722   1720  -4348   -526       O1-
ATOM   2245  N   VAL A 293      12.440  -1.649  49.205  1.00150.23           N  
ANISOU 2245  N   VAL A 293    19773  14139  23168   2832  -4466  -1582       N  
ATOM   2246  CA  VAL A 293      13.605  -2.135  49.936  1.00152.94           C  
ANISOU 2246  CA  VAL A 293    20061  14248  23802   3058  -4835  -1477       C  
ATOM   2247  C   VAL A 293      13.420  -1.907  51.430  1.00144.37           C  
ANISOU 2247  C   VAL A 293    19239  13104  22508   2800  -5016   -935       C  
ATOM   2248  O   VAL A 293      14.362  -2.079  52.213  1.00137.59           O  
ANISOU 2248  O   VAL A 293    18354  12129  21795   2931  -5316   -770       O  
ATOM   2249  CB  VAL A 293      14.893  -1.457  49.435  1.00151.66           C  
ANISOU 2249  CB  VAL A 293    19518  14438  23668   3335  -4725  -1788       C  
ATOM   2250  CG1 VAL A 293      15.097  -1.740  47.957  1.00151.20           C  
ANISOU 2250  CG1 VAL A 293    19196  14461  23794   3583  -4542  -2337       C  
ATOM   2251  CG2 VAL A 293      14.835   0.042  49.690  1.00146.37           C  
ANISOU 2251  CG2 VAL A 293    18802  14290  22520   3116  -4416  -1652       C  
ATOM   2252  N   THR A 294      12.208  -1.517  51.835  1.00140.22           N  
ANISOU 2252  N   THR A 294    18961  12683  21635   2433  -4836   -664       N  
ATOM   2253  CA  THR A 294      11.932  -1.300  53.253  1.00140.49           C  
ANISOU 2253  CA  THR A 294    19256  12701  21421   2156  -4975   -162       C  
ATOM   2254  C   THR A 294      12.176  -2.568  54.061  1.00146.41           C  
ANISOU 2254  C   THR A 294    20212  12917  22500   2191  -5457    124       C  
ATOM   2255  O   THR A 294      12.796  -2.523  55.131  1.00141.80           O  
ANISOU 2255  O   THR A 294    19710  12291  21876   2173  -5717    432       O  
ATOM   2256  CB  THR A 294      10.495  -0.815  53.446  1.00132.59           C  
ANISOU 2256  CB  THR A 294    18463  11883  20034   1770  -4689     30       C  
ATOM   2257  OG1 THR A 294      10.330   0.464  52.822  1.00144.28           O  
ANISOU 2257  OG1 THR A 294    19765  13853  21201   1740  -4279   -189       O  
ATOM   2258  CG2 THR A 294      10.161  -0.699  54.929  1.00129.96           C  
ANISOU 2258  CG2 THR A 294    18410  11536  19434   1470  -4829    536       C  
ATOM   2259  N   ASP A 295      11.702  -3.710  53.561  1.00149.35           N  
ANISOU 2259  N   ASP A 295    20677  12866  23205   2237  -5603     32       N  
ATOM   2260  CA  ASP A 295      11.932  -4.971  54.255  1.00153.06           C  
ANISOU 2260  CA  ASP A 295    21351  12768  24036   2279  -6093    302       C  
ATOM   2261  C   ASP A 295      13.420  -5.291  54.331  1.00154.86           C  
ANISOU 2261  C   ASP A 295    21372  12839  24630   2684  -6419    169       C  
ATOM   2262  O   ASP A 295      13.892  -5.853  55.326  1.00136.03           O  
ANISOU 2262  O   ASP A 295    19141  10147  22398   2694  -6836    517       O  
ATOM   2263  CB  ASP A 295      11.172  -6.097  53.555  1.00158.43           C  
ANISOU 2263  CB  ASP A 295    22144  13015  25037   2270  -6176    159       C  
ATOM   2264  CG  ASP A 295       9.734  -6.204  54.020  1.00169.75           C  
ANISOU 2264  CG  ASP A 295    23884  14414  26198   1808  -6068    508       C  
ATOM   2265  OD1 ASP A 295       9.408  -5.637  55.084  1.00164.81           O  
ANISOU 2265  OD1 ASP A 295    23425  14005  25189   1509  -6023    921       O  
ATOM   2266  OD2 ASP A 295       8.929  -6.852  53.318  1.00177.93           O1-
ANISOU 2266  OD2 ASP A 295    24981  15225  27398   1738  -6024    354       O1-
ATOM   2267  N   ALA A 296      14.177  -4.928  53.293  1.00160.46           N  
ANISOU 2267  N   ALA A 296    21720  13774  25475   3014  -6238   -328       N  
ATOM   2268  CA  ALA A 296      15.613  -5.185  53.298  1.00162.25           C  
ANISOU 2268  CA  ALA A 296    21688  13904  26057   3415  -6516   -501       C  
ATOM   2269  C   ALA A 296      16.343  -4.302  54.301  1.00159.23           C  
ANISOU 2269  C   ALA A 296    21260  13832  25407   3352  -6577   -219       C  
ATOM   2270  O   ALA A 296      17.357  -4.722  54.869  1.00145.69           O  
ANISOU 2270  O   ALA A 296    19473  11912  23970   3575  -6966   -118       O  
ATOM   2271  CB  ALA A 296      16.188  -4.982  51.898  1.00165.46           C  
ANISOU 2271  CB  ALA A 296    21698  14536  26631   3749  -6259  -1119       C  
ATOM   2272  N   MET A 297      15.852  -3.081  54.528  1.00157.60           N  
ANISOU 2272  N   MET A 297    21092  14110  24679   3061  -6217   -100       N  
ATOM   2273  CA  MET A 297      16.492  -2.196  55.496  1.00157.95           C  
ANISOU 2273  CA  MET A 297    21115  14456  24445   2973  -6269    153       C  
ATOM   2274  C   MET A 297      16.312  -2.715  56.917  1.00161.52           C  
ANISOU 2274  C   MET A 297    21914  14618  24837   2761  -6658    704       C  
ATOM   2275  O   MET A 297      17.264  -2.736  57.707  1.00150.65           O  
ANISOU 2275  O   MET A 297    20499  13203  23539   2868  -6984    889       O  
ATOM   2276  CB  MET A 297      15.934  -0.777  55.365  1.00142.40           C  
ANISOU 2276  CB  MET A 297    19122  13035  21948   2712  -5793    123       C  
ATOM   2277  CG  MET A 297      16.265  -0.093  54.049  1.00136.99           C  
ANISOU 2277  CG  MET A 297    18084  12699  21266   2896  -5424   -371       C  
ATOM   2278  SD  MET A 297      15.346   1.439  53.798  1.00144.70           S  
ANISOU 2278  SD  MET A 297    19095  14217  21667   2569  -4889   -382       S  
ATOM   2279  CE  MET A 297      15.936   2.419  55.176  1.00141.37           C  
ANISOU 2279  CE  MET A 297    18742  14052  20920   2402  -4997    -36       C  
ATOM   2280  N   VAL A 298      15.094  -3.141  57.260  1.00155.91           N  
ANISOU 2280  N   VAL A 298    21541  13720  23978   2444  -6634    982       N  
ATOM   2281  CA  VAL A 298      14.843  -3.681  58.594  1.00146.60           C  
ANISOU 2281  CA  VAL A 298    20713  12279  22708   2196  -6991   1533       C  
ATOM   2282  C   VAL A 298      15.617  -4.977  58.799  1.00149.24           C  
ANISOU 2282  C   VAL A 298    21071  12043  23589   2472  -7545   1620       C  
ATOM   2283  O   VAL A 298      16.101  -5.261  59.902  1.00139.55           O  
ANISOU 2283  O   VAL A 298    20002  10658  22363   2423  -7941   2017       O  
ATOM   2284  CB  VAL A 298      13.331  -3.880  58.812  1.00134.88           C  
ANISOU 2284  CB  VAL A 298    19550  10741  20958   1782  -6812   1782       C  
ATOM   2285  CG1 VAL A 298      13.056  -4.422  60.207  1.00125.84           C  
ANISOU 2285  CG1 VAL A 298    18773   9367  19674   1484  -7161   2374       C  
ATOM   2286  CG2 VAL A 298      12.588  -2.572  58.590  1.00132.96           C  
ANISOU 2286  CG2 VAL A 298    19255  11055  20209   1550  -6278   1668       C  
ATOM   2287  N   ASP A 299      15.758  -5.777  57.738  1.00173.99           N  
ANISOU 2287  N   ASP A 299    24049  14858  27199   2776  -7596   1242       N  
ATOM   2288  CA  ASP A 299      16.471  -7.047  57.853  1.00179.21           C  
ANISOU 2288  CA  ASP A 299    24665  15132  28297   2969  -7962   1217       C  
ATOM   2289  C   ASP A 299      17.935  -6.842  58.217  1.00166.52           C  
ANISOU 2289  C   ASP A 299    22785  13671  26813   3241  -8164   1149       C  
ATOM   2290  O   ASP A 299      18.529  -7.686  58.897  1.00158.32           O  
ANISOU 2290  O   ASP A 299    21796  12387  25970   3271  -8519   1341       O  
ATOM   2291  CB  ASP A 299      16.357  -7.836  56.548  1.00182.85           C  
ANISOU 2291  CB  ASP A 299    24953  15374  29149   3207  -7856    725       C  
ATOM   2292  CG  ASP A 299      14.979  -8.437  56.348  1.00193.51           C  
ANISOU 2292  CG  ASP A 299    26599  16460  30464   2915  -7778    846       C  
ATOM   2293  OD1 ASP A 299      14.152  -8.357  57.280  1.00195.10           O  
ANISOU 2293  OD1 ASP A 299    27138  16625  30366   2523  -7829   1337       O  
ATOM   2294  OD2 ASP A 299      14.722  -8.987  55.256  1.00203.21           O1-
ANISOU 2294  OD2 ASP A 299    27715  17547  31950   3061  -7658    445       O1-
ATOM   2295  N   GLN A 300      18.532  -5.735  57.780  1.00154.86           N  
ANISOU 2295  N   GLN A 300    21013  12595  25232   3430  -7952    881       N  
ATOM   2296  CA  GLN A 300      19.923  -5.427  58.076  1.00159.83           C  
ANISOU 2296  CA  GLN A 300    21346  13418  25962   3671  -8110    795       C  
ATOM   2297  C   GLN A 300      20.073  -4.471  59.255  1.00164.99           C  
ANISOU 2297  C   GLN A 300    22135  14358  26196   3440  -8196   1210       C  
ATOM   2298  O   GLN A 300      21.187  -4.016  59.532  1.00156.62           O  
ANISOU 2298  O   GLN A 300    20824  13523  25162   3602  -8303   1150       O  
ATOM   2299  CB  GLN A 300      20.606  -4.862  56.829  1.00159.38           C  
ANISOU 2299  CB  GLN A 300    20832  13656  26071   4020  -7828    213       C  
ATOM   2300  CG  GLN A 300      20.524  -5.800  55.629  1.00162.08           C  
ANISOU 2300  CG  GLN A 300    21024  13769  26792   4248  -7726   -242       C  
ATOM   2301  CD  GLN A 300      21.038  -5.175  54.347  1.00157.40           C  
ANISOU 2301  CD  GLN A 300    20001  13533  26272   4532  -7378   -816       C  
ATOM   2302  OE1 GLN A 300      21.818  -4.224  54.374  1.00162.46           O  
ANISOU 2302  OE1 GLN A 300    20371  14560  26798   4633  -7287   -907       O  
ATOM   2303  NE2 GLN A 300      20.599  -5.709  53.212  1.00148.37           N  
ANISOU 2303  NE2 GLN A 300    18789  12285  25300   4637  -7178  -1207       N  
ATOM   2304  N   ALA A 301      18.973  -4.158  59.947  1.00167.04           N  
ANISOU 2304  N   ALA A 301    22779  14634  26056   3051  -8143   1616       N  
ATOM   2305  CA  ALA A 301      18.997  -3.407  61.206  1.00158.93           C  
ANISOU 2305  CA  ALA A 301    21949  13865  24573   2763  -8238   2049       C  
ATOM   2306  C   ALA A 301      19.540  -1.991  61.019  1.00149.37           C  
ANISOU 2306  C   ALA A 301    20455  13246  23052   2774  -7898   1805       C  
ATOM   2307  O   ALA A 301      20.245  -1.458  61.879  1.00150.37           O  
ANISOU 2307  O   ALA A 301    20560  13575  22998   2730  -8080   1999       O  
ATOM   2308  CB  ALA A 301      19.790  -4.154  62.282  1.00145.34           C  
ANISOU 2308  CB  ALA A 301    20302  11962  22957   2742  -8660   2351       C  
ATOM   2309  N   TRP A 302      19.202  -1.375  59.891  1.00137.42           N  
ANISOU 2309  N   TRP A 302    18733  12008  21472   2818  -7417   1388       N  
ATOM   2310  CA  TRP A 302      19.572   0.013  59.652  1.00141.79           C  
ANISOU 2310  CA  TRP A 302    19051  13112  21712   2779  -7064   1173       C  
ATOM   2311  C   TRP A 302      18.813   0.930  60.605  1.00141.38           C  
ANISOU 2311  C   TRP A 302    19289  13362  21067   2349  -6884   1498       C  
ATOM   2312  O   TRP A 302      17.626   0.723  60.873  1.00150.36           O  
ANISOU 2312  O   TRP A 302    20736  14413  21980   2066  -6764   1710       O  
ATOM   2313  CB  TRP A 302      19.260   0.398  58.205  1.00149.46           C  
ANISOU 2313  CB  TRP A 302    19776  14281  22732   2892  -6602    692       C  
ATOM   2314  CG  TRP A 302      20.253  -0.108  57.199  1.00151.32           C  
ANISOU 2314  CG  TRP A 302    19620  14413  23462   3328  -6684    268       C  
ATOM   2315  CD1 TRP A 302      20.987  -1.256  57.276  1.00148.09           C  
ANISOU 2315  CD1 TRP A 302    19127  13582  23558   3644  -7124    252       C  
ATOM   2316  CD2 TRP A 302      20.587   0.498  55.944  1.00146.25           C  
ANISOU 2316  CD2 TRP A 302    18613  14099  22857   3496  -6308   -214       C  
ATOM   2317  NE1 TRP A 302      21.774  -1.391  56.157  1.00148.54           N  
ANISOU 2317  NE1 TRP A 302    18770  13705  23965   4014  -7031   -242       N  
ATOM   2318  CE2 TRP A 302      21.545  -0.328  55.323  1.00147.98           C  
ANISOU 2318  CE2 TRP A 302    18523  14108  23596   3915  -6525   -526       C  
ATOM   2319  CE3 TRP A 302      20.176   1.663  55.289  1.00138.19           C  
ANISOU 2319  CE3 TRP A 302    17497  13530  21478   3331  -5821   -407       C  
ATOM   2320  CZ2 TRP A 302      22.098  -0.027  54.080  1.00144.99           C  
ANISOU 2320  CZ2 TRP A 302    17738  13996  23354   4153  -6242  -1028       C  
ATOM   2321  CZ3 TRP A 302      20.727   1.961  54.054  1.00138.53           C  
ANISOU 2321  CZ3 TRP A 302    17159  13816  21660   3554  -5564   -868       C  
ATOM   2322  CH2 TRP A 302      21.677   1.119  53.463  1.00141.32           C  
ANISOU 2322  CH2 TRP A 302    17203  13991  22499   3951  -5762  -1177       C  
ATOM   2323  N   ASP A 303      19.499   1.942  61.126  1.00128.15           N  
ANISOU 2323  N   ASP A 303    17503  12046  19141   2297  -6866   1524       N  
ATOM   2324  CA  ASP A 303      18.850   2.984  61.908  1.00133.95           C  
ANISOU 2324  CA  ASP A 303    18463  13124  19307   1921  -6641   1731       C  
ATOM   2325  C   ASP A 303      18.880   4.296  61.130  1.00135.23           C  
ANISOU 2325  C   ASP A 303    18385  13725  19270   1911  -6181   1379       C  
ATOM   2326  O   ASP A 303      19.337   4.357  59.985  1.00136.43           O  
ANISOU 2326  O   ASP A 303    18216  13928  19692   2163  -6025   1005       O  
ATOM   2327  CB  ASP A 303      19.498   3.135  63.290  1.00143.12           C  
ANISOU 2327  CB  ASP A 303    19763  14339  20278   1804  -7014   2088       C  
ATOM   2328  CG  ASP A 303      20.992   3.409  63.223  1.00145.44           C  
ANISOU 2328  CG  ASP A 303    19705  14740  20815   2083  -7242   1922       C  
ATOM   2329  OD1 ASP A 303      21.527   3.624  62.116  1.00144.94           O  
ANISOU 2329  OD1 ASP A 303    19278  14773  21021   2343  -7058   1519       O  
ATOM   2330  OD2 ASP A 303      21.633   3.421  64.295  1.00137.26           O1-
ANISOU 2330  OD2 ASP A 303    18751  13718  19685   2027  -7607   2200       O1-
ATOM   2331  N   ALA A 304      18.381   5.355  61.771  1.00135.16           N  
ANISOU 2331  N   ALA A 304    18542  14036  18776   1609  -5968   1503       N  
ATOM   2332  CA  ALA A 304      18.319   6.655  61.110  1.00137.77           C  
ANISOU 2332  CA  ALA A 304    18692  14754  18900   1564  -5548   1211       C  
ATOM   2333  C   ALA A 304      19.707   7.155  60.735  1.00125.63           C  
ANISOU 2333  C   ALA A 304    16783  13393  17559   1791  -5628    978       C  
ATOM   2334  O   ALA A 304      19.892   7.754  59.669  1.00121.18           O  
ANISOU 2334  O   ALA A 304    15954  13027  17062   1893  -5331    648       O  
ATOM   2335  CB  ALA A 304      17.609   7.667  62.007  1.00140.58           C  
ANISOU 2335  CB  ALA A 304    19304  15383  18726   1217  -5365   1390       C  
ATOM   2336  N   GLN A 305      20.701   6.913  61.593  1.00114.65           N  
ANISOU 2336  N   GLN A 305    15359  11946  16258   1860  -6035   1156       N  
ATOM   2337  CA  GLN A 305      22.038   7.422  61.313  1.00127.90           C  
ANISOU 2337  CA  GLN A 305    16660  13822  18114   2051  -6120    946       C  
ATOM   2338  C   GLN A 305      22.688   6.692  60.144  1.00126.40           C  
ANISOU 2338  C   GLN A 305    16111  13490  18427   2420  -6143    630       C  
ATOM   2339  O   GLN A 305      23.466   7.297  59.399  1.00132.60           O  
ANISOU 2339  O   GLN A 305    16534  14527  19321   2552  -5987    332       O  
ATOM   2340  CB  GLN A 305      22.917   7.328  62.560  1.00124.77           C  
ANISOU 2340  CB  GLN A 305    16313  13407  17686   2028  -6576   1223       C  
ATOM   2341  CG  GLN A 305      24.138   8.236  62.504  1.00113.03           C  
ANISOU 2341  CG  GLN A 305    14485  12233  16228   2098  -6608   1046       C  
ATOM   2342  CD  GLN A 305      25.245   7.787  63.432  1.00133.62           C  
ANISOU 2342  CD  GLN A 305    17019  14751  19000   2209  -7138   1250       C  
ATOM   2343  OE1 GLN A 305      26.381   7.577  63.005  1.00142.39           O  
ANISOU 2343  OE1 GLN A 305    17740  15878  20484   2486  -7310   1064       O  
ATOM   2344  NE2 GLN A 305      24.923   7.640  64.711  1.00149.27           N  
ANISOU 2344  NE2 GLN A 305    19362  16658  20695   1988  -7403   1632       N  
ATOM   2345  N   ARG A 306      22.388   5.402  59.963  1.00128.65           N  
ANISOU 2345  N   ARG A 306    16483  13378  19019   2582  -6333    679       N  
ATOM   2346  CA  ARG A 306      22.876   4.702  58.780  1.00136.36           C  
ANISOU 2346  CA  ARG A 306    17132  14219  20461   2936  -6313    324       C  
ATOM   2347  C   ARG A 306      22.263   5.277  57.510  1.00125.32           C  
ANISOU 2347  C   ARG A 306    15614  13045  18958   2904  -5801    -14       C  
ATOM   2348  O   ARG A 306      22.926   5.350  56.468  1.00117.56           O  
ANISOU 2348  O   ARG A 306    14259  12202  18206   3135  -5658   -380       O  
ATOM   2349  CB  ARG A 306      22.581   3.205  58.880  1.00141.80           C  
ANISOU 2349  CB  ARG A 306    17985  14393  21498   3095  -6633    448       C  
ATOM   2350  CG  ARG A 306      22.940   2.450  57.611  1.00139.10           C  
ANISOU 2350  CG  ARG A 306    17334  13891  21625   3459  -6584     36       C  
ATOM   2351  CD  ARG A 306      24.442   2.449  57.386  1.00139.07           C  
ANISOU 2351  CD  ARG A 306    16881  14000  21961   3790  -6778   -198       C  
ATOM   2352  NE  ARG A 306      24.813   1.788  56.139  1.00141.81           N  
ANISOU 2352  NE  ARG A 306    16900  14249  22733   4145  -6692   -645       N  
ATOM   2353  CZ  ARG A 306      24.954   0.478  55.991  1.00145.62           C  
ANISOU 2353  CZ  ARG A 306    17378  14274  23678   4434  -7004   -707       C  
ATOM   2354  NH1 ARG A 306      24.734  -0.359  56.991  1.00145.96           N  
ANISOU 2354  NH1 ARG A 306    17738  13885  23834   4399  -7440   -317       N  
ATOM   2355  NH2 ARG A 306      25.324  -0.004  54.808  1.00142.10           N  
ANISOU 2355  NH2 ARG A 306    16605  13800  23586   4758  -6882  -1175       N  
ATOM   2356  N   ILE A 307      20.998   5.699  57.580  1.00120.84           N  
ANISOU 2356  N   ILE A 307    15348  12533  18033   2615  -5522    106       N  
ATOM   2357  CA  ILE A 307      20.326   6.270  56.415  1.00120.02           C  
ANISOU 2357  CA  ILE A 307    15159  12636  17806   2565  -5059   -177       C  
ATOM   2358  C   ILE A 307      21.051   7.528  55.952  1.00120.50           C  
ANISOU 2358  C   ILE A 307    14927  13127  17731   2551  -4822   -390       C  
ATOM   2359  O   ILE A 307      21.511   7.620  54.808  1.00112.70           O  
ANISOU 2359  O   ILE A 307    13620  12287  16916   2728  -4634   -730       O  
ATOM   2360  CB  ILE A 307      18.849   6.560  56.735  1.00115.86           C  
ANISOU 2360  CB  ILE A 307    15003  12104  16913   2248  -4838     22       C  
ATOM   2361  CG1 ILE A 307      18.102   5.256  57.017  1.00123.76           C  
ANISOU 2361  CG1 ILE A 307    16264  12680  18077   2246  -5044    210       C  
ATOM   2362  CG2 ILE A 307      18.191   7.317  55.592  1.00112.15           C  
ANISOU 2362  CG2 ILE A 307    14440  11884  16288   2184  -4379   -246       C  
ATOM   2363  CD1 ILE A 307      16.652   5.452  57.401  1.00138.31           C  
ANISOU 2363  CD1 ILE A 307    18450  14528  19574   1923  -4843    421       C  
ATOM   2364  N   PHE A 308      21.170   8.514  56.844  1.00127.13           N  
ANISOU 2364  N   PHE A 308    15876  14178  18251   2325  -4831   -195       N  
ATOM   2365  CA  PHE A 308      21.825   9.763  56.476  1.00116.01           C  
ANISOU 2365  CA  PHE A 308    14220  13155  16705   2268  -4624   -365       C  
ATOM   2366  C   PHE A 308      23.296   9.548  56.145  1.00110.68           C  
ANISOU 2366  C   PHE A 308    13124  12561  16368   2532  -4808   -558       C  
ATOM   2367  O   PHE A 308      23.863  10.291  55.336  1.00104.09           O  
ANISOU 2367  O   PHE A 308    11984  12028  15536   2555  -4581   -804       O  
ATOM   2368  CB  PHE A 308      21.671  10.784  57.604  1.00108.60           C  
ANISOU 2368  CB  PHE A 308    13505  12379  15378   1976  -4648   -121       C  
ATOM   2369  CG  PHE A 308      20.306  11.410  57.672  1.00116.27           C  
ANISOU 2369  CG  PHE A 308    14783  13409  15985   1714  -4344    -40       C  
ATOM   2370  CD1 PHE A 308      19.297  10.823  58.419  1.00116.99           C  
ANISOU 2370  CD1 PHE A 308    15228  13285  15936   1585  -4423    211       C  
ATOM   2371  CD2 PHE A 308      20.030  12.583  56.988  1.00113.29           C  
ANISOU 2371  CD2 PHE A 308    14330  13302  15414   1594  -3987   -209       C  
ATOM   2372  CE1 PHE A 308      18.040  11.396  58.487  1.00109.35           C  
ANISOU 2372  CE1 PHE A 308    14506  12396  14647   1355  -4137    264       C  
ATOM   2373  CE2 PHE A 308      18.775  13.161  57.051  1.00108.81           C  
ANISOU 2373  CE2 PHE A 308    14023  12777  14541   1381  -3726   -148       C  
ATOM   2374  CZ  PHE A 308      17.779  12.566  57.802  1.00106.21           C  
ANISOU 2374  CZ  PHE A 308    14018  12256  14081   1270  -3793     75       C  
ATOM   2375  N   LYS A 309      23.927   8.539  56.754  1.00131.97           N  
ANISOU 2375  N   LYS A 309    15789  14997  19356   2727  -5223   -444       N  
ATOM   2376  CA  LYS A 309      25.308   8.212  56.410  1.00139.27           C  
ANISOU 2376  CA  LYS A 309    16280  15981  20657   3022  -5415   -653       C  
ATOM   2377  C   LYS A 309      25.427   7.777  54.955  1.00136.19           C  
ANISOU 2377  C   LYS A 309    15585  15624  20538   3268  -5175  -1055       C  
ATOM   2378  O   LYS A 309      26.370   8.169  54.258  1.00133.16           O  
ANISOU 2378  O   LYS A 309    14787  15525  20284   3394  -5060  -1330       O  
ATOM   2379  CB  LYS A 309      25.841   7.116  57.335  1.00132.23           C  
ANISOU 2379  CB  LYS A 309    15443  14745  20053   3206  -5937   -440       C  
ATOM   2380  CG  LYS A 309      27.214   7.403  57.925  1.00123.40           C  
ANISOU 2380  CG  LYS A 309    14037  13785  19065   3299  -6241   -410       C  
ATOM   2381  CD  LYS A 309      27.140   8.435  59.033  1.00134.17           C  
ANISOU 2381  CD  LYS A 309    15629  15347  20004   2961  -6291   -123       C  
ATOM   2382  CE  LYS A 309      28.521   8.794  59.557  1.00154.99           C  
ANISOU 2382  CE  LYS A 309    17955  18174  22762   3033  -6584   -116       C  
ATOM   2383  NZ  LYS A 309      28.452   9.751  60.695  1.00144.08           N  
ANISOU 2383  NZ  LYS A 309    16820  16964  20962   2700  -6669    154       N  
ATOM   2384  N   GLU A 310      24.483   6.961  54.480  1.00120.28           N  
ANISOU 2384  N   GLU A 310    13760  13337  18602   3326  -5096  -1100       N  
ATOM   2385  CA  GLU A 310      24.512   6.538  53.084  1.00114.88           C  
ANISOU 2385  CA  GLU A 310    12817  12692  18140   3544  -4860  -1502       C  
ATOM   2386  C   GLU A 310      24.220   7.699  52.143  1.00116.71           C  
ANISOU 2386  C   GLU A 310    12937  13340  18067   3361  -4384  -1692       C  
ATOM   2387  O   GLU A 310      24.735   7.728  51.019  1.00109.29           O  
ANISOU 2387  O   GLU A 310    11650  12616  17260   3519  -4180  -2047       O  
ATOM   2388  CB  GLU A 310      23.517   5.400  52.856  1.00119.41           C  
ANISOU 2388  CB  GLU A 310    13653  12858  18860   3618  -4913  -1492       C  
ATOM   2389  CG  GLU A 310      23.926   4.082  53.493  1.00126.84           C  
ANISOU 2389  CG  GLU A 310    14641  13346  20207   3866  -5393  -1377       C  
ATOM   2390  CD  GLU A 310      25.060   3.405  52.746  1.00135.77           C  
ANISOU 2390  CD  GLU A 310    15327  14452  21809   4279  -5509  -1762       C  
ATOM   2391  OE1 GLU A 310      25.244   3.706  51.548  1.00112.97           O  
ANISOU 2391  OE1 GLU A 310    12146  11845  18931   4371  -5171  -2152       O  
ATOM   2392  OE2 GLU A 310      25.768   2.576  53.357  1.00153.02           O1-
ANISOU 2392  OE2 GLU A 310    17448  16344  24349   4514  -5943  -1677       O1-
ATOM   2393  N   ALA A 311      23.403   8.660  52.580  1.00106.15           N  
ANISOU 2393  N   ALA A 311    11888  12124  16320   3029  -4210  -1465       N  
ATOM   2394  CA  ALA A 311      23.169   9.855  51.776  1.00100.52           C  
ANISOU 2394  CA  ALA A 311    11085  11786  15321   2842  -3803  -1603       C  
ATOM   2395  C   ALA A 311      24.439  10.688  51.661  1.00101.41           C  
ANISOU 2395  C   ALA A 311    10831  12251  15449   2846  -3780  -1714       C  
ATOM   2396  O   ALA A 311      24.805  11.134  50.567  1.00 99.92           O  
ANISOU 2396  O   ALA A 311    10352  12358  15254   2870  -3506  -1981       O  
ATOM   2397  CB  ALA A 311      22.032  10.678  52.379  1.00107.48           C  
ANISOU 2397  CB  ALA A 311    12357  12680  15800   2512  -3665  -1335       C  
ATOM   2398  N   GLU A 312      25.119  10.911  52.789  1.00117.36           N  
ANISOU 2398  N   GLU A 312    12859  14257  17473   2802  -4072  -1504       N  
ATOM   2399  CA  GLU A 312      26.412  11.590  52.780  1.00122.61           C  
ANISOU 2399  CA  GLU A 312    13152  15234  18199   2812  -4110  -1599       C  
ATOM   2400  C   GLU A 312      27.375  10.926  51.806  1.00120.33           C  
ANISOU 2400  C   GLU A 312    12392  15049  18279   3129  -4096  -1952       C  
ATOM   2401  O   GLU A 312      28.043  11.599  51.012  1.00111.16           O  
ANISOU 2401  O   GLU A 312    10884  14256  17095   3099  -3865  -2167       O  
ATOM   2402  CB  GLU A 312      26.999  11.591  54.192  1.00132.05           C  
ANISOU 2402  CB  GLU A 312    14434  16328  19413   2775  -4514  -1326       C  
ATOM   2403  CG  GLU A 312      28.310  12.340  54.338  1.00129.46           C  
ANISOU 2403  CG  GLU A 312    13739  16315  19134   2747  -4593  -1390       C  
ATOM   2404  CD  GLU A 312      28.880  12.228  55.739  1.00126.98           C  
ANISOU 2404  CD  GLU A 312    13514  15884  18847   2726  -5034  -1122       C  
ATOM   2405  OE1 GLU A 312      28.820  11.122  56.316  1.00131.71           O  
ANISOU 2405  OE1 GLU A 312    14239  16154  19650   2913  -5361   -994       O  
ATOM   2406  OE2 GLU A 312      29.385  13.243  56.262  1.00124.69           O1-
ANISOU 2406  OE2 GLU A 312    13177  15825  18374   2514  -5068  -1034       O1-
ATOM   2407  N   LYS A 313      27.452   9.595  51.855  1.00123.61           N  
ANISOU 2407  N   LYS A 313    12789  15140  19039   3430  -4343  -2018       N  
ATOM   2408  CA  LYS A 313      28.347   8.858  50.971  1.00120.82           C  
ANISOU 2408  CA  LYS A 313    11984  14851  19069   3776  -4349  -2391       C  
ATOM   2409  C   LYS A 313      27.986   9.065  49.505  1.00120.14           C  
ANISOU 2409  C   LYS A 313    11748  15010  18888   3771  -3904  -2722       C  
ATOM   2410  O   LYS A 313      28.873   9.067  48.643  1.00116.99           O  
ANISOU 2410  O   LYS A 313    10899  14902  18650   3932  -3765  -3055       O  
ATOM   2411  CB  LYS A 313      28.310   7.374  51.341  1.00124.74           C  
ANISOU 2411  CB  LYS A 313    12568  14873  19953   4090  -4716  -2381       C  
ATOM   2412  CG  LYS A 313      29.142   6.457  50.465  1.00123.87           C  
ANISOU 2412  CG  LYS A 313    12020  14756  20289   4498  -4754  -2799       C  
ATOM   2413  CD  LYS A 313      28.686   5.014  50.635  1.00133.36           C  
ANISOU 2413  CD  LYS A 313    13426  15418  21825   4759  -5046  -2795       C  
ATOM   2414  CE  LYS A 313      29.283   4.380  51.883  1.00118.52           C  
ANISOU 2414  CE  LYS A 313    11600  13210  20222   4908  -5589  -2522       C  
ATOM   2415  NZ  LYS A 313      30.073   3.155  51.580  1.00123.88           N  
ANISOU 2415  NZ  LYS A 313    11969  13632  21467   5375  -5872  -2805       N  
ATOM   2416  N   PHE A 314      26.699   9.257  49.205  1.00117.35           N  
ANISOU 2416  N   PHE A 314    11752  14573  18263   3580  -3677  -2639       N  
ATOM   2417  CA  PHE A 314      26.282   9.480  47.824  1.00111.99           C  
ANISOU 2417  CA  PHE A 314    10964  14132  17456   3550  -3273  -2925       C  
ATOM   2418  C   PHE A 314      26.830  10.797  47.288  1.00110.01           C  
ANISOU 2418  C   PHE A 314    10463  14380  16956   3334  -2980  -2990       C  
ATOM   2419  O   PHE A 314      27.453  10.835  46.220  1.00105.52           O  
ANISOU 2419  O   PHE A 314     9515  14126  16451   3432  -2762  -3314       O  
ATOM   2420  CB  PHE A 314      24.756   9.453  47.728  1.00114.21           C  
ANISOU 2420  CB  PHE A 314    11690  14210  17496   3374  -3131  -2781       C  
ATOM   2421  CG  PHE A 314      24.216  10.060  46.463  1.00110.93           C  
ANISOU 2421  CG  PHE A 314    11227  14091  16830   3238  -2713  -2974       C  
ATOM   2422  CD1 PHE A 314      24.234   9.347  45.275  1.00109.16           C  
ANISOU 2422  CD1 PHE A 314    10804  13920  16752   3442  -2560  -3345       C  
ATOM   2423  CD2 PHE A 314      23.686  11.340  46.463  1.00109.17           C  
ANISOU 2423  CD2 PHE A 314    11167  14088  16225   2908  -2489  -2790       C  
ATOM   2424  CE1 PHE A 314      23.736   9.902  44.111  1.00 94.89           C  
ANISOU 2424  CE1 PHE A 314     8964  12406  14685   3302  -2192  -3506       C  
ATOM   2425  CE2 PHE A 314      23.189  11.900  45.303  1.00 99.95           C  
ANISOU 2425  CE2 PHE A 314     9966  13182  14827   2779  -2137  -2937       C  
ATOM   2426  CZ  PHE A 314      23.213  11.180  44.126  1.00 93.58           C  
ANISOU 2426  CZ  PHE A 314     8964  12451  14140   2967  -1989  -3285       C  
ATOM   2427  N   PHE A 315      26.592  11.895  48.011  1.00113.73           N  
ANISOU 2427  N   PHE A 315    11146  14932  17134   3024  -2970  -2688       N  
ATOM   2428  CA  PHE A 315      27.106  13.195  47.586  1.00114.73           C  
ANISOU 2428  CA  PHE A 315    11067  15489  17036   2786  -2728  -2710       C  
ATOM   2429  C   PHE A 315      28.626  13.185  47.496  1.00120.44           C  
ANISOU 2429  C   PHE A 315    11287  16478  17999   2927  -2821  -2889       C  
ATOM   2430  O   PHE A 315      29.207  13.703  46.537  1.00124.09           O  
ANISOU 2430  O   PHE A 315    11407  17335  18404   2869  -2556  -3100       O  
ATOM   2431  CB  PHE A 315      26.639  14.289  48.547  1.00111.81           C  
ANISOU 2431  CB  PHE A 315    11028  15090  16364   2460  -2770  -2362       C  
ATOM   2432  CG  PHE A 315      25.162  14.544  48.508  1.00105.36           C  
ANISOU 2432  CG  PHE A 315    10647  14108  15277   2288  -2612  -2214       C  
ATOM   2433  CD1 PHE A 315      24.594  15.231  47.449  1.00104.35           C  
ANISOU 2433  CD1 PHE A 315    10532  14194  14922   2131  -2263  -2304       C  
ATOM   2434  CD2 PHE A 315      24.341  14.098  49.529  1.00109.52           C  
ANISOU 2434  CD2 PHE A 315    11560  14282  15771   2275  -2816  -1976       C  
ATOM   2435  CE1 PHE A 315      23.235  15.472  47.411  1.00111.98           C  
ANISOU 2435  CE1 PHE A 315    11872  15015  15662   1987  -2132  -2174       C  
ATOM   2436  CE2 PHE A 315      22.981  14.333  49.493  1.00107.89           C  
ANISOU 2436  CE2 PHE A 315    11717  13952  15326   2118  -2660  -1855       C  
ATOM   2437  CZ  PHE A 315      22.427  15.023  48.434  1.00109.44           C  
ANISOU 2437  CZ  PHE A 315    11905  14353  15324   1985  -2323  -1960       C  
ATOM   2438  N   VAL A 316      29.290  12.601  48.497  1.00118.82           N  
ANISOU 2438  N   VAL A 316    11018  16073  18056   3102  -3203  -2797       N  
ATOM   2439  CA  VAL A 316      30.749  12.537  48.490  1.00116.91           C  
ANISOU 2439  CA  VAL A 316    10270  16071  18078   3258  -3331  -2965       C  
ATOM   2440  C   VAL A 316      31.249  11.792  47.260  1.00114.17           C  
ANISOU 2440  C   VAL A 316     9505  15896  17977   3549  -3153  -3398       C  
ATOM   2441  O   VAL A 316      32.306  12.123  46.707  1.00110.14           O  
ANISOU 2441  O   VAL A 316     8516  15784  17550   3577  -3029  -3618       O  
ATOM   2442  CB  VAL A 316      31.251  11.894  49.799  1.00114.64           C  
ANISOU 2442  CB  VAL A 316    10028  15481  18048   3428  -3821  -2775       C  
ATOM   2443  CG1 VAL A 316      32.731  11.563  49.710  1.00111.90           C  
ANISOU 2443  CG1 VAL A 316     9117  15338  18060   3678  -3986  -2999       C  
ATOM   2444  CG2 VAL A 316      30.986  12.819  50.977  1.00118.24           C  
ANISOU 2444  CG2 VAL A 316    10817  15890  18219   3105  -3966  -2392       C  
ATOM   2445  N   SER A 317      30.489  10.802  46.790  1.00117.84           N  
ANISOU 2445  N   SER A 317    10138  16088  18550   3754  -3123  -3541       N  
ATOM   2446  CA  SER A 317      30.891  10.017  45.630  1.00126.23           C  
ANISOU 2446  CA  SER A 317    10834  17285  19844   4049  -2962  -3990       C  
ATOM   2447  C   SER A 317      30.907  10.823  44.336  1.00130.36           C  
ANISOU 2447  C   SER A 317    11144  18308  20080   3855  -2489  -4208       C  
ATOM   2448  O   SER A 317      31.469  10.346  43.344  1.00131.90           O  
ANISOU 2448  O   SER A 317    10947  18743  20427   4068  -2319  -4611       O  
ATOM   2449  CB  SER A 317      29.967   8.809  45.475  1.00124.37           C  
ANISOU 2449  CB  SER A 317    10885  16601  19769   4274  -3058  -4074       C  
ATOM   2450  OG  SER A 317      28.674   9.209  45.058  1.00111.99           O  
ANISOU 2450  OG  SER A 317     9705  14998  17847   4021  -2802  -3962       O  
ATOM   2451  N   VAL A 318      30.314  12.016  44.311  1.00122.93           N  
ANISOU 2451  N   VAL A 318    10448  17529  18729   3461  -2280  -3958       N  
ATOM   2452  CA  VAL A 318      30.336  12.866  43.125  1.00114.93           C  
ANISOU 2452  CA  VAL A 318     9260  16987  17422   3235  -1859  -4104       C  
ATOM   2453  C   VAL A 318      31.232  14.078  43.299  1.00119.03           C  
ANISOU 2453  C   VAL A 318     9529  17894  17803   2960  -1789  -3977       C  
ATOM   2454  O   VAL A 318      31.278  14.934  42.403  1.00108.53           O  
ANISOU 2454  O   VAL A 318     8076  16959  16200   2708  -1457  -4027       O  
ATOM   2455  CB  VAL A 318      28.918  13.307  42.713  1.00100.46           C  
ANISOU 2455  CB  VAL A 318     7879  15059  15233   2995  -1644  -3950       C  
ATOM   2456  CG1 VAL A 318      27.984  12.107  42.655  1.00110.81           C  
ANISOU 2456  CG1 VAL A 318     9460  15955  16688   3235  -1745  -4042       C  
ATOM   2457  CG2 VAL A 318      28.387  14.381  43.647  1.00 96.84           C  
ANISOU 2457  CG2 VAL A 318     7788  14485  14521   2664  -1722  -3524       C  
ATOM   2458  N   GLY A 319      31.947  14.182  44.414  1.00130.92           N  
ANISOU 2458  N   GLY A 319    12263  18974  18506   4246  -1101  -4016       N  
ATOM   2459  CA  GLY A 319      32.880  15.266  44.626  1.00119.98           C  
ANISOU 2459  CA  GLY A 319    10468  17958  17162   4084   -990  -3939       C  
ATOM   2460  C   GLY A 319      32.415  16.362  45.555  1.00117.07           C  
ANISOU 2460  C   GLY A 319    10254  17649  16577   3768  -1240  -3519       C  
ATOM   2461  O   GLY A 319      33.089  17.393  45.647  1.00112.26           O  
ANISOU 2461  O   GLY A 319     9372  17351  15929   3558  -1128  -3447       O  
ATOM   2462  N   LEU A 320      31.286  16.173  46.253  1.00120.31           N  
ANISOU 2462  N   LEU A 320    11096  17762  16852   3712  -1552  -3255       N  
ATOM   2463  CA  LEU A 320      30.731  17.177  47.145  1.00115.69           C  
ANISOU 2463  CA  LEU A 320    10712  17194  16052   3419  -1750  -2881       C  
ATOM   2464  C   LEU A 320      31.158  16.905  48.586  1.00111.98           C  
ANISOU 2464  C   LEU A 320    10148  16532  15867   3554  -2177  -2666       C  
ATOM   2465  O   LEU A 320      31.400  15.754  48.960  1.00121.50           O  
ANISOU 2465  O   LEU A 320    11315  17464  17387   3878  -2404  -2739       O  
ATOM   2466  CB  LEU A 320      29.202  17.191  47.046  1.00115.26           C  
ANISOU 2466  CB  LEU A 320    11168  16941  15685   3250  -1793  -2734       C  
ATOM   2467  CG  LEU A 320      28.636  17.659  45.698  1.00102.90           C  
ANISOU 2467  CG  LEU A 320     9773  15557  13766   3054  -1464  -2872       C  
ATOM   2468  CD1 LEU A 320      27.119  17.532  45.661  1.00 87.96           C  
ANISOU 2468  CD1 LEU A 320     8317  13439  11664   2932  -1583  -2738       C  
ATOM   2469  CD2 LEU A 320      29.064  19.085  45.374  1.00 90.87           C  
ANISOU 2469  CD2 LEU A 320     8134  14391  12002   2760  -1247  -2790       C  
ATOM   2470  N   PRO A 321      31.273  17.941  49.417  1.00107.81           N  
ANISOU 2470  N   PRO A 321     9622  16118  15223   3307  -2314  -2397       N  
ATOM   2471  CA  PRO A 321      31.817  17.746  50.768  1.00129.67           C  
ANISOU 2471  CA  PRO A 321    12312  18729  18228   3405  -2743  -2200       C  
ATOM   2472  C   PRO A 321      30.884  16.940  51.660  1.00130.87           C  
ANISOU 2472  C   PRO A 321    12922  18444  18357   3484  -3057  -2006       C  
ATOM   2473  O   PRO A 321      29.667  16.915  51.462  1.00123.60           O  
ANISOU 2473  O   PRO A 321    12392  17384  17185   3347  -2945  -1943       O  
ATOM   2474  CB  PRO A 321      31.973  19.179  51.295  1.00132.73           C  
ANISOU 2474  CB  PRO A 321    12698  19345  18388   3040  -2748  -1976       C  
ATOM   2475  CG  PRO A 321      31.014  19.986  50.480  1.00118.41           C  
ANISOU 2475  CG  PRO A 321    11157  17653  16180   2765  -2402  -1963       C  
ATOM   2476  CD  PRO A 321      31.038  19.364  49.120  1.00 92.50           C  
ANISOU 2476  CD  PRO A 321     7754  14456  12936   2926  -2090  -2280       C  
ATOM   2477  N   ASN A 322      31.470  16.277  52.660  1.00118.34           N  
ANISOU 2477  N   ASN A 322    11285  16634  17044   3693  -3467  -1906       N  
ATOM   2478  CA  ASN A 322      30.638  15.609  53.648  1.00119.91           C  
ANISOU 2478  CA  ASN A 322    11978  16408  17173   3701  -3769  -1679       C  
ATOM   2479  C   ASN A 322      30.054  16.634  54.621  1.00113.66           C  
ANISOU 2479  C   ASN A 322    11523  15619  16043   3326  -3848  -1363       C  
ATOM   2480  O   ASN A 322      30.458  17.801  54.661  1.00114.78           O  
ANISOU 2480  O   ASN A 322    11496  16059  16055   3102  -3756  -1307       O  
ATOM   2481  CB  ASN A 322      31.411  14.496  54.383  1.00121.81           C  
ANISOU 2481  CB  ASN A 322    12143  16350  17789   4054  -4217  -1658       C  
ATOM   2482  CG  ASN A 322      32.588  15.000  55.230  1.00159.25           C  
ANISOU 2482  CG  ASN A 322    16578  21228  22701   4063  -4568  -1528       C  
ATOM   2483  OD1 ASN A 322      32.615  16.143  55.682  1.00168.29           O  
ANISOU 2483  OD1 ASN A 322    17756  22582  23604   3736  -4559  -1359       O  
ATOM   2484  ND2 ASN A 322      33.557  14.107  55.475  1.00173.02           N  
ANISOU 2484  ND2 ASN A 322    18034  22821  24885   4448  -4913  -1607       N  
ATOM   2485  N   MET A 323      29.074  16.186  55.401  1.00115.75           N  
ANISOU 2485  N   MET A 323    12289  15530  16160   3243  -3986  -1170       N  
ATOM   2486  CA  MET A 323      28.366  17.083  56.302  1.00120.71           C  
ANISOU 2486  CA  MET A 323    13290  16120  16456   2889  -3985   -906       C  
ATOM   2487  C   MET A 323      29.314  17.658  57.347  1.00125.09           C  
ANISOU 2487  C   MET A 323    13790  16735  17004   2801  -4312   -728       C  
ATOM   2488  O   MET A 323      30.277  17.013  57.768  1.00123.25           O  
ANISOU 2488  O   MET A 323    13385  16409  17035   3035  -4684   -724       O  
ATOM   2489  CB  MET A 323      27.221  16.345  56.994  1.00117.58           C  
ANISOU 2489  CB  MET A 323    13424  15309  15940   2820  -4053   -755       C  
ATOM   2490  CG  MET A 323      26.121  15.855  56.063  1.00116.79           C  
ANISOU 2490  CG  MET A 323    13414  15134  15827   2832  -3756   -906       C  
ATOM   2491  SD  MET A 323      25.174  17.173  55.278  1.00128.93           S  
ANISOU 2491  SD  MET A 323    14914  16973  17099   2539  -3325   -939       S  
ATOM   2492  CE  MET A 323      25.890  17.173  53.637  1.00114.04           C  
ANISOU 2492  CE  MET A 323    12554  15426  15349   2740  -3124  -1259       C  
ATOM   2493  N   THR A 324      29.034  18.892  57.761  1.00123.23           N  
ANISOU 2493  N   THR A 324    13705  16641  16474   2463  -4194   -586       N  
ATOM   2494  CA  THR A 324      29.769  19.476  58.872  1.00110.05           C  
ANISOU 2494  CA  THR A 324    12102  14985  14725   2308  -4520   -398       C  
ATOM   2495  C   THR A 324      29.494  18.688  60.147  1.00112.77           C  
ANISOU 2495  C   THR A 324    12945  14910  14992   2314  -4894   -178       C  
ATOM   2496  O   THR A 324      28.464  18.025  60.285  1.00112.60           O  
ANISOU 2496  O   THR A 324    13305  14600  14876   2310  -4788   -133       O  
ATOM   2497  CB  THR A 324      29.384  20.945  59.071  1.00108.58           C  
ANISOU 2497  CB  THR A 324    12074  14977  14206   1928  -4283   -301       C  
ATOM   2498  OG1 THR A 324      28.007  21.038  59.463  1.00 87.60           O  
ANISOU 2498  OG1 THR A 324     9922  12084  11278   1748  -4074   -188       O  
ATOM   2499  CG2 THR A 324      29.601  21.737  57.790  1.00 91.44           C  
ANISOU 2499  CG2 THR A 324     9492  13184  12068   1892  -3916   -491       C  
ATOM   2500  N   GLN A 325      30.447  18.748  61.079  1.00 97.73           N  
ANISOU 2500  N   GLN A 325    11041  12965  13125   2305  -5352    -38       N  
ATOM   2501  CA  GLN A 325      30.238  18.126  62.382  1.00109.10           C  
ANISOU 2501  CA  GLN A 325    13046  13997  14409   2252  -5746    209       C  
ATOM   2502  C   GLN A 325      29.012  18.708  63.074  1.00106.26           C  
ANISOU 2502  C   GLN A 325    13306  13475  13591   1868  -5474    369       C  
ATOM   2503  O   GLN A 325      28.241  17.978  63.708  1.00100.93           O  
ANISOU 2503  O   GLN A 325    13147  12433  12769   1819  -5511    497       O  
ATOM   2504  CB  GLN A 325      31.482  18.307  63.247  1.00110.51           C  
ANISOU 2504  CB  GLN A 325    13126  14201  14663   2254  -6314    341       C  
ATOM   2505  CG  GLN A 325      31.435  17.590  64.579  1.00100.28           C  
ANISOU 2505  CG  GLN A 325    12434  12466  13200   2220  -6817    610       C  
ATOM   2506  CD  GLN A 325      32.505  18.089  65.524  1.00153.11           C  
ANISOU 2506  CD  GLN A 325    19122  19209  19845   2099  -7373    770       C  
ATOM   2507  OE1 GLN A 325      33.158  19.099  65.257  1.00150.21           O  
ANISOU 2507  OE1 GLN A 325    18339  19209  19525   1969  -7323    686       O  
ATOM   2508  NE2 GLN A 325      32.688  17.391  66.638  1.00167.41           N  
ANISOU 2508  NE2 GLN A 325    21421  20642  21545   2101  -7875   1002       N  
ATOM   2509  N   GLY A 326      28.813  20.023  62.954  1.00100.27           N  
ANISOU 2509  N   GLY A 326    12508  12974  12618   1590  -5175    352       N  
ATOM   2510  CA  GLY A 326      27.626  20.642  63.515  1.00 98.00           C  
ANISOU 2510  CA  GLY A 326    12743  12543  11950   1259  -4848    458       C  
ATOM   2511  C   GLY A 326      26.337  20.061  62.971  1.00113.24           C  
ANISOU 2511  C   GLY A 326    14798  14323  13906   1312  -4464    381       C  
ATOM   2512  O   GLY A 326      25.307  20.084  63.648  1.00121.56           O  
ANISOU 2512  O   GLY A 326    16337  15135  14713   1090  -4268    485       O  
ATOM   2513  N   PHE A 327      26.371  19.534  61.745  1.00101.56           N  
ANISOU 2513  N   PHE A 327    12882  12982  12725   1584  -4339    184       N  
ATOM   2514  CA  PHE A 327      25.211  18.830  61.209  1.00 92.18           C  
ANISOU 2514  CA  PHE A 327    11798  11631  11594   1641  -4056    102       C  
ATOM   2515  C   PHE A 327      24.886  17.598  62.045  1.00 96.05           C  
ANISOU 2515  C   PHE A 327    12730  11691  12073   1673  -4284    233       C  
ATOM   2516  O   PHE A 327      23.743  17.408  62.475  1.00 94.31           O  
ANISOU 2516  O   PHE A 327    12905  11237  11692   1475  -4056    304       O  
ATOM   2517  CB  PHE A 327      25.464  18.439  59.752  1.00104.10           C  
ANISOU 2517  CB  PHE A 327    12798  13356  13398   1922  -3940   -144       C  
ATOM   2518  CG  PHE A 327      24.382  17.586  59.151  1.00105.74           C  
ANISOU 2518  CG  PHE A 327    13098  13387  13691   1992  -3732   -245       C  
ATOM   2519  CD1 PHE A 327      23.248  18.162  58.607  1.00104.90           C  
ANISOU 2519  CD1 PHE A 327    13005  13366  13486   1829  -3353   -300       C  
ATOM   2520  CD2 PHE A 327      24.500  16.204  59.132  1.00100.00           C  
ANISOU 2520  CD2 PHE A 327    12444  12388  13163   2220  -3943   -285       C  
ATOM   2521  CE1 PHE A 327      22.256  17.379  58.052  1.00108.99           C  
ANISOU 2521  CE1 PHE A 327    13578  13729  14104   1868  -3201   -398       C  
ATOM   2522  CE2 PHE A 327      23.511  15.417  58.579  1.00 97.62           C  
ANISOU 2522  CE2 PHE A 327    12240  11912  12938   2248  -3763   -386       C  
ATOM   2523  CZ  PHE A 327      22.387  16.005  58.039  1.00106.96           C  
ANISOU 2523  CZ  PHE A 327    13407  13210  14022   2058  -3398   -444       C  
ATOM   2524  N   TRP A 328      25.890  16.751  62.291  1.00 93.12           N  
ANISOU 2524  N   TRP A 328    12295  11197  11888   1919  -4733    266       N  
ATOM   2525  CA  TRP A 328      25.661  15.506  63.018  1.00 95.40           C  
ANISOU 2525  CA  TRP A 328    13031  11037  12178   1978  -4997    401       C  
ATOM   2526  C   TRP A 328      25.336  15.747  64.486  1.00100.68           C  
ANISOU 2526  C   TRP A 328    14356  11440  12457   1641  -5116    672       C  
ATOM   2527  O   TRP A 328      24.634  14.937  65.102  1.00 98.33           O  
ANISOU 2527  O   TRP A 328    14569  10758  12034   1532  -5121    794       O  
ATOM   2528  CB  TRP A 328      26.885  14.599  62.895  1.00 95.31           C  
ANISOU 2528  CB  TRP A 328    12764  10946  12502   2367  -5488    367       C  
ATOM   2529  CG  TRP A 328      27.132  14.131  61.500  1.00104.82           C  
ANISOU 2529  CG  TRP A 328    13421  12329  14078   2703  -5332     77       C  
ATOM   2530  CD1 TRP A 328      28.100  14.570  60.646  1.00108.12           C  
ANISOU 2530  CD1 TRP A 328    13217  13124  14740   2907  -5318   -118       C  
ATOM   2531  CD2 TRP A 328      26.397  13.126  60.793  1.00113.67           C  
ANISOU 2531  CD2 TRP A 328    14596  13248  15345   2842  -5147    -66       C  
ATOM   2532  NE1 TRP A 328      28.012  13.903  59.448  1.00115.45           N  
ANISOU 2532  NE1 TRP A 328    13839  14097  15931   3170  -5114   -382       N  
ATOM   2533  CE2 TRP A 328      26.974  13.010  59.513  1.00116.08           C  
ANISOU 2533  CE2 TRP A 328    14330  13820  15955   3139  -5029   -355       C  
ATOM   2534  CE3 TRP A 328      25.307  12.313  61.117  1.00116.60           C  
ANISOU 2534  CE3 TRP A 328    15456  13235  15611   2714  -5056     12       C  
ATOM   2535  CZ2 TRP A 328      26.498  12.115  58.558  1.00119.97           C  
ANISOU 2535  CZ2 TRP A 328    14759  14197  16626   3319  -4848   -570       C  
ATOM   2536  CZ3 TRP A 328      24.835  11.425  60.168  1.00125.99           C  
ANISOU 2536  CZ3 TRP A 328    16545  14314  17010   2886  -4894   -193       C  
ATOM   2537  CH2 TRP A 328      25.428  11.336  58.903  1.00126.58           C  
ANISOU 2537  CH2 TRP A 328    16078  14651  17365   3190  -4804   -483       C  
ATOM   2538  N   GLU A 329      25.833  16.839  65.063  1.00108.57           N  
ANISOU 2538  N   GLU A 329    15390  12623  13240   1445  -5198    762       N  
ATOM   2539  CA  GLU A 329      25.626  17.117  66.479  1.00105.71           C  
ANISOU 2539  CA  GLU A 329    15695  12011  12460   1107  -5325   1004       C  
ATOM   2540  C   GLU A 329      24.318  17.835  66.765  1.00106.75           C  
ANISOU 2540  C   GLU A 329    16166  12111  12284    744  -4760   1006       C  
ATOM   2541  O   GLU A 329      23.795  17.723  67.879  1.00106.53           O  
ANISOU 2541  O   GLU A 329    16790  11779  11909    454  -4729   1176       O  
ATOM   2542  CB  GLU A 329      26.775  17.969  67.022  1.00118.83           C  
ANISOU 2542  CB  GLU A 329    17274  13860  14014   1034  -5701   1089       C  
ATOM   2543  CG  GLU A 329      28.104  17.252  67.108  1.00126.63           C  
ANISOU 2543  CG  GLU A 329    18015  14811  15287   1350  -6356   1139       C  
ATOM   2544  CD  GLU A 329      29.239  18.194  67.450  1.00143.61           C  
ANISOU 2544  CD  GLU A 329    19933  17224  17407   1267  -6696   1178       C  
ATOM   2545  OE1 GLU A 329      29.011  19.423  67.446  1.00137.20           O  
ANISOU 2545  OE1 GLU A 329    19111  16647  16371    984  -6377   1137       O  
ATOM   2546  OE2 GLU A 329      30.357  17.710  67.719  1.00165.85           O1-
ANISOU 2546  OE2 GLU A 329    22566  20001  20447   1485  -7294   1245       O1-
ATOM   2547  N   ASN A 330      23.781  18.563  65.791  1.00109.26           N  
ANISOU 2547  N   ASN A 330    16070  12720  12722    754  -4311    818       N  
ATOM   2548  CA  ASN A 330      22.694  19.490  66.044  1.00109.59           C  
ANISOU 2548  CA  ASN A 330    16332  12779  12528    446  -3805    803       C  
ATOM   2549  C   ASN A 330      21.431  19.187  65.255  1.00102.56           C  
ANISOU 2549  C   ASN A 330    15281  11871  11815    473  -3350    661       C  
ATOM   2550  O   ASN A 330      20.398  19.806  65.527  1.00103.23           O  
ANISOU 2550  O   ASN A 330    15548  11916  11760    235  -2920    645       O  
ATOM   2551  CB  ASN A 330      23.156  20.923  65.739  1.00115.91           C  
ANISOU 2551  CB  ASN A 330    16843  13927  13272    378  -3706    735       C  
ATOM   2552  CG  ASN A 330      24.347  21.334  66.583  1.00112.27           C  
ANISOU 2552  CG  ASN A 330    16547  13490  12621    285  -4152    870       C  
ATOM   2553  OD1 ASN A 330      24.369  21.119  67.795  1.00 99.12           O  
ANISOU 2553  OD1 ASN A 330    15463  11546  10652     78  -4348   1045       O  
ATOM   2554  ND2 ASN A 330      25.361  21.902  65.940  1.00104.41           N  
ANISOU 2554  ND2 ASN A 330    15049  12822  11799    417  -4331    788       N  
ATOM   2555  N   SER A 331      21.476  18.268  64.297  1.00 94.98           N  
ANISOU 2555  N   SER A 331    13982  10933  11174    751  -3434    545       N  
ATOM   2556  CA  SER A 331      20.271  17.854  63.596  1.00105.00           C  
ANISOU 2556  CA  SER A 331    15136  12152  12609    750  -3074    418       C  
ATOM   2557  C   SER A 331      19.479  16.867  64.444  1.00104.24           C  
ANISOU 2557  C   SER A 331    15556  11639  12412    565  -3013    531       C  
ATOM   2558  O   SER A 331      20.031  16.158  65.290  1.00100.29           O  
ANISOU 2558  O   SER A 331    15454  10871  11782    551  -3351    693       O  
ATOM   2559  CB  SER A 331      20.616  17.212  62.253  1.00 97.65           C  
ANISOU 2559  CB  SER A 331    13712  11375  12015   1085  -3187    235       C  
ATOM   2560  OG  SER A 331      21.344  18.101  61.429  1.00 91.21           O  
ANISOU 2560  OG  SER A 331    12441  10942  11271   1222  -3199    126       O  
ATOM   2561  N   MET A 332      18.172  16.823  64.209  1.00106.59           N  
ANISOU 2561  N   MET A 332    15848  11875  12778    409  -2590    449       N  
ATOM   2562  CA  MET A 332      17.285  15.871  64.873  1.00112.06           C  
ANISOU 2562  CA  MET A 332    16975  12187  13414    191  -2444    524       C  
ATOM   2563  C   MET A 332      16.839  14.872  63.812  1.00109.86           C  
ANISOU 2563  C   MET A 332    16399  11869  13473    366  -2448    372       C  
ATOM   2564  O   MET A 332      15.927  15.152  63.030  1.00121.03           O  
ANISOU 2564  O   MET A 332    17476  13432  15076    338  -2137    217       O  
ATOM   2565  CB  MET A 332      16.094  16.574  65.517  1.00107.63           C  
ANISOU 2565  CB  MET A 332    16628  11567  12698   -165  -1922    530       C  
ATOM   2566  CG  MET A 332      15.415  15.755  66.603  1.00114.53           C  
ANISOU 2566  CG  MET A 332    18110  12027  13379   -488  -1764    660       C  
ATOM   2567  SD  MET A 332      13.925  16.541  67.238  1.00132.49           S  
ANISOU 2567  SD  MET A 332    20533  14251  15556   -895  -1040    600       S  
ATOM   2568  CE  MET A 332      12.824  16.335  65.846  1.00131.56           C  
ANISOU 2568  CE  MET A 332    19727  14306  15954   -766   -780    362       C  
ATOM   2569  N   LEU A 333      17.490  13.711  63.781  1.00 94.71           N  
ANISOU 2569  N   LEU A 333    14615   9732  11636    551  -2827    414       N  
ATOM   2570  CA  LEU A 333      17.223  12.697  62.772  1.00 93.85           C  
ANISOU 2570  CA  LEU A 333    14272   9554  11832    735  -2877    254       C  
ATOM   2571  C   LEU A 333      16.363  11.551  63.290  1.00 96.76           C  
ANISOU 2571  C   LEU A 333    15081   9486  12196    507  -2787    323       C  
ATOM   2572  O   LEU A 333      16.099  10.608  62.539  1.00103.99           O  
ANISOU 2572  O   LEU A 333    15881  10280  13350    621  -2842    195       O  
ATOM   2573  CB  LEU A 333      18.541  12.144  62.219  1.00 91.90           C  
ANISOU 2573  CB  LEU A 333    13821   9348  11748   1141  -3330    201       C  
ATOM   2574  CG  LEU A 333      19.607  13.176  61.853  1.00 88.99           C  
ANISOU 2574  CG  LEU A 333    13058   9379  11374   1342  -3462    156       C  
ATOM   2575  CD1 LEU A 333      20.805  12.491  61.218  1.00 87.37           C  
ANISOU 2575  CD1 LEU A 333    12585   9203  11409   1747  -3840     55       C  
ATOM   2576  CD2 LEU A 333      19.031  14.233  60.926  1.00 87.00           C  
ANISOU 2576  CD2 LEU A 333    12376   9509  11170   1295  -3106     -6       C  
ATOM   2577  N   THR A 334      15.949  11.592  64.555  1.00116.53           N  
ANISOU 2577  N   THR A 334    18124  11737  14415    166  -2643    517       N  
ATOM   2578  CA  THR A 334      15.047  10.608  65.137  1.00119.13           C  
ANISOU 2578  CA  THR A 334    18917  11649  14696   -139  -2474    595       C  
ATOM   2579  C   THR A 334      14.067  11.332  66.045  1.00131.54           C  
ANISOU 2579  C   THR A 334    20750  13198  16034   -577  -1973    662       C  
ATOM   2580  O   THR A 334      14.463  12.231  66.791  1.00142.87           O  
ANISOU 2580  O   THR A 334    22373  14728  17183   -662  -1949    769       O  
ATOM   2581  CB  THR A 334      15.787   9.529  65.961  1.00137.65           C  
ANISOU 2581  CB  THR A 334    21873  13552  16877   -107  -2912    814       C  
ATOM   2582  OG1 THR A 334      16.071  10.028  67.275  1.00156.18           O  
ANISOU 2582  OG1 THR A 334    24752  15781  18807   -345  -2943   1047       O  
ATOM   2583  CG2 THR A 334      17.088   9.112  65.299  1.00135.59           C  
ANISOU 2583  CG2 THR A 334    21344  13353  16821    387  -3452    767       C  
ATOM   2584  N   ASP A 335      12.795  10.947  65.980  1.00139.94           N  
ANISOU 2584  N   ASP A 335    21812  14131  17230   -864  -1562    580       N  
ATOM   2585  CA  ASP A 335      11.800  11.510  66.881  1.00153.20           C  
ANISOU 2585  CA  ASP A 335    23738  15745  18724  -1295  -1020    617       C  
ATOM   2586  C   ASP A 335      12.232  11.301  68.331  1.00158.85           C  
ANISOU 2586  C   ASP A 335    25270  16125  18962  -1552  -1101    878       C  
ATOM   2587  O   ASP A 335      12.420  10.149  68.754  1.00158.47           O  
ANISOU 2587  O   ASP A 335    25721  15684  18807  -1636  -1341   1026       O  
ATOM   2588  CB  ASP A 335      10.430  10.874  66.659  1.00158.95           C  
ANISOU 2588  CB  ASP A 335    24368  16322  19703  -1589   -607    499       C  
ATOM   2589  CG  ASP A 335       9.309  11.647  67.340  1.00162.29           C  
ANISOU 2589  CG  ASP A 335    24815  16781  20065  -1979     43    454       C  
ATOM   2590  OD1 ASP A 335       9.589  12.710  67.930  1.00164.50           O  
ANISOU 2590  OD1 ASP A 335    25203  17201  20098  -2001    179    500       O  
ATOM   2591  OD2 ASP A 335       8.151  11.180  67.303  1.00153.33           O1-
ANISOU 2591  OD2 ASP A 335    23594  15522  19144  -2274    432    359       O1-
ATOM   2592  N   PRO A 336      12.430  12.370  69.107  1.00155.44           N  
ANISOU 2592  N   PRO A 336    25038  15807  18214  -1680   -943    946       N  
ATOM   2593  CA  PRO A 336      12.567  12.181  70.558  1.00159.16           C  
ANISOU 2593  CA  PRO A 336    26369  15927  18177  -2036   -917   1180       C  
ATOM   2594  C   PRO A 336      11.370  11.463  71.137  1.00167.05           C  
ANISOU 2594  C   PRO A 336    27770  16589  19112  -2502   -421   1197       C  
ATOM   2595  O   PRO A 336      11.517  10.609  72.022  1.00166.34           O  
ANISOU 2595  O   PRO A 336    28429  16080  18693  -2749   -560   1413       O  
ATOM   2596  CB  PRO A 336      12.695  13.615  71.096  1.00157.90           C  
ANISOU 2596  CB  PRO A 336    26236  16003  17755  -2128   -681   1161       C  
ATOM   2597  CG  PRO A 336      12.230  14.508  69.988  1.00152.24           C  
ANISOU 2597  CG  PRO A 336    24683  15707  17454  -1907   -416    906       C  
ATOM   2598  CD  PRO A 336      12.520  13.784  68.715  1.00147.79           C  
ANISOU 2598  CD  PRO A 336    23587  15257  17310  -1534   -783    814       C  
ATOM   2599  N   GLY A 337      10.182  11.771  70.623  1.00175.67           N  
ANISOU 2599  N   GLY A 337    28364  17847  20535  -2632    139    975       N  
ATOM   2600  CA  GLY A 337       8.957  11.156  71.064  1.00176.28           C  
ANISOU 2600  CA  GLY A 337    28679  17658  20643  -3091    679    944       C  
ATOM   2601  C   GLY A 337       8.674  11.499  72.514  1.00181.35           C  
ANISOU 2601  C   GLY A 337    30072  18069  20763  -3565   1107   1072       C  
ATOM   2602  O   GLY A 337       9.220  12.448  73.087  1.00180.11           O  
ANISOU 2602  O   GLY A 337    30133  18025  20276  -3541   1084   1126       O  
ATOM   2603  N   ASN A 338       7.793  10.696  73.102  1.00185.25           N  
ANISOU 2603  N   ASN A 338    30993  18223  21172  -4033   1520   1111       N  
ATOM   2604  CA  ASN A 338       7.441  10.781  74.523  1.00193.94           C  
ANISOU 2604  CA  ASN A 338    32937  19026  21726  -4571   1982   1239       C  
ATOM   2605  C   ASN A 338       6.922  12.192  74.794  1.00188.46           C  
ANISOU 2605  C   ASN A 338    31965  18622  21018  -4656   2583   1043       C  
ATOM   2606  O   ASN A 338       6.027  12.660  74.070  1.00180.79           O  
ANISOU 2606  O   ASN A 338    30211  17921  20561  -4584   3006    780       O  
ATOM   2607  CB  ASN A 338       8.643  10.356  75.357  1.00193.85           C  
ANISOU 2607  CB  ASN A 338    33810  18709  21136  -4563   1361   1566       C  
ATOM   2608  CG  ASN A 338       9.093   8.940  75.060  1.00199.28           C  
ANISOU 2608  CG  ASN A 338    34749  19065  21903  -4444    783   1742       C  
ATOM   2609  OD1 ASN A 338       8.506   8.246  74.229  1.00199.66           O  
ANISOU 2609  OD1 ASN A 338    34344  19105  22413  -4394    860   1611       O  
ATOM   2610  ND2 ASN A 338      10.141   8.501  75.746  1.00192.87           N  
ANISOU 2610  ND2 ASN A 338    34675  17958  20648  -4395    172   2037       N  
ATOM   2611  N   VAL A 339       7.457  12.903  75.788  1.00179.48           N  
ANISOU 2611  N   VAL A 339    31438  17429  19328  -4791   2607   1156       N  
ATOM   2612  CA  VAL A 339       6.933  14.212  76.160  1.00180.63           C  
ANISOU 2612  CA  VAL A 339    31432  17779  19421  -4910   3232    960       C  
ATOM   2613  C   VAL A 339       7.318  15.262  75.125  1.00177.04           C  
ANISOU 2613  C   VAL A 339    30122  17778  19368  -4378   2986    796       C  
ATOM   2614  O   VAL A 339       6.514  16.134  74.773  1.00173.26           O  
ANISOU 2614  O   VAL A 339    29061  17532  19238  -4334   3507    546       O  
ATOM   2615  CB  VAL A 339       7.433  14.588  77.566  1.00184.02           C  
ANISOU 2615  CB  VAL A 339    32882  17967  19071  -5253   3296   1134       C  
ATOM   2616  CG1 VAL A 339       6.560  13.939  78.630  1.00169.15           C  
ANISOU 2616  CG1 VAL A 339    31757  15687  16825  -5900   3938   1184       C  
ATOM   2617  CG2 VAL A 339       8.886  14.161  77.743  1.00177.94           C  
ANISOU 2617  CG2 VAL A 339    32601  17076  17932  -5031   2352   1437       C  
ATOM   2618  N   GLN A 340       8.549  15.194  74.618  1.00170.96           N  
ANISOU 2618  N   GLN A 340    29259  17126  18571  -3969   2194    932       N  
ATOM   2619  CA  GLN A 340       9.065  16.197  73.694  1.00166.64           C  
ANISOU 2619  CA  GLN A 340    28008  16989  18317  -3504   1929    808       C  
ATOM   2620  C   GLN A 340       8.435  16.059  72.315  1.00170.61           C  
ANISOU 2620  C   GLN A 340    27577  17746  19500  -3214   1975    606       C  
ATOM   2621  O   GLN A 340       8.926  15.297  71.477  1.00173.59           O  
ANISOU 2621  O   GLN A 340    27683  18165  20108  -2932   1457    651       O  
ATOM   2622  CB  GLN A 340      10.587  16.085  73.592  1.00165.17           C  
ANISOU 2622  CB  GLN A 340    28000  16846  17911  -3193   1094   1008       C  
ATOM   2623  CG  GLN A 340      11.257  17.250  72.883  1.00159.79           C  
ANISOU 2623  CG  GLN A 340    26761  16561  17393  -2810    856    908       C  
ATOM   2624  CD  GLN A 340      12.770  17.152  72.919  1.00161.13           C  
ANISOU 2624  CD  GLN A 340    27117  16764  17339  -2563     78   1097       C  
ATOM   2625  OE1 GLN A 340      13.333  16.343  73.658  1.00158.72           O  
ANISOU 2625  OE1 GLN A 340    27446  16162  16696  -2693   -289   1319       O  
ATOM   2626  NE2 GLN A 340      13.437  17.974  72.117  1.00152.95           N  
ANISOU 2626  NE2 GLN A 340    25524  16082  16510  -2212   -187   1013       N  
ATOM   2627  N   LYS A 341       7.350  16.787  72.072  1.00176.13           N  
ANISOU 2627  N   LYS A 341    27792  18602  20528  -3276   2579    374       N  
ATOM   2628  CA  LYS A 341       6.745  16.783  70.750  1.00174.80           C  
ANISOU 2628  CA  LYS A 341    26734  18689  20994  -2998   2571    186       C  
ATOM   2629  C   LYS A 341       7.600  17.604  69.789  1.00163.95           C  
ANISOU 2629  C   LYS A 341    24874  17661  19759  -2515   2096    156       C  
ATOM   2630  O   LYS A 341       8.445  18.404  70.200  1.00167.06           O  
ANISOU 2630  O   LYS A 341    25530  18125  19821  -2434   1928    233       O  
ATOM   2631  CB  LYS A 341       5.323  17.344  70.810  1.00173.98           C  
ANISOU 2631  CB  LYS A 341    26231  18634  21240  -3194   3325    -48       C  
ATOM   2632  CG  LYS A 341       4.473  16.759  71.930  1.00178.61           C  
ANISOU 2632  CG  LYS A 341    27343  18890  21632  -3741   3942    -44       C  
ATOM   2633  CD  LYS A 341       3.266  15.987  71.416  1.00177.13           C  
ANISOU 2633  CD  LYS A 341    26663  18667  21972  -3909   4259   -191       C  
ATOM   2634  CE  LYS A 341       3.680  14.753  70.629  1.00176.24           C  
ANISOU 2634  CE  LYS A 341    26475  18495  21994  -3771   3652    -83       C  
ATOM   2635  NZ  LYS A 341       2.499  13.975  70.158  1.00180.24           N  
ANISOU 2635  NZ  LYS A 341    26541  18946  22996  -3988   3942   -230       N  
ATOM   2636  N   ALA A 342       7.372  17.402  68.492  1.00137.08           N  
ANISOU 2636  N   ALA A 342    20780  14470  16834  -2226   1883     40       N  
ATOM   2637  CA  ALA A 342       8.170  18.088  67.485  1.00128.28           C  
ANISOU 2637  CA  ALA A 342    19221  13677  15841  -1795   1445     11       C  
ATOM   2638  C   ALA A 342       7.459  18.051  66.139  1.00139.04           C  
ANISOU 2638  C   ALA A 342    19825  15255  17748  -1579   1420   -166       C  
ATOM   2639  O   ALA A 342       6.794  17.066  65.808  1.00152.45           O  
ANISOU 2639  O   ALA A 342    21383  16843  19698  -1688   1457   -219       O  
ATOM   2640  CB  ALA A 342       9.565  17.461  67.358  1.00125.46           C  
ANISOU 2640  CB  ALA A 342    19131  13300  15239  -1596    795    180       C  
ATOM   2641  N   VAL A 343       7.613  19.128  65.372  1.00130.03           N  
ANISOU 2641  N   VAL A 343    18237  14405  16766  -1295   1330   -250       N  
ATOM   2642  CA  VAL A 343       7.060  19.208  64.022  1.00131.89           C  
ANISOU 2642  CA  VAL A 343    17792  14859  17462  -1063   1210   -396       C  
ATOM   2643  C   VAL A 343       7.904  18.312  63.119  1.00129.85           C  
ANISOU 2643  C   VAL A 343    17467  14670  17202   -842    652   -357       C  
ATOM   2644  O   VAL A 343       9.068  18.617  62.843  1.00128.94           O  
ANISOU 2644  O   VAL A 343    17418  14695  16878   -617    293   -286       O  
ATOM   2645  CB  VAL A 343       7.033  20.654  63.511  1.00122.22           C  
ANISOU 2645  CB  VAL A 343    16204  13882  16352   -835   1256   -468       C  
ATOM   2646  CG1 VAL A 343       6.384  20.726  62.132  1.00150.53           C  
ANISOU 2646  CG1 VAL A 343    19136  17665  20392   -620   1101   -602       C  
ATOM   2647  CG2 VAL A 343       6.305  21.555  64.499  1.00123.81           C  
ANISOU 2647  CG2 VAL A 343    16534  13974  16535  -1030   1826   -522       C  
ATOM   2648  N   CYS A 344       7.320  17.212  62.647  1.00135.73           N  
ANISOU 2648  N   CYS A 344    18067  15311  18193   -915    597   -423       N  
ATOM   2649  CA  CYS A 344       8.082  16.137  62.021  1.00134.80           C  
ANISOU 2649  CA  CYS A 344    18022  15155  18042   -759    133   -396       C  
ATOM   2650  C   CYS A 344       8.207  16.261  60.508  1.00126.69           C  
ANISOU 2650  C   CYS A 344    16483  14400  17254   -454   -183   -527       C  
ATOM   2651  O   CYS A 344       8.865  15.413  59.895  1.00118.38           O  
ANISOU 2651  O   CYS A 344    15468  13328  16183   -298   -542   -543       O  
ATOM   2652  CB  CYS A 344       7.460  14.780  62.365  1.00143.66           C  
ANISOU 2652  CB  CYS A 344    19372  15960  19251  -1032    223   -394       C  
ATOM   2653  SG  CYS A 344       7.970  14.121  63.966  1.00158.26           S  
ANISOU 2653  SG  CYS A 344    22057  17420  20654  -1318    303   -171       S  
ATOM   2654  N   HIS A 345       7.590  17.266  59.890  1.00127.02           N  
ANISOU 2654  N   HIS A 345    16080  14669  17513   -366    -63   -624       N  
ATOM   2655  CA  HIS A 345       7.779  17.513  58.468  1.00129.99           C  
ANISOU 2655  CA  HIS A 345    16052  15304  18033    -93   -382   -725       C  
ATOM   2656  C   HIS A 345       9.271  17.583  58.147  1.00130.57           C  
ANISOU 2656  C   HIS A 345    16286  15508  17816    154   -726   -662       C  
ATOM   2657  O   HIS A 345       9.993  18.379  58.766  1.00132.99           O  
ANISOU 2657  O   HIS A 345    16780  15873  17879    189   -685   -557       O  
ATOM   2658  CB  HIS A 345       7.093  18.811  58.049  1.00126.19           C  
ANISOU 2658  CB  HIS A 345    15178  15021  17748    -15   -232   -782       C  
ATOM   2659  CG  HIS A 345       7.106  19.055  56.569  1.00134.93           C  
ANISOU 2659  CG  HIS A 345    15910  16364  18992    216   -559   -874       C  
ATOM   2660  ND1 HIS A 345       6.521  18.196  55.664  1.00141.72           N  
ANISOU 2660  ND1 HIS A 345    16543  17216  20088    200   -753   -994       N  
ATOM   2661  CD2 HIS A 345       7.634  20.067  55.839  1.00136.01           C  
ANISOU 2661  CD2 HIS A 345    15911  16736  19030    437   -729   -860       C  
ATOM   2662  CE1 HIS A 345       6.690  18.666  54.441  1.00143.77           C  
ANISOU 2662  CE1 HIS A 345    16563  17700  20364    405  -1036  -1049       C  
ATOM   2663  NE2 HIS A 345       7.362  19.801  54.519  1.00148.76           N  
ANISOU 2663  NE2 HIS A 345    17249  18480  20793    549  -1017   -964       N  
ATOM   2664  N   PRO A 346       9.771  16.767  57.219  1.00119.82           N  
ANISOU 2664  N   PRO A 346    14857  14187  16482    314  -1050   -739       N  
ATOM   2665  CA  PRO A 346      11.210  16.792  56.915  1.00111.34           C  
ANISOU 2665  CA  PRO A 346    13881  13241  15182    552  -1335   -708       C  
ATOM   2666  C   PRO A 346      11.619  18.139  56.340  1.00112.21           C  
ANISOU 2666  C   PRO A 346    13762  13663  15209    704  -1355   -709       C  
ATOM   2667  O   PRO A 346      11.100  18.582  55.312  1.00118.09           O  
ANISOU 2667  O   PRO A 346    14199  14580  16091    774  -1389   -805       O  
ATOM   2668  CB  PRO A 346      11.378  15.656  55.898  1.00103.73           C  
ANISOU 2668  CB  PRO A 346    12837  12246  14331    679  -1595   -848       C  
ATOM   2669  CG  PRO A 346      10.158  14.798  56.069  1.00116.95           C  
ANISOU 2669  CG  PRO A 346    14528  13678  16228    444  -1467   -900       C  
ATOM   2670  CD  PRO A 346       9.060  15.745  56.435  1.00123.33           C  
ANISOU 2670  CD  PRO A 346    15141  14546  17172    268  -1156   -876       C  
ATOM   2671  N   THR A 347      12.550  18.800  57.024  1.00 95.68           N  
ANISOU 2671  N   THR A 347    11851  11625  12878    733  -1356   -592       N  
ATOM   2672  CA  THR A 347      12.987  20.133  56.641  1.00 92.69           C  
ANISOU 2672  CA  THR A 347    11321  11504  12393    827  -1349   -572       C  
ATOM   2673  C   THR A 347      14.498  20.235  56.773  1.00 86.39           C  
ANISOU 2673  C   THR A 347    10634  10820  11373    948  -1556   -515       C  
ATOM   2674  O   THR A 347      15.103  19.638  57.666  1.00 96.54           O  
ANISOU 2674  O   THR A 347    12187  11943  12549    912  -1647   -430       O  
ATOM   2675  CB  THR A 347      12.314  21.216  57.495  1.00101.95           C  
ANISOU 2675  CB  THR A 347    12570  12624  13544    669  -1042   -495       C  
ATOM   2676  OG1 THR A 347      12.270  20.791  58.862  1.00 95.88           O  
ANISOU 2676  OG1 THR A 347    12170  11604  12655    476   -892   -399       O  
ATOM   2677  CG2 THR A 347      10.897  21.472  57.002  1.00130.30           C  
ANISOU 2677  CG2 THR A 347    15873  16203  17430    628   -865   -583       C  
ATOM   2678  N   ALA A 348      15.099  20.999  55.866  1.00 86.97           N  
ANISOU 2678  N   ALA A 348    10495  11165  11386   1079  -1643   -559       N  
ATOM   2679  CA  ALA A 348      16.533  21.259  55.862  1.00 84.41           C  
ANISOU 2679  CA  ALA A 348    10178  11001  10895   1178  -1809   -529       C  
ATOM   2680  C   ALA A 348      16.763  22.701  56.291  1.00 93.64           C  
ANISOU 2680  C   ALA A 348    11398  12281  11900   1077  -1690   -429       C  
ATOM   2681  O   ALA A 348      16.234  23.629  55.670  1.00100.65           O  
ANISOU 2681  O   ALA A 348    12150  13285  12806   1069  -1574   -449       O  
ATOM   2682  CB  ALA A 348      17.135  21.003  54.481  1.00 96.00           C  
ANISOU 2682  CB  ALA A 348    11388  12690  12397   1365  -1951   -677       C  
ATOM   2683  N   TRP A 349      17.551  22.884  57.344  1.00 89.79           N  
ANISOU 2683  N   TRP A 349    11130  11737  11249    998  -1750   -318       N  
ATOM   2684  CA  TRP A 349      17.760  24.193  57.943  1.00 79.17           C  
ANISOU 2684  CA  TRP A 349     9914  10442   9725    858  -1637   -224       C  
ATOM   2685  C   TRP A 349      19.102  24.766  57.507  1.00 79.52           C  
ANISOU 2685  C   TRP A 349     9812  10743   9660    913  -1808   -226       C  
ATOM   2686  O   TRP A 349      20.110  24.055  57.465  1.00 78.60           O  
ANISOU 2686  O   TRP A 349     9612  10687   9563   1017  -2038   -246       O  
ATOM   2687  CB  TRP A 349      17.700  24.102  59.470  1.00 83.03           C  
ANISOU 2687  CB  TRP A 349    10802  10685  10061    672  -1586   -103       C  
ATOM   2688  CG  TRP A 349      16.334  23.774  59.991  1.00 87.00           C  
ANISOU 2688  CG  TRP A 349    11462  10943  10652    552  -1314   -107       C  
ATOM   2689  CD1 TRP A 349      15.634  22.623  59.781  1.00 91.73           C  
ANISOU 2689  CD1 TRP A 349    12016  11404  11435    584  -1301   -161       C  
ATOM   2690  CD2 TRP A 349      15.501  24.605  60.810  1.00 90.65           C  
ANISOU 2690  CD2 TRP A 349    12137  11262  11041    364   -983    -75       C  
ATOM   2691  NE1 TRP A 349      14.418  22.684  60.415  1.00 98.29           N  
ANISOU 2691  NE1 TRP A 349    12985  12035  12326    409   -976   -161       N  
ATOM   2692  CE2 TRP A 349      14.311  23.891  61.054  1.00 94.44           C  
ANISOU 2692  CE2 TRP A 349    12650  11541  11690    286   -760   -117       C  
ATOM   2693  CE3 TRP A 349      15.645  25.883  61.359  1.00 91.71           C  
ANISOU 2693  CE3 TRP A 349    12445  11408  10995    245   -834    -32       C  
ATOM   2694  CZ2 TRP A 349      13.273  24.410  61.824  1.00104.31           C  
ANISOU 2694  CZ2 TRP A 349    14060  12620  12955    106   -363   -129       C  
ATOM   2695  CZ3 TRP A 349      14.612  26.397  62.123  1.00 96.79           C  
ANISOU 2695  CZ3 TRP A 349    13285  11855  11634     86   -451    -47       C  
ATOM   2696  CH2 TRP A 349      13.441  25.662  62.347  1.00103.29           C  
ANISOU 2696  CH2 TRP A 349    14098  12498  12649     24   -204   -101       C  
ATOM   2697  N   ASP A 350      19.102  26.053  57.171  1.00 93.96           N  
ANISOU 2697  N   ASP A 350    11595  12708  11398    843  -1687   -209       N  
ATOM   2698  CA  ASP A 350      20.319  26.814  56.894  1.00 88.35           C  
ANISOU 2698  CA  ASP A 350    10782  12227  10558    812  -1790   -196       C  
ATOM   2699  C   ASP A 350      20.303  27.997  57.858  1.00104.41           C  
ANISOU 2699  C   ASP A 350    13094  14173  12406    599  -1681    -87       C  
ATOM   2700  O   ASP A 350      19.829  29.083  57.518  1.00104.73           O  
ANISOU 2700  O   ASP A 350    13158  14232  12404    540  -1509    -78       O  
ATOM   2701  CB  ASP A 350      20.388  27.267  55.434  1.00 95.93           C  
ANISOU 2701  CB  ASP A 350    11480  13422  11547    895  -1745   -284       C  
ATOM   2702  CG  ASP A 350      21.655  28.046  55.121  1.00110.67           C  
ANISOU 2702  CG  ASP A 350    13235  15531  13283    817  -1802   -279       C  
ATOM   2703  OD1 ASP A 350      22.554  28.107  55.985  1.00109.87           O  
ANISOU 2703  OD1 ASP A 350    13192  15437  13117    727  -1928   -222       O  
ATOM   2704  OD2 ASP A 350      21.750  28.603  54.007  1.00123.06           O1-
ANISOU 2704  OD2 ASP A 350    14669  17278  14808    823  -1730   -328       O1-
ATOM   2705  N   LEU A 351      20.819  27.776  59.069  1.00 92.54           N  
ANISOU 2705  N   LEU A 351    11835  12546  10778    483  -1802     -5       N  
ATOM   2706  CA  LEU A 351      20.774  28.806  60.098  1.00 79.15           C  
ANISOU 2706  CA  LEU A 351    10481  10725   8866    253  -1696     82       C  
ATOM   2707  C   LEU A 351      21.776  29.923  59.847  1.00 77.49           C  
ANISOU 2707  C   LEU A 351    10200  10715   8528    139  -1772    100       C  
ATOM   2708  O   LEU A 351      21.604  31.025  60.379  1.00 78.55           O  
ANISOU 2708  O   LEU A 351    10592  10756   8495    -44  -1630    144       O  
ATOM   2709  CB  LEU A 351      21.028  28.187  61.475  1.00 80.34           C  
ANISOU 2709  CB  LEU A 351    10986  10669   8871    131  -1839    172       C  
ATOM   2710  CG  LEU A 351      20.036  27.125  61.961  1.00 84.06           C  
ANISOU 2710  CG  LEU A 351    11638  10887   9413    160  -1730    177       C  
ATOM   2711  CD1 LEU A 351      20.446  25.722  61.522  1.00 81.91           C  
ANISOU 2711  CD1 LEU A 351    11159  10644   9319    362  -1994    152       C  
ATOM   2712  CD2 LEU A 351      19.878  27.195  63.471  1.00 88.09           C  
ANISOU 2712  CD2 LEU A 351    12684  11132   9657    -85  -1680    279       C  
ATOM   2713  N   GLY A 352      22.807  29.667  59.050  1.00 75.28           N  
ANISOU 2713  N   GLY A 352     9581  10695   8328    230  -1962     53       N  
ATOM   2714  CA  GLY A 352      23.884  30.617  58.840  1.00 79.65           C  
ANISOU 2714  CA  GLY A 352    10031  11454   8778     82  -2038     64       C  
ATOM   2715  C   GLY A 352      25.033  30.388  59.807  1.00 99.27           C  
ANISOU 2715  C   GLY A 352    12567  13958  11193    -34  -2348    123       C  
ATOM   2716  O   GLY A 352      25.032  29.463  60.625  1.00 90.71           O  
ANISOU 2716  O   GLY A 352    11628  12716  10121     18  -2533    169       O  
ATOM   2717  N   LYS A 353      26.036  31.262  59.700  1.00 99.51           N  
ANISOU 2717  N   LYS A 353    12485  14177  11150   -212  -2429    129       N  
ATOM   2718  CA  LYS A 353      27.264  31.167  60.491  1.00 79.24           C  
ANISOU 2718  CA  LYS A 353     9877  11677   8554   -340  -2778    176       C  
ATOM   2719  C   LYS A 353      27.886  29.768  60.426  1.00 79.85           C  
ANISOU 2719  C   LYS A 353     9645  11819   8875    -87  -3069    136       C  
ATOM   2720  O   LYS A 353      28.630  29.372  61.332  1.00107.37           O  
ANISOU 2720  O   LYS A 353    13183  15252  12359   -130  -3431    205       O  
ATOM   2721  CB  LYS A 353      27.027  31.570  61.956  1.00 83.75           C  
ANISOU 2721  CB  LYS A 353    10987  11978   8856   -578  -2868    294       C  
ATOM   2722  CG  LYS A 353      26.889  33.072  62.215  1.00 85.33           C  
ANISOU 2722  CG  LYS A 353    11483  12123   8815   -876  -2678    320       C  
ATOM   2723  CD  LYS A 353      26.382  33.324  63.638  1.00106.80           C  
ANISOU 2723  CD  LYS A 353    14810  14521  11247  -1080  -2677    402       C  
ATOM   2724  CE  LYS A 353      26.584  34.766  64.105  1.00 98.49           C  
ANISOU 2724  CE  LYS A 353    14085  13399   9936  -1414  -2592    418       C  
ATOM   2725  NZ  LYS A 353      28.011  35.110  64.368  1.00 81.26           N  
ANISOU 2725  NZ  LYS A 353    11763  11404   7707  -1641  -2970    446       N  
ATOM   2726  N   GLY A 354      27.593  29.005  59.369  1.00 82.30           N  
ANISOU 2726  N   GLY A 354     9657  12220   9393    180  -2942     24       N  
ATOM   2727  CA  GLY A 354      28.109  27.663  59.201  1.00 89.80           C  
ANISOU 2727  CA  GLY A 354    10325  13195  10600    456  -3175    -42       C  
ATOM   2728  C   GLY A 354      27.229  26.548  59.732  1.00 88.83           C  
ANISOU 2728  C   GLY A 354    10483  12767  10500    613  -3232      6       C  
ATOM   2729  O   GLY A 354      27.575  25.371  59.557  1.00 82.18           O  
ANISOU 2729  O   GLY A 354     9449  11895   9880    863  -3423    -50       O  
ATOM   2730  N   ASP A 355      26.106  26.872  60.365  1.00 87.10           N  
ANISOU 2730  N   ASP A 355    10710  12308  10075    470  -3050     98       N  
ATOM   2731  CA  ASP A 355      25.254  25.881  61.012  1.00 89.25           C  
ANISOU 2731  CA  ASP A 355    11300  12273  10338    541  -3070    156       C  
ATOM   2732  C   ASP A 355      24.267  25.317  59.995  1.00 93.23           C  
ANISOU 2732  C   ASP A 355    11652  12766  11007    726  -2813     42       C  
ATOM   2733  O   ASP A 355      23.450  26.060  59.441  1.00 87.32           O  
ANISOU 2733  O   ASP A 355    10898  12062  10215    665  -2508      2       O  
ATOM   2734  CB  ASP A 355      24.517  26.517  62.191  1.00 86.77           C  
ANISOU 2734  CB  ASP A 355    11526  11712   9729    268  -2939    281       C  
ATOM   2735  CG  ASP A 355      23.937  25.495  63.149  1.00 93.64           C  
ANISOU 2735  CG  ASP A 355    12796  12252  10531    260  -3017    373       C  
ATOM   2736  OD1 ASP A 355      23.772  24.320  62.758  1.00 97.24           O  
ANISOU 2736  OD1 ASP A 355    13119  12638  11188    476  -3097    333       O  
ATOM   2737  OD2 ASP A 355      23.636  25.876  64.300  1.00 90.59           O1-
ANISOU 2737  OD2 ASP A 355    12898  11657   9864     13  -2979    481       O1-
ATOM   2738  N   PHE A 356      24.343  24.008  59.753  1.00 96.12           N  
ANISOU 2738  N   PHE A 356    11903  13049  11568    953  -2965    -12       N  
ATOM   2739  CA  PHE A 356      23.446  23.319  58.831  1.00 82.45           C  
ANISOU 2739  CA  PHE A 356    10054  11281   9994   1113  -2777   -130       C  
ATOM   2740  C   PHE A 356      22.838  22.116  59.532  1.00 86.56           C  
ANISOU 2740  C   PHE A 356    10866  11468  10556   1154  -2866    -71       C  
ATOM   2741  O   PHE A 356      23.566  21.286  60.085  1.00110.97           O  
ANISOU 2741  O   PHE A 356    14025  14434  13703   1254  -3182    -18       O  
ATOM   2742  CB  PHE A 356      24.180  22.868  57.566  1.00 79.92           C  
ANISOU 2742  CB  PHE A 356     9284  11200   9881   1351  -2829   -307       C  
ATOM   2743  CG  PHE A 356      24.830  23.986  56.811  1.00 80.91           C  
ANISOU 2743  CG  PHE A 356     9136  11654   9952   1279  -2715   -368       C  
ATOM   2744  CD1 PHE A 356      24.076  24.820  56.005  1.00 90.99           C  
ANISOU 2744  CD1 PHE A 356    10402  13035  11134   1192  -2435   -405       C  
ATOM   2745  CD2 PHE A 356      26.195  24.196  56.896  1.00 91.06           C  
ANISOU 2745  CD2 PHE A 356    10171  13132  11294   1289  -2901   -386       C  
ATOM   2746  CE1 PHE A 356      24.670  25.849  55.304  1.00 91.41           C  
ANISOU 2746  CE1 PHE A 356    10268  13358  11105   1097  -2328   -443       C  
ATOM   2747  CE2 PHE A 356      26.795  25.224  56.197  1.00 92.93           C  
ANISOU 2747  CE2 PHE A 356    10169  13667  11474   1176  -2762   -444       C  
ATOM   2748  CZ  PHE A 356      26.031  26.051  55.399  1.00 93.70           C  
ANISOU 2748  CZ  PHE A 356    10325  13844  11431   1070  -2466   -465       C  
ATOM   2749  N   ARG A 357      21.509  22.016  59.505  1.00 94.47           N  
ANISOU 2749  N   ARG A 357    12033  12311  11549   1073  -2601    -78       N  
ATOM   2750  CA  ARG A 357      20.806  20.962  60.221  1.00 95.57           C  
ANISOU 2750  CA  ARG A 357    12492  12116  11702   1035  -2617    -16       C  
ATOM   2751  C   ARG A 357      19.658  20.417  59.385  1.00 99.49           C  
ANISOU 2751  C   ARG A 357    12863  12559  12377   1092  -2402   -138       C  
ATOM   2752  O   ARG A 357      19.092  21.115  58.540  1.00 90.28           O  
ANISOU 2752  O   ARG A 357    11472  11570  11262   1090  -2192   -227       O  
ATOM   2753  CB  ARG A 357      20.257  21.456  61.564  1.00 91.61           C  
ANISOU 2753  CB  ARG A 357    12459  11399  10950    747  -2481    139       C  
ATOM   2754  CG  ARG A 357      21.279  22.140  62.444  1.00100.62           C  
ANISOU 2754  CG  ARG A 357    13786  12581  11863    629  -2697    262       C  
ATOM   2755  CD  ARG A 357      20.643  22.636  63.721  1.00107.96           C  
ANISOU 2755  CD  ARG A 357    15239  13281  12502    322  -2508    384       C  
ATOM   2756  NE  ARG A 357      21.528  23.525  64.460  1.00 93.81           N  
ANISOU 2756  NE  ARG A 357    13631  11553  10460    167  -2684    478       N  
ATOM   2757  CZ  ARG A 357      21.248  24.028  65.654  1.00 97.38           C  
ANISOU 2757  CZ  ARG A 357    14597  11810  10592   -120  -2578    580       C  
ATOM   2758  NH1 ARG A 357      20.123  23.728  66.280  1.00 97.78           N  
ANISOU 2758  NH1 ARG A 357    15021  11594  10538   -284  -2259    602       N  
ATOM   2759  NH2 ARG A 357      22.116  24.852  66.233  1.00 98.19           N  
ANISOU 2759  NH2 ARG A 357    14851  11986  10472   -268  -2778    649       N  
ATOM   2760  N   ILE A 358      19.320  19.156  59.642  1.00 92.77           N  
ANISOU 2760  N   ILE A 358    12184  11444  11622   1130  -2488   -132       N  
ATOM   2761  CA  ILE A 358      18.145  18.506  59.074  1.00 88.74           C  
ANISOU 2761  CA  ILE A 358    11622  10817  11276   1119  -2307   -233       C  
ATOM   2762  C   ILE A 358      17.269  18.043  60.228  1.00 95.15           C  
ANISOU 2762  C   ILE A 358    12856  11289  12009    877  -2167   -113       C  
ATOM   2763  O   ILE A 358      17.724  17.291  61.100  1.00107.55           O  
ANISOU 2763  O   ILE A 358    14766  12614  13485    849  -2369      7       O  
ATOM   2764  CB  ILE A 358      18.515  17.323  58.165  1.00 87.23           C  
ANISOU 2764  CB  ILE A 358    11251  10603  11289   1365  -2507   -376       C  
ATOM   2765  CG1 ILE A 358      19.007  17.814  56.803  1.00 83.15           C  
ANISOU 2765  CG1 ILE A 358    10315  10432  10845   1548  -2506   -544       C  
ATOM   2766  CG2 ILE A 358      17.322  16.390  57.997  1.00 90.08           C  
ANISOU 2766  CG2 ILE A 358    11713  10723  11791   1281  -2386   -436       C  
ATOM   2767  CD1 ILE A 358      19.284  16.693  55.817  1.00 82.51           C  
ANISOU 2767  CD1 ILE A 358    10074  10328  10948   1779  -2635   -731       C  
ATOM   2768  N   LEU A 359      16.022  18.499  60.240  1.00 86.86           N  
ANISOU 2768  N   LEU A 359    11787  10214  11002    698  -1823   -143       N  
ATOM   2769  CA  LEU A 359      15.014  18.026  61.179  1.00 90.28           C  
ANISOU 2769  CA  LEU A 359    12556  10340  11404    438  -1588    -75       C  
ATOM   2770  C   LEU A 359      14.157  16.991  60.460  1.00 94.18           C  
ANISOU 2770  C   LEU A 359    12896  10724  12166    454  -1547   -197       C  
ATOM   2771  O   LEU A 359      13.485  17.315  59.475  1.00113.28           O  
ANISOU 2771  O   LEU A 359    14940  13316  14786    510  -1435   -334       O  
ATOM   2772  CB  LEU A 359      14.170  19.195  61.690  1.00 91.00           C  
ANISOU 2772  CB  LEU A 359    12683  10467  11427    229  -1195    -62       C  
ATOM   2773  CG  LEU A 359      13.379  19.091  62.997  1.00 93.20           C  
ANISOU 2773  CG  LEU A 359    13397  10454  11561    -96   -871     25       C  
ATOM   2774  CD1 LEU A 359      12.808  20.448  63.356  1.00 94.11           C  
ANISOU 2774  CD1 LEU A 359    13483  10654  11622   -221   -499     -1       C  
ATOM   2775  CD2 LEU A 359      12.253  18.083  62.874  1.00103.19           C  
ANISOU 2775  CD2 LEU A 359    14634  11519  13054   -226   -683    -42       C  
ATOM   2776  N   MET A 360      14.182  15.751  60.944  1.00103.60           N  
ANISOU 2776  N   MET A 360    14401  11610  13353    395  -1669   -140       N  
ATOM   2777  CA  MET A 360      13.473  14.671  60.260  1.00109.80           C  
ANISOU 2777  CA  MET A 360    15077  12258  14384    396  -1672   -262       C  
ATOM   2778  C   MET A 360      13.242  13.521  61.225  1.00109.80           C  
ANISOU 2778  C   MET A 360    15570  11838  14312    195  -1683   -144       C  
ATOM   2779  O   MET A 360      14.204  12.914  61.705  1.00121.18           O  
ANISOU 2779  O   MET A 360    17320  13103  15619    303  -1993    -30       O  
ATOM   2780  CB  MET A 360      14.263  14.203  59.040  1.00102.12           C  
ANISOU 2780  CB  MET A 360    13818  11436  13546    727  -1987   -403       C  
ATOM   2781  CG  MET A 360      13.542  13.171  58.201  1.00104.54           C  
ANISOU 2781  CG  MET A 360    14012  11619  14091    727  -2004   -561       C  
ATOM   2782  SD  MET A 360      14.404  12.809  56.664  1.00110.46           S  
ANISOU 2782  SD  MET A 360    14434  12581  14957   1097  -2288   -776       S  
ATOM   2783  CE  MET A 360      13.399  11.466  56.044  1.00106.40           C  
ANISOU 2783  CE  MET A 360    13960  11798  14670    992  -2297   -934       C  
ATOM   2784  N   CYS A 361      11.972  13.213  61.495  1.00106.12           N  
ANISOU 2784  N   CYS A 361    15171  11200  13951   -102  -1357   -170       N  
ATOM   2785  CA  CYS A 361      11.596  12.104  62.374  1.00107.32           C  
ANISOU 2785  CA  CYS A 361    15819  10928  14028   -364  -1304    -61       C  
ATOM   2786  C   CYS A 361      11.679  10.793  61.587  1.00107.65           C  
ANISOU 2786  C   CYS A 361    15831  10793  14277   -229  -1575   -159       C  
ATOM   2787  O   CYS A 361      10.681  10.143  61.271  1.00126.56           O  
ANISOU 2787  O   CYS A 361    18160  13048  16877   -423  -1414   -257       O  
ATOM   2788  CB  CYS A 361      10.202  12.331  62.944  1.00114.59           C  
ANISOU 2788  CB  CYS A 361    16779  11753  15006   -764   -791    -76       C  
ATOM   2789  SG  CYS A 361       9.984  13.919  63.788  1.00127.02           S  
ANISOU 2789  SG  CYS A 361    18370  13515  16375   -908   -399    -20       S  
ATOM   2790  N   THR A 362      12.915  10.403  61.287  1.00 96.84           N  
ANISOU 2790  N   THR A 362    14508   9420  12868    105  -1993   -143       N  
ATOM   2791  CA  THR A 362      13.168   9.336  60.328  1.00 97.25           C  
ANISOU 2791  CA  THR A 362    14453   9364  13133    328  -2256   -291       C  
ATOM   2792  C   THR A 362      12.674   7.985  60.836  1.00103.70           C  
ANISOU 2792  C   THR A 362    15734   9689  13979    109  -2276   -226       C  
ATOM   2793  O   THR A 362      12.918   7.611  61.987  1.00109.09           O  
ANISOU 2793  O   THR A 362    16948  10054  14446    -37  -2336     -8       O  
ATOM   2794  CB  THR A 362      14.662   9.256  60.019  1.00 93.98           C  
ANISOU 2794  CB  THR A 362    13977   9038  12691    746  -2657   -296       C  
ATOM   2795  OG1 THR A 362      15.154  10.561  59.686  1.00 91.84           O  
ANISOU 2795  OG1 THR A 362    13335   9205  12356    885  -2614   -327       O  
ATOM   2796  CG2 THR A 362      14.920   8.317  58.857  1.00 93.43           C  
ANISOU 2796  CG2 THR A 362    13726   8914  12859   1012  -2860   -513       C  
ATOM   2797  N   LYS A 363      11.973   7.259  59.969  1.00126.62           N  
ANISOU 2797  N   LYS A 363    18470  12514  17127     61  -2242   -412       N  
ATOM   2798  CA  LYS A 363      11.695   5.842  60.146  1.00133.52           C  
ANISOU 2798  CA  LYS A 363    19748  12910  18072    -74  -2344   -398       C  
ATOM   2799  C   LYS A 363      12.606   5.031  59.229  1.00138.78           C  
ANISOU 2799  C   LYS A 363    20358  13494  18879    339  -2732   -550       C  
ATOM   2800  O   LYS A 363      13.354   5.574  58.414  1.00143.37           O  
ANISOU 2800  O   LYS A 363    20551  14415  19506    689  -2867   -683       O  
ATOM   2801  CB  LYS A 363      10.225   5.525  59.846  1.00140.84           C  
ANISOU 2801  CB  LYS A 363    20546  13769  19197   -462  -2029   -519       C  
ATOM   2802  CG  LYS A 363       9.217   6.510  60.415  1.00145.73           C  
ANISOU 2802  CG  LYS A 363    20995  14582  19793   -809  -1578   -467       C  
ATOM   2803  CD  LYS A 363       9.162   6.450  61.931  1.00142.07           C  
ANISOU 2803  CD  LYS A 363    21106  13826  19048  -1116  -1383   -212       C  
ATOM   2804  CE  LYS A 363       8.644   7.757  62.507  1.00150.10           C  
ANISOU 2804  CE  LYS A 363    21939  15120  19973  -1298   -975   -170       C  
ATOM   2805  NZ  LYS A 363       7.504   8.293  61.710  1.00165.81           N  
ANISOU 2805  NZ  LYS A 363    23310  17394  22297  -1405   -690   -381       N  
ATOM   2806  N   VAL A 364      12.533   3.709  59.363  1.00131.64           N  
ANISOU 2806  N   VAL A 364    19862  12112  18043    284  -2885   -540       N  
ATOM   2807  CA  VAL A 364      13.320   2.829  58.507  1.00126.84           C  
ANISOU 2807  CA  VAL A 364    19238  11356  17599    673  -3218   -716       C  
ATOM   2808  C   VAL A 364      12.432   2.328  57.375  1.00142.31           C  
ANISOU 2808  C   VAL A 364    20975  13322  19773    550  -3113   -992       C  
ATOM   2809  O   VAL A 364      11.969   1.182  57.386  1.00139.74           O  
ANISOU 2809  O   VAL A 364    20989  12562  19543    379  -3161  -1029       O  
ATOM   2810  CB  VAL A 364      13.940   1.665  59.303  1.00115.69           C  
ANISOU 2810  CB  VAL A 364    18442   9371  16145    763  -3525   -543       C  
ATOM   2811  CG1 VAL A 364      14.928   0.894  58.439  1.00126.00           C  
ANISOU 2811  CG1 VAL A 364    19670  10549  17654   1258  -3865   -745       C  
ATOM   2812  CG2 VAL A 364      14.632   2.189  60.552  1.00115.34           C  
ANISOU 2812  CG2 VAL A 364    18680   9299  15846    783  -3644   -235       C  
ATOM   2813  N   THR A 365      12.173   3.196  56.402  1.00145.49           N  
ANISOU 2813  N   THR A 365    20840  14202  20238    611  -2991  -1180       N  
ATOM   2814  CA  THR A 365      11.390   2.864  55.222  1.00133.24           C  
ANISOU 2814  CA  THR A 365    19043  12720  18864    512  -2951  -1451       C  
ATOM   2815  C   THR A 365      12.130   3.359  53.988  1.00130.11           C  
ANISOU 2815  C   THR A 365    18254  12707  18474    898  -3072  -1679       C  
ATOM   2816  O   THR A 365      13.090   4.129  54.080  1.00130.88           O  
ANISOU 2816  O   THR A 365    18190  13074  18463   1181  -3116  -1618       O  
ATOM   2817  CB  THR A 365       9.986   3.483  55.278  1.00137.63           C  
ANISOU 2817  CB  THR A 365    19338  13464  19490     80  -2649  -1440       C  
ATOM   2818  OG1 THR A 365      10.098   4.909  55.375  1.00129.97           O  
ANISOU 2818  OG1 THR A 365    18011  12949  18423    155  -2506  -1363       O  
ATOM   2819  CG2 THR A 365       9.205   2.953  56.475  1.00133.83           C  
ANISOU 2819  CG2 THR A 365    19247  12600  19001   -355  -2452  -1243       C  
ATOM   2820  N   MET A 366      11.679   2.907  52.816  1.00129.57           N  
ANISOU 2820  N   MET A 366    18054  12657  18518    876  -3119  -1950       N  
ATOM   2821  CA  MET A 366      12.280   3.391  51.579  1.00126.95           C  
ANISOU 2821  CA  MET A 366    17399  12693  18145   1181  -3189  -2181       C  
ATOM   2822  C   MET A 366      11.879   4.831  51.287  1.00122.61           C  
ANISOU 2822  C   MET A 366    16421  12652  17513   1097  -3039  -2136       C  
ATOM   2823  O   MET A 366      12.683   5.598  50.744  1.00120.52           O  
ANISOU 2823  O   MET A 366    15926  12730  17134   1364  -3053  -2194       O  
ATOM   2824  CB  MET A 366      11.893   2.486  50.408  1.00132.18           C  
ANISOU 2824  CB  MET A 366    18119  13206  18898   1152  -3295  -2492       C  
ATOM   2825  CG  MET A 366      12.523   2.900  49.084  1.00127.73           C  
ANISOU 2825  CG  MET A 366    17306  12989  18238   1436  -3341  -2753       C  
ATOM   2826  SD  MET A 366      12.129   1.787  47.723  1.00133.88           S  
ANISOU 2826  SD  MET A 366    18252  13554  19061   1388  -3472  -3142       S  
ATOM   2827  CE  MET A 366      13.034   2.554  46.381  1.00133.23           C  
ANISOU 2827  CE  MET A 366    17906  13944  18773   1716  -3445  -3389       C  
ATOM   2828  N   ASP A 367      10.656   5.220  51.650  1.00132.07           N  
ANISOU 2828  N   ASP A 367    17506  13889  18786    729  -2882  -2036       N  
ATOM   2829  CA  ASP A 367      10.192   6.572  51.359  1.00137.92           C  
ANISOU 2829  CA  ASP A 367    17844  15066  19494    668  -2760  -1998       C  
ATOM   2830  C   ASP A 367      10.916   7.617  52.201  1.00131.43           C  
ANISOU 2830  C   ASP A 367    16975  14442  18519    806  -2648  -1780       C  
ATOM   2831  O   ASP A 367      11.047   8.769  51.772  1.00126.11           O  
ANISOU 2831  O   ASP A 367    16006  14145  17763    900  -2602  -1776       O  
ATOM   2832  CB  ASP A 367       8.681   6.666  51.569  1.00146.96           C  
ANISOU 2832  CB  ASP A 367    18835  16172  20831    262  -2615  -1968       C  
ATOM   2833  CG  ASP A 367       7.894   6.052  50.424  1.00155.17           C  
ANISOU 2833  CG  ASP A 367    19764  17177  22016    120  -2773  -2210       C  
ATOM   2834  OD1 ASP A 367       8.374   6.110  49.272  1.00137.86           O  
ANISOU 2834  OD1 ASP A 367    17500  15163  19719    337  -2955  -2396       O  
ATOM   2835  OD2 ASP A 367       6.798   5.508  50.676  1.00154.10           O1-
ANISOU 2835  OD2 ASP A 367    19628  16834  22089   -232  -2710  -2222       O1-
ATOM   2836  N   ASP A 368      11.385   7.247  53.394  1.00132.18           N  
ANISOU 2836  N   ASP A 368    17392  14274  18557    800  -2625  -1592       N  
ATOM   2837  CA  ASP A 368      12.206   8.143  54.199  1.00127.52           C  
ANISOU 2837  CA  ASP A 368    16812  13843  17796    932  -2578  -1397       C  
ATOM   2838  C   ASP A 368      13.694   8.002  53.910  1.00115.91           C  
ANISOU 2838  C   ASP A 368    15362  12434  16246   1330  -2794  -1448       C  
ATOM   2839  O   ASP A 368      14.472   8.876  54.308  1.00109.10           O  
ANISOU 2839  O   ASP A 368    14409  11789  15253   1461  -2792  -1330       O  
ATOM   2840  CB  ASP A 368      11.948   7.914  55.693  1.00129.16           C  
ANISOU 2840  CB  ASP A 368    17389  13746  17940    692  -2460  -1151       C  
ATOM   2841  CG  ASP A 368      10.648   8.542  56.162  1.00140.58           C  
ANISOU 2841  CG  ASP A 368    18718  15254  19444    322  -2138  -1080       C  
ATOM   2842  OD1 ASP A 368       9.907   9.079  55.312  1.00141.78           O  
ANISOU 2842  OD1 ASP A 368    18479  15659  19732    271  -2061  -1217       O  
ATOM   2843  OD2 ASP A 368      10.369   8.507  57.379  1.00134.08           O1-
ANISOU 2843  OD2 ASP A 368    18196  14218  18530     83  -1961   -894       O1-
ATOM   2844  N   PHE A 369      14.107   6.927  53.236  1.00120.12           N  
ANISOU 2844  N   PHE A 369    15997  12770  16873   1518  -2970  -1636       N  
ATOM   2845  CA  PHE A 369      15.480   6.834  52.752  1.00117.90           C  
ANISOU 2845  CA  PHE A 369    15627  12593  16578   1921  -3128  -1751       C  
ATOM   2846  C   PHE A 369      15.721   7.829  51.624  1.00110.72           C  
ANISOU 2846  C   PHE A 369    14322  12161  15584   2031  -3042  -1910       C  
ATOM   2847  O   PHE A 369      16.707   8.576  51.638  1.00104.68           O  
ANISOU 2847  O   PHE A 369    13374  11662  14736   2229  -3044  -1876       O  
ATOM   2848  CB  PHE A 369      15.773   5.405  52.291  1.00121.07           C  
ANISOU 2848  CB  PHE A 369    16252  12625  17124   2096  -3296  -1946       C  
ATOM   2849  CG  PHE A 369      17.035   5.266  51.486  1.00112.04           C  
ANISOU 2849  CG  PHE A 369    14934  11615  16021   2515  -3390  -2163       C  
ATOM   2850  CD1 PHE A 369      18.267   5.178  52.111  1.00124.40           C  
ANISOU 2850  CD1 PHE A 369    16513  13114  17640   2819  -3544  -2070       C  
ATOM   2851  CD2 PHE A 369      16.987   5.206  50.102  1.00107.06           C  
ANISOU 2851  CD2 PHE A 369    14130  11168  15380   2594  -3324  -2470       C  
ATOM   2852  CE1 PHE A 369      19.429   5.045  51.371  1.00121.84           C  
ANISOU 2852  CE1 PHE A 369    15963  12920  17410   3207  -3590  -2297       C  
ATOM   2853  CE2 PHE A 369      18.144   5.074  49.358  1.00112.15           C  
ANISOU 2853  CE2 PHE A 369    14618  11936  16059   2959  -3338  -2699       C  
ATOM   2854  CZ  PHE A 369      19.366   4.990  49.993  1.00119.54           C  
ANISOU 2854  CZ  PHE A 369    15502  12816  17101   3273  -3451  -2621       C  
ATOM   2855  N   LEU A 370      14.821   7.850  50.638  1.00101.62           N  
ANISOU 2855  N   LEU A 370    13054  11113  14446   1881  -2983  -2077       N  
ATOM   2856  CA  LEU A 370      14.911   8.824  49.555  1.00 94.51           C  
ANISOU 2856  CA  LEU A 370    11852  10638  13421   1934  -2918  -2200       C  
ATOM   2857  C   LEU A 370      14.801  10.246  50.088  1.00 93.42           C  
ANISOU 2857  C   LEU A 370    11525  10794  13177   1834  -2791  -1982       C  
ATOM   2858  O   LEU A 370      15.560  11.135  49.684  1.00 93.46           O  
ANISOU 2858  O   LEU A 370    11344  11119  13049   1975  -2752  -1993       O  
ATOM   2859  CB  LEU A 370      13.817   8.556  48.523  1.00 99.32           C  
ANISOU 2859  CB  LEU A 370    12424  11253  14058   1745  -2945  -2380       C  
ATOM   2860  CG  LEU A 370      13.847   7.186  47.852  1.00 96.48           C  
ANISOU 2860  CG  LEU A 370    12282  10600  13777   1808  -3065  -2637       C  
ATOM   2861  CD1 LEU A 370      12.675   7.040  46.895  1.00102.00           C  
ANISOU 2861  CD1 LEU A 370    12942  11325  14487   1561  -3130  -2793       C  
ATOM   2862  CD2 LEU A 370      15.170   7.006  47.133  1.00 98.59           C  
ANISOU 2862  CD2 LEU A 370    12530  10972  13956   2160  -3071  -2844       C  
ATOM   2863  N   THR A 371      13.851  10.478  50.998  1.00 88.97           N  
ANISOU 2863  N   THR A 371    11020  10112  12673   1575  -2699  -1794       N  
ATOM   2864  CA  THR A 371      13.660  11.811  51.558  1.00 87.22           C  
ANISOU 2864  CA  THR A 371    10655  10120  12366   1475  -2552  -1605       C  
ATOM   2865  C   THR A 371      14.930  12.318  52.230  1.00 84.59           C  
ANISOU 2865  C   THR A 371    10357   9884  11897   1651  -2569  -1477       C  
ATOM   2866  O   THR A 371      15.206  13.522  52.211  1.00 81.69           O  
ANISOU 2866  O   THR A 371     9826   9803  11410   1662  -2487  -1402       O  
ATOM   2867  CB  THR A 371      12.496  11.791  52.552  1.00 90.20           C  
ANISOU 2867  CB  THR A 371    11129  10292  12849   1173  -2400  -1455       C  
ATOM   2868  OG1 THR A 371      11.325  11.282  51.903  1.00 93.33           O  
ANISOU 2868  OG1 THR A 371    11435  10606  13422    995  -2409  -1588       O  
ATOM   2869  CG2 THR A 371      12.194  13.192  53.059  1.00 92.05           C  
ANISOU 2869  CG2 THR A 371    11213  10744  13016   1078  -2214  -1301       C  
ATOM   2870  N   ALA A 372      15.724  11.412  52.808  1.00 98.41           N  
ANISOU 2870  N   ALA A 372    12323  11388  13680   1790  -2705  -1452       N  
ATOM   2871  CA  ALA A 372      16.974  11.817  53.442  1.00101.87           C  
ANISOU 2871  CA  ALA A 372    12765  11912  14029   1964  -2789  -1336       C  
ATOM   2872  C   ALA A 372      17.972  12.339  52.415  1.00100.22           C  
ANISOU 2872  C   ALA A 372    12255  12049  13775   2199  -2805  -1497       C  
ATOM   2873  O   ALA A 372      18.732  13.271  52.700  1.00104.45           O  
ANISOU 2873  O   ALA A 372    12659  12818  14210   2244  -2789  -1404       O  
ATOM   2874  CB  ALA A 372      17.568  10.654  54.231  1.00106.90           C  
ANISOU 2874  CB  ALA A 372    13697  12173  14748   2086  -2995  -1273       C  
ATOM   2875  N   HIS A 373      17.996  11.744  51.219  1.00 98.67           N  
ANISOU 2875  N   HIS A 373    11970  11883  13638   2324  -2819  -1750       N  
ATOM   2876  CA  HIS A 373      18.787  12.310  50.131  1.00 97.68           C  
ANISOU 2876  CA  HIS A 373    11582  12105  13426   2482  -2755  -1923       C  
ATOM   2877  C   HIS A 373      18.214  13.649  49.685  1.00100.92           C  
ANISOU 2877  C   HIS A 373    11846  12832  13666   2295  -2612  -1858       C  
ATOM   2878  O   HIS A 373      18.951  14.629  49.514  1.00101.17           O  
ANISOU 2878  O   HIS A 373    11710  13155  13575   2334  -2541  -1826       O  
ATOM   2879  CB  HIS A 373      18.832  11.345  48.948  1.00 92.48           C  
ANISOU 2879  CB  HIS A 373    10939  11376  12825   2621  -2772  -2226       C  
ATOM   2880  CG  HIS A 373      19.623  10.102  49.202  1.00 93.74           C  
ANISOU 2880  CG  HIS A 373    11204  11240  13174   2883  -2905  -2335       C  
ATOM   2881  ND1 HIS A 373      19.213   9.120  50.078  1.00 96.23           N  
ANISOU 2881  ND1 HIS A 373    11802  11131  13629   2851  -3051  -2230       N  
ATOM   2882  CD2 HIS A 373      20.800   9.679  48.685  1.00 99.08           C  
ANISOU 2882  CD2 HIS A 373    11743  11963  13941   3190  -2907  -2547       C  
ATOM   2883  CE1 HIS A 373      20.106   8.147  50.091  1.00102.30           C  
ANISOU 2883  CE1 HIS A 373    12624  11676  14569   3149  -3180  -2357       C  
ATOM   2884  NE2 HIS A 373      21.079   8.462  49.255  1.00 95.62           N  
ANISOU 2884  NE2 HIS A 373    11496  11116  13720   3374  -3088  -2562       N  
ATOM   2885  N   HIS A 374      16.894  13.698  49.488  1.00106.62           N  
ANISOU 2885  N   HIS A 374    12624  13485  14402   2089  -2584  -1838       N  
ATOM   2886  CA  HIS A 374      16.234  14.912  49.020  1.00112.77           C  
ANISOU 2886  CA  HIS A 374    13269  14513  15065   1940  -2496  -1777       C  
ATOM   2887  C   HIS A 374      16.497  16.086  49.957  1.00111.64           C  
ANISOU 2887  C   HIS A 374    13084  14489  14843   1874  -2401  -1548       C  
ATOM   2888  O   HIS A 374      16.880  17.175  49.514  1.00119.32           O  
ANISOU 2888  O   HIS A 374    13935  15736  15666   1876  -2337  -1522       O  
ATOM   2889  CB  HIS A 374      14.736  14.640  48.871  1.00120.28           C  
ANISOU 2889  CB  HIS A 374    14248  15316  16138   1742  -2519  -1782       C  
ATOM   2890  CG  HIS A 374      13.915  15.863  48.641  1.00116.24           C  
ANISOU 2890  CG  HIS A 374    13590  14988  15588   1606  -2462  -1682       C  
ATOM   2891  ND1 HIS A 374      13.460  16.237  47.394  1.00114.07           N  
ANISOU 2891  ND1 HIS A 374    13223  14882  15235   1582  -2549  -1787       N  
ATOM   2892  CD2 HIS A 374      13.441  16.784  49.509  1.00116.80           C  
ANISOU 2892  CD2 HIS A 374    13613  15069  15695   1494  -2341  -1488       C  
ATOM   2893  CE1 HIS A 374      12.758  17.349  47.502  1.00115.22           C  
ANISOU 2893  CE1 HIS A 374    13249  15129  15399   1487  -2512  -1648       C  
ATOM   2894  NE2 HIS A 374      12.711  17.685  48.778  1.00117.28           N  
ANISOU 2894  NE2 HIS A 374    13524  15292  15745   1436  -2362  -1480       N  
ATOM   2895  N   GLU A 375      16.299  15.884  51.262  1.00 96.80           N  
ANISOU 2895  N   GLU A 375    11353  12389  13037   1790  -2385  -1383       N  
ATOM   2896  CA  GLU A 375      16.541  16.964  52.215  1.00 92.57           C  
ANISOU 2896  CA  GLU A 375    10840  11935  12399   1705  -2294  -1181       C  
ATOM   2897  C   GLU A 375      18.020  17.326  52.283  1.00 92.29           C  
ANISOU 2897  C   GLU A 375    10731  12080  12255   1855  -2359  -1172       C  
ATOM   2898  O   GLU A 375      18.369  18.510  52.359  1.00 81.80           O  
ANISOU 2898  O   GLU A 375     9322  10964  10794   1800  -2283  -1086       O  
ATOM   2899  CB  GLU A 375      16.012  16.575  53.595  1.00 95.01           C  
ANISOU 2899  CB  GLU A 375    11393  11944  12762   1552  -2250  -1022       C  
ATOM   2900  CG  GLU A 375      14.501  16.434  53.656  1.00 89.75           C  
ANISOU 2900  CG  GLU A 375    10739  11130  12233   1352  -2115  -1023       C  
ATOM   2901  CD  GLU A 375      13.782  17.726  53.308  1.00 98.44           C  
ANISOU 2901  CD  GLU A 375    11644  12432  13326   1268  -1970   -994       C  
ATOM   2902  OE1 GLU A 375      14.298  18.810  53.653  1.00107.65           O  
ANISOU 2902  OE1 GLU A 375    12807  13748  14348   1275  -1902   -891       O  
ATOM   2903  OE2 GLU A 375      12.699  17.657  52.690  1.00117.98           O1-
ANISOU 2903  OE2 GLU A 375    13973  14899  15957   1196  -1948  -1073       O1-
ATOM   2904  N   MET A 376      18.904  16.326  52.253  1.00 96.87           N  
ANISOU 2904  N   MET A 376    11320  12567  12918   2046  -2502  -1267       N  
ATOM   2905  CA  MET A 376      20.334  16.619  52.235  1.00 98.37           C  
ANISOU 2905  CA  MET A 376    11351  12948  13076   2204  -2569  -1290       C  
ATOM   2906  C   MET A 376      20.740  17.344  50.959  1.00 95.64           C  
ANISOU 2906  C   MET A 376    10763  12950  12628   2241  -2444  -1440       C  
ATOM   2907  O   MET A 376      21.744  18.065  50.947  1.00 94.01           O  
ANISOU 2907  O   MET A 376    10391  12974  12354   2267  -2417  -1424       O  
ATOM   2908  CB  MET A 376      21.147  15.334  52.394  1.00 97.52           C  
ANISOU 2908  CB  MET A 376    11264  12643  13147   2445  -2758  -1386       C  
ATOM   2909  CG  MET A 376      22.626  15.578  52.663  1.00101.58           C  
ANISOU 2909  CG  MET A 376    11576  13314  13706   2611  -2871  -1383       C  
ATOM   2910  SD  MET A 376      23.536  14.103  53.161  1.00108.99           S  
ANISOU 2910  SD  MET A 376    12554  13941  14915   2927  -3168  -1439       S  
ATOM   2911  CE  MET A 376      22.819  13.771  54.769  1.00105.19           C  
ANISOU 2911  CE  MET A 376    12539  13061  14366   2737  -3348  -1130       C  
ATOM   2912  N   GLY A 377      19.981  17.162  49.876  1.00101.56           N  
ANISOU 2912  N   GLY A 377    11508  13734  13348   2216  -2375  -1584       N  
ATOM   2913  CA  GLY A 377      20.244  17.930  48.669  1.00101.15           C  
ANISOU 2913  CA  GLY A 377    11316  13990  13128   2198  -2255  -1696       C  
ATOM   2914  C   GLY A 377      20.155  19.423  48.914  1.00 98.46           C  
ANISOU 2914  C   GLY A 377    10950  13835  12626   2027  -2165  -1512       C  
ATOM   2915  O   GLY A 377      20.996  20.195  48.446  1.00 94.28           O  
ANISOU 2915  O   GLY A 377    10299  13562  11960   2013  -2074  -1536       O  
ATOM   2916  N   HIS A 378      19.133  19.848  49.662  1.00 92.00           N  
ANISOU 2916  N   HIS A 378    10252  12872  11831   1884  -2166  -1336       N  
ATOM   2917  CA  HIS A 378      19.023  21.253  50.038  1.00 90.94           C  
ANISOU 2917  CA  HIS A 378    10131  12853  11570   1739  -2076  -1163       C  
ATOM   2918  C   HIS A 378      20.239  21.700  50.836  1.00 97.42           C  
ANISOU 2918  C   HIS A 378    10916  13763  12337   1736  -2080  -1076       C  
ATOM   2919  O   HIS A 378      20.755  22.805  50.631  1.00 98.92           O  
ANISOU 2919  O   HIS A 378    11050  14156  12379   1650  -2003  -1023       O  
ATOM   2920  CB  HIS A 378      17.754  21.484  50.857  1.00 84.04           C  
ANISOU 2920  CB  HIS A 378     9381  11766  10783   1613  -2038  -1022       C  
ATOM   2921  CG  HIS A 378      16.488  21.206  50.110  1.00 88.01           C  
ANISOU 2921  CG  HIS A 378     9857  12198  11384   1588  -2059  -1093       C  
ATOM   2922  ND1 HIS A 378      16.219  21.748  48.873  1.00104.14           N  
ANISOU 2922  ND1 HIS A 378    11832  14411  13327   1588  -2089  -1156       N  
ATOM   2923  CD2 HIS A 378      15.418  20.440  50.427  1.00110.22           C  
ANISOU 2923  CD2 HIS A 378    12706  14785  14387   1539  -2075  -1109       C  
ATOM   2924  CE1 HIS A 378      15.037  21.328  48.460  1.00105.67           C  
ANISOU 2924  CE1 HIS A 378    12000  14490  13660   1556  -2164  -1208       C  
ATOM   2925  NE2 HIS A 378      14.527  20.537  49.386  1.00116.11           N  
ANISOU 2925  NE2 HIS A 378    13359  15579  15176   1520  -2140  -1187       N  
ATOM   2926  N   ILE A 379      20.695  20.858  51.766  1.00100.13           N  
ANISOU 2926  N   ILE A 379    11310  13938  12799   1814  -2199  -1049       N  
ATOM   2927  CA  ILE A 379      21.859  21.193  52.582  1.00100.90           C  
ANISOU 2927  CA  ILE A 379    11365  14102  12869   1812  -2281   -962       C  
ATOM   2928  C   ILE A 379      23.066  21.468  51.694  1.00106.03           C  
ANISOU 2928  C   ILE A 379    11736  15053  13498   1895  -2245  -1101       C  
ATOM   2929  O   ILE A 379      23.800  22.442  51.896  1.00106.02           O  
ANISOU 2929  O   ILE A 379    11648  15236  13398   1785  -2213  -1031       O  
ATOM   2930  CB  ILE A 379      22.147  20.066  53.591  1.00 93.88           C  
ANISOU 2930  CB  ILE A 379    10598  12951  12122   1916  -2483   -916       C  
ATOM   2931  CG1 ILE A 379      20.981  19.907  54.570  1.00 82.74           C  
ANISOU 2931  CG1 ILE A 379     9504  11246  10688   1764  -2456   -766       C  
ATOM   2932  CG2 ILE A 379      23.437  20.338  54.345  1.00 95.75           C  
ANISOU 2932  CG2 ILE A 379    10756  13267  12358   1937  -2649   -838       C  
ATOM   2933  CD1 ILE A 379      20.776  21.096  55.481  1.00 83.27           C  
ANISOU 2933  CD1 ILE A 379     9734  11322  10582   1544  -2363   -586       C  
ATOM   2934  N   GLN A 380      23.282  20.613  50.690  1.00102.00           N  
ANISOU 2934  N   GLN A 380    11090  14589  13076   2067  -2223  -1317       N  
ATOM   2935  CA  GLN A 380      24.401  20.807  49.772  1.00100.38           C  
ANISOU 2935  CA  GLN A 380    10615  14672  12855   2136  -2114  -1490       C  
ATOM   2936  C   GLN A 380      24.289  22.136  49.035  1.00 99.82           C  
ANISOU 2936  C   GLN A 380    10546  14848  12532   1927  -1923  -1453       C  
ATOM   2937  O   GLN A 380      25.284  22.853  48.874  1.00 97.58           O  
ANISOU 2937  O   GLN A 380    10085  14802  12188   1848  -1830  -1466       O  
ATOM   2938  CB  GLN A 380      24.469  19.647  48.778  1.00100.48           C  
ANISOU 2938  CB  GLN A 380    10555  14652  12972   2342  -2075  -1755       C  
ATOM   2939  CG  GLN A 380      25.041  18.363  49.354  1.00101.76           C  
ANISOU 2939  CG  GLN A 380    10646  14602  13416   2598  -2257  -1834       C  
ATOM   2940  CD  GLN A 380      26.551  18.410  49.484  1.00 98.58           C  
ANISOU 2940  CD  GLN A 380     9898  14381  13175   2734  -2276  -1918       C  
ATOM   2941  OE1 GLN A 380      27.203  19.307  48.949  1.00 92.62           O  
ANISOU 2941  OE1 GLN A 380     8938  13939  12316   2622  -2092  -1968       O  
ATOM   2942  NE2 GLN A 380      27.114  17.445  50.200  1.00 98.89           N  
ANISOU 2942  NE2 GLN A 380     9870  14215  13489   2967  -2511  -1929       N  
ATOM   2943  N   TYR A 381      23.083  22.479  48.576  1.00 94.72           N  
ANISOU 2943  N   TYR A 381    10099  14136  11755   1828  -1877  -1402       N  
ATOM   2944  CA  TYR A 381      22.875  23.774  47.934  1.00 99.14           C  
ANISOU 2944  CA  TYR A 381    10726  14869  12074   1639  -1748  -1328       C  
ATOM   2945  C   TYR A 381      23.107  24.912  48.921  1.00 95.10           C  
ANISOU 2945  C   TYR A 381    10261  14368  11504   1474  -1747  -1116       C  
ATOM   2946  O   TYR A 381      23.670  25.953  48.561  1.00 96.47           O  
ANISOU 2946  O   TYR A 381    10410  14735  11511   1322  -1634  -1079       O  
ATOM   2947  CB  TYR A 381      21.462  23.839  47.348  1.00102.67           C  
ANISOU 2947  CB  TYR A 381    11359  15197  12454   1602  -1778  -1302       C  
ATOM   2948  CG  TYR A 381      21.286  24.787  46.177  1.00 97.39           C  
ANISOU 2948  CG  TYR A 381    10781  14698  11525   1474  -1691  -1299       C  
ATOM   2949  CD1 TYR A 381      22.291  25.669  45.805  1.00 95.21           C  
ANISOU 2949  CD1 TYR A 381    10460  14654  11062   1348  -1543  -1291       C  
ATOM   2950  CD2 TYR A 381      20.105  24.798  45.443  1.00 87.63           C  
ANISOU 2950  CD2 TYR A 381     9689  13376  10229   1458  -1780  -1296       C  
ATOM   2951  CE1 TYR A 381      22.124  26.534  44.738  1.00100.74           C  
ANISOU 2951  CE1 TYR A 381    11316  15476  11483   1204  -1469  -1266       C  
ATOM   2952  CE2 TYR A 381      19.931  25.659  44.374  1.00 87.03           C  
ANISOU 2952  CE2 TYR A 381     9754  13424   9890   1340  -1758  -1267       C  
ATOM   2953  CZ  TYR A 381      20.945  26.524  44.026  1.00 92.87           C  
ANISOU 2953  CZ  TYR A 381    10507  14373  10408   1210  -1594  -1246       C  
ATOM   2954  OH  TYR A 381      20.779  27.383  42.963  1.00 93.31           O  
ANISOU 2954  OH  TYR A 381    10771  14522  10162   1066  -1574  -1197       O  
ATOM   2955  N   ASP A 382      22.692  24.725  50.178  1.00 87.93           N  
ANISOU 2955  N   ASP A 382     9462  13239  10709   1477  -1858   -983       N  
ATOM   2956  CA  ASP A 382      22.892  25.758  51.190  1.00 93.51           C  
ANISOU 2956  CA  ASP A 382    10272  13923  11335   1308  -1858   -801       C  
ATOM   2957  C   ASP A 382      24.370  25.950  51.507  1.00100.42           C  
ANISOU 2957  C   ASP A 382    10956  14980  12219   1271  -1904   -819       C  
ATOM   2958  O   ASP A 382      24.827  27.084  51.695  1.00 96.66           O  
ANISOU 2958  O   ASP A 382    10503  14618  11607   1079  -1847   -729       O  
ATOM   2959  CB  ASP A 382      22.111  25.410  52.458  1.00 89.82           C  
ANISOU 2959  CB  ASP A 382    10010  13165  10953   1299  -1937   -678       C  
ATOM   2960  CG  ASP A 382      20.611  25.538  52.273  1.00 93.71           C  
ANISOU 2960  CG  ASP A 382    10645  13494  11468   1280  -1851   -644       C  
ATOM   2961  OD1 ASP A 382      20.184  26.356  51.432  1.00 93.20           O  
ANISOU 2961  OD1 ASP A 382    10578  13523  11312   1231  -1766   -640       O  
ATOM   2962  OD2 ASP A 382      19.859  24.822  52.967  1.00 94.49           O1-
ANISOU 2962  OD2 ASP A 382    10854  13362  11687   1305  -1877   -617       O1-
ATOM   2963  N   MET A 383      25.135  24.857  51.575  1.00101.67           N  
ANISOU 2963  N   MET A 383    10912  15155  12563   1453  -2022   -940       N  
ATOM   2964  CA  MET A 383      26.563  24.980  51.849  1.00 93.95           C  
ANISOU 2964  CA  MET A 383     9669  14360  11668   1444  -2096   -975       C  
ATOM   2965  C   MET A 383      27.300  25.611  50.673  1.00103.87           C  
ANISOU 2965  C   MET A 383    10692  15936  12836   1355  -1873  -1108       C  
ATOM   2966  O   MET A 383      28.231  26.400  50.869  1.00 99.42           O  
ANISOU 2966  O   MET A 383     9974  15556  12243   1188  -1851  -1076       O  
ATOM   2967  CB  MET A 383      27.162  23.610  52.182  1.00 91.01           C  
ANISOU 2967  CB  MET A 383     9117  13892  11569   1710  -2299  -1079       C  
ATOM   2968  CG  MET A 383      26.620  22.974  53.456  1.00 98.22           C  
ANISOU 2968  CG  MET A 383    10304  14474  12540   1758  -2542   -924       C  
ATOM   2969  SD  MET A 383      27.468  21.451  53.946  1.00 77.65           S  
ANISOU 2969  SD  MET A 383     7534  11711  10259   2073  -2857  -1003       S  
ATOM   2970  CE  MET A 383      27.290  20.446  52.473  1.00121.21           C  
ANISOU 2970  CE  MET A 383    12869  17268  15918   2326  -2669  -1295       C  
ATOM   2971  N   ALA A 384      26.880  25.294  49.445  1.00 98.22           N  
ANISOU 2971  N   ALA A 384     9980  15286  12055   1428  -1702  -1258       N  
ATOM   2972  CA  ALA A 384      27.658  25.678  48.271  1.00 92.26           C  
ANISOU 2972  CA  ALA A 384     9030  14825  11199   1347  -1457  -1418       C  
ATOM   2973  C   ALA A 384      27.653  27.184  48.033  1.00 88.29           C  
ANISOU 2973  C   ALA A 384     8672  14451  10423   1034  -1315  -1278       C  
ATOM   2974  O   ALA A 384      28.666  27.736  47.588  1.00 92.38           O  
ANISOU 2974  O   ALA A 384     8990  15220  10888    879  -1144  -1350       O  
ATOM   2975  CB  ALA A 384      27.141  24.946  47.034  1.00 89.79           C  
ANISOU 2975  CB  ALA A 384     8780  14515  10821   1477  -1326  -1612       C  
ATOM   2976  N   TYR A 385      26.541  27.869  48.304  1.00 82.95           N  
ANISOU 2976  N   TYR A 385     8331  13596   9590    934  -1366  -1089       N  
ATOM   2977  CA  TYR A 385      26.493  29.312  48.104  1.00 84.10           C  
ANISOU 2977  CA  TYR A 385     8660  13805   9490    659  -1254   -947       C  
ATOM   2978  C   TYR A 385      26.620  30.093  49.405  1.00 99.42           C  
ANISOU 2978  C   TYR A 385    10696  15635  11444    511  -1366   -761       C  
ATOM   2979  O   TYR A 385      26.327  31.293  49.421  1.00 97.25           O  
ANISOU 2979  O   TYR A 385    10654  15316  10980    305  -1302   -621       O  
ATOM   2980  CB  TYR A 385      25.211  29.733  47.368  1.00104.91           C  
ANISOU 2980  CB  TYR A 385    11611  16312  11937    644  -1228   -871       C  
ATOM   2981  CG  TYR A 385      23.875  29.354  47.996  1.00 98.97           C  
ANISOU 2981  CG  TYR A 385    11026  15272  11307    791  -1388   -779       C  
ATOM   2982  CD1 TYR A 385      23.582  29.664  49.320  1.00 90.55           C  
ANISOU 2982  CD1 TYR A 385    10054  14018  10331    760  -1474   -635       C  
ATOM   2983  CD2 TYR A 385      22.878  28.760  47.235  1.00 95.32           C  
ANISOU 2983  CD2 TYR A 385    10645  14723  10850    924  -1434   -843       C  
ATOM   2984  CE1 TYR A 385      22.361  29.343  49.880  1.00 95.58           C  
ANISOU 2984  CE1 TYR A 385    10830  14401  11084    863  -1550   -570       C  
ATOM   2985  CE2 TYR A 385      21.648  28.441  47.787  1.00 98.97           C  
ANISOU 2985  CE2 TYR A 385    11208  14936  11458   1026  -1552   -771       C  
ATOM   2986  CZ  TYR A 385      21.396  28.736  49.109  1.00 95.24           C  
ANISOU 2986  CZ  TYR A 385    10801  14292  11094    996  -1584   -639       C  
ATOM   2987  OH  TYR A 385      20.176  28.420  49.661  1.00 91.66           O  
ANISOU 2987  OH  TYR A 385    10433  13598  10796   1072  -1637   -588       O  
ATOM   2988  N   ALA A 386      27.032  29.444  50.496  1.00107.53           N  
ANISOU 2988  N   ALA A 386    11595  16590  12673    608  -1549   -756       N  
ATOM   2989  CA  ALA A 386      27.129  30.138  51.775  1.00 82.53           C  
ANISOU 2989  CA  ALA A 386     8585  13298   9473    447  -1675   -588       C  
ATOM   2990  C   ALA A 386      28.184  31.234  51.764  1.00 80.13           C  
ANISOU 2990  C   ALA A 386     8189  13193   9064    159  -1609   -557       C  
ATOM   2991  O   ALA A 386      28.072  32.189  52.541  1.00 80.21           O  
ANISOU 2991  O   ALA A 386     8440  13089   8948    -48  -1648   -412       O  
ATOM   2992  CB  ALA A 386      27.423  29.142  52.896  1.00 79.69           C  
ANISOU 2992  CB  ALA A 386     8148  12815   9316    597  -1928   -582       C  
ATOM   2993  N   ALA A 387      29.200  31.122  50.906  1.00 78.97           N  
ANISOU 2993  N   ALA A 387     7704  13333   8968    123  -1485   -706       N  
ATOM   2994  CA  ALA A 387      30.211  32.168  50.793  1.00 82.46           C  
ANISOU 2994  CA  ALA A 387     8028  13981   9320   -196  -1381   -691       C  
ATOM   2995  C   ALA A 387      29.700  33.402  50.063  1.00 84.16           C  
ANISOU 2995  C   ALA A 387     8575  14176   9226   -438  -1164   -593       C  
ATOM   2996  O   ALA A 387      30.351  34.450  50.123  1.00 90.71           O  
ANISOU 2996  O   ALA A 387     9431  15099   9938   -757  -1087   -534       O  
ATOM   2997  CB  ALA A 387      31.453  31.626  50.086  1.00 98.80           C  
ANISOU 2997  CB  ALA A 387     9595  16370  11575   -166  -1262   -907       C  
ATOM   2998  N   GLN A 388      28.564  33.302  49.375  1.00 94.79           N  
ANISOU 2998  N   GLN A 388    10178  15387  10450   -303  -1093   -570       N  
ATOM   2999  CA  GLN A 388      27.937  34.463  48.772  1.00 81.43           C  
ANISOU 2999  CA  GLN A 388     8853  13605   8483   -487   -967   -442       C  
ATOM   3000  C   GLN A 388      27.455  35.418  49.863  1.00 80.77           C  
ANISOU 3000  C   GLN A 388     9081  13265   8344   -613  -1070   -255       C  
ATOM   3001  O   GLN A 388      27.347  35.033  51.031  1.00 93.89           O  
ANISOU 3001  O   GLN A 388    10729  14796  10149   -525  -1233   -228       O  
ATOM   3002  CB  GLN A 388      26.763  34.030  47.894  1.00 80.14           C  
ANISOU 3002  CB  GLN A 388     8866  13329   8253   -276   -957   -457       C  
ATOM   3003  CG  GLN A 388      27.154  33.190  46.687  1.00 82.24           C  
ANISOU 3003  CG  GLN A 388     8931  13820   8497   -186   -824   -654       C  
ATOM   3004  CD  GLN A 388      27.759  34.017  45.569  1.00 98.05           C  
ANISOU 3004  CD  GLN A 388    11028  16014  10213   -471   -581   -669       C  
ATOM   3005  OE1 GLN A 388      27.627  35.240  45.547  1.00 88.05           O  
ANISOU 3005  OE1 GLN A 388    10051  14661   8742   -711   -548   -499       O  
ATOM   3006  NE2 GLN A 388      28.428  33.351  44.633  1.00 97.19           N  
ANISOU 3006  NE2 GLN A 388    10706  16146  10078   -457   -389   -879       N  
ATOM   3007  N   PRO A 389      27.172  36.675  49.514  1.00 87.32           N  
ANISOU 3007  N   PRO A 389    10232  13995   8949   -826   -973   -128       N  
ATOM   3008  CA  PRO A 389      26.585  37.601  50.492  1.00 91.78           C  
ANISOU 3008  CA  PRO A 389    11138  14268   9465   -913  -1037     25       C  
ATOM   3009  C   PRO A 389      25.289  37.056  51.074  1.00 89.55           C  
ANISOU 3009  C   PRO A 389    10976  13723   9325   -620  -1134     52       C  
ATOM   3010  O   PRO A 389      24.699  36.095  50.575  1.00101.48           O  
ANISOU 3010  O   PRO A 389    12356  15254  10947   -368  -1166    -21       O  
ATOM   3011  CB  PRO A 389      26.342  38.870  49.671  1.00 89.78           C  
ANISOU 3011  CB  PRO A 389    11218  13929   8967  -1112   -915    141       C  
ATOM   3012  CG  PRO A 389      27.401  38.825  48.628  1.00 94.39           C  
ANISOU 3012  CG  PRO A 389    11598  14833   9431  -1306   -765     55       C  
ATOM   3013  CD  PRO A 389      27.559  37.369  48.272  1.00 90.04           C  
ANISOU 3013  CD  PRO A 389    10665  14487   9058  -1044   -783   -124       C  
ATOM   3014  N   PHE A 390      24.834  37.697  52.154  1.00 87.77           N  
ANISOU 3014  N   PHE A 390    11017  13239   9094   -678  -1159    144       N  
ATOM   3015  CA  PHE A 390      23.679  37.179  52.880  1.00 88.33           C  
ANISOU 3015  CA  PHE A 390    11182  13064   9316   -444  -1196    151       C  
ATOM   3016  C   PHE A 390      22.401  37.276  52.054  1.00105.03           C  
ANISOU 3016  C   PHE A 390    13387  15035  11484   -241  -1156    180       C  
ATOM   3017  O   PHE A 390      21.582  36.350  52.062  1.00 98.77           O  
ANISOU 3017  O   PHE A 390    12477  14184  10868     -7  -1196    126       O  
ATOM   3018  CB  PHE A 390      23.524  37.911  54.215  1.00 87.36           C  
ANISOU 3018  CB  PHE A 390    11360  12691   9140   -584  -1176    219       C  
ATOM   3019  CG  PHE A 390      22.272  37.548  54.965  1.00 89.60           C  
ANISOU 3019  CG  PHE A 390    11781  12701   9561   -388  -1128    218       C  
ATOM   3020  CD1 PHE A 390      22.208  36.384  55.713  1.00 92.60           C  
ANISOU 3020  CD1 PHE A 390    12051  13078  10053   -281  -1202    165       C  
ATOM   3021  CD2 PHE A 390      21.174  38.392  54.953  1.00 89.52           C  
ANISOU 3021  CD2 PHE A 390    12014  12419   9582   -321   -997    267       C  
ATOM   3022  CE1 PHE A 390      21.058  36.052  56.408  1.00 89.52           C  
ANISOU 3022  CE1 PHE A 390    11795  12438   9779   -149  -1107    157       C  
ATOM   3023  CE2 PHE A 390      20.026  38.070  55.650  1.00 90.08           C  
ANISOU 3023  CE2 PHE A 390    12160  12249   9815   -157   -899    240       C  
ATOM   3024  CZ  PHE A 390      19.967  36.900  56.379  1.00 89.03           C  
ANISOU 3024  CZ  PHE A 390    11923  12135   9768    -93   -933    183       C  
ATOM   3025  N   LEU A 391      22.212  38.378  51.331  1.00106.20           N  
ANISOU 3025  N   LEU A 391    13748  15112  11491   -336  -1105    269       N  
ATOM   3026  CA  LEU A 391      21.017  38.536  50.510  1.00 95.73           C  
ANISOU 3026  CA  LEU A 391    12509  13636  10226   -138  -1139    314       C  
ATOM   3027  C   LEU A 391      21.070  37.734  49.215  1.00 95.50           C  
ANISOU 3027  C   LEU A 391    12291  13833  10161    -42  -1209    247       C  
ATOM   3028  O   LEU A 391      20.112  37.785  48.437  1.00 94.58           O  
ANISOU 3028  O   LEU A 391    12242  13613  10080    111  -1298    284       O  
ATOM   3029  CB  LEU A 391      20.785  40.016  50.192  1.00 96.74           C  
ANISOU 3029  CB  LEU A 391    12986  13559  10210   -259  -1107    453       C  
ATOM   3030  CG  LEU A 391      20.467  40.901  51.399  1.00 94.79           C  
ANISOU 3030  CG  LEU A 391    12993  13009  10012   -315  -1018    503       C  
ATOM   3031  CD1 LEU A 391      20.455  42.375  51.010  1.00 97.58           C  
ANISOU 3031  CD1 LEU A 391    13717  13156  10204   -461   -993    635       C  
ATOM   3032  CD2 LEU A 391      19.147  40.486  52.038  1.00 94.29           C  
ANISOU 3032  CD2 LEU A 391    12878  12712  10236    -34   -995    461       C  
ATOM   3033  N   LEU A 392      22.150  36.988  48.967  1.00 83.07           N  
ANISOU 3033  N   LEU A 392    10483  12551   8529   -120  -1181    137       N  
ATOM   3034  CA  LEU A 392      22.297  36.206  47.745  1.00 84.59           C  
ANISOU 3034  CA  LEU A 392    10526  12956   8660    -47  -1198     35       C  
ATOM   3035  C   LEU A 392      22.411  34.710  48.024  1.00 82.10           C  
ANISOU 3035  C   LEU A 392     9899  12749   8548    143  -1244   -125       C  
ATOM   3036  O   LEU A 392      22.878  33.958  47.163  1.00 82.61           O  
ANISOU 3036  O   LEU A 392     9802  13021   8565    179  -1217   -258       O  
ATOM   3037  CB  LEU A 392      23.509  36.690  46.947  1.00 87.00           C  
ANISOU 3037  CB  LEU A 392    10841  13509   8707   -314  -1063     15       C  
ATOM   3038  CG  LEU A 392      23.494  38.167  46.553  1.00 86.75           C  
ANISOU 3038  CG  LEU A 392    11174  13358   8431   -547  -1015    184       C  
ATOM   3039  CD1 LEU A 392      24.710  38.514  45.709  1.00 91.51           C  
ANISOU 3039  CD1 LEU A 392    11772  14226   8771   -852   -835    146       C  
ATOM   3040  CD2 LEU A 392      22.208  38.511  45.820  1.00 88.00           C  
ANISOU 3040  CD2 LEU A 392    11598  13292   8546   -390  -1158    294       C  
ATOM   3041  N   ARG A 393      21.991  34.261  49.208  1.00 79.61           N  
ANISOU 3041  N   ARG A 393     9532  12275   8442    256  -1298   -121       N  
ATOM   3042  CA  ARG A 393      22.043  32.844  49.571  1.00 96.88           C  
ANISOU 3042  CA  ARG A 393    11485  14503  10822    431  -1364   -246       C  
ATOM   3043  C   ARG A 393      20.656  32.232  49.391  1.00101.98           C  
ANISOU 3043  C   ARG A 393    12149  14969  11629    636  -1439   -262       C  
ATOM   3044  O   ARG A 393      19.886  32.061  50.336  1.00 98.91           O  
ANISOU 3044  O   ARG A 393    11806  14369  11404    703  -1448   -222       O  
ATOM   3045  CB  ARG A 393      22.549  32.665  50.997  1.00 83.91           C  
ANISOU 3045  CB  ARG A 393     9816  12795   9272    383  -1395   -222       C  
ATOM   3046  CG  ARG A 393      23.973  33.115  51.211  1.00 79.95           C  
ANISOU 3046  CG  ARG A 393     9220  12489   8668    180  -1377   -226       C  
ATOM   3047  CD  ARG A 393      24.317  33.091  52.682  1.00 92.58           C  
ANISOU 3047  CD  ARG A 393    10880  13975  10322    109  -1471   -170       C  
ATOM   3048  NE  ARG A 393      25.613  33.699  52.950  1.00 92.93           N  
ANISOU 3048  NE  ARG A 393    10840  14188  10280   -126  -1494   -158       N  
ATOM   3049  CZ  ARG A 393      26.021  34.079  54.152  1.00 95.82           C  
ANISOU 3049  CZ  ARG A 393    11333  14462  10611   -282  -1594    -86       C  
ATOM   3050  NH1 ARG A 393      25.253  33.930  55.219  1.00 98.34           N  
ANISOU 3050  NH1 ARG A 393    11908  14517  10940   -236  -1641    -21       N  
ATOM   3051  NH2 ARG A 393      27.226  34.623  54.286  1.00 98.58           N  
ANISOU 3051  NH2 ARG A 393    11561  14990  10905   -517  -1640    -87       N  
ATOM   3052  N   ASN A 394      20.352  31.884  48.146  1.00 86.44           N  
ANISOU 3052  N   ASN A 394    10148  13091   9606    708  -1486   -332       N  
ATOM   3053  CA  ASN A 394      19.085  31.259  47.799  1.00 89.19           C  
ANISOU 3053  CA  ASN A 394    10477  13300  10112    878  -1599   -364       C  
ATOM   3054  C   ASN A 394      19.217  30.703  46.392  1.00 95.44           C  
ANISOU 3054  C   ASN A 394    11240  14257  10767    910  -1658   -484       C  
ATOM   3055  O   ASN A 394      20.067  31.146  45.614  1.00 98.67           O  
ANISOU 3055  O   ASN A 394    11712  14853  10925    782  -1578   -503       O  
ATOM   3056  CB  ASN A 394      17.923  32.255  47.884  1.00 96.81           C  
ANISOU 3056  CB  ASN A 394    11597  14046  11140    895  -1639   -223       C  
ATOM   3057  CG  ASN A 394      16.647  31.620  48.398  1.00117.38           C  
ANISOU 3057  CG  ASN A 394    14098  16448  14053   1046  -1694   -247       C  
ATOM   3058  OD1 ASN A 394      16.297  30.501  48.020  1.00117.10           O  
ANISOU 3058  OD1 ASN A 394    13926  16440  14128   1140  -1784   -360       O  
ATOM   3059  ND2 ASN A 394      15.946  32.333  49.272  1.00115.57           N  
ANISOU 3059  ND2 ASN A 394    13936  16004  13970   1054  -1614   -156       N  
ATOM   3060  N   GLY A 395      18.372  29.722  46.077  1.00 92.14           N  
ANISOU 3060  N   GLY A 395    10746  13763  10502   1052  -1781   -576       N  
ATOM   3061  CA  GLY A 395      18.337  29.150  44.744  1.00100.85           C  
ANISOU 3061  CA  GLY A 395    11877  14982  11458   1076  -1860   -705       C  
ATOM   3062  C   GLY A 395      18.170  30.212  43.677  1.00106.70           C  
ANISOU 3062  C   GLY A 395    12855  15770  11918    963  -1918   -603       C  
ATOM   3063  O   GLY A 395      17.637  31.289  43.961  1.00102.36           O  
ANISOU 3063  O   GLY A 395    12423  15082  11387    932  -1967   -424       O  
ATOM   3064  N   ALA A 396      18.627  29.922  42.455  1.00103.94           N  
ANISOU 3064  N   ALA A 396    12610  15587  11294    898  -1905   -720       N  
ATOM   3065  CA  ALA A 396      18.651  30.925  41.392  1.00 85.59           C  
ANISOU 3065  CA  ALA A 396    10589  13313   8620    743  -1944   -614       C  
ATOM   3066  C   ALA A 396      17.308  31.637  41.265  1.00 90.57           C  
ANISOU 3066  C   ALA A 396    11365  13714   9334    806  -2228   -427       C  
ATOM   3067  O   ALA A 396      17.248  32.870  41.191  1.00 93.99           O  
ANISOU 3067  O   ALA A 396    12007  14067   9637    716  -2254   -237       O  
ATOM   3068  CB  ALA A 396      19.045  30.272  40.070  1.00 87.46           C  
ANISOU 3068  CB  ALA A 396    10958  13720   8553    676  -1913   -797       C  
ATOM   3069  N   ASN A 397      16.218  30.874  41.248  1.00100.51           N  
ANISOU 3069  N   ASN A 397    12500  14848  10842    961  -2451   -482       N  
ATOM   3070  CA  ASN A 397      14.872  31.428  41.305  1.00 97.55           C  
ANISOU 3070  CA  ASN A 397    12135  14247  10684   1065  -2725   -331       C  
ATOM   3071  C   ASN A 397      14.044  30.547  42.238  1.00 99.26           C  
ANISOU 3071  C   ASN A 397    12027  14334  11354   1219  -2752   -411       C  
ATOM   3072  O   ASN A 397      14.580  29.690  42.948  1.00106.30           O  
ANISOU 3072  O   ASN A 397    12755  15282  12351   1233  -2559   -536       O  
ATOM   3073  CB  ASN A 397      14.278  31.564  39.895  1.00 87.04           C  
ANISOU 3073  CB  ASN A 397    11054  12904   9114   1032  -3053   -296       C  
ATOM   3074  CG  ASN A 397      14.233  30.248  39.139  1.00 91.23           C  
ANISOU 3074  CG  ASN A 397    11564  13543   9558   1028  -3145   -517       C  
ATOM   3075  OD1 ASN A 397      13.971  29.189  39.709  1.00 95.45           O  
ANISOU 3075  OD1 ASN A 397    11829  14051  10388   1126  -3110   -662       O  
ATOM   3076  ND2 ASN A 397      14.488  30.314  37.838  1.00 92.84           N  
ANISOU 3076  ND2 ASN A 397    12102  13845   9329    895  -3256   -545       N  
ATOM   3077  N   GLU A 398      12.723  30.753  42.239  1.00 83.06           N  
ANISOU 3077  N   GLU A 398     9878  12095   9585   1328  -2996   -336       N  
ATOM   3078  CA  GLU A 398      11.879  30.057  43.204  1.00 92.54           C  
ANISOU 3078  CA  GLU A 398    10767  13159  11236   1434  -2962   -401       C  
ATOM   3079  C   GLU A 398      11.821  28.554  42.960  1.00 94.42           C  
ANISOU 3079  C   GLU A 398    10883  13460  11531   1430  -3011   -602       C  
ATOM   3080  O   GLU A 398      11.391  27.816  43.852  1.00109.70           O  
ANISOU 3080  O   GLU A 398    12602  15296  13784   1468  -2912   -671       O  
ATOM   3081  CB  GLU A 398      10.454  30.617  43.195  1.00 83.25           C  
ANISOU 3081  CB  GLU A 398     9448  11778  10405   1552  -3200   -301       C  
ATOM   3082  CG  GLU A 398       9.714  30.455  41.879  1.00 99.25           C  
ANISOU 3082  CG  GLU A 398    11524  13806  12380   1571  -3630   -304       C  
ATOM   3083  CD  GLU A 398       8.362  31.146  41.883  1.00103.13           C  
ANISOU 3083  CD  GLU A 398    11830  14090  13265   1717  -3902   -189       C  
ATOM   3084  OE1 GLU A 398       8.123  31.986  42.777  1.00101.45           O  
ANISOU 3084  OE1 GLU A 398    11524  13730  13292   1807  -3720    -94       O  
ATOM   3085  OE2 GLU A 398       7.533  30.837  41.001  1.00 93.94           O1-
ANISOU 3085  OE2 GLU A 398    10606  12900  12188   1746  -4305   -206       O1-
ATOM   3086  N   GLY A 399      12.244  28.085  41.789  1.00 86.12           N  
ANISOU 3086  N   GLY A 399    10006  12549  10166   1368  -3140   -704       N  
ATOM   3087  CA  GLY A 399      12.129  26.678  41.464  1.00 92.95           C  
ANISOU 3087  CA  GLY A 399    10800  13436  11082   1367  -3208   -912       C  
ATOM   3088  C   GLY A 399      13.431  25.903  41.494  1.00 98.38           C  
ANISOU 3088  C   GLY A 399    11548  14269  11562   1340  -2954  -1076       C  
ATOM   3089  O   GLY A 399      13.421  24.671  41.405  1.00101.44           O  
ANISOU 3089  O   GLY A 399    11880  14632  12029   1364  -2968  -1260       O  
ATOM   3090  N   PHE A 400      14.559  26.604  41.629  1.00 99.16           N  
ANISOU 3090  N   PHE A 400    11746  14504  11426   1293  -2726  -1019       N  
ATOM   3091  CA  PHE A 400      15.856  25.938  41.543  1.00 93.55           C  
ANISOU 3091  CA  PHE A 400    11043  13952  10549   1281  -2495  -1188       C  
ATOM   3092  C   PHE A 400      16.109  25.038  42.746  1.00 87.52           C  
ANISOU 3092  C   PHE A 400    10063  13101  10090   1380  -2368  -1256       C  
ATOM   3093  O   PHE A 400      16.566  23.899  42.594  1.00 83.23           O  
ANISOU 3093  O   PHE A 400     9480  12572   9570   1442  -2322  -1451       O  
ATOM   3094  CB  PHE A 400      16.975  26.968  41.406  1.00 92.76           C  
ANISOU 3094  CB  PHE A 400    11055  14027  10162   1174  -2287  -1107       C  
ATOM   3095  CG  PHE A 400      17.488  27.121  40.006  1.00 96.95           C  
ANISOU 3095  CG  PHE A 400    11836  14727  10273   1053  -2261  -1198       C  
ATOM   3096  CD1 PHE A 400      16.668  27.604  38.999  1.00 91.94           C  
ANISOU 3096  CD1 PHE A 400    11459  14044   9428    981  -2519  -1115       C  
ATOM   3097  CD2 PHE A 400      18.787  26.760  39.692  1.00 98.87           C  
ANISOU 3097  CD2 PHE A 400    12062  15171  10334   1006  -1980  -1374       C  
ATOM   3098  CE1 PHE A 400      17.143  27.738  37.706  1.00 93.26           C  
ANISOU 3098  CE1 PHE A 400    11938  14354   9143    832  -2485  -1194       C  
ATOM   3099  CE2 PHE A 400      19.267  26.891  38.403  1.00110.68           C  
ANISOU 3099  CE2 PHE A 400    13815  16822  11415    863  -1888  -1480       C  
ATOM   3100  CZ  PHE A 400      18.444  27.379  37.409  1.00104.89           C  
ANISOU 3100  CZ  PHE A 400    13413  16033  10408    760  -2136  -1385       C  
ATOM   3101  N   HIS A 401      15.828  25.535  43.953  1.00 85.77           N  
ANISOU 3101  N   HIS A 401     9739  12763  10087   1394  -2309  -1098       N  
ATOM   3102  CA  HIS A 401      16.187  24.798  45.162  1.00 88.13           C  
ANISOU 3102  CA  HIS A 401     9911  12970  10603   1454  -2193  -1126       C  
ATOM   3103  C   HIS A 401      15.479  23.450  45.219  1.00 88.52           C  
ANISOU 3103  C   HIS A 401     9898  12860  10876   1516  -2300  -1258       C  
ATOM   3104  O   HIS A 401      16.107  22.414  45.469  1.00 79.15           O  
ANISOU 3104  O   HIS A 401     8685  11646   9743   1586  -2254  -1386       O  
ATOM   3105  CB  HIS A 401      15.859  25.632  46.398  1.00 92.63           C  
ANISOU 3105  CB  HIS A 401    10458  13420  11316   1419  -2108   -937       C  
ATOM   3106  CG  HIS A 401      16.952  25.646  47.419  1.00101.46           C  
ANISOU 3106  CG  HIS A 401    11563  14572  12415   1406  -1960   -904       C  
ATOM   3107  ND1 HIS A 401      17.512  24.493  47.925  1.00101.37           N  
ANISOU 3107  ND1 HIS A 401    11491  14519  12506   1479  -1954  -1005       N  
ATOM   3108  CD2 HIS A 401      17.595  26.673  48.023  1.00 94.29           C  
ANISOU 3108  CD2 HIS A 401    10707  13719  11401   1323  -1851   -778       C  
ATOM   3109  CE1 HIS A 401      18.450  24.809  48.799  1.00 88.25           C  
ANISOU 3109  CE1 HIS A 401     9827  12896  10808   1450  -1878   -934       C  
ATOM   3110  NE2 HIS A 401      18.521  26.126  48.877  1.00 89.54           N  
ANISOU 3110  NE2 HIS A 401    10056  13126  10839   1340  -1807   -804       N  
ATOM   3111  N   GLU A 402      14.167  23.444  44.982  1.00 92.05           N  
ANISOU 3111  N   GLU A 402    10312  13184  11480   1491  -2459  -1230       N  
ATOM   3112  CA  GLU A 402      13.401  22.204  45.018  1.00 83.80           C  
ANISOU 3112  CA  GLU A 402     9204  11975  10660   1501  -2565  -1354       C  
ATOM   3113  C   GLU A 402      13.745  21.269  43.867  1.00 77.75           C  
ANISOU 3113  C   GLU A 402     8538  11274   9731   1522  -2673  -1572       C  
ATOM   3114  O   GLU A 402      13.499  20.062  43.974  1.00 76.49           O  
ANISOU 3114  O   GLU A 402     8371  10969   9725   1538  -2720  -1708       O  
ATOM   3115  CB  GLU A 402      11.908  22.527  45.021  1.00 99.30           C  
ANISOU 3115  CB  GLU A 402    11045  13812  12872   1450  -2712  -1278       C  
ATOM   3116  CG  GLU A 402      11.068  21.533  45.776  1.00120.62           C  
ANISOU 3116  CG  GLU A 402    13623  16298  15908   1408  -2697  -1328       C  
ATOM   3117  CD  GLU A 402      11.550  21.346  47.192  1.00126.66           C  
ANISOU 3117  CD  GLU A 402    14414  16956  16755   1405  -2448  -1255       C  
ATOM   3118  OE1 GLU A 402      11.482  22.301  47.994  1.00128.17           O  
ANISOU 3118  OE1 GLU A 402    14585  17133  16981   1389  -2296  -1107       O  
ATOM   3119  OE2 GLU A 402      12.003  20.232  47.491  1.00126.28           O1-
ANISOU 3119  OE2 GLU A 402    14442  16817  16722   1417  -2423  -1349       O1-
ATOM   3120  N   ALA A 403      14.310  21.790  42.776  1.00 83.10           N  
ANISOU 3120  N   ALA A 403     9346  12145  10083   1505  -2692  -1616       N  
ATOM   3121  CA  ALA A 403      14.747  20.928  41.682  1.00 85.66           C  
ANISOU 3121  CA  ALA A 403     9811  12534  10204   1514  -2730  -1854       C  
ATOM   3122  C   ALA A 403      16.022  20.172  42.038  1.00 88.35           C  
ANISOU 3122  C   ALA A 403    10120  12908  10542   1626  -2507  -2003       C  
ATOM   3123  O   ALA A 403      16.161  18.992  41.698  1.00 87.65           O  
ANISOU 3123  O   ALA A 403    10083  12730  10491   1689  -2524  -2220       O  
ATOM   3124  CB  ALA A 403      14.952  21.756  40.412  1.00 94.49           C  
ANISOU 3124  CB  ALA A 403    11130  13841  10931   1426  -2784  -1853       C  
ATOM   3125  N   VAL A 404      16.963  20.840  42.713  1.00102.35           N  
ANISOU 3125  N   VAL A 404    11804  14793  12290   1658  -2319  -1895       N  
ATOM   3126  CA  VAL A 404      18.176  20.169  43.180  1.00 98.98           C  
ANISOU 3126  CA  VAL A 404    11282  14390  11937   1787  -2157  -2014       C  
ATOM   3127  C   VAL A 404      17.821  19.025  44.119  1.00 94.38           C  
ANISOU 3127  C   VAL A 404    10655  13538  11667   1882  -2238  -2035       C  
ATOM   3128  O   VAL A 404      18.350  17.913  44.004  1.00 99.22           O  
ANISOU 3128  O   VAL A 404    11272  14064  12362   2014  -2221  -2229       O  
ATOM   3129  CB  VAL A 404      19.118  21.179  43.862  1.00 79.68           C  
ANISOU 3129  CB  VAL A 404     8728  12101   9446   1766  -2003  -1860       C  
ATOM   3130  CG1 VAL A 404      20.225  20.453  44.610  1.00 92.59           C  
ANISOU 3130  CG1 VAL A 404    10210  13714  11257   1916  -1923  -1942       C  
ATOM   3131  CG2 VAL A 404      19.706  22.118  42.834  1.00 82.91           C  
ANISOU 3131  CG2 VAL A 404     9206  12770   9527   1656  -1875  -1883       C  
ATOM   3132  N   GLY A 405      16.917  19.284  45.066  1.00 87.14           N  
ANISOU 3132  N   GLY A 405     9716  12465  10929   1812  -2309  -1842       N  
ATOM   3133  CA  GLY A 405      16.513  18.250  46.001  1.00 94.56           C  
ANISOU 3133  CA  GLY A 405    10667  13130  12130   1847  -2363  -1837       C  
ATOM   3134  C   GLY A 405      15.906  17.030  45.336  1.00101.63           C  
ANISOU 3134  C   GLY A 405    11647  13860  13108   1855  -2485  -2035       C  
ATOM   3135  O   GLY A 405      16.095  15.907  45.810  1.00106.71           O  
ANISOU 3135  O   GLY A 405    12347  14288  13911   1935  -2509  -2115       O  
ATOM   3136  N   GLU A 406      15.187  17.225  44.228  1.00 97.79           N  
ANISOU 3136  N   GLU A 406    11202  13450  12505   1765  -2594  -2114       N  
ATOM   3137  CA  GLU A 406      14.472  16.115  43.604  1.00101.95           C  
ANISOU 3137  CA  GLU A 406    11825  13804  13106   1724  -2747  -2301       C  
ATOM   3138  C   GLU A 406      15.421  15.156  42.895  1.00107.50           C  
ANISOU 3138  C   GLU A 406    12653  14499  13694   1861  -2695  -2573       C  
ATOM   3139  O   GLU A 406      15.309  13.934  43.053  1.00110.77           O  
ANISOU 3139  O   GLU A 406    13155  14666  14268   1907  -2747  -2712       O  
ATOM   3140  CB  GLU A 406      13.420  16.646  42.630  1.00113.30           C  
ANISOU 3140  CB  GLU A 406    13277  15324  14447   1578  -2938  -2297       C  
ATOM   3141  CG  GLU A 406      12.173  17.185  43.303  1.00124.08           C  
ANISOU 3141  CG  GLU A 406    14478  16600  16066   1459  -3025  -2097       C  
ATOM   3142  CD  GLU A 406      11.352  16.095  43.965  1.00129.23           C  
ANISOU 3142  CD  GLU A 406    15090  16973  17038   1376  -3069  -2138       C  
ATOM   3143  OE1 GLU A 406      11.480  14.919  43.560  1.00112.70           O  
ANISOU 3143  OE1 GLU A 406    13134  14743  14944   1381  -3136  -2338       O  
ATOM   3144  OE2 GLU A 406      10.582  16.413  44.895  1.00148.95           O1-
ANISOU 3144  OE2 GLU A 406    17436  19374  19786   1292  -3011  -1981       O1-
ATOM   3145  N   ILE A 407      16.361  15.685  42.106  1.00 96.17           N  
ANISOU 3145  N   ILE A 407    11238  13314  11988   1921  -2567  -2665       N  
ATOM   3146  CA  ILE A 407      17.239  14.840  41.305  1.00 97.16           C  
ANISOU 3146  CA  ILE A 407    11469  13449  12000   2050  -2461  -2967       C  
ATOM   3147  C   ILE A 407      18.058  13.878  42.151  1.00102.62           C  
ANISOU 3147  C   ILE A 407    12087  13951  12950   2267  -2383  -3042       C  
ATOM   3148  O   ILE A 407      18.638  12.931  41.611  1.00106.82           O  
ANISOU 3148  O   ILE A 407    12702  14396  13489   2412  -2315  -3318       O  
ATOM   3149  CB  ILE A 407      18.179  15.699  40.430  1.00 97.74           C  
ANISOU 3149  CB  ILE A 407    11548  13846  11744   2046  -2261  -3038       C  
ATOM   3150  CG1 ILE A 407      19.156  16.495  41.296  1.00 96.81           C  
ANISOU 3150  CG1 ILE A 407    11204  13886  11695   2122  -2091  -2868       C  
ATOM   3151  CG2 ILE A 407      17.375  16.644  39.565  1.00 97.47           C  
ANISOU 3151  CG2 ILE A 407    11656  13957  11422   1834  -2388  -2941       C  
ATOM   3152  CD1 ILE A 407      20.110  17.366  40.496  1.00106.35           C  
ANISOU 3152  CD1 ILE A 407    12395  15411  12600   2074  -1858  -2931       C  
ATOM   3153  N   MET A 408      18.116  14.093  43.466  1.00105.67           N  
ANISOU 3153  N   MET A 408    12350  14253  13547   2297  -2403  -2805       N  
ATOM   3154  CA  MET A 408      18.842  13.177  44.337  1.00104.49           C  
ANISOU 3154  CA  MET A 408    12173  13886  13643   2501  -2405  -2834       C  
ATOM   3155  C   MET A 408      18.072  11.875  44.529  1.00112.71           C  
ANISOU 3155  C   MET A 408    13405  14548  14871   2491  -2554  -2917       C  
ATOM   3156  O   MET A 408      18.648  10.785  44.437  1.00108.70           O  
ANISOU 3156  O   MET A 408    12978  13836  14488   2686  -2562  -3114       O  
ATOM   3157  CB  MET A 408      19.127  13.850  45.679  1.00 97.36           C  
ANISOU 3157  CB  MET A 408    11150  13000  12843   2494  -2410  -2543       C  
ATOM   3158  CG  MET A 408      19.800  15.208  45.542  1.00102.39           C  
ANISOU 3158  CG  MET A 408    11616  13989  13296   2452  -2274  -2444       C  
ATOM   3159  SD  MET A 408      21.219  15.138  44.427  1.00 99.95           S  
ANISOU 3159  SD  MET A 408    11168  13938  12870   2625  -2074  -2738       S  
ATOM   3160  CE  MET A 408      21.513  16.878  44.121  1.00 90.39           C  
ANISOU 3160  CE  MET A 408     9851  13115  11380   2432  -1923  -2578       C  
ATOM   3161  N   SER A 409      16.767  11.965  44.793  1.00111.56           N  
ANISOU 3161  N   SER A 409    13326  14288  14774   2263  -2666  -2780       N  
ATOM   3162  CA  SER A 409      15.960  10.760  44.937  1.00108.91           C  
ANISOU 3162  CA  SER A 409    13172  13596  14614   2189  -2796  -2859       C  
ATOM   3163  C   SER A 409      15.583  10.139  43.597  1.00106.34           C  
ANISOU 3163  C   SER A 409    12988  13241  14175   2141  -2866  -3151       C  
ATOM   3164  O   SER A 409      15.019   9.040  43.582  1.00103.05           O  
ANISOU 3164  O   SER A 409    12748  12512  13896   2078  -2977  -3266       O  
ATOM   3165  CB  SER A 409      14.700  11.052  45.757  1.00 99.83           C  
ANISOU 3165  CB  SER A 409    11997  12334  13598   1936  -2852  -2624       C  
ATOM   3166  OG  SER A 409      14.041  12.218  45.300  1.00 97.65           O  
ANISOU 3166  OG  SER A 409    11569  12326  13207   1788  -2853  -2533       O  
ATOM   3167  N   LEU A 410      15.864  10.814  42.480  1.00110.35           N  
ANISOU 3167  N   LEU A 410    13469  14049  14410   2138  -2808  -3271       N  
ATOM   3168  CA  LEU A 410      15.851  10.135  41.188  1.00107.80           C  
ANISOU 3168  CA  LEU A 410    13350  13693  13915   2133  -2839  -3595       C  
ATOM   3169  C   LEU A 410      16.959   9.093  41.126  1.00116.28           C  
ANISOU 3169  C   LEU A 410    14515  14593  15074   2409  -2708  -3850       C  
ATOM   3170  O   LEU A 410      16.710   7.912  40.857  1.00119.09           O  
ANISOU 3170  O   LEU A 410    15088  14642  15519   2428  -2787  -4063       O  
ATOM   3171  CB  LEU A 410      16.008  11.147  40.049  1.00111.75           C  
ANISOU 3171  CB  LEU A 410    13859  14551  14050   2053  -2781  -3648       C  
ATOM   3172  CG  LEU A 410      14.808  11.990  39.611  1.00103.15           C  
ANISOU 3172  CG  LEU A 410    12768  13591  12834   1792  -2992  -3492       C  
ATOM   3173  CD1 LEU A 410      15.195  12.881  38.442  1.00102.35           C  
ANISOU 3173  CD1 LEU A 410    12768  13800  12318   1738  -2931  -3556       C  
ATOM   3174  CD2 LEU A 410      13.635  11.102  39.230  1.00108.67           C  
ANISOU 3174  CD2 LEU A 410    13618  14045  13626   1611  -3255  -3610       C  
ATOM   3175  N   SER A 411      18.196   9.518  41.389  1.00112.79           N  
ANISOU 3175  N   SER A 411    13891  14330  14635   2631  -2514  -3837       N  
ATOM   3176  CA  SER A 411      19.330   8.604  41.328  1.00110.61           C  
ANISOU 3176  CA  SER A 411    13621  13906  14500   2942  -2385  -4090       C  
ATOM   3177  C   SER A 411      19.250   7.560  42.434  1.00111.11           C  
ANISOU 3177  C   SER A 411    13760  13546  14912   3071  -2544  -4006       C  
ATOM   3178  O   SER A 411      19.491   6.369  42.199  1.00113.30           O  
ANISOU 3178  O   SER A 411    14215  13509  15324   3239  -2561  -4253       O  
ATOM   3179  CB  SER A 411      20.635   9.393  41.427  1.00102.40           C  
ANISOU 3179  CB  SER A 411    12291  13180  13436   3123  -2162  -4072       C  
ATOM   3180  OG  SER A 411      20.745  10.332  40.371  1.00101.86           O  
ANISOU 3180  OG  SER A 411    12211  13478  13013   2976  -1989  -4150       O  
ATOM   3181  N   ALA A 412      18.893   7.988  43.646  1.00104.73           N  
ANISOU 3181  N   ALA A 412    12865  12696  14232   2979  -2655  -3659       N  
ATOM   3182  CA  ALA A 412      18.970   7.107  44.805  1.00 98.99           C  
ANISOU 3182  CA  ALA A 412    12246  11576  13789   3092  -2798  -3535       C  
ATOM   3183  C   ALA A 412      17.972   5.961  44.739  1.00114.76           C  
ANISOU 3183  C   ALA A 412    14557  13163  15883   2948  -2941  -3622       C  
ATOM   3184  O   ALA A 412      18.174   4.940  45.406  1.00114.42           O  
ANISOU 3184  O   ALA A 412    14695  12720  16058   3081  -3050  -3614       O  
ATOM   3185  CB  ALA A 412      18.755   7.913  46.087  1.00 96.48           C  
ANISOU 3185  CB  ALA A 412    11825  11322  13512   2966  -2852  -3149       C  
ATOM   3186  N   ALA A 413      16.912   6.093  43.945  1.00128.27           N  
ANISOU 3186  N   ALA A 413    16346  14947  17443   2670  -2970  -3703       N  
ATOM   3187  CA  ALA A 413      15.844   5.104  43.922  1.00119.77           C  
ANISOU 3187  CA  ALA A 413    15531  13505  16470   2457  -3119  -3766       C  
ATOM   3188  C   ALA A 413      15.947   4.119  42.766  1.00125.40           C  
ANISOU 3188  C   ALA A 413    16485  14040  17120   2526  -3134  -4159       C  
ATOM   3189  O   ALA A 413      15.204   3.132  42.752  1.00129.70           O  
ANISOU 3189  O   ALA A 413    17286  14221  17774   2369  -3267  -4246       O  
ATOM   3190  CB  ALA A 413      14.480   5.800  43.869  1.00113.82           C  
ANISOU 3190  CB  ALA A 413    14686  12904  15656   2078  -3194  -3603       C  
ATOM   3191  N   THR A 414      16.835   4.357  41.803  1.00123.07           N  
ANISOU 3191  N   THR A 414    16137  13981  16644   2729  -2977  -4409       N  
ATOM   3192  CA  THR A 414      16.956   3.457  40.669  1.00128.08           C  
ANISOU 3192  CA  THR A 414    17042  14448  17177   2786  -2946  -4816       C  
ATOM   3193  C   THR A 414      17.412   2.075  41.139  1.00133.45           C  
ANISOU 3193  C   THR A 414    17941  14618  18146   3034  -2986  -4958       C  
ATOM   3194  O   THR A 414      18.072   1.950  42.175  1.00134.77           O  
ANISOU 3194  O   THR A 414    17998  14652  18556   3269  -2997  -4779       O  
ATOM   3195  CB  THR A 414      17.948   4.011  39.647  1.00119.90           C  
ANISOU 3195  CB  THR A 414    15906  13766  15886   2964  -2691  -5059       C  
ATOM   3196  OG1 THR A 414      19.217   4.224  40.277  1.00125.80           O  
ANISOU 3196  OG1 THR A 414    16387  14597  16814   3311  -2527  -5002       O  
ATOM   3197  CG2 THR A 414      17.444   5.325  39.071  1.00122.82           C  
ANISOU 3197  CG2 THR A 414    16152  14584  15929   2696  -2687  -4922       C  
ATOM   3198  N   PRO A 415      17.058   1.015  40.404  1.00136.18           N  
ANISOU 3198  N   PRO A 415    18634  14641  18469   2979  -3041  -5273       N  
ATOM   3199  CA  PRO A 415      17.558  -0.317  40.782  1.00144.42           C  
ANISOU 3199  CA  PRO A 415    19924  15154  19795   3251  -3077  -5432       C  
ATOM   3200  C   PRO A 415      19.071  -0.409  40.749  1.00149.46           C  
ANISOU 3200  C   PRO A 415    20391  15831  20565   3752  -2872  -5605       C  
ATOM   3201  O   PRO A 415      19.665  -1.092  41.592  1.00146.02           O  
ANISOU 3201  O   PRO A 415    19984  15045  20454   4048  -2953  -5538       O  
ATOM   3202  CB  PRO A 415      16.905  -1.246  39.746  1.00149.93           C  
ANISOU 3202  CB  PRO A 415    21028  15574  20364   3064  -3137  -5792       C  
ATOM   3203  CG  PRO A 415      15.745  -0.476  39.206  1.00145.67           C  
ANISOU 3203  CG  PRO A 415    20444  15352  19552   2610  -3251  -5696       C  
ATOM   3204  CD  PRO A 415      16.161   0.960  39.238  1.00144.17           C  
ANISOU 3204  CD  PRO A 415    19860  15718  19201   2658  -3114  -5489       C  
ATOM   3205  N   LYS A 416      19.713   0.276  39.799  1.00158.78           N  
ANISOU 3205  N   LYS A 416    21390  17426  21513   3843  -2613  -5822       N  
ATOM   3206  CA  LYS A 416      21.169   0.245  39.707  1.00157.81           C  
ANISOU 3206  CA  LYS A 416    21024  17386  21550   4301  -2368  -6019       C  
ATOM   3207  C   LYS A 416      21.820   0.749  40.990  1.00143.15           C  
ANISOU 3207  C   LYS A 416    18806  15616  19968   4503  -2456  -5655       C  
ATOM   3208  O   LYS A 416      22.843   0.212  41.429  1.00143.76           O  
ANISOU 3208  O   LYS A 416    18754  15490  20380   4921  -2446  -5735       O  
ATOM   3209  CB  LYS A 416      21.631   1.073  38.507  1.00158.87           C  
ANISOU 3209  CB  LYS A 416    21022  18009  21334   4258  -2037  -6265       C  
ATOM   3210  CG  LYS A 416      23.115   1.403  38.507  1.00166.99           C  
ANISOU 3210  CG  LYS A 416    21652  19268  22527   4654  -1737  -6399       C  
ATOM   3211  CD  LYS A 416      23.477   2.333  37.361  1.00159.20           C  
ANISOU 3211  CD  LYS A 416    20564  18786  21141   4518  -1380  -6597       C  
ATOM   3212  CE  LYS A 416      24.820   3.003  37.602  1.00170.63           C  
ANISOU 3212  CE  LYS A 416    21503  20565  22764   4798  -1108  -6596       C  
ATOM   3213  NZ  LYS A 416      25.932   2.291  36.914  1.00180.87           N  
ANISOU 3213  NZ  LYS A 416    22724  21768  24231   5173   -737  -7093       N  
ATOM   3214  N   HIS A 417      21.234   1.773  41.614  1.00120.81           N  
ANISOU 3214  N   HIS A 417    15820  13070  17014   4216  -2565  -5260       N  
ATOM   3215  CA  HIS A 417      21.825   2.331  42.825  1.00126.10           C  
ANISOU 3215  CA  HIS A 417    16192  13837  17884   4358  -2656  -4916       C  
ATOM   3216  C   HIS A 417      21.534   1.469  44.049  1.00133.08           C  
ANISOU 3216  C   HIS A 417    17301  14215  19048   4408  -2954  -4678       C  
ATOM   3217  O   HIS A 417      22.428   1.236  44.870  1.00137.57           O  
ANISOU 3217  O   HIS A 417    17744  14635  19890   4727  -3063  -4570       O  
ATOM   3218  CB  HIS A 417      21.324   3.756  43.053  1.00120.26           C  
ANISOU 3218  CB  HIS A 417    15244  13553  16895   4036  -2635  -4601       C  
ATOM   3219  CG  HIS A 417      21.946   4.428  44.237  1.00117.37           C  
ANISOU 3219  CG  HIS A 417    14602  13316  16679   4143  -2714  -4269       C  
ATOM   3220  ND1 HIS A 417      23.167   5.063  44.176  1.00122.04           N  
ANISOU 3220  ND1 HIS A 417    14820  14226  17324   4377  -2559  -4318       N  
ATOM   3221  CD2 HIS A 417      21.521   4.551  45.517  1.00120.67           C  
ANISOU 3221  CD2 HIS A 417    15082  13578  17190   4022  -2928  -3895       C  
ATOM   3222  CE1 HIS A 417      23.465   5.555  45.366  1.00124.24           C  
ANISOU 3222  CE1 HIS A 417    14945  14539  17722   4397  -2718  -3982       C  
ATOM   3223  NE2 HIS A 417      22.483   5.258  46.197  1.00124.40           N  
ANISOU 3223  NE2 HIS A 417    15250  14270  17747   4186  -2934  -3722       N  
ATOM   3224  N   LEU A 418      20.292   0.994  44.193  1.00138.35           N  
ANISOU 3224  N   LEU A 418    18308  14608  19651   4078  -3101  -4587       N  
ATOM   3225  CA  LEU A 418      19.940   0.186  45.358  1.00141.40           C  
ANISOU 3225  CA  LEU A 418    18972  14498  20256   4053  -3353  -4345       C  
ATOM   3226  C   LEU A 418      20.741  -1.108  45.413  1.00140.17           C  
ANISOU 3226  C   LEU A 418    19022  13839  20398   4468  -3449  -4559       C  
ATOM   3227  O   LEU A 418      21.011  -1.624  46.504  1.00135.12           O  
ANISOU 3227  O   LEU A 418    18527  12832  19979   4612  -3675  -4329       O  
ATOM   3228  CB  LEU A 418      18.442  -0.121  45.355  1.00149.95           C  
ANISOU 3228  CB  LEU A 418    20354  15391  21230   3585  -3439  -4264       C  
ATOM   3229  CG  LEU A 418      17.492   1.056  45.585  1.00139.29           C  
ANISOU 3229  CG  LEU A 418    18812  14430  19681   3179  -3398  -3993       C  
ATOM   3230  CD1 LEU A 418      16.056   0.641  45.327  1.00129.69           C  
ANISOU 3230  CD1 LEU A 418    17822  13034  18418   2747  -3471  -4013       C  
ATOM   3231  CD2 LEU A 418      17.645   1.590  47.000  1.00129.02           C  
ANISOU 3231  CD2 LEU A 418    17425  13145  18453   3160  -3466  -3585       C  
ATOM   3232  N   LYS A 419      21.124  -1.649  44.256  1.00146.14           N  
ANISOU 3232  N   LYS A 419    19825  14544  21156   4666  -3286  -4999       N  
ATOM   3233  CA  LYS A 419      21.932  -2.862  44.240  1.00143.12           C  
ANISOU 3233  CA  LYS A 419    19614  13669  21096   5112  -3348  -5247       C  
ATOM   3234  C   LYS A 419      23.354  -2.588  44.708  1.00143.94           C  
ANISOU 3234  C   LYS A 419    19314  13899  21477   5598  -3347  -5214       C  
ATOM   3235  O   LYS A 419      23.989  -3.459  45.315  1.00141.70           O  
ANISOU 3235  O   LYS A 419    19135  13159  21547   5972  -3555  -5204       O  
ATOM   3236  CB  LYS A 419      21.936  -3.458  42.832  1.00144.96           C  
ANISOU 3236  CB  LYS A 419    20020  13829  21230   5172  -3123  -5765       C  
ATOM   3237  CG  LYS A 419      20.572  -3.963  42.379  1.00150.58           C  
ANISOU 3237  CG  LYS A 419    21174  14312  21727   4714  -3203  -5831       C  
ATOM   3238  CD  LYS A 419      20.663  -5.282  41.632  1.00157.41           C  
ANISOU 3238  CD  LYS A 419    22451  14666  22693   4885  -3171  -6272       C  
ATOM   3239  CE  LYS A 419      21.285  -5.097  40.256  1.00153.93           C  
ANISOU 3239  CE  LYS A 419    21900  14517  22070   5055  -2822  -6754       C  
ATOM   3240  NZ  LYS A 419      20.714  -6.052  39.266  1.00167.70           N  
ANISOU 3240  NZ  LYS A 419    24142  15907  23669   4902  -2787  -7161       N  
ATOM   3241  N   SER A 420      23.858  -1.382  44.454  1.00142.85           N  
ANISOU 3241  N   SER A 420    18716  14361  21202   5588  -3145  -5186       N  
ATOM   3242  CA  SER A 420      25.245  -1.056  44.749  1.00137.48           C  
ANISOU 3242  CA  SER A 420    17575  13866  20796   6018  -3111  -5207       C  
ATOM   3243  C   SER A 420      25.493  -0.771  46.223  1.00138.24           C  
ANISOU 3243  C   SER A 420    17585  13883  21058   6061  -3456  -4742       C  
ATOM   3244  O   SER A 420      26.652  -0.760  46.649  1.00152.70           O  
ANISOU 3244  O   SER A 420    19083  15730  23207   6459  -3555  -4735       O  
ATOM   3245  CB  SER A 420      25.673   0.149  43.917  1.00136.24           C  
ANISOU 3245  CB  SER A 420    16989  14372  20404   5929  -2750  -5346       C  
ATOM   3246  OG  SER A 420      24.997   1.316  44.350  1.00125.58           O  
ANISOU 3246  OG  SER A 420    15567  13393  18756   5513  -2793  -4977       O  
ATOM   3247  N   ILE A 421      24.443  -0.535  47.007  1.00127.06           N  
ANISOU 3247  N   ILE A 421    16454  12384  19437   5654  -3638  -4366       N  
ATOM   3248  CA  ILE A 421      24.578  -0.312  48.439  1.00119.20           C  
ANISOU 3248  CA  ILE A 421    15494  11269  18526   5636  -3958  -3923       C  
ATOM   3249  C   ILE A 421      24.065  -1.497  49.245  1.00133.13           C  
ANISOU 3249  C   ILE A 421    17809  12356  20419   5619  -4273  -3754       C  
ATOM   3250  O   ILE A 421      23.959  -1.409  50.472  1.00147.91           O  
ANISOU 3250  O   ILE A 421    19859  14058  22282   5514  -4543  -3361       O  
ATOM   3251  CB  ILE A 421      23.886   0.991  48.873  1.00113.29           C  
ANISOU 3251  CB  ILE A 421    14643  10958  17443   5183  -3885  -3600       C  
ATOM   3252  CG1 ILE A 421      22.378   0.905  48.634  1.00118.59           C  
ANISOU 3252  CG1 ILE A 421    15660  11545  17854   4708  -3800  -3554       C  
ATOM   3253  CG2 ILE A 421      24.486   2.184  48.138  1.00119.47           C  
ANISOU 3253  CG2 ILE A 421    14917  12374  18102   5204  -3601  -3736       C  
ATOM   3254  CD1 ILE A 421      21.626   2.136  49.087  1.00131.97           C  
ANISOU 3254  CD1 ILE A 421    17254  13616  19272   4291  -3722  -3251       C  
ATOM   3255  N   GLY A 422      23.737  -2.605  48.585  1.00142.70           N  
ANISOU 3255  N   GLY A 422    19341  13158  21721   5693  -4239  -4043       N  
ATOM   3256  CA  GLY A 422      23.384  -3.820  49.291  1.00143.60           C  
ANISOU 3256  CA  GLY A 422    20001  12571  21989   5714  -4538  -3911       C  
ATOM   3257  C   GLY A 422      21.987  -3.867  49.864  1.00153.92           C  
ANISOU 3257  C   GLY A 422    21738  13707  23039   5142  -4585  -3622       C  
ATOM   3258  O   GLY A 422      21.759  -4.565  50.857  1.00159.78           O  
ANISOU 3258  O   GLY A 422    22918  13938  23852   5082  -4859  -3354       O  
ATOM   3259  N   LEU A 423      21.038  -3.141  49.275  1.00150.00           N  
ANISOU 3259  N   LEU A 423    21127  13612  22253   4712  -4327  -3666       N  
ATOM   3260  CA  LEU A 423      19.643  -3.220  49.690  1.00145.63           C  
ANISOU 3260  CA  LEU A 423    20909  12910  21516   4161  -4326  -3455       C  
ATOM   3261  C   LEU A 423      18.760  -3.969  48.708  1.00163.29           C  
ANISOU 3261  C   LEU A 423    23395  14936  23712   3935  -4227  -3762       C  
ATOM   3262  O   LEU A 423      17.736  -4.520  49.115  1.00177.97           O  
ANISOU 3262  O   LEU A 423    25629  16452  25539   3550  -4291  -3631       O  
ATOM   3263  CB  LEU A 423      19.064  -1.817  49.908  1.00140.57           C  
ANISOU 3263  CB  LEU A 423    19954  12841  20617   3800  -4158  -3231       C  
ATOM   3264  CG  LEU A 423      19.441  -1.130  51.221  1.00150.59           C  
ANISOU 3264  CG  LEU A 423    21167  14206  21847   3793  -4280  -2823       C  
ATOM   3265  CD1 LEU A 423      18.721   0.203  51.355  1.00147.10           C  
ANISOU 3265  CD1 LEU A 423    20463  14273  21156   3412  -4075  -2647       C  
ATOM   3266  CD2 LEU A 423      19.130  -2.035  52.405  1.00150.61           C  
ANISOU 3266  CD2 LEU A 423    21712  13605  21908   3670  -4519  -2542       C  
ATOM   3267  N   LEU A 424      19.127  -4.006  47.432  1.00159.33           N  
ANISOU 3267  N   LEU A 424    22713  14626  23198   4134  -4064  -4173       N  
ATOM   3268  CA  LEU A 424      18.373  -4.724  46.414  1.00150.40           C  
ANISOU 3268  CA  LEU A 424    21848  13296  22001   3930  -3995  -4503       C  
ATOM   3269  C   LEU A 424      19.187  -5.928  45.963  1.00149.29           C  
ANISOU 3269  C   LEU A 424    21956  12669  22098   4378  -4047  -4846       C  
ATOM   3270  O   LEU A 424      20.378  -5.798  45.660  1.00140.34           O  
ANISOU 3270  O   LEU A 424    20547  11676  21101   4861  -3965  -5030       O  
ATOM   3271  CB  LEU A 424      18.043  -3.809  45.233  1.00144.89           C  
ANISOU 3271  CB  LEU A 424    20837  13182  21034   3749  -3766  -4720       C  
ATOM   3272  CG  LEU A 424      16.971  -4.302  44.261  1.00147.87           C  
ANISOU 3272  CG  LEU A 424    21475  13445  21265   3381  -3750  -4982       C  
ATOM   3273  CD1 LEU A 424      15.698  -4.664  45.008  1.00148.63           C  
ANISOU 3273  CD1 LEU A 424    21830  13247  21394   2895  -3901  -4718       C  
ATOM   3274  CD2 LEU A 424      16.688  -3.242  43.212  1.00148.46           C  
ANISOU 3274  CD2 LEU A 424    21244  14124  21042   3205  -3585  -5119       C  
ATOM   3275  N   SER A 425      18.544  -7.092  45.929  1.00163.80           N  
ANISOU 3275  N   SER A 425    24303  13926  24009   4213  -4168  -4942       N  
ATOM   3276  CA  SER A 425      19.258  -8.335  45.680  1.00171.36           C  
ANISOU 3276  CA  SER A 425    25580  14300  25230   4644  -4252  -5232       C  
ATOM   3277  C   SER A 425      19.930  -8.303  44.309  1.00176.28           C  
ANISOU 3277  C   SER A 425    25999  15158  25820   4954  -3991  -5749       C  
ATOM   3278  O   SER A 425      19.334  -7.827  43.334  1.00178.27           O  
ANISOU 3278  O   SER A 425    26170  15784  25780   4644  -3805  -5951       O  
ATOM   3279  CB  SER A 425      18.303  -9.528  45.763  1.00163.70           C  
ANISOU 3279  CB  SER A 425    25229  12679  24292   4316  -4401  -5267       C  
ATOM   3280  OG  SER A 425      17.498  -9.460  46.926  1.00155.78           O  
ANISOU 3280  OG  SER A 425    24416  11525  23250   3902  -4558  -4806       O  
ATOM   3281  N   PRO A 426      21.166  -8.798  44.195  1.00170.66           N  
ANISOU 3281  N   PRO A 426    25208  14232  25404   5560  -3968  -5979       N  
ATOM   3282  CA  PRO A 426      21.812  -8.880  42.874  1.00176.15           C  
ANISOU 3282  CA  PRO A 426    25760  15095  26073   5849  -3651  -6522       C  
ATOM   3283  C   PRO A 426      21.079  -9.779  41.891  1.00175.85           C  
ANISOU 3283  C   PRO A 426    26229  14700  25887   5616  -3580  -6916       C  
ATOM   3284  O   PRO A 426      21.480  -9.839  40.721  1.00172.94           O  
ANISOU 3284  O   PRO A 426    25800  14522  25385   5731  -3263  -7336       O  
ATOM   3285  CB  PRO A 426      23.206  -9.437  43.198  1.00164.73           C  
ANISOU 3285  CB  PRO A 426    24107  13466  25017   6451  -3633  -6540       C  
ATOM   3286  CG  PRO A 426      23.437  -9.070  44.629  1.00155.99           C  
ANISOU 3286  CG  PRO A 426    22856  12326  24088   6530  -3963  -6028       C  
ATOM   3287  CD  PRO A 426      22.089  -9.155  45.286  1.00153.05           C  
ANISOU 3287  CD  PRO A 426    22944  11664  23543   6018  -4221  -5740       C  
ATOM   3288  N   ASP A 427      20.030 -10.476  42.322  1.00177.76           N  
ANISOU 3288  N   ASP A 427    26954  14481  26104   5223  -3823  -6748       N  
ATOM   3289  CA  ASP A 427      19.251 -11.348  41.457  1.00180.63           C  
ANISOU 3289  CA  ASP A 427    27791  14534  26305   4898  -3778  -7050       C  
ATOM   3290  C   ASP A 427      17.957 -10.697  40.983  1.00186.01           C  
ANISOU 3290  C   ASP A 427    28489  15567  26620   4255  -3800  -7023       C  
ATOM   3291  O   ASP A 427      17.077 -11.393  40.468  1.00179.97           O  
ANISOU 3291  O   ASP A 427    28153  14488  25741   3883  -3881  -7215       O  
ATOM   3292  CB  ASP A 427      18.954 -12.665  42.174  1.00175.18           C  
ANISOU 3292  CB  ASP A 427    27597  13139  25825   4818  -3985  -6851       C  
ATOM   3293  CG  ASP A 427      20.140 -13.608  42.168  1.00187.27           C  
ANISOU 3293  CG  ASP A 427    29162  14344  27646   5368  -3880  -6960       C  
ATOM   3294  OD1 ASP A 427      20.979 -13.502  41.247  1.00189.80           O  
ANISOU 3294  OD1 ASP A 427    29237  14914  27962   5705  -3571  -7326       O  
ATOM   3295  OD2 ASP A 427      20.239 -14.451  43.084  1.00198.83           O1-
ANISOU 3295  OD2 ASP A 427    30902  15303  29341   5453  -4096  -6680       O1-
ATOM   3296  N   PHE A 428      17.820  -9.386  41.154  1.00192.46           N  
ANISOU 3296  N   PHE A 428    28818  17054  27253   4088  -3732  -6748       N  
ATOM   3297  CA  PHE A 428      16.714  -8.626  40.588  1.00196.71           C  
ANISOU 3297  CA  PHE A 428    29252  18043  27447   3529  -3724  -6703       C  
ATOM   3298  C   PHE A 428      17.201  -7.943  39.319  1.00204.23           C  
ANISOU 3298  C   PHE A 428    29988  19504  28106   3647  -3460  -7051       C  
ATOM   3299  O   PHE A 428      18.248  -7.287  39.326  1.00200.61           O  
ANISOU 3299  O   PHE A 428    29153  19391  27679   4032  -3260  -7056       O  
ATOM   3300  CB  PHE A 428      16.188  -7.591  41.587  1.00182.69           C  
ANISOU 3300  CB  PHE A 428    27114  16646  25652   3258  -3811  -6178       C  
ATOM   3301  CG  PHE A 428      14.958  -6.857  41.119  1.00193.23           C  
ANISOU 3301  CG  PHE A 428    28319  18380  26718   2697  -3851  -6101       C  
ATOM   3302  CD1 PHE A 428      15.061  -5.760  40.276  1.00189.39           C  
ANISOU 3302  CD1 PHE A 428    27501  18512  25945   2670  -3710  -6191       C  
ATOM   3303  CD2 PHE A 428      13.699  -7.258  41.533  1.00199.80           C  
ANISOU 3303  CD2 PHE A 428    29353  18959  27604   2191  -4038  -5933       C  
ATOM   3304  CE1 PHE A 428      13.933  -5.090  39.846  1.00191.76           C  
ANISOU 3304  CE1 PHE A 428    27682  19148  26031   2190  -3805  -6108       C  
ATOM   3305  CE2 PHE A 428      12.567  -6.588  41.110  1.00196.95           C  
ANISOU 3305  CE2 PHE A 428    28806  18960  27065   1704  -4104  -5870       C  
ATOM   3306  CZ  PHE A 428      12.684  -5.502  40.267  1.00194.93           C  
ANISOU 3306  CZ  PHE A 428    28225  19300  26538   1723  -4013  -5952       C  
ATOM   3307  N   GLN A 429      16.450  -8.102  38.233  1.00207.77           N  
ANISOU 3307  N   GLN A 429    30694  19991  28259   3290  -3466  -7341       N  
ATOM   3308  CA  GLN A 429      16.815  -7.522  36.949  1.00207.78           C  
ANISOU 3308  CA  GLN A 429    30616  20430  27902   3328  -3225  -7685       C  
ATOM   3309  C   GLN A 429      15.605  -6.838  36.333  1.00196.30           C  
ANISOU 3309  C   GLN A 429    29156  19342  26085   2750  -3383  -7607       C  
ATOM   3310  O   GLN A 429      14.494  -7.377  36.363  1.00182.87           O  
ANISOU 3310  O   GLN A 429    27724  17365  24395   2329  -3647  -7573       O  
ATOM   3311  CB  GLN A 429      17.367  -8.586  35.995  1.00202.51           C  
ANISOU 3311  CB  GLN A 429    30389  19356  27199   3573  -3051  -8258       C  
ATOM   3312  CG  GLN A 429      18.222  -8.021  34.874  1.00205.08           C  
ANISOU 3312  CG  GLN A 429    30593  20104  27224   3789  -2672  -8625       C  
ATOM   3313  CD  GLN A 429      19.534  -7.450  35.376  1.00199.13           C  
ANISOU 3313  CD  GLN A 429    29332  19618  26710   4314  -2409  -8530       C  
ATOM   3314  OE1 GLN A 429      19.696  -6.234  35.480  1.00185.23           O  
ANISOU 3314  OE1 GLN A 429    27138  18439  24803   4253  -2326  -8278       O  
ATOM   3315  NE2 GLN A 429      20.478  -8.328  35.694  1.00188.50           N  
ANISOU 3315  NE2 GLN A 429    28031  17832  25759   4835  -2298  -8731       N  
ATOM   3316  N   GLU A 430      15.829  -5.652  35.771  1.00186.78           N  
ANISOU 3316  N   GLU A 430    27641  18747  24578   2727  -3235  -7577       N  
ATOM   3317  CA  GLU A 430      14.734  -4.855  35.231  1.00178.01           C  
ANISOU 3317  CA  GLU A 430    26472  18017  23147   2228  -3429  -7452       C  
ATOM   3318  C   GLU A 430      14.174  -5.509  33.976  1.00189.53           C  
ANISOU 3318  C   GLU A 430    28431  19292  24289   1939  -3531  -7874       C  
ATOM   3319  O   GLU A 430      14.875  -5.639  32.967  1.00199.54           O  
ANISOU 3319  O   GLU A 430    29930  20611  25274   2111  -3285  -8278       O  
ATOM   3320  CB  GLU A 430      15.200  -3.435  34.915  1.00183.97           C  
ANISOU 3320  CB  GLU A 430    26838  19424  23640   2300  -3250  -7316       C  
ATOM   3321  CG  GLU A 430      15.868  -2.702  36.065  1.00180.45           C  
ANISOU 3321  CG  GLU A 430    25908  19195  23460   2586  -3134  -6936       C  
ATOM   3322  CD  GLU A 430      17.348  -3.010  36.166  1.00182.38           C  
ANISOU 3322  CD  GLU A 430    26068  19358  23870   3130  -2814  -7139       C  
ATOM   3323  OE1 GLU A 430      18.053  -2.862  35.146  1.00180.50           O  
ANISOU 3323  OE1 GLU A 430    25893  19314  23375   3275  -2530  -7490       O  
ATOM   3324  OE2 GLU A 430      17.806  -3.401  37.261  1.00185.18           O1-
ANISOU 3324  OE2 GLU A 430    26295  19450  24614   3405  -2848  -6954       O1-
ATOM   3325  N   ASP A 431      12.917  -5.924  34.043  1.00198.20           N  
ANISOU 3325  N   ASP A 431    29700  20176  25433   1479  -3881  -7794       N  
ATOM   3326  CA  ASP A 431      12.148  -6.310  32.873  1.00197.31           C  
ANISOU 3326  CA  ASP A 431    30002  19981  24984   1083  -4088  -8116       C  
ATOM   3327  C   ASP A 431      11.312  -5.122  32.411  1.00180.47           C  
ANISOU 3327  C   ASP A 431    27610  18390  22571    712  -4322  -7897       C  
ATOM   3328  O   ASP A 431      11.068  -4.179  33.167  1.00171.98           O  
ANISOU 3328  O   ASP A 431    26046  17643  21654    696  -4366  -7474       O  
ATOM   3329  CB  ASP A 431      11.258  -7.514  33.187  1.00192.17           C  
ANISOU 3329  CB  ASP A 431    29685  18749  24581    771  -4365  -8177       C  
ATOM   3330  CG  ASP A 431      10.212  -7.203  34.235  1.00182.58           C  
ANISOU 3330  CG  ASP A 431    28108  17578  23685    440  -4621  -7709       C  
ATOM   3331  OD1 ASP A 431       9.161  -6.645  33.874  1.00177.36           O  
ANISOU 3331  OD1 ASP A 431    27288  17196  22905      6  -4904  -7595       O  
ATOM   3332  OD2 ASP A 431      10.444  -7.506  35.424  1.00178.34           O1-
ANISOU 3332  OD2 ASP A 431    27448  16793  23522    615  -4539  -7457       O1-
ATOM   3333  N   ASN A 432      10.873  -5.171  31.152  1.00165.00           N  
ANISOU 3333  N   ASN A 432    18469  15568  28654   3085  -2078  -6878       N  
ATOM   3334  CA  ASN A 432      10.152  -4.028  30.602  1.00153.20           C  
ANISOU 3334  CA  ASN A 432    17042  14571  26596   2887  -1879  -6971       C  
ATOM   3335  C   ASN A 432       8.801  -3.794  31.271  1.00154.79           C  
ANISOU 3335  C   ASN A 432    17513  14468  26831   2613  -1920  -6543       C  
ATOM   3336  O   ASN A 432       8.200  -2.738  31.047  1.00152.16           O  
ANISOU 3336  O   ASN A 432    17271  14632  25910   2386  -1759  -6378       O  
ATOM   3337  CB  ASN A 432       9.959  -4.193  29.092  1.00155.61           C  
ANISOU 3337  CB  ASN A 432    17167  15312  26647   2840  -1764  -7616       C  
ATOM   3338  CG  ASN A 432       9.074  -5.371  28.737  1.00165.45           C  
ANISOU 3338  CG  ASN A 432    18422  16150  28290   2726  -1899  -7796       C  
ATOM   3339  OD1 ASN A 432       8.963  -6.333  29.496  1.00159.79           O  
ANISOU 3339  OD1 ASN A 432    17780  14809  28125   2752  -2087  -7538       O  
ATOM   3340  ND2 ASN A 432       8.433  -5.297  27.576  1.00165.92           N  
ANISOU 3340  ND2 ASN A 432    18406  16577  28058   2590  -1808  -8223       N  
ATOM   3341  N   GLU A 433       8.317  -4.730  32.092  1.00153.03           N  
ANISOU 3341  N   GLU A 433    17420  13605  27118   2542  -2106  -6188       N  
ATOM   3342  CA  GLU A 433       7.000  -4.571  32.704  1.00140.55           C  
ANISOU 3342  CA  GLU A 433    16071  11769  25564   2241  -2127  -5773       C  
ATOM   3343  C   GLU A 433       7.069  -3.745  33.987  1.00130.82           C  
ANISOU 3343  C   GLU A 433    15031  10644  24032   2135  -2092  -4994       C  
ATOM   3344  O   GLU A 433       6.273  -2.819  34.175  1.00116.43           O  
ANISOU 3344  O   GLU A 433    13338   9168  21733   1879  -1959  -4680       O  
ATOM   3345  CB  GLU A 433       6.373  -5.941  32.970  1.00132.63           C  
ANISOU 3345  CB  GLU A 433    15114  10149  25129   2137  -2303  -5676       C  
ATOM   3346  CG  GLU A 433       5.889  -6.648  31.712  1.00143.32           C  
ANISOU 3346  CG  GLU A 433    16312  11590  26554   2082  -2295  -6273       C  
ATOM   3347  CD  GLU A 433       4.940  -7.792  32.010  1.00152.57           C  
ANISOU 3347  CD  GLU A 433    17562  12193  28216   1890  -2440  -6119       C  
ATOM   3348  OE1 GLU A 433       4.689  -8.063  33.203  1.00154.21           O  
ANISOU 3348  OE1 GLU A 433    17948  11949  28694   1792  -2539  -5529       O  
ATOM   3349  OE2 GLU A 433       4.451  -8.425  31.050  1.00159.55           O1-
ANISOU 3349  OE2 GLU A 433    18322  13100  29198   1830  -2454  -6581       O1-
ATOM   3350  N   THR A 434       8.005  -4.064  34.889  1.00152.49           N  
ANISOU 3350  N   THR A 434    17789  13099  27051   2336  -2223  -4687       N  
ATOM   3351  CA  THR A 434       8.183  -3.217  36.066  1.00144.12           C  
ANISOU 3351  CA  THR A 434    16894  12219  25647   2250  -2189  -4001       C  
ATOM   3352  C   THR A 434       8.649  -1.822  35.676  1.00130.82           C  
ANISOU 3352  C   THR A 434    15151  11296  23258   2243  -1975  -4050       C  
ATOM   3353  O   THR A 434       8.378  -0.853  36.394  1.00118.88           O  
ANISOU 3353  O   THR A 434    13791  10059  21317   2072  -1885  -3562       O  
ATOM   3354  CB  THR A 434       9.177  -3.846  37.046  1.00141.81           C  
ANISOU 3354  CB  THR A 434    16606  11501  25774   2489  -2398  -3695       C  
ATOM   3355  OG1 THR A 434      10.354  -4.265  36.344  1.00145.38           O  
ANISOU 3355  OG1 THR A 434    16803  11971  26464   2838  -2453  -4235       O  
ATOM   3356  CG2 THR A 434       8.550  -5.036  37.756  1.00127.46           C  
ANISOU 3356  CG2 THR A 434    14931   8917  24580   2409  -2613  -3397       C  
ATOM   3357  N   GLU A 435       9.344  -1.706  34.543  1.00150.96           N  
ANISOU 3357  N   GLU A 435    17479  14193  25685   2418  -1888  -4641       N  
ATOM   3358  CA  GLU A 435       9.771  -0.402  34.048  1.00154.36           C  
ANISOU 3358  CA  GLU A 435    17848  15348  25453   2382  -1678  -4707       C  
ATOM   3359  C   GLU A 435       8.576   0.500  33.763  1.00142.49           C  
ANISOU 3359  C   GLU A 435    16490  14190  23460   2071  -1530  -4563       C  
ATOM   3360  O   GLU A 435       8.618   1.706  34.035  1.00131.73           O  
ANISOU 3360  O   GLU A 435    15209  13260  21581   1956  -1404  -4253       O  
ATOM   3361  CB  GLU A 435      10.627  -0.592  32.795  1.00166.50           C  
ANISOU 3361  CB  GLU A 435    19108  17182  26974   2598  -1605  -5406       C  
ATOM   3362  CG  GLU A 435      11.064   0.681  32.101  1.00177.14           C  
ANISOU 3362  CG  GLU A 435    20372  19288  27643   2537  -1378  -5524       C  
ATOM   3363  CD  GLU A 435      11.474   0.428  30.656  1.00188.19           C  
ANISOU 3363  CD  GLU A 435    21520  21018  28964   2658  -1274  -6263       C  
ATOM   3364  OE1 GLU A 435      10.789  -0.361  29.967  1.00175.68           O  
ANISOU 3364  OE1 GLU A 435    19904  19222  27623   2641  -1325  -6668       O  
ATOM   3365  OE2 GLU A 435      12.478   1.019  30.207  1.00188.87           O1-
ANISOU 3365  OE2 GLU A 435    21432  21593  28735   2755  -1137  -6450       O1-
ATOM   3366  N   ILE A 436       7.492  -0.070  33.237  1.00128.01           N  
ANISOU 3366  N   ILE A 436    14682  12150  21805   1934  -1560  -4787       N  
ATOM   3367  CA  ILE A 436       6.319   0.731  32.903  1.00123.74           C  
ANISOU 3367  CA  ILE A 436    14248  11933  20835   1660  -1443  -4689       C  
ATOM   3368  C   ILE A 436       5.527   1.084  34.157  1.00119.21           C  
ANISOU 3368  C   ILE A 436    13896  11176  20223   1452  -1460  -4030       C  
ATOM   3369  O   ILE A 436       5.058   2.219  34.303  1.00123.20           O  
ANISOU 3369  O   ILE A 436    14498  12071  20241   1289  -1338  -3763       O  
ATOM   3370  CB  ILE A 436       5.453  -0.010  31.867  1.00127.53           C  
ANISOU 3370  CB  ILE A 436    14646  12291  21517   1587  -1481  -5198       C  
ATOM   3371  CG1 ILE A 436       6.166  -0.051  30.514  1.00131.38           C  
ANISOU 3371  CG1 ILE A 436    14916  13156  21845   1756  -1412  -5867       C  
ATOM   3372  CG2 ILE A 436       4.092   0.654  31.723  1.00126.53           C  
ANISOU 3372  CG2 ILE A 436    14633  12385  21058   1298  -1412  -5026       C  
ATOM   3373  CD1 ILE A 436       6.474   1.318  29.942  1.00129.77           C  
ANISOU 3373  CD1 ILE A 436    14694  13686  20926   1703  -1224  -5853       C  
ATOM   3374  N   ASN A 437       5.364   0.126  35.076  1.00114.67           N  
ANISOU 3374  N   ASN A 437    13400  10012  20157   1451  -1610  -3758       N  
ATOM   3375  CA  ASN A 437       4.634   0.397  36.312  1.00110.04           C  
ANISOU 3375  CA  ASN A 437    13015   9274  19523   1242  -1613  -3129       C  
ATOM   3376  C   ASN A 437       5.183   1.628  37.013  1.00111.85           C  
ANISOU 3376  C   ASN A 437    13327   9914  19257   1246  -1513  -2733       C  
ATOM   3377  O   ASN A 437       4.432   2.528  37.406  1.00107.53           O  
ANISOU 3377  O   ASN A 437    12897   9624  18338   1046  -1406  -2428       O  
ATOM   3378  CB  ASN A 437       4.712  -0.812  37.247  1.00105.52           C  
ANISOU 3378  CB  ASN A 437    12512   8031  19551   1278  -1801  -2854       C  
ATOM   3379  CG  ASN A 437       3.791  -1.937  36.833  1.00119.30           C  
ANISOU 3379  CG  ASN A 437    14233   9305  21790   1160  -1895  -3093       C  
ATOM   3380  OD1 ASN A 437       3.303  -1.976  35.706  1.00118.36           O  
ANISOU 3380  OD1 ASN A 437    14004   9347  21621   1119  -1845  -3587       O  
ATOM   3381  ND2 ASN A 437       3.568  -2.875  37.742  1.00134.21           N  
ANISOU 3381  ND2 ASN A 437    16225  10605  24162   1099  -2043  -2740       N  
ATOM   3382  N   PHE A 438       6.503   1.683  37.168  1.00114.00           N  
ANISOU 3382  N   PHE A 438    13521  10253  19539   1479  -1554  -2762       N  
ATOM   3383  CA  PHE A 438       7.128   2.808  37.849  1.00114.95           C  
ANISOU 3383  CA  PHE A 438    13704  10742  19228   1486  -1479  -2413       C  
ATOM   3384  C   PHE A 438       6.884   4.104  37.098  1.00111.10           C  
ANISOU 3384  C   PHE A 438    13202  10844  18165   1377  -1290  -2552       C  
ATOM   3385  O   PHE A 438       6.482   5.113  37.688  1.00110.56           O  
ANISOU 3385  O   PHE A 438    13265  11016  17725   1224  -1205  -2195       O  
ATOM   3386  CB  PHE A 438       8.621   2.531  37.994  1.00112.75           C  
ANISOU 3386  CB  PHE A 438    13294  10431  19113   1767  -1570  -2504       C  
ATOM   3387  CG  PHE A 438       9.438   3.714  38.416  1.00112.66           C  
ANISOU 3387  CG  PHE A 438    13288  10866  18654   1791  -1488  -2287       C  
ATOM   3388  CD1 PHE A 438       9.481   4.125  39.740  1.00119.41           C  
ANISOU 3388  CD1 PHE A 438    14299  11684  19386   1719  -1535  -1739       C  
ATOM   3389  CD2 PHE A 438      10.205   4.388  37.485  1.00115.21           C  
ANISOU 3389  CD2 PHE A 438    13446  11649  18680   1878  -1366  -2643       C  
ATOM   3390  CE1 PHE A 438      10.267   5.202  40.116  1.00128.59           C  
ANISOU 3390  CE1 PHE A 438    15454  13245  20160   1738  -1473  -1578       C  
ATOM   3391  CE2 PHE A 438      10.986   5.459  37.851  1.00109.94           C  
ANISOU 3391  CE2 PHE A 438    12770  11368  17635   1881  -1295  -2454       C  
ATOM   3392  CZ  PHE A 438      11.020   5.869  39.167  1.00123.88           C  
ANISOU 3392  CZ  PHE A 438    14690  13072  19305   1815  -1356  -1935       C  
ATOM   3393  N   LEU A 439       7.114   4.093  35.784  1.00107.32           N  
ANISOU 3393  N   LEU A 439    12566  10607  17606   1453  -1229  -3072       N  
ATOM   3394  CA  LEU A 439       6.990   5.327  35.019  1.00103.20           C  
ANISOU 3394  CA  LEU A 439    12031  10652  16527   1356  -1067  -3180       C  
ATOM   3395  C   LEU A 439       5.562   5.850  35.039  1.00101.59           C  
ANISOU 3395  C   LEU A 439    11964  10522  16113   1112  -1014  -2999       C  
ATOM   3396  O   LEU A 439       5.349   7.059  34.899  1.00 96.67           O  
ANISOU 3396  O   LEU A 439    11402  10299  15031   1007   -906  -2866       O  
ATOM   3397  CB  LEU A 439       7.474   5.114  33.587  1.00104.10           C  
ANISOU 3397  CB  LEU A 439    11947  11023  16583   1469  -1014  -3774       C  
ATOM   3398  CG  LEU A 439       8.885   5.615  33.270  1.00 90.71           C  
ANISOU 3398  CG  LEU A 439    10104   9689  14674   1625   -936  -3922       C  
ATOM   3399  CD1 LEU A 439       9.922   4.691  33.883  1.00111.11           C  
ANISOU 3399  CD1 LEU A 439    12581  11916  17719   1864  -1063  -3946       C  
ATOM   3400  CD2 LEU A 439       9.088   5.705  31.777  1.00111.92           C  
ANISOU 3400  CD2 LEU A 439    12620  12776  17127   1653   -829  -4465       C  
ATOM   3401  N   LEU A 440       4.573   4.974  35.223  1.00105.68           N  
ANISOU 3401  N   LEU A 440    12523  10653  16979   1018  -1095  -2988       N  
ATOM   3402  CA  LEU A 440       3.201   5.455  35.333  1.00104.75           C  
ANISOU 3402  CA  LEU A 440    12505  10608  16687    788  -1046  -2806       C  
ATOM   3403  C   LEU A 440       2.987   6.196  36.643  1.00105.80           C  
ANISOU 3403  C   LEU A 440    12798  10761  16640    683  -1004  -2250       C  
ATOM   3404  O   LEU A 440       2.436   7.304  36.661  1.00105.86           O  
ANISOU 3404  O   LEU A 440    12870  11093  16258    566   -909  -2101       O  
ATOM   3405  CB  LEU A 440       2.214   4.294  35.229  1.00101.78           C  
ANISOU 3405  CB  LEU A 440    12108   9810  16754    689  -1138  -2939       C  
ATOM   3406  CG  LEU A 440       0.766   4.770  35.327  1.00 98.95           C  
ANISOU 3406  CG  LEU A 440    11813   9551  16234    449  -1086  -2775       C  
ATOM   3407  CD1 LEU A 440       0.157   5.042  33.954  1.00 98.40           C  
ANISOU 3407  CD1 LEU A 440    11639   9795  15954    404  -1065  -3207       C  
ATOM   3408  CD2 LEU A 440      -0.032   3.753  36.097  1.00100.94           C  
ANISOU 3408  CD2 LEU A 440    12108   9303  16942    308  -1162  -2575       C  
ATOM   3409  N   LYS A 441       3.386   5.570  37.757  1.00111.15           N  
ANISOU 3409  N   LYS A 441    13541  11086  17607    725  -1086  -1943       N  
ATOM   3410  CA  LYS A 441       3.326   6.213  39.064  1.00111.55           C  
ANISOU 3410  CA  LYS A 441    13738  11180  17468    639  -1052  -1431       C  
ATOM   3411  C   LYS A 441       3.973   7.582  38.992  1.00110.19           C  
ANISOU 3411  C   LYS A 441    13580  11476  16813    682   -955  -1384       C  
ATOM   3412  O   LYS A 441       3.456   8.567  39.527  1.00109.75           O  
ANISOU 3412  O   LYS A 441    13625  11634  16442    556   -872  -1123       O  
ATOM   3413  CB  LYS A 441       4.052   5.358  40.107  1.00122.31           C  
ANISOU 3413  CB  LYS A 441    15146  12161  19165    737  -1182  -1156       C  
ATOM   3414  CG  LYS A 441       4.284   6.068  41.422  1.00133.43           C  
ANISOU 3414  CG  LYS A 441    16690  13690  20317    684  -1160   -667       C  
ATOM   3415  CD  LYS A 441       3.236   5.731  42.468  1.00145.16           C  
ANISOU 3415  CD  LYS A 441    18306  14951  21896    475  -1156   -265       C  
ATOM   3416  CE  LYS A 441       3.456   4.352  43.069  1.00150.97           C  
ANISOU 3416  CE  LYS A 441    19072  15163  23125    512  -1322    -81       C  
ATOM   3417  NZ  LYS A 441       2.627   4.194  44.297  1.00156.78           N  
ANISOU 3417  NZ  LYS A 441    19953  15765  23852    290  -1300    411       N  
ATOM   3418  N   GLN A 442       5.131   7.647  38.334  1.00102.48           N  
ANISOU 3418  N   GLN A 442    12490  10655  15793    857   -964  -1650       N  
ATOM   3419  CA  GLN A 442       5.798   8.928  38.150  1.00 99.54           C  
ANISOU 3419  CA  GLN A 442    12115  10724  14983    875   -869  -1628       C  
ATOM   3420  C   GLN A 442       4.979   9.842  37.253  1.00104.99           C  
ANISOU 3420  C   GLN A 442    12817  11748  15326    748   -764  -1767       C  
ATOM   3421  O   GLN A 442       4.874  11.046  37.515  1.00105.23           O  
ANISOU 3421  O   GLN A 442    12932  12049  15002    666   -689  -1565       O  
ATOM   3422  CB  GLN A 442       7.198   8.709  37.583  1.00100.75           C  
ANISOU 3422  CB  GLN A 442    12110  10984  15189   1073   -889  -1907       C  
ATOM   3423  CG  GLN A 442       8.109   7.920  38.511  1.00102.14           C  
ANISOU 3423  CG  GLN A 442    12260  10851  15696   1229  -1020  -1746       C  
ATOM   3424  CD  GLN A 442       8.572   8.744  39.696  1.00 99.78           C  
ANISOU 3424  CD  GLN A 442    12066  10676  15169   1196  -1024  -1326       C  
ATOM   3425  OE1 GLN A 442       8.103   8.560  40.819  1.00103.85           O  
ANISOU 3425  OE1 GLN A 442    12721  10976  15760   1120  -1083   -953       O  
ATOM   3426  NE2 GLN A 442       9.493   9.668  39.447  1.00 96.42           N  
ANISOU 3426  NE2 GLN A 442    11568  10617  14448   1236   -956  -1390       N  
ATOM   3427  N   ALA A 443       4.375   9.290  36.200  1.00102.73           N  
ANISOU 3427  N   ALA A 443    12448  11437  15146    732   -773  -2112       N  
ATOM   3428  CA  ALA A 443       3.588  10.124  35.301  1.00 88.82           C  
ANISOU 3428  CA  ALA A 443    10693  10003  13052    622   -704  -2237       C  
ATOM   3429  C   ALA A 443       2.336  10.644  35.991  1.00 88.78           C  
ANISOU 3429  C   ALA A 443    10808   9958  12965    459   -685  -1931       C  
ATOM   3430  O   ALA A 443       1.936  11.794  35.781  1.00 85.82           O  
ANISOU 3430  O   ALA A 443    10488   9878  12244    386   -627  -1840       O  
ATOM   3431  CB  ALA A 443       3.220   9.344  34.039  1.00 84.23           C  
ANISOU 3431  CB  ALA A 443     9986   9418  12601    642   -739  -2697       C  
ATOM   3432  N   LEU A 444       1.711   9.814  36.830  1.00 83.16           N  
ANISOU 3432  N   LEU A 444    10134   8885  12579    397   -733  -1763       N  
ATOM   3433  CA  LEU A 444       0.510  10.246  37.537  1.00 79.45           C  
ANISOU 3433  CA  LEU A 444     9748   8398  12041    235   -694  -1489       C  
ATOM   3434  C   LEU A 444       0.799  11.412  38.471  1.00 87.62           C  
ANISOU 3434  C   LEU A 444    10897   9624  12771    218   -625  -1147       C  
ATOM   3435  O   LEU A 444      -0.080  12.248  38.710  1.00 90.55           O  
ANISOU 3435  O   LEU A 444    11316  10146  12942    116   -568  -1013       O  
ATOM   3436  CB  LEU A 444      -0.092   9.079  38.319  1.00 83.10           C  
ANISOU 3436  CB  LEU A 444    10222   8441  12909    149   -744  -1344       C  
ATOM   3437  CG  LEU A 444      -0.814   7.990  37.525  1.00 92.51           C  
ANISOU 3437  CG  LEU A 444    11309   9405  14437     97   -812  -1656       C  
ATOM   3438  CD1 LEU A 444      -1.389   6.944  38.466  1.00 87.95           C  
ANISOU 3438  CD1 LEU A 444    10764   8396  14257    -25   -853  -1423       C  
ATOM   3439  CD2 LEU A 444      -1.908   8.604  36.668  1.00102.32           C  
ANISOU 3439  CD2 LEU A 444    12492  10918  15468     -3   -779  -1842       C  
ATOM   3440  N   THR A 445       2.020  11.492  38.999  1.00 97.43           N  
ANISOU 3440  N   THR A 445    12169  10864  13986    323   -639  -1030       N  
ATOM   3441  CA  THR A 445       2.395  12.545  39.935  1.00 83.38           C  
ANISOU 3441  CA  THR A 445    10493   9254  11936    306   -590   -732       C  
ATOM   3442  C   THR A 445       3.051  13.726  39.229  1.00 86.15           C  
ANISOU 3442  C   THR A 445    10833   9955  11945    349   -544   -843       C  
ATOM   3443  O   THR A 445       2.671  14.880  39.453  1.00 86.34           O  
ANISOU 3443  O   THR A 445    10933  10173  11700    280   -489   -707       O  
ATOM   3444  CB  THR A 445       3.350  11.989  40.995  1.00 82.82           C  
ANISOU 3444  CB  THR A 445    10456   8992  12020    382   -654   -515       C  
ATOM   3445  OG1 THR A 445       2.726  10.894  41.671  1.00 88.60           O  
ANISOU 3445  OG1 THR A 445    11216   9382  13068    319   -704   -360       O  
ATOM   3446  CG2 THR A 445       3.697  13.067  42.011  1.00 95.57           C  
ANISOU 3446  CG2 THR A 445    12173  10796  13342    350   -613   -229       C  
ATOM   3447  N   ILE A 446       4.034  13.449  38.378  1.00 94.93           N  
ANISOU 3447  N   ILE A 446    11844  11147  13078    457   -562  -1091       N  
ATOM   3448  CA  ILE A 446       4.809  14.513  37.748  1.00 98.63           C  
ANISOU 3448  CA  ILE A 446    12294  11954  13227    474   -508  -1166       C  
ATOM   3449  C   ILE A 446       4.048  15.108  36.569  1.00 94.72           C  
ANISOU 3449  C   ILE A 446    11789  11687  12513    404   -472  -1338       C  
ATOM   3450  O   ILE A 446       3.831  16.323  36.497  1.00 93.77           O  
ANISOU 3450  O   ILE A 446    11746  11776  12107    335   -434  -1211       O  
ATOM   3451  CB  ILE A 446       6.190  13.983  37.324  1.00 89.29           C  
ANISOU 3451  CB  ILE A 446    10979  10809  12138    610   -524  -1369       C  
ATOM   3452  CG1 ILE A 446       6.938  13.435  38.542  1.00 96.37           C  
ANISOU 3452  CG1 ILE A 446    11885  11479  13253    694   -595  -1165       C  
ATOM   3453  CG2 ILE A 446       6.996  15.072  36.641  1.00 83.05           C  
ANISOU 3453  CG2 ILE A 446    10153  10393  11010    591   -449  -1437       C  
ATOM   3454  CD1 ILE A 446       8.186  12.653  38.197  1.00100.16           C  
ANISOU 3454  CD1 ILE A 446    12201  11921  13934    863   -642  -1388       C  
ATOM   3455  N   VAL A 447       3.630  14.259  35.627  1.00 91.07           N  
ANISOU 3455  N   VAL A 447    11233  11180  12191    425   -502  -1632       N  
ATOM   3456  CA  VAL A 447       2.908  14.749  34.456  1.00 86.27           C  
ANISOU 3456  CA  VAL A 447    10607  10813  11358    363   -494  -1804       C  
ATOM   3457  C   VAL A 447       1.505  15.198  34.840  1.00 88.50           C  
ANISOU 3457  C   VAL A 447    10970  11039  11616    261   -512  -1629       C  
ATOM   3458  O   VAL A 447       1.015  16.224  34.354  1.00 82.27           O  
ANISOU 3458  O   VAL A 447    10226  10477  10557    209   -508  -1581       O  
ATOM   3459  CB  VAL A 447       2.873  13.671  33.357  1.00 78.24           C  
ANISOU 3459  CB  VAL A 447     9453   9783  10491    413   -530  -2210       C  
ATOM   3460  CG1 VAL A 447       2.045  14.144  32.176  1.00 80.36           C  
ANISOU 3460  CG1 VAL A 447     9705  10323  10505    341   -546  -2377       C  
ATOM   3461  CG2 VAL A 447       4.279  13.323  32.914  1.00 78.28           C  
ANISOU 3461  CG2 VAL A 447     9348   9896  10498    528   -495  -2423       C  
ATOM   3462  N   GLY A 448       0.841  14.447  35.721  1.00 80.12           N  
ANISOU 3462  N   GLY A 448     9920   9678  10843    230   -535  -1522       N  
ATOM   3463  CA  GLY A 448      -0.542  14.752  36.051  1.00 75.13           C  
ANISOU 3463  CA  GLY A 448     9319   9010  10217    130   -538  -1400       C  
ATOM   3464  C   GLY A 448      -0.731  16.151  36.603  1.00 78.65           C  
ANISOU 3464  C   GLY A 448     9868   9622  10394     99   -493  -1146       C  
ATOM   3465  O   GLY A 448      -1.724  16.818  36.300  1.00 95.60           O  
ANISOU 3465  O   GLY A 448    12016  11884  12423     53   -507  -1138       O  
ATOM   3466  N   THR A 449       0.225  16.624  37.405  1.00 83.09           N  
ANISOU 3466  N   THR A 449    10508  10193  10869    132   -454   -955       N  
ATOM   3467  CA  THR A 449       0.087  17.921  38.059  1.00 88.98           C  
ANISOU 3467  CA  THR A 449    11355  11056  11398    102   -416   -732       C  
ATOM   3468  C   THR A 449       0.358  19.100  37.131  1.00 83.00           C  
ANISOU 3468  C   THR A 449    10628  10557  10351    108   -426   -776       C  
ATOM   3469  O   THR A 449      -0.124  20.204  37.408  1.00 79.03           O  
ANISOU 3469  O   THR A 449    10198  10127   9703     82   -422   -640       O  
ATOM   3470  CB  THR A 449       1.020  18.006  39.275  1.00 78.14           C  
ANISOU 3470  CB  THR A 449    10051   9609  10031    121   -386   -526       C  
ATOM   3471  OG1 THR A 449       0.628  19.107  40.105  1.00 76.46           O  
ANISOU 3471  OG1 THR A 449     9930   9464   9659     79   -349   -334       O  
ATOM   3472  CG2 THR A 449       2.473  18.189  38.842  1.00 72.91           C  
ANISOU 3472  CG2 THR A 449     9370   9066   9266    185   -392   -592       C  
ATOM   3473  N   LEU A 450       1.096  18.896  36.040  1.00 81.40           N  
ANISOU 3473  N   LEU A 450    10368  10494  10064    138   -439   -962       N  
ATOM   3474  CA  LEU A 450       1.499  20.021  35.196  1.00 80.23           C  
ANISOU 3474  CA  LEU A 450    10261  10607   9617    116   -440   -953       C  
ATOM   3475  C   LEU A 450       0.324  20.762  34.567  1.00 90.81           C  
ANISOU 3475  C   LEU A 450    11631  12050  10823     81   -500   -938       C  
ATOM   3476  O   LEU A 450       0.316  22.005  34.618  1.00 91.80           O  
ANISOU 3476  O   LEU A 450    11849  12262  10766     56   -512   -770       O  
ATOM   3477  CB  LEU A 450       2.496  19.530  34.141  1.00 77.88           C  
ANISOU 3477  CB  LEU A 450     9871  10479   9243    142   -421  -1177       C  
ATOM   3478  CG  LEU A 450       3.809  19.038  34.749  1.00 93.18           C  
ANISOU 3478  CG  LEU A 450    11763  12347  11295    196   -374  -1177       C  
ATOM   3479  CD1 LEU A 450       4.744  18.514  33.678  1.00106.72           C  
ANISOU 3479  CD1 LEU A 450    13348  14249  12950    236   -341  -1448       C  
ATOM   3480  CD2 LEU A 450       4.469  20.158  35.544  1.00 88.44           C  
ANISOU 3480  CD2 LEU A 450    11257  11792  10555    157   -343   -925       C  
ATOM   3481  N   PRO A 451      -0.675  20.104  33.963  1.00 99.27           N  
ANISOU 3481  N   PRO A 451    12623  13108  11986     81   -557  -1106       N  
ATOM   3482  CA  PRO A 451      -1.828  20.875  33.461  1.00 83.41           C  
ANISOU 3482  CA  PRO A 451    10629  11199   9862     64   -639  -1070       C  
ATOM   3483  C   PRO A 451      -2.594  21.571  34.570  1.00 87.08           C  
ANISOU 3483  C   PRO A 451    11150  11530  10406     66   -630   -865       C  
ATOM   3484  O   PRO A 451      -2.884  22.770  34.468  1.00 84.90           O  
ANISOU 3484  O   PRO A 451    10947  11332   9980     75   -676   -734       O  
ATOM   3485  CB  PRO A 451      -2.677  19.809  32.753  1.00 83.99           C  
ANISOU 3485  CB  PRO A 451    10575  11263  10073     58   -701  -1323       C  
ATOM   3486  CG  PRO A 451      -1.726  18.711  32.442  1.00 83.79           C  
ANISOU 3486  CG  PRO A 451    10485  11211  10139     76   -657  -1528       C  
ATOM   3487  CD  PRO A 451      -0.789  18.681  33.604  1.00 97.60           C  
ANISOU 3487  CD  PRO A 451    12294  12799  11991     98   -569  -1356       C  
ATOM   3488  N   PHE A 452      -2.938  20.832  35.628  1.00 90.98           N  
ANISOU 3488  N   PHE A 452    11608  11822  11138     55   -572   -839       N  
ATOM   3489  CA  PHE A 452      -3.554  21.422  36.813  1.00 84.13           C  
ANISOU 3489  CA  PHE A 452    10781  10860  10325     49   -529   -665       C  
ATOM   3490  C   PHE A 452      -2.802  22.669  37.261  1.00 77.10           C  
ANISOU 3490  C   PHE A 452    10018  10021   9254     68   -509   -494       C  
ATOM   3491  O   PHE A 452      -3.408  23.705  37.558  1.00 75.09           O  
ANISOU 3491  O   PHE A 452     9804   9781   8945     89   -531   -407       O  
ATOM   3492  CB  PHE A 452      -3.594  20.377  37.932  1.00 83.38           C  
ANISOU 3492  CB  PHE A 452    10653  10572  10455     10   -448   -620       C  
ATOM   3493  CG  PHE A 452      -4.168  20.878  39.227  1.00 75.94           C  
ANISOU 3493  CG  PHE A 452     9741   9576   9536    -12   -378   -454       C  
ATOM   3494  CD1 PHE A 452      -3.371  21.533  40.153  1.00 71.93           C  
ANISOU 3494  CD1 PHE A 452     9343   9072   8917      1   -327   -298       C  
ATOM   3495  CD2 PHE A 452      -5.498  20.666  39.534  1.00 88.67           C  
ANISOU 3495  CD2 PHE A 452    11255  11157  11277    -53   -356   -478       C  
ATOM   3496  CE1 PHE A 452      -3.898  21.985  41.346  1.00 76.62           C  
ANISOU 3496  CE1 PHE A 452     9958   9652   9504    -20   -255   -183       C  
ATOM   3497  CE2 PHE A 452      -6.026  21.114  40.725  1.00 83.49           C  
ANISOU 3497  CE2 PHE A 452    10606  10495  10621    -77   -268   -355       C  
ATOM   3498  CZ  PHE A 452      -5.228  21.771  41.633  1.00 74.36           C  
ANISOU 3498  CZ  PHE A 452     9570   9354   9331    -57   -216   -214       C  
ATOM   3499  N   THR A 453      -1.472  22.586  37.299  1.00 72.92           N  
ANISOU 3499  N   THR A 453     9538   9514   8653     64   -474   -465       N  
ATOM   3500  CA  THR A 453      -0.669  23.697  37.799  1.00 74.98           C  
ANISOU 3500  CA  THR A 453     9909   9810   8770     57   -454   -314       C  
ATOM   3501  C   THR A 453      -0.674  24.868  36.822  1.00 73.47           C  
ANISOU 3501  C   THR A 453     9777   9755   8383     49   -526   -279       C  
ATOM   3502  O   THR A 453      -0.858  26.022  37.226  1.00 72.12           O  
ANISOU 3502  O   THR A 453     9692   9555   8156     53   -549   -158       O  
ATOM   3503  CB  THR A 453       0.758  23.223  38.075  1.00 76.80           C  
ANISOU 3503  CB  THR A 453    10142  10044   8997     50   -407   -306       C  
ATOM   3504  OG1 THR A 453       0.742  22.261  39.137  1.00 83.14           O  
ANISOU 3504  OG1 THR A 453    10915  10692   9981     61   -366   -275       O  
ATOM   3505  CG2 THR A 453       1.650  24.391  38.467  1.00 76.29           C  
ANISOU 3505  CG2 THR A 453    10172  10035   8781     20   -397   -173       C  
ATOM   3506  N   TYR A 454      -0.471  24.592  35.531  1.00 77.58           N  
ANISOU 3506  N   TYR A 454    10256  10424   8796     36   -566   -385       N  
ATOM   3507  CA  TYR A 454      -0.476  25.670  34.547  1.00 81.36           C  
ANISOU 3507  CA  TYR A 454    10803  11050   9060      9   -644   -310       C  
ATOM   3508  C   TYR A 454      -1.843  26.336  34.474  1.00 81.51           C  
ANISOU 3508  C   TYR A 454    10837  11020   9113     58   -748   -260       C  
ATOM   3509  O   TYR A 454      -1.939  27.561  34.329  1.00 78.93           O  
ANISOU 3509  O   TYR A 454    10607  10691   8691     58   -820   -111       O  
ATOM   3510  CB  TYR A 454      -0.069  25.143  33.170  1.00 78.51           C  
ANISOU 3510  CB  TYR A 454    10381  10908   8540    -23   -661   -450       C  
ATOM   3511  CG  TYR A 454      -0.506  26.048  32.038  1.00 79.00           C  
ANISOU 3511  CG  TYR A 454    10500  11139   8378    -50   -774   -370       C  
ATOM   3512  CD1 TYR A 454      -0.029  27.350  31.945  1.00 84.57           C  
ANISOU 3512  CD1 TYR A 454    11332  11872   8927   -107   -801   -147       C  
ATOM   3513  CD2 TYR A 454      -1.401  25.609  31.071  1.00 77.45           C  
ANISOU 3513  CD2 TYR A 454    10233  11066   8129    -26   -870   -505       C  
ATOM   3514  CE1 TYR A 454      -0.426  28.188  30.921  1.00 91.27           C  
ANISOU 3514  CE1 TYR A 454    12250  12855   9575   -137   -925    -26       C  
ATOM   3515  CE2 TYR A 454      -1.803  26.442  30.040  1.00 80.97           C  
ANISOU 3515  CE2 TYR A 454    10736  11681   8348    -48   -999   -402       C  
ATOM   3516  CZ  TYR A 454      -1.312  27.729  29.971  1.00 90.04           C  
ANISOU 3516  CZ  TYR A 454    12025  12841   9344   -101  -1028   -144       C  
ATOM   3517  OH  TYR A 454      -1.712  28.558  28.949  1.00111.26           O  
ANISOU 3517  OH  TYR A 454    14786  15678  11811   -126  -1176      4       O  
ATOM   3518  N   MET A 455      -2.913  25.548  34.582  1.00 83.92           N  
ANISOU 3518  N   MET A 455    11035  11273   9579     99   -765   -386       N  
ATOM   3519  CA  MET A 455      -4.255  26.108  34.466  1.00 83.99           C  
ANISOU 3519  CA  MET A 455    11013  11261   9640    157   -870   -371       C  
ATOM   3520  C   MET A 455      -4.638  26.904  35.709  1.00 87.57           C  
ANISOU 3520  C   MET A 455    11510  11559  10205    201   -834   -263       C  
ATOM   3521  O   MET A 455      -5.268  27.963  35.600  1.00 93.17           O  
ANISOU 3521  O   MET A 455    12252  12244  10903    263   -932   -190       O  
ATOM   3522  CB  MET A 455      -5.266  24.992  34.203  1.00 73.26           C  
ANISOU 3522  CB  MET A 455     9496   9910   8430    166   -892   -558       C  
ATOM   3523  CG  MET A 455      -6.703  25.464  34.149  1.00 73.92           C  
ANISOU 3523  CG  MET A 455     9500   9987   8601    231   -998   -571       C  
ATOM   3524  SD  MET A 455      -7.577  25.119  35.684  1.00 81.31           S  
ANISOU 3524  SD  MET A 455    10336  10754   9806    239   -876   -588       S  
ATOM   3525  CE  MET A 455      -8.624  26.564  35.791  1.00 77.70           C  
ANISOU 3525  CE  MET A 455     9865  10292   9365    359   -991   -518       C  
ATOM   3526  N   LEU A 456      -4.270  26.416  36.899  1.00 73.00           N  
ANISOU 3526  N   LEU A 456     9660   9610   8465    176   -703   -259       N  
ATOM   3527  CA  LEU A 456      -4.597  27.145  38.122  1.00 72.42           C  
ANISOU 3527  CA  LEU A 456     9622   9432   8462    210   -654   -189       C  
ATOM   3528  C   LEU A 456      -3.906  28.503  38.157  1.00 78.42           C  
ANISOU 3528  C   LEU A 456    10525  10164   9105    219   -700    -65       C  
ATOM   3529  O   LEU A 456      -4.514  29.506  38.549  1.00 79.62           O  
ANISOU 3529  O   LEU A 456    10705  10243   9306    285   -746    -38       O  
ATOM   3530  CB  LEU A 456      -4.221  26.319  39.355  1.00 79.74           C  
ANISOU 3530  CB  LEU A 456    10531  10293   9472    164   -513   -184       C  
ATOM   3531  CG  LEU A 456      -4.605  26.901  40.723  1.00 66.46           C  
ANISOU 3531  CG  LEU A 456     8867   8554   7831    184   -437   -144       C  
ATOM   3532  CD1 LEU A 456      -4.960  25.793  41.697  1.00 67.04           C  
ANISOU 3532  CD1 LEU A 456     8860   8603   8011    130   -317   -153       C  
ATOM   3533  CD2 LEU A 456      -3.484  27.759  41.301  1.00 68.21           C  
ANISOU 3533  CD2 LEU A 456     9226   8753   7938    170   -424    -54       C  
ATOM   3534  N   GLU A 457      -2.632  28.556  37.762  1.00 79.02           N  
ANISOU 3534  N   GLU A 457    10682  10292   9048    149   -688     -1       N  
ATOM   3535  CA  GLU A 457      -1.932  29.836  37.753  1.00 81.00           C  
ANISOU 3535  CA  GLU A 457    11066  10507   9204    121   -733    127       C  
ATOM   3536  C   GLU A 457      -2.413  30.734  36.623  1.00 83.67           C  
ANISOU 3536  C   GLU A 457    11454  10868   9468    146   -884    208       C  
ATOM   3537  O   GLU A 457      -2.403  31.962  36.766  1.00 84.45           O  
ANISOU 3537  O   GLU A 457    11656  10856   9577    159   -957    315       O  
ATOM   3538  CB  GLU A 457      -0.421  29.622  37.656  1.00 77.35           C  
ANISOU 3538  CB  GLU A 457    10645  10118   8627     21   -669    171       C  
ATOM   3539  CG  GLU A 457       0.402  30.851  38.041  1.00 88.83           C  
ANISOU 3539  CG  GLU A 457    12220  11505  10027    -39   -685    293       C  
ATOM   3540  CD  GLU A 457       0.530  31.047  39.544  1.00 83.21           C  
ANISOU 3540  CD  GLU A 457    11529  10682   9406    -21   -622    269       C  
ATOM   3541  OE1 GLU A 457      -0.488  30.947  40.261  1.00 76.29           O  
ANISOU 3541  OE1 GLU A 457    10614   9737   8636     61   -606    201       O  
ATOM   3542  OE2 GLU A 457       1.657  31.316  40.011  1.00 84.74           O1-
ANISOU 3542  OE2 GLU A 457    11766  10882   9551    -98   -588    309       O1-
ATOM   3543  N   LYS A 458      -2.834  30.154  35.496  1.00 80.32           N  
ANISOU 3543  N   LYS A 458    10963  10580   8974    150   -946    159       N  
ATOM   3544  CA  LYS A 458      -3.352  30.983  34.413  1.00 76.62           C  
ANISOU 3544  CA  LYS A 458    10544  10156   8411    177  -1115    261       C  
ATOM   3545  C   LYS A 458      -4.677  31.626  34.799  1.00 79.11           C  
ANISOU 3545  C   LYS A 458    10825  10334   8900    313  -1221    251       C  
ATOM   3546  O   LYS A 458      -4.925  32.790  34.463  1.00 81.51           O  
ANISOU 3546  O   LYS A 458    11219  10550   9200    358  -1365    390       O  
ATOM   3547  CB  LYS A 458      -3.508  30.167  33.132  1.00 85.70           C  
ANISOU 3547  CB  LYS A 458    11620  11527   9415    149  -1165    183       C  
ATOM   3548  CG  LYS A 458      -3.467  31.032  31.884  1.00 88.29           C  
ANISOU 3548  CG  LYS A 458    12044  11974   9530    115  -1321    353       C  
ATOM   3549  CD  LYS A 458      -4.102  30.356  30.686  1.00 88.94           C  
ANISOU 3549  CD  LYS A 458    12032  12279   9480    128  -1421    248       C  
ATOM   3550  CE  LYS A 458      -3.728  31.088  29.410  1.00 99.84           C  
ANISOU 3550  CE  LYS A 458    13524  13848  10563     49  -1544    442       C  
ATOM   3551  NZ  LYS A 458      -3.761  32.566  29.599  1.00106.80           N  
ANISOU 3551  NZ  LYS A 458    14560  14540  11478     63  -1661    719       N  
ATOM   3552  N   TRP A 459      -5.539  30.886  35.500  1.00 78.52           N  
ANISOU 3552  N   TRP A 459    10610  10233   8992    377  -1154     91       N  
ATOM   3553  CA  TRP A 459      -6.774  31.478  36.001  1.00 84.54           C  
ANISOU 3553  CA  TRP A 459    11300  10885   9934    510  -1223     44       C  
ATOM   3554  C   TRP A 459      -6.483  32.669  36.904  1.00 86.58           C  
ANISOU 3554  C   TRP A 459    11669  10962  10264    550  -1214    114       C  
ATOM   3555  O   TRP A 459      -7.146  33.707  36.808  1.00 85.38           O  
ANISOU 3555  O   TRP A 459    11535  10694  10210    665  -1354    150       O  
ATOM   3556  CB  TRP A 459      -7.599  30.435  36.755  1.00 85.25           C  
ANISOU 3556  CB  TRP A 459    11212  11000  10179    528  -1104   -134       C  
ATOM   3557  CG  TRP A 459      -8.886  30.984  37.300  1.00 86.21           C  
ANISOU 3557  CG  TRP A 459    11215  11055  10486    660  -1145   -216       C  
ATOM   3558  CD1 TRP A 459     -10.095  31.020  36.668  1.00 92.78           C  
ANISOU 3558  CD1 TRP A 459    11902  11940  11409    758  -1284   -288       C  
ATOM   3559  CD2 TRP A 459      -9.085  31.596  38.581  1.00 83.46           C  
ANISOU 3559  CD2 TRP A 459    10863  10598  10250    718  -1050   -262       C  
ATOM   3560  NE1 TRP A 459     -11.036  31.605  37.481  1.00 97.26           N  
ANISOU 3560  NE1 TRP A 459    12360  12434  12162    880  -1273   -379       N  
ATOM   3561  CE2 TRP A 459     -10.441  31.969  38.660  1.00 88.71           C  
ANISOU 3561  CE2 TRP A 459    11364  11256  11085    857  -1122   -375       C  
ATOM   3562  CE3 TRP A 459      -8.249  31.860  39.669  1.00 85.70           C  
ANISOU 3562  CE3 TRP A 459    11252  10812  10499    667   -916   -240       C  
ATOM   3563  CZ2 TRP A 459     -10.979  32.591  39.785  1.00 97.84           C  
ANISOU 3563  CZ2 TRP A 459    12454  12344  12376    950  -1044   -484       C  
ATOM   3564  CZ3 TRP A 459      -8.785  32.479  40.784  1.00 85.96           C  
ANISOU 3564  CZ3 TRP A 459    11236  10782  10644    749   -848   -342       C  
ATOM   3565  CH2 TRP A 459     -10.136  32.839  40.833  1.00 95.08           C  
ANISOU 3565  CH2 TRP A 459    12223  11936  11965    891   -903   -471       C  
ATOM   3566  N   ARG A 460      -5.487  32.540  37.783  1.00 90.09           N  
ANISOU 3566  N   ARG A 460    12183  11372  10674    464  -1067    120       N  
ATOM   3567  CA  ARG A 460      -5.171  33.624  38.708  1.00 91.00           C  
ANISOU 3567  CA  ARG A 460    12397  11325  10855    488  -1056    144       C  
ATOM   3568  C   ARG A 460      -4.498  34.785  37.988  1.00 88.99           C  
ANISOU 3568  C   ARG A 460    12308  10970  10534    449  -1194    324       C  
ATOM   3569  O   ARG A 460      -4.846  35.951  38.214  1.00 97.80           O  
ANISOU 3569  O   ARG A 460    13486  11900  11774    532  -1300    351       O  
ATOM   3570  CB  ARG A 460      -4.287  33.106  39.841  1.00 89.25           C  
ANISOU 3570  CB  ARG A 460    12192  11126  10593    398   -879    100       C  
ATOM   3571  CG  ARG A 460      -5.005  32.177  40.797  1.00 84.30           C  
ANISOU 3571  CG  ARG A 460    11426  10561  10045    427   -743    -39       C  
ATOM   3572  CD  ARG A 460      -4.345  32.188  42.158  1.00 80.54           C  
ANISOU 3572  CD  ARG A 460    10992  10071   9536    377   -613    -67       C  
ATOM   3573  NE  ARG A 460      -2.993  31.648  42.101  1.00 84.74           N  
ANISOU 3573  NE  ARG A 460    11594  10656   9946    259   -569     21       N  
ATOM   3574  CZ  ARG A 460      -2.247  31.390  43.165  1.00 86.29           C  
ANISOU 3574  CZ  ARG A 460    11819  10879  10090    201   -474     20       C  
ATOM   3575  NH1 ARG A 460      -2.689  31.617  44.390  1.00 83.37           N  
ANISOU 3575  NH1 ARG A 460    11430  10508   9740    231   -400    -60       N  
ATOM   3576  NH2 ARG A 460      -1.024  30.895  42.995  1.00 83.40           N  
ANISOU 3576  NH2 ARG A 460    11490  10562   9635    113   -458     94       N  
ATOM   3577  N   TRP A 461      -3.519  34.485  37.127  1.00 82.91           N  
ANISOU 3577  N   TRP A 461    11604  10318   9580    315  -1191    446       N  
ATOM   3578  CA  TRP A 461      -2.876  35.523  36.326  1.00 87.56           C  
ANISOU 3578  CA  TRP A 461    12345  10847  10078    237  -1312    654       C  
ATOM   3579  C   TRP A 461      -3.907  36.392  35.622  1.00 96.48           C  
ANISOU 3579  C   TRP A 461    13503  11866  11288    357  -1527    751       C  
ATOM   3580  O   TRP A 461      -3.769  37.620  35.569  1.00 99.77           O  
ANISOU 3580  O   TRP A 461    14052  12080  11778    360  -1650    895       O  
ATOM   3581  CB  TRP A 461      -1.947  34.888  35.290  1.00 97.52           C  
ANISOU 3581  CB  TRP A 461    13619  12336  11100     87  -1270    741       C  
ATOM   3582  CG  TRP A 461      -0.621  34.438  35.815  1.00 87.68           C  
ANISOU 3582  CG  TRP A 461    12376  11160   9779    -45  -1106    711       C  
ATOM   3583  CD1 TRP A 461      -0.056  34.756  37.013  1.00 96.88           C  
ANISOU 3583  CD1 TRP A 461    13572  12200  11039    -69  -1027    670       C  
ATOM   3584  CD2 TRP A 461       0.311  33.581  35.145  1.00 88.22           C  
ANISOU 3584  CD2 TRP A 461    12396  11459   9665   -159  -1013    701       C  
ATOM   3585  NE1 TRP A 461       1.171  34.149  37.133  1.00102.68           N  
ANISOU 3585  NE1 TRP A 461    14278  13067  11667   -188   -905    655       N  
ATOM   3586  CE2 TRP A 461       1.420  33.422  35.998  1.00 94.74           C  
ANISOU 3586  CE2 TRP A 461    13218  12275  10505   -239   -888    666       C  
ATOM   3587  CE3 TRP A 461       0.315  32.933  33.906  1.00 93.08           C  
ANISOU 3587  CE3 TRP A 461    12959  12304  10102   -196  -1027    694       C  
ATOM   3588  CZ2 TRP A 461       2.520  32.641  35.652  1.00 97.58           C  
ANISOU 3588  CZ2 TRP A 461    13509  12830  10737   -337   -780    626       C  
ATOM   3589  CZ3 TRP A 461       1.408  32.160  33.565  1.00 87.36           C  
ANISOU 3589  CZ3 TRP A 461    12173  11780   9240   -298   -903    632       C  
ATOM   3590  CH2 TRP A 461       2.495  32.020  34.434  1.00 93.23           C  
ANISOU 3590  CH2 TRP A 461    12900  12492  10031   -360   -782    600       C  
ATOM   3591  N   MET A 462      -4.955  35.768  35.083  1.00 94.98           N  
ANISOU 3591  N   MET A 462    13187  11795  11106    459  -1590    672       N  
ATOM   3592  CA  MET A 462      -5.981  36.512  34.364  1.00 99.36           C  
ANISOU 3592  CA  MET A 462    13744  12272  11736    593  -1823    762       C  
ATOM   3593  C   MET A 462      -6.884  37.273  35.327  1.00101.14           C  
ANISOU 3593  C   MET A 462    13919  12257  12251    776  -1874    648       C  
ATOM   3594  O   MET A 462      -7.198  38.448  35.097  1.00109.41           O  
ANISOU 3594  O   MET A 462    15055  13094  13421    870  -2066    772       O  
ATOM   3595  CB  MET A 462      -6.796  35.554  33.497  1.00 90.18           C  
ANISOU 3595  CB  MET A 462    12436  11341  10488    636  -1881    682       C  
ATOM   3596  CG  MET A 462      -5.991  34.909  32.383  1.00 97.29           C  
ANISOU 3596  CG  MET A 462    13380  12497  11089    475  -1859    769       C  
ATOM   3597  SD  MET A 462      -6.881  33.562  31.582  1.00 88.23           S  
ANISOU 3597  SD  MET A 462    12035  11622   9865    511  -1889    575       S  
ATOM   3598  CE  MET A 462      -8.250  34.449  30.845  1.00111.80           C  
ANISOU 3598  CE  MET A 462    14990  14562  12925    688  -2205    679       C  
ATOM   3599  N   VAL A 463      -7.323  36.613  36.407  1.00 89.76           N  
ANISOU 3599  N   VAL A 463    12332  10848  10924    831  -1707    409       N  
ATOM   3600  CA  VAL A 463      -8.143  37.279  37.421  1.00 90.29           C  
ANISOU 3600  CA  VAL A 463    12324  10738  11243    998  -1712    250       C  
ATOM   3601  C   VAL A 463      -7.483  38.575  37.868  1.00 92.48           C  
ANISOU 3601  C   VAL A 463    12778  10752  11608    994  -1769    330       C  
ATOM   3602  O   VAL A 463      -8.101  39.646  37.863  1.00 99.58           O  
ANISOU 3602  O   VAL A 463    13696  11428  12712   1151  -1940    333       O  
ATOM   3603  CB  VAL A 463      -8.395  36.339  38.615  1.00 89.11           C  
ANISOU 3603  CB  VAL A 463    12022  10706  11129    986  -1473     18       C  
ATOM   3604  CG1 VAL A 463      -8.914  37.124  39.807  1.00 89.72           C  
ANISOU 3604  CG1 VAL A 463    12050  10632  11406   1119  -1431   -160       C  
ATOM   3605  CG2 VAL A 463      -9.398  35.274  38.239  1.00 87.22           C  
ANISOU 3605  CG2 VAL A 463    11578  10656  10907   1024  -1456    -88       C  
ATOM   3606  N   PHE A 464      -6.204  38.496  38.238  1.00 89.73           N  
ANISOU 3606  N   PHE A 464    12553  10414  11128    816  -1642    388       N  
ATOM   3607  CA  PHE A 464      -5.470  39.693  38.628  1.00 96.24           C  
ANISOU 3607  CA  PHE A 464    13544  10989  12036    772  -1697    460       C  
ATOM   3608  C   PHE A 464      -5.346  40.667  37.463  1.00 98.88           C  
ANISOU 3608  C   PHE A 464    14029  11158  12381    755  -1934    738       C  
ATOM   3609  O   PHE A 464      -5.456  41.885  37.647  1.00109.06           O  
ANISOU 3609  O   PHE A 464    15418  12144  13875    827  -2078    779       O  
ATOM   3610  CB  PHE A 464      -4.090  39.303  39.155  1.00102.57           C  
ANISOU 3610  CB  PHE A 464    14417  11879  12674    567  -1522    474       C  
ATOM   3611  CG  PHE A 464      -4.133  38.393  40.349  1.00 97.85           C  
ANISOU 3611  CG  PHE A 464    13697  11430  12051    574  -1312    249       C  
ATOM   3612  CD1 PHE A 464      -5.130  38.520  41.303  1.00 97.89           C  
ANISOU 3612  CD1 PHE A 464    13589  11392  12214    732  -1268     24       C  
ATOM   3613  CD2 PHE A 464      -3.183  37.399  40.509  1.00 80.09           C  
ANISOU 3613  CD2 PHE A 464    11438   9374   9618    422  -1160    270       C  
ATOM   3614  CE1 PHE A 464      -5.169  37.679  42.400  1.00 84.09           C  
ANISOU 3614  CE1 PHE A 464    11738   9806  10407    711  -1070   -143       C  
ATOM   3615  CE2 PHE A 464      -3.218  36.556  41.600  1.00 76.52           C  
ANISOU 3615  CE2 PHE A 464    10890   9046   9140    422   -989    111       C  
ATOM   3616  CZ  PHE A 464      -4.211  36.696  42.547  1.00 77.63           C  
ANISOU 3616  CZ  PHE A 464    10934   9156   9404    554   -940    -80       C  
ATOM   3617  N   LYS A 465      -5.127  40.147  36.252  1.00 97.72           N  
ANISOU 3617  N   LYS A 465    13904  11207  12016    656  -1982    931       N  
ATOM   3618  CA  LYS A 465      -4.993  41.002  35.078  1.00102.44           C  
ANISOU 3618  CA  LYS A 465    14654  11702  12565    611  -2204   1239       C  
ATOM   3619  C   LYS A 465      -6.258  41.799  34.791  1.00 97.57           C  
ANISOU 3619  C   LYS A 465    14014  10877  12183    848  -2458   1268       C  
ATOM   3620  O   LYS A 465      -6.179  42.860  34.163  1.00 99.02           O  
ANISOU 3620  O   LYS A 465    14354  10838  12431    843  -2676   1528       O  
ATOM   3621  CB  LYS A 465      -4.624  40.158  33.854  1.00109.26           C  
ANISOU 3621  CB  LYS A 465    15513  12895  13106    470  -2188   1390       C  
ATOM   3622  CG  LYS A 465      -3.299  40.526  33.204  1.00121.69           C  
ANISOU 3622  CG  LYS A 465    17254  14518  14465    216  -2166   1654       C  
ATOM   3623  CD  LYS A 465      -2.759  39.382  32.357  1.00116.47           C  
ANISOU 3623  CD  LYS A 465    16530  14251  13473     73  -2044   1664       C  
ATOM   3624  CE  LYS A 465      -1.449  39.767  31.687  1.00115.43           C  
ANISOU 3624  CE  LYS A 465    16533  14212  13112   -189  -2002   1914       C  
ATOM   3625  NZ  LYS A 465      -0.811  38.616  30.992  1.00 87.13           N  
ANISOU 3625  NZ  LYS A 465    12859  11028   9219   -320  -1845   1854       N  
ATOM   3626  N   GLY A 466      -7.417  41.319  35.242  1.00114.43           N  
ANISOU 3626  N   GLY A 466    15948  13072  14460   1051  -2442   1016       N  
ATOM   3627  CA  GLY A 466      -8.692  41.929  34.928  1.00117.59           C  
ANISOU 3627  CA  GLY A 466    16269  13324  15086   1300  -2685   1009       C  
ATOM   3628  C   GLY A 466      -9.439  41.263  33.792  1.00107.75           C  
ANISOU 3628  C   GLY A 466    14916  12332  13692   1349  -2816   1086       C  
ATOM   3629  O   GLY A 466     -10.577  41.656  33.504  1.00103.60           O  
ANISOU 3629  O   GLY A 466    14285  11725  13352   1570  -3032   1064       O  
ATOM   3630  N   GLU A 467      -8.837  40.255  33.156  1.00101.73           N  
ANISOU 3630  N   GLU A 467    14160  11881  12611   1157  -2699   1148       N  
ATOM   3631  CA  GLU A 467      -9.416  39.653  31.963  1.00 96.58           C  
ANISOU 3631  CA  GLU A 467    13429  11492  11776   1173  -2839   1221       C  
ATOM   3632  C   GLU A 467     -10.667  38.836  32.257  1.00 96.43           C  
ANISOU 3632  C   GLU A 467    13135  11611  11894   1336  -2817    930       C  
ATOM   3633  O   GLU A 467     -11.407  38.508  31.324  1.00113.85           O  
ANISOU 3633  O   GLU A 467    15244  13995  14020   1399  -2990    957       O  
ATOM   3634  CB  GLU A 467      -8.382  38.765  31.270  1.00107.95           C  
ANISOU 3634  CB  GLU A 467    14934  13233  12849    925  -2695   1303       C  
ATOM   3635  CG  GLU A 467      -7.117  39.486  30.831  1.00116.83           C  
ANISOU 3635  CG  GLU A 467    16300  14294  13796    724  -2700   1602       C  
ATOM   3636  CD  GLU A 467      -6.117  38.547  30.181  1.00122.90           C  
ANISOU 3636  CD  GLU A 467    17085  15402  14209    496  -2532   1625       C  
ATOM   3637  OE1 GLU A 467      -6.418  37.339  30.078  1.00118.53           O  
ANISOU 3637  OE1 GLU A 467    16370  15096  13571    507  -2427   1401       O  
ATOM   3638  OE2 GLU A 467      -5.039  39.015  29.759  1.00126.01           O1-
ANISOU 3638  OE2 GLU A 467    17643  15812  14422    303  -2505   1856       O1-
ATOM   3639  N   ILE A 468     -10.920  38.491  33.514  1.00 86.64           N  
ANISOU 3639  N   ILE A 468    11760  10317  10840   1390  -2610    656       N  
ATOM   3640  CA  ILE A 468     -12.082  37.699  33.889  1.00 88.87           C  
ANISOU 3640  CA  ILE A 468    11767  10739  11261   1508  -2553    383       C  
ATOM   3641  C   ILE A 468     -12.897  38.493  34.903  1.00 96.23           C  
ANISOU 3641  C   ILE A 468    12586  11449  12528   1724  -2570    208       C  
ATOM   3642  O   ILE A 468     -12.415  38.765  36.007  1.00100.96           O  
ANISOU 3642  O   ILE A 468    13236  11918  13206   1697  -2390    107       O  
ATOM   3643  CB  ILE A 468     -11.693  36.325  34.460  1.00 84.75           C  
ANISOU 3643  CB  ILE A 468    11154  10420  10627   1345  -2256    204       C  
ATOM   3644  CG1 ILE A 468     -10.819  35.561  33.463  1.00 83.99           C  
ANISOU 3644  CG1 ILE A 468    11159  10530  10221   1151  -2235    333       C  
ATOM   3645  CG2 ILE A 468     -12.938  35.529  34.805  1.00 84.54           C  
ANISOU 3645  CG2 ILE A 468    10838  10526  10757   1436  -2203    -51       C  
ATOM   3646  CD1 ILE A 468     -10.436  34.170  33.927  1.00 82.88           C  
ANISOU 3646  CD1 ILE A 468    10929  10553  10008   1009  -1980    162       C  
ATOM   3647  N   PRO A 469     -14.121  38.896  34.575  1.00 96.68           N  
ANISOU 3647  N   PRO A 469    12475  11472  12785   1946  -2786    148       N  
ATOM   3648  CA  PRO A 469     -14.927  39.672  35.522  1.00100.66           C  
ANISOU 3648  CA  PRO A 469    12841  11778  13628   2176  -2800    -61       C  
ATOM   3649  C   PRO A 469     -15.431  38.817  36.676  1.00100.92           C  
ANISOU 3649  C   PRO A 469    12631  11978  13736   2161  -2503   -391       C  
ATOM   3650  O   PRO A 469     -15.510  37.588  36.596  1.00 90.89           O  
ANISOU 3650  O   PRO A 469    11247  10965  12322   2017  -2350   -458       O  
ATOM   3651  CB  PRO A 469     -16.091  40.186  34.665  1.00112.10           C  
ANISOU 3651  CB  PRO A 469    14150  13194  15250   2416  -3137    -18       C  
ATOM   3652  CG  PRO A 469     -15.620  40.052  33.245  1.00109.39           C  
ANISOU 3652  CG  PRO A 469    13980  12956  14626   2294  -3340    307       C  
ATOM   3653  CD  PRO A 469     -14.739  38.844  33.242  1.00104.47           C  
ANISOU 3653  CD  PRO A 469    13414  12584  13694   2013  -3070    293       C  
ATOM   3654  N   LYS A 470     -15.793  39.511  37.760  1.00108.32           N  
ANISOU 3654  N   LYS A 470    13487  12761  14910   2310  -2426   -600       N  
ATOM   3655  CA  LYS A 470     -16.207  38.851  38.996  1.00104.50           C  
ANISOU 3655  CA  LYS A 470    12791  12441  14473   2282  -2122   -900       C  
ATOM   3656  C   LYS A 470     -17.368  37.889  38.775  1.00107.21           C  
ANISOU 3656  C   LYS A 470    12815  13053  14868   2307  -2090  -1053       C  
ATOM   3657  O   LYS A 470     -17.416  36.812  39.381  1.00102.32           O  
ANISOU 3657  O   LYS A 470    12076  12646  14154   2145  -1826  -1170       O  
ATOM   3658  CB  LYS A 470     -16.593  39.901  40.037  1.00100.58           C  
ANISOU 3658  CB  LYS A 470    12224  11756  14233   2483  -2092  -1135       C  
ATOM   3659  CG  LYS A 470     -15.473  40.333  40.962  1.00 99.50           C  
ANISOU 3659  CG  LYS A 470    12312  11482  14012   2372  -1930  -1145       C  
ATOM   3660  CD  LYS A 470     -15.955  41.449  41.873  1.00114.94           C  
ANISOU 3660  CD  LYS A 470    14184  13242  16245   2600  -1941  -1420       C  
ATOM   3661  CE  LYS A 470     -17.309  41.109  42.479  1.00100.67           C  
ANISOU 3661  CE  LYS A 470    12001  11650  14600   2755  -1816  -1754       C  
ATOM   3662  NZ  LYS A 470     -17.660  41.997  43.619  1.00117.01           N  
ANISOU 3662  NZ  LYS A 470    13966  13614  16877   2938  -1728  -2098       N  
ATOM   3663  N   ASP A 471     -18.321  38.261  37.922  1.00113.93           N  
ANISOU 3663  N   ASP A 471    13518  13891  15881   2501  -2367  -1046       N  
ATOM   3664  CA  ASP A 471     -19.500  37.436  37.690  1.00120.84           C  
ANISOU 3664  CA  ASP A 471    14055  15018  16840   2533  -2365  -1215       C  
ATOM   3665  C   ASP A 471     -19.225  36.250  36.772  1.00120.88           C  
ANISOU 3665  C   ASP A 471    14093  15232  16603   2315  -2374  -1080       C  
ATOM   3666  O   ASP A 471     -20.176  35.599  36.326  1.00104.83           O  
ANISOU 3666  O   ASP A 471    11798  13393  14638   2331  -2439  -1194       O  
ATOM   3667  CB  ASP A 471     -20.639  38.287  37.119  1.00132.42           C  
ANISOU 3667  CB  ASP A 471    15326  16405  18583   2841  -2688  -1275       C  
ATOM   3668  CG  ASP A 471     -20.335  38.825  35.732  1.00135.21           C  
ANISOU 3668  CG  ASP A 471    15890  16638  18845   2897  -3058   -955       C  
ATOM   3669  OD1 ASP A 471     -19.145  38.889  35.358  1.00129.34           O  
ANISOU 3669  OD1 ASP A 471    15476  15808  17858   2726  -3056   -696       O  
ATOM   3670  OD2 ASP A 471     -21.292  39.187  35.015  1.00140.41           O1-
ANISOU 3670  OD2 ASP A 471    16374  17308  19668   3108  -3356   -957       O1-
ATOM   3671  N   GLN A 472     -17.952  35.960  36.479  1.00122.45           N  
ANISOU 3671  N   GLN A 472    14590  15400  16537   2114  -2313   -868       N  
ATOM   3672  CA  GLN A 472     -17.598  34.814  35.651  1.00122.05           C  
ANISOU 3672  CA  GLN A 472    14572  15542  16258   1911  -2300   -783       C  
ATOM   3673  C   GLN A 472     -16.346  34.110  36.170  1.00113.34           C  
ANISOU 3673  C   GLN A 472    13664  14450  14950   1671  -2033   -720       C  
ATOM   3674  O   GLN A 472     -15.708  33.364  35.416  1.00109.43           O  
ANISOU 3674  O   GLN A 472    13274  14060  14246   1512  -2039   -618       O  
ATOM   3675  CB  GLN A 472     -17.407  35.248  34.190  1.00110.62           C  
ANISOU 3675  CB  GLN A 472    13272  14093  14667   1954  -2626   -550       C  
ATOM   3676  CG  GLN A 472     -18.705  35.686  33.518  1.00122.21           C  
ANISOU 3676  CG  GLN A 472    14516  15604  16314   2180  -2928   -602       C  
ATOM   3677  CD  GLN A 472     -18.516  36.144  32.088  1.00136.73           C  
ANISOU 3677  CD  GLN A 472    16516  17463  17972   2216  -3266   -336       C  
ATOM   3678  OE1 GLN A 472     -17.391  36.318  31.621  1.00135.98           O  
ANISOU 3678  OE1 GLN A 472    16713  17327  17627   2079  -3270    -98       O  
ATOM   3679  NE2 GLN A 472     -19.623  36.351  31.384  1.00142.43           N  
ANISOU 3679  NE2 GLN A 472    17036  18271  18809   2394  -3556   -368       N  
ATOM   3680  N   TRP A 473     -15.984  34.332  37.437  1.00106.13           N  
ANISOU 3680  N   TRP A 473    12791  13445  14089   1651  -1809   -795       N  
ATOM   3681  CA  TRP A 473     -14.837  33.657  38.037  1.00108.67           C  
ANISOU 3681  CA  TRP A 473    13273  13783  14233   1440  -1570   -739       C  
ATOM   3682  C   TRP A 473     -14.975  32.142  37.946  1.00104.69           C  
ANISOU 3682  C   TRP A 473    12643  13466  13669   1265  -1428   -806       C  
ATOM   3683  O   TRP A 473     -14.091  31.451  37.428  1.00112.44           O  
ANISOU 3683  O   TRP A 473    13762  14487  14475   1115  -1405   -700       O  
ATOM   3684  CB  TRP A 473     -14.684  34.087  39.498  1.00105.33           C  
ANISOU 3684  CB  TRP A 473    12856  13282  13882   1460  -1363   -850       C  
ATOM   3685  CG  TRP A 473     -13.840  35.303  39.698  1.00 92.43           C  
ANISOU 3685  CG  TRP A 473    11459  11431  12228   1520  -1435   -747       C  
ATOM   3686  CD1 TRP A 473     -13.350  36.134  38.734  1.00 95.39           C  
ANISOU 3686  CD1 TRP A 473    12023  11655  12563   1566  -1670   -548       C  
ATOM   3687  CD2 TRP A 473     -13.386  35.828  40.949  1.00 90.43           C  
ANISOU 3687  CD2 TRP A 473    11277  11090  11991   1520  -1275   -838       C  
ATOM   3688  NE1 TRP A 473     -12.615  37.143  39.308  1.00 93.46           N  
ANISOU 3688  NE1 TRP A 473    11962  11204  12344   1586  -1666   -508       N  
ATOM   3689  CE2 TRP A 473     -12.624  36.979  40.668  1.00 94.01           C  
ANISOU 3689  CE2 TRP A 473    11959  11312  12447   1566  -1431   -703       C  
ATOM   3690  CE3 TRP A 473     -13.551  35.438  42.282  1.00 93.70           C  
ANISOU 3690  CE3 TRP A 473    11584  11615  12404   1471  -1018  -1016       C  
ATOM   3691  CZ2 TRP A 473     -12.027  37.741  41.668  1.00 97.18           C  
ANISOU 3691  CZ2 TRP A 473    12476  11574  12872   1571  -1346   -775       C  
ATOM   3692  CZ3 TRP A 473     -12.958  36.195  43.273  1.00 94.71           C  
ANISOU 3692  CZ3 TRP A 473    11830  11640  12515   1484   -933  -1084       C  
ATOM   3693  CH2 TRP A 473     -12.205  37.333  42.961  1.00 96.02           C  
ANISOU 3693  CH2 TRP A 473    12216  11561  12706   1537  -1101   -981       C  
ATOM   3694  N   MET A 474     -16.083  31.607  38.458  1.00 98.20           N  
ANISOU 3694  N   MET A 474    11546  12755  13011   1277  -1329   -993       N  
ATOM   3695  CA  MET A 474     -16.272  30.163  38.449  1.00101.90           C  
ANISOU 3695  CA  MET A 474    11888  13360  13471   1093  -1195  -1057       C  
ATOM   3696  C   MET A 474     -16.643  29.640  37.069  1.00106.75           C  
ANISOU 3696  C   MET A 474    12429  14070  14061   1079  -1402  -1064       C  
ATOM   3697  O   MET A 474     -16.296  28.502  36.732  1.00104.16           O  
ANISOU 3697  O   MET A 474    12110  13801  13665    912  -1341  -1071       O  
ATOM   3698  CB  MET A 474     -17.337  29.766  39.470  1.00 99.01           C  
ANISOU 3698  CB  MET A 474    11242  13094  13283   1074  -1005  -1240       C  
ATOM   3699  CG  MET A 474     -16.943  30.073  40.902  1.00105.10           C  
ANISOU 3699  CG  MET A 474    12078  13832  14022   1048   -766  -1251       C  
ATOM   3700  SD  MET A 474     -15.263  29.537  41.286  1.00 99.81           S  
ANISOU 3700  SD  MET A 474    11729  13078  13118    861   -631  -1053       S  
ATOM   3701  CE  MET A 474     -15.344  27.793  40.874  1.00 98.72           C  
ANISOU 3701  CE  MET A 474    11497  13016  12994    642   -560  -1038       C  
ATOM   3702  N   LYS A 475     -17.341  30.442  36.264  1.00116.78           N  
ANISOU 3702  N   LYS A 475    13625  15355  15392   1258  -1661  -1071       N  
ATOM   3703  CA  LYS A 475     -17.653  30.018  34.904  1.00107.75           C  
ANISOU 3703  CA  LYS A 475    12426  14337  14177   1247  -1887  -1072       C  
ATOM   3704  C   LYS A 475     -16.386  29.871  34.074  1.00102.10           C  
ANISOU 3704  C   LYS A 475    11990  13617  13185   1144  -1940   -900       C  
ATOM   3705  O   LYS A 475     -16.257  28.928  33.285  1.00100.48           O  
ANISOU 3705  O   LYS A 475    11761  13540  12876   1025  -1975   -952       O  
ATOM   3706  CB  LYS A 475     -18.610  31.010  34.246  1.00100.46           C  
ANISOU 3706  CB  LYS A 475    11381  13429  13359   1477  -2182  -1077       C  
ATOM   3707  CG  LYS A 475     -19.087  30.575  32.873  1.00107.98           C  
ANISOU 3707  CG  LYS A 475    12241  14559  14227   1473  -2438  -1098       C  
ATOM   3708  CD  LYS A 475     -19.764  31.716  32.139  1.00121.43           C  
ANISOU 3708  CD  LYS A 475    13905  16253  15982   1714  -2778  -1016       C  
ATOM   3709  CE  LYS A 475     -20.320  31.257  30.805  1.00125.12           C  
ANISOU 3709  CE  LYS A 475    14256  16942  16342   1708  -3048  -1050       C  
ATOM   3710  NZ  LYS A 475     -20.818  32.405  30.000  1.00141.99           N  
ANISOU 3710  NZ  LYS A 475    16405  19064  18480   1940  -3418   -899       N  
ATOM   3711  N   LYS A 476     -15.434  30.790  34.240  1.00101.14           N  
ANISOU 3711  N   LYS A 476    12120  13359  12949   1180  -1941   -716       N  
ATOM   3712  CA  LYS A 476     -14.181  30.695  33.505  1.00 99.90           C  
ANISOU 3712  CA  LYS A 476    12208  13223  12526   1067  -1964   -554       C  
ATOM   3713  C   LYS A 476     -13.225  29.687  34.127  1.00101.37           C  
ANISOU 3713  C   LYS A 476    12465  13402  12649    886  -1702   -589       C  
ATOM   3714  O   LYS A 476     -12.346  29.175  33.427  1.00 95.17           O  
ANISOU 3714  O   LYS A 476    11794  12694  11670    776  -1699   -543       O  
ATOM   3715  CB  LYS A 476     -13.509  32.067  33.422  1.00 99.31           C  
ANISOU 3715  CB  LYS A 476    12365  12998  12369   1147  -2068   -331       C  
ATOM   3716  CG  LYS A 476     -13.527  32.688  32.030  1.00120.08           C  
ANISOU 3716  CG  LYS A 476    15092  15702  14830   1199  -2358   -156       C  
ATOM   3717  CD  LYS A 476     -12.658  31.937  31.035  1.00129.88           C  
ANISOU 3717  CD  LYS A 476    16438  17138  15772   1028  -2347   -104       C  
ATOM   3718  CE  LYS A 476     -12.670  32.637  29.679  1.00115.83           C  
ANISOU 3718  CE  LYS A 476    14767  15469  13774   1064  -2631    100       C  
ATOM   3719  NZ  LYS A 476     -11.712  32.033  28.711  1.00126.73           N  
ANISOU 3719  NZ  LYS A 476    16260  17075  14817    890  -2598    147       N  
ATOM   3720  N   TRP A 477     -13.379  29.392  35.420  1.00101.98           N  
ANISOU 3720  N   TRP A 477    12467  13401  12880    858  -1489   -670       N  
ATOM   3721  CA  TRP A 477     -12.550  28.371  36.053  1.00 88.43           C  
ANISOU 3721  CA  TRP A 477    10806  11668  11126    696  -1267   -683       C  
ATOM   3722  C   TRP A 477     -12.826  26.997  35.458  1.00 89.97           C  
ANISOU 3722  C   TRP A 477    10870  11964  11349    583  -1260   -813       C  
ATOM   3723  O   TRP A 477     -11.899  26.282  35.061  1.00 93.44           O  
ANISOU 3723  O   TRP A 477    11410  12420  11675    480  -1218   -801       O  
ATOM   3724  CB  TRP A 477     -12.790  28.356  37.566  1.00 87.22           C  
ANISOU 3724  CB  TRP A 477    10590  11441  11108    684  -1058   -724       C  
ATOM   3725  CG  TRP A 477     -12.091  27.226  38.273  1.00 92.26           C  
ANISOU 3725  CG  TRP A 477    11265  12059  11730    521   -853   -714       C  
ATOM   3726  CD1 TRP A 477     -12.625  26.015  38.612  1.00 93.96           C  
ANISOU 3726  CD1 TRP A 477    11323  12304  12074    407   -739   -804       C  
ATOM   3727  CD2 TRP A 477     -10.732  27.205  38.730  1.00 86.53           C  
ANISOU 3727  CD2 TRP A 477    10740  11265  10871    455   -756   -592       C  
ATOM   3728  NE1 TRP A 477     -11.683  25.242  39.247  1.00100.96           N  
ANISOU 3728  NE1 TRP A 477    12317  13125  12919    286   -590   -727       N  
ATOM   3729  CE2 TRP A 477     -10.513  25.950  39.333  1.00 83.88           C  
ANISOU 3729  CE2 TRP A 477    10364  10916  10593    322   -601   -607       C  
ATOM   3730  CE3 TRP A 477      -9.682  28.126  38.691  1.00 79.85           C  
ANISOU 3730  CE3 TRP A 477    10096  10364   9879    487   -794   -468       C  
ATOM   3731  CZ2 TRP A 477      -9.287  25.592  39.887  1.00 77.00           C  
ANISOU 3731  CZ2 TRP A 477     9639   9986   9633    248   -500   -504       C  
ATOM   3732  CZ3 TRP A 477      -8.464  27.768  39.237  1.00 77.67           C  
ANISOU 3732  CZ3 TRP A 477     9950  10050   9511    397   -679   -387       C  
ATOM   3733  CH2 TRP A 477      -8.277  26.514  39.830  1.00 91.08           C  
ANISOU 3733  CH2 TRP A 477    11597  11745  11266    291   -541   -407       C  
ATOM   3734  N   TRP A 478     -14.101  26.611  35.385  1.00 86.26           N  
ANISOU 3734  N   TRP A 478    10161  11561  11052    601  -1304   -962       N  
ATOM   3735  CA  TRP A 478     -14.450  25.280  34.908  1.00 86.60           C  
ANISOU 3735  CA  TRP A 478    10062  11672  11170    476  -1297  -1114       C  
ATOM   3736  C   TRP A 478     -14.433  25.165  33.391  1.00 89.92           C  
ANISOU 3736  C   TRP A 478    10490  12233  11443    492  -1520  -1172       C  
ATOM   3737  O   TRP A 478     -14.362  24.045  32.874  1.00 95.30           O  
ANISOU 3737  O   TRP A 478    11110  12960  12139    379  -1516  -1312       O  
ATOM   3738  CB  TRP A 478     -15.816  24.864  35.455  1.00 87.48           C  
ANISOU 3738  CB  TRP A 478     9890  11814  11533    454  -1244  -1260       C  
ATOM   3739  CG  TRP A 478     -15.746  24.470  36.893  1.00 86.10           C  
ANISOU 3739  CG  TRP A 478     9696  11547  11471    356   -982  -1224       C  
ATOM   3740  CD1 TRP A 478     -16.264  25.144  37.958  1.00 88.69           C  
ANISOU 3740  CD1 TRP A 478     9948  11874  11877    419   -867  -1210       C  
ATOM   3741  CD2 TRP A 478     -15.087  23.316  37.428  1.00 93.26           C  
ANISOU 3741  CD2 TRP A 478    10665  12359  12410    181   -809  -1190       C  
ATOM   3742  NE1 TRP A 478     -15.982  24.474  39.124  1.00 93.30           N  
ANISOU 3742  NE1 TRP A 478    10547  12403  12499    275   -625  -1158       N  
ATOM   3743  CE2 TRP A 478     -15.259  23.348  38.825  1.00 98.44           C  
ANISOU 3743  CE2 TRP A 478    11289  12979  13135    130   -597  -1124       C  
ATOM   3744  CE3 TRP A 478     -14.375  22.256  36.860  1.00104.34           C  
ANISOU 3744  CE3 TRP A 478    12143  13704  13796     71   -820  -1219       C  
ATOM   3745  CZ2 TRP A 478     -14.744  22.361  39.662  1.00109.19           C  
ANISOU 3745  CZ2 TRP A 478    12706  14243  14537    -34   -414  -1039       C  
ATOM   3746  CZ3 TRP A 478     -13.864  21.277  37.692  1.00101.03           C  
ANISOU 3746  CZ3 TRP A 478    11769  13152  13464    -72   -644  -1156       C  
ATOM   3747  CH2 TRP A 478     -14.051  21.336  39.077  1.00105.45           C  
ANISOU 3747  CH2 TRP A 478    12311  13673  14081   -127   -452  -1044       C  
ATOM   3748  N   GLU A 479     -14.497  26.283  32.663  1.00 97.09           N  
ANISOU 3748  N   GLU A 479    11475  13209  12206    625  -1720  -1069       N  
ATOM   3749  CA  GLU A 479     -14.225  26.230  31.230  1.00 97.73           C  
ANISOU 3749  CA  GLU A 479    11617  13459  12058    619  -1916  -1075       C  
ATOM   3750  C   GLU A 479     -12.785  25.811  30.971  1.00103.58           C  
ANISOU 3750  C   GLU A 479    12557  14205  12593    510  -1805  -1022       C  
ATOM   3751  O   GLU A 479     -12.510  25.022  30.059  1.00 96.96           O  
ANISOU 3751  O   GLU A 479    11702  13507  11631    433  -1851  -1153       O  
ATOM   3752  CB  GLU A 479     -14.500  27.585  30.580  1.00105.49           C  
ANISOU 3752  CB  GLU A 479    12673  14493  12915    773  -2156   -907       C  
ATOM   3753  CG  GLU A 479     -15.953  27.854  30.245  1.00124.39           C  
ANISOU 3753  CG  GLU A 479    14835  16969  15458    899  -2366  -1002       C  
ATOM   3754  CD  GLU A 479     -16.138  29.186  29.547  1.00134.19           C  
ANISOU 3754  CD  GLU A 479    16173  18233  16580   1063  -2638   -800       C  
ATOM   3755  OE1 GLU A 479     -15.130  29.754  29.073  1.00114.08           O  
ANISOU 3755  OE1 GLU A 479    13877  15683  13787   1036  -2673   -589       O  
ATOM   3756  OE2 GLU A 479     -17.289  29.666  29.475  1.00139.00           O1-
ANISOU 3756  OE2 GLU A 479    16600  18858  17354   1216  -2819   -842       O1-
ATOM   3757  N   MET A 480     -11.853  26.329  31.770  1.00 91.22           N  
ANISOU 3757  N   MET A 480    11164  12501  10995    506  -1661   -858       N  
ATOM   3758  CA  MET A 480     -10.440  26.029  31.583  1.00 80.90           C  
ANISOU 3758  CA  MET A 480    10024  11207   9507    415  -1556   -804       C  
ATOM   3759  C   MET A 480     -10.067  24.666  32.150  1.00 78.88           C  
ANISOU 3759  C   MET A 480     9706  10872   9394    308  -1372   -952       C  
ATOM   3760  O   MET A 480      -9.143  24.022  31.641  1.00 94.39           O  
ANISOU 3760  O   MET A 480    11725  12896  11242    241  -1329  -1017       O  
ATOM   3761  CB  MET A 480      -9.604  27.141  32.215  1.00 79.50           C  
ANISOU 3761  CB  MET A 480    10038  10913   9256    445  -1495   -577       C  
ATOM   3762  CG  MET A 480      -9.902  28.504  31.605  1.00 82.65           C  
ANISOU 3762  CG  MET A 480    10522  11339   9541    544  -1696   -404       C  
ATOM   3763  SD  MET A 480      -9.302  29.916  32.551  1.00 97.54           S  
ANISOU 3763  SD  MET A 480    12591  13010  11460    595  -1650   -180       S  
ATOM   3764  CE  MET A 480      -7.529  29.694  32.427  1.00 87.69           C  
ANISOU 3764  CE  MET A 480    11521  11807   9992    442  -1505    -86       C  
ATOM   3765  N   LYS A 481     -10.771  24.206  33.187  1.00 85.22           N  
ANISOU 3765  N   LYS A 481    10386  11543  10450    292  -1266  -1006       N  
ATOM   3766  CA  LYS A 481     -10.558  22.848  33.680  1.00 88.90           C  
ANISOU 3766  CA  LYS A 481    10787  11908  11083    181  -1123  -1120       C  
ATOM   3767  C   LYS A 481     -10.958  21.819  32.628  1.00 91.56           C  
ANISOU 3767  C   LYS A 481    10994  12337  11459    124  -1222  -1355       C  
ATOM   3768  O   LYS A 481     -10.292  20.790  32.467  1.00 93.79           O  
ANISOU 3768  O   LYS A 481    11286  12565  11783     50  -1159  -1468       O  
ATOM   3769  CB  LYS A 481     -11.349  22.630  34.971  1.00 85.27           C  
ANISOU 3769  CB  LYS A 481    10216  11321  10862    149   -993  -1099       C  
ATOM   3770  CG  LYS A 481     -10.617  23.046  36.239  1.00 85.47           C  
ANISOU 3770  CG  LYS A 481    10376  11230  10870    150   -831   -921       C  
ATOM   3771  CD  LYS A 481      -9.778  21.918  36.813  1.00 97.66           C  
ANISOU 3771  CD  LYS A 481    11969  12649  12490     44   -695   -903       C  
ATOM   3772  CE  LYS A 481      -9.002  22.391  38.033  1.00 95.70           C  
ANISOU 3772  CE  LYS A 481    11856  12323  12182     49   -564   -722       C  
ATOM   3773  NZ  LYS A 481      -8.640  21.264  38.932  1.00 85.11           N  
ANISOU 3773  NZ  LYS A 481    10514  10848  10976    -55   -433   -672       N  
ATOM   3774  N   ARG A 482     -12.047  22.087  31.904  1.00 91.85           N  
ANISOU 3774  N   ARG A 482    10897  12510  11493    166  -1391  -1450       N  
ATOM   3775  CA  ARG A 482     -12.506  21.189  30.848  1.00 98.06           C  
ANISOU 3775  CA  ARG A 482    11546  13416  12296    110  -1513  -1702       C  
ATOM   3776  C   ARG A 482     -11.527  21.167  29.681  1.00 98.25           C  
ANISOU 3776  C   ARG A 482    11693  13613  12026    114  -1587  -1759       C  
ATOM   3777  O   ARG A 482     -11.159  20.099  29.178  1.00 95.07           O  
ANISOU 3777  O   ARG A 482    11248  13225  11648     41  -1570  -1979       O  
ATOM   3778  CB  ARG A 482     -13.881  21.635  30.357  1.00100.56           C  
ANISOU 3778  CB  ARG A 482    11685  13871  12651    170  -1703  -1771       C  
ATOM   3779  CG  ARG A 482     -15.040  21.370  31.295  1.00 98.18           C  
ANISOU 3779  CG  ARG A 482    11178  13461  12667    137  -1633  -1815       C  
ATOM   3780  CD  ARG A 482     -16.248  22.150  30.802  1.00 93.33           C  
ANISOU 3780  CD  ARG A 482    10401  13007  12055    249  -1841  -1845       C  
ATOM   3781  NE  ARG A 482     -17.398  22.061  31.693  1.00 94.14           N  
ANISOU 3781  NE  ARG A 482    10273  13050  12447    232  -1767  -1894       N  
ATOM   3782  CZ  ARG A 482     -18.480  21.334  31.447  1.00116.40           C  
ANISOU 3782  CZ  ARG A 482    12824  15935  15469    152  -1833  -2107       C  
ATOM   3783  NH1 ARG A 482     -18.588  20.605  30.349  1.00123.23           N  
ANISOU 3783  NH1 ARG A 482    13621  16912  16289     86  -1989  -2311       N  
ATOM   3784  NH2 ARG A 482     -19.482  21.349  32.320  1.00125.02           N  
ANISOU 3784  NH2 ARG A 482    13695  16998  16810    130  -1738  -2134       N  
ATOM   3785  N   GLU A 483     -11.108  22.350  29.229  1.00 94.57           N  
ANISOU 3785  N   GLU A 483    11371  13280  11281    191  -1669  -1568       N  
ATOM   3786  CA  GLU A 483     -10.309  22.476  28.016  1.00 91.30           C  
ANISOU 3786  CA  GLU A 483    11056  13101  10531    178  -1748  -1598       C  
ATOM   3787  C   GLU A 483      -8.846  22.131  28.262  1.00 93.22           C  
ANISOU 3787  C   GLU A 483    11428  13290  10702    128  -1566  -1578       C  
ATOM   3788  O   GLU A 483      -8.240  21.381  27.489  1.00 95.41           O  
ANISOU 3788  O   GLU A 483    11687  13702  10862     80  -1551  -1781       O  
ATOM   3789  CB  GLU A 483     -10.429  23.900  27.470  1.00102.67           C  
ANISOU 3789  CB  GLU A 483    12609  14688  11715    258  -1910  -1353       C  
ATOM   3790  CG  GLU A 483      -9.572  24.177  26.252  1.00116.24           C  
ANISOU 3790  CG  GLU A 483    14448  16682  13036    219  -1976  -1318       C  
ATOM   3791  CD  GLU A 483      -9.517  25.652  25.914  1.00130.52           C  
ANISOU 3791  CD  GLU A 483    16410  18560  14621    274  -2112   -991       C  
ATOM   3792  OE1 GLU A 483     -10.145  26.451  26.641  1.00133.40           O  
ANISOU 3792  OE1 GLU A 483    16782  18736  15170    367  -2162   -825       O  
ATOM   3793  OE2 GLU A 483      -8.857  26.009  24.917  1.00136.12           O1-
ANISOU 3793  OE2 GLU A 483    17228  19515  14975    222  -2169   -903       O1-
ATOM   3794  N   ILE A 484      -8.263  22.675  29.329  1.00 96.01           N  
ANISOU 3794  N   ILE A 484    11895  13462  11124    145  -1432  -1359       N  
ATOM   3795  CA  ILE A 484      -6.831  22.526  29.562  1.00 82.46           C  
ANISOU 3795  CA  ILE A 484    10293  11717   9323    108  -1282  -1312       C  
ATOM   3796  C   ILE A 484      -6.535  21.208  30.265  1.00 75.87           C  
ANISOU 3796  C   ILE A 484     9381  10685   8760     70  -1146  -1473       C  
ATOM   3797  O   ILE A 484      -5.692  20.420  29.821  1.00 73.91           O  
ANISOU 3797  O   ILE A 484     9119  10484   8481     44  -1093  -1642       O  
ATOM   3798  CB  ILE A 484      -6.303  23.720  30.376  1.00 74.66           C  
ANISOU 3798  CB  ILE A 484     9457  10628   8282    136  -1222  -1015       C  
ATOM   3799  CG1 ILE A 484      -6.625  25.033  29.658  1.00 84.33           C  
ANISOU 3799  CG1 ILE A 484    10767  11995   9279    174  -1382   -833       C  
ATOM   3800  CG2 ILE A 484      -4.807  23.580  30.618  1.00 74.26           C  
ANISOU 3800  CG2 ILE A 484     9498  10569   8148     92  -1078   -972       C  
ATOM   3801  CD1 ILE A 484      -6.186  26.264  30.425  1.00 81.66           C  
ANISOU 3801  CD1 ILE A 484    10578  11521   8928    199  -1347   -563       C  
ATOM   3802  N   VAL A 485      -7.226  20.950  31.376  1.00 74.34           N  
ANISOU 3802  N   VAL A 485     9132  10270   8844     65  -1089  -1422       N  
ATOM   3803  CA  VAL A 485      -6.912  19.800  32.214  1.00 77.24           C  
ANISOU 3803  CA  VAL A 485     9458  10411   9477     18   -964  -1488       C  
ATOM   3804  C   VAL A 485      -7.719  18.560  31.841  1.00 79.49           C  
ANISOU 3804  C   VAL A 485     9579  10631   9992    -40  -1012  -1748       C  
ATOM   3805  O   VAL A 485      -7.358  17.450  32.256  1.00 89.13           O  
ANISOU 3805  O   VAL A 485    10768  11656  11442    -84   -939  -1837       O  
ATOM   3806  CB  VAL A 485      -7.136  20.162  33.695  1.00 81.49           C  
ANISOU 3806  CB  VAL A 485    10036  10764  10161     15   -857  -1267       C  
ATOM   3807  CG1 VAL A 485      -6.395  19.197  34.616  1.00 89.74           C  
ANISOU 3807  CG1 VAL A 485    11105  11598  11395    -27   -731  -1237       C  
ATOM   3808  CG2 VAL A 485      -6.708  21.599  33.958  1.00 71.88           C  
ANISOU 3808  CG2 VAL A 485     8959   9622   8732     74   -855  -1046       C  
ATOM   3809  N   GLY A 486      -8.784  18.708  31.059  1.00 81.64           N  
ANISOU 3809  N   GLY A 486     9742  11050  10226    -42  -1151  -1873       N  
ATOM   3810  CA  GLY A 486      -9.641  17.573  30.764  1.00 89.00           C  
ANISOU 3810  CA  GLY A 486    10500  11912  11404   -118  -1206  -2129       C  
ATOM   3811  C   GLY A 486     -10.410  17.094  31.976  1.00 95.86           C  
ANISOU 3811  C   GLY A 486    11283  12534  12604   -194  -1112  -2043       C  
ATOM   3812  O   GLY A 486     -10.551  15.881  32.181  1.00 95.44           O  
ANISOU 3812  O   GLY A 486    11146  12286  12831   -289  -1076  -2182       O  
ATOM   3813  N   VAL A 487     -10.912  18.023  32.784  1.00101.06           N  
ANISOU 3813  N   VAL A 487    11958  13199  13241   -163  -1067  -1820       N  
ATOM   3814  CA  VAL A 487     -11.565  17.720  34.051  1.00103.92           C  
ANISOU 3814  CA  VAL A 487    12247  13383  13854   -243   -941  -1704       C  
ATOM   3815  C   VAL A 487     -12.890  18.468  34.085  1.00104.37           C  
ANISOU 3815  C   VAL A 487    12158  13572  13927   -215  -1005  -1700       C  
ATOM   3816  O   VAL A 487     -12.935  19.666  33.787  1.00107.35           O  
ANISOU 3816  O   VAL A 487    12592  14101  14096    -92  -1086  -1615       O  
ATOM   3817  CB  VAL A 487     -10.680  18.124  35.247  1.00 84.48           C  
ANISOU 3817  CB  VAL A 487     9951  10809  11340   -220   -785  -1442       C  
ATOM   3818  CG1 VAL A 487     -11.460  18.058  36.544  1.00 84.46           C  
ANISOU 3818  CG1 VAL A 487     9872  10708  11512   -299   -653  -1305       C  
ATOM   3819  CG2 VAL A 487      -9.432  17.255  35.307  1.00 80.45           C  
ANISOU 3819  CG2 VAL A 487     9546  10148  10874   -241   -732  -1452       C  
ATOM   3820  N   VAL A 488     -13.964  17.767  34.440  1.00 91.33           N  
ANISOU 3820  N   VAL A 488    10308  11853  12540   -331   -975  -1790       N  
ATOM   3821  CA  VAL A 488     -15.300  18.348  34.462  1.00 90.19           C  
ANISOU 3821  CA  VAL A 488     9967  11846  12456   -308  -1035  -1830       C  
ATOM   3822  C   VAL A 488     -15.886  18.198  35.860  1.00 97.55           C  
ANISOU 3822  C   VAL A 488    10805  12679  13580   -407   -838  -1702       C  
ATOM   3823  O   VAL A 488     -15.742  17.152  36.502  1.00 98.57           O  
ANISOU 3823  O   VAL A 488    10927  12627  13898   -568   -707  -1666       O  
ATOM   3824  CB  VAL A 488     -16.220  17.712  33.397  1.00100.83           C  
ANISOU 3824  CB  VAL A 488    11100  13290  13922   -367  -1208  -2108       C  
ATOM   3825  CG1 VAL A 488     -16.391  16.218  33.637  1.00106.78           C  
ANISOU 3825  CG1 VAL A 488    11750  13839  14981   -571  -1130  -2235       C  
ATOM   3826  CG2 VAL A 488     -17.570  18.420  33.362  1.00 94.45           C  
ANISOU 3826  CG2 VAL A 488    10068  12652  13168   -311  -1298  -2151       C  
ATOM   3827  N   GLU A 489     -16.531  19.259  36.331  1.00 97.51           N  
ANISOU 3827  N   GLU A 489    10730  12796  13522   -309   -818  -1631       N  
ATOM   3828  CA  GLU A 489     -17.144  19.240  37.648  1.00 97.70           C  
ANISOU 3828  CA  GLU A 489    10644  12797  13681   -397   -615  -1535       C  
ATOM   3829  C   GLU A 489     -18.349  18.300  37.660  1.00 93.44           C  
ANISOU 3829  C   GLU A 489     9814  12265  13423   -577   -589  -1683       C  
ATOM   3830  O   GLU A 489     -19.102  18.242  36.683  1.00 97.24           O  
ANISOU 3830  O   GLU A 489    10118  12854  13976   -554   -767  -1884       O  
ATOM   3831  CB  GLU A 489     -17.562  20.655  38.057  1.00105.14           C  
ANISOU 3831  CB  GLU A 489    11558  13880  14511   -222   -613  -1485       C  
ATOM   3832  CG  GLU A 489     -18.727  21.238  37.261  1.00104.41           C  
ANISOU 3832  CG  GLU A 489    11234  13957  14480   -106   -800  -1657       C  
ATOM   3833  CD  GLU A 489     -18.302  21.807  35.916  1.00105.32           C  
ANISOU 3833  CD  GLU A 489    11471  14133  14412     49  -1062  -1691       C  
ATOM   3834  OE1 GLU A 489     -17.249  21.390  35.389  1.00107.49           O  
ANISOU 3834  OE1 GLU A 489    11948  14339  14555     14  -1094  -1655       O  
ATOM   3835  OE2 GLU A 489     -19.029  22.669  35.379  1.00 98.91           O1-
ANISOU 3835  OE2 GLU A 489    10545  13452  13586    206  -1239  -1752       O1-
ATOM   3836  N   PRO A 490     -18.545  17.535  38.741  1.00 89.55           N  
ANISOU 3836  N   PRO A 490     9266  11668  13091   -774   -378  -1578       N  
ATOM   3837  CA  PRO A 490     -19.706  16.635  38.803  1.00 93.13           C  
ANISOU 3837  CA  PRO A 490     9432  12122  13832   -985   -337  -1699       C  
ATOM   3838  C   PRO A 490     -21.018  17.341  39.083  1.00 94.40           C  
ANISOU 3838  C   PRO A 490     9299  12517  14053   -950   -302  -1793       C  
ATOM   3839  O   PRO A 490     -22.075  16.746  38.845  1.00 94.23           O  
ANISOU 3839  O   PRO A 490     8992  12547  14265  -1097   -322  -1950       O  
ATOM   3840  CB  PRO A 490     -19.354  15.686  39.952  1.00 95.09           C  
ANISOU 3840  CB  PRO A 490     9757  12178  14195  -1212   -112  -1488       C  
ATOM   3841  CG  PRO A 490     -18.445  16.493  40.821  1.00100.11           C  
ANISOU 3841  CG  PRO A 490    10632  12835  14571  -1086      3  -1265       C  
ATOM   3842  CD  PRO A 490     -17.662  17.392  39.908  1.00100.67           C  
ANISOU 3842  CD  PRO A 490    10879  12953  14419   -833   -183  -1329       C  
ATOM   3843  N   VAL A 491     -20.985  18.574  39.571  1.00101.84           N  
ANISOU 3843  N   VAL A 491    10286  13594  14814   -759   -258  -1724       N  
ATOM   3844  CA  VAL A 491     -22.177  19.301  39.976  1.00106.32           C  
ANISOU 3844  CA  VAL A 491    10566  14379  15451   -696   -204  -1826       C  
ATOM   3845  C   VAL A 491     -22.047  20.742  39.496  1.00104.56           C  
ANISOU 3845  C   VAL A 491    10419  14254  15054   -378   -379  -1866       C  
ATOM   3846  O   VAL A 491     -20.966  21.337  39.604  1.00104.98           O  
ANISOU 3846  O   VAL A 491    10771  14222  14897   -255   -389  -1724       O  
ATOM   3847  CB  VAL A 491     -22.377  19.214  41.496  1.00112.01           C  
ANISOU 3847  CB  VAL A 491    11234  15151  16175   -840    112  -1687       C  
ATOM   3848  CG1 VAL A 491     -23.158  20.420  42.036  1.00122.59           C  
ANISOU 3848  CG1 VAL A 491    12383  16723  17475   -663    179  -1785       C  
ATOM   3849  CG2 VAL A 491     -23.065  17.908  41.890  1.00107.67           C  
ANISOU 3849  CG2 VAL A 491    10475  14567  15868  -1172    265  -1680       C  
ATOM   3850  N   PRO A 492     -23.103  21.342  38.947  1.00101.94           N  
ANISOU 3850  N   PRO A 492     9823  14088  14820   -239   -534  -2048       N  
ATOM   3851  CA  PRO A 492     -22.972  22.706  38.412  1.00 95.34           C  
ANISOU 3851  CA  PRO A 492     9077  13302  13848     68   -740  -2057       C  
ATOM   3852  C   PRO A 492     -22.676  23.681  39.535  1.00 98.00           C  
ANISOU 3852  C   PRO A 492     9514  13636  14085    189   -567  -1961       C  
ATOM   3853  O   PRO A 492     -23.143  23.516  40.669  1.00101.82           O  
ANISOU 3853  O   PRO A 492     9845  14200  14641     82   -312  -1977       O  
ATOM   3854  CB  PRO A 492     -24.339  22.966  37.765  1.00 96.51           C  
ANISOU 3854  CB  PRO A 492     8858  13630  14181    166   -926  -2276       C  
ATOM   3855  CG  PRO A 492     -25.270  22.003  38.418  1.00107.23           C  
ANISOU 3855  CG  PRO A 492     9897  15074  15772    -84   -719  -2384       C  
ATOM   3856  CD  PRO A 492     -24.441  20.775  38.673  1.00107.89           C  
ANISOU 3856  CD  PRO A 492    10183  14978  15831   -357   -567  -2252       C  
ATOM   3857  N   HIS A 493     -21.865  24.686  39.234  1.00 87.44           N  
ANISOU 3857  N   HIS A 493     8439  12216  12569    394   -699  -1862       N  
ATOM   3858  CA  HIS A 493     -21.416  25.605  40.264  1.00 89.02           C  
ANISOU 3858  CA  HIS A 493     8775  12382  12667    500   -553  -1785       C  
ATOM   3859  C   HIS A 493     -21.706  27.043  39.885  1.00 88.84           C  
ANISOU 3859  C   HIS A 493     8740  12358  12655    802   -758  -1842       C  
ATOM   3860  O   HIS A 493     -21.408  27.484  38.772  1.00 86.45           O  
ANISOU 3860  O   HIS A 493     8565  11995  12286    929  -1029  -1788       O  
ATOM   3861  CB  HIS A 493     -19.928  25.425  40.580  1.00 97.45           C  
ANISOU 3861  CB  HIS A 493    10212  13295  13521    419   -465  -1577       C  
ATOM   3862  CG  HIS A 493     -19.678  24.334  41.567  1.00 88.92           C  
ANISOU 3862  CG  HIS A 493     9142  12204  12441    166   -196  -1495       C  
ATOM   3863  ND1 HIS A 493     -18.450  24.105  42.157  1.00 83.06           N  
ANISOU 3863  ND1 HIS A 493     8680  11348  11530     84    -81  -1312       N  
ATOM   3864  CD2 HIS A 493     -20.520  23.397  42.071  1.00 92.51           C  
ANISOU 3864  CD2 HIS A 493     9352  12747  13052    -35    -30  -1552       C  
ATOM   3865  CE1 HIS A 493     -18.551  23.083  42.993  1.00 92.54           C  
ANISOU 3865  CE1 HIS A 493     9823  12560  12778   -142    131  -1242       C  
ATOM   3866  NE2 HIS A 493     -19.793  22.630  42.954  1.00 85.62           N  
ANISOU 3866  NE2 HIS A 493     8635  11799  12098   -232    175  -1377       N  
ATOM   3867  N   ASP A 494     -22.353  27.740  40.810  1.00114.65           N  
ANISOU 3867  N   ASP A 494    11836  15706  16020    911   -631  -1961       N  
ATOM   3868  CA  ASP A 494     -22.731  29.141  40.691  1.00108.37           C  
ANISOU 3868  CA  ASP A 494    10996  14881  15300   1216   -799  -2048       C  
ATOM   3869  C   ASP A 494     -21.491  30.017  40.844  1.00109.87           C  
ANISOU 3869  C   ASP A 494    11563  14874  15309   1311   -839  -1884       C  
ATOM   3870  O   ASP A 494     -20.352  29.537  40.808  1.00119.09           O  
ANISOU 3870  O   ASP A 494    13011  15952  16285   1158   -781  -1704       O  
ATOM   3871  CB  ASP A 494     -23.810  29.450  41.719  1.00102.04           C  
ANISOU 3871  CB  ASP A 494     9856  14245  14669   1279   -607  -2276       C  
ATOM   3872  CG  ASP A 494     -24.680  30.623  41.329  1.00151.77           C  
ANISOU 3872  CG  ASP A 494    15952  20546  21168   1607   -838  -2446       C  
ATOM   3873  OD1 ASP A 494     -24.402  31.234  40.291  1.00167.58           O  
ANISOU 3873  OD1 ASP A 494    18110  22402  23159   1777  -1155  -2344       O  
ATOM   3874  OD2 ASP A 494     -25.624  30.950  42.090  1.00172.62           O1-
ANISOU 3874  OD2 ASP A 494    18275  23338  23974   1697   -698  -2678       O1-
ATOM   3875  N   GLU A 495     -21.705  31.322  40.998  1.00100.20           N  
ANISOU 3875  N   GLU A 495    10333  13569  14168   1569   -949  -1957       N  
ATOM   3876  CA  GLU A 495     -20.642  32.255  41.314  1.00114.22           C  
ANISOU 3876  CA  GLU A 495    12428  15150  15819   1653   -968  -1840       C  
ATOM   3877  C   GLU A 495     -20.606  32.583  42.799  1.00115.60           C  
ANISOU 3877  C   GLU A 495    12568  15372  15984   1648   -687  -1975       C  
ATOM   3878  O   GLU A 495     -19.871  33.489  43.205  1.00100.54           O  
ANISOU 3878  O   GLU A 495    10879  13309  14014   1739   -700  -1943       O  
ATOM   3879  CB  GLU A 495     -20.759  33.536  40.467  1.00111.87           C  
ANISOU 3879  CB  GLU A 495    12201  14677  15626   1931  -1303  -1806       C  
ATOM   3880  CG  GLU A 495     -20.634  33.254  38.985  1.00112.74           C  
ANISOU 3880  CG  GLU A 495    12396  14773  15667   1917  -1583  -1637       C  
ATOM   3881  CD  GLU A 495     -19.200  33.043  38.553  1.00115.80           C  
ANISOU 3881  CD  GLU A 495    13154  15056  15790   1760  -1592  -1385       C  
ATOM   3882  OE1 GLU A 495     -18.272  33.571  39.200  1.00102.01           O  
ANISOU 3882  OE1 GLU A 495    11636  13171  13954   1741  -1489  -1307       O  
ATOM   3883  OE2 GLU A 495     -19.011  32.350  37.541  1.00132.86           O1-
ANISOU 3883  OE2 GLU A 495    15358  17289  17834   1655  -1707  -1288       O1-
ATOM   3884  N   THR A 496     -21.394  31.869  43.612  1.00125.76           N  
ANISOU 3884  N   THR A 496    13577  16885  17322   1528   -434  -2128       N  
ATOM   3885  CA  THR A 496     -21.220  31.869  45.056  1.00120.11           C  
ANISOU 3885  CA  THR A 496    12854  16282  16501   1438   -121  -2214       C  
ATOM   3886  C   THR A 496     -20.026  31.039  45.483  1.00120.04           C  
ANISOU 3886  C   THR A 496    13126  16247  16236   1179     35  -1984       C  
ATOM   3887  O   THR A 496     -19.484  31.248  46.580  1.00129.40           O  
ANISOU 3887  O   THR A 496    14425  17473  17267   1125    226  -1992       O  
ATOM   3888  CB  THR A 496     -22.473  31.351  45.760  1.00117.63           C  
ANISOU 3888  CB  THR A 496    12139  16254  16303   1366    110  -2428       C  
ATOM   3889  OG1 THR A 496     -22.763  30.025  45.297  1.00129.81           O  
ANISOU 3889  OG1 THR A 496    13576  17886  17861   1127    148  -2322       O  
ATOM   3890  CG2 THR A 496     -23.625  32.229  45.436  1.00112.97           C  
ANISOU 3890  CG2 THR A 496    11243  15699  15982   1650    -41  -2686       C  
ATOM   3891  N   TYR A 497     -19.576  30.141  44.613  1.00105.68           N  
ANISOU 3891  N   TYR A 497    11423  14361  14371   1035    -64  -1794       N  
ATOM   3892  CA  TYR A 497     -18.434  29.279  44.858  1.00107.70           C  
ANISOU 3892  CA  TYR A 497    11928  14564  14427    814     42  -1577       C  
ATOM   3893  C   TYR A 497     -17.133  30.039  44.620  1.00105.21           C  
ANISOU 3893  C   TYR A 497    11954  14055  13967    894    -89  -1441       C  
ATOM   3894  O   TYR A 497     -17.099  31.068  43.942  1.00104.02           O  
ANISOU 3894  O   TYR A 497    11869  13776  13877   1090   -306  -1463       O  
ATOM   3895  CB  TYR A 497     -18.494  28.059  43.943  1.00111.13           C  
ANISOU 3895  CB  TYR A 497    12329  14986  14909    655    -30  -1480       C  
ATOM   3896  CG  TYR A 497     -19.567  27.048  44.287  1.00113.27           C  
ANISOU 3896  CG  TYR A 497    12297  15427  15315    485    134  -1567       C  
ATOM   3897  CD1 TYR A 497     -20.869  27.198  43.822  1.00100.33           C  
ANISOU 3897  CD1 TYR A 497    10333  13902  13886    576     52  -1759       C  
ATOM   3898  CD2 TYR A 497     -19.264  25.911  45.022  1.00122.49           C  
ANISOU 3898  CD2 TYR A 497    13498  16630  16414    224    352  -1439       C  
ATOM   3899  CE1 TYR A 497     -21.852  26.261  44.121  1.00100.08           C  
ANISOU 3899  CE1 TYR A 497    10002  14032  13991    391    208  -1841       C  
ATOM   3900  CE2 TYR A 497     -20.233  24.971  45.318  1.00114.24           C  
ANISOU 3900  CE2 TYR A 497    12182  15720  15506     34    503  -1490       C  
ATOM   3901  CZ  TYR A 497     -21.523  25.147  44.867  1.00101.89           C  
ANISOU 3901  CZ  TYR A 497    10283  14282  14149    107    440  -1698       C  
ATOM   3902  OH  TYR A 497     -22.481  24.204  45.168  1.00103.91           O  
ANISOU 3902  OH  TYR A 497    10250  14680  14553   -111    599  -1751       O  
ATOM   3903  N   CYS A 498     -16.054  29.517  45.190  1.00 99.83           N  
ANISOU 3903  N   CYS A 498    11483  13349  13100    733     36  -1284       N  
ATOM   3904  CA  CYS A 498     -14.710  30.026  44.942  1.00 97.52           C  
ANISOU 3904  CA  CYS A 498    11497  12893  12663    758    -71  -1140       C  
ATOM   3905  C   CYS A 498     -13.751  28.839  45.031  1.00 93.15           C  
ANISOU 3905  C   CYS A 498    11086  12329  11977    549     14   -952       C  
ATOM   3906  O   CYS A 498     -12.816  28.810  45.825  1.00101.25           O  
ANISOU 3906  O   CYS A 498    12276  13346  12849    475    112   -860       O  
ATOM   3907  CB  CYS A 498     -14.354  31.140  45.925  1.00 96.04           C  
ANISOU 3907  CB  CYS A 498    11403  12683  12406    854     -8  -1222       C  
ATOM   3908  SG  CYS A 498     -12.987  32.181  45.384  1.00106.08           S  
ANISOU 3908  SG  CYS A 498    12996  13722  13590    932   -207  -1094       S  
ATOM   3909  N   ASP A 499     -14.000  27.837  44.187  1.00 85.81           N  
ANISOU 3909  N   ASP A 499    10084  11398  11124    462    -42   -912       N  
ATOM   3910  CA  ASP A 499     -13.280  26.568  44.289  1.00 95.59           C  
ANISOU 3910  CA  ASP A 499    11409  12606  12303    274     38   -768       C  
ATOM   3911  C   ASP A 499     -11.766  26.676  44.126  1.00 94.77           C  
ANISOU 3911  C   ASP A 499    11573  12393  12043    263    -21   -622       C  
ATOM   3912  O   ASP A 499     -11.054  25.928  44.818  1.00 97.11           O  
ANISOU 3912  O   ASP A 499    11957  12678  12264    138     91   -504       O  
ATOM   3913  CB  ASP A 499     -13.858  25.574  43.277  1.00 86.43           C  
ANISOU 3913  CB  ASP A 499    10112  11439  11287    204    -44   -806       C  
ATOM   3914  CG  ASP A 499     -15.348  25.401  43.433  1.00101.69           C  
ANISOU 3914  CG  ASP A 499    11749  13495  13393    191     15   -955       C  
ATOM   3915  OD1 ASP A 499     -15.870  25.741  44.515  1.00 92.42           O  
ANISOU 3915  OD1 ASP A 499    10471  12430  12214    187    182  -1006       O  
ATOM   3916  OD2 ASP A 499     -15.996  24.944  42.468  1.00108.55           O1-
ANISOU 3916  OD2 ASP A 499    12475  14373  14394    182   -105  -1040       O1-
ATOM   3917  N   PRO A 500     -11.201  27.552  43.256  1.00 80.42           N  
ANISOU 3917  N   PRO A 500     9886  10498  10171    379   -196   -608       N  
ATOM   3918  CA  PRO A 500      -9.740  27.723  43.245  1.00 73.82           C  
ANISOU 3918  CA  PRO A 500     9277   9587   9183    350   -222   -478       C  
ATOM   3919  C   PRO A 500      -9.176  28.018  44.625  1.00 84.33           C  
ANISOU 3919  C   PRO A 500    10696  10938  10407    314    -83   -438       C  
ATOM   3920  O   PRO A 500      -8.056  27.595  44.914  1.00 89.16           O  
ANISOU 3920  O   PRO A 500    11438  11524  10914    234    -53   -322       O  
ATOM   3921  CB  PRO A 500      -9.524  28.901  42.289  1.00 75.38           C  
ANISOU 3921  CB  PRO A 500     9568   9722   9353    475   -409   -475       C  
ATOM   3922  CG  PRO A 500     -10.867  29.538  42.164  1.00 75.93           C  
ANISOU 3922  CG  PRO A 500     9474   9814   9561    603   -471   -604       C  
ATOM   3923  CD  PRO A 500     -11.832  28.409  42.247  1.00 81.91           C  
ANISOU 3923  CD  PRO A 500    10020  10670  10431    528   -382   -684       C  
ATOM   3924  N   ALA A 501      -9.951  28.691  45.478  1.00 93.68           N  
ANISOU 3924  N   ALA A 501    11791  12188  11614    374     -2   -550       N  
ATOM   3925  CA  ALA A 501      -9.597  28.937  46.862  1.00 88.77           C  
ANISOU 3925  CA  ALA A 501    11223  11640  10866    334    143   -552       C  
ATOM   3926  C   ALA A 501      -9.840  27.738  47.812  1.00 88.46           C  
ANISOU 3926  C   ALA A 501    11105  11725  10780    174    331   -478       C  
ATOM   3927  O   ALA A 501      -9.397  27.809  48.973  1.00 95.53           O  
ANISOU 3927  O   ALA A 501    12068  12712  11518    116    444   -440       O  
ATOM   3928  CB  ALA A 501     -10.356  30.160  47.401  1.00 93.08           C  
ANISOU 3928  CB  ALA A 501    11690  12225  11451    470    163   -744       C  
ATOM   3929  N   SER A 502     -10.482  26.636  47.366  1.00 73.73           N  
ANISOU 3929  N   SER A 502     9110   9865   9041     87    358   -444       N  
ATOM   3930  CA  SER A 502     -10.529  25.413  48.153  1.00 74.64           C  
ANISOU 3930  CA  SER A 502     9188  10039   9131    -92    508   -311       C  
ATOM   3931  C   SER A 502      -9.169  24.740  48.269  1.00 81.47           C  
ANISOU 3931  C   SER A 502    10243  10806   9907   -165    469   -117       C  
ATOM   3932  O   SER A 502      -9.021  23.783  49.044  1.00 84.63           O  
ANISOU 3932  O   SER A 502    10654  11229  10272   -306    571     38       O  
ATOM   3933  CB  SER A 502     -11.525  24.385  47.552  1.00 78.78           C  
ANISOU 3933  CB  SER A 502     9526  10547   9860   -182    524   -331       C  
ATOM   3934  OG  SER A 502     -11.031  23.832  46.342  1.00112.22           O  
ANISOU 3934  OG  SER A 502    13819  14625  14194   -172    367   -303       O  
ATOM   3935  N   LEU A 503      -8.181  25.203  47.525  1.00 97.26           N  
ANISOU 3935  N   LEU A 503    12380  12700  11873    -78    322   -111       N  
ATOM   3936  CA  LEU A 503      -6.825  24.718  47.667  1.00 84.06           C  
ANISOU 3936  CA  LEU A 503    10863  10959  10118   -122    281     40       C  
ATOM   3937  C   LEU A 503      -6.023  25.681  48.533  1.00 91.57           C  
ANISOU 3937  C   LEU A 503    11940  11978  10874    -86    290     52       C  
ATOM   3938  O   LEU A 503      -6.188  26.901  48.457  1.00 91.13           O  
ANISOU 3938  O   LEU A 503    11900  11941  10783     10    255    -77       O  
ATOM   3939  CB  LEU A 503      -6.164  24.548  46.294  1.00 83.46           C  
ANISOU 3939  CB  LEU A 503    10833  10761  10116    -70    131     24       C  
ATOM   3940  CG  LEU A 503      -4.720  24.046  46.270  1.00 89.27           C  
ANISOU 3940  CG  LEU A 503    11690  11430  10798    -92     78    141       C  
ATOM   3941  CD1 LEU A 503      -4.636  22.636  46.826  1.00 94.93           C  
ANISOU 3941  CD1 LEU A 503    12384  12086  11598   -194    134    274       C  
ATOM   3942  CD2 LEU A 503      -4.128  24.096  44.835  1.00 85.85           C  
ANISOU 3942  CD2 LEU A 503    11280  10937  10403    -35    -49     76       C  
ATOM   3943  N   PHE A 504      -5.154  25.097  49.374  1.00 85.17           N  
ANISOU 3943  N   PHE A 504    11217  11192   9952   -164    322    208       N  
ATOM   3944  CA  PHE A 504      -4.300  25.843  50.303  1.00 85.55           C  
ANISOU 3944  CA  PHE A 504    11380  11328   9798   -154    321    225       C  
ATOM   3945  C   PHE A 504      -3.614  27.026  49.609  1.00 87.58           C  
ANISOU 3945  C   PHE A 504    11718  11514  10044    -56    198    119       C  
ATOM   3946  O   PHE A 504      -3.796  28.195  49.987  1.00 93.69           O  
ANISOU 3946  O   PHE A 504    12514  12332  10752     -2    202    -13       O  
ATOM   3947  CB  PHE A 504      -3.305  24.883  50.959  1.00 86.08           C  
ANISOU 3947  CB  PHE A 504    11525  11398   9784   -235    308    433       C  
ATOM   3948  CG  PHE A 504      -2.278  25.573  51.805  1.00 84.26           C  
ANISOU 3948  CG  PHE A 504    11406  11264   9346   -228    271    449       C  
ATOM   3949  CD1 PHE A 504      -2.520  25.824  53.131  1.00 71.31           C  
ANISOU 3949  CD1 PHE A 504     9780   9815   7500   -283    368    459       C  
ATOM   3950  CD2 PHE A 504      -1.039  25.928  51.271  1.00 87.13           C  
ANISOU 3950  CD2 PHE A 504    11845  11551   9710   -181    139    448       C  
ATOM   3951  CE1 PHE A 504      -1.586  26.483  53.926  1.00 97.65           C  
ANISOU 3951  CE1 PHE A 504    13210  13259  10632   -281    319    444       C  
ATOM   3952  CE2 PHE A 504      -0.090  26.579  52.071  1.00 83.00           C  
ANISOU 3952  CE2 PHE A 504    11406  11124   9007   -189     94    446       C  
ATOM   3953  CZ  PHE A 504      -0.367  26.854  53.395  1.00 99.43           C  
ANISOU 3953  CZ  PHE A 504    13507  13387  10885   -235    174    438       C  
ATOM   3954  N   HIS A 505      -2.854  26.730  48.560  1.00 75.80           N  
ANISOU 3954  N   HIS A 505    10262   9910   8628    -40     90    166       N  
ATOM   3955  CA  HIS A 505      -1.952  27.681  47.920  1.00 75.00           C  
ANISOU 3955  CA  HIS A 505    10248   9756   8494      5    -20    127       C  
ATOM   3956  C   HIS A 505      -2.657  28.937  47.390  1.00 87.66           C  
ANISOU 3956  C   HIS A 505    11847  11314  10145     85    -65     -6       C  
ATOM   3957  O   HIS A 505      -2.049  30.021  47.323  1.00 94.35           O  
ANISOU 3957  O   HIS A 505    12782  12117  10948    105   -135    -40       O  
ATOM   3958  CB  HIS A 505      -1.211  26.971  46.776  1.00 75.88           C  
ANISOU 3958  CB  HIS A 505    10358   9797   8677     -2    -97    185       C  
ATOM   3959  CG  HIS A 505      -0.483  25.738  47.222  1.00 79.54           C  
ANISOU 3959  CG  HIS A 505    10816  10259   9146    -50    -82    305       C  
ATOM   3960  ND1 HIS A 505      -1.147  24.557  47.486  1.00 77.84           N  
ANISOU 3960  ND1 HIS A 505    10534  10014   9029    -88    -23    366       N  
ATOM   3961  CD2 HIS A 505       0.830  25.497  47.476  1.00 81.00           C  
ANISOU 3961  CD2 HIS A 505    11046  10456   9276    -64   -132    382       C  
ATOM   3962  CE1 HIS A 505      -0.277  23.642  47.881  1.00 81.24           C  
ANISOU 3962  CE1 HIS A 505    10984  10411   9472   -113    -48    489       C  
ATOM   3963  NE2 HIS A 505       0.928  24.185  47.883  1.00 88.79           N  
ANISOU 3963  NE2 HIS A 505    11999  11403  10334    -88   -116    492       N  
ATOM   3964  N   VAL A 506      -3.928  28.822  46.998  1.00 90.16           N  
ANISOU 3964  N   VAL A 506    12057  11625  10574    131    -40    -79       N  
ATOM   3965  CA  VAL A 506      -4.651  29.977  46.472  1.00 91.24           C  
ANISOU 3965  CA  VAL A 506    12177  11703  10786    234   -112   -195       C  
ATOM   3966  C   VAL A 506      -5.217  30.829  47.599  1.00 88.29           C  
ANISOU 3966  C   VAL A 506    11782  11378  10386    284    -40   -330       C  
ATOM   3967  O   VAL A 506      -5.115  32.058  47.567  1.00 88.11           O  
ANISOU 3967  O   VAL A 506    11822  11269  10387    358   -117   -416       O  
ATOM   3968  CB  VAL A 506      -5.750  29.506  45.503  1.00 83.45           C  
ANISOU 3968  CB  VAL A 506    11062  10707   9938    276   -144   -233       C  
ATOM   3969  CG1 VAL A 506      -6.591  30.683  45.047  1.00 74.54           C  
ANISOU 3969  CG1 VAL A 506     9900   9519   8905    406   -239   -342       C  
ATOM   3970  CG2 VAL A 506      -5.134  28.778  44.314  1.00 79.79           C  
ANISOU 3970  CG2 VAL A 506    10626  10212   9481    234   -226   -147       C  
ATOM   3971  N   SER A 507      -5.823  30.203  48.613  1.00 87.11           N  
ANISOU 3971  N   SER A 507    11540  11368  10190    239    111   -358       N  
ATOM   3972  CA  SER A 507      -6.374  30.981  49.719  1.00 88.33           C  
ANISOU 3972  CA  SER A 507    11653  11620  10288    284    204   -524       C  
ATOM   3973  C   SER A 507      -5.337  31.324  50.783  1.00 97.04           C  
ANISOU 3973  C   SER A 507    12882  12793  11198    226    230   -517       C  
ATOM   3974  O   SER A 507      -5.663  32.054  51.726  1.00 95.60           O  
ANISOU 3974  O   SER A 507    12679  12705  10942    262    300   -690       O  
ATOM   3975  CB  SER A 507      -7.546  30.241  50.370  1.00 79.33           C  
ANISOU 3975  CB  SER A 507    10339  10652   9152    242    376   -569       C  
ATOM   3976  OG  SER A 507      -7.154  28.957  50.813  1.00 75.95           O  
ANISOU 3976  OG  SER A 507     9928  10305   8626     92    460   -377       O  
ATOM   3977  N   ASN A 508      -4.110  30.818  50.661  1.00 88.50           N  
ANISOU 3977  N   ASN A 508    11911  11682  10033    142    171   -347       N  
ATOM   3978  CA  ASN A 508      -3.007  31.214  51.529  1.00 81.92           C  
ANISOU 3978  CA  ASN A 508    11190  10906   9028     91    152   -342       C  
ATOM   3979  C   ASN A 508      -1.964  32.042  50.786  1.00 84.89           C  
ANISOU 3979  C   ASN A 508    11678  11121   9455    105     -3   -334       C  
ATOM   3980  O   ASN A 508      -0.842  32.206  51.276  1.00107.64           O  
ANISOU 3980  O   ASN A 508    14642  14038  12219     42    -46   -299       O  
ATOM   3981  CB  ASN A 508      -2.364  29.987  52.175  1.00 87.97           C  
ANISOU 3981  CB  ASN A 508    11976  11795   9652    -20    200   -148       C  
ATOM   3982  CG  ASN A 508      -3.250  29.359  53.232  1.00 78.58           C  
ANISOU 3982  CG  ASN A 508    10704  10800   8351    -75    364   -136       C  
ATOM   3983  OD1 ASN A 508      -3.125  29.656  54.420  1.00 81.46           O  
ANISOU 3983  OD1 ASN A 508    11094  11345   8509   -113    430   -190       O  
ATOM   3984  ND2 ASN A 508      -4.165  28.500  52.803  1.00 77.81           N  
ANISOU 3984  ND2 ASN A 508    10500  10686   8377    -96    434    -71       N  
ATOM   3985  N   ASP A 509      -2.315  32.549  49.602  1.00 77.89           N  
ANISOU 3985  N   ASP A 509    10788  10074   8733    174    -91   -352       N  
ATOM   3986  CA  ASP A 509      -1.546  33.578  48.902  1.00 74.28           C  
ANISOU 3986  CA  ASP A 509    10435   9456   8333    177   -229   -348       C  
ATOM   3987  C   ASP A 509      -0.117  33.109  48.614  1.00 80.41           C  
ANISOU 3987  C   ASP A 509    11275  10254   9025     69   -275   -195       C  
ATOM   3988  O   ASP A 509       0.868  33.693  49.068  1.00100.36           O  
ANISOU 3988  O   ASP A 509    13873  12774  11483      8   -320   -213       O  
ATOM   3989  CB  ASP A 509      -1.565  34.887  49.702  1.00 68.78           C  
ANISOU 3989  CB  ASP A 509     9791   8702   7641    216   -253   -536       C  
ATOM   3990  CG  ASP A 509      -0.989  36.057  48.930  1.00 85.72           C  
ANISOU 3990  CG  ASP A 509    12042  10628   9901    213   -405   -525       C  
ATOM   3991  OD1 ASP A 509      -1.401  36.268  47.771  1.00 89.69           O  
ANISOU 3991  OD1 ASP A 509    12546  11000  10531    262   -487   -447       O  
ATOM   3992  OD2 ASP A 509      -0.133  36.775  49.490  1.00107.73           O1-
ANISOU 3992  OD2 ASP A 509    14910  13375  12646    149   -448   -588       O1-
ATOM   3993  N   TYR A 510      -0.024  32.030  47.839  1.00 79.30           N  
ANISOU 3993  N   TYR A 510    11086  10139   8904     49   -266    -70       N  
ATOM   3994  CA  TYR A 510       1.247  31.460  47.413  1.00 81.14           C  
ANISOU 3994  CA  TYR A 510    11339  10401   9088    -27   -303     49       C  
ATOM   3995  C   TYR A 510       1.253  31.354  45.896  1.00 86.67           C  
ANISOU 3995  C   TYR A 510    12026  11042   9862    -21   -361    105       C  
ATOM   3996  O   TYR A 510       0.297  30.840  45.306  1.00 94.24           O  
ANISOU 3996  O   TYR A 510    12923  11992  10892     32   -346     95       O  
ATOM   3997  CB  TYR A 510       1.470  30.073  48.026  1.00 80.74           C  
ANISOU 3997  CB  TYR A 510    11233  10457   8987    -52   -237    131       C  
ATOM   3998  CG  TYR A 510       1.931  30.081  49.466  1.00 97.40           C  
ANISOU 3998  CG  TYR A 510    13373  12675  10960    -90   -208    132       C  
ATOM   3999  CD1 TYR A 510       3.245  30.383  49.797  1.00112.07           C  
ANISOU 3999  CD1 TYR A 510    15273  14573  12735   -145   -277    156       C  
ATOM   4000  CD2 TYR A 510       1.051  29.771  50.494  1.00 95.09           C  
ANISOU 4000  CD2 TYR A 510    13053  12474  10602    -82   -113    108       C  
ATOM   4001  CE1 TYR A 510       3.666  30.387  51.116  1.00114.79           C  
ANISOU 4001  CE1 TYR A 510    15642  15044  12929   -179   -274    152       C  
ATOM   4002  CE2 TYR A 510       1.462  29.771  51.813  1.00 95.68           C  
ANISOU 4002  CE2 TYR A 510    13161  12691  10503   -126    -90    117       C  
ATOM   4003  CZ  TYR A 510       2.770  30.080  52.119  1.00109.85           C  
ANISOU 4003  CZ  TYR A 510    15006  14521  12211   -169   -182    138       C  
ATOM   4004  OH  TYR A 510       3.186  30.082  53.430  1.00119.89           O  
ANISOU 4004  OH  TYR A 510    16307  15959  13285   -213   -182    142       O  
ATOM   4005  N   SER A 511       2.321  31.839  45.267  1.00 78.21           N  
ANISOU 4005  N   SER A 511    11004   9955   8758    -89   -424    159       N  
ATOM   4006  CA  SER A 511       2.469  31.649  43.831  1.00 73.95           C  
ANISOU 4006  CA  SER A 511    10447   9420   8230   -106   -464    219       C  
ATOM   4007  C   SER A 511       2.601  30.163  43.524  1.00 79.20           C  
ANISOU 4007  C   SER A 511    11016  10175   8902    -93   -412    228       C  
ATOM   4008  O   SER A 511       3.321  29.432  44.209  1.00 87.95           O  
ANISOU 4008  O   SER A 511    12090  11336   9990   -111   -377    245       O  
ATOM   4009  CB  SER A 511       3.684  32.415  43.306  1.00 72.74           C  
ANISOU 4009  CB  SER A 511    10348   9270   8019   -214   -515    284       C  
ATOM   4010  OG  SER A 511       4.892  31.849  43.780  1.00 85.33           O  
ANISOU 4010  OG  SER A 511    11896  10966   9558   -274   -483    294       O  
ATOM   4011  N   PHE A 512       1.886  29.713  42.492  1.00 81.92           N  
ANISOU 4011  N   PHE A 512    11314  10526   9286    -56   -425    212       N  
ATOM   4012  CA  PHE A 512       1.775  28.294  42.185  1.00 72.47           C  
ANISOU 4012  CA  PHE A 512    10021   9374   8141    -34   -385    180       C  
ATOM   4013  C   PHE A 512       2.565  27.856  40.960  1.00 73.20           C  
ANISOU 4013  C   PHE A 512    10070   9555   8187    -65   -403    163       C  
ATOM   4014  O   PHE A 512       2.722  26.648  40.752  1.00 70.71           O  
ANISOU 4014  O   PHE A 512     9671   9262   7935    -43   -375    107       O  
ATOM   4015  CB  PHE A 512       0.302  27.910  41.986  1.00 68.07           C  
ANISOU 4015  CB  PHE A 512     9407   8779   7677     26   -380    123       C  
ATOM   4016  CG  PHE A 512       0.004  26.473  42.298  1.00 72.90           C  
ANISOU 4016  CG  PHE A 512     9930   9379   8390     32   -323     96       C  
ATOM   4017  CD1 PHE A 512       0.018  26.015  43.603  1.00 74.56           C  
ANISOU 4017  CD1 PHE A 512    10141   9563   8626     18   -258    148       C  
ATOM   4018  CD2 PHE A 512      -0.287  25.578  41.282  1.00 76.89           C  
ANISOU 4018  CD2 PHE A 512    10356   9896   8964     41   -343     22       C  
ATOM   4019  CE1 PHE A 512      -0.257  24.688  43.890  1.00 79.21           C  
ANISOU 4019  CE1 PHE A 512    10661  10108   9328      5   -217    163       C  
ATOM   4020  CE2 PHE A 512      -0.561  24.253  41.561  1.00 78.17           C  
ANISOU 4020  CE2 PHE A 512    10440   9998   9262     36   -304     -5       C  
ATOM   4021  CZ  PHE A 512      -0.546  23.807  42.865  1.00 77.36           C  
ANISOU 4021  CZ  PHE A 512    10348   9839   9206     14   -242     84       C  
ATOM   4022  N   ILE A 513       3.065  28.790  40.147  1.00 65.59           N  
ANISOU 4022  N   ILE A 513     9159   8644   7120   -123   -445    206       N  
ATOM   4023  CA  ILE A 513       3.762  28.403  38.926  1.00 67.05           C  
ANISOU 4023  CA  ILE A 513     9288   8969   7218   -166   -440    177       C  
ATOM   4024  C   ILE A 513       5.082  27.703  39.222  1.00 82.08           C  
ANISOU 4024  C   ILE A 513    11113  10947   9126   -190   -386    141       C  
ATOM   4025  O   ILE A 513       5.628  27.027  38.342  1.00 88.26           O  
ANISOU 4025  O   ILE A 513    11805  11856   9875   -195   -359     57       O  
ATOM   4026  CB  ILE A 513       3.989  29.630  38.023  1.00 76.27           C  
ANISOU 4026  CB  ILE A 513    10538  10192   8250   -252   -492    275       C  
ATOM   4027  CG1 ILE A 513       4.256  29.195  36.579  1.00 69.67           C  
ANISOU 4027  CG1 ILE A 513     9641   9548   7283   -291   -486    232       C  
ATOM   4028  CG2 ILE A 513       5.134  30.481  38.550  1.00 78.20           C  
ANISOU 4028  CG2 ILE A 513    10832  10429   8453   -353   -480    358       C  
ATOM   4029  CD1 ILE A 513       3.143  28.366  35.977  1.00 71.26           C  
ANISOU 4029  CD1 ILE A 513     9783   9769   7523   -204   -516    122       C  
ATOM   4030  N   ARG A 514       5.604  27.834  40.447  1.00 89.16           N  
ANISOU 4030  N   ARG A 514    12030  11785  10063   -194   -377    186       N  
ATOM   4031  CA  ARG A 514       6.889  27.224  40.777  1.00 83.38           C  
ANISOU 4031  CA  ARG A 514    11209  11125   9348   -202   -355    161       C  
ATOM   4032  C   ARG A 514       6.856  25.715  40.566  1.00 82.46           C  
ANISOU 4032  C   ARG A 514    10981  11000   9351   -110   -336     63       C  
ATOM   4033  O   ARG A 514       7.841  25.123  40.111  1.00 90.42           O  
ANISOU 4033  O   ARG A 514    11876  12104  10375    -97   -319    -17       O  
ATOM   4034  CB  ARG A 514       7.277  27.555  42.220  1.00 74.94           C  
ANISOU 4034  CB  ARG A 514    10182   9998   8292   -210   -375    227       C  
ATOM   4035  CG  ARG A 514       6.475  26.799  43.273  1.00 85.94           C  
ANISOU 4035  CG  ARG A 514    11592  11288   9772   -131   -372    248       C  
ATOM   4036  CD  ARG A 514       5.985  27.700  44.383  1.00 90.20           C  
ANISOU 4036  CD  ARG A 514    12234  11778  10259   -154   -380    296       C  
ATOM   4037  NE  ARG A 514       7.087  28.254  45.158  1.00 94.85           N  
ANISOU 4037  NE  ARG A 514    12835  12425  10778   -209   -416    321       N  
ATOM   4038  CZ  ARG A 514       6.957  29.222  46.054  1.00102.73           C  
ANISOU 4038  CZ  ARG A 514    13917  13405  11712   -247   -434    320       C  
ATOM   4039  NH1 ARG A 514       5.779  29.757  46.328  1.00 84.79           N  
ANISOU 4039  NH1 ARG A 514    11717  11059   9442   -220   -412    292       N  
ATOM   4040  NH2 ARG A 514       8.036  29.660  46.695  1.00122.28           N  
ANISOU 4040  NH2 ARG A 514    16386  15947  14127   -308   -481    322       N  
ATOM   4041  N   TYR A 515       5.721  25.080  40.870  1.00 71.29           N  
ANISOU 4041  N   TYR A 515     9582   9464   8039    -49   -339     54       N  
ATOM   4042  CA  TYR A 515       5.618  23.634  40.729  1.00 72.81           C  
ANISOU 4042  CA  TYR A 515     9681   9593   8391     25   -335    -33       C  
ATOM   4043  C   TYR A 515       5.727  23.217  39.270  1.00 80.41           C  
ANISOU 4043  C   TYR A 515    10557  10659   9335     35   -324   -196       C  
ATOM   4044  O   TYR A 515       6.223  22.126  38.969  1.00 81.70           O  
ANISOU 4044  O   TYR A 515    10612  10810   9620     97   -322   -321       O  
ATOM   4045  CB  TYR A 515       4.300  23.156  41.337  1.00 72.49           C  
ANISOU 4045  CB  TYR A 515     9675   9407   8462     48   -332      6       C  
ATOM   4046  CG  TYR A 515       4.139  23.556  42.787  1.00 73.53           C  
ANISOU 4046  CG  TYR A 515     9885   9485   8568     29   -324    150       C  
ATOM   4047  CD1 TYR A 515       4.761  22.843  43.803  1.00 97.21           C  
ANISOU 4047  CD1 TYR A 515    12872  12432  11630     51   -339    238       C  
ATOM   4048  CD2 TYR A 515       3.384  24.668  43.138  1.00 81.61           C  
ANISOU 4048  CD2 TYR A 515    10990  10522   9495     -4   -310    190       C  
ATOM   4049  CE1 TYR A 515       4.619  23.215  45.128  1.00 98.53           C  
ANISOU 4049  CE1 TYR A 515    13112  12600  11724     22   -332    365       C  
ATOM   4050  CE2 TYR A 515       3.238  25.049  44.458  1.00 79.42           C  
ANISOU 4050  CE2 TYR A 515    10774  10233   9170    -21   -292    278       C  
ATOM   4051  CZ  TYR A 515       3.857  24.319  45.449  1.00 82.72           C  
ANISOU 4051  CZ  TYR A 515    11184  10637   9608    -17   -298    366       C  
ATOM   4052  OH  TYR A 515       3.715  24.693  46.765  1.00 92.79           O  
ANISOU 4052  OH  TYR A 515    12521  11946  10789    -44   -280    449       O  
ATOM   4053  N   TYR A 516       5.278  24.074  38.355  1.00 75.10           N  
ANISOU 4053  N   TYR A 516     9930  10094   8512    -20   -327   -203       N  
ATOM   4054  CA  TYR A 516       5.497  23.834  36.934  1.00 75.88           C  
ANISOU 4054  CA  TYR A 516     9953  10362   8516    -33   -314   -349       C  
ATOM   4055  C   TYR A 516       6.963  24.033  36.567  1.00 78.13           C  
ANISOU 4055  C   TYR A 516    10164  10825   8696    -78   -266   -382       C  
ATOM   4056  O   TYR A 516       7.603  23.140  36.000  1.00 77.67           O  
ANISOU 4056  O   TYR A 516     9971  10860   8680    -32   -232   -561       O  
ATOM   4057  CB  TYR A 516       4.597  24.758  36.111  1.00 73.77           C  
ANISOU 4057  CB  TYR A 516     9768  10171   8092    -86   -354   -298       C  
ATOM   4058  CG  TYR A 516       4.651  24.525  34.618  1.00 75.63           C  
ANISOU 4058  CG  TYR A 516     9938  10619   8177   -111   -352   -438       C  
ATOM   4059  CD1 TYR A 516       5.585  25.184  33.829  1.00 83.30           C  
ANISOU 4059  CD1 TYR A 516    10905  11817   8928   -206   -313   -407       C  
ATOM   4060  CD2 TYR A 516       3.771  23.650  33.997  1.00 71.63           C  
ANISOU 4060  CD2 TYR A 516     9369  10110   7736    -57   -386   -606       C  
ATOM   4061  CE1 TYR A 516       5.640  24.983  32.468  1.00 86.57           C  
ANISOU 4061  CE1 TYR A 516    11259  12478   9156   -242   -300   -534       C  
ATOM   4062  CE2 TYR A 516       3.818  23.441  32.633  1.00 72.82           C  
ANISOU 4062  CE2 TYR A 516     9459  10493   7716    -82   -390   -760       C  
ATOM   4063  CZ  TYR A 516       4.756  24.111  31.874  1.00 83.44           C  
ANISOU 4063  CZ  TYR A 516    10806  12090   8807   -173   -343   -720       C  
ATOM   4064  OH  TYR A 516       4.813  23.910  30.515  1.00 90.97           O  
ANISOU 4064  OH  TYR A 516    11697  13324   9541   -212   -335   -872       O  
ATOM   4065  N   THR A 517       7.512  25.207  36.889  1.00 77.33           N  
ANISOU 4065  N   THR A 517    10135  10774   8473   -171   -261   -230       N  
ATOM   4066  CA  THR A 517       8.878  25.530  36.488  1.00 81.06           C  
ANISOU 4066  CA  THR A 517    10522  11444   8834   -251   -206   -250       C  
ATOM   4067  C   THR A 517       9.880  24.558  37.098  1.00 93.82           C  
ANISOU 4067  C   THR A 517    11993  13047  10609   -163   -190   -353       C  
ATOM   4068  O   THR A 517      10.783  24.067  36.411  1.00100.04           O  
ANISOU 4068  O   THR A 517    12622  14011  11376   -153   -134   -509       O  
ATOM   4069  CB  THR A 517       9.216  26.966  36.888  1.00 81.60           C  
ANISOU 4069  CB  THR A 517    10700  11511   8794   -382   -221    -59       C  
ATOM   4070  OG1 THR A 517       9.089  27.109  38.309  1.00 80.68           O  
ANISOU 4070  OG1 THR A 517    10649  11204   8803   -339   -267     24       O  
ATOM   4071  CG2 THR A 517       8.287  27.951  36.191  1.00 86.01           C  
ANISOU 4071  CG2 THR A 517    11398  12062   9219   -454   -260     57       C  
ATOM   4072  N   ARG A 518       9.734  24.268  38.394  1.00 95.42           N  
ANISOU 4072  N   ARG A 518    12237  13052  10965    -95   -244   -270       N  
ATOM   4073  CA  ARG A 518      10.662  23.363  39.064  1.00 85.86           C  
ANISOU 4073  CA  ARG A 518    10902  11806   9916      2   -266   -326       C  
ATOM   4074  C   ARG A 518      10.642  21.972  38.445  1.00 97.09           C  
ANISOU 4074  C   ARG A 518    12192  13196  11501    128   -260   -529       C  
ATOM   4075  O   ARG A 518      11.678  21.298  38.398  1.00100.64           O  
ANISOU 4075  O   ARG A 518    12479  13701  12059    209   -261   -653       O  
ATOM   4076  CB  ARG A 518      10.329  23.287  40.554  1.00 84.55           C  
ANISOU 4076  CB  ARG A 518    10830  11446   9847     41   -337   -167       C  
ATOM   4077  CG  ARG A 518      11.072  22.204  41.306  1.00 99.96           C  
ANISOU 4077  CG  ARG A 518    12677  13318  11987    162   -398   -181       C  
ATOM   4078  CD  ARG A 518      10.128  21.415  42.194  1.00107.15           C  
ANISOU 4078  CD  ARG A 518    13674  13998  13040    229   -449    -76       C  
ATOM   4079  NE  ARG A 518       9.404  20.393  41.448  1.00114.45           N  
ANISOU 4079  NE  ARG A 518    14560  14808  14117    294   -434   -203       N  
ATOM   4080  CZ  ARG A 518       8.394  19.686  41.935  1.00131.35           C  
ANISOU 4080  CZ  ARG A 518    16766  16747  16393    318   -457   -132       C  
ATOM   4081  NH1 ARG A 518       7.975  19.846  43.180  1.00131.89           N  
ANISOU 4081  NH1 ARG A 518    16941  16729  16440    286   -483     74       N  
ATOM   4082  NH2 ARG A 518       7.789  18.795  41.154  1.00132.51           N  
ANISOU 4082  NH2 ARG A 518    16862  16793  16691    359   -449   -280       N  
ATOM   4083  N   THR A 519       9.483  21.529  37.955  1.00 83.03           N  
ANISOU 4083  N   THR A 519    10464  11323   9760    153   -263   -590       N  
ATOM   4084  CA  THR A 519       9.395  20.203  37.352  1.00 79.71           C  
ANISOU 4084  CA  THR A 519     9923  10842   9520    264   -268   -815       C  
ATOM   4085  C   THR A 519      10.195  20.126  36.057  1.00 80.82           C  
ANISOU 4085  C   THR A 519     9910  11253   9544    258   -194  -1053       C  
ATOM   4086  O   THR A 519      10.930  19.156  35.834  1.00 82.64           O  
ANISOU 4086  O   THR A 519     9974  11488   9938    373   -190  -1261       O  
ATOM   4087  CB  THR A 519       7.933  19.842  37.103  1.00 86.33           C  
ANISOU 4087  CB  THR A 519    10844  11539  10417    262   -292   -835       C  
ATOM   4088  OG1 THR A 519       7.237  19.784  38.355  1.00 77.91           O  
ANISOU 4088  OG1 THR A 519     9888  10245   9467    264   -338   -631       O  
ATOM   4089  CG2 THR A 519       7.831  18.503  36.405  1.00 84.75           C  
ANISOU 4089  CG2 THR A 519    10519  11267  10416    360   -305  -1102       C  
ATOM   4090  N   LEU A 520      10.062  21.131  35.189  1.00 88.21           N  
ANISOU 4090  N   LEU A 520    10895  12424  10198    127   -136  -1027       N  
ATOM   4091  CA  LEU A 520      10.870  21.163  33.976  1.00 93.78           C  
ANISOU 4091  CA  LEU A 520    11453  13449  10729     87    -44  -1226       C  
ATOM   4092  C   LEU A 520      12.348  21.335  34.299  1.00 96.73           C  
ANISOU 4092  C   LEU A 520    11682  13960  11110     80      7  -1237       C  
ATOM   4093  O   LEU A 520      13.206  20.853  33.551  1.00 96.90           O  
ANISOU 4093  O   LEU A 520    11504  14202  11111    115     85  -1480       O  
ATOM   4094  CB  LEU A 520      10.395  22.286  33.051  1.00103.99           C  
ANISOU 4094  CB  LEU A 520    12855  14961  11697    -77     -8  -1122       C  
ATOM   4095  CG  LEU A 520       9.326  21.947  32.007  1.00101.49           C  
ANISOU 4095  CG  LEU A 520    12568  14710  11283    -70    -29  -1259       C  
ATOM   4096  CD1 LEU A 520       8.026  21.504  32.666  1.00 93.61           C  
ANISOU 4096  CD1 LEU A 520    11676  13394  10498      9   -131  -1205       C  
ATOM   4097  CD2 LEU A 520       9.079  23.126  31.078  1.00 89.75           C  
ANISOU 4097  CD2 LEU A 520    11179  13474   9447   -235    -10  -1116       C  
ATOM   4098  N   TYR A 521      12.659  22.010  35.408  1.00 99.61           N  
ANISOU 4098  N   TYR A 521    12125  14216  11505     36    -38  -1003       N  
ATOM   4099  CA  TYR A 521      14.050  22.215  35.799  1.00 87.51           C  
ANISOU 4099  CA  TYR A 521    10443  12815   9991     20    -12  -1008       C  
ATOM   4100  C   TYR A 521      14.734  20.898  36.145  1.00 84.39           C  
ANISOU 4100  C   TYR A 521     9854  12331   9879    224    -55  -1202       C  
ATOM   4101  O   TYR A 521      15.854  20.632  35.695  1.00 93.44           O  
ANISOU 4101  O   TYR A 521    10772  13691  11040    258      8  -1393       O  
ATOM   4102  CB  TYR A 521      14.121  23.179  36.985  1.00 80.43           C  
ANISOU 4102  CB  TYR A 521     9683  11801   9076    -66    -78   -736       C  
ATOM   4103  CG  TYR A 521      13.848  24.627  36.644  1.00 79.44           C  
ANISOU 4103  CG  TYR A 521     9704  11775   8705   -273    -40   -559       C  
ATOM   4104  CD1 TYR A 521      14.040  25.110  35.356  1.00 80.16           C  
ANISOU 4104  CD1 TYR A 521     9754  12130   8572   -406     62   -609       C  
ATOM   4105  CD2 TYR A 521      13.389  25.509  37.613  1.00 79.84           C  
ANISOU 4105  CD2 TYR A 521     9937  11651   8747   -337   -111   -342       C  
ATOM   4106  CE1 TYR A 521      13.793  26.435  35.048  1.00 79.85           C  
ANISOU 4106  CE1 TYR A 521     9864  12143   8333   -599     73   -407       C  
ATOM   4107  CE2 TYR A 521      13.136  26.832  37.313  1.00 83.68           C  
ANISOU 4107  CE2 TYR A 521    10560  12175   9059   -511    -98   -187       C  
ATOM   4108  CZ  TYR A 521      13.339  27.290  36.030  1.00 78.43           C  
ANISOU 4108  CZ  TYR A 521     9864  11736   8198   -643    -14   -200       C  
ATOM   4109  OH  TYR A 521      13.089  28.609  35.727  1.00 77.18           O  
ANISOU 4109  OH  TYR A 521     9856  11580   7888   -820    -22     -8       O  
ATOM   4110  N   GLN A 522      14.075  20.054  36.947  1.00 83.34           N  
ANISOU 4110  N   GLN A 522     9800  11879   9987    361   -164  -1153       N  
ATOM   4111  CA  GLN A 522      14.762  18.901  37.520  1.00 86.87           C  
ANISOU 4111  CA  GLN A 522    10094  12176  10738    556   -248  -1257       C  
ATOM   4112  C   GLN A 522      15.120  17.846  36.481  1.00 86.97           C  
ANISOU 4112  C   GLN A 522     9897  12259  10889    691   -202  -1617       C  
ATOM   4113  O   GLN A 522      16.060  17.078  36.704  1.00 92.35           O  
ANISOU 4113  O   GLN A 522    10381  12908  11800    853   -251  -1761       O  
ATOM   4114  CB  GLN A 522      13.921  18.257  38.624  1.00 85.83           C  
ANISOU 4114  CB  GLN A 522    10116  11678  10819    641   -377  -1074       C  
ATOM   4115  CG  GLN A 522      12.809  17.348  38.133  1.00 84.46           C  
ANISOU 4115  CG  GLN A 522     9996  11304  10792    699   -386  -1191       C  
ATOM   4116  CD  GLN A 522      11.996  16.768  39.271  1.00 85.96           C  
ANISOU 4116  CD  GLN A 522    10332  11152  11179    740   -495   -972       C  
ATOM   4117  OE1 GLN A 522      11.463  17.500  40.106  1.00 87.26           O  
ANISOU 4117  OE1 GLN A 522    10661  11282  11210    639   -507   -713       O  
ATOM   4118  NE2 GLN A 522      11.915  15.444  39.325  1.00 84.84           N  
ANISOU 4118  NE2 GLN A 522    10123  10754  11359    883   -573  -1078       N  
ATOM   4119  N   PHE A 523      14.401  17.780  35.363  1.00 87.48           N  
ANISOU 4119  N   PHE A 523     9988  12424  10826    640   -122  -1784       N  
ATOM   4120  CA  PHE A 523      14.767  16.829  34.323  1.00 90.32           C  
ANISOU 4120  CA  PHE A 523    10138  12894  11286    760    -68  -2178       C  
ATOM   4121  C   PHE A 523      15.807  17.400  33.371  1.00 93.51           C  
ANISOU 4121  C   PHE A 523    10347  13750  11432    675     87  -2358       C  
ATOM   4122  O   PHE A 523      16.637  16.644  32.850  1.00 94.35           O  
ANISOU 4122  O   PHE A 523    10199  13985  11665    809    134  -2692       O  
ATOM   4123  CB  PHE A 523      13.520  16.372  33.561  1.00 90.91           C  
ANISOU 4123  CB  PHE A 523    10310  12884  11346    750    -68  -2315       C  
ATOM   4124  CG  PHE A 523      12.584  15.538  34.393  1.00 95.68           C  
ANISOU 4124  CG  PHE A 523    11043  13044  12266    841   -205  -2207       C  
ATOM   4125  CD1 PHE A 523      12.865  14.206  34.653  1.00 90.36           C  
ANISOU 4125  CD1 PHE A 523    10250  12094  11989   1038   -295  -2389       C  
ATOM   4126  CD2 PHE A 523      11.434  16.091  34.930  1.00 89.76           C  
ANISOU 4126  CD2 PHE A 523    10523  12149  11431    725   -245  -1918       C  
ATOM   4127  CE1 PHE A 523      12.009  13.440  35.428  1.00 85.95           C  
ANISOU 4127  CE1 PHE A 523     9816  11120  11723   1089   -418  -2250       C  
ATOM   4128  CE2 PHE A 523      10.575  15.329  35.704  1.00 85.45           C  
ANISOU 4128  CE2 PHE A 523    10079  11228  11159    778   -348  -1806       C  
ATOM   4129  CZ  PHE A 523      10.864  14.002  35.952  1.00 86.52           C  
ANISOU 4129  CZ  PHE A 523    10110  11089  11676    946   -434  -1955       C  
ATOM   4130  N   GLN A 524      15.792  18.716  33.144  1.00 87.87           N  
ANISOU 4130  N   GLN A 524     9738  13277  10374    451    168  -2147       N  
ATOM   4131  CA  GLN A 524      16.928  19.365  32.496  1.00 87.13           C  
ANISOU 4131  CA  GLN A 524     9457  13599  10048    330    314  -2232       C  
ATOM   4132  C   GLN A 524      18.207  19.111  33.280  1.00101.07           C  
ANISOU 4132  C   GLN A 524    11009  15360  12032    437    282  -2269       C  
ATOM   4133  O   GLN A 524      19.222  18.685  32.715  1.00120.61           O  
ANISOU 4133  O   GLN A 524    13195  18090  14542    507    375  -2563       O  
ATOM   4134  CB  GLN A 524      16.680  20.869  32.360  1.00 85.68           C  
ANISOU 4134  CB  GLN A 524     9457  13575   9521     60    368  -1920       C  
ATOM   4135  CG  GLN A 524      15.533  21.248  31.444  1.00 84.59           C  
ANISOU 4135  CG  GLN A 524     9502  13510   9127    -53    394  -1875       C  
ATOM   4136  CD  GLN A 524      15.410  22.744  31.255  1.00 84.00           C  
ANISOU 4136  CD  GLN A 524     9593  13580   8742   -309    432  -1561       C  
ATOM   4137  OE1 GLN A 524      14.453  23.364  31.717  1.00 82.21           O  
ANISOU 4137  OE1 GLN A 524     9608  13127   8499   -359    336  -1303       O  
ATOM   4138  NE2 GLN A 524      16.384  23.335  30.574  1.00 85.28           N  
ANISOU 4138  NE2 GLN A 524     9616  14116   8671   -476    573  -1583       N  
ATOM   4139  N   PHE A 525      18.175  19.380  34.589  1.00 94.91           N  
ANISOU 4139  N   PHE A 525    10354  14314  11392    453    146  -1984       N  
ATOM   4140  CA  PHE A 525      19.284  19.029  35.470  1.00 94.32           C  
ANISOU 4140  CA  PHE A 525    10091  14192  11553    584     61  -1998       C  
ATOM   4141  C   PHE A 525      19.684  17.570  35.292  1.00101.11           C  
ANISOU 4141  C   PHE A 525    10727  14941  12750    865      9  -2323       C  
ATOM   4142  O   PHE A 525      20.823  17.259  34.925  1.00107.56           O  
ANISOU 4142  O   PHE A 525    11236  15986  13645    952     68  -2580       O  
ATOM   4143  CB  PHE A 525      18.900  19.281  36.931  1.00 89.10           C  
ANISOU 4143  CB  PHE A 525     9639  13217  10999    593   -109  -1658       C  
ATOM   4144  CG  PHE A 525      18.806  20.732  37.310  1.00 86.52           C  
ANISOU 4144  CG  PHE A 525     9480  12987  10408    348    -83  -1378       C  
ATOM   4145  CD1 PHE A 525      19.343  21.722  36.506  1.00 86.93           C  
ANISOU 4145  CD1 PHE A 525     9456  13376  10196    134     65  -1400       C  
ATOM   4146  CD2 PHE A 525      18.190  21.098  38.496  1.00 83.61           C  
ANISOU 4146  CD2 PHE A 525     9340  12366  10062    325   -208  -1096       C  
ATOM   4147  CE1 PHE A 525      19.255  23.054  36.876  1.00 84.92           C  
ANISOU 4147  CE1 PHE A 525     9364  13155   9748    -92     70  -1143       C  
ATOM   4148  CE2 PHE A 525      18.100  22.422  38.869  1.00 81.84           C  
ANISOU 4148  CE2 PHE A 525     9264  12202   9630    116   -195   -881       C  
ATOM   4149  CZ  PHE A 525      18.633  23.402  38.059  1.00 81.81           C  
ANISOU 4149  CZ  PHE A 525     9193  12483   9406    -89    -66   -902       C  
ATOM   4150  N   GLN A 526      18.738  16.661  35.551  1.00 97.18           N  
ANISOU 4150  N   GLN A 526    10369  14078  12476   1006   -103  -2323       N  
ATOM   4151  CA  GLN A 526      19.030  15.230  35.553  1.00 99.48           C  
ANISOU 4151  CA  GLN A 526    10486  14151  13162   1284   -197  -2593       C  
ATOM   4152  C   GLN A 526      19.660  14.774  34.244  1.00103.77           C  
ANISOU 4152  C   GLN A 526    10741  15000  13688   1358    -48  -3061       C  
ATOM   4153  O   GLN A 526      20.622  13.998  34.246  1.00 99.67           O  
ANISOU 4153  O   GLN A 526     9942  14484  13444   1572    -85  -3323       O  
ATOM   4154  CB  GLN A 526      17.748  14.441  35.826  1.00 96.79           C  
ANISOU 4154  CB  GLN A 526    10365  13391  13021   1354   -308  -2519       C  
ATOM   4155  CG  GLN A 526      17.944  12.935  35.925  1.00103.53           C  
ANISOU 4155  CG  GLN A 526    11076  13921  14338   1632   -438  -2754       C  
ATOM   4156  CD  GLN A 526      18.616  12.504  37.216  1.00127.63           C  
ANISOU 4156  CD  GLN A 526    14089  16717  17689   1795   -634  -2540       C  
ATOM   4157  OE1 GLN A 526      19.037  13.331  38.025  1.00124.04           O  
ANISOU 4157  OE1 GLN A 526    13682  16373  17074   1702   -665  -2255       O  
ATOM   4158  NE2 GLN A 526      18.724  11.194  37.411  1.00128.71           N  
ANISOU 4158  NE2 GLN A 526    14136  16500  18268   2040   -783  -2680       N  
ATOM   4159  N   GLU A 527      19.133  15.249  33.114  1.00114.16           N  
ANISOU 4159  N   GLU A 527    12111  16591  14675   1188    115  -3180       N  
ATOM   4160  CA  GLU A 527      19.659  14.823  31.821  1.00113.86           C  
ANISOU 4160  CA  GLU A 527    11806  16896  14560   1239    274  -3644       C  
ATOM   4161  C   GLU A 527      21.085  15.320  31.618  1.00117.07           C  
ANISOU 4161  C   GLU A 527    11915  17720  14848   1197    404  -3756       C  
ATOM   4162  O   GLU A 527      21.957  14.565  31.172  1.00128.14           O  
ANISOU 4162  O   GLU A 527    12991  19267  16429   1381    456  -4157       O  
ATOM   4163  CB  GLU A 527      18.749  15.318  30.698  1.00104.40           C  
ANISOU 4163  CB  GLU A 527    10755  15939  12974   1040    404  -3691       C  
ATOM   4164  CG  GLU A 527      19.086  14.746  29.333  1.00115.87           C  
ANISOU 4164  CG  GLU A 527    11961  17743  14322   1096    558  -4202       C  
ATOM   4165  CD  GLU A 527      18.241  15.346  28.230  1.00134.77           C  
ANISOU 4165  CD  GLU A 527    14505  20435  16268    876    673  -4204       C  
ATOM   4166  OE1 GLU A 527      18.439  16.537  27.909  1.00140.77           O  
ANISOU 4166  OE1 GLU A 527    15324  21539  16624    625    792  -3970       O  
ATOM   4167  OE2 GLU A 527      17.377  14.628  27.687  1.00136.26           O1-
ANISOU 4167  OE2 GLU A 527    14753  20505  16515    949    628  -4432       O1-
ATOM   4168  N   ALA A 528      21.343  16.588  31.947  1.00 96.51           N  
ANISOU 4168  N   ALA A 528     9401  15305  11963    954    457  -3421       N  
ATOM   4169  CA  ALA A 528      22.683  17.141  31.776  1.00 96.98           C  
ANISOU 4169  CA  ALA A 528     9172  15770  11906    868    587  -3502       C  
ATOM   4170  C   ALA A 528      23.705  16.394  32.626  1.00110.73           C  
ANISOU 4170  C   ALA A 528    10650  17360  14060   1130    451  -3620       C  
ATOM   4171  O   ALA A 528      24.808  16.089  32.158  1.00100.49           O  
ANISOU 4171  O   ALA A 528     8982  16369  12830   1220    554  -3952       O  
ATOM   4172  CB  ALA A 528      22.683  18.629  32.120  1.00 97.91           C  
ANISOU 4172  CB  ALA A 528     9470  16022  11709    552    628  -3087       C  
ATOM   4173  N   LEU A 529      23.349  16.080  33.874  1.00117.93           N  
ANISOU 4173  N   LEU A 529    11741  17819  15250   1260    214  -3352       N  
ATOM   4174  CA  LEU A 529      24.293  15.424  34.775  1.00116.62           C  
ANISOU 4174  CA  LEU A 529    11353  17494  15465   1509     42  -3396       C  
ATOM   4175  C   LEU A 529      24.548  13.981  34.357  1.00119.44           C  
ANISOU 4175  C   LEU A 529    11472  17702  16208   1843    -10  -3822       C  
ATOM   4176  O   LEU A 529      25.691  13.509  34.402  1.00115.63           O  
ANISOU 4176  O   LEU A 529    10634  17337  15964   2038    -37  -4073       O  
ATOM   4177  CB  LEU A 529      23.767  15.478  36.208  1.00100.50           C  
ANISOU 4177  CB  LEU A 529     9593  15030  13565   1538   -199  -2967       C  
ATOM   4178  CG  LEU A 529      23.586  16.875  36.799  1.00 99.63           C  
ANISOU 4178  CG  LEU A 529     9701  15023  13131   1244   -181  -2575       C  
ATOM   4179  CD1 LEU A 529      23.352  16.786  38.298  1.00102.34           C  
ANISOU 4179  CD1 LEU A 529    10233  15013  13638   1319   -426  -2228       C  
ATOM   4180  CD2 LEU A 529      24.786  17.752  36.481  1.00101.98           C  
ANISOU 4180  CD2 LEU A 529     9732  15773  13241   1079    -44  -2653       C  
ATOM   4181  N   CYS A 530      23.494  13.265  33.955  1.00118.84           N  
ANISOU 4181  N   CYS A 530    11574  17356  16224   1917    -34  -3925       N  
ATOM   4182  CA  CYS A 530      23.639  11.888  33.501  1.00116.48           C  
ANISOU 4182  CA  CYS A 530    11071  16871  16316   2224    -89  -4360       C  
ATOM   4183  C   CYS A 530      24.402  11.782  32.188  1.00128.84           C  
ANISOU 4183  C   CYS A 530    12278  18925  17751   2248    147  -4886       C  
ATOM   4184  O   CYS A 530      25.018  10.743  31.929  1.00135.38           O  
ANISOU 4184  O   CYS A 530    12810  19686  18942   2542    106  -5306       O  
ATOM   4185  CB  CYS A 530      22.262  11.240  33.365  1.00110.92           C  
ANISOU 4185  CB  CYS A 530    10654  15771  15720   2246   -166  -4338       C  
ATOM   4186  SG  CYS A 530      21.431  11.018  34.946  1.00109.45           S  
ANISOU 4186  SG  CYS A 530    10823  14980  15781   2276   -448  -3788       S  
ATOM   4187  N   GLN A 531      24.365  12.823  31.356  1.00145.10           N  
ANISOU 4187  N   GLN A 531    14356  21472  19303   1946    390  -4874       N  
ATOM   4188  CA  GLN A 531      25.235  12.863  30.187  1.00155.52           C  
ANISOU 4188  CA  GLN A 531    15312  23348  20432   1924    641  -5329       C  
ATOM   4189  C   GLN A 531      26.701  12.876  30.599  1.00158.78           C  
ANISOU 4189  C   GLN A 531    15335  23964  21032   2045    642  -5444       C  
ATOM   4190  O   GLN A 531      27.530  12.185  29.994  1.00165.17           O  
ANISOU 4190  O   GLN A 531    15750  24995  22013   2249    732  -5944       O  
ATOM   4191  CB  GLN A 531      24.911  14.090  29.335  1.00157.22           C  
ANISOU 4191  CB  GLN A 531    15658  24036  20040   1536    881  -5180       C  
ATOM   4192  CG  GLN A 531      25.863  14.297  28.171  1.00169.74           C  
ANISOU 4192  CG  GLN A 531    16874  26275  21346   1444   1170  -5577       C  
ATOM   4193  CD  GLN A 531      26.937  15.329  28.465  1.00191.77           C  
ANISOU 4193  CD  GLN A 531    19483  29424  23955   1235   1279  -5371       C  
ATOM   4194  OE1 GLN A 531      26.929  15.976  29.514  1.00192.62           O  
ANISOU 4194  OE1 GLN A 531    19769  29301  24118   1142   1135  -4928       O  
ATOM   4195  NE2 GLN A 531      27.875  15.481  27.538  1.00179.94           N  
ANISOU 4195  NE2 GLN A 531    17616  28513  22239   1150   1541  -5711       N  
ATOM   4196  N   ALA A 532      27.040  13.668  31.621  1.00131.78           N  
ANISOU 4196  N   ALA A 532    12000  20487  17582   1923    540  -5012       N  
ATOM   4197  CA  ALA A 532      28.408  13.686  32.129  1.00126.10           C  
ANISOU 4197  CA  ALA A 532    10910  19939  17064   2038    500  -5094       C  
ATOM   4198  C   ALA A 532      28.808  12.325  32.682  1.00129.45           C  
ANISOU 4198  C   ALA A 532    11135  19969  18081   2482    258  -5331       C  
ATOM   4199  O   ALA A 532      29.940  11.871  32.478  1.00128.34           O  
ANISOU 4199  O   ALA A 532    10551  20045  18166   2688    287  -5702       O  
ATOM   4200  CB  ALA A 532      28.558  14.767  33.200  1.00113.41           C  
ANISOU 4200  CB  ALA A 532     9476  18292  15321   1820    397  -4576       C  
ATOM   4201  N   ALA A 533      27.890  11.654  33.384  1.00115.27           N  
ANISOU 4201  N   ALA A 533     9650  17588  16558   2634     14  -5116       N  
ATOM   4202  CA  ALA A 533      28.130  10.286  33.824  1.00123.22           C  
ANISOU 4202  CA  ALA A 533    10513  18154  18151   3050   -231  -5321       C  
ATOM   4203  C   ALA A 533      28.196   9.300  32.664  1.00126.98           C  
ANISOU 4203  C   ALA A 533    10739  18694  18813   3265   -111  -5943       C  
ATOM   4204  O   ALA A 533      28.492   8.122  32.895  1.00124.95           O  
ANISOU 4204  O   ALA A 533    10314  18075  19088   3634   -305  -6191       O  
ATOM   4205  CB  ALA A 533      27.042   9.851  34.809  1.00112.47           C  
ANISOU 4205  CB  ALA A 533     9573  16165  16997   3103   -497  -4903       C  
ATOM   4206  N   LYS A 534      27.931   9.754  31.436  1.00143.36           N  
ANISOU 4206  N   LYS A 534    12789  21215  20465   3045    189  -6199       N  
ATOM   4207  CA  LYS A 534      27.962   8.907  30.244  1.00145.31           C  
ANISOU 4207  CA  LYS A 534    12800  21606  20804   3212    333  -6832       C  
ATOM   4208  C   LYS A 534      27.027   7.712  30.396  1.00148.14           C  
ANISOU 4208  C   LYS A 534    13364  21331  21591   3450    115  -6929       C  
ATOM   4209  O   LYS A 534      27.362   6.586  30.020  1.00151.63           O  
ANISOU 4209  O   LYS A 534    13548  21608  22455   3775     58  -7433       O  
ATOM   4210  CB  LYS A 534      29.386   8.446  29.922  1.00140.00           C  
ANISOU 4210  CB  LYS A 534    11569  21244  20380   3471    405  -7338       C  
ATOM   4211  CG  LYS A 534      30.372   9.579  29.703  1.00140.78           C  
ANISOU 4211  CG  LYS A 534    11413  22003  20075   3217    642  -7285       C  
ATOM   4212  CD  LYS A 534      31.799   9.057  29.660  1.00163.35           C  
ANISOU 4212  CD  LYS A 534    13735  25072  23260   3491    644  -7703       C  
ATOM   4213  CE  LYS A 534      32.807  10.192  29.594  1.00169.98           C  
ANISOU 4213  CE  LYS A 534    14315  26528  23741   3216    853  -7598       C  
ATOM   4214  NZ  LYS A 534      32.665  10.996  28.352  1.00182.04           N  
ANISOU 4214  NZ  LYS A 534    15861  28666  24640   2826   1228  -7706       N  
ATOM   4215  N   HIS A 535      25.850   7.954  30.967  1.00137.72           N  
ANISOU 4215  N   HIS A 535    12499  19642  20186   3283     -9  -6452       N  
ATOM   4216  CA  HIS A 535      24.872   6.886  31.101  1.00137.86           C  
ANISOU 4216  CA  HIS A 535    12728  19068  20584   3446   -200  -6505       C  
ATOM   4217  C   HIS A 535      24.447   6.395  29.725  1.00140.55           C  
ANISOU 4217  C   HIS A 535    12976  19600  20826   3455    -23  -7075       C  
ATOM   4218  O   HIS A 535      24.196   7.187  28.813  1.00144.25           O  
ANISOU 4218  O   HIS A 535    13476  20582  20750   3184    229  -7153       O  
ATOM   4219  CB  HIS A 535      23.644   7.354  31.880  1.00129.80           C  
ANISOU 4219  CB  HIS A 535    12190  17713  19415   3217   -316  -5902       C  
ATOM   4220  CG  HIS A 535      22.633   6.272  32.101  1.00138.12           C  
ANISOU 4220  CG  HIS A 535    13456  18149  20873   3349   -513  -5909       C  
ATOM   4221  ND1 HIS A 535      21.485   6.161  31.347  1.00143.00           N  
ANISOU 4221  ND1 HIS A 535    14269  18737  21326   3201   -429  -6039       N  
ATOM   4222  CD2 HIS A 535      22.602   5.247  32.987  1.00146.66           C  
ANISOU 4222  CD2 HIS A 535    14581  18618  22526   3602   -796  -5791       C  
ATOM   4223  CE1 HIS A 535      20.790   5.115  31.756  1.00144.20           C  
ANISOU 4223  CE1 HIS A 535    14564  18283  21942   3344   -641  -6019       C  
ATOM   4224  NE2 HIS A 535      21.444   4.544  32.752  1.00152.38           N  
ANISOU 4224  NE2 HIS A 535    15522  18946  23429   3583   -864  -5853       N  
ATOM   4225  N   GLU A 536      24.377   5.078  29.579  1.00141.07           N  
ANISOU 4225  N   GLU A 536    12928  19247  21424   3768   -170  -7474       N  
ATOM   4226  CA  GLU A 536      23.959   4.443  28.337  1.00150.09           C  
ANISOU 4226  CA  GLU A 536    13973  20503  22550   3816    -43  -8077       C  
ATOM   4227  C   GLU A 536      22.588   3.825  28.573  1.00143.27           C  
ANISOU 4227  C   GLU A 536    13471  19051  21915   3784   -228  -7917       C  
ATOM   4228  O   GLU A 536      22.458   2.862  29.336  1.00155.32           O  
ANISOU 4228  O   GLU A 536    15054  19926  24035   4017   -496  -7840       O  
ATOM   4229  CB  GLU A 536      24.974   3.395  27.887  1.00147.14           C  
ANISOU 4229  CB  GLU A 536    13270  20098  22537   4061    -98  -8556       C  
ATOM   4230  CG  GLU A 536      26.220   3.987  27.246  1.00149.96           C  
ANISOU 4230  CG  GLU A 536    13284  21156  22539   3984    140  -8784       C  
ATOM   4231  CD  GLU A 536      25.932   4.692  25.935  1.00161.40           C  
ANISOU 4231  CD  GLU A 536    14727  23274  23325   3674    456  -9006       C  
ATOM   4232  OE1 GLU A 536      25.287   4.086  25.052  1.00147.92           O  
ANISOU 4232  OE1 GLU A 536    13092  21532  21577   3633    466  -9318       O  
ATOM   4233  OE2 GLU A 536      26.356   5.858  25.787  1.00175.91           O1-
ANISOU 4233  OE2 GLU A 536    16486  25675  24678   3456    682  -8844       O1-
ATOM   4234  N   GLY A 537      21.568   4.389  27.934  1.00113.65           N  
ANISOU 4234  N   GLY A 537     9957  15526  17696   3487    -93  -7846       N  
ATOM   4235  CA  GLY A 537      20.225   3.881  28.050  1.00130.11           C  
ANISOU 4235  CA  GLY A 537    12356  17132  19949   3419   -239  -7725       C  
ATOM   4236  C   GLY A 537      19.209   4.966  28.320  1.00135.71           C  
ANISOU 4236  C   GLY A 537    13434  17951  20178   3060   -195  -7157       C  
ATOM   4237  O   GLY A 537      19.479   6.163  28.171  1.00135.53           O  
ANISOU 4237  O   GLY A 537    13433  18431  19629   2841    -23  -6924       O  
ATOM   4238  N   PRO A 538      18.004   4.568  28.712  1.00124.64           N  
ANISOU 4238  N   PRO A 538    12320  16071  18967   2991   -351  -6933       N  
ATOM   4239  CA  PRO A 538      16.979   5.560  29.052  1.00106.50           C  
ANISOU 4239  CA  PRO A 538    10362  13837  16266   2677   -327  -6398       C  
ATOM   4240  C   PRO A 538      17.362   6.344  30.300  1.00112.58           C  
ANISOU 4240  C   PRO A 538    11258  14547  16971   2612   -385  -5790       C  
ATOM   4241  O   PRO A 538      17.947   5.808  31.238  1.00116.28           O  
ANISOU 4241  O   PRO A 538    11670  14657  17855   2809   -550  -5647       O  
ATOM   4242  CB  PRO A 538      15.730   4.698  29.297  1.00109.96           C  
ANISOU 4242  CB  PRO A 538    11011  13707  17061   2671   -504  -6356       C  
ATOM   4243  CG  PRO A 538      16.014   3.418  28.565  1.00115.41           C  
ANISOU 4243  CG  PRO A 538    11461  14213  18178   2920   -552  -7015       C  
ATOM   4244  CD  PRO A 538      17.473   3.203  28.823  1.00123.02           C  
ANISOU 4244  CD  PRO A 538    12136  15244  19362   3180   -553  -7173       C  
ATOM   4245  N   LEU A 539      17.013   7.628  30.301  1.00115.28           N  
ANISOU 4245  N   LEU A 539    11774  15240  16789   2336   -263  -5435       N  
ATOM   4246  CA  LEU A 539      17.212   8.470  31.465  1.00112.05           C  
ANISOU 4246  CA  LEU A 539    11516  14783  16274   2238   -315  -4869       C  
ATOM   4247  C   LEU A 539      16.498   7.960  32.716  1.00117.46           C  
ANISOU 4247  C   LEU A 539    12437  14872  17318   2275   -536  -4466       C  
ATOM   4248  O   LEU A 539      16.798   8.429  33.823  1.00116.81           O  
ANISOU 4248  O   LEU A 539    12450  14701  17231   2251   -616  -4037       O  
ATOM   4249  CB  LEU A 539      16.779   9.899  31.142  1.00 98.08           C  
ANISOU 4249  CB  LEU A 539     9915  13440  13912   1930   -157  -4598       C  
ATOM   4250  CG  LEU A 539      17.543  11.004  31.853  1.00101.24           C  
ANISOU 4250  CG  LEU A 539    10324  14060  14082   1824   -117  -4227       C  
ATOM   4251  CD1 LEU A 539      18.950  11.097  31.282  1.00112.16           C  
ANISOU 4251  CD1 LEU A 539    11362  15859  15394   1906     17  -4550       C  
ATOM   4252  CD2 LEU A 539      16.813  12.354  31.730  1.00108.87           C  
ANISOU 4252  CD2 LEU A 539    11536  15273  14556   1519    -20  -3883       C  
ATOM   4253  N   HIS A 540      15.573   7.016  32.560  1.00138.42           N  
ANISOU 4253  N   HIS A 540    15183  17140  20272   2318   -634  -4601       N  
ATOM   4254  CA  HIS A 540      14.794   6.492  33.682  1.00137.67           C  
ANISOU 4254  CA  HIS A 540    15313  16490  20503   2314   -825  -4211       C  
ATOM   4255  C   HIS A 540      15.665   5.793  34.731  1.00119.27           C  
ANISOU 4255  C   HIS A 540    12904  13797  18617   2546  -1016  -4052       C  
ATOM   4256  O   HIS A 540      15.387   5.870  35.935  1.00124.93           O  
ANISOU 4256  O   HIS A 540    13812  14240  19414   2497  -1143  -3561       O  
ATOM   4257  CB  HIS A 540      13.711   5.533  33.132  1.00132.40           C  
ANISOU 4257  CB  HIS A 540    14707  15497  20102   2306   -882  -4468       C  
ATOM   4258  CG  HIS A 540      13.276   4.454  34.088  1.00152.01           C  
ANISOU 4258  CG  HIS A 540    17304  17324  23130   2395  -1101  -4252       C  
ATOM   4259  ND1 HIS A 540      12.593   4.705  35.261  1.00165.17           N  
ANISOU 4259  ND1 HIS A 540    19222  18744  24791   2251  -1183  -3685       N  
ATOM   4260  CD2 HIS A 540      13.422   3.108  34.026  1.00138.62           C  
ANISOU 4260  CD2 HIS A 540    15502  15161  22005   2604  -1254  -4527       C  
ATOM   4261  CE1 HIS A 540      12.339   3.561  35.874  1.00154.95           C  
ANISOU 4261  CE1 HIS A 540    17978  16877  24019   2348  -1371  -3589       C  
ATOM   4262  NE2 HIS A 540      12.832   2.579  35.147  1.00147.83           N  
ANISOU 4262  NE2 HIS A 540    16869  15804  23496   2566  -1429  -4086       N  
ATOM   4263  N   LYS A 541      16.709   5.096  34.294  1.00104.76           N  
ANISOU 4263  N   LYS A 541    10775  11961  17067   2807  -1045  -4468       N  
ATOM   4264  CA  LYS A 541      17.557   4.332  35.193  1.00117.88           C  
ANISOU 4264  CA  LYS A 541    12332  13257  19202   3069  -1260  -4360       C  
ATOM   4265  C   LYS A 541      18.967   4.894  35.295  1.00127.57           C  
ANISOU 4265  C   LYS A 541    13306  14871  20293   3185  -1212  -4416       C  
ATOM   4266  O   LYS A 541      19.934   4.124  35.278  1.00128.95           O  
ANISOU 4266  O   LYS A 541    13215  14916  20862   3479  -1320  -4692       O  
ATOM   4267  CB  LYS A 541      17.626   2.866  34.747  1.00120.74           C  
ANISOU 4267  CB  LYS A 541    12539  13177  20158   3334  -1394  -4804       C  
ATOM   4268  CG  LYS A 541      17.819   2.704  33.242  1.00119.23           C  
ANISOU 4268  CG  LYS A 541    12105  13328  19868   3389  -1211  -5493       C  
ATOM   4269  CD  LYS A 541      17.584   1.273  32.787  1.00117.25           C  
ANISOU 4269  CD  LYS A 541    11758  12591  20202   3604  -1347  -5944       C  
ATOM   4270  CE  LYS A 541      16.261   0.726  33.290  1.00131.21           C  
ANISOU 4270  CE  LYS A 541    13832  13809  22213   3462  -1491  -5642       C  
ATOM   4271  NZ  LYS A 541      16.071  -0.693  32.896  1.00126.63           N  
ANISOU 4271  NZ  LYS A 541    13158  12696  22260   3664  -1646  -6074       N  
ATOM   4272  N   CYS A 542      19.120   6.211  35.407  1.00126.99           N  
ANISOU 4272  N   CYS A 542    13294  15257  19700   2963  -1063  -4169       N  
ATOM   4273  CA  CYS A 542      20.455   6.785  35.556  1.00113.57           C  
ANISOU 4273  CA  CYS A 542    11347  13927  17877   3038  -1020  -4200       C  
ATOM   4274  C   CYS A 542      20.810   6.986  37.023  1.00125.67           C  
ANISOU 4274  C   CYS A 542    12986  15260  19503   3068  -1223  -3683       C  
ATOM   4275  O   CYS A 542      19.960   7.354  37.841  1.00119.15           O  
ANISOU 4275  O   CYS A 542    12474  14257  18541   2891  -1284  -3221       O  
ATOM   4276  CB  CYS A 542      20.575   8.122  34.827  1.00121.37           C  
ANISOU 4276  CB  CYS A 542    12312  15537  18268   2772   -751  -4239       C  
ATOM   4277  SG  CYS A 542      21.919   9.128  35.490  1.00116.26           S  
ANISOU 4277  SG  CYS A 542    11488  15269  17416   2739   -733  -4022       S  
ATOM   4278  N   ASP A 543      22.080   6.752  37.339  1.00147.99           N  
ANISOU 4278  N   ASP A 543    15532  18149  22548   3294  -1325  -3783       N  
ATOM   4279  CA  ASP A 543      22.650   7.020  38.653  1.00129.07           C  
ANISOU 4279  CA  ASP A 543    13173  15671  20195   3336  -1521  -3346       C  
ATOM   4280  C   ASP A 543      23.885   7.890  38.456  1.00124.07           C  
ANISOU 4280  C   ASP A 543    12248  15576  19316   3314  -1404  -3483       C  
ATOM   4281  O   ASP A 543      24.796   7.514  37.710  1.00132.29           O  
ANISOU 4281  O   ASP A 543    12926  16813  20525   3504  -1340  -3944       O  
ATOM   4282  CB  ASP A 543      23.013   5.712  39.366  1.00121.57           C  
ANISOU 4282  CB  ASP A 543    12151  14190  19849   3670  -1835  -3297       C  
ATOM   4283  CG  ASP A 543      23.335   5.912  40.838  1.00130.47           C  
ANISOU 4283  CG  ASP A 543    13398  15182  20991   3686  -2076  -2758       C  
ATOM   4284  OD1 ASP A 543      23.144   7.037  41.349  1.00132.87           O  
ANISOU 4284  OD1 ASP A 543    13872  15768  20846   3426  -1996  -2430       O  
ATOM   4285  OD2 ASP A 543      23.788   4.942  41.486  1.00130.94           O1-
ANISOU 4285  OD2 ASP A 543    13383  14853  21516   3964  -2359  -2666       O1-
ATOM   4286  N   ILE A 544      23.920   9.051  39.112  1.00104.16           N  
ANISOU 4286  N   ILE A 544     9867  13300  16408   3076  -1371  -3107       N  
ATOM   4287  CA  ILE A 544      25.062   9.946  38.954  1.00114.53           C  
ANISOU 4287  CA  ILE A 544    10911  15118  17486   3008  -1258  -3211       C  
ATOM   4288  C   ILE A 544      26.133   9.588  39.978  1.00121.19           C  
ANISOU 4288  C   ILE A 544    11558  15863  18627   3242  -1524  -3082       C  
ATOM   4289  O   ILE A 544      27.116  10.319  40.145  1.00114.95           O  
ANISOU 4289  O   ILE A 544    10548  15447  17680   3187  -1493  -3092       O  
ATOM   4290  CB  ILE A 544      24.660  11.428  39.080  1.00103.97           C  
ANISOU 4290  CB  ILE A 544     9795  14102  15608   2630  -1095  -2917       C  
ATOM   4291  CG1 ILE A 544      24.130  11.733  40.481  1.00113.39           C  
ANISOU 4291  CG1 ILE A 544    11305  15035  16743   2544  -1291  -2385       C  
ATOM   4292  CG2 ILE A 544      23.622  11.790  38.031  1.00106.64           C  
ANISOU 4292  CG2 ILE A 544    10313  14549  15656   2416   -858  -3036       C  
ATOM   4293  CD1 ILE A 544      23.862  13.204  40.719  1.00106.62           C  
ANISOU 4293  CD1 ILE A 544    10634  14468  15407   2207  -1161  -2125       C  
ATOM   4294  N   SER A 545      25.951   8.461  40.662  1.00118.05           N  
ANISOU 4294  N   SER A 545    11231  14958  18666   3498  -1800  -2950       N  
ATOM   4295  CA  SER A 545      26.908   8.025  41.670  1.00112.40           C  
ANISOU 4295  CA  SER A 545    10347  14106  18256   3748  -2101  -2790       C  
ATOM   4296  C   SER A 545      28.255   7.698  41.032  1.00125.13           C  
ANISOU 4296  C   SER A 545    11451  15974  20118   4004  -2081  -3277       C  
ATOM   4297  O   SER A 545      28.334   7.287  39.871  1.00130.89           O  
ANISOU 4297  O   SER A 545    11976  16796  20958   4095  -1900  -3767       O  
ATOM   4298  CB  SER A 545      26.368   6.804  42.418  1.00119.69           C  
ANISOU 4298  CB  SER A 545    11463  14396  19617   3966  -2400  -2542       C  
ATOM   4299  OG  SER A 545      25.168   7.115  43.106  1.00116.05           O  
ANISOU 4299  OG  SER A 545    11442  13737  18914   3718  -2414  -2076       O  
ATOM   4300  N   ASN A 546      29.323   7.884  41.811  1.00132.38           N  
ANISOU 4300  N   ASN A 546    12150  17031  21117   4123  -2272  -3155       N  
ATOM   4301  CA  ASN A 546      30.698   7.685  41.342  1.00134.96           C  
ANISOU 4301  CA  ASN A 546    11951  17656  21672   4359  -2264  -3592       C  
ATOM   4302  C   ASN A 546      30.945   8.448  40.032  1.00141.56           C  
ANISOU 4302  C   ASN A 546    12571  19051  22165   4143  -1857  -4019       C  
ATOM   4303  O   ASN A 546      31.377   7.883  39.025  1.00157.22           O  
ANISOU 4303  O   ASN A 546    14230  21155  24352   4325  -1722  -4545       O  
ATOM   4304  CB  ASN A 546      31.025   6.186  41.185  1.00135.35           C  
ANISOU 4304  CB  ASN A 546    11782  17275  22368   4816  -2483  -3884       C  
ATOM   4305  CG  ASN A 546      31.195   5.449  42.537  1.00152.63           C  
ANISOU 4305  CG  ASN A 546    14072  18983  24938   5074  -2936  -3457       C  
ATOM   4306  OD1 ASN A 546      30.799   5.954  43.587  1.00150.04           O  
ANISOU 4306  OD1 ASN A 546    14056  18592  24358   4888  -3071  -2920       O  
ATOM   4307  ND2 ASN A 546      31.798   4.240  42.495  1.00167.00           N  
ANISOU 4307  ND2 ASN A 546    15618  20466  27367   5510  -3176  -3708       N  
ATOM   4308  N   SER A 547      30.660   9.768  40.046  1.00131.84           N  
ANISOU 4308  N   SER A 547    11524  18172  20399   3742  -1658  -3788       N  
ATOM   4309  CA  SER A 547      30.748  10.574  38.813  1.00133.50           C  
ANISOU 4309  CA  SER A 547    11601  18895  20228   3479  -1271  -4099       C  
ATOM   4310  C   SER A 547      31.049  12.034  39.177  1.00136.70           C  
ANISOU 4310  C   SER A 547    12057  19699  20183   3115  -1166  -3820       C  
ATOM   4311  O   SER A 547      30.173  12.905  39.171  1.00133.34           O  
ANISOU 4311  O   SER A 547    11988  19306  19370   2791  -1040  -3545       O  
ATOM   4312  CB  SER A 547      29.472  10.474  37.977  1.00125.93           C  
ANISOU 4312  CB  SER A 547    10952  17808  19088   3333  -1078  -4163       C  
ATOM   4313  OG  SER A 547      29.508  11.371  36.879  1.00128.09           O  
ANISOU 4313  OG  SER A 547    11146  18594  18927   3042   -728  -4369       O  
ATOM   4314  N   THR A 548      32.329  12.307  39.454  1.00135.76           N  
ANISOU 4314  N   THR A 548    11552  19890  20142   3172  -1220  -3924       N  
ATOM   4315  CA  THR A 548      32.740  13.651  39.855  1.00130.81           C  
ANISOU 4315  CA  THR A 548    10931  19621  19149   2834  -1150  -3687       C  
ATOM   4316  C   THR A 548      32.503  14.679  38.755  1.00135.16           C  
ANISOU 4316  C   THR A 548    11518  20587  19249   2450   -764  -3796       C  
ATOM   4317  O   THR A 548      32.361  15.873  39.044  1.00134.73           O  
ANISOU 4317  O   THR A 548    11646  20699  18848   2105   -694  -3512       O  
ATOM   4318  CB  THR A 548      34.214  13.655  40.260  1.00128.58           C  
ANISOU 4318  CB  THR A 548    10165  19614  19075   2979  -1279  -3838       C  
ATOM   4319  OG1 THR A 548      35.019  13.243  39.148  1.00134.73           O  
ANISOU 4319  OG1 THR A 548    10470  20725  19995   3113  -1070  -4374       O  
ATOM   4320  CG2 THR A 548      34.450  12.712  41.427  1.00134.12           C  
ANISOU 4320  CG2 THR A 548    10857  19906  20198   3351  -1703  -3662       C  
ATOM   4321  N   GLU A 549      32.474  14.246  37.492  1.00136.87           N  
ANISOU 4321  N   GLU A 549    11560  20981  19462   2501   -522  -4205       N  
ATOM   4322  CA  GLU A 549      32.211  15.180  36.401  1.00128.29           C  
ANISOU 4322  CA  GLU A 549    10525  20301  17919   2133   -166  -4280       C  
ATOM   4323  C   GLU A 549      30.796  15.736  36.487  1.00108.88           C  
ANISOU 4323  C   GLU A 549     8614  17593  15161   1891   -141  -3909       C  
ATOM   4324  O   GLU A 549      30.580  16.935  36.274  1.00107.42           O  
ANISOU 4324  O   GLU A 549     8589  17641  14583   1522     21  -3700       O  
ATOM   4325  CB  GLU A 549      32.442  14.497  35.053  1.00123.22           C  
ANISOU 4325  CB  GLU A 549     9583  19914  17320   2261     73  -4817       C  
ATOM   4326  CG  GLU A 549      33.799  13.820  34.920  1.00153.99           C  
ANISOU 4326  CG  GLU A 549    12902  24043  21565   2554     52  -5253       C  
ATOM   4327  CD  GLU A 549      33.824  12.423  35.513  1.00155.01           C  
ANISOU 4327  CD  GLU A 549    12963  23670  22262   3041   -265  -5381       C  
ATOM   4328  OE1 GLU A 549      33.111  11.537  34.996  1.00165.84           O  
ANISOU 4328  OE1 GLU A 549    14456  24767  23790   3224   -260  -5590       O  
ATOM   4329  OE2 GLU A 549      34.558  12.212  36.502  1.00138.60           O1-
ANISOU 4329  OE2 GLU A 549    10714  21465  20483   3237   -534  -5264       O1-
ATOM   4330  N   ALA A 550      29.822  14.879  36.795  1.00103.84           N  
ANISOU 4330  N   ALA A 550     8256  16474  14726   2093   -306  -3824       N  
ATOM   4331  CA  ALA A 550      28.468  15.357  37.043  1.00101.67           C  
ANISOU 4331  CA  ALA A 550     8479  15939  14213   1892   -316  -3460       C  
ATOM   4332  C   ALA A 550      28.439  16.292  38.245  1.00102.87           C  
ANISOU 4332  C   ALA A 550     8844  16016  14226   1710   -462  -3010       C  
ATOM   4333  O   ALA A 550      27.802  17.351  38.208  1.00102.13           O  
ANISOU 4333  O   ALA A 550     9028  15991  13786   1401   -357  -2763       O  
ATOM   4334  CB  ALA A 550      27.526  14.172  37.255  1.00104.85           C  
ANISOU 4334  CB  ALA A 550     9093  15832  14914   2149   -483  -3458       C  
ATOM   4335  N   GLY A 551      29.143  15.919  39.316  1.00114.39           N  
ANISOU 4335  N   GLY A 551    10168  17341  15956   1907   -718  -2914       N  
ATOM   4336  CA  GLY A 551      29.145  16.741  40.515  1.00104.23           C  
ANISOU 4336  CA  GLY A 551     9070  15999  14534   1751   -878  -2522       C  
ATOM   4337  C   GLY A 551      29.695  18.134  40.276  1.00102.31           C  
ANISOU 4337  C   GLY A 551     8742  16172  13961   1398   -703  -2484       C  
ATOM   4338  O   GLY A 551      29.156  19.119  40.786  1.00101.09           O  
ANISOU 4338  O   GLY A 551     8884  15974  13552   1144   -709  -2181       O  
ATOM   4339  N   GLN A 552      30.772  18.238  39.493  1.00107.65           N  
ANISOU 4339  N   GLN A 552     9002  17252  14647   1371   -539  -2801       N  
ATOM   4340  CA  GLN A 552      31.364  19.548  39.240  1.00107.87           C  
ANISOU 4340  CA  GLN A 552     8924  17676  14386   1007   -367  -2757       C  
ATOM   4341  C   GLN A 552      30.427  20.432  38.428  1.00107.96           C  
ANISOU 4341  C   GLN A 552     9247  17753  14020    678   -125  -2632       C  
ATOM   4342  O   GLN A 552      30.313  21.633  38.697  1.00111.55           O  
ANISOU 4342  O   GLN A 552     9874  18276  14233    362    -89  -2385       O  
ATOM   4343  CB  GLN A 552      32.709  19.394  38.531  1.00112.33           C  
ANISOU 4343  CB  GLN A 552     8945  18688  15047   1042   -221  -3135       C  
ATOM   4344  CG  GLN A 552      33.477  20.700  38.387  1.00129.88           C  
ANISOU 4344  CG  GLN A 552    11007  21320  17021    654    -66  -3077       C  
ATOM   4345  CD  GLN A 552      33.980  21.228  39.719  1.00134.70           C  
ANISOU 4345  CD  GLN A 552    11618  21856  17708    604   -325  -2841       C  
ATOM   4346  OE1 GLN A 552      34.703  20.541  40.440  1.00127.43           O  
ANISOU 4346  OE1 GLN A 552    10441  20890  17087    886   -560  -2930       O  
ATOM   4347  NE2 GLN A 552      33.592  22.454  40.056  1.00120.90           N  
ANISOU 4347  NE2 GLN A 552    10155  20088  15692    252   -301  -2548       N  
ATOM   4348  N   LYS A 553      29.741  19.857  37.437  1.00120.04           N  
ANISOU 4348  N   LYS A 553    10851  19251  15508    754     23  -2804       N  
ATOM   4349  CA  LYS A 553      28.829  20.648  36.615  1.00113.79           C  
ANISOU 4349  CA  LYS A 553    10347  18532  14356    464    227  -2681       C  
ATOM   4350  C   LYS A 553      27.666  21.177  37.446  1.00106.34           C  
ANISOU 4350  C   LYS A 553     9876  17213  13317    369     83  -2288       C  
ATOM   4351  O   LYS A 553      27.299  22.353  37.342  1.00105.11           O  
ANISOU 4351  O   LYS A 553     9932  17123  12884     59    169  -2063       O  
ATOM   4352  CB  LYS A 553      28.319  19.813  35.440  1.00106.88           C  
ANISOU 4352  CB  LYS A 553     9442  17702  13466    594    379  -2973       C  
ATOM   4353  CG  LYS A 553      28.022  20.628  34.190  1.00114.82           C  
ANISOU 4353  CG  LYS A 553    10512  19051  14062    277    660  -2988       C  
ATOM   4354  CD  LYS A 553      28.058  19.763  32.940  1.00133.63           C  
ANISOU 4354  CD  LYS A 553    12683  21664  16425    412    839  -3408       C  
ATOM   4355  CE  LYS A 553      28.539  20.554  31.735  1.00143.54           C  
ANISOU 4355  CE  LYS A 553    13773  23476  17289     94   1146  -3507       C  
ATOM   4356  NZ  LYS A 553      27.703  21.761  31.490  1.00139.38           N  
ANISOU 4356  NZ  LYS A 553    13624  22945  16388   -258   1209  -3122       N  
ATOM   4357  N   LEU A 554      27.073  20.318  38.278  1.00 99.91           N  
ANISOU 4357  N   LEU A 554     9225  15998  12738    631   -135  -2201       N  
ATOM   4358  CA  LEU A 554      26.031  20.773  39.193  1.00 95.75           C  
ANISOU 4358  CA  LEU A 554     9107  15145  12128    554   -271  -1846       C  
ATOM   4359  C   LEU A 554      26.569  21.832  40.146  1.00 99.17           C  
ANISOU 4359  C   LEU A 554     9562  15652  12466    364   -364  -1628       C  
ATOM   4360  O   LEU A 554      25.926  22.861  40.379  1.00 95.17           O  
ANISOU 4360  O   LEU A 554     9337  15083  11741    130   -340  -1396       O  
ATOM   4361  CB  LEU A 554      25.462  19.591  39.977  1.00 95.66           C  
ANISOU 4361  CB  LEU A 554     9217  14731  12398    858   -488  -1787       C  
ATOM   4362  CG  LEU A 554      24.384  19.944  41.007  1.00 93.85           C  
ANISOU 4362  CG  LEU A 554     9383  14190  12086    793   -621  -1434       C  
ATOM   4363  CD1 LEU A 554      23.121  20.452  40.326  1.00 94.12           C  
ANISOU 4363  CD1 LEU A 554     9710  14162  11891    620   -470  -1357       C  
ATOM   4364  CD2 LEU A 554      24.075  18.759  41.910  1.00 93.17           C  
ANISOU 4364  CD2 LEU A 554     9365  13748  12287   1073   -848  -1343       C  
ATOM   4365  N   PHE A 555      27.763  21.598  40.700  1.00109.80           N  
ANISOU 4365  N   PHE A 555    10598  17131  13990    470   -483  -1719       N  
ATOM   4366  CA  PHE A 555      28.318  22.526  41.680  1.00104.62           C  
ANISOU 4366  CA  PHE A 555     9942  16546  13264    302   -604  -1542       C  
ATOM   4367  C   PHE A 555      28.598  23.894  41.072  1.00 99.83           C  
ANISOU 4367  C   PHE A 555     9321  16213  12395    -81   -405  -1514       C  
ATOM   4368  O   PHE A 555      28.496  24.910  41.769  1.00103.70           O  
ANISOU 4368  O   PHE A 555     9985  16655  12760   -292   -474  -1312       O  
ATOM   4369  CB  PHE A 555      29.596  21.952  42.287  1.00107.66           C  
ANISOU 4369  CB  PHE A 555     9950  17056  13901    502   -780  -1676       C  
ATOM   4370  CG  PHE A 555      30.178  22.803  43.377  1.00111.83           C  
ANISOU 4370  CG  PHE A 555    10463  17659  14369    351   -944  -1515       C  
ATOM   4371  CD1 PHE A 555      29.731  22.682  44.681  1.00107.68           C  
ANISOU 4371  CD1 PHE A 555    10176  16876  13861    449  -1199  -1277       C  
ATOM   4372  CD2 PHE A 555      31.164  23.734  43.094  1.00116.86           C  
ANISOU 4372  CD2 PHE A 555    10842  18640  14918     91   -840  -1608       C  
ATOM   4373  CE1 PHE A 555      30.262  23.469  45.685  1.00116.45           C  
ANISOU 4373  CE1 PHE A 555    11271  18081  14894    308  -1358  -1162       C  
ATOM   4374  CE2 PHE A 555      31.697  24.524  44.091  1.00117.84           C  
ANISOU 4374  CE2 PHE A 555    10946  18829  14999    -60  -1003  -1490       C  
ATOM   4375  CZ  PHE A 555      31.247  24.391  45.389  1.00123.65           C  
ANISOU 4375  CZ  PHE A 555    11923  19315  15744     57  -1267  -1281       C  
ATOM   4376  N   ASN A 556      28.959  23.942  39.785  1.00103.97           N  
ANISOU 4376  N   ASN A 556     9643  17028  12833   -184   -160  -1715       N  
ATOM   4377  CA  ASN A 556      29.220  25.225  39.137  1.00109.64           C  
ANISOU 4377  CA  ASN A 556    10356  18005  13297   -574     36  -1648       C  
ATOM   4378  C   ASN A 556      28.008  26.145  39.209  1.00115.07           C  
ANISOU 4378  C   ASN A 556    11498  18452  13771   -778     46  -1361       C  
ATOM   4379  O   ASN A 556      28.159  27.372  39.201  1.00113.76           O  
ANISOU 4379  O   ASN A 556    11411  18359  13452  -1098    101  -1211       O  
ATOM   4380  CB  ASN A 556      29.632  25.005  37.680  1.00124.96           C  
ANISOU 4380  CB  ASN A 556    12040  20307  15133   -641    310  -1894       C  
ATOM   4381  CG  ASN A 556      30.967  24.295  37.548  1.00131.56           C  
ANISOU 4381  CG  ASN A 556    12367  21447  16175   -480    332  -2214       C  
ATOM   4382  OD1 ASN A 556      31.746  24.228  38.499  1.00131.37           O  
ANISOU 4382  OD1 ASN A 556    12154  21414  16344   -393    148  -2220       O  
ATOM   4383  ND2 ASN A 556      31.233  23.754  36.364  1.00136.64           N  
ANISOU 4383  ND2 ASN A 556    12770  22376  16772   -431    550  -2501       N  
ATOM   4384  N   MET A 557      26.806  25.574  39.283  1.00109.55           N  
ANISOU 4384  N   MET A 557    11088  17454  13084   -599    -11  -1290       N  
ATOM   4385  CA  MET A 557      25.575  26.338  39.435  1.00 95.33           C  
ANISOU 4385  CA  MET A 557     9699  15402  11119   -737    -25  -1040       C  
ATOM   4386  C   MET A 557      25.193  26.538  40.895  1.00 99.05           C  
ANISOU 4386  C   MET A 557    10380  15588  11667   -673   -250   -858       C  
ATOM   4387  O   MET A 557      24.644  27.588  41.250  1.00 98.87           O  
ANISOU 4387  O   MET A 557    10611  15438  11517   -866   -271   -672       O  
ATOM   4388  CB  MET A 557      24.434  25.634  38.701  1.00100.37           C  
ANISOU 4388  CB  MET A 557    10515  15902  11719   -594     42  -1076       C  
ATOM   4389  CG  MET A 557      23.055  26.254  38.888  1.00109.91           C  
ANISOU 4389  CG  MET A 557    12127  16835  12798   -678      8   -842       C  
ATOM   4390  SD  MET A 557      22.143  25.606  40.309  1.00100.09           S  
ANISOU 4390  SD  MET A 557    11116  15190  11723   -435   -218   -714       S  
ATOM   4391  CE  MET A 557      22.027  23.868  39.895  1.00 92.08           C  
ANISOU 4391  CE  MET A 557     9951  14111  10923   -108   -228   -933       C  
ATOM   4392  N   LEU A 558      25.462  25.541  41.741  1.00102.84           N  
ANISOU 4392  N   LEU A 558    10758  15966  12350   -402   -423   -910       N  
ATOM   4393  CA  LEU A 558      25.062  25.617  43.143  1.00 95.97           C  
ANISOU 4393  CA  LEU A 558    10090  14862  11514   -332   -635   -731       C  
ATOM   4394  C   LEU A 558      25.675  26.831  43.829  1.00 93.49           C  
ANISOU 4394  C   LEU A 558     9765  14648  11108   -573   -699   -652       C  
ATOM   4395  O   LEU A 558      24.985  27.577  44.532  1.00 86.31           O  
ANISOU 4395  O   LEU A 558     9131  13571  10092   -678   -766   -495       O  
ATOM   4396  CB  LEU A 558      25.465  24.331  43.868  1.00 89.15           C  
ANISOU 4396  CB  LEU A 558     9073  13917  10881    -17   -822   -782       C  
ATOM   4397  CG  LEU A 558      24.808  23.030  43.403  1.00 89.15           C  
ANISOU 4397  CG  LEU A 558     9106  13734  11033    241   -807   -854       C  
ATOM   4398  CD1 LEU A 558      25.353  21.846  44.183  1.00 90.33           C  
ANISOU 4398  CD1 LEU A 558     9094  13780  11447    540  -1024   -875       C  
ATOM   4399  CD2 LEU A 558      23.294  23.108  43.535  1.00 95.91           C  
ANISOU 4399  CD2 LEU A 558    10341  14317  11784    216   -786   -679       C  
ATOM   4400  N   ARG A 559      26.975  27.051  43.626  1.00 92.83           N  
ANISOU 4400  N   ARG A 559     9348  14846  11078   -667   -677   -785       N  
ATOM   4401  CA  ARG A 559      27.660  28.140  44.312  1.00 93.19           C  
ANISOU 4401  CA  ARG A 559     9345  14990  11072   -901   -759   -740       C  
ATOM   4402  C   ARG A 559      27.135  29.510  43.909  1.00 93.24           C  
ANISOU 4402  C   ARG A 559     9586  14936  10903  -1230   -635   -620       C  
ATOM   4403  O   ARG A 559      27.299  30.470  44.668  1.00111.60           O  
ANISOU 4403  O   ARG A 559    11996  17217  13190  -1412   -734   -554       O  
ATOM   4404  CB  ARG A 559      29.160  28.078  44.033  1.00 95.66           C  
ANISOU 4404  CB  ARG A 559     9212  15643  11491   -955   -736   -924       C  
ATOM   4405  CG  ARG A 559      29.505  27.940  42.562  1.00110.30           C  
ANISOU 4405  CG  ARG A 559    10855  17737  13318  -1036   -474  -1070       C  
ATOM   4406  CD  ARG A 559      30.974  28.212  42.340  1.00100.60           C  
ANISOU 4406  CD  ARG A 559     9189  16876  12160  -1181   -424  -1237       C  
ATOM   4407  NE  ARG A 559      31.325  29.522  42.873  1.00112.32           N  
ANISOU 4407  NE  ARG A 559    10725  18383  13570  -1513   -473  -1126       N  
ATOM   4408  CZ  ARG A 559      31.373  30.637  42.158  1.00125.21           C  
ANISOU 4408  CZ  ARG A 559    12408  20106  15061  -1884   -292  -1050       C  
ATOM   4409  NH1 ARG A 559      31.122  30.638  40.858  1.00124.96           N  
ANISOU 4409  NH1 ARG A 559    12377  20198  14903  -1984    -41  -1057       N  
ATOM   4410  NH2 ARG A 559      31.672  31.783  42.764  1.00135.97           N  
ANISOU 4410  NH2 ARG A 559    13828  21428  16405  -2168   -374   -959       N  
ATOM   4411  N   LEU A 560      26.518  29.625  42.731  1.00 92.69           N  
ANISOU 4411  N   LEU A 560     9624  14861  10734  -1308   -437   -596       N  
ATOM   4412  CA  LEU A 560      26.109  30.936  42.239  1.00 96.88           C  
ANISOU 4412  CA  LEU A 560    10358  15336  11118  -1623   -332   -459       C  
ATOM   4413  C   LEU A 560      25.060  31.568  43.145  1.00 96.97           C  
ANISOU 4413  C   LEU A 560    10734  15021  11090  -1630   -461   -308       C  
ATOM   4414  O   LEU A 560      25.062  32.787  43.352  1.00 90.28           O  
ANISOU 4414  O   LEU A 560    10009  14093  10200  -1881   -479   -224       O  
ATOM   4415  CB  LEU A 560      25.586  30.819  40.808  1.00113.99           C  
ANISOU 4415  CB  LEU A 560    12576  17573  13161  -1671   -122   -446       C  
ATOM   4416  CG  LEU A 560      26.550  30.226  39.780  1.00110.24           C  
ANISOU 4416  CG  LEU A 560    11738  17463  12684  -1676     47   -630       C  
ATOM   4417  CD1 LEU A 560      25.938  30.264  38.390  1.00 96.02           C  
ANISOU 4417  CD1 LEU A 560    10033  15752  10699  -1762    248   -601       C  
ATOM   4418  CD2 LEU A 560      27.874  30.973  39.804  1.00101.52           C  
ANISOU 4418  CD2 LEU A 560    10352  16623  11596  -1948     90   -672       C  
ATOM   4419  N   GLY A 561      24.169  30.755  43.709  1.00 94.83           N  
ANISOU 4419  N   GLY A 561    10626  14559  10844  -1363   -551   -282       N  
ATOM   4420  CA  GLY A 561      23.078  31.302  44.499  1.00 89.89           C  
ANISOU 4420  CA  GLY A 561    10329  13658  10164  -1359   -641   -163       C  
ATOM   4421  C   GLY A 561      22.225  32.218  43.646  1.00107.09           C  
ANISOU 4421  C   GLY A 561    12734  15707  12247  -1533   -522    -56       C  
ATOM   4422  O   GLY A 561      21.812  31.866  42.535  1.00113.10           O  
ANISOU 4422  O   GLY A 561    13507  16508  12960  -1507   -390    -43       O  
ATOM   4423  N   LYS A 562      21.960  33.416  44.163  1.00 99.58           N  
ANISOU 4423  N   LYS A 562    11964  14598  11273  -1707   -584     13       N  
ATOM   4424  CA  LYS A 562      21.274  34.456  43.409  1.00102.57           C  
ANISOU 4424  CA  LYS A 562    12550  14825  11595  -1890   -508    134       C  
ATOM   4425  C   LYS A 562      22.230  35.461  42.782  1.00103.60           C  
ANISOU 4425  C   LYS A 562    12568  15073  11724  -2217   -441    175       C  
ATOM   4426  O   LYS A 562      21.771  36.429  42.169  1.00104.76           O  
ANISOU 4426  O   LYS A 562    12890  15077  11837  -2401   -399    311       O  
ATOM   4427  CB  LYS A 562      20.275  35.198  44.303  1.00 99.27           C  
ANISOU 4427  CB  LYS A 562    12414  14113  11190  -1868   -617    176       C  
ATOM   4428  CG  LYS A 562      18.933  34.504  44.455  1.00116.05           C  
ANISOU 4428  CG  LYS A 562    14717  16088  13288  -1619   -620    200       C  
ATOM   4429  CD  LYS A 562      17.936  35.398  45.177  1.00121.06           C  
ANISOU 4429  CD  LYS A 562    15606  16458  13933  -1623   -697    221       C  
ATOM   4430  CE  LYS A 562      17.842  36.763  44.509  1.00115.27           C  
ANISOU 4430  CE  LYS A 562    14996  15574  13230  -1856   -680    309       C  
ATOM   4431  NZ  LYS A 562      16.892  37.676  45.204  1.00 86.47           N  
ANISOU 4431  NZ  LYS A 562    11577  11643   9634  -1839   -767    291       N  
ATOM   4432  N   SER A 563      23.543  35.252  42.915  1.00 91.66           N  
ANISOU 4432  N   SER A 563    10758  13814  10255  -2299   -437     71       N  
ATOM   4433  CA  SER A 563      24.509  36.227  42.419  1.00 96.74           C  
ANISOU 4433  CA  SER A 563    11266  14582  10908  -2646   -371    109       C  
ATOM   4434  C   SER A 563      24.477  36.344  40.901  1.00101.85           C  
ANISOU 4434  C   SER A 563    11891  15369  11438  -2800   -172    222       C  
ATOM   4435  O   SER A 563      24.811  37.401  40.355  1.00 94.80           O  
ANISOU 4435  O   SER A 563    11024  14473  10524  -3124   -111    353       O  
ATOM   4436  CB  SER A 563      25.914  35.856  42.893  1.00118.92           C  
ANISOU 4436  CB  SER A 563    13716  17673  13797  -2676   -409    -52       C  
ATOM   4437  OG  SER A 563      26.295  34.579  42.408  1.00117.79           O  
ANISOU 4437  OG  SER A 563    13328  17783  13644  -2464   -326   -163       O  
ATOM   4438  N   GLU A 564      24.085  35.280  40.207  1.00117.49           N  
ANISOU 4438  N   GLU A 564    13828  17477  13338  -2585    -76    178       N  
ATOM   4439  CA  GLU A 564      24.003  35.290  38.759  1.00114.16           C  
ANISOU 4439  CA  GLU A 564    13383  17236  12757  -2709    110    261       C  
ATOM   4440  C   GLU A 564      22.565  35.032  38.322  1.00115.09           C  
ANISOU 4440  C   GLU A 564    13785  17155  12790  -2534    103    352       C  
ATOM   4441  O   GLU A 564      21.816  34.347  39.026  1.00110.57           O  
ANISOU 4441  O   GLU A 564    13316  16405  12290  -2252      1    281       O  
ATOM   4442  CB  GLU A 564      24.928  34.229  38.147  1.00112.21           C  
ANISOU 4442  CB  GLU A 564    12772  17385  12476  -2627    250     66       C  
ATOM   4443  CG  GLU A 564      26.410  34.412  38.479  1.00119.11           C  
ANISOU 4443  CG  GLU A 564    13302  18513  13441  -2793    268    -48       C  
ATOM   4444  CD  GLU A 564      27.065  35.568  37.738  1.00123.75           C  
ANISOU 4444  CD  GLU A 564    13828  19256  13937  -3226    402     98       C  
ATOM   4445  OE1 GLU A 564      26.374  36.274  36.973  1.00133.61           O  
ANISOU 4445  OE1 GLU A 564    15323  20396  15045  -3399    466    318       O  
ATOM   4446  OE2 GLU A 564      28.285  35.768  37.921  1.00108.15           O1-
ANISOU 4446  OE2 GLU A 564    11546  17513  12034  -3402    436      4       O1-
ATOM   4447  N   PRO A 565      22.146  35.580  37.179  1.00110.81           N  
ANISOU 4447  N   PRO A 565    13369  16646  12090  -2705    202    523       N  
ATOM   4448  CA  PRO A 565      20.768  35.363  36.719  1.00 95.78           C  
ANISOU 4448  CA  PRO A 565    11716  14572  10104  -2541    177    606       C  
ATOM   4449  C   PRO A 565      20.471  33.884  36.532  1.00 95.27           C  
ANISOU 4449  C   PRO A 565    11535  14640  10025  -2234    218    403       C  
ATOM   4450  O   PRO A 565      21.339  33.098  36.146  1.00101.15           O  
ANISOU 4450  O   PRO A 565    11999  15689  10745  -2200    327    230       O  
ATOM   4451  CB  PRO A 565      20.717  36.117  35.386  1.00 98.53           C  
ANISOU 4451  CB  PRO A 565    12139  15049  10248  -2811    288    819       C  
ATOM   4452  CG  PRO A 565      21.798  37.140  35.491  1.00 95.08           C  
ANISOU 4452  CG  PRO A 565    11608  14669   9850  -3153    318    922       C  
ATOM   4453  CD  PRO A 565      22.888  36.487  36.287  1.00104.80           C  
ANISOU 4453  CD  PRO A 565    12533  16074  11211  -3077    328    675       C  
ATOM   4454  N   TRP A 566      19.217  33.507  36.808  1.00 86.66           N  
ANISOU 4454  N   TRP A 566    10650  13305   8970  -2010    128    413       N  
ATOM   4455  CA  TRP A 566      18.857  32.093  36.802  1.00 90.99           C  
ANISOU 4455  CA  TRP A 566    11109  13903   9560  -1720    138    224       C  
ATOM   4456  C   TRP A 566      19.034  31.459  35.430  1.00100.60           C  
ANISOU 4456  C   TRP A 566    12180  15431  10611  -1728    291    124       C  
ATOM   4457  O   TRP A 566      19.141  30.232  35.338  1.00103.21           O  
ANISOU 4457  O   TRP A 566    12350  15860  11004  -1516    321    -93       O  
ATOM   4458  CB  TRP A 566      17.417  31.895  37.291  1.00 93.74           C  
ANISOU 4458  CB  TRP A 566    11703  13942   9972  -1524     25    270       C  
ATOM   4459  CG  TRP A 566      16.344  32.366  36.348  1.00100.19           C  
ANISOU 4459  CG  TRP A 566    12719  14698  10652  -1573     35    408       C  
ATOM   4460  CD1 TRP A 566      15.685  33.561  36.385  1.00 99.88           C  
ANISOU 4460  CD1 TRP A 566    12910  14444  10595  -1693    -41    611       C  
ATOM   4461  CD2 TRP A 566      15.785  31.636  35.246  1.00100.10           C  
ANISOU 4461  CD2 TRP A 566    12687  14833  10513  -1488    102    339       C  
ATOM   4462  NE1 TRP A 566      14.763  33.626  35.368  1.00 94.54           N  
ANISOU 4462  NE1 TRP A 566    12356  13781   9784  -1682    -36    699       N  
ATOM   4463  CE2 TRP A 566      14.805  32.456  34.655  1.00 96.11           C  
ANISOU 4463  CE2 TRP A 566    12404  14215   9897  -1567     53    531       C  
ATOM   4464  CE3 TRP A 566      16.025  30.371  34.699  1.00101.68           C  
ANISOU 4464  CE3 TRP A 566    12697  15244  10694  -1347    185    116       C  
ATOM   4465  CZ2 TRP A 566      14.067  32.054  33.543  1.00102.20           C  
ANISOU 4465  CZ2 TRP A 566    13210  15110  10509  -1519     80    517       C  
ATOM   4466  CZ3 TRP A 566      15.291  29.974  33.595  1.00 86.92           C  
ANISOU 4466  CZ3 TRP A 566    10864  13487   8674  -1307    225     74       C  
ATOM   4467  CH2 TRP A 566      14.324  30.813  33.029  1.00100.46           C  
ANISOU 4467  CH2 TRP A 566    12801  15119  10251  -1398    170    278       C  
ATOM   4468  N   THR A 567      19.068  32.263  34.366  1.00105.45           N  
ANISOU 4468  N   THR A 567    12850  16202  11016  -1970    382    274       N  
ATOM   4469  CA  THR A 567      19.362  31.723  33.044  1.00 97.51           C  
ANISOU 4469  CA  THR A 567    11683  15568   9798  -2012    546    164       C  
ATOM   4470  C   THR A 567      20.824  31.303  32.945  1.00109.08           C  
ANISOU 4470  C   THR A 567    12794  17372  11280  -2073    680    -33       C  
ATOM   4471  O   THR A 567      21.134  30.193  32.496  1.00107.79           O  
ANISOU 4471  O   THR A 567    12411  17433  11111  -1908    769   -301       O  
ATOM   4472  CB  THR A 567      19.022  32.756  31.970  1.00 89.07           C  
ANISOU 4472  CB  THR A 567    10780  14597   8466  -2278    597    424       C  
ATOM   4473  OG1 THR A 567      19.696  33.986  32.258  1.00 99.14           O  
ANISOU 4473  OG1 THR A 567    12087  15821   9760  -2569    593    639       O  
ATOM   4474  CG2 THR A 567      17.522  33.008  31.940  1.00 91.33           C  
ANISOU 4474  CG2 THR A 567    11374  14580   8744  -2166    454    575       C  
ATOM   4475  N   LEU A 568      21.739  32.183  33.362  1.00111.20           N  
ANISOU 4475  N   LEU A 568    12986  17675  11588  -2306    692     76       N  
ATOM   4476  CA  LEU A 568      23.151  31.821  33.421  1.00106.62           C  
ANISOU 4476  CA  LEU A 568    12038  17407  11065  -2356    800   -120       C  
ATOM   4477  C   LEU A 568      23.405  30.744  34.468  1.00 96.94           C  
ANISOU 4477  C   LEU A 568    10661  16063  10110  -2033    686   -355       C  
ATOM   4478  O   LEU A 568      24.350  29.959  34.333  1.00 97.97           O  
ANISOU 4478  O   LEU A 568    10459  16458  10308  -1939    766   -604       O  
ATOM   4479  CB  LEU A 568      23.992  33.068  33.705  1.00108.29           C  
ANISOU 4479  CB  LEU A 568    12213  17647  11284  -2700    813     63       C  
ATOM   4480  CG  LEU A 568      25.484  32.934  34.018  1.00 99.01           C  
ANISOU 4480  CG  LEU A 568    10654  16751  10214  -2790    886   -110       C  
ATOM   4481  CD1 LEU A 568      26.235  32.278  32.870  1.00 99.19           C  
ANISOU 4481  CD1 LEU A 568    10346  17271  10069  -2826   1122   -318       C  
ATOM   4482  CD2 LEU A 568      26.069  34.304  34.327  1.00 98.66           C  
ANISOU 4482  CD2 LEU A 568    10642  16652  10190  -3161    869    108       C  
ATOM   4483  N   ALA A 569      22.573  30.689  35.510  1.00 91.84           N  
ANISOU 4483  N   ALA A 569    10246  15029   9619  -1859    499   -277       N  
ATOM   4484  CA  ALA A 569      22.662  29.594  36.470  1.00 99.63           C  
ANISOU 4484  CA  ALA A 569    11131  15886  10836  -1548    378   -451       C  
ATOM   4485  C   ALA A 569      22.305  28.269  35.811  1.00 96.89           C  
ANISOU 4485  C   ALA A 569    10691  15615  10509  -1295    434   -668       C  
ATOM   4486  O   ALA A 569      23.042  27.283  35.924  1.00103.36           O  
ANISOU 4486  O   ALA A 569    11238  16557  11479  -1112    440   -901       O  
ATOM   4487  CB  ALA A 569      21.749  29.869  37.664  1.00 92.91           C  
ANISOU 4487  CB  ALA A 569    10567  14641  10095  -1451    189   -299       C  
ATOM   4488  N   LEU A 570      21.172  28.233  35.106  1.00101.75           N  
ANISOU 4488  N   LEU A 570    11521  16149  10990  -1278    463   -608       N  
ATOM   4489  CA  LEU A 570      20.760  27.025  34.398  1.00102.67           C  
ANISOU 4489  CA  LEU A 570    11560  16332  11118  -1064    513   -835       C  
ATOM   4490  C   LEU A 570      21.800  26.613  33.363  1.00108.57           C  
ANISOU 4490  C   LEU A 570    11977  17511  11763  -1111    698  -1084       C  
ATOM   4491  O   LEU A 570      22.149  25.432  33.251  1.00110.58           O  
ANISOU 4491  O   LEU A 570    12012  17832  12171   -878    713  -1375       O  
ATOM   4492  CB  LEU A 570      19.402  27.260  33.734  1.00 93.38           C  
ANISOU 4492  CB  LEU A 570    10660  15045   9776  -1091    508   -716       C  
ATOM   4493  CG  LEU A 570      18.772  26.129  32.921  1.00 91.34           C  
ANISOU 4493  CG  LEU A 570    10363  14839   9502   -905    546   -945       C  
ATOM   4494  CD1 LEU A 570      18.506  24.914  33.794  1.00 88.92           C  
ANISOU 4494  CD1 LEU A 570    10023  14253   9511   -605    423  -1092       C  
ATOM   4495  CD2 LEU A 570      17.494  26.609  32.256  1.00 91.30           C  
ANISOU 4495  CD2 LEU A 570    10623  14765   9301   -981    526   -790       C  
ATOM   4496  N   GLU A 571      22.312  27.586  32.601  1.00114.95           N  
ANISOU 4496  N   GLU A 571    12741  18615  12321  -1416    844   -977       N  
ATOM   4497  CA  GLU A 571      23.269  27.294  31.538  1.00113.26           C  
ANISOU 4497  CA  GLU A 571    12206  18876  11951  -1503   1057  -1207       C  
ATOM   4498  C   GLU A 571      24.527  26.619  32.070  1.00122.40           C  
ANISOU 4498  C   GLU A 571    12989  20166  13350  -1362   1067  -1466       C  
ATOM   4499  O   GLU A 571      25.173  25.853  31.344  1.00130.80           O  
ANISOU 4499  O   GLU A 571    13746  21556  14397  -1273   1210  -1786       O  
ATOM   4500  CB  GLU A 571      23.634  28.584  30.803  1.00103.18           C  
ANISOU 4500  CB  GLU A 571    10964  17871  10370  -1904   1201   -971       C  
ATOM   4501  CG  GLU A 571      24.329  28.376  29.470  1.00101.99           C  
ANISOU 4501  CG  GLU A 571    10543  18264   9946  -2042   1454  -1166       C  
ATOM   4502  CD  GLU A 571      24.879  29.667  28.898  1.00108.82           C  
ANISOU 4502  CD  GLU A 571    11410  19399  10538  -2475   1597   -893       C  
ATOM   4503  OE1 GLU A 571      25.687  30.326  29.584  1.00121.76           O  
ANISOU 4503  OE1 GLU A 571    12951  21002  12310  -2639   1579   -782       O  
ATOM   4504  OE2 GLU A 571      24.505  30.023  27.762  1.00119.06           O1-
ANISOU 4504  OE2 GLU A 571    12807  20945  11486  -2663   1718   -782       O1-
ATOM   4505  N   ASN A 572      24.897  26.890  33.325  1.00105.28           N  
ANISOU 4505  N   ASN A 572    10828  17767  11407  -1332    910  -1352       N  
ATOM   4506  CA  ASN A 572      26.085  26.259  33.891  1.00113.81           C  
ANISOU 4506  CA  ASN A 572    11548  18964  12731  -1181    879  -1579       C  
ATOM   4507  C   ASN A 572      25.921  24.750  34.007  1.00120.53           C  
ANISOU 4507  C   ASN A 572    12280  19690  13827   -785    801  -1865       C  
ATOM   4508  O   ASN A 572      26.895  24.007  33.842  1.00139.96           O  
ANISOU 4508  O   ASN A 572    14371  22371  16436   -636    852  -2164       O  
ATOM   4509  CB  ASN A 572      26.404  26.875  35.255  1.00122.02           C  
ANISOU 4509  CB  ASN A 572    12654  19775  13935  -1229    692  -1382       C  
ATOM   4510  CG  ASN A 572      27.128  28.202  35.138  1.00121.29           C  
ANISOU 4510  CG  ASN A 572    12503  19888  13694  -1616    784  -1217       C  
ATOM   4511  OD1 ASN A 572      27.045  28.879  34.113  1.00115.11           O  
ANISOU 4511  OD1 ASN A 572    11767  19319  12651  -1885    963  -1124       O  
ATOM   4512  ND2 ASN A 572      27.847  28.580  36.189  1.00117.80           N  
ANISOU 4512  ND2 ASN A 572    11959  19384  13414  -1658    652  -1171       N  
ATOM   4513  N   VAL A 573      24.705  24.278  34.276  1.00 94.21           N  
ANISOU 4513  N   VAL A 573     9240  15999  10558   -613    677  -1788       N  
ATOM   4514  CA  VAL A 573      24.454  22.839  34.314  1.00 87.65           C  
ANISOU 4514  CA  VAL A 573     8322  15004   9975   -263    600  -2043       C  
ATOM   4515  C   VAL A 573      24.205  22.301  32.914  1.00111.39           C  
ANISOU 4515  C   VAL A 573    11237  18258  12827   -239    780  -2318       C  
ATOM   4516  O   VAL A 573      24.924  21.423  32.424  1.00108.86           O  
ANISOU 4516  O   VAL A 573    10592  18140  12628    -71    858  -2679       O  
ATOM   4517  CB  VAL A 573      23.261  22.516  35.233  1.00 86.40           C  
ANISOU 4517  CB  VAL A 573     8499  14364   9965   -111    396  -1843       C  
ATOM   4518  CG1 VAL A 573      23.270  21.043  35.623  1.00 86.90           C  
ANISOU 4518  CG1 VAL A 573     8445  14200  10374    243    267  -2053       C  
ATOM   4519  CG2 VAL A 573      23.268  23.391  36.450  1.00 85.53           C  
ANISOU 4519  CG2 VAL A 573     8559  14071   9869   -224    257  -1533       C  
ATOM   4520  N   VAL A 574      23.178  22.830  32.250  1.00122.60           N  
ANISOU 4520  N   VAL A 574    12932  19674  13976   -401    840  -2168       N  
ATOM   4521  CA  VAL A 574      22.585  22.167  31.096  1.00104.36           C  
ANISOU 4521  CA  VAL A 574    10617  17497  11538   -330    941  -2412       C  
ATOM   4522  C   VAL A 574      23.013  22.755  29.753  1.00101.24           C  
ANISOU 4522  C   VAL A 574    10092  17625  10748   -586   1186  -2496       C  
ATOM   4523  O   VAL A 574      22.801  22.107  28.717  1.00107.83           O  
ANISOU 4523  O   VAL A 574    10834  18681  11457   -518   1295  -2789       O  
ATOM   4524  CB  VAL A 574      21.047  22.178  31.215  1.00 99.76           C  
ANISOU 4524  CB  VAL A 574    10409  16566  10927   -300    818  -2220       C  
ATOM   4525  CG1 VAL A 574      20.624  21.749  32.614  1.00 95.77           C  
ANISOU 4525  CG1 VAL A 574    10047  15579  10763   -105    596  -2075       C  
ATOM   4526  CG2 VAL A 574      20.500  23.558  30.895  1.00104.99           C  
ANISOU 4526  CG2 VAL A 574    11331  17303  11255   -607    858  -1873       C  
ATOM   4527  N   GLY A 575      23.598  23.950  29.733  1.00103.60           N  
ANISOU 4527  N   GLY A 575    10385  18137  10842   -890   1275  -2252       N  
ATOM   4528  CA  GLY A 575      24.050  24.533  28.485  1.00114.24           C  
ANISOU 4528  CA  GLY A 575    11610  20000  11798  -1169   1516  -2285       C  
ATOM   4529  C   GLY A 575      22.988  25.233  27.669  1.00110.54           C  
ANISOU 4529  C   GLY A 575    11460  19572  10968  -1373   1540  -2037       C  
ATOM   4530  O   GLY A 575      23.269  25.636  26.534  1.00100.10           O  
ANISOU 4530  O   GLY A 575    10056  18702   9275  -1604   1736  -2053       O  
ATOM   4531  N   ALA A 576      21.778  25.380  28.199  1.00118.64           N  
ANISOU 4531  N   ALA A 576    12834  20163  12082  -1294   1346  -1809       N  
ATOM   4532  CA  ALA A 576      20.724  26.157  27.565  1.00115.34           C  
ANISOU 4532  CA  ALA A 576    12730  19729  11365  -1472   1321  -1528       C  
ATOM   4533  C   ALA A 576      20.296  27.271  28.508  1.00120.21           C  
ANISOU 4533  C   ALA A 576    13633  19969  12072  -1597   1167  -1105       C  
ATOM   4534  O   ALA A 576      20.301  27.105  29.732  1.00120.08           O  
ANISOU 4534  O   ALA A 576    13650  19600  12374  -1447   1026  -1074       O  
ATOM   4535  CB  ALA A 576      19.519  25.282  27.198  1.00118.49           C  
ANISOU 4535  CB  ALA A 576    13264  19972  11783  -1249   1228  -1693       C  
ATOM   4536  N   LYS A 577      19.930  28.413  27.932  1.00114.66           N  
ANISOU 4536  N   LYS A 577    13136  19347  11084  -1872   1186   -782       N  
ATOM   4537  CA  LYS A 577      19.585  29.583  28.726  1.00107.95           C  
ANISOU 4537  CA  LYS A 577    12546  18152  10320  -2011   1049   -401       C  
ATOM   4538  C   LYS A 577      18.133  29.607  29.179  1.00110.79           C  
ANISOU 4538  C   LYS A 577    13216  18088  10791  -1846    848   -266       C  
ATOM   4539  O   LYS A 577      17.725  30.579  29.821  1.00117.11           O  
ANISOU 4539  O   LYS A 577    14240  18588  11670  -1935    727     20       O  
ATOM   4540  CB  LYS A 577      19.881  30.872  27.947  1.00 97.91           C  
ANISOU 4540  CB  LYS A 577    11360  17103   8738  -2392   1140    -81       C  
ATOM   4541  CG  LYS A 577      21.346  31.107  27.634  1.00105.99           C  
ANISOU 4541  CG  LYS A 577    12082  18528   9660  -2627   1345   -145       C  
ATOM   4542  CD  LYS A 577      21.532  32.393  26.843  1.00118.50           C  
ANISOU 4542  CD  LYS A 577    13785  20304  10934  -3034   1429    224       C  
ATOM   4543  CE  LYS A 577      22.996  32.641  26.514  1.00138.55           C  
ANISOU 4543  CE  LYS A 577    16002  23274  13368  -3307   1655    167       C  
ATOM   4544  NZ  LYS A 577      23.186  33.882  25.713  1.00151.15           N  
ANISOU 4544  NZ  LYS A 577    17718  25058  14654  -3740   1745    563       N  
ATOM   4545  N   ASN A 578      17.338  28.582  28.882  1.00106.33           N  
ANISOU 4545  N   ASN A 578    12659  17488  10253  -1612    809   -482       N  
ATOM   4546  CA  ASN A 578      15.917  28.690  29.172  1.00 99.51           C  
ANISOU 4546  CA  ASN A 578    12070  16278   9460  -1496    636   -343       C  
ATOM   4547  C   ASN A 578      15.299  27.316  29.393  1.00 97.94           C  
ANISOU 4547  C   ASN A 578    11812  15938   9463  -1197    579   -637       C  
ATOM   4548  O   ASN A 578      15.937  26.275  29.211  1.00 97.87           O  
ANISOU 4548  O   ASN A 578    11563  16091   9531  -1072    665   -954       O  
ATOM   4549  CB  ASN A 578      15.190  29.442  28.050  1.00106.63           C  
ANISOU 4549  CB  ASN A 578    13155  17330  10031  -1664    625   -128       C  
ATOM   4550  CG  ASN A 578      13.909  30.094  28.525  1.00129.28           C  
ANISOU 4550  CG  ASN A 578    16316  19808  12995  -1614    430    125       C  
ATOM   4551  OD1 ASN A 578      13.398  29.771  29.598  1.00117.93           O  
ANISOU 4551  OD1 ASN A 578    14937  18024  11849  -1429    323     82       O  
ATOM   4552  ND2 ASN A 578      13.383  31.020  27.730  1.00136.42           N  
ANISOU 4552  ND2 ASN A 578    17400  20780  13653  -1780    381    396       N  
ATOM   4553  N   MET A 579      14.026  27.348  29.782  1.00 90.85           N  
ANISOU 4553  N   MET A 579    11130  14723   8667  -1090    429   -529       N  
ATOM   4554  CA  MET A 579      13.268  26.163  30.154  1.00 85.49           C  
ANISOU 4554  CA  MET A 579    10435  13829   8217   -838    352   -742       C  
ATOM   4555  C   MET A 579      12.877  25.353  28.926  1.00106.03           C  
ANISOU 4555  C   MET A 579    12952  16678  10657   -783    399  -1000       C  
ATOM   4556  O   MET A 579      12.437  25.902  27.913  1.00126.70           O  
ANISOU 4556  O   MET A 579    15659  19511  12972   -914    407   -906       O  
ATOM   4557  CB  MET A 579      12.010  26.596  30.906  1.00 83.90           C  
ANISOU 4557  CB  MET A 579    10476  13258   8144   -781    195   -531       C  
ATOM   4558  CG  MET A 579      11.512  25.675  31.992  1.00104.69           C  
ANISOU 4558  CG  MET A 579    13108  15567  11102   -570    113   -630       C  
ATOM   4559  SD  MET A 579       9.921  26.279  32.601  1.00109.00           S  
ANISOU 4559  SD  MET A 579    13909  15784  11723   -536    -34   -408       S  
ATOM   4560  CE  MET A 579      10.132  28.054  32.430  1.00 83.47           C  
ANISOU 4560  CE  MET A 579    10834  12598   8282   -758    -48    -89       C  
ATOM   4561  N   ASN A 580      13.024  24.034  29.022  1.00104.22           N  
ANISOU 4561  N   ASN A 580    12555  16408  10637   -587    413  -1329       N  
ATOM   4562  CA  ASN A 580      12.592  23.142  27.956  1.00112.69           C  
ANISOU 4562  CA  ASN A 580    13540  17667  11610   -510    440  -1637       C  
ATOM   4563  C   ASN A 580      12.042  21.863  28.562  1.00116.86           C  
ANISOU 4563  C   ASN A 580    14029  17863  12511   -273    347  -1858       C  
ATOM   4564  O   ASN A 580      12.594  21.334  29.530  1.00104.61           O  
ANISOU 4564  O   ASN A 580    12394  16090  11264   -150    328  -1899       O  
ATOM   4565  CB  ASN A 580      13.730  22.814  26.984  1.00 93.64           C  
ANISOU 4565  CB  ASN A 580    10875  15708   8995   -563    619  -1917       C  
ATOM   4566  CG  ASN A 580      13.247  22.048  25.767  1.00110.06           C  
ANISOU 4566  CG  ASN A 580    12878  18040  10898   -514    649  -2248       C  
ATOM   4567  OD1 ASN A 580      12.048  21.969  25.506  1.00127.23           O  
ANISOU 4567  OD1 ASN A 580    15207  20097  13037   -487    531  -2215       O  
ATOM   4568  ND2 ASN A 580      14.183  21.477  25.015  1.00116.83           N  
ANISOU 4568  ND2 ASN A 580    13480  19266  11645   -500    807  -2596       N  
ATOM   4569  N   VAL A 581      10.952  21.371  27.976  1.00121.29           N  
ANISOU 4569  N   VAL A 581    14648  18392  13046   -221    277  -1989       N  
ATOM   4570  CA  VAL A 581      10.291  20.189  28.509  1.00110.63           C  
ANISOU 4570  CA  VAL A 581    13278  16698  12058    -32    181  -2171       C  
ATOM   4571  C   VAL A 581      10.823  18.895  27.890  1.00107.42           C  
ANISOU 4571  C   VAL A 581    12639  16401  11776    105    239  -2633       C  
ATOM   4572  O   VAL A 581      10.595  17.811  28.448  1.00106.42           O  
ANISOU 4572  O   VAL A 581    12462  15949  12025    271    165  -2794       O  
ATOM   4573  CB  VAL A 581       8.766  20.333  28.328  1.00 86.44           C  
ANISOU 4573  CB  VAL A 581    10385  13497   8960    -51     58  -2073       C  
ATOM   4574  CG1 VAL A 581       8.417  20.635  26.871  1.00104.53           C  
ANISOU 4574  CG1 VAL A 581    12675  16180  10863   -155     78  -2183       C  
ATOM   4575  CG2 VAL A 581       8.031  19.117  28.833  1.00 84.78           C  
ANISOU 4575  CG2 VAL A 581    10148  12939   9125    104    -32  -2251       C  
ATOM   4576  N   ARG A 582      11.548  18.980  26.772  1.00105.03           N  
ANISOU 4576  N   ARG A 582    12187  16544  11176     36    372  -2851       N  
ATOM   4577  CA  ARG A 582      12.122  17.794  26.122  1.00107.37           C  
ANISOU 4577  CA  ARG A 582    12234  16984  11578    176    443  -3348       C  
ATOM   4578  C   ARG A 582      12.781  16.808  27.079  1.00123.55           C  
ANISOU 4578  C   ARG A 582    14141  18694  14107    388    407  -3495       C  
ATOM   4579  O   ARG A 582      12.553  15.599  26.936  1.00113.28           O  
ANISOU 4579  O   ARG A 582    12739  17210  13093    558    353  -3841       O  
ATOM   4580  CB  ARG A 582      13.118  18.244  25.043  1.00128.67           C  
ANISOU 4580  CB  ARG A 582    14766  20253  13869     48    633  -3498       C  
ATOM   4581  CG  ARG A 582      13.992  17.114  24.520  1.00145.67           C  
ANISOU 4581  CG  ARG A 582    16611  22582  16154    209    738  -4033       C  
ATOM   4582  CD  ARG A 582      15.136  17.641  23.653  1.00161.07           C  
ANISOU 4582  CD  ARG A 582    18366  25120  17714     67    958  -4146       C  
ATOM   4583  NE  ARG A 582      16.054  18.495  24.404  1.00164.15           N  
ANISOU 4583  NE  ARG A 582    18738  25517  18114    -33   1018  -3818       N  
ATOM   4584  CZ  ARG A 582      17.149  18.075  25.022  1.00155.63           C  
ANISOU 4584  CZ  ARG A 582    17435  24372  17325     98   1063  -3955       C  
ATOM   4585  NH1 ARG A 582      17.488  16.795  25.035  1.00154.49           N  
ANISOU 4585  NH1 ARG A 582    17070  24106  17523    357   1047  -4398       N  
ATOM   4586  NH2 ARG A 582      17.917  18.961  25.647  1.00146.77           N  
ANISOU 4586  NH2 ARG A 582    16305  23292  16169    -29   1107  -3644       N  
ATOM   4587  N   PRO A 583      13.571  17.242  28.059  1.00122.66           N  
ANISOU 4587  N   PRO A 583    14018  18470  14116    390    414  -3251       N  
ATOM   4588  CA  PRO A 583      14.145  16.288  29.021  1.00102.30           C  
ANISOU 4588  CA  PRO A 583    11318  15551  12000    605    340  -3350       C  
ATOM   4589  C   PRO A 583      13.071  15.512  29.750  1.00107.98           C  
ANISOU 4589  C   PRO A 583    12184  15774  13070    717    172  -3284       C  
ATOM   4590  O   PRO A 583      13.165  14.291  29.862  1.00111.35           O  
ANISOU 4590  O   PRO A 583    12492  15956  13859    906    108  -3556       O  
ATOM   4591  CB  PRO A 583      14.944  17.184  29.985  1.00101.20           C  
ANISOU 4591  CB  PRO A 583    11203  15408  11841    531    349  -3005       C  
ATOM   4592  CG  PRO A 583      15.096  18.511  29.277  1.00110.72           C  
ANISOU 4592  CG  PRO A 583    12469  17023  12578    277    474  -2830       C  
ATOM   4593  CD  PRO A 583      14.112  18.605  28.185  1.00105.70           C  
ANISOU 4593  CD  PRO A 583    11935  16555  11670    189    493  -2915       C  
ATOM   4594  N   LEU A 584      12.037  16.207  30.228  1.00106.22           N  
ANISOU 4594  N   LEU A 584    12210  15396  12753    597    103  -2933       N  
ATOM   4595  CA  LEU A 584      10.908  15.536  30.852  1.00102.01           C  
ANISOU 4595  CA  LEU A 584    11808  14442  12511    662    -32  -2861       C  
ATOM   4596  C   LEU A 584      10.321  14.499  29.902  1.00109.49           C  
ANISOU 4596  C   LEU A 584    12668  15370  13562    733    -54  -3261       C  
ATOM   4597  O   LEU A 584      10.000  13.369  30.297  1.00106.59           O  
ANISOU 4597  O   LEU A 584    12272  14637  13592    863   -150  -3394       O  
ATOM   4598  CB  LEU A 584       9.836  16.543  31.248  1.00 89.62           C  
ANISOU 4598  CB  LEU A 584    10479  12812  10760    511    -74  -2490       C  
ATOM   4599  CG  LEU A 584       8.438  16.038  31.624  1.00 87.79           C  
ANISOU 4599  CG  LEU A 584    10372  12252  10730    521   -183  -2428       C  
ATOM   4600  CD1 LEU A 584       8.520  15.168  32.856  1.00 87.81           C  
ANISOU 4600  CD1 LEU A 584    10380  11841  11144    638   -265  -2334       C  
ATOM   4601  CD2 LEU A 584       7.525  17.205  31.873  1.00 90.86           C  
ANISOU 4601  CD2 LEU A 584    10955  12673  10894    381   -203  -2104       C  
ATOM   4602  N   LEU A 585      10.180  14.872  28.631  1.00104.75           N  
ANISOU 4602  N   LEU A 585    12029  15168  12605    639     27  -3454       N  
ATOM   4603  CA  LEU A 585       9.588  13.961  27.662  1.00106.16           C  
ANISOU 4603  CA  LEU A 585    12125  15379  12834    690      0  -3866       C  
ATOM   4604  C   LEU A 585      10.503  12.772  27.426  1.00113.14           C  
ANISOU 4604  C   LEU A 585    12766  16211  14011    882     27  -4311       C  
ATOM   4605  O   LEU A 585      10.057  11.618  27.431  1.00118.21           O  
ANISOU 4605  O   LEU A 585    13360  16538  15018   1002    -68  -4576       O  
ATOM   4606  CB  LEU A 585       9.303  14.707  26.357  1.00119.71           C  
ANISOU 4606  CB  LEU A 585    13855  17592  14036    536     74  -3950       C  
ATOM   4607  CG  LEU A 585       8.364  15.911  26.451  1.00108.37           C  
ANISOU 4607  CG  LEU A 585    12649  16209  12316    365     23  -3530       C  
ATOM   4608  CD1 LEU A 585       8.340  16.694  25.153  1.00111.60           C  
ANISOU 4608  CD1 LEU A 585    13064  17141  12198    216     91  -3571       C  
ATOM   4609  CD2 LEU A 585       6.975  15.417  26.753  1.00101.75           C  
ANISOU 4609  CD2 LEU A 585    11914  15034  11712    386   -124  -3510       C  
ATOM   4610  N   ASN A 586      11.802  13.041  27.246  1.00109.05           N  
ANISOU 4610  N   ASN A 586    12082  15983  13369    914    151  -4400       N  
ATOM   4611  CA  ASN A 586      12.785  11.970  27.115  1.00109.51           C  
ANISOU 4611  CA  ASN A 586    11879  15991  13738   1127    175  -4822       C  
ATOM   4612  C   ASN A 586      12.703  11.036  28.305  1.00100.21           C  
ANISOU 4612  C   ASN A 586    10729  14212  13132   1305     11  -4728       C  
ATOM   4613  O   ASN A 586      12.794   9.811  28.162  1.00 98.89           O  
ANISOU 4613  O   ASN A 586    10427  13791  13355   1490    -58  -5097       O  
ATOM   4614  CB  ASN A 586      14.196  12.554  27.015  1.00115.48           C  
ANISOU 4614  CB  ASN A 586    12452  17126  14299   1119    327  -4832       C  
ATOM   4615  CG  ASN A 586      15.276  11.483  26.927  1.00140.76           C  
ANISOU 4615  CG  ASN A 586    15348  20287  17849   1368    348  -5279       C  
ATOM   4616  OD1 ASN A 586      15.012  10.352  26.514  1.00145.25           O  
ANISOU 4616  OD1 ASN A 586    15817  20671  18700   1527    289  -5696       O  
ATOM   4617  ND2 ASN A 586      16.496  11.835  27.313  1.00136.70           N  
ANISOU 4617  ND2 ASN A 586    14670  19934  17338   1406    421  -5212       N  
ATOM   4618  N   TYR A 587      12.533  11.600  29.499  1.00102.28           N  
ANISOU 4618  N   TYR A 587    11171  14239  13453   1246    -60  -4231       N  
ATOM   4619  CA  TYR A 587      12.412  10.764  30.684  1.00107.24           C  
ANISOU 4619  CA  TYR A 587    11851  14320  14574   1386   -220  -4073       C  
ATOM   4620  C   TYR A 587      11.246   9.794  30.563  1.00103.59           C  
ANISOU 4620  C   TYR A 587    11467  13491  14402   1409   -332  -4214       C  
ATOM   4621  O   TYR A 587      11.326   8.656  31.037  1.00102.82           O  
ANISOU 4621  O   TYR A 587    11316  12965  14785   1570   -454  -4320       O  
ATOM   4622  CB  TYR A 587      12.263  11.655  31.915  1.00105.24           C  
ANISOU 4622  CB  TYR A 587    11798  13952  14236   1279   -262  -3518       C  
ATOM   4623  CG  TYR A 587      12.185  10.921  33.232  1.00100.79           C  
ANISOU 4623  CG  TYR A 587    11307  12885  14104   1392   -422  -3279       C  
ATOM   4624  CD1 TYR A 587      10.964  10.476  33.722  1.00100.18           C  
ANISOU 4624  CD1 TYR A 587    11405  12444  14216   1338   -520  -3110       C  
ATOM   4625  CD2 TYR A 587      13.321  10.685  33.993  1.00100.52           C  
ANISOU 4625  CD2 TYR A 587    11160  12759  14274   1540   -481  -3203       C  
ATOM   4626  CE1 TYR A 587      10.876   9.812  34.929  1.00 95.75           C  
ANISOU 4626  CE1 TYR A 587    10921  11444  14015   1412   -659  -2850       C  
ATOM   4627  CE2 TYR A 587      13.243  10.021  35.205  1.00102.40           C  
ANISOU 4627  CE2 TYR A 587    11480  12552  14876   1636   -646  -2942       C  
ATOM   4628  CZ  TYR A 587      12.016   9.586  35.669  1.00 90.47           C  
ANISOU 4628  CZ  TYR A 587    10160  10688  13525   1563   -728  -2754       C  
ATOM   4629  OH  TYR A 587      11.927   8.923  36.874  1.00 91.13           O  
ANISOU 4629  OH  TYR A 587    10335  10350  13942   1630   -884  -2459       O  
ATOM   4630  N   PHE A 588      10.161  10.219  29.920  1.00104.27           N  
ANISOU 4630  N   PHE A 588    11670  13730  14218   1244   -307  -4215       N  
ATOM   4631  CA  PHE A 588       8.952   9.415  29.818  1.00101.40           C  
ANISOU 4631  CA  PHE A 588    11377  13045  14104   1224   -413  -4326       C  
ATOM   4632  C   PHE A 588       8.743   8.771  28.454  1.00106.44           C  
ANISOU 4632  C   PHE A 588    11869  13866  14707   1257   -391  -4884       C  
ATOM   4633  O   PHE A 588       7.745   8.066  28.279  1.00110.07           O  
ANISOU 4633  O   PHE A 588    12365  14069  15387   1230   -488  -5028       O  
ATOM   4634  CB  PHE A 588       7.719  10.262  30.157  1.00 89.90           C  
ANISOU 4634  CB  PHE A 588    10143  11591  12425   1026   -433  -3941       C  
ATOM   4635  CG  PHE A 588       7.544  10.544  31.624  1.00 87.00           C  
ANISOU 4635  CG  PHE A 588     9933  10916  12207    996   -489  -3446       C  
ATOM   4636  CD1 PHE A 588       7.102   9.548  32.478  1.00 88.35           C  
ANISOU 4636  CD1 PHE A 588    10147  10592  12832   1046   -605  -3351       C  
ATOM   4637  CD2 PHE A 588       7.779  11.804  32.142  1.00 86.44           C  
ANISOU 4637  CD2 PHE A 588     9971  11053  11817    902   -428  -3077       C  
ATOM   4638  CE1 PHE A 588       6.919   9.796  33.827  1.00 87.81           C  
ANISOU 4638  CE1 PHE A 588    10222  10288  12853   1003   -647  -2893       C  
ATOM   4639  CE2 PHE A 588       7.595  12.055  33.494  1.00 87.56           C  
ANISOU 4639  CE2 PHE A 588    10252  10944  12071    874   -477  -2660       C  
ATOM   4640  CZ  PHE A 588       7.165  11.053  34.334  1.00 85.89           C  
ANISOU 4640  CZ  PHE A 588    10079  10289  12268    922   -581  -2566       C  
ATOM   4641  N   GLU A 589       9.637   8.996  27.489  1.00 99.05           N  
ANISOU 4641  N   GLU A 589    10760  13383  13491   1298   -264  -5210       N  
ATOM   4642  CA  GLU A 589       9.420   8.479  26.139  1.00 99.87           C  
ANISOU 4642  CA  GLU A 589    10727  13745  13476   1310   -230  -5758       C  
ATOM   4643  C   GLU A 589       9.040   7.002  26.094  1.00119.34           C  
ANISOU 4643  C   GLU A 589    13107  15753  16485   1453   -362  -6152       C  
ATOM   4644  O   GLU A 589       8.101   6.663  25.352  1.00134.69           O  
ANISOU 4644  O   GLU A 589    15064  17729  18384   1377   -413  -6415       O  
ATOM   4645  CB  GLU A 589      10.656   8.723  25.260  1.00107.00           C  
ANISOU 4645  CB  GLU A 589    11408  15170  14076   1367    -59  -6090       C  
ATOM   4646  CG  GLU A 589      10.504   8.100  23.878  1.00136.08           C  
ANISOU 4646  CG  GLU A 589    14928  19147  17628   1395    -17  -6714       C  
ATOM   4647  CD  GLU A 589      11.522   8.585  22.872  1.00168.64           C  
ANISOU 4647  CD  GLU A 589    18858  23928  21290   1376    188  -6993       C  
ATOM   4648  OE1 GLU A 589      12.284   9.520  23.192  1.00178.26           O  
ANISOU 4648  OE1 GLU A 589    20082  25391  22259   1306    301  -6663       O  
ATOM   4649  OE2 GLU A 589      11.567   8.015  21.759  1.00161.91           O1-
ANISOU 4649  OE2 GLU A 589    17837  23359  20322   1421    241  -7558       O1-
ATOM   4650  N   PRO A 590       9.690   6.089  26.831  1.00111.33           N  
ANISOU 4650  N   PRO A 590    12006  14297  15999   1652   -441  -6210       N  
ATOM   4651  CA  PRO A 590       9.232   4.693  26.799  1.00122.27           C  
ANISOU 4651  CA  PRO A 590    13335  15180  17941   1767   -588  -6554       C  
ATOM   4652  C   PRO A 590       7.813   4.509  27.319  1.00117.86           C  
ANISOU 4652  C   PRO A 590    12982  14238  17562   1606   -717  -6267       C  
ATOM   4653  O   PRO A 590       7.132   3.564  26.901  1.00103.60           O  
ANISOU 4653  O   PRO A 590    11137  12164  16064   1610   -816  -6610       O  
ATOM   4654  CB  PRO A 590      10.252   3.974  27.687  1.00111.38           C  
ANISOU 4654  CB  PRO A 590    11860  13391  17066   2003   -665  -6511       C  
ATOM   4655  CG  PRO A 590      11.481   4.787  27.595  1.00106.45           C  
ANISOU 4655  CG  PRO A 590    11112  13231  16102   2059   -516  -6469       C  
ATOM   4656  CD  PRO A 590      10.987   6.209  27.526  1.00103.72           C  
ANISOU 4656  CD  PRO A 590    10945  13312  15152   1801   -405  -6064       C  
ATOM   4657  N   LEU A 591       7.351   5.361  28.241  1.00109.40           N  
ANISOU 4657  N   LEU A 591    12113  13125  16327   1461   -716  -5669       N  
ATOM   4658  CA  LEU A 591       5.942   5.319  28.616  1.00109.16           C  
ANISOU 4658  CA  LEU A 591    12247  12840  16387   1284   -804  -5425       C  
ATOM   4659  C   LEU A 591       5.079   5.981  27.556  1.00119.71           C  
ANISOU 4659  C   LEU A 591    13602  14618  17264   1121   -757  -5576       C  
ATOM   4660  O   LEU A 591       3.927   5.581  27.357  1.00124.38           O  
ANISOU 4660  O   LEU A 591    14227  15043  17986   1011   -846  -5661       O  
ATOM   4661  CB  LEU A 591       5.716   5.980  29.978  1.00104.10           C  
ANISOU 4661  CB  LEU A 591    11798  12024  15730   1195   -813  -4773       C  
ATOM   4662  CG  LEU A 591       4.268   5.957  30.495  1.00 99.87           C  
ANISOU 4662  CG  LEU A 591    11411  11237  15297   1008   -882  -4494       C  
ATOM   4663  CD1 LEU A 591       3.778   4.534  30.708  1.00117.26           C  
ANISOU 4663  CD1 LEU A 591    13578  12884  18092   1031  -1016  -4669       C  
ATOM   4664  CD2 LEU A 591       4.130   6.740  31.787  1.00 95.09           C  
ANISOU 4664  CD2 LEU A 591    10979  10561  14591    924   -859  -3890       C  
ATOM   4665  N   PHE A 592       5.628   6.975  26.851  1.00120.09           N  
ANISOU 4665  N   PHE A 592    13618  15230  16778   1096   -629  -5608       N  
ATOM   4666  CA  PHE A 592       4.871   7.653  25.805  1.00120.84           C  
ANISOU 4666  CA  PHE A 592    13738  15776  16400    946   -604  -5717       C  
ATOM   4667  C   PHE A 592       4.538   6.707  24.656  1.00106.57           C  
ANISOU 4667  C   PHE A 592    11779  14034  14678    979   -657  -6340       C  
ATOM   4668  O   PHE A 592       3.426   6.745  24.118  1.00113.41           O  
ANISOU 4668  O   PHE A 592    12681  14988  15422    853   -734  -6430       O  
ATOM   4669  CB  PHE A 592       5.652   8.864  25.292  1.00125.78           C  
ANISOU 4669  CB  PHE A 592    14362  16975  16452    904   -457  -5600       C  
ATOM   4670  CG  PHE A 592       4.889   9.699  24.305  1.00121.43           C  
ANISOU 4670  CG  PHE A 592    13869  16885  15382    744   -452  -5601       C  
ATOM   4671  CD1 PHE A 592       3.553   9.996  24.518  1.00110.73           C  
ANISOU 4671  CD1 PHE A 592    12649  15402  14021    620   -563  -5364       C  
ATOM   4672  CD2 PHE A 592       5.502  10.177  23.159  1.00120.92           C  
ANISOU 4672  CD2 PHE A 592    13715  17397  14833    716   -340  -5834       C  
ATOM   4673  CE1 PHE A 592       2.843  10.760  23.609  1.00104.64           C  
ANISOU 4673  CE1 PHE A 592    11924  15045  12788    493   -591  -5353       C  
ATOM   4674  CE2 PHE A 592       4.798  10.942  22.245  1.00117.33           C  
ANISOU 4674  CE2 PHE A 592    13327  17368  13885    567   -360  -5797       C  
ATOM   4675  CZ  PHE A 592       3.467  11.233  22.471  1.00109.26           C  
ANISOU 4675  CZ  PHE A 592    12442  16189  12882    467   -499  -5555       C  
ATOM   4676  N   THR A 593       5.484   5.852  24.263  1.00 94.53           N  
ANISOU 4676  N   THR A 593    10070  12475  13370   1155   -626  -6803       N  
ATOM   4677  CA  THR A 593       5.211   4.915  23.177  1.00111.52           C  
ANISOU 4677  CA  THR A 593    12066  14684  15622   1198   -677  -7457       C  
ATOM   4678  C   THR A 593       4.400   3.713  23.646  1.00118.02           C  
ANISOU 4678  C   THR A 593    12900  14859  17082   1211   -851  -7583       C  
ATOM   4679  O   THR A 593       3.641   3.142  22.857  1.00126.13           O  
ANISOU 4679  O   THR A 593    13862  15899  18162   1154   -936  -8002       O  
ATOM   4680  CB  THR A 593       6.515   4.449  22.532  1.00102.49           C  
ANISOU 4680  CB  THR A 593    10697  13767  14479   1391   -569  -7965       C  
ATOM   4681  OG1 THR A 593       7.392   3.930  23.539  1.00112.67           O  
ANISOU 4681  OG1 THR A 593    11944  14609  16255   1575   -586  -7834       O  
ATOM   4682  CG2 THR A 593       7.194   5.606  21.818  1.00101.73           C  
ANISOU 4682  CG2 THR A 593    10567  14396  13692   1323   -384  -7909       C  
ATOM   4683  N   TRP A 594       4.549   3.310  24.911  1.00114.47           N  
ANISOU 4683  N   TRP A 594    12529  13849  17115   1271   -913  -7226       N  
ATOM   4684  CA  TRP A 594       3.675   2.276  25.454  1.00117.85           C  
ANISOU 4684  CA  TRP A 594    12999  13651  18128   1228  -1075  -7228       C  
ATOM   4685  C   TRP A 594       2.250   2.791  25.595  1.00120.19           C  
ANISOU 4685  C   TRP A 594    13433  13979  18257    984  -1124  -6921       C  
ATOM   4686  O   TRP A 594       1.289   2.054  25.342  1.00120.82           O  
ANISOU 4686  O   TRP A 594    13482  13804  18620    889  -1241  -7153       O  
ATOM   4687  CB  TRP A 594       4.203   1.783  26.800  1.00123.42           C  
ANISOU 4687  CB  TRP A 594    13771  13788  19337   1336  -1131  -6854       C  
ATOM   4688  CG  TRP A 594       3.353   0.710  27.417  1.00120.62           C  
ANISOU 4688  CG  TRP A 594    13470  12766  19594   1268  -1292  -6796       C  
ATOM   4689  CD1 TRP A 594       3.464  -0.636  27.222  1.00118.98           C  
ANISOU 4689  CD1 TRP A 594    13152  12079  19976   1382  -1419  -7222       C  
ATOM   4690  CD2 TRP A 594       2.263   0.894  28.329  1.00113.48           C  
ANISOU 4690  CD2 TRP A 594    12733  11598  18784   1056  -1339  -6281       C  
ATOM   4691  NE1 TRP A 594       2.511  -1.301  27.954  1.00111.06           N  
ANISOU 4691  NE1 TRP A 594    12251  10514  19433   1234  -1546  -6974       N  
ATOM   4692  CE2 TRP A 594       1.762  -0.385  28.644  1.00107.80           C  
ANISOU 4692  CE2 TRP A 594    12000  10247  18710   1028  -1488  -6397       C  
ATOM   4693  CE3 TRP A 594       1.662   2.016  28.911  1.00105.76           C  
ANISOU 4693  CE3 TRP A 594    11906  10857  17420    887  -1266  -5748       C  
ATOM   4694  CZ2 TRP A 594       0.690  -0.574  29.514  1.00109.94           C  
ANISOU 4694  CZ2 TRP A 594    12397  10153  19222    813  -1548  -5979       C  
ATOM   4695  CZ3 TRP A 594       0.598   1.826  29.774  1.00106.52           C  
ANISOU 4695  CZ3 TRP A 594    12114  10604  17755    700  -1324  -5372       C  
ATOM   4696  CH2 TRP A 594       0.122   0.542  30.066  1.00115.33           C  
ANISOU 4696  CH2 TRP A 594    13206  11127  19486    654  -1455  -5479       C  
ATOM   4697  N   LEU A 595       2.093   4.055  26.002  1.00115.09           N  
ANISOU 4697  N   LEU A 595    12923  13635  17173    882  -1042  -6418       N  
ATOM   4698  CA  LEU A 595       0.769   4.667  26.007  1.00112.18           C  
ANISOU 4698  CA  LEU A 595    12652  13379  16594    676  -1083  -6172       C  
ATOM   4699  C   LEU A 595       0.206   4.790  24.598  1.00113.16           C  
ANISOU 4699  C   LEU A 595    12681  13946  16368    608  -1116  -6615       C  
ATOM   4700  O   LEU A 595      -1.008   4.660  24.407  1.00120.56           O  
ANISOU 4700  O   LEU A 595    13620  14829  17359    464  -1218  -6653       O  
ATOM   4701  CB  LEU A 595       0.819   6.042  26.682  1.00107.69           C  
ANISOU 4701  CB  LEU A 595    12237  13049  15631    612   -992  -5587       C  
ATOM   4702  CG  LEU A 595       0.890   6.067  28.212  1.00101.79           C  
ANISOU 4702  CG  LEU A 595    11616  11885  15173    606   -985  -5060       C  
ATOM   4703  CD1 LEU A 595       1.080   7.489  28.718  1.00 93.14           C  
ANISOU 4703  CD1 LEU A 595    10651  11092  13644    561   -889  -4584       C  
ATOM   4704  CD2 LEU A 595      -0.338   5.429  28.843  1.00100.64           C  
ANISOU 4704  CD2 LEU A 595    11509  11311  15420    466  -1082  -4922       C  
ATOM   4705  N   LYS A 596       1.061   5.036  23.602  1.00107.05           N  
ANISOU 4705  N   LYS A 596    11812  13639  15223    700  -1032  -6954       N  
ATOM   4706  CA  LYS A 596       0.619   5.089  22.211  1.00117.05           C  
ANISOU 4706  CA  LYS A 596    12984  15373  16118    640  -1067  -7407       C  
ATOM   4707  C   LYS A 596       0.412   3.708  21.600  1.00135.94           C  
ANISOU 4707  C   LYS A 596    15215  17523  18914    691  -1172  -8059       C  
ATOM   4708  O   LYS A 596       0.205   3.607  20.388  1.00150.99           O  
ANISOU 4708  O   LYS A 596    17014  19834  20519    665  -1200  -8536       O  
ATOM   4709  CB  LYS A 596       1.614   5.873  21.345  1.00105.31           C  
ANISOU 4709  CB  LYS A 596    11451  14525  14039    692   -922  -7524       C  
ATOM   4710  CG  LYS A 596       1.561   7.380  21.511  1.00 98.92           C  
ANISOU 4710  CG  LYS A 596    10796  14084  12704    587   -851  -6968       C  
ATOM   4711  CD  LYS A 596       2.382   8.073  20.434  1.00104.35           C  
ANISOU 4711  CD  LYS A 596    11426  15442  12781    587   -722  -7132       C  
ATOM   4712  CE  LYS A 596       3.876   7.909  20.641  1.00117.27           C  
ANISOU 4712  CE  LYS A 596    12964  17107  14486    732   -560  -7231       C  
ATOM   4713  NZ  LYS A 596       4.627   8.520  19.508  1.00115.76           N  
ANISOU 4713  NZ  LYS A 596    12689  17612  13684    699   -416  -7430       N  
ATOM   4714  N   ASP A 597       0.486   2.646  22.401  1.00132.57           N  
ANISOU 4714  N   ASP A 597    14769  16445  19155    761  -1238  -8094       N  
ATOM   4715  CA  ASP A 597       0.167   1.303  21.935  1.00132.00           C  
ANISOU 4715  CA  ASP A 597    14561  16032  19562    791  -1365  -8682       C  
ATOM   4716  C   ASP A 597      -0.892   0.679  22.838  1.00132.05           C  
ANISOU 4716  C   ASP A 597    14639  15411  20122    652  -1500  -8426       C  
ATOM   4717  O   ASP A 597      -1.266  -0.482  22.644  1.00135.12           O  
ANISOU 4717  O   ASP A 597    14933  15430  20976    640  -1606  -8714       O  
ATOM   4718  CB  ASP A 597       1.453   0.457  21.854  1.00125.45           C  
ANISOU 4718  CB  ASP A 597    13597  15038  19031   1025  -1307  -8949       C  
ATOM   4719  CG  ASP A 597       1.215  -0.974  21.382  1.00142.76           C  
ANISOU 4719  CG  ASP A 597    15637  16900  21705   1061  -1415  -9319       C  
ATOM   4720  OD1 ASP A 597       0.943  -1.864  22.219  1.00155.26           O  
ANISOU 4720  OD1 ASP A 597    17256  17812  23922   1060  -1527  -9192       O  
ATOM   4721  OD2 ASP A 597       1.296  -1.205  20.159  1.00149.65           O1-
ANISOU 4721  OD2 ASP A 597    16356  18193  22312   1080  -1390  -9725       O1-
ATOM   4722  N   GLN A 598      -1.408   1.449  23.797  1.00129.82           N  
ANISOU 4722  N   GLN A 598    14513  15063  19750    531  -1473  -7770       N  
ATOM   4723  CA  GLN A 598      -2.525   1.049  24.638  1.00127.55           C  
ANISOU 4723  CA  GLN A 598    14287  14299  19877    355  -1569  -7474       C  
ATOM   4724  C   GLN A 598      -3.812   1.779  24.282  1.00114.95           C  
ANISOU 4724  C   GLN A 598    12701  13037  17937    153  -1612  -7355       C  
ATOM   4725  O   GLN A 598      -4.886   1.357  24.721  1.00119.51           O  
ANISOU 4725  O   GLN A 598    13271  13290  18849    -18  -1699  -7246       O  
ATOM   4726  CB  GLN A 598      -2.192   1.314  26.114  1.00116.41           C  
ANISOU 4726  CB  GLN A 598    13029  12549  18652    366  -1503  -6818       C  
ATOM   4727  CG  GLN A 598      -1.263   0.293  26.760  1.00114.79           C  
ANISOU 4727  CG  GLN A 598    12817  11796  19000    526  -1532  -6853       C  
ATOM   4728  CD  GLN A 598      -1.928  -1.034  27.051  1.00120.49           C  
ANISOU 4728  CD  GLN A 598    13503  11870  20409    433  -1679  -7005       C  
ATOM   4729  OE1 GLN A 598      -3.050  -1.081  27.552  1.00123.93           O  
ANISOU 4729  OE1 GLN A 598    13988  12111  20990    210  -1720  -6732       O  
ATOM   4730  NE2 GLN A 598      -1.228  -2.125  26.758  1.00111.81           N  
ANISOU 4730  NE2 GLN A 598    12307  10418  19759    600  -1757  -7442       N  
ATOM   4731  N   ASN A 599      -3.725   2.858  23.498  1.00110.11           N  
ANISOU 4731  N   ASN A 599    12097  13064  16678    166  -1559  -7365       N  
ATOM   4732  CA  ASN A 599      -4.857   3.721  23.181  1.00137.27           C  
ANISOU 4732  CA  ASN A 599    15554  16857  19748     11  -1614  -7191       C  
ATOM   4733  C   ASN A 599      -5.177   3.713  21.691  1.00138.58           C  
ANISOU 4733  C   ASN A 599    15594  17508  19551     -9  -1706  -7728       C  
ATOM   4734  O   ASN A 599      -5.867   4.617  21.203  1.00124.28           O  
ANISOU 4734  O   ASN A 599    13798  16130  17292    -91  -1756  -7600       O  
ATOM   4735  CB  ASN A 599      -4.579   5.150  23.654  1.00127.43           C  
ANISOU 4735  CB  ASN A 599    14454  15926  18037     30  -1500  -6628       C  
ATOM   4736  CG  ASN A 599      -4.359   5.238  25.153  1.00119.03           C  
ANISOU 4736  CG  ASN A 599    13514  14438  17273     33  -1418  -6092       C  
ATOM   4737  OD1 ASN A 599      -4.849   4.406  25.916  1.00118.58           O  
ANISOU 4737  OD1 ASN A 599    13446  13881  17727    -42  -1463  -6018       O  
ATOM   4738  ND2 ASN A 599      -3.604   6.245  25.581  1.00108.00           N  
ANISOU 4738  ND2 ASN A 599    12236  13249  15553    107  -1299  -5714       N  
ATOM   4739  N   LYS A 600      -4.675   2.714  20.959  1.00136.21           N  
ANISOU 4739  N   LYS A 600    15168  17151  19434     74  -1740  -8337       N  
ATOM   4740  CA  LYS A 600      -4.898   2.652  19.518  1.00130.46           C  
ANISOU 4740  CA  LYS A 600    14318  16931  18318     66  -1796  -8785       C  
ATOM   4741  C   LYS A 600      -6.384   2.666  19.188  1.00131.19           C  
ANISOU 4741  C   LYS A 600    14355  17092  18400   -115  -1960  -8794       C  
ATOM   4742  O   LYS A 600      -6.823   3.391  18.288  1.00145.51           O  
ANISOU 4742  O   LYS A 600    16152  19464  19673   -159  -2012  -8813       O  
ATOM   4743  CB  LYS A 600      -4.231   1.400  18.945  1.00135.53           C  
ANISOU 4743  CB  LYS A 600    14819  17412  19262    194  -1763  -9216       C  
ATOM   4744  CG  LYS A 600      -4.079   1.383  17.430  1.00137.69           C  
ANISOU 4744  CG  LYS A 600    14968  18286  19062    231  -1746  -9591       C  
ATOM   4745  CD  LYS A 600      -3.851   2.774  16.857  1.00142.73           C  
ANISOU 4745  CD  LYS A 600    15686  19617  18927    212  -1677  -9391       C  
ATOM   4746  CE  LYS A 600      -3.484   2.699  15.385  1.00145.59           C  
ANISOU 4746  CE  LYS A 600    15925  20563  18828    253  -1629  -9739       C  
ATOM   4747  NZ  LYS A 600      -3.874   3.935  14.656  1.00148.11           N  
ANISOU 4747  NZ  LYS A 600    16320  21527  18427    158  -1650  -9518       N  
ATOM   4748  N   ASN A 601      -7.174   1.876  19.914  1.00123.54           N  
ANISOU 4748  N   ASN A 601    13351  15561  18028   -228  -2046  -8755       N  
ATOM   4749  CA  ASN A 601      -8.617   1.801  19.730  1.00119.84           C  
ANISOU 4749  CA  ASN A 601    12797  15101  17634   -413  -2196  -8760       C  
ATOM   4750  C   ASN A 601      -9.364   2.564  20.815  1.00117.84           C  
ANISOU 4750  C   ASN A 601    12620  14695  17458   -548  -2220  -8285       C  
ATOM   4751  O   ASN A 601     -10.451   2.156  21.240  1.00116.52           O  
ANISOU 4751  O   ASN A 601    12374  14235  17664   -720  -2310  -8228       O  
ATOM   4752  CB  ASN A 601      -9.062   0.339  19.674  1.00117.65           C  
ANISOU 4752  CB  ASN A 601    12396  14348  17957   -473  -2263  -9042       C  
ATOM   4753  CG  ASN A 601      -8.427  -0.408  18.522  1.00122.29           C  
ANISOU 4753  CG  ASN A 601    12879  15129  18456   -336  -2245  -9519       C  
ATOM   4754  OD1 ASN A 601      -8.237   0.148  17.439  1.00123.22           O  
ANISOU 4754  OD1 ASN A 601    12966  15854  17999   -277  -2236  -9690       O  
ATOM   4755  ND2 ASN A 601      -8.078  -1.665  18.752  1.00131.50           N  
ANISOU 4755  ND2 ASN A 601    13989  15784  20191   -287  -2243  -9720       N  
ATOM   4756  N   SER A 602      -8.780   3.667  21.273  1.00108.42           N  
ANISOU 4756  N   SER A 602    11580  13719  15894   -454  -2083  -7790       N  
ATOM   4757  CA  SER A 602      -9.359   4.530  22.292  1.00114.98           C  
ANISOU 4757  CA  SER A 602    12506  14482  16700   -521  -2030  -7164       C  
ATOM   4758  C   SER A 602      -9.221   5.980  21.851  1.00110.71           C  
ANISOU 4758  C   SER A 602    12055  14520  15491   -452  -2006  -6894       C  
ATOM   4759  O   SER A 602      -8.287   6.332  21.129  1.00121.69           O  
ANISOU 4759  O   SER A 602    13491  16267  16479   -338  -1955  -7034       O  
ATOM   4760  CB  SER A 602      -8.673   4.335  23.649  1.00129.28           C  
ANISOU 4760  CB  SER A 602    14444  15814  18862   -476  -1876  -6753       C  
ATOM   4761  OG  SER A 602      -8.739   2.986  24.073  1.00136.83           O  
ANISOU 4761  OG  SER A 602    15338  16199  20453   -538  -1911  -6957       O  
ATOM   4762  N   PHE A 603     -10.157   6.821  22.283  1.00 96.11           N  
ANISOU 4762  N   PHE A 603    10222  12760  13534   -526  -2043  -6506       N  
ATOM   4763  CA  PHE A 603     -10.174   8.217  21.861  1.00 94.09           C  
ANISOU 4763  CA  PHE A 603    10050  13004  12695   -467  -2060  -6232       C  
ATOM   4764  C   PHE A 603      -9.156   8.985  22.687  1.00 95.38           C  
ANISOU 4764  C   PHE A 603    10401  13110  12727   -366  -1873  -5775       C  
ATOM   4765  O   PHE A 603      -9.231   8.963  23.916  1.00 98.03           O  
ANISOU 4765  O   PHE A 603    10795  13074  13380   -389  -1777  -5435       O  
ATOM   4766  CB  PHE A 603     -11.576   8.815  22.021  1.00 93.64           C  
ANISOU 4766  CB  PHE A 603     9917  13038  12623   -559  -2188  -6021       C  
ATOM   4767  CG  PHE A 603     -11.698  10.205  21.448  1.00 96.10           C  
ANISOU 4767  CG  PHE A 603    10304  13846  12363   -490  -2260  -5776       C  
ATOM   4768  CD1 PHE A 603     -11.172  10.498  20.210  1.00107.19           C  
ANISOU 4768  CD1 PHE A 603    11734  15719  13273   -434  -2326  -6000       C  
ATOM   4769  CD2 PHE A 603     -12.283  11.230  22.183  1.00 94.45           C  
ANISOU 4769  CD2 PHE A 603    10146  13626  12113   -479  -2252  -5307       C  
ATOM   4770  CE1 PHE A 603     -11.237  11.774  19.687  1.00118.28           C  
ANISOU 4770  CE1 PHE A 603    13230  17555  14158   -383  -2401  -5726       C  
ATOM   4771  CE2 PHE A 603     -12.351  12.523  21.659  1.00 98.95           C  
ANISOU 4771  CE2 PHE A 603    10800  14602  12194   -404  -2336  -5063       C  
ATOM   4772  CZ  PHE A 603     -11.822  12.787  20.404  1.00116.97           C  
ANISOU 4772  CZ  PHE A 603    13123  17329  13992   -363  -2417  -5252       C  
ATOM   4773  N   VAL A 604      -8.177   9.611  22.034  1.00 90.56           N  
ANISOU 4773  N   VAL A 604     9878  12872  11658   -268  -1816  -5780       N  
ATOM   4774  CA  VAL A 604      -7.178  10.439  22.697  1.00109.91           C  
ANISOU 4774  CA  VAL A 604    12494  15326  13939   -185  -1652  -5368       C  
ATOM   4775  C   VAL A 604      -7.603  11.881  22.508  1.00108.71           C  
ANISOU 4775  C   VAL A 604    12434  15524  13349   -189  -1705  -4999       C  
ATOM   4776  O   VAL A 604      -7.529  12.417  21.396  1.00103.65           O  
ANISOU 4776  O   VAL A 604    11797  15342  12243   -182  -1783  -5104       O  
ATOM   4777  CB  VAL A 604      -5.766  10.189  22.151  1.00112.96           C  
ANISOU 4777  CB  VAL A 604    12898  15880  14142    -91  -1539  -5604       C  
ATOM   4778  CG1 VAL A 604      -4.792  11.230  22.723  1.00 92.47           C  
ANISOU 4778  CG1 VAL A 604    10460  13370  11306    -29  -1388  -5162       C  
ATOM   4779  CG2 VAL A 604      -5.302   8.759  22.522  1.00116.37           C  
ANISOU 4779  CG2 VAL A 604    13244  15870  15102    -53  -1495  -5933       C  
ATOM   4780  N   GLY A 605      -8.050  12.501  23.589  1.00106.87           N  
ANISOU 4780  N   GLY A 605    12272  15073  13262   -200  -1668  -4570       N  
ATOM   4781  CA  GLY A 605      -8.673  13.808  23.528  1.00 94.40           C  
ANISOU 4781  CA  GLY A 605    10756  13731  11380   -194  -1749  -4235       C  
ATOM   4782  C   GLY A 605      -9.848  13.865  24.482  1.00100.34           C  
ANISOU 4782  C   GLY A 605    11447  14210  12468   -242  -1783  -4037       C  
ATOM   4783  O   GLY A 605     -10.172  12.902  25.175  1.00116.98           O  
ANISOU 4783  O   GLY A 605    13470  15963  15012   -307  -1736  -4132       O  
ATOM   4784  N   TRP A 606     -10.482  15.034  24.509  1.00 90.75           N  
ANISOU 4784  N   TRP A 606    10269  13169  11045   -213  -1865  -3752       N  
ATOM   4785  CA  TRP A 606     -11.675  15.231  25.320  1.00100.99           C  
ANISOU 4785  CA  TRP A 606    11475  14286  12612   -245  -1901  -3587       C  
ATOM   4786  C   TRP A 606     -12.607  16.210  24.618  1.00112.77           C  
ANISOU 4786  C   TRP A 606    12916  16093  13839   -202  -2107  -3511       C  
ATOM   4787  O   TRP A 606     -12.178  17.077  23.856  1.00122.85           O  
ANISOU 4787  O   TRP A 606    14306  17669  14703   -136  -2183  -3401       O  
ATOM   4788  CB  TRP A 606     -11.343  15.751  26.733  1.00105.12           C  
ANISOU 4788  CB  TRP A 606    12115  14543  13284   -218  -1723  -3202       C  
ATOM   4789  CG  TRP A 606     -10.316  16.845  26.795  1.00107.21           C  
ANISOU 4789  CG  TRP A 606    12582  14932  13222   -128  -1652  -2919       C  
ATOM   4790  CD1 TRP A 606     -10.529  18.168  26.544  1.00103.26           C  
ANISOU 4790  CD1 TRP A 606    12161  14638  12435    -60  -1740  -2676       C  
ATOM   4791  CD2 TRP A 606      -8.921  16.714  27.109  1.00 99.20           C  
ANISOU 4791  CD2 TRP A 606    11702  13834  12154   -105  -1494  -2854       C  
ATOM   4792  NE1 TRP A 606      -9.362  18.871  26.713  1.00103.35           N  
ANISOU 4792  NE1 TRP A 606    12356  14684  12228    -18  -1635  -2455       N  
ATOM   4793  CE2 TRP A 606      -8.360  18.003  27.051  1.00 97.98           C  
ANISOU 4793  CE2 TRP A 606    11701  13850  11675    -45  -1481  -2568       C  
ATOM   4794  CE3 TRP A 606      -8.092  15.633  27.436  1.00 86.89           C  
ANISOU 4794  CE3 TRP A 606    10139  12061  10815   -124  -1375  -3010       C  
ATOM   4795  CZ2 TRP A 606      -7.016  18.245  27.306  1.00 94.25           C  
ANISOU 4795  CZ2 TRP A 606    11362  13369  11080    -22  -1343  -2445       C  
ATOM   4796  CZ3 TRP A 606      -6.750  15.878  27.690  1.00 94.37           C  
ANISOU 4796  CZ3 TRP A 606    11214  13005  11637    -74  -1248  -2888       C  
ATOM   4797  CH2 TRP A 606      -6.229  17.174  27.623  1.00100.43           C  
ANISOU 4797  CH2 TRP A 606    12118  13974  12068    -32  -1228  -2614       C  
ATOM   4798  N   SER A 607     -13.897  16.062  24.901  1.00101.60           N  
ANISOU 4798  N   SER A 607    11321  14605  12676   -244  -2200  -3554       N  
ATOM   4799  CA  SER A 607     -14.938  16.963  24.444  1.00 96.00           C  
ANISOU 4799  CA  SER A 607    10525  14138  11813   -183  -2408  -3466       C  
ATOM   4800  C   SER A 607     -15.355  17.861  25.591  1.00103.93           C  
ANISOU 4800  C   SER A 607    11552  14975  12961   -119  -2327  -3115       C  
ATOM   4801  O   SER A 607     -15.697  17.371  26.672  1.00103.16           O  
ANISOU 4801  O   SER A 607    11374  14602  13222   -188  -2178  -3086       O  
ATOM   4802  CB  SER A 607     -16.138  16.150  23.936  1.00106.91           C  
ANISOU 4802  CB  SER A 607    11640  15581  13398   -273  -2579  -3810       C  
ATOM   4803  OG  SER A 607     -17.193  16.998  23.533  1.00108.91           O  
ANISOU 4803  OG  SER A 607    11778  16067  13534   -198  -2801  -3729       O  
ATOM   4804  N   THR A 608     -15.327  19.168  25.336  1.00110.93           N  
ANISOU 4804  N   THR A 608    12548  16035  13565      7  -2429  -2854       N  
ATOM   4805  CA  THR A 608     -15.589  20.150  26.376  1.00110.15           C  
ANISOU 4805  CA  THR A 608    12493  15784  13573     94  -2356  -2541       C  
ATOM   4806  C   THR A 608     -16.998  20.014  26.932  1.00122.57           C  
ANISOU 4806  C   THR A 608    13808  17286  15476     83  -2400  -2614       C  
ATOM   4807  O   THR A 608     -17.214  20.182  28.138  1.00135.36           O  
ANISOU 4807  O   THR A 608    15403  18699  17330     82  -2232  -2475       O  
ATOM   4808  CB  THR A 608     -15.367  21.563  25.822  1.00117.67           C  
ANISOU 4808  CB  THR A 608    13602  16924  14183    231  -2507  -2277       C  
ATOM   4809  OG1 THR A 608     -16.272  21.806  24.735  1.00126.08           O  
ANISOU 4809  OG1 THR A 608    14538  18264  15103    281  -2799  -2377       O  
ATOM   4810  CG2 THR A 608     -13.940  21.726  25.325  1.00 97.76           C  
ANISOU 4810  CG2 THR A 608    11321  14493  11332    211  -2431  -2186       C  
ATOM   4811  N   ASP A 609     -17.971  19.689  26.076  1.00121.05           N  
ANISOU 4811  N   ASP A 609    13406  17288  15301     65  -2620  -2847       N  
ATOM   4812  CA  ASP A 609     -19.369  19.856  26.465  1.00116.49           C  
ANISOU 4812  CA  ASP A 609    12559  16714  14990     87  -2705  -2890       C  
ATOM   4813  C   ASP A 609     -19.844  18.773  27.429  1.00119.68           C  
ANISOU 4813  C   ASP A 609    12781  16884  15809    -84  -2504  -3031       C  
ATOM   4814  O   ASP A 609     -20.637  19.066  28.331  1.00140.91           O  
ANISOU 4814  O   ASP A 609    15314  19493  18732    -74  -2423  -2949       O  
ATOM   4815  CB  ASP A 609     -20.273  19.911  25.234  1.00137.75           C  
ANISOU 4815  CB  ASP A 609    15066  19711  17561    126  -3033  -3085       C  
ATOM   4816  CG  ASP A 609     -19.629  20.632  24.070  1.00146.19           C  
ANISOU 4816  CG  ASP A 609    16340  21041  18164    230  -3230  -2978       C  
ATOM   4817  OD1 ASP A 609     -19.321  21.831  24.227  1.00144.96           O  
ANISOU 4817  OD1 ASP A 609    16352  20881  17844    374  -3258  -2660       O  
ATOM   4818  OD2 ASP A 609     -19.456  20.016  22.996  1.00149.90           O1-
ANISOU 4818  OD2 ASP A 609    16798  21726  18430    160  -3360  -3214       O1-
ATOM   4819  N   TRP A 610     -19.403  17.521  27.257  1.00100.34           N  
ANISOU 4819  N   TRP A 610    10336  14321  13466   -246  -2424  -3245       N  
ATOM   4820  CA  TRP A 610     -19.935  16.454  28.104  1.00101.38           C  
ANISOU 4820  CA  TRP A 610    10291  14216  14015   -435  -2263  -3357       C  
ATOM   4821  C   TRP A 610     -19.744  16.794  29.572  1.00104.83           C  
ANISOU 4821  C   TRP A 610    10803  14436  14592   -438  -2000  -3066       C  
ATOM   4822  O   TRP A 610     -18.654  17.183  30.002  1.00111.12           O  
ANISOU 4822  O   TRP A 610    11857  15135  15229   -370  -1869  -2852       O  
ATOM   4823  CB  TRP A 610     -19.288  15.097  27.823  1.00 93.73           C  
ANISOU 4823  CB  TRP A 610     9369  13075  13170   -591  -2203  -3587       C  
ATOM   4824  CG  TRP A 610     -19.904  14.030  28.718  1.00 94.50           C  
ANISOU 4824  CG  TRP A 610     9288  12895  13724   -806  -2053  -3655       C  
ATOM   4825  CD1 TRP A 610     -21.076  13.359  28.507  1.00103.36           C  
ANISOU 4825  CD1 TRP A 610    10112  14034  15127   -960  -2148  -3900       C  
ATOM   4826  CD2 TRP A 610     -19.413  13.580  29.993  1.00103.74           C  
ANISOU 4826  CD2 TRP A 610    10563  13746  15110   -905  -1787  -3440       C  
ATOM   4827  NE1 TRP A 610     -21.326  12.497  29.549  1.00105.48           N  
ANISOU 4827  NE1 TRP A 610    10298  14000  15778  -1166  -1945  -3842       N  
ATOM   4828  CE2 TRP A 610     -20.323  12.616  30.475  1.00115.56           C  
ANISOU 4828  CE2 TRP A 610    11827  15071  17010  -1131  -1727  -3550       C  
ATOM   4829  CE3 TRP A 610     -18.287  13.887  30.763  1.00 97.39           C  
ANISOU 4829  CE3 TRP A 610    10021  12793  14190   -835  -1605  -3162       C  
ATOM   4830  CZ2 TRP A 610     -20.138  11.955  31.691  1.00115.97           C  
ANISOU 4830  CZ2 TRP A 610    11919  14812  17332  -1292  -1491  -3358       C  
ATOM   4831  CZ3 TRP A 610     -18.107  13.230  31.970  1.00 98.00           C  
ANISOU 4831  CZ3 TRP A 610    10131  12574  14531   -975  -1387  -2993       C  
ATOM   4832  CH2 TRP A 610     -19.028  12.277  32.422  1.00 94.19           C  
ANISOU 4832  CH2 TRP A 610     9431  11927  14429  -1202  -1331  -3076       C  
ATOM   4833  N   SER A 611     -20.823  16.650  30.334  1.00 96.42           N  
ANISOU 4833  N   SER A 611     9495  13325  13813   -526  -1924  -3071       N  
ATOM   4834  CA  SER A 611     -20.852  16.946  31.743  1.00 91.09           C  
ANISOU 4834  CA  SER A 611     8840  12506  13263   -549  -1674  -2831       C  
ATOM   4835  C   SER A 611     -21.737  15.909  32.416  1.00102.29           C  
ANISOU 4835  C   SER A 611    10005  13800  15062   -792  -1542  -2930       C  
ATOM   4836  O   SER A 611     -22.794  15.549  31.878  1.00110.90           O  
ANISOU 4836  O   SER A 611    10811  15006  16318   -870  -1680  -3161       O  
ATOM   4837  CB  SER A 611     -21.395  18.357  32.010  1.00 88.96           C  
ANISOU 4837  CB  SER A 611     8516  12405  12879   -347  -1723  -2692       C  
ATOM   4838  OG  SER A 611     -22.566  18.605  31.249  1.00125.43           O  
ANISOU 4838  OG  SER A 611    12859  17244  17555   -290  -1956  -2880       O  
ATOM   4839  N   PRO A 612     -21.331  15.405  33.582  1.00105.37           N  
ANISOU 4839  N   PRO A 612    10484  13962  15590   -928  -1283  -2749       N  
ATOM   4840  CA  PRO A 612     -22.156  14.421  34.290  1.00105.15           C  
ANISOU 4840  CA  PRO A 612    10227  13809  15917  -1194  -1137  -2788       C  
ATOM   4841  C   PRO A 612     -23.376  15.013  34.976  1.00116.47           C  
ANISOU 4841  C   PRO A 612    11376  15423  17453  -1208  -1049  -2759       C  
ATOM   4842  O   PRO A 612     -24.160  14.255  35.558  1.00117.20           O  
ANISOU 4842  O   PRO A 612    11242  15458  17831  -1451   -916  -2787       O  
ATOM   4843  CB  PRO A 612     -21.179  13.836  35.320  1.00 95.80           C  
ANISOU 4843  CB  PRO A 612     9280  12342  14777  -1305   -905  -2541       C  
ATOM   4844  CG  PRO A 612     -20.212  14.935  35.580  1.00 96.29           C  
ANISOU 4844  CG  PRO A 612     9610  12467  14507  -1073   -870  -2335       C  
ATOM   4845  CD  PRO A 612     -20.080  15.709  34.299  1.00 93.75           C  
ANISOU 4845  CD  PRO A 612     9327  12349  13945   -857  -1122  -2485       C  
ATOM   4846  N   TYR A 613     -23.577  16.329  34.914  1.00121.41           N  
ANISOU 4846  N   TYR A 613    11993  16262  17874   -960  -1121  -2712       N  
ATOM   4847  CA  TYR A 613     -24.630  16.982  35.679  1.00117.58           C  
ANISOU 4847  CA  TYR A 613    11244  15947  17483   -933  -1013  -2694       C  
ATOM   4848  C   TYR A 613     -25.840  17.374  34.836  1.00138.92           C  
ANISOU 4848  C   TYR A 613    13611  18896  20276   -838  -1252  -2939       C  
ATOM   4849  O   TYR A 613     -26.737  18.053  35.348  1.00153.57           O  
ANISOU 4849  O   TYR A 613    15220  20921  22211   -760  -1198  -2962       O  
ATOM   4850  CB  TYR A 613     -24.072  18.208  36.412  1.00112.95           C  
ANISOU 4850  CB  TYR A 613    10856  15395  16664   -715   -906  -2480       C  
ATOM   4851  CG  TYR A 613     -23.468  19.306  35.550  1.00114.01           C  
ANISOU 4851  CG  TYR A 613    11199  15597  16524   -422  -1139  -2452       C  
ATOM   4852  CD1 TYR A 613     -24.273  20.174  34.821  1.00122.77           C  
ANISOU 4852  CD1 TYR A 613    12126  16906  17616   -219  -1379  -2577       C  
ATOM   4853  CD2 TYR A 613     -22.092  19.502  35.506  1.00116.37           C  
ANISOU 4853  CD2 TYR A 613    11869  15759  16587   -352  -1120  -2281       C  
ATOM   4854  CE1 TYR A 613     -23.724  21.186  34.050  1.00131.35           C  
ANISOU 4854  CE1 TYR A 613    13418  18037  18452     28  -1597  -2503       C  
ATOM   4855  CE2 TYR A 613     -21.535  20.513  34.740  1.00117.56           C  
ANISOU 4855  CE2 TYR A 613    12208  15974  16486   -120  -1317  -2227       C  
ATOM   4856  CZ  TYR A 613     -22.355  21.350  34.014  1.00124.47           C  
ANISOU 4856  CZ  TYR A 613    12920  17031  17342     62  -1555  -2323       C  
ATOM   4857  OH  TYR A 613     -21.801  22.354  33.251  1.00137.93           O  
ANISOU 4857  OH  TYR A 613    14828  18783  18796    272  -1758  -2225       O  
ATOM   4858  N   ALA A 614     -25.889  16.959  33.571  1.00131.01           N  
ANISOU 4858  N   ALA A 614    12580  17934  19262   -837  -1519  -3139       N  
ATOM   4859  CA  ALA A 614     -27.037  17.215  32.698  1.00122.24           C  
ANISOU 4859  CA  ALA A 614    11141  17071  18235   -763  -1784  -3383       C  
ATOM   4860  C   ALA A 614     -27.408  18.697  32.647  1.00119.94           C  
ANISOU 4860  C   ALA A 614    10798  16976  17797   -443  -1914  -3315       C  
ATOM   4861  O   ALA A 614     -27.421  19.311  31.580  1.00129.91           O  
ANISOU 4861  O   ALA A 614    12098  18380  18882   -240  -2220  -3369       O  
ATOM   4862  CB  ALA A 614     -28.237  16.384  33.145  1.00100.61           C  
ANISOU 4862  CB  ALA A 614     7994  14367  15865  -1027  -1676  -3549       C  
TER    4863      ALA A 614                                                      
ATOM   4864  N   THR B 333      68.834  30.002  83.576  1.00152.05           N  
ANISOU 4864  N   THR B 333    14338  22350  21085   6115  -6034  -3002       N  
ATOM   4865  CA  THR B 333      67.723  29.090  83.821  1.00155.31           C  
ANISOU 4865  CA  THR B 333    15549  22330  21133   6279  -6010  -2845       C  
ATOM   4866  C   THR B 333      66.423  29.841  84.086  1.00152.79           C  
ANISOU 4866  C   THR B 333    15774  21868  20411   5770  -5915  -2852       C  
ATOM   4867  O   THR B 333      65.456  29.262  84.581  1.00150.83           O  
ANISOU 4867  O   THR B 333    16133  21370  19806   5805  -5977  -2670       O  
ATOM   4868  CB  THR B 333      68.009  28.153  85.010  1.00174.10           C  
ANISOU 4868  CB  THR B 333    18087  24672  23393   6705  -6570  -2612       C  
ATOM   4869  OG1 THR B 333      68.169  28.926  86.207  1.00177.60           O  
ANISOU 4869  OG1 THR B 333    18434  25429  23616   6469  -7051  -2608       O  
ATOM   4870  CG2 THR B 333      69.265  27.340  84.757  1.00154.73           C  
ANISOU 4870  CG2 THR B 333    15096  22318  21376   7299  -6699  -2616       C  
ATOM   4871  N   ASN B 334      66.402  31.132  83.762  1.00151.35           N  
ANISOU 4871  N   ASN B 334    15348  21847  20310   5301  -5781  -3039       N  
ATOM   4872  CA  ASN B 334      65.173  31.913  83.835  1.00157.35           C  
ANISOU 4872  CA  ASN B 334    16577  22453  20756   4870  -5649  -3102       C  
ATOM   4873  C   ASN B 334      64.373  31.655  82.565  1.00163.94           C  
ANISOU 4873  C   ASN B 334    17704  22995  21591   4784  -5089  -3084       C  
ATOM   4874  O   ASN B 334      64.742  32.124  81.483  1.00160.18           O  
ANISOU 4874  O   ASN B 334    16900  22580  21379   4628  -4756  -3174       O  
ATOM   4875  CB  ASN B 334      65.475  33.399  84.006  1.00155.16           C  
ANISOU 4875  CB  ASN B 334    15964  22367  20623   4427  -5817  -3319       C  
ATOM   4876  CG  ASN B 334      64.220  34.226  84.230  1.00170.70           C  
ANISOU 4876  CG  ASN B 334    18417  24168  22272   4079  -5762  -3436       C  
ATOM   4877  OD1 ASN B 334      63.254  33.756  84.833  1.00173.57           O  
ANISOU 4877  OD1 ASN B 334    19299  24446  22202   4188  -5782  -3351       O  
ATOM   4878  ND2 ASN B 334      64.226  35.460  83.740  1.00171.15           N  
ANISOU 4878  ND2 ASN B 334    18283  24184  22563   3661  -5698  -3605       N  
ATOM   4879  N   LEU B 335      63.288  30.900  82.693  1.00161.05           N  
ANISOU 4879  N   LEU B 335    17938  22339  20915   4865  -5004  -2937       N  
ATOM   4880  CA  LEU B 335      62.501  30.516  81.534  1.00153.54           C  
ANISOU 4880  CA  LEU B 335    17302  21084  19952   4808  -4556  -2926       C  
ATOM   4881  C   LEU B 335      61.717  31.710  80.997  1.00151.75           C  
ANISOU 4881  C   LEU B 335    17158  20843  19657   4325  -4305  -3045       C  
ATOM   4882  O   LEU B 335      61.457  32.689  81.701  1.00147.67           O  
ANISOU 4882  O   LEU B 335    16629  20451  19029   4063  -4503  -3127       O  
ATOM   4883  CB  LEU B 335      61.551  29.374  81.892  1.00157.73           C  
ANISOU 4883  CB  LEU B 335    18423  21283  20225   4966  -4614  -2693       C  
ATOM   4884  CG  LEU B 335      62.236  28.049  82.228  1.00153.13           C  
ANISOU 4884  CG  LEU B 335    17851  20559  19771   5473  -4868  -2534       C  
ATOM   4885  CD1 LEU B 335      61.239  27.063  82.821  1.00152.16           C  
ANISOU 4885  CD1 LEU B 335    18323  20101  19389   5506  -5025  -2201       C  
ATOM   4886  CD2 LEU B 335      62.927  27.462  81.002  1.00145.60           C  
ANISOU 4886  CD2 LEU B 335    16689  19477  19154   5800  -4605  -2709       C  
ATOM   4887  N   CYS B 336      61.347  31.622  79.725  1.00146.82           N  
ANISOU 4887  N   CYS B 336    16634  20055  19095   4242  -3898  -3076       N  
ATOM   4888  CA  CYS B 336      60.555  32.706  79.163  1.00138.32           C  
ANISOU 4888  CA  CYS B 336    15666  18927  17964   3805  -3691  -3140       C  
ATOM   4889  C   CYS B 336      59.080  32.500  79.502  1.00129.14           C  
ANISOU 4889  C   CYS B 336    15060  17527  16479   3691  -3688  -3052       C  
ATOM   4890  O   CYS B 336      58.580  31.373  79.446  1.00123.04           O  
ANISOU 4890  O   CYS B 336    14624  16540  15584   3879  -3650  -2917       O  
ATOM   4891  CB  CYS B 336      60.742  32.789  77.651  1.00125.66           C  
ANISOU 4891  CB  CYS B 336    13933  17318  16495   3732  -3271  -3176       C  
ATOM   4892  SG  CYS B 336      62.380  33.366  77.123  1.00143.54           S  
ANISOU 4892  SG  CYS B 336    15413  19999  19126   3723  -3172  -3220       S  
ATOM   4893  N   PRO B 337      58.367  33.566  79.861  1.00132.48           N  
ANISOU 4893  N   PRO B 337    15566  17979  16791   3390  -3748  -3125       N  
ATOM   4894  CA  PRO B 337      56.983  33.434  80.354  1.00123.21           C  
ANISOU 4894  CA  PRO B 337    14817  16702  15294   3310  -3750  -3041       C  
ATOM   4895  C   PRO B 337      55.965  33.272  79.229  1.00139.38           C  
ANISOU 4895  C   PRO B 337    17139  18499  17319   3145  -3435  -2977       C  
ATOM   4896  O   PRO B 337      55.092  34.117  79.015  1.00149.03           O  
ANISOU 4896  O   PRO B 337    18458  19681  18487   2904  -3358  -3036       O  
ATOM   4897  CB  PRO B 337      56.790  34.743  81.130  1.00133.39           C  
ANISOU 4897  CB  PRO B 337    16012  18155  16514   3134  -3956  -3240       C  
ATOM   4898  CG  PRO B 337      57.663  35.716  80.422  1.00142.03           C  
ANISOU 4898  CG  PRO B 337    16742  19243  17979   2942  -3943  -3385       C  
ATOM   4899  CD  PRO B 337      58.866  34.948  79.961  1.00134.11           C  
ANISOU 4899  CD  PRO B 337    15442  18322  17192   3134  -3877  -3297       C  
ATOM   4900  N   PHE B 338      56.072  32.164  78.493  1.00144.63           N  
ANISOU 4900  N   PHE B 338    17941  18976  18035   3305  -3291  -2881       N  
ATOM   4901  CA  PHE B 338      55.093  31.896  77.448  1.00129.57           C  
ANISOU 4901  CA  PHE B 338    16330  16826  16076   3158  -3060  -2839       C  
ATOM   4902  C   PHE B 338      53.755  31.454  78.021  1.00123.45           C  
ANISOU 4902  C   PHE B 338    15898  15934  15075   3051  -3129  -2650       C  
ATOM   4903  O   PHE B 338      52.739  31.529  77.322  1.00114.24           O  
ANISOU 4903  O   PHE B 338    14930  14617  13860   2847  -2993  -2616       O  
ATOM   4904  CB  PHE B 338      55.625  30.842  76.479  1.00118.19           C  
ANISOU 4904  CB  PHE B 338    14959  15207  14740   3396  -2927  -2873       C  
ATOM   4905  CG  PHE B 338      56.645  31.373  75.518  1.00125.51           C  
ANISOU 4905  CG  PHE B 338    15538  16326  15824   3428  -2711  -3036       C  
ATOM   4906  CD1 PHE B 338      56.427  32.567  74.853  1.00120.63           C  
ANISOU 4906  CD1 PHE B 338    14796  15819  15219   3098  -2547  -3066       C  
ATOM   4907  CD2 PHE B 338      57.819  30.682  75.277  1.00141.99           C  
ANISOU 4907  CD2 PHE B 338    17396  18505  18050   3793  -2673  -3127       C  
ATOM   4908  CE1 PHE B 338      57.363  33.064  73.969  1.00120.49           C  
ANISOU 4908  CE1 PHE B 338    14428  16031  15322   3068  -2329  -3121       C  
ATOM   4909  CE2 PHE B 338      58.756  31.174  74.391  1.00142.08           C  
ANISOU 4909  CE2 PHE B 338    17011  18803  18171   3811  -2420  -3236       C  
ATOM   4910  CZ  PHE B 338      58.528  32.368  73.738  1.00131.75           C  
ANISOU 4910  CZ  PHE B 338    15578  17635  16846   3416  -2237  -3202       C  
ATOM   4911  N   GLY B 339      53.735  31.002  79.275  1.00145.70           N  
ANISOU 4911  N   GLY B 339    18758  18863  17738   3171  -3343  -2492       N  
ATOM   4912  CA  GLY B 339      52.478  30.615  79.892  1.00130.09           C  
ANISOU 4912  CA  GLY B 339    17031  16884  15515   3035  -3373  -2242       C  
ATOM   4913  C   GLY B 339      51.503  31.770  80.012  1.00123.13           C  
ANISOU 4913  C   GLY B 339    16096  16199  14490   2809  -3271  -2346       C  
ATOM   4914  O   GLY B 339      50.294  31.590  79.852  1.00126.82           O  
ANISOU 4914  O   GLY B 339    16719  16615  14851   2630  -3175  -2191       O  
ATOM   4915  N   GLU B 340      52.013  32.977  80.287  1.00122.86           N  
ANISOU 4915  N   GLU B 340    15824  16368  14490   2819  -3325  -2618       N  
ATOM   4916  CA  GLU B 340      51.117  34.119  80.450  1.00124.50           C  
ANISOU 4916  CA  GLU B 340    15996  16709  14600   2679  -3282  -2774       C  
ATOM   4917  C   GLU B 340      50.445  34.516  79.141  1.00135.44           C  
ANISOU 4917  C   GLU B 340    17447  17846  16166   2470  -3095  -2801       C  
ATOM   4918  O   GLU B 340      49.341  35.069  79.164  1.00147.18           O  
ANISOU 4918  O   GLU B 340    18969  19386  17567   2370  -3042  -2824       O  
ATOM   4919  CB  GLU B 340      51.848  35.331  81.033  1.00120.66           C  
ANISOU 4919  CB  GLU B 340    15285  16391  14168   2736  -3471  -3094       C  
ATOM   4920  CG  GLU B 340      52.481  35.137  82.401  1.00142.29           C  
ANISOU 4920  CG  GLU B 340    17955  19438  16670   2947  -3722  -3126       C  
ATOM   4921  CD  GLU B 340      53.788  35.892  82.544  1.00157.18           C  
ANISOU 4921  CD  GLU B 340    19577  21347  18798   2979  -3961  -3390       C  
ATOM   4922  OE1 GLU B 340      53.840  37.070  82.128  1.00159.98           O  
ANISOU 4922  OE1 GLU B 340    19819  21579  19386   2826  -4003  -3638       O  
ATOM   4923  OE2 GLU B 340      54.754  35.323  83.094  1.00152.15           O1-
ANISOU 4923  OE2 GLU B 340    18831  20836  18144   3143  -4146  -3326       O1-
ATOM   4924  N   VAL B 341      51.083  34.260  78.000  1.00127.05           N  
ANISOU 4924  N   VAL B 341    16386  16562  15325   2430  -2997  -2805       N  
ATOM   4925  CA  VAL B 341      50.463  34.613  76.726  1.00118.90           C  
ANISOU 4925  CA  VAL B 341    15445  15338  14394   2232  -2842  -2806       C  
ATOM   4926  C   VAL B 341      49.472  33.541  76.291  1.00109.99           C  
ANISOU 4926  C   VAL B 341    14584  14044  13162   2165  -2775  -2606       C  
ATOM   4927  O   VAL B 341      48.300  33.829  76.028  1.00113.77           O  
ANISOU 4927  O   VAL B 341    15137  14498  13592   2001  -2744  -2546       O  
ATOM   4928  CB  VAL B 341      51.537  34.857  75.649  1.00113.16           C  
ANISOU 4928  CB  VAL B 341    14591  14538  13865   2208  -2736  -2885       C  
ATOM   4929  CG1 VAL B 341      50.881  35.206  74.318  1.00111.35           C  
ANISOU 4929  CG1 VAL B 341    14492  14161  13656   2002  -2591  -2846       C  
ATOM   4930  CG2 VAL B 341      52.482  35.964  76.085  1.00102.78           C  
ANISOU 4930  CG2 VAL B 341    12969  13361  12723   2184  -2852  -3030       C  
ATOM   4931  N   PHE B 342      49.923  32.287  76.223  1.00 97.00           N  
ANISOU 4931  N   PHE B 342    13077  12258  11520   2294  -2798  -2506       N  
ATOM   4932  CA  PHE B 342      49.115  31.228  75.627  1.00 98.13           C  
ANISOU 4932  CA  PHE B 342    13509  12132  11644   2200  -2800  -2350       C  
ATOM   4933  C   PHE B 342      47.998  30.741  76.542  1.00108.40           C  
ANISOU 4933  C   PHE B 342    14888  13487  12811   2074  -2892  -2068       C  
ATOM   4934  O   PHE B 342      46.921  30.382  76.054  1.00129.49           O  
ANISOU 4934  O   PHE B 342    17702  16012  15487   1858  -2898  -1930       O  
ATOM   4935  CB  PHE B 342      50.006  30.051  75.231  1.00 94.71           C  
ANISOU 4935  CB  PHE B 342    13224  11455  11307   2426  -2845  -2383       C  
ATOM   4936  CG  PHE B 342      50.848  30.314  74.020  1.00 94.94           C  
ANISOU 4936  CG  PHE B 342    13195  11468  11409   2529  -2684  -2632       C  
ATOM   4937  CD1 PHE B 342      52.044  31.003  74.124  1.00 95.10           C  
ANISOU 4937  CD1 PHE B 342    12891  11737  11505   2667  -2601  -2768       C  
ATOM   4938  CD2 PHE B 342      50.445  29.867  72.773  1.00115.70           C  
ANISOU 4938  CD2 PHE B 342    16076  13879  14006   2474  -2622  -2719       C  
ATOM   4939  CE1 PHE B 342      52.821  31.245  73.007  1.00 94.56           C  
ANISOU 4939  CE1 PHE B 342    12708  11751  11471   2734  -2403  -2931       C  
ATOM   4940  CE2 PHE B 342      51.217  30.104  71.653  1.00125.76           C  
ANISOU 4940  CE2 PHE B 342    17287  15245  15251   2587  -2431  -2932       C  
ATOM   4941  CZ  PHE B 342      52.406  30.793  71.771  1.00105.19           C  
ANISOU 4941  CZ  PHE B 342    14315  12941  12713   2712  -2292  -3011       C  
ATOM   4942  N   ASN B 343      48.224  30.703  77.851  1.00 98.33           N  
ANISOU 4942  N   ASN B 343    13502  12462  11396   2186  -2969  -1954       N  
ATOM   4943  CA  ASN B 343      47.229  30.206  78.789  1.00 99.55           C  
ANISOU 4943  CA  ASN B 343    13690  12779  11356   2062  -3013  -1616       C  
ATOM   4944  C   ASN B 343      46.489  31.330  79.516  1.00101.73           C  
ANISOU 4944  C   ASN B 343    13735  13505  11413   2030  -2918  -1688       C  
ATOM   4945  O   ASN B 343      45.817  31.067  80.520  1.00105.07           O  
ANISOU 4945  O   ASN B 343    14099  14246  11577   1991  -2906  -1428       O  
ATOM   4946  CB  ASN B 343      47.889  29.235  79.784  1.00114.74           C  
ANISOU 4946  CB  ASN B 343    15690  14714  13193   2224  -3178  -1366       C  
ATOM   4947  CG  ASN B 343      48.207  27.865  79.150  1.00122.73           C  
ANISOU 4947  CG  ASN B 343    16990  15198  14443   2248  -3325  -1218       C  
ATOM   4948  OD1 ASN B 343      47.946  27.648  77.968  1.00 98.02           O  
ANISOU 4948  OD1 ASN B 343    14011  11734  11498   2152  -3292  -1350       O  
ATOM   4949  ND2 ASN B 343      48.774  26.941  79.942  1.00134.36           N  
ANISOU 4949  ND2 ASN B 343    18565  16584  15904   2405  -3526   -960       N  
ATOM   4950  N   ALA B 344      46.578  32.566  79.017  1.00 97.79           N  
ANISOU 4950  N   ALA B 344    13105  13042  11008   2056  -2855  -2026       N  
ATOM   4951  CA  ALA B 344      45.835  33.679  79.598  1.00100.30           C  
ANISOU 4951  CA  ALA B 344    13232  13703  11175   2088  -2803  -2176       C  
ATOM   4952  C   ALA B 344      44.336  33.405  79.558  1.00112.64           C  
ANISOU 4952  C   ALA B 344    14755  15398  12645   1906  -2701  -1928       C  
ATOM   4953  O   ALA B 344      43.825  32.786  78.622  1.00127.11           O  
ANISOU 4953  O   ALA B 344    16709  16943  14645   1688  -2698  -1751       O  
ATOM   4954  CB  ALA B 344      46.151  34.975  78.852  1.00106.24           C  
ANISOU 4954  CB  ALA B 344    13905  14309  12152   2104  -2818  -2528       C  
ATOM   4955  N   THR B 345      43.626  33.889  80.582  1.00112.22           N  
ANISOU 4955  N   THR B 345    14505  15823  12312   2008  -2628  -1938       N  
ATOM   4956  CA  THR B 345      42.215  33.545  80.734  1.00115.88           C  
ANISOU 4956  CA  THR B 345    14827  16549  12654   1842  -2500  -1636       C  
ATOM   4957  C   THR B 345      41.360  34.202  79.653  1.00123.52           C  
ANISOU 4957  C   THR B 345    15712  17340  13880   1732  -2478  -1764       C  
ATOM   4958  O   THR B 345      40.520  33.542  79.029  1.00127.76           O  
ANISOU 4958  O   THR B 345    16253  17753  14538   1459  -2474  -1473       O  
ATOM   4959  CB  THR B 345      41.725  33.934  82.129  1.00128.36           C  
ANISOU 4959  CB  THR B 345    16169  18804  13798   2046  -2378  -1646       C  
ATOM   4960  OG1 THR B 345      42.418  33.154  83.111  1.00123.88           O  
ANISOU 4960  OG1 THR B 345    15701  18424  12942   2099  -2427  -1411       O  
ATOM   4961  CG2 THR B 345      40.233  33.669  82.258  1.00133.36           C  
ANISOU 4961  CG2 THR B 345    16546  19810  14314   1876  -2197  -1320       C  
ATOM   4962  N   ARG B 346      41.551  35.499  79.419  1.00126.00           N  
ANISOU 4962  N   ARG B 346    15960  17611  14304   1926  -2517  -2177       N  
ATOM   4963  CA  ARG B 346      40.902  36.185  78.313  1.00126.96           C  
ANISOU 4963  CA  ARG B 346    16046  17495  14699   1843  -2557  -2280       C  
ATOM   4964  C   ARG B 346      41.946  36.777  77.376  1.00122.67           C  
ANISOU 4964  C   ARG B 346    15692  16503  14415   1837  -2679  -2508       C  
ATOM   4965  O   ARG B 346      43.012  37.230  77.807  1.00121.07           O  
ANISOU 4965  O   ARG B 346    15519  16271  14212   1986  -2739  -2731       O  
ATOM   4966  CB  ARG B 346      39.949  37.296  78.792  1.00134.67           C  
ANISOU 4966  CB  ARG B 346    16738  18811  15620   2080  -2519  -2511       C  
ATOM   4967  CG  ARG B 346      38.992  37.770  77.694  1.00147.71           C  
ANISOU 4967  CG  ARG B 346    18309  20266  17546   1974  -2584  -2486       C  
ATOM   4968  CD  ARG B 346      38.190  39.007  78.083  1.00144.53           C  
ANISOU 4968  CD  ARG B 346    17636  20106  17172   2302  -2599  -2792       C  
ATOM   4969  NE  ARG B 346      37.542  38.879  79.382  1.00173.88           N  
ANISOU 4969  NE  ARG B 346    21056  24478  20531   2528  -2401  -2804       N  
ATOM   4970  CZ  ARG B 346      36.271  38.538  79.545  1.00180.85           C  
ANISOU 4970  CZ  ARG B 346    21600  25793  21322   2485  -2246  -2560       C  
ATOM   4971  NH1 ARG B 346      35.485  38.285  78.510  1.00172.75           N  
ANISOU 4971  NH1 ARG B 346    20497  24571  20569   2221  -2320  -2308       N  
ATOM   4972  NH2 ARG B 346      35.775  38.451  80.775  1.00181.19           N  
ANISOU 4972  NH2 ARG B 346    21348  26530  20967   2706  -2017  -2558       N  
ATOM   4973  N   PHE B 347      41.630  36.756  76.087  1.00112.51           N  
ANISOU 4973  N   PHE B 347    14511  14907  13331   1640  -2726  -2420       N  
ATOM   4974  CA  PHE B 347      42.466  37.340  75.051  1.00106.30           C  
ANISOU 4974  CA  PHE B 347    13873  13771  12746   1588  -2802  -2549       C  
ATOM   4975  C   PHE B 347      41.902  38.692  74.625  1.00108.54           C  
ANISOU 4975  C   PHE B 347    14060  13964  13218   1642  -2914  -2696       C  
ATOM   4976  O   PHE B 347      40.805  39.094  75.020  1.00112.83           O  
ANISOU 4976  O   PHE B 347    14418  14700  13751   1753  -2931  -2730       O  
ATOM   4977  CB  PHE B 347      42.566  36.399  73.848  1.00103.63           C  
ANISOU 4977  CB  PHE B 347    13765  13176  12434   1362  -2794  -2361       C  
ATOM   4978  CG  PHE B 347      43.696  35.413  73.936  1.00101.30           C  
ANISOU 4978  CG  PHE B 347    13623  12793  12073   1388  -2741  -2339       C  
ATOM   4979  CD1 PHE B 347      43.896  34.665  75.085  1.00111.37           C  
ANISOU 4979  CD1 PHE B 347    14862  14236  13219   1485  -2718  -2257       C  
ATOM   4980  CD2 PHE B 347      44.551  35.223  72.862  1.00 99.10           C  
ANISOU 4980  CD2 PHE B 347    13513  12299  11841   1343  -2714  -2386       C  
ATOM   4981  CE1 PHE B 347      44.934  33.754  75.165  1.00110.19           C  
ANISOU 4981  CE1 PHE B 347    14848  13967  13052   1556  -2717  -2231       C  
ATOM   4982  CE2 PHE B 347      45.590  34.313  72.936  1.00 99.82           C  
ANISOU 4982  CE2 PHE B 347    13706  12327  11896   1445  -2666  -2407       C  
ATOM   4983  CZ  PHE B 347      45.781  33.577  74.089  1.00 99.55           C  
ANISOU 4983  CZ  PHE B 347    13641  12386  11796   1560  -2692  -2332       C  
ATOM   4984  N   ALA B 348      42.667  39.392  73.798  1.00101.50           N  
ANISOU 4984  N   ALA B 348    13273  12785  12508   1570  -2995  -2757       N  
ATOM   4985  CA  ALA B 348      42.288  40.722  73.353  1.00102.11           C  
ANISOU 4985  CA  ALA B 348    13304  12672  12820   1604  -3166  -2849       C  
ATOM   4986  C   ALA B 348      41.436  40.655  72.091  1.00 99.88           C  
ANISOU 4986  C   ALA B 348    13111  12253  12585   1423  -3226  -2623       C  
ATOM   4987  O   ALA B 348      41.475  39.684  71.331  1.00 98.10           O  
ANISOU 4987  O   ALA B 348    13041  12011  12222   1233  -3147  -2439       O  
ATOM   4988  CB  ALA B 348      43.530  41.577  73.097  1.00113.89           C  
ANISOU 4988  CB  ALA B 348    14845  13915  14512   1548  -3263  -2939       C  
ATOM   4989  N   SER B 349      40.646  41.705  71.883  1.00104.54           N  
ANISOU 4989  N   SER B 349    13614  12732  13375   1515  -3410  -2666       N  
ATOM   4990  CA  SER B 349      39.971  41.902  70.609  1.00103.10           C  
ANISOU 4990  CA  SER B 349    13525  12381  13267   1351  -3548  -2442       C  
ATOM   4991  C   SER B 349      40.984  42.387  69.581  1.00103.59           C  
ANISOU 4991  C   SER B 349    13798  12169  13394   1147  -3599  -2304       C  
ATOM   4992  O   SER B 349      41.854  43.207  69.889  1.00107.48           O  
ANISOU 4992  O   SER B 349    14273  12498  14064   1176  -3655  -2404       O  
ATOM   4993  CB  SER B 349      38.824  42.901  70.753  1.00104.25           C  
ANISOU 4993  CB  SER B 349    13483  12489  13640   1567  -3764  -2520       C  
ATOM   4994  OG  SER B 349      37.793  42.374  71.573  1.00104.90           O  
ANISOU 4994  OG  SER B 349    13300  12941  13614   1730  -3663  -2584       O  
ATOM   4995  N   VAL B 350      40.860  41.879  68.351  1.00 88.19           N  
ANISOU 4995  N   VAL B 350    12033  10196  11281    924  -3592  -2066       N  
ATOM   4996  CA  VAL B 350      41.953  41.976  67.385  1.00 85.82           C  
ANISOU 4996  CA  VAL B 350    11916   9808  10883    720  -3514  -1908       C  
ATOM   4997  C   VAL B 350      42.317  43.426  67.078  1.00 85.45           C  
ANISOU 4997  C   VAL B 350    11854   9494  11120    656  -3706  -1786       C  
ATOM   4998  O   VAL B 350      43.476  43.725  66.763  1.00 93.49           O  
ANISOU 4998  O   VAL B 350    12896  10474  12152    500  -3614  -1679       O  
ATOM   4999  CB  VAL B 350      41.596  41.192  66.104  1.00 94.24           C  
ANISOU 4999  CB  VAL B 350    13211  10951  11646    543  -3500  -1723       C  
ATOM   5000  CG1 VAL B 350      40.377  41.794  65.423  1.00108.83           C  
ANISOU 5000  CG1 VAL B 350    15081  12697  13574    500  -3795  -1548       C  
ATOM   5001  CG2 VAL B 350      42.787  41.133  65.153  1.00 96.31           C  
ANISOU 5001  CG2 VAL B 350    13633  11268  11693    384  -3329  -1590       C  
ATOM   5002  N   TYR B 351      41.358  44.351  67.177  1.00 84.93           N  
ANISOU 5002  N   TYR B 351    11724   9228  11317    775  -3993  -1784       N  
ATOM   5003  CA  TYR B 351      41.674  45.748  66.894  1.00 87.75           C  
ANISOU 5003  CA  TYR B 351    12108   9218  12016    710  -4257  -1647       C  
ATOM   5004  C   TYR B 351      42.547  46.352  67.987  1.00 92.75           C  
ANISOU 5004  C   TYR B 351    12616   9702  12922    806  -4288  -1912       C  
ATOM   5005  O   TYR B 351      43.360  47.241  67.709  1.00 93.83           O  
ANISOU 5005  O   TYR B 351    12785   9553  13311    612  -4433  -1754       O  
ATOM   5006  CB  TYR B 351      40.390  46.564  66.717  1.00107.19           C  
ANISOU 5006  CB  TYR B 351    14542  11455  14731    882  -4610  -1608       C  
ATOM   5007  CG  TYR B 351      39.810  47.099  68.006  1.00 90.97           C  
ANISOU 5007  CG  TYR B 351    12276   9327  12961   1279  -4746  -2018       C  
ATOM   5008  CD1 TYR B 351      39.016  46.300  68.814  1.00 89.59           C  
ANISOU 5008  CD1 TYR B 351    11904   9528  12608   1519  -4574  -2266       C  
ATOM   5009  CD2 TYR B 351      40.046  48.408  68.409  1.00 94.22           C  
ANISOU 5009  CD2 TYR B 351    12687   9304  13809   1416  -5060  -2156       C  
ATOM   5010  CE1 TYR B 351      38.487  46.781  69.989  1.00 91.94           C  
ANISOU 5010  CE1 TYR B 351    11985   9876  13071   1920  -4645  -2652       C  
ATOM   5011  CE2 TYR B 351      39.518  48.899  69.587  1.00100.87           C  
ANISOU 5011  CE2 TYR B 351    13359  10113  14855   1852  -5187  -2618       C  
ATOM   5012  CZ  TYR B 351      38.738  48.081  70.374  1.00 95.53           C  
ANISOU 5012  CZ  TYR B 351    12464   9921  13913   2122  -4947  -2871       C  
ATOM   5013  OH  TYR B 351      38.207  48.563  71.549  1.00 96.72           O  
ANISOU 5013  OH  TYR B 351    12420  10155  14176   2594  -5022  -3342       O  
ATOM   5014  N   ALA B 352      42.396  45.886  69.226  1.00102.18           N  
ANISOU 5014  N   ALA B 352    13664  11098  14060   1075  -4180  -2287       N  
ATOM   5015  CA  ALA B 352      43.244  46.333  70.323  1.00100.02           C  
ANISOU 5015  CA  ALA B 352    13290  10748  13964   1184  -4231  -2589       C  
ATOM   5016  C   ALA B 352      44.206  45.219  70.711  1.00104.77           C  
ANISOU 5016  C   ALA B 352    13847  11684  14277   1113  -3912  -2633       C  
ATOM   5017  O   ALA B 352      44.309  44.864  71.890  1.00103.04           O  
ANISOU 5017  O   ALA B 352    13523  11663  13965   1335  -3852  -2934       O  
ATOM   5018  CB  ALA B 352      42.396  46.757  71.524  1.00 88.39           C  
ANISOU 5018  CB  ALA B 352    11690   9298  12596   1603  -4382  -3013       C  
ATOM   5019  N   TRP B 353      44.908  44.667  69.722  1.00112.51           N  
ANISOU 5019  N   TRP B 353    14905  12752  15090    841  -3714  -2338       N  
ATOM   5020  CA  TRP B 353      45.731  43.487  69.951  1.00104.57           C  
ANISOU 5020  CA  TRP B 353    13865  12052  13815    837  -3418  -2380       C  
ATOM   5021  C   TRP B 353      46.789  43.767  71.012  1.00107.46           C  
ANISOU 5021  C   TRP B 353    14059  12431  14338    903  -3465  -2604       C  
ATOM   5022  O   TRP B 353      47.317  44.877  71.122  1.00 95.05           O  
ANISOU 5022  O   TRP B 353    12413  10604  13095    795  -3691  -2619       O  
ATOM   5023  CB  TRP B 353      46.385  43.024  68.646  1.00101.72           C  
ANISOU 5023  CB  TRP B 353    13597  11796  13257    593  -3210  -2082       C  
ATOM   5024  CG  TRP B 353      47.095  44.095  67.866  1.00 97.98           C  
ANISOU 5024  CG  TRP B 353    13085  11155  12989    312  -3296  -1801       C  
ATOM   5025  CD1 TRP B 353      46.531  45.006  67.021  1.00104.45           C  
ANISOU 5025  CD1 TRP B 353    14020  11734  13933    144  -3501  -1524       C  
ATOM   5026  CD2 TRP B 353      48.510  44.323  67.814  1.00101.21           C  
ANISOU 5026  CD2 TRP B 353    13303  11649  13502    130  -3185  -1697       C  
ATOM   5027  NE1 TRP B 353      47.503  45.807  66.470  1.00107.46           N  
ANISOU 5027  NE1 TRP B 353    14316  12023  14490   -164  -3526  -1218       N  
ATOM   5028  CE2 TRP B 353      48.726  45.406  66.939  1.00102.34           C  
ANISOU 5028  CE2 TRP B 353    13450  11595  13837   -190  -3319  -1320       C  
ATOM   5029  CE3 TRP B 353      49.612  43.726  68.433  1.00109.82           C  
ANISOU 5029  CE3 TRP B 353    14188  12974  14565    201  -3008  -1853       C  
ATOM   5030  CZ2 TRP B 353      50.000  45.902  66.666  1.00108.09           C  
ANISOU 5030  CZ2 TRP B 353    13951  12384  14732   -487  -3253  -1071       C  
ATOM   5031  CZ3 TRP B 353      50.874  44.221  68.162  1.00112.72           C  
ANISOU 5031  CZ3 TRP B 353    14308  13414  15107    -49  -2952  -1655       C  
ATOM   5032  CH2 TRP B 353      51.058  45.298  67.286  1.00110.57           C  
ANISOU 5032  CH2 TRP B 353    14012  12972  15026   -412  -3059  -1256       C  
ATOM   5033  N   ASN B 354      47.084  42.744  71.807  1.00119.61           N  
ANISOU 5033  N   ASN B 354    15546  14242  15660   1069  -3302  -2763       N  
ATOM   5034  CA  ASN B 354      47.904  42.883  73.001  1.00124.12           C  
ANISOU 5034  CA  ASN B 354    15961  14888  16310   1196  -3392  -3013       C  
ATOM   5035  C   ASN B 354      49.323  42.411  72.714  1.00124.04           C  
ANISOU 5035  C   ASN B 354    15822  15008  16298   1065  -3240  -2900       C  
ATOM   5036  O   ASN B 354      49.520  41.343  72.127  1.00122.53           O  
ANISOU 5036  O   ASN B 354    15686  14992  15876   1068  -2984  -2763       O  
ATOM   5037  CB  ASN B 354      47.301  42.086  74.159  1.00106.01           C  
ANISOU 5037  CB  ASN B 354    13672  12857  13750   1481  -3338  -3212       C  
ATOM   5038  CG  ASN B 354      47.790  42.560  75.510  1.00124.88           C  
ANISOU 5038  CG  ASN B 354    15942  15325  16183   1668  -3531  -3534       C  
ATOM   5039  OD1 ASN B 354      47.144  43.380  76.162  1.00115.13           O  
ANISOU 5039  OD1 ASN B 354    14702  14031  15010   1844  -3727  -3794       O  
ATOM   5040  ND2 ASN B 354      48.935  42.044  75.941  1.00143.91           N  
ANISOU 5040  ND2 ASN B 354    18251  17884  18544   1669  -3502  -3552       N  
ATOM   5041  N   ARG B 355      50.305  43.206  73.131  1.00114.45           N  
ANISOU 5041  N   ARG B 355    14418  13706  15361    968  -3425  -2982       N  
ATOM   5042  CA  ARG B 355      51.711  42.923  72.882  1.00107.24           C  
ANISOU 5042  CA  ARG B 355    13273  12959  14515    832  -3303  -2861       C  
ATOM   5043  C   ARG B 355      52.422  42.718  74.211  1.00108.53           C  
ANISOU 5043  C   ARG B 355    13268  13268  14703   1016  -3462  -3134       C  
ATOM   5044  O   ARG B 355      52.339  43.571  75.100  1.00112.78           O  
ANISOU 5044  O   ARG B 355    13785  13648  15417   1058  -3793  -3388       O  
ATOM   5045  CB  ARG B 355      52.367  44.063  72.096  1.00115.35           C  
ANISOU 5045  CB  ARG B 355    14149  13788  15892    455  -3412  -2614       C  
ATOM   5046  CG  ARG B 355      53.887  44.069  72.135  1.00118.83           C  
ANISOU 5046  CG  ARG B 355    14218  14423  16510    289  -3370  -2521       C  
ATOM   5047  CD  ARG B 355      54.464  44.869  70.972  1.00124.95           C  
ANISOU 5047  CD  ARG B 355    14827  15139  17508   -148  -3312  -2096       C  
ATOM   5048  NE  ARG B 355      54.244  44.224  69.681  1.00116.04           N  
ANISOU 5048  NE  ARG B 355    13809  14259  16023   -176  -2906  -1812       N  
ATOM   5049  CZ  ARG B 355      54.757  44.650  68.534  1.00120.33           C  
ANISOU 5049  CZ  ARG B 355    14211  14930  16581   -516  -2730  -1388       C  
ATOM   5050  NH1 ARG B 355      55.538  45.716  68.479  1.00124.87           N  
ANISOU 5050  NH1 ARG B 355    14496  15378  17571   -916  -2919  -1124       N  
ATOM   5051  NH2 ARG B 355      54.475  43.992  67.413  1.00124.60           N  
ANISOU 5051  NH2 ARG B 355    14905  15742  16694   -471  -2374  -1209       N  
ATOM   5052  N   LYS B 356      53.112  41.588  74.345  1.00116.80           N  
ANISOU 5052  N   LYS B 356    14212  14603  15564   1159  -3262  -3106       N  
ATOM   5053  CA  LYS B 356      53.906  41.277  75.528  1.00123.77           C  
ANISOU 5053  CA  LYS B 356    14915  15666  16444   1339  -3424  -3303       C  
ATOM   5054  C   LYS B 356      55.364  41.158  75.109  1.00123.19           C  
ANISOU 5054  C   LYS B 356    14477  15764  16565   1215  -3343  -3164       C  
ATOM   5055  O   LYS B 356      55.707  40.309  74.280  1.00110.27           O  
ANISOU 5055  O   LYS B 356    12796  14301  14800   1267  -3020  -2993       O  
ATOM   5056  CB  LYS B 356      53.424  39.985  76.195  1.00120.67           C  
ANISOU 5056  CB  LYS B 356    14698  15465  15685   1660  -3315  -3355       C  
ATOM   5057  CG  LYS B 356      53.639  39.926  77.706  1.00 99.44           C  
ANISOU 5057  CG  LYS B 356    11961  12938  12882   1880  -3580  -3586       C  
ATOM   5058  CD  LYS B 356      55.065  39.517  78.053  1.00133.02           C  
ANISOU 5058  CD  LYS B 356    15920  17380  17242   1945  -3665  -3581       C  
ATOM   5059  CE  LYS B 356      55.288  39.477  79.558  1.00146.09           C  
ANISOU 5059  CE  LYS B 356    17550  19225  18732   2162  -3982  -3800       C  
ATOM   5060  NZ  LYS B 356      55.756  40.787  80.090  1.00143.55           N  
ANISOU 5060  NZ  LYS B 356    17064  18814  18663   2023  -4364  -4070       N  
ATOM   5061  N   ARG B 357      56.216  42.006  75.678  1.00143.26           N  
ANISOU 5061  N   ARG B 357    16737  18274  19420   1065  -3649  -3261       N  
ATOM   5062  CA  ARG B 357      57.634  42.012  75.344  1.00134.76           C  
ANISOU 5062  CA  ARG B 357    15204  17410  18589    905  -3601  -3104       C  
ATOM   5063  C   ARG B 357      58.368  41.000  76.215  1.00134.51           C  
ANISOU 5063  C   ARG B 357    15000  17682  18428   1239  -3642  -3239       C  
ATOM   5064  O   ARG B 357      58.319  41.079  77.447  1.00141.16           O  
ANISOU 5064  O   ARG B 357    15898  18519  19217   1397  -3982  -3490       O  
ATOM   5065  CB  ARG B 357      58.235  43.405  75.514  1.00137.67           C  
ANISOU 5065  CB  ARG B 357    15315  17565  19429    517  -3976  -3100       C  
ATOM   5066  CG  ARG B 357      59.730  43.443  75.260  1.00152.03           C  
ANISOU 5066  CG  ARG B 357    16558  19664  21542    303  -3949  -2902       C  
ATOM   5067  CD  ARG B 357      60.277  44.856  75.291  1.00149.09           C  
ANISOU 5067  CD  ARG B 357    15929  19015  21704   -193  -4348  -2813       C  
ATOM   5068  NE  ARG B 357      61.722  44.869  75.106  1.00170.57           N  
ANISOU 5068  NE  ARG B 357    18009  22071  24730   -431  -4328  -2587       N  
ATOM   5069  CZ  ARG B 357      62.453  45.968  74.977  1.00188.74           C  
ANISOU 5069  CZ  ARG B 357    19942  24212  27556   -957  -4631  -2385       C  
ATOM   5070  NH1 ARG B 357      61.900  47.169  74.972  1.00186.08           N  
ANISOU 5070  NH1 ARG B 357    19865  23310  27528  -1291  -5009  -2387       N  
ATOM   5071  NH2 ARG B 357      63.772  45.858  74.845  1.00184.91           N  
ANISOU 5071  NH2 ARG B 357    18795  24132  27333  -1153  -4578  -2161       N  
ATOM   5072  N   ILE B 358      59.046  40.057  75.571  1.00120.50           N  
ANISOU 5072  N   ILE B 358    13022  16183  16578   1380  -3314  -3082       N  
ATOM   5073  CA  ILE B 358      59.812  39.018  76.246  1.00129.97           C  
ANISOU 5073  CA  ILE B 358    14038  17644  17701   1740  -3353  -3164       C  
ATOM   5074  C   ILE B 358      61.292  39.341  76.097  1.00135.43           C  
ANISOU 5074  C   ILE B 358    14095  18618  18744   1603  -3396  -3069       C  
ATOM   5075  O   ILE B 358      61.736  39.792  75.034  1.00128.05           O  
ANISOU 5075  O   ILE B 358    12880  17799  17976   1325  -3140  -2847       O  
ATOM   5076  CB  ILE B 358      59.467  37.628  75.679  1.00111.76           C  
ANISOU 5076  CB  ILE B 358    11978  15397  15090   2084  -3002  -3110       C  
ATOM   5077  CG1 ILE B 358      57.966  37.370  75.825  1.00110.16           C  
ANISOU 5077  CG1 ILE B 358    12338  14924  14593   2130  -2992  -3151       C  
ATOM   5078  CG2 ILE B 358      60.235  36.551  76.394  1.00131.86           C  
ANISOU 5078  CG2 ILE B 358    14365  18130  17604   2489  -3102  -3174       C  
ATOM   5079  CD1 ILE B 358      57.399  36.441  74.784  1.00130.13           C  
ANISOU 5079  CD1 ILE B 358    15152  17387  16903   2251  -2652  -3065       C  
ATOM   5080  N   SER B 359      62.050  39.122  77.168  1.00159.68           N  
ANISOU 5080  N   SER B 359    16914  21844  21912   1780  -3729  -3204       N  
ATOM   5081  CA  SER B 359      63.429  39.584  77.242  1.00170.93           C  
ANISOU 5081  CA  SER B 359    17676  23534  23736   1599  -3893  -3133       C  
ATOM   5082  C   SER B 359      64.141  38.870  78.381  1.00166.30           C  
ANISOU 5082  C   SER B 359    16894  23162  23132   1970  -4218  -3281       C  
ATOM   5083  O   SER B 359      63.514  38.482  79.371  1.00172.69           O  
ANISOU 5083  O   SER B 359    18113  23852  23651   2221  -4463  -3453       O  
ATOM   5084  CB  SER B 359      63.487  41.102  77.450  1.00172.43           C  
ANISOU 5084  CB  SER B 359    17745  23485  24284   1073  -4265  -3148       C  
ATOM   5085  OG  SER B 359      63.022  41.449  78.743  1.00178.10           O  
ANISOU 5085  OG  SER B 359    18768  23990  24911   1161  -4767  -3472       O  
ATOM   5086  N   ASN B 360      65.454  38.702  78.223  1.00156.58           N  
ANISOU 5086  N   ASN B 360    15002  22296  22196   2002  -4212  -3177       N  
ATOM   5087  CA  ASN B 360      66.343  38.200  79.273  1.00163.52           C  
ANISOU 5087  CA  ASN B 360    15557  23414  23160   2303  -4606  -3281       C  
ATOM   5088  C   ASN B 360      65.836  36.884  79.866  1.00161.56           C  
ANISOU 5088  C   ASN B 360    15767  23112  22507   2872  -4610  -3360       C  
ATOM   5089  O   ASN B 360      65.631  36.756  81.074  1.00156.23           O  
ANISOU 5089  O   ASN B 360    15328  22389  21645   3024  -5040  -3490       O  
ATOM   5090  CB  ASN B 360      66.524  39.248  80.377  1.00162.24           C  
ANISOU 5090  CB  ASN B 360    15325  23141  23178   1999  -5249  -3465       C  
ATOM   5091  CG  ASN B 360      66.986  40.592  79.847  1.00168.10           C  
ANISOU 5091  CG  ASN B 360    15660  23813  24398   1372  -5347  -3357       C  
ATOM   5092  OD1 ASN B 360      68.169  40.793  79.575  1.00176.71           O  
ANISOU 5092  OD1 ASN B 360    16027  25218  25896   1181  -5385  -3186       O  
ATOM   5093  ND2 ASN B 360      66.049  41.522  79.701  1.00146.68           N  
ANISOU 5093  ND2 ASN B 360    13384  20680  21666   1041  -5408  -3427       N  
ATOM   5094  N   CYS B 361      65.639  35.891  79.000  1.00154.57           N  
ANISOU 5094  N   CYS B 361    15020  22236  21474   3181  -4146  -3269       N  
ATOM   5095  CA  CYS B 361      65.133  34.605  79.461  1.00149.71           C  
ANISOU 5095  CA  CYS B 361    14865  21473  20545   3671  -4171  -3289       C  
ATOM   5096  C   CYS B 361      65.556  33.502  78.499  1.00150.50           C  
ANISOU 5096  C   CYS B 361    14839  21666  20677   4086  -3773  -3247       C  
ATOM   5097  O   CYS B 361      66.261  33.738  77.514  1.00153.13           O  
ANISOU 5097  O   CYS B 361    14694  22278  21212   4025  -3438  -3216       O  
ATOM   5098  CB  CYS B 361      63.610  34.633  79.619  1.00158.59           C  
ANISOU 5098  CB  CYS B 361    16720  22235  21300   3551  -4120  -3308       C  
ATOM   5099  SG  CYS B 361      62.709  35.102  78.129  1.00171.02           S  
ANISOU 5099  SG  CYS B 361    18547  23615  22819   3224  -3599  -3257       S  
ATOM   5100  N   VAL B 362      65.111  32.285  78.805  1.00157.26           N  
ANISOU 5100  N   VAL B 362    16136  22292  21324   4516  -3824  -3244       N  
ATOM   5101  CA  VAL B 362      65.387  31.094  78.010  1.00164.64           C  
ANISOU 5101  CA  VAL B 362    17093  23186  22276   5004  -3541  -3283       C  
ATOM   5102  C   VAL B 362      64.057  30.551  77.509  1.00153.52           C  
ANISOU 5102  C   VAL B 362    16417  21345  20569   4981  -3336  -3282       C  
ATOM   5103  O   VAL B 362      63.174  30.218  78.310  1.00153.41           O  
ANISOU 5103  O   VAL B 362    16905  21032  20352   4949  -3586  -3186       O  
ATOM   5104  CB  VAL B 362      66.143  30.029  78.820  1.00163.25           C  
ANISOU 5104  CB  VAL B 362    16781  23025  22220   5570  -3893  -3265       C  
ATOM   5105  CG1 VAL B 362      66.074  28.680  78.120  1.00156.91           C  
ANISOU 5105  CG1 VAL B 362    16250  21966  21401   6112  -3693  -3347       C  
ATOM   5106  CG2 VAL B 362      67.588  30.451  79.036  1.00156.33           C  
ANISOU 5106  CG2 VAL B 362    15058  22644  21696   5654  -4037  -3285       C  
ATOM   5107  N   ALA B 363      63.911  30.469  76.189  1.00151.55           N  
ANISOU 5107  N   ALA B 363    16204  21110  20270   4980  -2891  -3370       N  
ATOM   5108  CA  ALA B 363      62.690  29.996  75.551  1.00165.82           C  
ANISOU 5108  CA  ALA B 363    18659  22528  21816   4926  -2711  -3395       C  
ATOM   5109  C   ALA B 363      62.955  28.664  74.867  1.00168.16           C  
ANISOU 5109  C   ALA B 363    19110  22669  22116   5487  -2579  -3565       C  
ATOM   5110  O   ALA B 363      63.895  28.544  74.074  1.00166.83           O  
ANISOU 5110  O   ALA B 363    18509  22838  22039   5774  -2298  -3723       O  
ATOM   5111  CB  ALA B 363      62.175  31.014  74.533  1.00150.45           C  
ANISOU 5111  CB  ALA B 363    16726  20687  19752   4460  -2364  -3384       C  
ATOM   5112  N   ASP B 364      62.122  27.668  75.169  1.00171.62           N  
ANISOU 5112  N   ASP B 364    20150  22599  22457   5645  -2788  -3534       N  
ATOM   5113  CA  ASP B 364      62.249  26.338  74.577  1.00171.79           C  
ANISOU 5113  CA  ASP B 364    20439  22310  22522   6183  -2770  -3731       C  
ATOM   5114  C   ASP B 364      61.234  26.237  73.441  1.00175.12           C  
ANISOU 5114  C   ASP B 364    21341  22493  22703   5990  -2511  -3862       C  
ATOM   5115  O   ASP B 364      60.154  25.663  73.579  1.00178.68           O  
ANISOU 5115  O   ASP B 364    22376  22445  23071   5861  -2703  -3777       O  
ATOM   5116  CB  ASP B 364      62.044  25.259  75.637  1.00170.63           C  
ANISOU 5116  CB  ASP B 364    20654  21692  22488   6452  -3249  -3562       C  
ATOM   5117  CG  ASP B 364      62.427  23.876  75.147  1.00185.24           C  
ANISOU 5117  CG  ASP B 364    22716  23163  24504   7099  -3338  -3790       C  
ATOM   5118  OD1 ASP B 364      62.999  23.768  74.042  1.00187.36           O  
ANISOU 5118  OD1 ASP B 364    22771  23642  24774   7422  -3002  -4143       O  
ATOM   5119  OD2 ASP B 364      62.160  22.895  75.873  1.00191.90           O1-
ANISOU 5119  OD2 ASP B 364    23945  23499  25469   7298  -3757  -3614       O1-
ATOM   5120  N   TYR B 365      61.603  26.816  72.292  1.00156.97           N  
ANISOU 5120  N   TYR B 365    17539  20296  21807   2408  -3982   2193       N  
ATOM   5121  CA  TYR B 365      60.699  26.873  71.146  1.00157.21           C  
ANISOU 5121  CA  TYR B 365    17776  20227  21732   2082  -3766   1805       C  
ATOM   5122  C   TYR B 365      60.255  25.494  70.671  1.00155.97           C  
ANISOU 5122  C   TYR B 365    17762  19403  22094   2248  -3698   1637       C  
ATOM   5123  O   TYR B 365      59.213  25.386  70.016  1.00148.93           O  
ANISOU 5123  O   TYR B 365    17127  18267  21194   1990  -3602   1448       O  
ATOM   5124  CB  TYR B 365      61.352  27.617  69.978  1.00154.29           C  
ANISOU 5124  CB  TYR B 365    17196  20315  21113   1944  -3575   1314       C  
ATOM   5125  CG  TYR B 365      61.651  29.081  70.224  1.00158.47           C  
ANISOU 5125  CG  TYR B 365    17661  21451  21097   1646  -3717   1444       C  
ATOM   5126  CD1 TYR B 365      60.627  30.016  70.308  1.00136.70           C  
ANISOU 5126  CD1 TYR B 365    15266  18842  17832   1267  -3834   1504       C  
ATOM   5127  CD2 TYR B 365      62.960  29.533  70.338  1.00162.95           C  
ANISOU 5127  CD2 TYR B 365    17820  22450  21645   1749  -3794   1491       C  
ATOM   5128  CE1 TYR B 365      60.898  31.356  70.520  1.00143.01           C  
ANISOU 5128  CE1 TYR B 365    16092  20140  18106   1020  -4093   1606       C  
ATOM   5129  CE2 TYR B 365      63.240  30.870  70.548  1.00155.67           C  
ANISOU 5129  CE2 TYR B 365    16872  22014  20262   1438  -4031   1645       C  
ATOM   5130  CZ  TYR B 365      62.206  31.776  70.638  1.00159.86           C  
ANISOU 5130  CZ  TYR B 365    17838  22621  20280   1083  -4213   1697       C  
ATOM   5131  OH  TYR B 365      62.485  33.107  70.847  1.00160.66           O  
ANISOU 5131  OH  TYR B 365    17994  23152  19896    800  -4574   1838       O  
ATOM   5132  N   SER B 366      61.017  24.443  70.974  1.00155.89           N  
ANISOU 5132  N   SER B 366    17629  19068  22534   2691  -3808   1677       N  
ATOM   5133  CA  SER B 366      60.656  23.101  70.533  1.00157.87           C  
ANISOU 5133  CA  SER B 366    18080  18620  23282   2888  -3886   1518       C  
ATOM   5134  C   SER B 366      59.519  22.491  71.343  1.00156.07           C  
ANISOU 5134  C   SER B 366    18170  17861  23270   2681  -4057   2043       C  
ATOM   5135  O   SER B 366      58.982  21.455  70.938  1.00158.95           O  
ANISOU 5135  O   SER B 366    18761  17582  24051   2706  -4187   1967       O  
ATOM   5136  CB  SER B 366      61.878  22.181  70.591  1.00167.12           C  
ANISOU 5136  CB  SER B 366    19067  19637  24793   3482  -4034   1347       C  
ATOM   5137  OG  SER B 366      62.728  22.531  71.668  1.00171.88           O  
ANISOU 5137  OG  SER B 366    19445  20563  25299   3660  -4124   1674       O  
ATOM   5138  N   VAL B 367      59.144  23.096  72.472  1.00150.65           N  
ANISOU 5138  N   VAL B 367    17497  17440  22301   2501  -4099   2598       N  
ATOM   5139  CA  VAL B 367      58.015  22.584  73.243  1.00153.05           C  
ANISOU 5139  CA  VAL B 367    18032  17386  22734   2284  -4212   3170       C  
ATOM   5140  C   VAL B 367      56.700  22.929  72.554  1.00175.44           C  
ANISOU 5140  C   VAL B 367    21032  20231  25397   1808  -4079   3050       C  
ATOM   5141  O   VAL B 367      55.772  22.112  72.509  1.00180.72           O  
ANISOU 5141  O   VAL B 367    21876  20390  26401   1602  -4164   3262       O  
ATOM   5142  CB  VAL B 367      58.066  23.129  74.684  1.00155.12           C  
ANISOU 5142  CB  VAL B 367    18242  18017  22681   2372  -4305   3802       C  
ATOM   5143  CG1 VAL B 367      56.717  22.968  75.373  1.00152.03           C  
ANISOU 5143  CG1 VAL B 367    18016  17552  22197   2075  -4331   4412       C  
ATOM   5144  CG2 VAL B 367      59.160  22.431  75.478  1.00161.66           C  
ANISOU 5144  CG2 VAL B 367    18998  18599  23827   2863  -4489   3984       C  
ATOM   5145  N   LEU B 368      56.607  24.132  71.986  1.00165.77           N  
ANISOU 5145  N   LEU B 368    19768  19562  23656   1614  -3908   2698       N  
ATOM   5146  CA  LEU B 368      55.359  24.584  71.378  1.00156.97           C  
ANISOU 5146  CA  LEU B 368    18840  18517  22285   1197  -3797   2526       C  
ATOM   5147  C   LEU B 368      55.077  23.845  70.074  1.00160.64           C  
ANISOU 5147  C   LEU B 368    19436  18420  23178   1161  -3737   1981       C  
ATOM   5148  O   LEU B 368      54.036  23.194  69.927  1.00161.88           O  
ANISOU 5148  O   LEU B 368    19762  18116  23630    936  -3808   2103       O  
ATOM   5149  CB  LEU B 368      55.421  26.094  71.141  1.00148.80           C  
ANISOU 5149  CB  LEU B 368    17805  18197  20536   1040  -3711   2262       C  
ATOM   5150  CG  LEU B 368      55.923  26.916  72.329  1.00132.98           C  
ANISOU 5150  CG  LEU B 368    15694  16734  18098   1190  -3883   2708       C  
ATOM   5151  CD1 LEU B 368      56.133  28.368  71.933  1.00119.69           C  
ANISOU 5151  CD1 LEU B 368    14060  15656  15758   1033  -3916   2381       C  
ATOM   5152  CD2 LEU B 368      54.953  26.810  73.496  1.00138.37           C  
ANISOU 5152  CD2 LEU B 368    16463  17502  18609   1156  -4011   3374       C  
ATOM   5153  N   TYR B 369      56.001  23.941  69.113  1.00168.49           N  
ANISOU 5153  N   TYR B 369    20341  19469  24208   1410  -3632   1394       N  
ATOM   5154  CA  TYR B 369      55.790  23.345  67.796  1.00176.11           C  
ANISOU 5154  CA  TYR B 369    21455  19962  25496   1504  -3596    808       C  
ATOM   5155  C   TYR B 369      55.620  21.834  67.882  1.00181.26           C  
ANISOU 5155  C   TYR B 369    22242  19780  26850   1710  -3894    972       C  
ATOM   5156  O   TYR B 369      54.955  21.234  67.030  1.00177.05           O  
ANISOU 5156  O   TYR B 369    21937  18687  26648   1689  -4000    663       O  
ATOM   5157  CB  TYR B 369      56.961  23.705  66.878  1.00182.61           C  
ANISOU 5157  CB  TYR B 369    22087  21131  26167   1836  -3424    240       C  
ATOM   5158  CG  TYR B 369      56.858  23.184  65.459  1.00191.45           C  
ANISOU 5158  CG  TYR B 369    23355  21864  27524   2081  -3381   -415       C  
ATOM   5159  CD1 TYR B 369      55.856  23.627  64.604  1.00181.89           C  
ANISOU 5159  CD1 TYR B 369    22410  20555  26146   1802  -3254   -790       C  
ATOM   5160  CD2 TYR B 369      57.775  22.261  64.969  1.00195.21           C  
ANISOU 5160  CD2 TYR B 369    23729  22093  28349   2672  -3503   -698       C  
ATOM   5161  CE1 TYR B 369      55.765  23.161  63.305  1.00177.12           C  
ANISOU 5161  CE1 TYR B 369    21975  19567  25757   2111  -3242  -1410       C  
ATOM   5162  CE2 TYR B 369      57.691  21.789  63.670  1.00199.69           C  
ANISOU 5162  CE2 TYR B 369    24456  22330  29089   3021  -3517  -1308       C  
ATOM   5163  CZ  TYR B 369      56.684  22.242  62.844  1.00193.77           C  
ANISOU 5163  CZ  TYR B 369    23979  21440  28206   2742  -3382  -1653       C  
ATOM   5164  OH  TYR B 369      56.596  21.776  61.552  1.00192.33           O  
ANISOU 5164  OH  TYR B 369    23989  20893  28196   3168  -3422  -2278       O  
ATOM   5165  N   ASN B 370      56.196  21.207  68.906  1.00181.99           N  
ANISOU 5165  N   ASN B 370    22242  19730  27176   1920  -4093   1450       N  
ATOM   5166  CA  ASN B 370      56.094  19.770  69.110  1.00188.28           C  
ANISOU 5166  CA  ASN B 370    23226  19705  28607   2100  -4471   1666       C  
ATOM   5167  C   ASN B 370      55.158  19.420  70.267  1.00194.68           C  
ANISOU 5167  C   ASN B 370    24127  20286  29557   1704  -4616   2479       C  
ATOM   5168  O   ASN B 370      55.399  18.457  70.999  1.00199.25           O  
ANISOU 5168  O   ASN B 370    24792  20401  30513   1852  -4916   2902       O  
ATOM   5169  CB  ASN B 370      57.485  19.173  69.331  1.00189.98           C  
ANISOU 5169  CB  ASN B 370    23326  19867  28992   2698  -4642   1546       C  
ATOM   5170  CG  ASN B 370      57.530  17.685  69.065  1.00198.81           C  
ANISOU 5170  CG  ASN B 370    24732  20089  30718   3027  -5124   1465       C  
ATOM   5171  OD1 ASN B 370      56.625  17.121  68.450  1.00197.43           O  
ANISOU 5171  OD1 ASN B 370    24831  19306  30877   2850  -5337   1377       O  
ATOM   5172  ND2 ASN B 370      58.595  17.039  69.523  1.00200.88           N  
ANISOU 5172  ND2 ASN B 370    24964  20241  31122   3535  -5364   1470       N  
ATOM   5173  N   SER B 371      54.087  20.200  70.445  1.00204.78           N  
ANISOU 5173  N   SER B 371    25388  21929  30488   1222  -4416   2708       N  
ATOM   5174  CA  SER B 371      53.050  19.893  71.422  1.00213.62           C  
ANISOU 5174  CA  SER B 371    26533  22947  31685    830  -4512   3492       C  
ATOM   5175  C   SER B 371      51.757  19.401  70.790  1.00219.28           C  
ANISOU 5175  C   SER B 371    27411  23172  32734    404  -4625   3490       C  
ATOM   5176  O   SER B 371      50.927  18.819  71.497  1.00222.43           O  
ANISOU 5176  O   SER B 371    27811  23333  33369     63  -4780   4190       O  
ATOM   5177  CB  SER B 371      52.738  21.124  72.288  1.00203.05           C  
ANISOU 5177  CB  SER B 371    25020  22499  29632    667  -4264   3856       C  
ATOM   5178  OG  SER B 371      51.575  20.929  73.076  1.00210.41           O  
ANISOU 5178  OG  SER B 371    25927  23488  30530    296  -4300   4575       O  
ATOM   5179  N   ALA B 372      51.569  19.632  69.489  1.00202.66           N  
ANISOU 5179  N   ALA B 372    25427  20924  30650    419  -4557   2744       N  
ATOM   5180  CA  ALA B 372      50.417  19.138  68.734  1.00200.72           C  
ANISOU 5180  CA  ALA B 372    25365  20112  30789     91  -4718   2609       C  
ATOM   5181  C   ALA B 372      49.098  19.653  69.300  1.00192.65           C  
ANISOU 5181  C   ALA B 372    24224  19514  29461   -475  -4570   3110       C  
ATOM   5182  O   ALA B 372      48.068  18.979  69.213  1.00187.80           O  
ANISOU 5182  O   ALA B 372    23664  18417  29275   -856  -4784   3406       O  
ATOM   5183  CB  ALA B 372      50.412  17.608  68.666  1.00197.64           C  
ANISOU 5183  CB  ALA B 372    25180  18690  31224    168  -5244   2835       C  
ATOM   5184  N   SER B 373      49.114  20.853  69.878  1.00178.05           N  
ANISOU 5184  N   SER B 373    22207  18592  26850   -512  -4255   3212       N  
ATOM   5185  CA  SER B 373      47.903  21.471  70.400  1.00180.64           C  
ANISOU 5185  CA  SER B 373    22414  19498  26722   -925  -4122   3609       C  
ATOM   5186  C   SER B 373      47.319  22.524  69.472  1.00170.24           C  
ANISOU 5186  C   SER B 373    21218  18575  24890  -1044  -3920   2884       C  
ATOM   5187  O   SER B 373      46.150  22.890  69.635  1.00163.46           O  
ANISOU 5187  O   SER B 373    20303  18079  23726  -1384  -3866   3060       O  
ATOM   5188  CB  SER B 373      48.179  22.110  71.768  1.00175.97           C  
ANISOU 5188  CB  SER B 373    21617  19704  25540   -807  -4016   4244       C  
ATOM   5189  OG  SER B 373      46.972  22.442  72.432  1.00182.21           O  
ANISOU 5189  OG  SER B 373    22252  21048  25933  -1132  -3953   4791       O  
ATOM   5190  N   PHE B 374      48.089  23.005  68.501  1.00151.40           N  
ANISOU 5190  N   PHE B 374    18994  16154  22378   -764  -3814   2082       N  
ATOM   5191  CA  PHE B 374      47.692  24.131  67.670  1.00129.46           C  
ANISOU 5191  CA  PHE B 374    16386  13796  19008   -841  -3624   1378       C  
ATOM   5192  C   PHE B 374      47.250  23.660  66.292  1.00135.11           C  
ANISOU 5192  C   PHE B 374    17347  13806  20182   -856  -3668    686       C  
ATOM   5193  O   PHE B 374      47.880  22.786  65.689  1.00135.49           O  
ANISOU 5193  O   PHE B 374    17470  13168  20841   -572  -3806    452       O  
ATOM   5194  CB  PHE B 374      48.843  25.127  67.528  1.00131.60           C  
ANISOU 5194  CB  PHE B 374    16672  14588  18743   -553  -3476    999       C  
ATOM   5195  CG  PHE B 374      49.532  25.441  68.823  1.00143.44           C  
ANISOU 5195  CG  PHE B 374    17953  16606  19943   -411  -3519   1630       C  
ATOM   5196  CD1 PHE B 374      48.915  26.235  69.775  1.00132.68           C  
ANISOU 5196  CD1 PHE B 374    16539  15947  17925   -538  -3549   2060       C  
ATOM   5197  CD2 PHE B 374      50.799  24.947  69.088  1.00140.42           C  
ANISOU 5197  CD2 PHE B 374    17428  16024  19903    -75  -3565   1762       C  
ATOM   5198  CE1 PHE B 374      49.546  26.529  70.966  1.00122.07           C  
ANISOU 5198  CE1 PHE B 374    15033  15042  16307   -315  -3639   2622       C  
ATOM   5199  CE2 PHE B 374      51.436  25.238  70.278  1.00135.11           C  
ANISOU 5199  CE2 PHE B 374    16578  15776  18982     98  -3631   2306       C  
ATOM   5200  CZ  PHE B 374      50.808  26.030  71.218  1.00133.75           C  
ANISOU 5200  CZ  PHE B 374    16382  16247  18189    -12  -3675   2743       C  
ATOM   5201  N   SER B 375      46.163  24.254  65.797  1.00144.60           N  
ANISOU 5201  N   SER B 375    18700  15193  21050  -1120  -3592    322       N  
ATOM   5202  CA  SER B 375      45.701  23.985  64.442  1.00138.25           C  
ANISOU 5202  CA  SER B 375    18180  13758  20592  -1082  -3630   -434       C  
ATOM   5203  C   SER B 375      46.510  24.731  63.389  1.00139.96           C  
ANISOU 5203  C   SER B 375    18628  14099  20453   -744  -3429  -1285       C  
ATOM   5204  O   SER B 375      46.462  24.357  62.212  1.00142.31           O  
ANISOU 5204  O   SER B 375    19166  13794  21112   -524  -3467  -1928       O  
ATOM   5205  CB  SER B 375      44.221  24.352  64.311  1.00124.43           C  
ANISOU 5205  CB  SER B 375    16506  12171  18602  -1474  -3629   -542       C  
ATOM   5206  OG  SER B 375      44.022  25.738  64.524  1.00113.80           O  
ANISOU 5206  OG  SER B 375    15234  11742  16265  -1541  -3436   -771       O  
ATOM   5207  N   THR B 376      47.246  25.769  63.779  1.00131.74           N  
ANISOU 5207  N   THR B 376    16354  15841  17859   1335  -1817  -2688       N  
ATOM   5208  CA  THR B 376      48.066  26.532  62.847  1.00129.08           C  
ANISOU 5208  CA  THR B 376    15890  15926  17228   1301  -1669  -2939       C  
ATOM   5209  C   THR B 376      49.399  26.862  63.501  1.00133.33           C  
ANISOU 5209  C   THR B 376    16170  16712  17776   1471  -1639  -2844       C  
ATOM   5210  O   THR B 376      49.435  27.366  64.628  1.00125.69           O  
ANISOU 5210  O   THR B 376    15161  15810  16786   1449  -1744  -2534       O  
ATOM   5211  CB  THR B 376      47.362  27.821  62.403  1.00117.98           C  
ANISOU 5211  CB  THR B 376    14585  14804  15439    990  -1625  -2863       C  
ATOM   5212  OG1 THR B 376      46.137  27.493  61.736  1.00115.51           O  
ANISOU 5212  OG1 THR B 376    14466  14320  15100    854  -1679  -2983       O  
ATOM   5213  CG2 THR B 376      48.250  28.618  61.457  1.00120.14           C  
ANISOU 5213  CG2 THR B 376    14724  15494  15431    962  -1422  -3055       C  
ATOM   5214  N   PHE B 377      50.488  26.569  62.789  1.00135.19           N  
ANISOU 5214  N   PHE B 377    16217  17114  18036   1655  -1502  -3134       N  
ATOM   5215  CA  PHE B 377      51.838  26.881  63.264  1.00125.17           C  
ANISOU 5215  CA  PHE B 377    14628  16138  16792   1811  -1464  -3098       C  
ATOM   5216  C   PHE B 377      52.720  26.993  62.014  1.00127.49           C  
ANISOU 5216  C   PHE B 377    14745  16728  16969   1870  -1223  -3438       C  
ATOM   5217  O   PHE B 377      53.370  26.026  61.616  1.00136.14           O  
ANISOU 5217  O   PHE B 377    15738  17744  18245   2174  -1156  -3678       O  
ATOM   5218  CB  PHE B 377      52.357  25.829  64.229  1.00136.04           C  
ANISOU 5218  CB  PHE B 377    15905  17287  18499   2171  -1596  -2985       C  
ATOM   5219  CG  PHE B 377      53.451  26.318  65.149  1.00147.62           C  
ANISOU 5219  CG  PHE B 377    17052  19079  19957   2293  -1669  -2838       C  
ATOM   5220  CD1 PHE B 377      54.556  26.995  64.653  1.00150.14           C  
ANISOU 5220  CD1 PHE B 377    17050  19825  20172   2256  -1530  -3020       C  
ATOM   5221  CD2 PHE B 377      53.374  26.093  66.514  1.00141.07           C  
ANISOU 5221  CD2 PHE B 377    16224  18154  19224   2453  -1879  -2518       C  
ATOM   5222  CE1 PHE B 377      55.557  27.436  65.500  1.00127.36           C  
ANISOU 5222  CE1 PHE B 377    13825  17253  17315   2342  -1629  -2931       C  
ATOM   5223  CE2 PHE B 377      54.372  26.534  67.365  1.00124.59           C  
ANISOU 5223  CE2 PHE B 377    13826  16415  17100   2584  -1992  -2430       C  
ATOM   5224  CZ  PHE B 377      55.465  27.205  66.856  1.00124.49           C  
ANISOU 5224  CZ  PHE B 377    13467  16814  17020   2512  -1884  -2659       C  
ATOM   5225  N   LYS B 378      52.711  28.176  61.403  1.00131.29           N  
ANISOU 5225  N   LYS B 378    15201  17537  17147   1597  -1070  -3437       N  
ATOM   5226  CA  LYS B 378      53.507  28.470  60.219  1.00145.87           C  
ANISOU 5226  CA  LYS B 378    16877  19724  18825   1626   -788  -3682       C  
ATOM   5227  C   LYS B 378      54.512  29.560  60.559  1.00136.39           C  
ANISOU 5227  C   LYS B 378    15345  18887  17589   1486   -676  -3546       C  
ATOM   5228  O   LYS B 378      54.129  30.626  61.052  1.00132.56           O  
ANISOU 5228  O   LYS B 378    14913  18456  16997   1193   -726  -3314       O  
ATOM   5229  CB  LYS B 378      52.628  28.922  59.047  1.00151.06           C  
ANISOU 5229  CB  LYS B 378    17788  20465  19142   1440   -654  -3781       C  
ATOM   5230  CG  LYS B 378      51.431  28.032  58.745  1.00148.70           C  
ANISOU 5230  CG  LYS B 378    17810  19819  18871   1480   -814  -3927       C  
ATOM   5231  CD  LYS B 378      50.672  28.561  57.531  1.00147.21           C  
ANISOU 5231  CD  LYS B 378    17819  19829  18285   1331   -697  -4049       C  
ATOM   5232  CE  LYS B 378      49.376  27.802  57.290  1.00139.94           C  
ANISOU 5232  CE  LYS B 378    17177  18592  17401   1307   -903  -4204       C  
ATOM   5233  NZ  LYS B 378      49.355  27.137  55.956  1.00135.23           N  
ANISOU 5233  NZ  LYS B 378    16654  18092  16634   1485   -818  -4667       N  
ATOM   5234  N   CYS B 379      55.788  29.299  60.293  1.00140.63           N  
ANISOU 5234  N   CYS B 379    15526  19665  18241   1693   -522  -3708       N  
ATOM   5235  CA  CYS B 379      56.851  30.260  60.546  1.00140.27           C  
ANISOU 5235  CA  CYS B 379    15088  19977  18231   1547   -402  -3626       C  
ATOM   5236  C   CYS B 379      57.452  30.735  59.230  1.00146.97           C  
ANISOU 5236  C   CYS B 379    15777  21167  18900   1494     -3  -3762       C  
ATOM   5237  O   CYS B 379      57.617  29.951  58.290  1.00161.40           O  
ANISOU 5237  O   CYS B 379    17635  23036  20654   1757    161  -4005       O  
ATOM   5238  CB  CYS B 379      57.942  29.661  61.440  1.00142.58           C  
ANISOU 5238  CB  CYS B 379    15001  20346  18826   1830   -550  -3658       C  
ATOM   5239  SG  CYS B 379      57.374  29.149  63.081  1.00153.74           S  
ANISOU 5239  SG  CYS B 379    16569  21437  20409   1955   -990  -3428       S  
ATOM   5240  N   TYR B 380      57.778  32.024  59.174  1.00150.90           N  
ANISOU 5240  N   TYR B 380    16108  21897  19330   1161    167  -3603       N  
ATOM   5241  CA  TYR B 380      58.253  32.677  57.960  1.00158.37           C  
ANISOU 5241  CA  TYR B 380    16924  23163  20086   1058    595  -3625       C  
ATOM   5242  C   TYR B 380      59.674  33.168  58.201  1.00163.53           C  
ANISOU 5242  C   TYR B 380    17011  24130  20992    987    761  -3618       C  
ATOM   5243  O   TYR B 380      59.906  33.973  59.108  1.00161.31           O  
ANISOU 5243  O   TYR B 380    16553  23841  20896    712    623  -3478       O  
ATOM   5244  CB  TYR B 380      57.334  33.841  57.576  1.00149.49           C  
ANISOU 5244  CB  TYR B 380    16108  22000  18691    704    710  -3393       C  
ATOM   5245  CG  TYR B 380      55.874  33.464  57.420  1.00150.96           C  
ANISOU 5245  CG  TYR B 380    16804  21912  18643    739    512  -3386       C  
ATOM   5246  CD1 TYR B 380      55.046  33.339  58.530  1.00147.63           C  
ANISOU 5246  CD1 TYR B 380    16590  21166  18335    666    141  -3272       C  
ATOM   5247  CD2 TYR B 380      55.321  33.243  56.165  1.00153.36           C  
ANISOU 5247  CD2 TYR B 380    17355  22315  18600    852    696  -3496       C  
ATOM   5248  CE1 TYR B 380      53.714  32.997  58.396  1.00143.93           C  
ANISOU 5248  CE1 TYR B 380    16530  20461  17695    675    -27  -3257       C  
ATOM   5249  CE2 TYR B 380      53.987  32.902  56.021  1.00153.04           C  
ANISOU 5249  CE2 TYR B 380    17725  22052  18372    864    487  -3521       C  
ATOM   5250  CZ  TYR B 380      53.190  32.780  57.140  1.00149.46           C  
ANISOU 5250  CZ  TYR B 380    17439  21259  18091    760    134  -3394       C  
ATOM   5251  OH  TYR B 380      51.863  32.441  57.005  1.00142.27           O  
ANISOU 5251  OH  TYR B 380    16883  20138  17034    752    -61  -3410       O  
ATOM   5252  N   GLY B 381      60.620  32.682  57.398  1.00179.03           N  
ANISOU 5252  N   GLY B 381    18672  26381  22970   1239   1052  -3795       N  
ATOM   5253  CA  GLY B 381      62.010  33.072  57.549  1.00189.25           C  
ANISOU 5253  CA  GLY B 381    19362  28014  24532   1188   1235  -3803       C  
ATOM   5254  C   GLY B 381      62.786  32.120  58.432  1.00185.33           C  
ANISOU 5254  C   GLY B 381    18530  27540  24347   1521    957  -3962       C  
ATOM   5255  O   GLY B 381      63.607  31.337  57.949  1.00185.90           O  
ANISOU 5255  O   GLY B 381    18326  27821  24488   1883   1125  -4152       O  
ATOM   5256  N   VAL B 382      62.534  32.182  59.740  1.00182.94           N  
ANISOU 5256  N   VAL B 382    18254  27043  24212   1440    537  -3876       N  
ATOM   5257  CA  VAL B 382      63.116  31.205  60.650  1.00181.00           C  
ANISOU 5257  CA  VAL B 382    17766  26796  24209   1820    231  -3978       C  
ATOM   5258  C   VAL B 382      62.454  29.848  60.421  1.00184.77           C  
ANISOU 5258  C   VAL B 382    18645  26952  24609   2241    129  -4086       C  
ATOM   5259  O   VAL B 382      61.402  29.742  59.781  1.00186.53           O  
ANISOU 5259  O   VAL B 382    19347  26930  24597   2174    194  -4089       O  
ATOM   5260  CB  VAL B 382      62.957  31.688  62.103  1.00180.88           C  
ANISOU 5260  CB  VAL B 382    17707  26697  24322   1640   -186  -3840       C  
ATOM   5261  CG1 VAL B 382      61.471  31.909  62.430  1.00174.41           C  
ANISOU 5261  CG1 VAL B 382    17501  25478  23290   1453   -377  -3671       C  
ATOM   5262  CG2 VAL B 382      63.637  30.740  63.112  1.00168.66           C  
ANISOU 5262  CG2 VAL B 382    15871  25219  22993   2072   -511  -3900       C  
ATOM   5263  N   SER B 383      63.110  28.789  60.899  1.00166.28           N  
ANISOU 5263  N   SER B 383    16081  24612  22485   2691    -22  -4191       N  
ATOM   5264  CA  SER B 383      62.546  27.452  60.823  1.00170.44           C  
ANISOU 5264  CA  SER B 383    16967  24755  23037   3096   -135  -4291       C  
ATOM   5265  C   SER B 383      62.113  26.985  62.201  1.00169.54           C  
ANISOU 5265  C   SER B 383    17001  24344  23073   3227   -558  -4099       C  
ATOM   5266  O   SER B 383      62.920  27.013  63.140  1.00162.59           O  
ANISOU 5266  O   SER B 383    15737  23678  22363   3368   -751  -4022       O  
ATOM   5267  CB  SER B 383      63.569  26.477  60.238  1.00173.10           C  
ANISOU 5267  CB  SER B 383    17001  25254  23517   3591     62  -4540       C  
ATOM   5268  OG  SER B 383      63.985  26.908  58.954  1.00162.64           O  
ANISOU 5268  OG  SER B 383    15532  24253  22012   3504    489  -4698       O  
ATOM   5269  N   PRO B 384      60.864  26.545  62.373  1.00193.58           N  
ANISOU 5269  N   PRO B 384    20570  26927  26054   3200   -711  -4008       N  
ATOM   5270  CA  PRO B 384      60.465  25.997  63.675  1.00188.25           C  
ANISOU 5270  CA  PRO B 384    20036  25968  25522   3380  -1064  -3779       C  
ATOM   5271  C   PRO B 384      61.250  24.758  64.021  1.00187.90           C  
ANISOU 5271  C   PRO B 384    19794  25852  25748   3950  -1131  -3832       C  
ATOM   5272  O   PRO B 384      61.210  24.315  65.173  1.00183.97           O  
ANISOU 5272  O   PRO B 384    19309  25220  25372   4182  -1404  -3603       O  
ATOM   5273  CB  PRO B 384      58.973  25.688  63.491  1.00199.75           C  
ANISOU 5273  CB  PRO B 384    22068  26938  26890   3231  -1117  -3708       C  
ATOM   5274  CG  PRO B 384      58.835  25.488  62.022  1.00195.18           C  
ANISOU 5274  CG  PRO B 384    21615  26346  26199   3207   -824  -4010       C  
ATOM   5275  CD  PRO B 384      59.763  26.486  61.402  1.00196.12           C  
ANISOU 5275  CD  PRO B 384    21354  26989  26174   3028   -572  -4104       C  
ATOM   5276  N   THR B 385      61.993  24.205  63.064  1.00203.43           N  
ANISOU 5276  N   THR B 385    21570  27930  27792   4221   -876  -4112       N  
ATOM   5277  CA  THR B 385      62.722  22.950  63.246  1.00206.92           C  
ANISOU 5277  CA  THR B 385    21855  28258  28508   4818   -896  -4192       C  
ATOM   5278  C   THR B 385      63.974  23.175  64.094  1.00191.99           C  
ANISOU 5278  C   THR B 385    19381  26834  26732   5038  -1032  -4092       C  
ATOM   5279  O   THR B 385      65.099  23.236  63.596  1.00190.03           O  
ANISOU 5279  O   THR B 385    18663  26996  26543   5202   -842  -4282       O  
ATOM   5280  CB  THR B 385      63.101  22.373  61.890  1.00202.27           C  
ANISOU 5280  CB  THR B 385    21249  27676  27926   5040   -560  -4567       C  
ATOM   5281  OG1 THR B 385      63.902  23.326  61.182  1.00200.90           O  
ANISOU 5281  OG1 THR B 385    20673  28074  27586   4826   -297  -4694       O  
ATOM   5282  CG2 THR B 385      61.862  22.057  61.083  1.00190.77           C  
ANISOU 5282  CG2 THR B 385    20353  25776  26354   4864   -484  -4719       C  
ATOM   5283  N   LYS B 386      63.764  23.284  65.404  1.00176.37           N  
ANISOU 5283  N   LYS B 386    17419  24821  24772   5060  -1370  -3795       N  
ATOM   5284  CA  LYS B 386      64.864  23.416  66.363  1.00195.22           C  
ANISOU 5284  CA  LYS B 386    19271  27658  27245   5316  -1587  -3700       C  
ATOM   5285  C   LYS B 386      65.799  24.580  66.027  1.00199.72           C  
ANISOU 5285  C   LYS B 386    19286  28840  27757   4981  -1472  -3873       C  
ATOM   5286  O   LYS B 386      67.010  24.495  66.253  1.00200.22           O  
ANISOU 5286  O   LYS B 386    18773  29340  27962   5255  -1507  -3955       O  
ATOM   5287  CB  LYS B 386      65.678  22.115  66.478  1.00200.91           C  
ANISOU 5287  CB  LYS B 386    19792  28323  28223   6024  -1585  -3729       C  
ATOM   5288  CG  LYS B 386      65.133  21.128  67.498  1.00194.34           C  
ANISOU 5288  CG  LYS B 386    19295  27042  27502   6431  -1836  -3407       C  
ATOM   5289  CD  LYS B 386      65.528  21.512  68.913  1.00187.93           C  
ANISOU 5289  CD  LYS B 386    18200  26605  26601   6556  -2209  -3132       C  
ATOM   5290  CE  LYS B 386      65.123  20.447  69.918  1.00179.34           C  
ANISOU 5290  CE  LYS B 386    17408  25121  25614   7067  -2410  -2756       C  
ATOM   5291  NZ  LYS B 386      65.419  20.868  71.316  1.00178.05           N  
ANISOU 5291  NZ  LYS B 386    17009  25374  25268   7206  -2790  -2482       N  
ATOM   5292  N   LEU B 387      65.261  25.675  65.485  1.00179.45           N  
ANISOU 5292  N   LEU B 387    16865  26309  25011   4392  -1325  -3917       N  
ATOM   5293  CA  LEU B 387      66.080  26.875  65.325  1.00182.07           C  
ANISOU 5293  CA  LEU B 387    16682  27156  25339   4013  -1227  -4022       C  
ATOM   5294  C   LEU B 387      66.020  27.735  66.564  1.00185.19           C  
ANISOU 5294  C   LEU B 387    16954  27723  25687   3754  -1595  -3883       C  
ATOM   5295  O   LEU B 387      66.336  28.931  66.518  1.00177.94           O  
ANISOU 5295  O   LEU B 387    15757  27088  24763   3286  -1548  -3953       O  
ATOM   5296  CB  LEU B 387      65.659  27.674  64.092  1.00175.84           C  
ANISOU 5296  CB  LEU B 387    16071  26344  24398   3542   -844  -4117       C  
ATOM   5297  CG  LEU B 387      66.693  27.659  62.960  1.00168.28           C  
ANISOU 5297  CG  LEU B 387    14677  25744  23519   3632   -431  -4331       C  
ATOM   5298  CD1 LEU B 387      66.810  26.269  62.363  1.00164.66           C  
ANISOU 5298  CD1 LEU B 387    14354  25095  23113   4206   -294  -4480       C  
ATOM   5299  CD2 LEU B 387      66.335  28.666  61.883  1.00180.35           C  
ANISOU 5299  CD2 LEU B 387    16336  27329  24860   3137    -59  -4349       C  
ATOM   5300  N   ASN B 388      65.599  27.125  67.673  1.00194.89           N  
ANISOU 5300  N   ASN B 388    18404  28764  26883   4066  -1948  -3685       N  
ATOM   5301  CA  ASN B 388      65.784  27.728  68.976  1.00182.95           C  
ANISOU 5301  CA  ASN B 388    16686  27522  25306   3997  -2345  -3592       C  
ATOM   5302  C   ASN B 388      67.256  27.972  69.246  1.00182.41           C  
ANISOU 5302  C   ASN B 388    15841  28054  25411   4123  -2444  -3778       C  
ATOM   5303  O   ASN B 388      67.600  28.678  70.200  1.00180.49           O  
ANISOU 5303  O   ASN B 388    15304  28146  25130   3985  -2770  -3808       O  
ATOM   5304  CB  ASN B 388      65.200  26.815  70.061  1.00175.13           C  
ANISOU 5304  CB  ASN B 388    16034  26270  24236   4451  -2658  -3309       C  
ATOM   5305  CG  ASN B 388      65.528  25.350  69.833  1.00186.27           C  
ANISOU 5305  CG  ASN B 388    17464  27481  25829   5083  -2572  -3255       C  
ATOM   5306  OD1 ASN B 388      66.441  25.023  69.077  1.00192.60           O  
ANISOU 5306  OD1 ASN B 388    17896  28478  26807   5267  -2356  -3463       O  
ATOM   5307  ND2 ASN B 388      64.807  24.466  70.512  1.00176.58           N  
ANISOU 5307  ND2 ASN B 388    16655  25860  24579   5433  -2723  -2963       N  
ATOM   5308  N   ASP B 389      68.135  27.391  68.420  1.00185.11           N  
ANISOU 5308  N   ASP B 389    15830  28559  25946   4395  -2176  -3928       N  
ATOM   5309  CA  ASP B 389      69.574  27.585  68.565  1.00195.28           C  
ANISOU 5309  CA  ASP B 389    16312  30450  27436   4522  -2227  -4111       C  
ATOM   5310  C   ASP B 389      69.955  29.057  68.540  1.00196.89           C  
ANISOU 5310  C   ASP B 389    16124  30992  27694   3866  -2209  -4273       C  
ATOM   5311  O   ASP B 389      70.936  29.451  69.175  1.00201.14           O  
ANISOU 5311  O   ASP B 389    16020  32030  28375   3864  -2450  -4411       O  
ATOM   5312  CB  ASP B 389      70.306  26.852  67.440  1.00190.05           C  
ANISOU 5312  CB  ASP B 389    15394  29867  26949   4842  -1828  -4253       C  
ATOM   5313  CG  ASP B 389      69.992  25.378  67.409  1.00194.05           C  
ANISOU 5313  CG  ASP B 389    16277  29984  27469   5494  -1824  -4140       C  
ATOM   5314  OD1 ASP B 389      69.531  24.841  68.437  1.00200.45           O  
ANISOU 5314  OD1 ASP B 389    17362  30588  28212   5797  -2168  -3918       O  
ATOM   5315  OD2 ASP B 389      70.177  24.765  66.337  1.00198.52           O1-
ANISOU 5315  OD2 ASP B 389    16885  30429  28115   5702  -1456  -4272       O1-
ATOM   5316  N   LEU B 390      69.191  29.883  67.829  1.00188.00           N  
ANISOU 5316  N   LEU B 390    15364  29592  26474   3310  -1937  -4262       N  
ATOM   5317  CA  LEU B 390      69.573  31.263  67.562  1.00183.90           C  
ANISOU 5317  CA  LEU B 390    14494  29306  26073   2672  -1797  -4398       C  
ATOM   5318  C   LEU B 390      69.192  32.198  68.711  1.00178.36           C  
ANISOU 5318  C   LEU B 390    13858  28618  25294   2325  -2210  -4403       C  
ATOM   5319  O   LEU B 390      68.251  31.946  69.469  1.00180.17           O  
ANISOU 5319  O   LEU B 390    14605  28569  25283   2464  -2494  -4244       O  
ATOM   5320  CB  LEU B 390      68.935  31.741  66.259  1.00179.08           C  
ANISOU 5320  CB  LEU B 390    14260  28403  25378   2281  -1297  -4348       C  
ATOM   5321  CG  LEU B 390      69.114  30.785  65.077  1.00178.44           C  
ANISOU 5321  CG  LEU B 390    14243  28272  25285   2649   -892  -4372       C  
ATOM   5322  CD1 LEU B 390      68.354  31.301  63.864  1.00165.46           C  
ANISOU 5322  CD1 LEU B 390    13030  26371  23464   2285   -453  -4314       C  
ATOM   5323  CD2 LEU B 390      70.593  30.573  64.758  1.00177.42           C  
ANISOU 5323  CD2 LEU B 390    13320  28662  25429   2866   -720  -4540       C  
ATOM   5324  N   CYS B 391      69.946  33.292  68.823  1.00176.12           N  
ANISOU 5324  N   CYS B 391    13026  28660  25232   1868  -2223  -4600       N  
ATOM   5325  CA  CYS B 391      69.726  34.341  69.808  1.00176.79           C  
ANISOU 5325  CA  CYS B 391    13097  28781  25294   1471  -2583  -4702       C  
ATOM   5326  C   CYS B 391      69.060  35.548  69.157  1.00184.32           C  
ANISOU 5326  C   CYS B 391    14367  29399  26266    799  -2264  -4670       C  
ATOM   5327  O   CYS B 391      69.266  35.830  67.974  1.00193.39           O  
ANISOU 5327  O   CYS B 391    15430  30496  27554    551  -1765  -4636       O  
ATOM   5328  CB  CYS B 391      71.047  34.771  70.457  1.00185.82           C  
ANISOU 5328  CB  CYS B 391    13374  30501  26729   1396  -2866  -4999       C  
ATOM   5329  SG  CYS B 391      71.826  33.486  71.458  1.00199.04           S  
ANISOU 5329  SG  CYS B 391    14648  32642  28335   2226  -3344  -5023       S  
ATOM   5330  N   PHE B 392      68.264  36.269  69.946  1.00181.10           N  
ANISOU 5330  N   PHE B 392    14331  28778  25699    540  -2541  -4666       N  
ATOM   5331  CA  PHE B 392      67.513  37.406  69.437  1.00178.39           C  
ANISOU 5331  CA  PHE B 392    14362  28067  25352    -41  -2271  -4605       C  
ATOM   5332  C   PHE B 392      67.457  38.499  70.491  1.00177.41           C  
ANISOU 5332  C   PHE B 392    14162  27965  25280   -408  -2641  -4810       C  
ATOM   5333  O   PHE B 392      67.383  38.215  71.690  1.00173.09           O  
ANISOU 5333  O   PHE B 392    13628  27582  24556   -121  -3142  -4898       O  
ATOM   5334  CB  PHE B 392      66.096  36.990  69.018  1.00150.96           C  
ANISOU 5334  CB  PHE B 392    11714  24118  21526     92  -2116  -4309       C  
ATOM   5335  CG  PHE B 392      66.063  36.137  67.783  1.00151.13           C  
ANISOU 5335  CG  PHE B 392    11855  24058  21508    335  -1696  -4170       C  
ATOM   5336  CD1 PHE B 392      66.226  36.706  66.531  1.00152.83           C  
ANISOU 5336  CD1 PHE B 392    12007  24230  21831      0  -1182  -4134       C  
ATOM   5337  CD2 PHE B 392      65.895  34.766  67.875  1.00151.03           C  
ANISOU 5337  CD2 PHE B 392    12017  24015  21353    917  -1804  -4081       C  
ATOM   5338  CE1 PHE B 392      66.208  35.926  65.392  1.00158.48           C  
ANISOU 5338  CE1 PHE B 392    12836  24921  22458    258   -808  -4050       C  
ATOM   5339  CE2 PHE B 392      65.878  33.980  66.739  1.00161.29           C  
ANISOU 5339  CE2 PHE B 392    13432  25229  22624   1148  -1436  -4023       C  
ATOM   5340  CZ  PHE B 392      66.034  34.561  65.496  1.00163.35           C  
ANISOU 5340  CZ  PHE B 392    13629  25497  22938    827   -949  -4027       C  
ATOM   5341  N   THR B 393      67.501  39.750  70.029  1.00180.51           N  
ANISOU 5341  N   THR B 393    14481  28190  25913  -1026  -2379  -4887       N  
ATOM   5342  CA  THR B 393      67.438  40.890  70.937  1.00167.44           C  
ANISOU 5342  CA  THR B 393    12774  26484  24362  -1430  -2691  -5133       C  
ATOM   5343  C   THR B 393      66.139  40.887  71.732  1.00165.61           C  
ANISOU 5343  C   THR B 393    13261  25959  23703  -1265  -2982  -5014       C  
ATOM   5344  O   THR B 393      66.145  40.768  72.962  1.00161.78           O  
ANISOU 5344  O   THR B 393    12738  25683  23049  -1037  -3495  -5184       O  
ATOM   5345  CB  THR B 393      67.586  42.191  70.148  1.00169.95           C  
ANISOU 5345  CB  THR B 393    12983  26546  25043  -2116  -2262  -5162       C  
ATOM   5346  OG1 THR B 393      68.710  42.094  69.263  1.00175.99           O  
ANISOU 5346  OG1 THR B 393    13115  27577  26176  -2234  -1891  -5185       O  
ATOM   5347  CG2 THR B 393      67.770  43.365  71.089  1.00162.57           C  
ANISOU 5347  CG2 THR B 393    11861  25575  24334  -2557  -2597  -5514       C  
ATOM   5348  N   ASN B 394      65.010  41.021  71.041  1.00161.08           N  
ANISOU 5348  N   ASN B 394    13333  24939  22932  -1355  -2655  -4716       N  
ATOM   5349  CA  ASN B 394      63.705  41.041  71.682  1.00143.18           C  
ANISOU 5349  CA  ASN B 394    11743  22381  20278  -1216  -2861  -4564       C  
ATOM   5350  C   ASN B 394      62.744  40.124  70.944  1.00143.81           C  
ANISOU 5350  C   ASN B 394    12358  22207  20075   -908  -2604  -4194       C  
ATOM   5351  O   ASN B 394      62.703  40.110  69.710  1.00141.52           O  
ANISOU 5351  O   ASN B 394    12128  21779  19865  -1042  -2153  -4048       O  
ATOM   5352  CB  ASN B 394      63.126  42.459  71.737  1.00137.32           C  
ANISOU 5352  CB  ASN B 394    11275  21291  19608  -1737  -2774  -4629       C  
ATOM   5353  CG  ASN B 394      63.813  43.327  72.769  1.00157.90           C  
ANISOU 5353  CG  ASN B 394    13478  24088  22429  -1997  -3157  -5054       C  
ATOM   5354  OD1 ASN B 394      63.666  43.114  73.972  1.00167.36           O  
ANISOU 5354  OD1 ASN B 394    14729  25480  23380  -1716  -3644  -5207       O  
ATOM   5355  ND2 ASN B 394      64.569  44.315  72.303  1.00169.33           N  
ANISOU 5355  ND2 ASN B 394    14513  25484  24339  -2534  -2935  -5254       N  
ATOM   5356  N   VAL B 395      61.976  39.361  71.714  1.00145.87           N  
ANISOU 5356  N   VAL B 395    12997  22422  20006   -491  -2894  -4049       N  
ATOM   5357  CA  VAL B 395      60.886  38.543  71.199  1.00130.56           C  
ANISOU 5357  CA  VAL B 395    11606  20188  17814   -235  -2718  -3723       C  
ATOM   5358  C   VAL B 395      59.583  39.169  71.672  1.00130.75           C  
ANISOU 5358  C   VAL B 395    12197  19901  17581   -366  -2798  -3585       C  
ATOM   5359  O   VAL B 395      59.372  39.342  72.879  1.00140.87           O  
ANISOU 5359  O   VAL B 395    13548  21273  18702   -244  -3168  -3650       O  
ATOM   5360  CB  VAL B 395      60.999  37.084  71.666  1.00133.01           C  
ANISOU 5360  CB  VAL B 395    11893  20639  18007    357  -2932  -3613       C  
ATOM   5361  CG1 VAL B 395      59.784  36.287  71.214  1.00111.74           C  
ANISOU 5361  CG1 VAL B 395     9774  17580  15104    563  -2774  -3307       C  
ATOM   5362  CG2 VAL B 395      62.280  36.457  71.139  1.00145.21           C  
ANISOU 5362  CG2 VAL B 395    12878  22488  19809    528  -2825  -3750       C  
ATOM   5363  N   TYR B 396      58.719  39.522  70.727  1.00119.65           N  
ANISOU 5363  N   TYR B 396    11185  18167  16110   -584  -2453  -3399       N  
ATOM   5364  CA  TYR B 396      57.410  40.074  71.033  1.00107.80           C  
ANISOU 5364  CA  TYR B 396    10225  16368  14368   -680  -2480  -3235       C  
ATOM   5365  C   TYR B 396      56.346  39.014  70.782  1.00107.80           C  
ANISOU 5365  C   TYR B 396    10650  16179  14131   -357  -2432  -2944       C  
ATOM   5366  O   TYR B 396      56.481  38.176  69.887  1.00121.48           O  
ANISOU 5366  O   TYR B 396    12347  17897  15914   -217  -2229  -2878       O  
ATOM   5367  CB  TYR B 396      57.123  41.323  70.192  1.00103.41           C  
ANISOU 5367  CB  TYR B 396     9812  15572  13909  -1150  -2138  -3214       C  
ATOM   5368  CG  TYR B 396      58.112  42.451  70.406  1.00126.03           C  
ANISOU 5368  CG  TYR B 396    12269  18530  17088  -1541  -2147  -3497       C  
ATOM   5369  CD1 TYR B 396      58.019  43.288  71.513  1.00123.00           C  
ANISOU 5369  CD1 TYR B 396    11916  18121  16699  -1675  -2449  -3697       C  
ATOM   5370  CD2 TYR B 396      59.135  42.683  69.496  1.00131.34           C  
ANISOU 5370  CD2 TYR B 396    12515  19312  18076  -1782  -1840  -3581       C  
ATOM   5371  CE1 TYR B 396      58.923  44.320  71.708  1.00116.71           C  
ANISOU 5371  CE1 TYR B 396    10729  17370  16247  -2070  -2474  -4008       C  
ATOM   5372  CE2 TYR B 396      60.041  43.712  69.682  1.00134.07           C  
ANISOU 5372  CE2 TYR B 396    12449  19712  18781  -2186  -1829  -3838       C  
ATOM   5373  CZ  TYR B 396      59.931  44.527  70.788  1.00130.47           C  
ANISOU 5373  CZ  TYR B 396    12025  19192  18355  -2345  -2159  -4068       C  
ATOM   5374  OH  TYR B 396      60.833  45.550  70.974  1.00131.63           O  
ANISOU 5374  OH  TYR B 396    11745  19355  18913  -2782  -2165  -4374       O  
ATOM   5375  N   ALA B 397      55.287  39.051  71.589  1.00116.87           N  
ANISOU 5375  N   ALA B 397    12185  17186  15034   -240  -2619  -2789       N  
ATOM   5376  CA  ALA B 397      54.205  38.070  71.519  1.00113.17           C  
ANISOU 5376  CA  ALA B 397    12096  16522  14382     39  -2603  -2506       C  
ATOM   5377  C   ALA B 397      52.877  38.817  71.429  1.00112.19           C  
ANISOU 5377  C   ALA B 397    12427  16134  14065   -148  -2502  -2334       C  
ATOM   5378  O   ALA B 397      52.389  39.356  72.427  1.00115.68           O  
ANISOU 5378  O   ALA B 397    13033  16573  14348   -130  -2697  -2308       O  
ATOM   5379  CB  ALA B 397      54.233  37.132  72.721  1.00111.35           C  
ANISOU 5379  CB  ALA B 397    11841  16421  14046    471  -2929  -2415       C  
ATOM   5380  N   ASP B 398      52.297  38.841  70.234  1.00110.96           N  
ANISOU 5380  N   ASP B 398    12469  15792  13899   -291  -2204  -2224       N  
ATOM   5381  CA  ASP B 398      51.026  39.505  69.981  1.00108.93           C  
ANISOU 5381  CA  ASP B 398    12618  15309  13462   -441  -2086  -2042       C  
ATOM   5382  C   ASP B 398      49.902  38.482  70.072  1.00 97.78           C  
ANISOU 5382  C   ASP B 398    11489  13753  11908   -188  -2141  -1806       C  
ATOM   5383  O   ASP B 398      49.998  37.400  69.486  1.00 95.74           O  
ANISOU 5383  O   ASP B 398    11178  13468  11731    -33  -2083  -1794       O  
ATOM   5384  CB  ASP B 398      51.032  40.172  68.606  1.00103.44           C  
ANISOU 5384  CB  ASP B 398    11958  14538  12808   -721  -1734  -2043       C  
ATOM   5385  CG  ASP B 398      52.123  41.216  68.473  1.00111.68           C  
ANISOU 5385  CG  ASP B 398    12706  15671  14055  -1016  -1622  -2236       C  
ATOM   5386  OD1 ASP B 398      52.541  41.776  69.507  1.00107.50           O  
ANISOU 5386  OD1 ASP B 398    12046  15200  13598  -1079  -1841  -2385       O  
ATOM   5387  OD2 ASP B 398      52.562  41.479  67.333  1.00113.14           O1-
ANISOU 5387  OD2 ASP B 398    12780  15877  14333  -1184  -1310  -2244       O1-
ATOM   5388  N   SER B 399      48.840  38.824  70.800  1.00 97.11           N  
ANISOU 5388  N   SER B 399    11692  13565  11639   -152  -2242  -1631       N  
ATOM   5389  CA  SER B 399      47.748  37.889  71.043  1.00 99.81           C  
ANISOU 5389  CA  SER B 399    12263  13772  11889     66  -2296  -1381       C  
ATOM   5390  C   SER B 399      46.408  38.581  70.850  1.00105.74           C  
ANISOU 5390  C   SER B 399    13342  14374  12460    -59  -2194  -1199       C  
ATOM   5391  O   SER B 399      46.194  39.686  71.356  1.00108.42           O  
ANISOU 5391  O   SER B 399    13788  14725  12681   -164  -2217  -1207       O  
ATOM   5392  CB  SER B 399      47.836  37.292  72.454  1.00110.73           C  
ANISOU 5392  CB  SER B 399    13608  15248  13218    373  -2556  -1280       C  
ATOM   5393  OG  SER B 399      47.803  38.304  73.445  1.00122.83           O  
ANISOU 5393  OG  SER B 399    15193  16896  14580    344  -2697  -1325       O  
ATOM   5394  N   PHE B 400      45.512  37.918  70.125  1.00100.90           N  
ANISOU 5394  N   PHE B 400    12874  13623  11841    -36  -2094  -1059       N  
ATOM   5395  CA  PHE B 400      44.165  38.415  69.873  1.00 90.84           C  
ANISOU 5395  CA  PHE B 400    11870  12241  10404   -116  -2011   -870       C  
ATOM   5396  C   PHE B 400      43.283  37.224  69.518  1.00 83.40           C  
ANISOU 5396  C   PHE B 400    10996  11169   9525    -10  -2015   -733       C  
ATOM   5397  O   PHE B 400      43.750  36.084  69.442  1.00 87.10           O  
ANISOU 5397  O   PHE B 400    11332  11587  10174    117  -2063   -794       O  
ATOM   5398  CB  PHE B 400      44.161  39.471  68.764  1.00 97.97           C  
ANISOU 5398  CB  PHE B 400    12837  13151  11235   -357  -1798   -943       C  
ATOM   5399  CG  PHE B 400      44.967  39.087  67.554  1.00 94.19           C  
ANISOU 5399  CG  PHE B 400    12192  12734  10862   -429  -1650  -1120       C  
ATOM   5400  CD1 PHE B 400      44.427  38.271  66.572  1.00 94.98           C  
ANISOU 5400  CD1 PHE B 400    12342  12800  10944   -384  -1583  -1119       C  
ATOM   5401  CD2 PHE B 400      46.264  39.546  67.396  1.00 97.18           C  
ANISOU 5401  CD2 PHE B 400    12345  13220  11358   -538  -1574  -1309       C  
ATOM   5402  CE1 PHE B 400      45.166  37.918  65.458  1.00 99.11           C  
ANISOU 5402  CE1 PHE B 400    12726  13414  11516   -407  -1438  -1306       C  
ATOM   5403  CE2 PHE B 400      47.008  39.197  66.284  1.00104.90           C  
ANISOU 5403  CE2 PHE B 400    13157  14288  12412   -575  -1401  -1453       C  
ATOM   5404  CZ  PHE B 400      46.459  38.382  65.314  1.00108.26           C  
ANISOU 5404  CZ  PHE B 400    13668  14697  12770   -490  -1329  -1452       C  
ATOM   5405  N   VAL B 401      41.999  37.497  69.296  1.00 81.49           N  
ANISOU 5405  N   VAL B 401    10947  10858   9160    -62  -1964   -558       N  
ATOM   5406  CA  VAL B 401      41.033  36.476  68.907  1.00 85.77           C  
ANISOU 5406  CA  VAL B 401    11530  11268   9792    -20  -1973   -452       C  
ATOM   5407  C   VAL B 401      40.320  36.926  67.640  1.00 90.10           C  
ANISOU 5407  C   VAL B 401    12169  11850  10214   -173  -1854   -498       C  
ATOM   5408  O   VAL B 401      39.890  38.081  67.537  1.00 86.69           O  
ANISOU 5408  O   VAL B 401    11864  11492   9581   -251  -1777   -412       O  
ATOM   5409  CB  VAL B 401      40.014  36.184  70.026  1.00 74.82           C  
ANISOU 5409  CB  VAL B 401    10234   9805   8391    108  -2054   -148       C  
ATOM   5410  CG1 VAL B 401      38.755  35.551  69.458  1.00 80.42           C  
ANISOU 5410  CG1 VAL B 401    10983  10390   9182     53  -2027    -36       C  
ATOM   5411  CG2 VAL B 401      40.625  35.272  71.065  1.00100.67           C  
ANISOU 5411  CG2 VAL B 401    13407  13030  11813    322  -2164    -70       C  
ATOM   5412  N   ILE B 402      40.203  36.012  66.679  1.00 84.33           N  
ANISOU 5412  N   ILE B 402    11381  11068   9594   -189  -1844   -643       N  
ATOM   5413  CA  ILE B 402      39.478  36.216  65.436  1.00 82.87           C  
ANISOU 5413  CA  ILE B 402    11262  10963   9264   -285  -1775   -714       C  
ATOM   5414  C   ILE B 402      38.673  34.952  65.151  1.00 91.96           C  
ANISOU 5414  C   ILE B 402    12370  11967  10605   -268  -1879   -764       C  
ATOM   5415  O   ILE B 402      38.670  34.005  65.941  1.00 92.77           O  
ANISOU 5415  O   ILE B 402    12412  11868  10970   -191  -1965   -692       O  
ATOM   5416  CB  ILE B 402      40.421  36.546  64.261  1.00 80.24           C  
ANISOU 5416  CB  ILE B 402    10880  10784   8823   -336  -1631   -954       C  
ATOM   5417  CG1 ILE B 402      41.559  35.522  64.199  1.00 90.93           C  
ANISOU 5417  CG1 ILE B 402    12063  12081  10407   -252  -1651  -1187       C  
ATOM   5418  CG2 ILE B 402      40.966  37.959  64.392  1.00 80.68           C  
ANISOU 5418  CG2 ILE B 402    10987  10949   8719   -416  -1492   -871       C  
ATOM   5419  CD1 ILE B 402      42.565  35.786  63.102  1.00 96.35           C  
ANISOU 5419  CD1 ILE B 402    12666  12949  10996   -275  -1478  -1412       C  
ATOM   5420  N   ARG B 403      37.986  34.935  64.013  1.00 96.10           N  
ANISOU 5420  N   ARG B 403    12919  12589  11006   -336  -1872   -889       N  
ATOM   5421  CA  ARG B 403      37.238  33.745  63.637  1.00 90.24           C  
ANISOU 5421  CA  ARG B 403    12109  11700  10479   -360  -1992  -1018       C  
ATOM   5422  C   ARG B 403      38.066  32.861  62.709  1.00 85.24           C  
ANISOU 5422  C   ARG B 403    11402  11032   9955   -322  -1990  -1405       C  
ATOM   5423  O   ARG B 403      39.038  33.302  62.090  1.00 85.32           O  
ANISOU 5423  O   ARG B 403    11409  11220   9787   -283  -1872  -1560       O  
ATOM   5424  CB  ARG B 403      35.913  34.109  62.968  1.00 98.48           C  
ANISOU 5424  CB  ARG B 403    13183  12896  11337   -438  -2042   -983       C  
ATOM   5425  CG  ARG B 403      35.989  35.328  62.087  1.00102.55           C  
ANISOU 5425  CG  ARG B 403    13801  13727  11438   -428  -1929   -990       C  
ATOM   5426  CD  ARG B 403      34.669  35.599  61.394  1.00108.15           C  
ANISOU 5426  CD  ARG B 403    14517  14628  11947   -453  -2008   -958       C  
ATOM   5427  NE  ARG B 403      34.421  34.617  60.347  1.00105.50           N  
ANISOU 5427  NE  ARG B 403    14084  14338  11661   -477  -2137  -1324       N  
ATOM   5428  CZ  ARG B 403      33.457  34.705  59.442  1.00108.14           C  
ANISOU 5428  CZ  ARG B 403    14386  14916  11785   -480  -2244  -1429       C  
ATOM   5429  NH1 ARG B 403      32.614  35.725  59.426  1.00118.24           N  
ANISOU 5429  NH1 ARG B 403    15720  16414  12790   -441  -2223  -1156       N  
ATOM   5430  NH2 ARG B 403      33.340  33.749  58.526  1.00112.65           N  
ANISOU 5430  NH2 ARG B 403    14865  15522  12414   -500  -2388  -1839       N  
ATOM   5431  N   GLY B 404      37.648  31.596  62.610  1.00 87.17           N  
ANISOU 5431  N   GLY B 404    11576  11028  10516   -334  -2106  -1561       N  
ATOM   5432  CA  GLY B 404      38.455  30.599  61.923  1.00 94.46           C  
ANISOU 5432  CA  GLY B 404    12439  11839  11614   -258  -2110  -1942       C  
ATOM   5433  C   GLY B 404      38.730  30.934  60.469  1.00102.33           C  
ANISOU 5433  C   GLY B 404    13458  13149  12275   -241  -2053  -2279       C  
ATOM   5434  O   GLY B 404      39.826  30.679  59.963  1.00104.76           O  
ANISOU 5434  O   GLY B 404    13729  13516  12561   -128  -1958  -2522       O  
ATOM   5435  N   ASP B 405      37.741  31.501  59.773  1.00108.69           N  
ANISOU 5435  N   ASP B 405    14312  14190  12793   -321  -2100  -2283       N  
ATOM   5436  CA  ASP B 405      37.944  31.873  58.376  1.00 96.76           C  
ANISOU 5436  CA  ASP B 405    12839  13038  10888   -259  -2036  -2558       C  
ATOM   5437  C   ASP B 405      38.955  33.001  58.212  1.00100.09           C  
ANISOU 5437  C   ASP B 405    13311  13716  11004   -195  -1794  -2403       C  
ATOM   5438  O   ASP B 405      39.466  33.199  57.105  1.00 95.64           O  
ANISOU 5438  O   ASP B 405    12763  13432  10145   -103  -1670  -2612       O  
ATOM   5439  CB  ASP B 405      36.618  32.281  57.727  1.00114.32           C  
ANISOU 5439  CB  ASP B 405    15094  15502  12843   -319  -2158  -2551       C  
ATOM   5440  CG  ASP B 405      35.769  31.088  57.325  1.00128.86           C  
ANISOU 5440  CG  ASP B 405    16839  17190  14932   -389  -2400  -2900       C  
ATOM   5441  OD1 ASP B 405      36.339  30.003  57.091  1.00148.42           O  
ANISOU 5441  OD1 ASP B 405    19273  19444  17676   -350  -2438  -3257       O  
ATOM   5442  OD2 ASP B 405      34.533  31.241  57.225  1.00117.90           O1-
ANISOU 5442  OD2 ASP B 405    15406  15899  13492   -482  -2552  -2836       O1-
ATOM   5443  N   GLU B 406      39.261  33.737  59.279  1.00105.07           N  
ANISOU 5443  N   GLU B 406    13958  14260  11704   -241  -1715  -2056       N  
ATOM   5444  CA  GLU B 406      40.103  34.922  59.184  1.00110.43           C  
ANISOU 5444  CA  GLU B 406    14669  15136  12151   -239  -1490  -1898       C  
ATOM   5445  C   GLU B 406      41.557  34.672  59.559  1.00106.54           C  
ANISOU 5445  C   GLU B 406    14048  14573  11859   -191  -1383  -1989       C  
ATOM   5446  O   GLU B 406      42.368  35.599  59.469  1.00 98.32           O  
ANISOU 5446  O   GLU B 406    12984  13681  10694   -222  -1186  -1891       O  
ATOM   5447  CB  GLU B 406      39.540  36.044  60.063  1.00102.62           C  
ANISOU 5447  CB  GLU B 406    13779  14119  11095   -323  -1474  -1509       C  
ATOM   5448  CG  GLU B 406      38.247  36.649  59.549  1.00105.87           C  
ANISOU 5448  CG  GLU B 406    14307  14694  11224   -334  -1511  -1368       C  
ATOM   5449  CD  GLU B 406      37.673  37.684  60.497  1.00114.80           C  
ANISOU 5449  CD  GLU B 406    15539  15758  12320   -379  -1492  -1000       C  
ATOM   5450  OE1 GLU B 406      38.091  37.711  61.674  1.00107.88           O  
ANISOU 5450  OE1 GLU B 406    14639  14686  11664   -407  -1511   -888       O  
ATOM   5451  OE2 GLU B 406      36.797  38.462  60.067  1.00125.74           O1-
ANISOU 5451  OE2 GLU B 406    17029  17306  13440   -354  -1464   -834       O1-
ATOM   5452  N   VAL B 407      41.913  33.452  59.973  1.00103.91           N  
ANISOU 5452  N   VAL B 407    13614  14010  11857   -113  -1500  -2166       N  
ATOM   5453  CA  VAL B 407      43.290  33.182  60.381  1.00103.71           C  
ANISOU 5453  CA  VAL B 407    13434  13946  12026    -26  -1420  -2242       C  
ATOM   5454  C   VAL B 407      44.246  33.329  59.203  1.00107.59           C  
ANISOU 5454  C   VAL B 407    13845  14709  12327     47  -1204  -2481       C  
ATOM   5455  O   VAL B 407      45.418  33.685  59.382  1.00114.24           O  
ANISOU 5455  O   VAL B 407    14534  15650  13222     66  -1057  -2469       O  
ATOM   5456  CB  VAL B 407      43.388  31.784  61.026  1.00 98.36           C  
ANISOU 5456  CB  VAL B 407    12686  12943  11742     94  -1581  -2349       C  
ATOM   5457  CG1 VAL B 407      44.822  31.472  61.437  1.00104.45           C  
ANISOU 5457  CG1 VAL B 407    13273  13714  12700    237  -1514  -2424       C  
ATOM   5458  CG2 VAL B 407      42.460  31.690  62.226  1.00 98.14           C  
ANISOU 5458  CG2 VAL B 407    12730  12678  11883     35  -1742  -2044       C  
ATOM   5459  N   ARG B 408      43.762  33.083  57.982  1.00107.94           N  
ANISOU 5459  N   ARG B 408    13969  14912  12131     96  -1177  -2703       N  
ATOM   5460  CA  ARG B 408      44.611  33.200  56.800  1.00107.39           C  
ANISOU 5460  CA  ARG B 408    13838  15149  11817    209   -943  -2918       C  
ATOM   5461  C   ARG B 408      45.105  34.623  56.575  1.00102.90           C  
ANISOU 5461  C   ARG B 408    13260  14839  10997    114   -672  -2646       C  
ATOM   5462  O   ARG B 408      46.112  34.816  55.886  1.00105.27           O  
ANISOU 5462  O   ARG B 408    13441  15370  11185    188   -415  -2735       O  
ATOM   5463  CB  ARG B 408      43.855  32.705  55.563  1.00113.90           C  
ANISOU 5463  CB  ARG B 408    14776  16138  12364    306  -1003  -3216       C  
ATOM   5464  CG  ARG B 408      42.616  33.518  55.205  1.00129.25           C  
ANISOU 5464  CG  ARG B 408    16886  18248  13975    212  -1062  -3019       C  
ATOM   5465  CD  ARG B 408      42.190  33.259  53.765  1.00141.36           C  
ANISOU 5465  CD  ARG B 408    18494  20113  15103    358  -1065  -3331       C  
ATOM   5466  NE  ARG B 408      41.225  34.240  53.281  1.00152.88           N  
ANISOU 5466  NE  ARG B 408    20090  21843  16154    330  -1060  -3094       N  
ATOM   5467  CZ  ARG B 408      41.545  35.410  52.744  1.00154.43           C  
ANISOU 5467  CZ  ARG B 408    20352  22345  15980    371   -778  -2817       C  
ATOM   5468  NH1 ARG B 408      42.806  35.785  52.603  1.00146.37           N  
ANISOU 5468  NH1 ARG B 408    19248  21410  14957    402   -466  -2746       N  
ATOM   5469  NH2 ARG B 408      40.574  36.222  52.335  1.00154.31           N  
ANISOU 5469  NH2 ARG B 408    20473  22548  15610    387   -797  -2587       N  
ATOM   5470  N   GLN B 409      44.425  35.622  57.140  1.00 92.11           N  
ANISOU 5470  N   GLN B 409    12012  13420   9565    -44   -699  -2311       N  
ATOM   5471  CA  GLN B 409      44.847  37.010  57.006  1.00 94.89           C  
ANISOU 5471  CA  GLN B 409    12376  13924   9753   -158   -436  -2038       C  
ATOM   5472  C   GLN B 409      46.018  37.363  57.914  1.00112.31           C  
ANISOU 5472  C   GLN B 409    14381  16027  12265   -260   -356  -1969       C  
ATOM   5473  O   GLN B 409      46.639  38.413  57.714  1.00119.80           O  
ANISOU 5473  O   GLN B 409    15275  17081  13161   -376    -99  -1809       O  
ATOM   5474  CB  GLN B 409      43.673  37.945  57.292  1.00105.16           C  
ANISOU 5474  CB  GLN B 409    13888  15173  10894   -259   -497  -1731       C  
ATOM   5475  CG  GLN B 409      42.487  37.713  56.380  1.00109.95           C  
ANISOU 5475  CG  GLN B 409    14654  15946  11177   -156   -593  -1787       C  
ATOM   5476  CD  GLN B 409      41.434  38.790  56.506  1.00 91.07           C  
ANISOU 5476  CD  GLN B 409    12449  13572   8583   -211   -593  -1450       C  
ATOM   5477  OE1 GLN B 409      41.730  39.925  56.880  1.00 90.48           O  
ANISOU 5477  OE1 GLN B 409    12424  13437   8517   -310   -414  -1172       O  
ATOM   5478  NE2 GLN B 409      40.194  38.441  56.192  1.00 94.47           N  
ANISOU 5478  NE2 GLN B 409    12967  14075   8852   -145   -799  -1490       N  
ATOM   5479  N   ILE B 410      46.330  36.523  58.897  1.00100.42           N  
ANISOU 5479  N   ILE B 410    12752  14319  11083   -217   -570  -2079       N  
ATOM   5480  CA  ILE B 410      47.528  36.701  59.701  1.00 87.31           C  
ANISOU 5480  CA  ILE B 410    10849  12632   9693   -264   -538  -2079       C  
ATOM   5481  C   ILE B 410      48.694  36.055  58.966  1.00100.43           C  
ANISOU 5481  C   ILE B 410    12272  14473  11413   -122   -368  -2334       C  
ATOM   5482  O   ILE B 410      49.153  34.969  59.340  1.00103.42           O  
ANISOU 5482  O   ILE B 410    12514  14763  12019     46   -506  -2522       O  
ATOM   5483  CB  ILE B 410      47.349  36.111  61.113  1.00 90.42           C  
ANISOU 5483  CB  ILE B 410    11218  12782  10356   -220   -840  -2044       C  
ATOM   5484  CG1 ILE B 410      45.993  36.520  61.680  1.00 82.95           C  
ANISOU 5484  CG1 ILE B 410    10527  11683   9309   -300   -994  -1815       C  
ATOM   5485  CG2 ILE B 410      48.462  36.591  62.020  1.00105.88           C  
ANISOU 5485  CG2 ILE B 410    12936  14772  12521   -286   -844  -2020       C  
ATOM   5486  CD1 ILE B 410      45.805  38.010  61.777  1.00 84.05           C  
ANISOU 5486  CD1 ILE B 410    10767  11870   9298   -487   -864  -1597       C  
ATOM   5487  N   ALA B 411      49.159  36.714  57.911  1.00107.17           N  
ANISOU 5487  N   ALA B 411    13080  15581  12057   -161    -46  -2315       N  
ATOM   5488  CA  ALA B 411      50.208  36.225  57.025  1.00114.72           C  
ANISOU 5488  CA  ALA B 411    13818  16777  12991     -6    188  -2534       C  
ATOM   5489  C   ALA B 411      50.704  37.390  56.176  1.00121.00           C  
ANISOU 5489  C   ALA B 411    14557  17829  13587   -132    590  -2351       C  
ATOM   5490  O   ALA B 411      49.955  38.349  55.947  1.00117.57           O  
ANISOU 5490  O   ALA B 411    14347  17384  12940   -266    673  -2095       O  
ATOM   5491  CB  ALA B 411      49.695  35.089  56.134  1.00132.37           C  
ANISOU 5491  CB  ALA B 411    16189  19064  15041    244    118  -2819       C  
ATOM   5492  N   PRO B 412      51.951  37.357  55.709  1.00122.63           N  
ANISOU 5492  N   PRO B 412    14460  18260  13873    -83    870  -2442       N  
ATOM   5493  CA  PRO B 412      52.456  38.463  54.888  1.00122.06           C  
ANISOU 5493  CA  PRO B 412    14313  18417  13646   -213   1311  -2217       C  
ATOM   5494  C   PRO B 412      51.676  38.597  53.589  1.00134.45           C  
ANISOU 5494  C   PRO B 412    16174  20207  14704    -62   1495  -2147       C  
ATOM   5495  O   PRO B 412      51.332  37.604  52.944  1.00128.41           O  
ANISOU 5495  O   PRO B 412    15511  19571  13709    208   1396  -2419       O  
ATOM   5496  CB  PRO B 412      53.914  38.070  54.629  1.00126.97           C  
ANISOU 5496  CB  PRO B 412    14512  19267  14462   -123   1546  -2386       C  
ATOM   5497  CG  PRO B 412      54.259  37.176  55.784  1.00135.17           C  
ANISOU 5497  CG  PRO B 412    15372  20115  15872    -54   1177  -2609       C  
ATOM   5498  CD  PRO B 412      53.010  36.385  56.027  1.00129.22           C  
ANISOU 5498  CD  PRO B 412    14972  19134  14993     85    814  -2709       C  
ATOM   5499  N   GLY B 413      51.386  39.841  53.220  1.00137.69           N  
ANISOU 5499  N   GLY B 413    16721  20653  14941   -224   1753  -1788       N  
ATOM   5500  CA  GLY B 413      50.765  40.123  51.936  1.00132.60           C  
ANISOU 5500  CA  GLY B 413    16326  20290  13765    -49   1978  -1655       C  
ATOM   5501  C   GLY B 413      49.422  39.460  51.721  1.00125.01           C  
ANISOU 5501  C   GLY B 413    15677  19324  12496    136   1625  -1816       C  
ATOM   5502  O   GLY B 413      49.167  38.915  50.640  1.00144.95           O  
ANISOU 5502  O   GLY B 413    18301  22164  14610    408   1678  -1998       O  
ATOM   5503  N   GLN B 414      48.559  39.481  52.732  1.00102.48           N  
ANISOU 5503  N   GLN B 414    12963  16142   9834      0   1262  -1775       N  
ATOM   5504  CA  GLN B 414      47.193  39.001  52.611  1.00 97.46           C  
ANISOU 5504  CA  GLN B 414    12589  15480   8963    117    935  -1873       C  
ATOM   5505  C   GLN B 414      46.254  40.153  52.934  1.00104.11           C  
ANISOU 5505  C   GLN B 414    13657  16193   9710    -27    921  -1482       C  
ATOM   5506  O   GLN B 414      46.552  40.979  53.800  1.00103.64           O  
ANISOU 5506  O   GLN B 414    13554  15885   9942   -255    981  -1251       O  
ATOM   5507  CB  GLN B 414      46.937  37.810  53.542  1.00 98.12           C  
ANISOU 5507  CB  GLN B 414    12616  15280   9386    125    520  -2178       C  
ATOM   5508  CG  GLN B 414      47.828  36.609  53.251  1.00101.78           C  
ANISOU 5508  CG  GLN B 414    12877  15818   9976    309    523  -2574       C  
ATOM   5509  CD  GLN B 414      47.109  35.490  52.524  1.00122.91           C  
ANISOU 5509  CD  GLN B 414    15682  18576  12442    533    313  -2949       C  
ATOM   5510  OE1 GLN B 414      45.999  35.668  52.022  1.00125.75           O  
ANISOU 5510  OE1 GLN B 414    16253  19041  12485    563    197  -2919       O  
ATOM   5511  NE2 GLN B 414      47.742  34.323  52.467  1.00135.42           N  
ANISOU 5511  NE2 GLN B 414    17125  20107  14220    700    251  -3326       N  
ATOM   5512  N   THR B 415      45.135  40.223  52.216  1.00116.66           N  
ANISOU 5512  N   THR B 415    15477  17966  10884    124    837  -1431       N  
ATOM   5513  CA  THR B 415      44.185  41.318  52.347  1.00101.73           C  
ANISOU 5513  CA  THR B 415    13810  16007   8837     63    850  -1045       C  
ATOM   5514  C   THR B 415      42.920  40.842  53.056  1.00 93.81           C  
ANISOU 5514  C   THR B 415    12912  14820   7910     50    415  -1133       C  
ATOM   5515  O   THR B 415      42.664  39.641  53.179  1.00 98.43           O  
ANISOU 5515  O   THR B 415    13427  15377   8595    110    124  -1487       O  
ATOM   5516  CB  THR B 415      43.826  41.909  50.976  1.00103.52           C  
ANISOU 5516  CB  THR B 415    14202  16637   8493    284   1112   -838       C  
ATOM   5517  OG1 THR B 415      43.482  40.858  50.064  1.00124.19           O  
ANISOU 5517  OG1 THR B 415    16826  19598  10762    541    945  -1211       O  
ATOM   5518  CG2 THR B 415      45.008  42.677  50.404  1.00112.12           C  
ANISOU 5518  CG2 THR B 415    15201  17852   9548    255   1626   -594       C  
ATOM   5519  N   GLY B 416      42.135  41.799  53.524  1.00 88.33           N  
ANISOU 5519  N   GLY B 416    12382  13983   7198    -25    395   -797       N  
ATOM   5520  CA  GLY B 416      40.870  41.510  54.163  1.00 99.13           C  
ANISOU 5520  CA  GLY B 416    13837  15218   8611    -26     39   -807       C  
ATOM   5521  C   GLY B 416      40.523  42.598  55.158  1.00 97.29           C  
ANISOU 5521  C   GLY B 416    13716  14695   8555   -167     69   -462       C  
ATOM   5522  O   GLY B 416      41.102  43.676  55.155  1.00 97.61           O  
ANISOU 5522  O   GLY B 416    13809  14652   8628   -252    368   -204       O  
ATOM   5523  N   LYS B 417      39.549  42.293  56.018  1.00 97.70           N  
ANISOU 5523  N   LYS B 417    13799  14582   8741   -191   -234   -467       N  
ATOM   5524  CA  LYS B 417      39.192  43.235  57.077  1.00103.78           C  
ANISOU 5524  CA  LYS B 417    14677  15077   9678   -292   -231   -191       C  
ATOM   5525  C   LYS B 417      40.228  43.226  58.194  1.00102.61           C  
ANISOU 5525  C   LYS B 417    14407  14645   9937   -478   -224   -277       C  
ATOM   5526  O   LYS B 417      40.628  44.286  58.688  1.00101.33           O  
ANISOU 5526  O   LYS B 417    14307  14297   9897   -594    -59    -97       O  
ATOM   5527  CB  LYS B 417      37.808  42.906  57.630  1.00 92.34           C  
ANISOU 5527  CB  LYS B 417    13278  13592   8216   -230   -528   -150       C  
ATOM   5528  CG  LYS B 417      36.673  43.134  56.650  1.00 84.21           C  
ANISOU 5528  CG  LYS B 417    12350  12861   6784    -42   -562    -30       C  
ATOM   5529  CD  LYS B 417      36.404  44.617  56.449  1.00103.19           C  
ANISOU 5529  CD  LYS B 417    14964  15260   8985     36   -311    371       C  
ATOM   5530  CE  LYS B 417      35.417  44.854  55.314  1.00123.14           C  
ANISOU 5530  CE  LYS B 417    17578  18164  11047    284   -324    507       C  
ATOM   5531  NZ  LYS B 417      34.894  46.251  55.309  1.00124.92           N  
ANISOU 5531  NZ  LYS B 417    18020  18332  11112    406   -123    945       N  
ATOM   5532  N   ILE B 418      40.670  42.038  58.607  1.00 90.34           N  
ANISOU 5532  N   ILE B 418    12674  13049   8604   -496   -414   -562       N  
ATOM   5533  CA  ILE B 418      41.657  41.941  59.677  1.00 97.42           C  
ANISOU 5533  CA  ILE B 418    13425  13739   9853   -623   -448   -655       C  
ATOM   5534  C   ILE B 418      42.994  42.512  59.224  1.00 97.59           C  
ANISOU 5534  C   ILE B 418    13325  13812   9942   -727   -153   -676       C  
ATOM   5535  O   ILE B 418      43.577  43.376  59.888  1.00108.57           O  
ANISOU 5535  O   ILE B 418    14687  15037  11526   -883    -57   -591       O  
ATOM   5536  CB  ILE B 418      41.798  40.481  60.142  1.00 93.37           C  
ANISOU 5536  CB  ILE B 418    12754  13175   9548   -564   -701   -915       C  
ATOM   5537  CG1 ILE B 418      40.441  39.931  60.581  1.00 82.99           C  
ANISOU 5537  CG1 ILE B 418    11531  11786   8217   -497   -954   -857       C  
ATOM   5538  CG2 ILE B 418      42.826  40.369  61.257  1.00 91.09           C  
ANISOU 5538  CG2 ILE B 418    12302  12731   9577   -640   -758   -992       C  
ATOM   5539  CD1 ILE B 418      39.765  40.771  61.643  1.00 93.70           C  
ANISOU 5539  CD1 ILE B 418    13015  12994   9594   -534  -1009   -598       C  
ATOM   5540  N   ALA B 419      43.494  42.044  58.080  1.00 92.31           N  
ANISOU 5540  N   ALA B 419    12570  13380   9125   -644      2   -806       N  
ATOM   5541  CA  ALA B 419      44.827  42.431  57.640  1.00 96.61           C  
ANISOU 5541  CA  ALA B 419    12939  14006   9764   -734    307   -830       C  
ATOM   5542  C   ALA B 419      44.900  43.880  57.178  1.00100.54           C  
ANISOU 5542  C   ALA B 419    13562  14484  10156   -838    651   -504       C  
ATOM   5543  O   ALA B 419      45.992  44.456  57.169  1.00110.40           O  
ANISOU 5543  O   ALA B 419    14647  15688  11611  -1002    906   -469       O  
ATOM   5544  CB  ALA B 419      45.296  41.501  56.525  1.00101.00           C  
ANISOU 5544  CB  ALA B 419    13376  14849  10149   -568    401  -1058       C  
ATOM   5545  N   ASP B 420      43.777  44.484  56.794  1.00 99.47           N  
ANISOU 5545  N   ASP B 420    13695  14369   9732   -745    674   -255       N  
ATOM   5546  CA  ASP B 420      43.781  45.893  56.419  1.00106.56           C  
ANISOU 5546  CA  ASP B 420    14747  15181  10558   -816   1012    102       C  
ATOM   5547  C   ASP B 420      43.350  46.822  57.544  1.00104.14           C  
ANISOU 5547  C   ASP B 420    14582  14511  10477   -956    928    254       C  
ATOM   5548  O   ASP B 420      43.791  47.975  57.572  1.00112.06           O  
ANISOU 5548  O   ASP B 420    15636  15306  11635  -1113   1210    460       O  
ATOM   5549  CB  ASP B 420      42.874  46.142  55.205  1.00122.96           C  
ANISOU 5549  CB  ASP B 420    17046  17534  12141   -572   1141    334       C  
ATOM   5550  CG  ASP B 420      43.246  45.289  54.001  1.00123.73           C  
ANISOU 5550  CG  ASP B 420    17037  18038  11935   -390   1232    159       C  
ATOM   5551  OD1 ASP B 420      44.449  45.030  53.796  1.00134.23           O  
ANISOU 5551  OD1 ASP B 420    18148  19428  13425   -473   1425     24       O  
ATOM   5552  OD2 ASP B 420      42.328  44.883  53.255  1.00103.22           O1-
ANISOU 5552  OD2 ASP B 420    14562  15724   8932   -151   1103    136       O1-
ATOM   5553  N   TYR B 421      42.507  46.363  58.473  1.00 91.58           N  
ANISOU 5553  N   TYR B 421    13053  12822   8921   -901    569    156       N  
ATOM   5554  CA  TYR B 421      41.914  47.247  59.470  1.00 98.90           C  
ANISOU 5554  CA  TYR B 421    14155  13454   9970   -959    492    302       C  
ATOM   5555  C   TYR B 421      42.187  46.862  60.922  1.00 96.06           C  
ANISOU 5555  C   TYR B 421    13675  12912   9910  -1060    204     74       C  
ATOM   5556  O   TYR B 421      41.725  47.575  61.820  1.00 95.08           O  
ANISOU 5556  O   TYR B 421    13697  12564   9866  -1086    130    152       O  
ATOM   5557  CB  TYR B 421      40.390  47.333  59.281  1.00104.83           C  
ANISOU 5557  CB  TYR B 421    15136  14285  10407   -737    370    501       C  
ATOM   5558  CG  TYR B 421      39.902  47.977  57.998  1.00102.28           C  
ANISOU 5558  CG  TYR B 421    14988  14141   9731   -578    631    798       C  
ATOM   5559  CD1 TYR B 421      40.728  48.788  57.231  1.00107.21           C  
ANISOU 5559  CD1 TYR B 421    15634  14740  10359   -653   1028    981       C  
ATOM   5560  CD2 TYR B 421      38.593  47.788  57.570  1.00111.70           C  
ANISOU 5560  CD2 TYR B 421    16307  15546  10587   -337    486    920       C  
ATOM   5561  CE1 TYR B 421      40.267  49.379  56.065  1.00116.30           C  
ANISOU 5561  CE1 TYR B 421    16963  16080  11146   -455   1284   1307       C  
ATOM   5562  CE2 TYR B 421      38.124  48.373  56.409  1.00123.89           C  
ANISOU 5562  CE2 TYR B 421    18006  17309  11759   -138    697   1203       C  
ATOM   5563  CZ  TYR B 421      38.964  49.168  55.661  1.00120.70           C  
ANISOU 5563  CZ  TYR B 421    17656  16881  11323   -179   1102   1412       C  
ATOM   5564  OH  TYR B 421      38.497  49.751  54.505  1.00101.75           O  
ANISOU 5564  OH  TYR B 421    15426  14723   8513     67   1332   1745       O  
ATOM   5565  N   ASN B 422      42.904  45.770  61.194  1.00 94.62           N  
ANISOU 5565  N   ASN B 422    13245  12831   9874  -1080     41   -200       N  
ATOM   5566  CA  ASN B 422      43.067  45.353  62.586  1.00 98.00           C  
ANISOU 5566  CA  ASN B 422    13578  13134  10523  -1108   -248   -372       C  
ATOM   5567  C   ASN B 422      44.496  44.956  62.945  1.00 97.99           C  
ANISOU 5567  C   ASN B 422    13268  13159  10804  -1231   -270   -625       C  
ATOM   5568  O   ASN B 422      45.050  45.454  63.931  1.00 93.83           O  
ANISOU 5568  O   ASN B 422    12662  12495  10494  -1355   -352   -724       O  
ATOM   5569  CB  ASN B 422      42.118  44.198  62.907  1.00 92.13           C  
ANISOU 5569  CB  ASN B 422    12862  12472   9671   -921   -531   -405       C  
ATOM   5570  CG  ASN B 422      40.663  44.593  62.783  1.00 92.46           C  
ANISOU 5570  CG  ASN B 422    13150  12506   9475   -802   -558   -170       C  
ATOM   5571  OD1 ASN B 422      40.033  44.997  63.760  1.00 84.48           O  
ANISOU 5571  OD1 ASN B 422    12256  11362   8480   -766   -672    -74       O  
ATOM   5572  ND2 ASN B 422      40.119  44.477  61.579  1.00 96.46           N  
ANISOU 5572  ND2 ASN B 422    13722  13192   9735   -712   -457    -85       N  
ATOM   5573  N   TYR B 423      45.099  44.063  62.165  1.00 93.87           N  
ANISOU 5573  N   TYR B 423    12561  12833  10274  -1177   -211   -756       N  
ATOM   5574  CA  TYR B 423      46.431  43.553  62.479  1.00 90.04           C  
ANISOU 5574  CA  TYR B 423    11746  12415  10051  -1240   -243   -996       C  
ATOM   5575  C   TYR B 423      47.136  43.211  61.175  1.00 97.54           C  
ANISOU 5575  C   TYR B 423    12543  13577  10939  -1219     25  -1050       C  
ATOM   5576  O   TYR B 423      46.821  42.196  60.546  1.00105.08           O  
ANISOU 5576  O   TYR B 423    13513  14678  11734  -1032    -28  -1134       O  
ATOM   5577  CB  TYR B 423      46.350  42.332  63.393  1.00 92.62           C  
ANISOU 5577  CB  TYR B 423    11980  12750  10462  -1076   -585  -1152       C  
ATOM   5578  CG  TYR B 423      47.696  41.802  63.827  1.00 99.92           C  
ANISOU 5578  CG  TYR B 423    12557  13762  11646  -1085   -654  -1383       C  
ATOM   5579  CD1 TYR B 423      48.376  42.361  64.900  1.00105.20           C  
ANISOU 5579  CD1 TYR B 423    13073  14380  12518  -1202   -775  -1475       C  
ATOM   5580  CD2 TYR B 423      48.286  40.735  63.161  1.00104.54           C  
ANISOU 5580  CD2 TYR B 423    12953  14500  12265   -952   -612  -1536       C  
ATOM   5581  CE1 TYR B 423      49.609  41.871  65.297  1.00109.95           C  
ANISOU 5581  CE1 TYR B 423    13315  15114  13346  -1186   -864  -1691       C  
ATOM   5582  CE2 TYR B 423      49.514  40.239  63.549  1.00107.42           C  
ANISOU 5582  CE2 TYR B 423    12979  14968  12868   -918   -671  -1733       C  
ATOM   5583  CZ  TYR B 423      50.171  40.810  64.617  1.00106.80           C  
ANISOU 5583  CZ  TYR B 423    12724  14869  12984  -1035   -803  -1799       C  
ATOM   5584  OH  TYR B 423      51.396  40.320  65.007  1.00102.47           O  
ANISOU 5584  OH  TYR B 423    11799  14473  12662   -980   -888  -1999       O  
ATOM   5585  N   LYS B 424      48.089  44.046  60.778  1.00101.67           N  
ANISOU 5585  N   LYS B 424    12912  14116  11602  -1409    322  -1014       N  
ATOM   5586  CA  LYS B 424      48.807  43.875  59.521  1.00107.92           C  
ANISOU 5586  CA  LYS B 424    13551  15141  12315  -1383    649  -1018       C  
ATOM   5587  C   LYS B 424      50.232  43.415  59.802  1.00109.19           C  
ANISOU 5587  C   LYS B 424    13289  15411  12789  -1447    660  -1260       C  
ATOM   5588  O   LYS B 424      50.996  44.120  60.471  1.00113.19           O  
ANISOU 5588  O   LYS B 424    13592  15809  13608  -1681    683  -1298       O  
ATOM   5589  CB  LYS B 424      48.810  45.174  58.712  1.00109.34           C  
ANISOU 5589  CB  LYS B 424    13852  15277  12413  -1531   1058   -720       C  
ATOM   5590  CG  LYS B 424      49.590  45.078  57.407  1.00107.21           C  
ANISOU 5590  CG  LYS B 424    13420  15286  12030  -1486   1455   -672       C  
ATOM   5591  CD  LYS B 424      49.037  43.981  56.508  1.00109.81           C  
ANISOU 5591  CD  LYS B 424    13857  15903  11963  -1165   1388   -773       C  
ATOM   5592  CE  LYS B 424      49.784  43.913  55.187  1.00113.01           C  
ANISOU 5592  CE  LYS B 424    14125  16634  12182  -1069   1800   -731       C  
ATOM   5593  NZ  LYS B 424      49.256  42.826  54.315  1.00114.17           N  
ANISOU 5593  NZ  LYS B 424    14382  17071  11928   -741   1702   -910       N  
ATOM   5594  N   LEU B 425      50.583  42.234  59.296  1.00104.20           N  
ANISOU 5594  N   LEU B 425    12513  14995  12085  -1232    633  -1446       N  
ATOM   5595  CA  LEU B 425      51.965  41.787  59.298  1.00100.15           C  
ANISOU 5595  CA  LEU B 425    11578  14649  11826  -1237    717  -1650       C  
ATOM   5596  C   LEU B 425      52.709  42.387  58.106  1.00114.28           C  
ANISOU 5596  C   LEU B 425    13215  16636  13570  -1328   1206  -1531       C  
ATOM   5597  O   LEU B 425      52.123  42.592  57.039  1.00138.15           O  
ANISOU 5597  O   LEU B 425    16479  19761  16251  -1234   1442  -1358       O  
ATOM   5598  CB  LEU B 425      52.034  40.265  59.232  1.00101.61           C  
ANISOU 5598  CB  LEU B 425    11687  14951  11968   -929    514  -1896       C  
ATOM   5599  CG  LEU B 425      51.693  39.488  60.502  1.00101.23           C  
ANISOU 5599  CG  LEU B 425    11665  14733  12067   -816     74  -2010       C  
ATOM   5600  CD1 LEU B 425      51.710  37.996  60.219  1.00101.41           C  
ANISOU 5600  CD1 LEU B 425    11654  14812  12066   -507    -51  -2219       C  
ATOM   5601  CD2 LEU B 425      52.674  39.838  61.610  1.00117.39           C  
ANISOU 5601  CD2 LEU B 425    13388  16768  14444   -950    -56  -2091       C  
ATOM   5602  N   PRO B 426      54.003  42.678  58.257  1.00127.30           N  
ANISOU 5602  N   PRO B 426    14446  18371  15551  -1497   1374  -1608       N  
ATOM   5603  CA  PRO B 426      54.763  43.223  57.124  1.00136.75           C  
ANISOU 5603  CA  PRO B 426    15458  19769  16732  -1586   1892  -1456       C  
ATOM   5604  C   PRO B 426      55.038  42.171  56.061  1.00142.21           C  
ANISOU 5604  C   PRO B 426    16077  20805  17150  -1252   2053  -1583       C  
ATOM   5605  O   PRO B 426      54.724  40.988  56.238  1.00142.05           O  
ANISOU 5605  O   PRO B 426    16124  20825  17024   -976   1748  -1826       O  
ATOM   5606  CB  PRO B 426      56.055  43.725  57.780  1.00141.55           C  
ANISOU 5606  CB  PRO B 426    15576  20363  17845  -1879   1954  -1555       C  
ATOM   5607  CG  PRO B 426      56.229  42.840  58.959  1.00145.25           C  
ANISOU 5607  CG  PRO B 426    15891  20813  18484  -1756   1458  -1863       C  
ATOM   5608  CD  PRO B 426      54.836  42.537  59.463  1.00134.30           C  
ANISOU 5608  CD  PRO B 426    14982  19212  16836  -1607   1103  -1826       C  
ATOM   5609  N   ASP B 427      55.631  42.596  54.947  1.00148.49           N  
ANISOU 5609  N   ASP B 427    16741  21840  17840  -1264   2553  -1418       N  
ATOM   5610  CA  ASP B 427      55.889  41.674  53.849  1.00149.42           C  
ANISOU 5610  CA  ASP B 427    16811  22324  17637   -915   2746  -1551       C  
ATOM   5611  C   ASP B 427      57.137  40.835  54.093  1.00148.45           C  
ANISOU 5611  C   ASP B 427    16202  22393  17811   -809   2730  -1850       C  
ATOM   5612  O   ASP B 427      57.199  39.681  53.655  1.00131.64           O  
ANISOU 5612  O   ASP B 427    14069  20455  15493   -455   2657  -2111       O  
ATOM   5613  CB  ASP B 427      56.015  42.458  52.541  1.00138.00           C  
ANISOU 5613  CB  ASP B 427    15426  21112  15895   -914   3318  -1220       C  
ATOM   5614  CG  ASP B 427      54.703  43.085  52.115  1.00145.29           C  
ANISOU 5614  CG  ASP B 427    16858  21928  16418   -884   3324   -934       C  
ATOM   5615  OD1 ASP B 427      53.665  42.760  52.729  1.00133.50           O  
ANISOU 5615  OD1 ASP B 427    15657  20221  14848   -835   2880  -1042       O  
ATOM   5616  OD2 ASP B 427      54.711  43.915  51.181  1.00165.47           O1-
ANISOU 5616  OD2 ASP B 427    19508  24620  18743   -899   3785   -576       O1-
ATOM   5617  N   ASP B 428      58.124  41.390  54.793  1.00158.00           N  
ANISOU 5617  N   ASP B 428    16989  23549  19494  -1100   2781  -1840       N  
ATOM   5618  CA  ASP B 428      59.353  40.685  55.155  1.00151.28           C  
ANISOU 5618  CA  ASP B 428    15613  22898  18968  -1009   2734  -2109       C  
ATOM   5619  C   ASP B 428      59.294  40.141  56.577  1.00140.57           C  
ANISOU 5619  C   ASP B 428    14190  21336  17886   -996   2166  -2346       C  
ATOM   5620  O   ASP B 428      60.295  40.150  57.298  1.00134.94           O  
ANISOU 5620  O   ASP B 428    13007  20697  17567  -1102   2067  -2483       O  
ATOM   5621  CB  ASP B 428      60.558  41.604  54.982  1.00136.89           C  
ANISOU 5621  CB  ASP B 428    13286  21215  17509  -1330   3155  -1966       C  
ATOM   5622  CG  ASP B 428      60.441  42.880  55.798  1.00139.59           C  
ANISOU 5622  CG  ASP B 428    13626  21219  18193  -1811   3084  -1800       C  
ATOM   5623  OD1 ASP B 428      59.361  43.124  56.378  1.00139.50           O  
ANISOU 5623  OD1 ASP B 428    14051  20894  18058  -1862   2764  -1753       O  
ATOM   5624  OD2 ASP B 428      61.431  43.639  55.862  1.00141.61           O1-
ANISOU 5624  OD2 ASP B 428    13431  21516  18860  -2141   3355  -1732       O1-
ATOM   5625  N   PHE B 429      58.126  39.663  57.001  1.00138.32           N  
ANISOU 5625  N   PHE B 429    14350  20818  17389   -854   1790  -2384       N  
ATOM   5626  CA  PHE B 429      57.954  39.193  58.368  1.00137.53           C  
ANISOU 5626  CA  PHE B 429    14239  20519  17498   -819   1280  -2537       C  
ATOM   5627  C   PHE B 429      58.808  37.959  58.631  1.00143.70           C  
ANISOU 5627  C   PHE B 429    14680  21478  18444   -494   1128  -2811       C  
ATOM   5628  O   PHE B 429      58.749  36.975  57.888  1.00148.83           O  
ANISOU 5628  O   PHE B 429    15410  22234  18905   -160   1209  -2942       O  
ATOM   5629  CB  PHE B 429      56.480  38.882  58.630  1.00134.97           C  
ANISOU 5629  CB  PHE B 429    14455  19927  16901   -714    982  -2478       C  
ATOM   5630  CG  PHE B 429      56.226  38.193  59.940  1.00132.23           C  
ANISOU 5630  CG  PHE B 429    14133  19401  16707   -592    498  -2598       C  
ATOM   5631  CD1 PHE B 429      56.460  38.844  61.139  1.00130.54           C  
ANISOU 5631  CD1 PHE B 429    13781  19088  16732   -805    269  -2579       C  
ATOM   5632  CD2 PHE B 429      55.744  36.894  59.971  1.00134.72           C  
ANISOU 5632  CD2 PHE B 429    14618  19642  16926   -255    279  -2731       C  
ATOM   5633  CE1 PHE B 429      56.223  38.212  62.345  1.00134.31           C  
ANISOU 5633  CE1 PHE B 429    14292  19450  17288   -644   -159  -2654       C  
ATOM   5634  CE2 PHE B 429      55.505  36.257  61.173  1.00126.50           C  
ANISOU 5634  CE2 PHE B 429    13609  18429  16027   -122   -121  -2773       C  
ATOM   5635  CZ  PHE B 429      55.742  36.918  62.362  1.00122.83           C  
ANISOU 5635  CZ  PHE B 429    13011  17922  15738   -298   -335  -2716       C  
ATOM   5636  N   THR B 430      59.609  38.020  59.692  1.00144.13           N  
ANISOU 5636  N   THR B 430    14348  21569  18847   -572    899  -2915       N  
ATOM   5637  CA  THR B 430      60.415  36.892  60.154  1.00142.94           C  
ANISOU 5637  CA  THR B 430    13860  21574  18877   -234    697  -3144       C  
ATOM   5638  C   THR B 430      59.905  36.502  61.538  1.00148.64           C  
ANISOU 5638  C   THR B 430    14735  22079  19664   -139    178  -3170       C  
ATOM   5639  O   THR B 430      60.216  37.162  62.534  1.00151.91           O  
ANISOU 5639  O   THR B 430    14951  22496  20270   -351    -36  -3174       O  
ATOM   5640  CB  THR B 430      61.904  37.234  60.180  1.00150.04           C  
ANISOU 5640  CB  THR B 430    14096  22800  20112   -343    878  -3240       C  
ATOM   5641  OG1 THR B 430      62.241  37.825  61.441  1.00160.57           O  
ANISOU 5641  OG1 THR B 430    15186  24100  21723   -576    552  -3283       O  
ATOM   5642  CG2 THR B 430      62.257  38.199  59.055  1.00147.34           C  
ANISOU 5642  CG2 THR B 430    13630  22604  19750   -631   1422  -3086       C  
ATOM   5643  N   GLY B 431      59.118  35.433  61.592  1.00150.59           N  
ANISOU 5643  N   GLY B 431    15329  22139  19750    180    -13  -3193       N  
ATOM   5644  CA  GLY B 431      58.526  34.997  62.842  1.00143.27           C  
ANISOU 5644  CA  GLY B 431    14590  20996  18851    304   -450  -3151       C  
ATOM   5645  C   GLY B 431      57.510  33.903  62.581  1.00141.23           C  
ANISOU 5645  C   GLY B 431    14756  20476  18430    583   -544  -3139       C  
ATOM   5646  O   GLY B 431      57.516  33.280  61.519  1.00149.44           O  
ANISOU 5646  O   GLY B 431    15858  21543  19380    753   -326  -3255       O  
ATOM   5647  N   CYS B 432      56.631  33.688  63.557  1.00116.43           N  
ANISOU 5647  N   CYS B 432    11896  17084  15258    623   -862  -3011       N  
ATOM   5648  CA  CYS B 432      55.657  32.610  63.475  1.00129.06           C  
ANISOU 5648  CA  CYS B 432    13856  18390  16790    857   -976  -2986       C  
ATOM   5649  C   CYS B 432      54.250  33.122  63.749  1.00119.06           C  
ANISOU 5649  C   CYS B 432    13014  16887  15336    648  -1082  -2784       C  
ATOM   5650  O   CYS B 432      54.046  34.160  64.385  1.00109.23           O  
ANISOU 5650  O   CYS B 432    11798  15669  14038    406  -1157  -2650       O  
ATOM   5651  CB  CYS B 432      55.994  31.471  64.447  1.00119.21           C  
ANISOU 5651  CB  CYS B 432    12502  17044  15749   1228  -1244  -2988       C  
ATOM   5652  SG  CYS B 432      57.654  30.791  64.247  1.00132.12           S  
ANISOU 5652  SG  CYS B 432    13606  18972  17621   1555  -1154  -3211       S  
ATOM   5653  N   VAL B 433      53.281  32.364  63.242  1.00133.83           N  
ANISOU 5653  N   VAL B 433    15200  18525  17126    750  -1088  -2793       N  
ATOM   5654  CA  VAL B 433      51.861  32.583  63.488  1.00117.80           C  
ANISOU 5654  CA  VAL B 433    13546  16262  14950    613  -1206  -2608       C  
ATOM   5655  C   VAL B 433      51.300  31.304  64.092  1.00112.63           C  
ANISOU 5655  C   VAL B 433    13031  15301  14462    862  -1418  -2564       C  
ATOM   5656  O   VAL B 433      51.437  30.222  63.506  1.00112.43           O  
ANISOU 5656  O   VAL B 433    13005  15153  14560   1074  -1376  -2748       O  
ATOM   5657  CB  VAL B 433      51.105  32.960  62.205  1.00124.96           C  
ANISOU 5657  CB  VAL B 433    14680  17195  15605    460  -1003  -2654       C  
ATOM   5658  CG1 VAL B 433      49.617  33.119  62.489  1.00120.28           C  
ANISOU 5658  CG1 VAL B 433    14429  16385  14887    346  -1145  -2467       C  
ATOM   5659  CG2 VAL B 433      51.677  34.235  61.612  1.00125.94           C  
ANISOU 5659  CG2 VAL B 433    14676  17591  15586    230   -742  -2627       C  
ATOM   5660  N   ILE B 434      50.680  31.425  65.262  1.00107.37           N  
ANISOU 5660  N   ILE B 434    12488  14497  13809    848  -1626  -2317       N  
ATOM   5661  CA  ILE B 434      50.105  30.294  65.976  1.00108.72           C  
ANISOU 5661  CA  ILE B 434    12792  14360  14157   1070  -1798  -2181       C  
ATOM   5662  C   ILE B 434      48.633  30.588  66.224  1.00108.19           C  
ANISOU 5662  C   ILE B 434    13032  14107  13969    893  -1861  -1962       C  
ATOM   5663  O   ILE B 434      48.243  31.742  66.426  1.00106.48           O  
ANISOU 5663  O   ILE B 434    12891  14027  13539    675  -1854  -1846       O  
ATOM   5664  CB  ILE B 434      50.847  30.028  67.306  1.00115.55           C  
ANISOU 5664  CB  ILE B 434    13470  15289  15146   1313  -1982  -2036       C  
ATOM   5665  CG1 ILE B 434      52.359  30.018  67.082  1.00124.03           C  
ANISOU 5665  CG1 ILE B 434    14167  16646  16312   1449  -1925  -2256       C  
ATOM   5666  CG2 ILE B 434      50.413  28.707  67.910  1.00127.25           C  
ANISOU 5666  CG2 ILE B 434    15072  16428  16850   1601  -2093  -1868       C  
ATOM   5667  CD1 ILE B 434      53.166  29.937  68.359  1.00133.28           C  
ANISOU 5667  CD1 ILE B 434    15101  17989  17551   1683  -2137  -2146       C  
ATOM   5668  N   ALA B 435      47.812  29.540  66.203  1.00111.46           N  
ANISOU 5668  N   ALA B 435    13607  14191  14551    986  -1913  -1911       N  
ATOM   5669  CA  ALA B 435      46.385  29.712  66.442  1.00 99.06           C  
ANISOU 5669  CA  ALA B 435    12277  12451  12911    826  -1967  -1696       C  
ATOM   5670  C   ALA B 435      45.760  28.373  66.803  1.00107.33           C  
ANISOU 5670  C   ALA B 435    13415  13094  14273    975  -2040  -1587       C  
ATOM   5671  O   ALA B 435      46.209  27.320  66.343  1.00116.04           O  
ANISOU 5671  O   ALA B 435    14463  14000  15628   1139  -2013  -1788       O  
ATOM   5672  CB  ALA B 435      45.676  30.316  65.224  1.00 97.59           C  
ANISOU 5672  CB  ALA B 435    12213  12358  12511    580  -1859  -1851       C  
ATOM   5673  N   TRP B 436      44.712  28.427  67.626  1.00110.85           N  
ANISOU 5673  N   TRP B 436    13997  13399  14721    918  -2110  -1260       N  
ATOM   5674  CA  TRP B 436      43.990  27.225  68.020  1.00120.49           C  
ANISOU 5674  CA  TRP B 436    15299  14201  16280   1011  -2142  -1088       C  
ATOM   5675  C   TRP B 436      42.528  27.572  68.273  1.00113.42           C  
ANISOU 5675  C   TRP B 436    14547  13229  15318    801  -2156   -841       C  
ATOM   5676  O   TRP B 436      42.180  28.724  68.536  1.00110.68           O  
ANISOU 5676  O   TRP B 436    14247  13155  14652    678  -2161   -716       O  
ATOM   5677  CB  TRP B 436      44.615  26.576  69.265  1.00124.65           C  
ANISOU 5677  CB  TRP B 436    15761  14623  16975   1338  -2198   -802       C  
ATOM   5678  CG  TRP B 436      44.570  27.414  70.511  1.00112.79           C  
ANISOU 5678  CG  TRP B 436    14270  13385  15201   1402  -2272   -466       C  
ATOM   5679  CD1 TRP B 436      43.662  27.320  71.528  1.00111.77           C  
ANISOU 5679  CD1 TRP B 436    14257  13148  15064   1449  -2289    -51       C  
ATOM   5680  CD2 TRP B 436      45.475  28.462  70.878  1.00112.05           C  
ANISOU 5680  CD2 TRP B 436    14056  13710  14806   1432  -2336   -541       C  
ATOM   5681  NE1 TRP B 436      43.944  28.247  72.501  1.00109.22           N  
ANISOU 5681  NE1 TRP B 436    13919  13174  14407   1540  -2371    113       N  
ATOM   5682  CE2 TRP B 436      45.051  28.961  72.127  1.00115.70           C  
ANISOU 5682  CE2 TRP B 436    14592  14303  15064   1512  -2417   -203       C  
ATOM   5683  CE3 TRP B 436      46.599  29.029  70.272  1.00111.86           C  
ANISOU 5683  CE3 TRP B 436    13854  13965  14682   1390  -2322   -868       C  
ATOM   5684  CZ2 TRP B 436      45.712  29.999  72.779  1.00111.72           C  
ANISOU 5684  CZ2 TRP B 436    14002  14180  14268   1545  -2520   -240       C  
ATOM   5685  CZ3 TRP B 436      47.254  30.061  70.922  1.00106.02           C  
ANISOU 5685  CZ3 TRP B 436    13001  13582  13702   1388  -2407   -870       C  
ATOM   5686  CH2 TRP B 436      46.809  30.535  72.162  1.00104.99           C  
ANISOU 5686  CH2 TRP B 436    12959  13556  13378   1461  -2523   -586       C  
ATOM   5687  N   ASN B 437      41.674  26.550  68.217  1.00105.71           N  
ANISOU 5687  N   ASN B 437    13624  11858  14682    764  -2153   -772       N  
ATOM   5688  CA  ASN B 437      40.237  26.751  68.386  1.00114.52           C  
ANISOU 5688  CA  ASN B 437    14819  12893  15799    555  -2156   -550       C  
ATOM   5689  C   ASN B 437      39.900  27.055  69.840  1.00117.50           C  
ANISOU 5689  C   ASN B 437    15235  13324  16086    678  -2149    -44       C  
ATOM   5690  O   ASN B 437      40.343  26.350  70.749  1.00123.46           O  
ANISOU 5690  O   ASN B 437    15973  13911  17023    929  -2140    208       O  
ATOM   5691  CB  ASN B 437      39.476  25.513  67.919  1.00123.37           C  
ANISOU 5691  CB  ASN B 437    15939  13553  17382    454  -2154   -648       C  
ATOM   5692  CG  ASN B 437      37.974  25.663  68.055  1.00121.10           C  
ANISOU 5692  CG  ASN B 437    15668  13195  17148    217  -2158   -432       C  
ATOM   5693  OD1 ASN B 437      37.381  25.201  69.029  1.00127.14           O  
ANISOU 5693  OD1 ASN B 437    16433  13727  18146    256  -2106    -18       O  
ATOM   5694  ND2 ASN B 437      37.351  26.315  67.081  1.00112.45           N  
ANISOU 5694  ND2 ASN B 437    14572  12329  15826     -7  -2206   -687       N  
ATOM   5695  N   SER B 438      39.094  28.097  70.057  1.00107.42           N  
ANISOU 5695  N   SER B 438    14017  12292  14507    536  -2146    114       N  
ATOM   5696  CA  SER B 438      38.709  28.521  71.397  1.00 98.76           C  
ANISOU 5696  CA  SER B 438    12971  11309  13245    668  -2130    559       C  
ATOM   5697  C   SER B 438      37.211  28.385  71.648  1.00104.95           C  
ANISOU 5697  C   SER B 438    13780  11956  14139    528  -2066    856       C  
ATOM   5698  O   SER B 438      36.676  29.072  72.525  1.00105.45           O  
ANISOU 5698  O   SER B 438    13898  12214  13953    592  -2033   1172       O  
ATOM   5699  CB  SER B 438      39.144  29.961  71.648  1.00 95.08           C  
ANISOU 5699  CB  SER B 438    12547  11264  12315    677  -2167    505       C  
ATOM   5700  OG  SER B 438      38.720  30.806  70.594  1.00104.69           O  
ANISOU 5700  OG  SER B 438    13797  12627  13353    429  -2150    264       O  
ATOM   5701  N   ASN B 439      36.523  27.508  70.898  1.00 96.23           N  
ANISOU 5701  N   ASN B 439    12618  10531  13414    341  -2050    738       N  
ATOM   5702  CA  ASN B 439      35.073  27.360  71.043  1.00106.72           C  
ANISOU 5702  CA  ASN B 439    13905  11741  14902    164  -1995    988       C  
ATOM   5703  C   ASN B 439      34.703  26.962  72.458  1.00109.37           C  
ANISOU 5703  C   ASN B 439    14250  11957  15348    352  -1876   1554       C  
ATOM   5704  O   ASN B 439      33.641  27.340  72.966  1.00111.07           O  
ANISOU 5704  O   ASN B 439    14446  12274  15484    296  -1798   1874       O  
ATOM   5705  CB  ASN B 439      34.533  26.312  70.067  1.00115.27           C  
ANISOU 5705  CB  ASN B 439    14889  12450  16459    -69  -2024    718       C  
ATOM   5706  CG  ASN B 439      33.220  26.726  69.427  1.00102.86           C  
ANISOU 5706  CG  ASN B 439    13231  10998  14853   -350  -2062    643       C  
ATOM   5707  OD1 ASN B 439      33.044  27.884  69.053  1.00 98.02           O  
ANISOU 5707  OD1 ASN B 439    12659  10785  13800   -388  -2103    551       O  
ATOM   5708  ND2 ASN B 439      32.303  25.778  69.275  1.00101.66           N  
ANISOU 5708  ND2 ASN B 439    12945  10492  15190   -547  -2049    676       N  
ATOM   5709  N   ASN B 440      35.563  26.182  73.108  1.00115.00           N  
ANISOU 5709  N   ASN B 440    14986  12474  16234    610  -1847   1708       N  
ATOM   5710  CA  ASN B 440      35.270  25.764  74.470  1.00108.78           C  
ANISOU 5710  CA  ASN B 440    14221  11599  15509    847  -1714   2293       C  
ATOM   5711  C   ASN B 440      35.174  26.965  75.397  1.00105.39           C  
ANISOU 5711  C   ASN B 440    13873  11656  14517   1019  -1714   2530       C  
ATOM   5712  O   ASN B 440      34.340  26.990  76.308  1.00102.79           O  
ANISOU 5712  O   ASN B 440    13551  11369  14135   1109  -1580   2997       O  
ATOM   5713  CB  ASN B 440      36.345  24.797  74.960  1.00113.14           C  
ANISOU 5713  CB  ASN B 440    14795  11914  16277   1159  -1702   2404       C  
ATOM   5714  CG  ASN B 440      37.722  25.157  74.449  1.00122.92           C  
ANISOU 5714  CG  ASN B 440    16040  13368  17297   1270  -1858   1958       C  
ATOM   5715  OD1 ASN B 440      37.975  26.298  74.065  1.00127.84           O  
ANISOU 5715  OD1 ASN B 440    16674  14382  17516   1174  -1956   1674       O  
ATOM   5716  ND2 ASN B 440      38.629  24.190  74.466  1.00125.80           N  
ANISOU 5716  ND2 ASN B 440    16385  13469  17946   1488  -1862   1919       N  
ATOM   5717  N   LEU B 441      36.000  27.984  75.166  1.00103.91           N  
ANISOU 5717  N   LEU B 441    13738  11827  13916   1061  -1850   2204       N  
ATOM   5718  CA  LEU B 441      36.150  29.082  76.115  1.00107.45           C  
ANISOU 5718  CA  LEU B 441    14275  12700  13851   1261  -1881   2353       C  
ATOM   5719  C   LEU B 441      35.409  30.338  75.674  1.00101.29           C  
ANISOU 5719  C   LEU B 441    13541  12173  12773   1050  -1887   2205       C  
ATOM   5720  O   LEU B 441      34.577  30.870  76.416  1.00104.83           O  
ANISOU 5720  O   LEU B 441    14042  12792  12998   1129  -1805   2506       O  
ATOM   5721  CB  LEU B 441      37.639  29.390  76.313  1.00116.86           C  
ANISOU 5721  CB  LEU B 441    15473  14107  14824   1465  -2031   2103       C  
ATOM   5722  CG  LEU B 441      38.543  28.184  76.572  1.00112.93           C  
ANISOU 5722  CG  LEU B 441    14912  13382  14614   1707  -2048   2180       C  
ATOM   5723  CD1 LEU B 441      39.989  28.513  76.262  1.00107.01           C  
ANISOU 5723  CD1 LEU B 441    14091  12837  13731   1792  -2207   1781       C  
ATOM   5724  CD2 LEU B 441      38.413  27.713  78.001  1.00108.94           C  
ANISOU 5724  CD2 LEU B 441    14453  12918  14023   2081  -1980   2722       C  
ATOM   5725  N   ASP B 442      35.706  30.825  74.473  1.00 96.90           N  
ANISOU 5725  N   ASP B 442    12970  11653  12194    816  -1965   1765       N  
ATOM   5726  CA  ASP B 442      35.220  32.118  74.007  1.00107.44           C  
ANISOU 5726  CA  ASP B 442    14370  13237  13214    664  -1972   1614       C  
ATOM   5727  C   ASP B 442      33.888  32.031  73.276  1.00 96.40           C  
ANISOU 5727  C   ASP B 442    12914  11749  11965    430  -1911   1656       C  
ATOM   5728  O   ASP B 442      33.522  32.973  72.565  1.00 92.50           O  
ANISOU 5728  O   ASP B 442    12458  11430  11258    294  -1926   1482       O  
ATOM   5729  CB  ASP B 442      36.276  32.768  73.109  1.00109.83           C  
ANISOU 5729  CB  ASP B 442    14687  13661  13383    562  -2058   1169       C  
ATOM   5730  CG  ASP B 442      37.627  32.874  73.790  1.00110.20           C  
ANISOU 5730  CG  ASP B 442    14728  13828  13315    767  -2142   1085       C  
ATOM   5731  OD1 ASP B 442      37.663  32.953  75.038  1.00111.25           O  
ANISOU 5731  OD1 ASP B 442    14904  14078  13288   1008  -2160   1345       O  
ATOM   5732  OD2 ASP B 442      38.653  32.872  73.080  1.00111.65           O1-
ANISOU 5732  OD2 ASP B 442    14845  14025  13553    705  -2191    755       O1-
ATOM   5733  N   SER B 443      33.151  30.938  73.443  1.00 95.04           N  
ANISOU 5733  N   SER B 443    12635  11310  12168    384  -1842   1893       N  
ATOM   5734  CA  SER B 443      31.834  30.776  72.845  1.00 92.31           C  
ANISOU 5734  CA  SER B 443    12171  10892  12011    152  -1803   1935       C  
ATOM   5735  C   SER B 443      30.823  30.518  73.946  1.00 92.58           C  
ANISOU 5735  C   SER B 443    12145  10900  12130    248  -1648   2458       C  
ATOM   5736  O   SER B 443      31.032  29.638  74.785  1.00102.88           O  
ANISOU 5736  O   SER B 443    13435  11997  13657    396  -1558   2762       O  
ATOM   5737  CB  SER B 443      31.813  29.613  71.861  1.00 96.59           C  
ANISOU 5737  CB  SER B 443    12583  11091  13024    -64  -1860   1670       C  
ATOM   5738  OG  SER B 443      32.717  29.846  70.806  1.00112.57           O  
ANISOU 5738  OG  SER B 443    14657  13182  14933   -123  -1976   1194       O  
ATOM   5739  N   LYS B 444      29.723  31.261  73.927  1.00 98.80           N  
ANISOU 5739  N   LYS B 444    12888  11905  12745    186  -1595   2587       N  
ATOM   5740  CA  LYS B 444      28.683  31.117  74.933  1.00105.39           C  
ANISOU 5740  CA  LYS B 444    13639  12774  13631    284  -1414   3095       C  
ATOM   5741  C   LYS B 444      27.330  30.988  74.253  1.00101.04           C  
ANISOU 5741  C   LYS B 444    12856  12206  13328     16  -1390   3112       C  
ATOM   5742  O   LYS B 444      27.056  31.680  73.269  1.00100.96           O  
ANISOU 5742  O   LYS B 444    12828  12375  13157   -122  -1510   2797       O  
ATOM   5743  CB  LYS B 444      28.676  32.312  75.892  1.00109.00           C  
ANISOU 5743  CB  LYS B 444    14266  13603  13546    575  -1350   3288       C  
ATOM   5744  CG  LYS B 444      27.711  32.185  77.062  1.00115.16           C  
ANISOU 5744  CG  LYS B 444    14980  14477  14299    759  -1128   3841       C  
ATOM   5745  CD  LYS B 444      27.694  33.449  77.917  1.00126.96           C  
ANISOU 5745  CD  LYS B 444    16663  16359  15214   1066  -1085   3938       C  
ATOM   5746  CE  LYS B 444      27.049  34.624  77.192  1.00100.84           C  
ANISOU 5746  CE  LYS B 444    13372  13266  11678    966  -1129   3720       C  
ATOM   5747  NZ  LYS B 444      26.945  35.815  78.085  1.00 94.97           N  
ANISOU 5747  NZ  LYS B 444    12822  12842  10421   1280  -1063   3817       N  
ATOM   5748  N   VAL B 445      26.492  30.093  74.783  1.00 80.73           N  
ANISOU 5748  N   VAL B 445    10086   9428  11158    -49  -1229   3497       N  
ATOM   5749  CA  VAL B 445      25.127  29.956  74.292  1.00 82.64           C  
ANISOU 5749  CA  VAL B 445    10043   9686  11673   -305  -1199   3554       C  
ATOM   5750  C   VAL B 445      24.430  31.302  74.380  1.00 82.47           C  
ANISOU 5750  C   VAL B 445    10044  10125  11165   -176  -1176   3627       C  
ATOM   5751  O   VAL B 445      24.482  31.979  75.412  1.00 93.90           O  
ANISOU 5751  O   VAL B 445    11645  11798  12233    128  -1038   3929       O  
ATOM   5752  CB  VAL B 445      24.384  28.872  75.093  1.00 87.24           C  
ANISOU 5752  CB  VAL B 445    10406   9982  12760   -366   -964   4055       C  
ATOM   5753  CG1 VAL B 445      22.962  28.707  74.583  1.00 89.82           C  
ANISOU 5753  CG1 VAL B 445    10367  10333  13426   -668   -942   4094       C  
ATOM   5754  CG2 VAL B 445      25.139  27.560  75.012  1.00 89.67           C  
ANISOU 5754  CG2 VAL B 445    10730   9774  13566   -457   -973   3989       C  
ATOM   5755  N   GLY B 446      23.787  31.708  73.288  1.00108.37           N  
ANISOU 5755  N   GLY B 446    13183  13559  14435   -376  -1318   3334       N  
ATOM   5756  CA  GLY B 446      23.240  33.036  73.176  1.00101.80           C  
ANISOU 5756  CA  GLY B 446    12403  13139  13136   -231  -1320   3345       C  
ATOM   5757  C   GLY B 446      24.206  34.029  72.563  1.00 99.34           C  
ANISOU 5757  C   GLY B 446    12388  12975  12382   -131  -1466   2970       C  
ATOM   5758  O   GLY B 446      23.773  35.014  71.955  1.00 98.44           O  
ANISOU 5758  O   GLY B 446    12297  13133  11973    -95  -1523   2851       O  
ATOM   5759  N   GLY B 447      25.506  33.794  72.717  1.00103.87           N  
ANISOU 5759  N   GLY B 447    13172  13374  12919    -74  -1511   2808       N  
ATOM   5760  CA  GLY B 447      26.516  34.606  72.035  1.00106.39           C  
ANISOU 5760  CA  GLY B 447    13723  13789  12910    -38  -1634   2433       C  
ATOM   5761  C   GLY B 447      27.434  35.341  72.993  1.00 93.42           C  
ANISOU 5761  C   GLY B 447    12346  12225  10924    223  -1575   2509       C  
ATOM   5762  O   GLY B 447      27.010  35.970  73.958  1.00103.51           O  
ANISOU 5762  O   GLY B 447    13699  13668  11962    440  -1456   2791       O  
ATOM   5763  N   ASN B 448      28.737  35.258  72.703  1.00 92.00           N  
ANISOU 5763  N   ASN B 448    12295  11942  10718    207  -1668   2218       N  
ATOM   5764  CA  ASN B 448      29.763  36.031  73.404  1.00100.48           C  
ANISOU 5764  CA  ASN B 448    13590  13110  11479    404  -1669   2167       C  
ATOM   5765  C   ASN B 448      30.135  37.209  72.512  1.00100.02           C  
ANISOU 5765  C   ASN B 448    13666  13182  11155    342  -1717   1866       C  
ATOM   5766  O   ASN B 448      30.851  37.051  71.523  1.00 95.26           O  
ANISOU 5766  O   ASN B 448    13055  12513  10626    193  -1793   1559       O  
ATOM   5767  CB  ASN B 448      30.980  35.176  73.737  1.00 98.40           C  
ANISOU 5767  CB  ASN B 448    13334  12670  11384    445  -1730   2074       C  
ATOM   5768  CG  ASN B 448      32.064  35.961  74.446  1.00105.48           C  
ANISOU 5768  CG  ASN B 448    14403  13701  11973    631  -1772   1972       C  
ATOM   5769  OD1 ASN B 448      31.789  36.966  75.100  1.00114.02           O  
ANISOU 5769  OD1 ASN B 448    15613  14970  12740    782  -1730   2065       O  
ATOM   5770  ND2 ASN B 448      33.304  35.501  74.327  1.00116.42           N  
ANISOU 5770  ND2 ASN B 448    15777  14996  13461    629  -1863   1756       N  
ATOM   5771  N   TYR B 449      29.637  38.393  72.868  1.00100.21           N  
ANISOU 5771  N   TYR B 449    13820  13381  10873    477  -1646   1974       N  
ATOM   5772  CA  TYR B 449      29.824  39.600  72.078  1.00 91.75           C  
ANISOU 5772  CA  TYR B 449    12894  12397   9568    441  -1643   1772       C  
ATOM   5773  C   TYR B 449      30.939  40.488  72.619  1.00100.55           C  
ANISOU 5773  C   TYR B 449    14213  13506  10487    529  -1646   1613       C  
ATOM   5774  O   TYR B 449      30.957  41.690  72.335  1.00107.96           O  
ANISOU 5774  O   TYR B 449    15311  14484  11224    551  -1592   1533       O  
ATOM   5775  CB  TYR B 449      28.511  40.382  72.010  1.00 76.30           C  
ANISOU 5775  CB  TYR B 449    10947  10602   7441    539  -1556   1979       C  
ATOM   5776  CG  TYR B 449      27.406  39.645  71.291  1.00 86.25           C  
ANISOU 5776  CG  TYR B 449    11959  11914   8898    415  -1586   2072       C  
ATOM   5777  CD1 TYR B 449      27.263  39.739  69.912  1.00 97.30           C  
ANISOU 5777  CD1 TYR B 449    13302  13377  10290    272  -1661   1870       C  
ATOM   5778  CD2 TYR B 449      26.510  38.846  71.989  1.00 94.74           C  
ANISOU 5778  CD2 TYR B 449    12837  12990  10168    442  -1537   2358       C  
ATOM   5779  CE1 TYR B 449      26.253  39.065  69.251  1.00 93.06           C  
ANISOU 5779  CE1 TYR B 449    12510  12920   9928    154  -1733   1892       C  
ATOM   5780  CE2 TYR B 449      25.499  38.167  71.337  1.00102.45           C  
ANISOU 5780  CE2 TYR B 449    13540  14002  11384    286  -1580   2406       C  
ATOM   5781  CZ  TYR B 449      25.375  38.279  69.969  1.00 90.40           C  
ANISOU 5781  CZ  TYR B 449    11953  12555   9841    139  -1701   2143       C  
ATOM   5782  OH  TYR B 449      24.368  37.602  69.321  1.00 91.88           O  
ANISOU 5782  OH  TYR B 449    11842  12809  10260    -19  -1787   2133       O  
ATOM   5783  N   ASN B 450      31.867  39.923  73.391  1.00 96.54           N  
ANISOU 5783  N   ASN B 450    13692  12940  10051    585  -1710   1563       N  
ATOM   5784  CA  ASN B 450      32.941  40.708  73.986  1.00 88.45           C  
ANISOU 5784  CA  ASN B 450    12808  11938   8862    659  -1753   1371       C  
ATOM   5785  C   ASN B 450      34.129  40.896  73.055  1.00 98.47           C  
ANISOU 5785  C   ASN B 450    14060  13131  10224    460  -1797   1039       C  
ATOM   5786  O   ASN B 450      34.882  41.863  73.221  1.00 94.65           O  
ANISOU 5786  O   ASN B 450    13683  12650   9630    444  -1802    848       O  
ATOM   5787  CB  ASN B 450      33.408  40.058  75.291  1.00 94.62           C  
ANISOU 5787  CB  ASN B 450    13559  12765   9628    858  -1824   1473       C  
ATOM   5788  CG  ASN B 450      32.348  40.102  76.373  1.00109.03           C  
ANISOU 5788  CG  ASN B 450    15432  14713  11280   1107  -1740   1815       C  
ATOM   5789  OD1 ASN B 450      31.334  40.788  76.236  1.00103.99           O  
ANISOU 5789  OD1 ASN B 450    14858  14134  10518   1140  -1636   1936       O  
ATOM   5790  ND2 ASN B 450      32.574  39.367  77.455  1.00110.60           N  
ANISOU 5790  ND2 ASN B 450    15594  14976  11455   1314  -1767   1996       N  
ATOM   5791  N   TYR B 451      34.317  40.005  72.086  1.00110.85           N  
ANISOU 5791  N   TYR B 451    15486  14628  12003    308  -1817    953       N  
ATOM   5792  CA  TYR B 451      35.367  40.171  71.094  1.00104.45           C  
ANISOU 5792  CA  TYR B 451    14646  13784  11257    141  -1816    662       C  
ATOM   5793  C   TYR B 451      34.846  41.011  69.937  1.00 82.43           C  
ANISOU 5793  C   TYR B 451    11942  11034   8344     34  -1709    640       C  
ATOM   5794  O   TYR B 451      33.720  40.815  69.469  1.00 88.93           O  
ANISOU 5794  O   TYR B 451    12744  11905   9142     41  -1691    783       O  
ATOM   5795  CB  TYR B 451      35.862  38.815  70.592  1.00 94.01           C  
ANISOU 5795  CB  TYR B 451    13148  12381  10190     78  -1879    551       C  
ATOM   5796  CG  TYR B 451      36.538  37.992  71.666  1.00 98.79           C  
ANISOU 5796  CG  TYR B 451    13673  12942  10920    220  -1973    591       C  
ATOM   5797  CD1 TYR B 451      37.891  38.145  71.935  1.00107.05           C  
ANISOU 5797  CD1 TYR B 451    14669  14028  11978    240  -2033    382       C  
ATOM   5798  CD2 TYR B 451      35.825  37.057  72.404  1.00107.19           C  
ANISOU 5798  CD2 TYR B 451    14690  13937  12099    346  -1992    860       C  
ATOM   5799  CE1 TYR B 451      38.514  37.396  72.919  1.00115.83           C  
ANISOU 5799  CE1 TYR B 451    15696  15145  13168    421  -2138    433       C  
ATOM   5800  CE2 TYR B 451      36.440  36.300  73.387  1.00116.80           C  
ANISOU 5800  CE2 TYR B 451    15850  15124  13405    525  -2060    952       C  
ATOM   5801  CZ  TYR B 451      37.785  36.473  73.638  1.00111.93           C  
ANISOU 5801  CZ  TYR B 451    15193  14580  12753    581  -2146    733       C  
ATOM   5802  OH  TYR B 451      38.402  35.724  74.614  1.00111.73           O  
ANISOU 5802  OH  TYR B 451    15100  14570  12782    808  -2232    837       O  
ATOM   5803  N   ARG B 452      35.667  41.957  69.487  1.00 75.52           N  
ANISOU 5803  N   ARG B 452    11146  10147   7400    -56  -1632    474       N  
ATOM   5804  CA  ARG B 452      35.279  42.923  68.469  1.00 73.99           C  
ANISOU 5804  CA  ARG B 452    11071   9982   7060   -114  -1493    505       C  
ATOM   5805  C   ARG B 452      36.300  42.928  67.338  1.00 94.01           C  
ANISOU 5805  C   ARG B 452    13545  12527   9648   -267  -1411    302       C  
ATOM   5806  O   ARG B 452      37.315  42.224  67.374  1.00 97.21           O  
ANISOU 5806  O   ARG B 452    13805  12916  10214   -328  -1466    115       O  
ATOM   5807  CB  ARG B 452      35.164  44.336  69.049  1.00 72.26           C  
ANISOU 5807  CB  ARG B 452    11056   9694   6705    -55  -1402    572       C  
ATOM   5808  CG  ARG B 452      34.011  44.589  69.990  1.00 70.52           C  
ANISOU 5808  CG  ARG B 452    10933   9504   6359    141  -1425    792       C  
ATOM   5809  CD  ARG B 452      34.320  45.867  70.741  1.00 93.33           C  
ANISOU 5809  CD  ARG B 452    14018  12281   9163    196  -1367    731       C  
ATOM   5810  NE  ARG B 452      33.152  46.680  71.049  1.00 95.17           N  
ANISOU 5810  NE  ARG B 452    14423  12519   9218    385  -1282    937       N  
ATOM   5811  CZ  ARG B 452      33.223  47.886  71.594  1.00110.98           C  
ANISOU 5811  CZ  ARG B 452    16637  14387  11144    461  -1210    881       C  
ATOM   5812  NH1 ARG B 452      34.387  48.439  71.897  1.00105.95           N  
ANISOU 5812  NH1 ARG B 452    16048  13596  10611    328  -1226    613       N  
ATOM   5813  NH2 ARG B 452      32.101  48.559  71.832  1.00120.86           N  
ANISOU 5813  NH2 ARG B 452    18039  15650  12233    675  -1121   1078       N  
ATOM   5814  N   TYR B 453      36.023  43.757  66.334  1.00 97.80           N  
ANISOU 5814  N   TYR B 453    14135  13051   9975   -296  -1258    365       N  
ATOM   5815  CA  TYR B 453      36.927  43.966  65.212  1.00 94.45           C  
ANISOU 5815  CA  TYR B 453    13678  12666   9545   -413  -1114    234       C  
ATOM   5816  C   TYR B 453      36.606  45.309  64.572  1.00100.82           C  
ANISOU 5816  C   TYR B 453    14680  13455  10171   -400   -902    408       C  
ATOM   5817  O   TYR B 453      35.507  45.847  64.732  1.00 97.10           O  
ANISOU 5817  O   TYR B 453    14348  12990   9554   -271   -897    616       O  
ATOM   5818  CB  TYR B 453      36.848  42.802  64.206  1.00 92.02           C  
ANISOU 5818  CB  TYR B 453    13225  12510   9228   -414  -1175    112       C  
ATOM   5819  CG  TYR B 453      35.522  42.586  63.474  1.00 99.19           C  
ANISOU 5819  CG  TYR B 453    14160  13577   9949   -320  -1226    226       C  
ATOM   5820  CD1 TYR B 453      34.891  43.605  62.769  1.00 98.05           C  
ANISOU 5820  CD1 TYR B 453    14166  13541   9547   -244  -1094    413       C  
ATOM   5821  CD2 TYR B 453      34.902  41.344  63.502  1.00103.32           C  
ANISOU 5821  CD2 TYR B 453    14540  14136  10580   -304  -1415    147       C  
ATOM   5822  CE1 TYR B 453      33.692  43.389  62.115  1.00102.95           C  
ANISOU 5822  CE1 TYR B 453    14769  14364   9984   -136  -1177    498       C  
ATOM   5823  CE2 TYR B 453      33.707  41.119  62.852  1.00108.13           C  
ANISOU 5823  CE2 TYR B 453    15119  14909  11055   -245  -1495    204       C  
ATOM   5824  CZ  TYR B 453      33.104  42.144  62.161  1.00110.34           C  
ANISOU 5824  CZ  TYR B 453    15525  15358  11040   -153  -1392    370       C  
ATOM   5825  OH  TYR B 453      31.911  41.920  61.515  1.00123.32           O  
ANISOU 5825  OH  TYR B 453    17102  17222  12533    -73  -1505    412       O  
ATOM   5826  N   ARG B 454      37.587  45.850  63.853  1.00 97.82           N  
ANISOU 5826  N   ARG B 454    14301  13049   9816   -519   -705    348       N  
ATOM   5827  CA  ARG B 454      37.374  47.062  63.073  1.00 91.09           C  
ANISOU 5827  CA  ARG B 454    13637  12163   8810   -498   -452    557       C  
ATOM   5828  C   ARG B 454      36.785  46.700  61.717  1.00101.41           C  
ANISOU 5828  C   ARG B 454    14943  13745   9844   -379   -404    649       C  
ATOM   5829  O   ARG B 454      37.391  45.947  60.948  1.00101.16           O  
ANISOU 5829  O   ARG B 454    14768  13876   9793   -421   -392    484       O  
ATOM   5830  CB  ARG B 454      38.675  47.838  62.898  1.00 91.73           C  
ANISOU 5830  CB  ARG B 454    13703  12080   9068   -692   -221    492       C  
ATOM   5831  CG  ARG B 454      38.451  49.313  62.625  1.00 92.60           C  
ANISOU 5831  CG  ARG B 454    14055  11993   9136   -687     45    741       C  
ATOM   5832  CD  ARG B 454      39.730  50.107  62.757  1.00104.20           C  
ANISOU 5832  CD  ARG B 454    15480  13212  10897   -937    253    650       C  
ATOM   5833  NE  ARG B 454      39.970  50.446  64.152  1.00109.34           N  
ANISOU 5833  NE  ARG B 454    16138  13627  11780  -1027     90    461       N  
ATOM   5834  CZ  ARG B 454      39.589  51.582  64.718  1.00105.93           C  
ANISOU 5834  CZ  ARG B 454    15932  12904  11411  -1014    162    542       C  
ATOM   5835  NH1 ARG B 454      38.962  52.521  64.028  1.00110.05           N  
ANISOU 5835  NH1 ARG B 454    16698  13298  11818   -914    414    849       N  
ATOM   5836  NH2 ARG B 454      39.834  51.776  66.008  1.00106.60           N  
ANISOU 5836  NH2 ARG B 454    16007  12832  11662  -1070    -26    304       N  
ATOM   5837  N   LEU B 455      35.605  47.242  61.423  1.00103.31           N  
ANISOU 5837  N   LEU B 455    15336  14063   9854   -202   -384    894       N  
ATOM   5838  CA  LEU B 455      34.942  46.977  60.156  1.00 95.11           C  
ANISOU 5838  CA  LEU B 455    14291  13342   8503    -50   -377    976       C  
ATOM   5839  C   LEU B 455      35.176  48.070  59.122  1.00 90.13           C  
ANISOU 5839  C   LEU B 455    13832  12753   7658     27    -59   1221       C  
ATOM   5840  O   LEU B 455      35.077  47.795  57.922  1.00106.57           O  
ANISOU 5840  O   LEU B 455    15889  15146   9456    141    -10   1237       O  
ATOM   5841  CB  LEU B 455      33.435  46.787  60.383  1.00 97.24           C  
ANISOU 5841  CB  LEU B 455    14564  13752   8633    128   -578   1102       C  
ATOM   5842  CG  LEU B 455      32.561  46.436  59.177  1.00 90.52           C  
ANISOU 5842  CG  LEU B 455    13658  13284   7450    302   -660   1140       C  
ATOM   5843  CD1 LEU B 455      33.039  45.147  58.527  1.00 85.39           C  
ANISOU 5843  CD1 LEU B 455    12811  12819   6814    213   -800    802       C  
ATOM   5844  CD2 LEU B 455      31.103  46.315  59.593  1.00 92.89           C  
ANISOU 5844  CD2 LEU B 455    13904  13700   7691    446   -860   1264       C  
ATOM   5845  N   PHE B 456      35.513  49.285  59.551  1.00 92.02           N  
ANISOU 5845  N   PHE B 456    14249  12683   8031    -25    166   1405       N  
ATOM   5846  CA  PHE B 456      35.717  50.399  58.637  1.00106.40           C  
ANISOU 5846  CA  PHE B 456    16256  14468   9704     48    517   1706       C  
ATOM   5847  C   PHE B 456      36.895  51.253  59.095  1.00107.15           C  
ANISOU 5847  C   PHE B 456    16401  14162  10150   -201    773   1700       C  
ATOM   5848  O   PHE B 456      37.085  51.468  60.296  1.00113.68           O  
ANISOU 5848  O   PHE B 456    17231  14694  11268   -337    665   1553       O  
ATOM   5849  CB  PHE B 456      34.457  51.267  58.533  1.00111.99           C  
ANISOU 5849  CB  PHE B 456    17186  15181  10185    327    559   2051       C  
ATOM   5850  CG  PHE B 456      33.244  50.543  58.023  1.00112.74           C  
ANISOU 5850  CG  PHE B 456    17193  15702   9940    571    307   2068       C  
ATOM   5851  CD1 PHE B 456      33.233  49.986  56.756  1.00104.29           C  
ANISOU 5851  CD1 PHE B 456    16036  15045   8544    682    300   2040       C  
ATOM   5852  CD2 PHE B 456      32.097  50.460  58.796  1.00104.89           C  
ANISOU 5852  CD2 PHE B 456    16190  14717   8948    698     84   2105       C  
ATOM   5853  CE1 PHE B 456      32.113  49.333  56.281  1.00 97.28           C  
ANISOU 5853  CE1 PHE B 456    15038  14559   7363    887     32   1999       C  
ATOM   5854  CE2 PHE B 456      30.972  49.811  58.326  1.00 96.69           C  
ANISOU 5854  CE2 PHE B 456    15018  14074   7647    890   -152   2108       C  
ATOM   5855  CZ  PHE B 456      30.980  49.247  57.066  1.00102.27           C  
ANISOU 5855  CZ  PHE B 456    15626  15179   8055    972   -197   2036       C  
ATOM   5856  N   ARG B 457      37.673  51.748  58.128  1.0