CNRS Nantes University UFIP UFIP
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***  abc  ***

elNémo ID: 22051816202125081

Job options:

ID        	=	 22051816202125081
JOBID     	=	 abc
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 abc

HEADER    VIRAL PROTEIN                           19-APR-20   6WLC              
TITLE     CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE FROM SARS COV-2 IN THE    
TITLE    2 COMPLEX WITH URIDINE-5'-MONOPHOSPHATE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: URIDYLATE-SPECIFIC ENDORIBONUCLEASE;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NSP15 ENDORIBNUCLEASE;                                      
COMPND   5 EC: 3.1.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: GOLD;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG53                                   
KEYWDS    SARS CORONA VIRUS 2, ENDORIBONUCLEASE, COVID-19, STRUCTURAL GENOMICS, 
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, VIRAL  
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,N.MALTSEVA,R.JEDRZEJCZAK,M.ENDRES,C.CHANG,A.GODZIK,K.MICHALSKA, 
AUTHOR   2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   5   24-FEB-21 6WLC    1       JRNL                                     
REVDAT   4   09-DEC-20 6WLC    1       JRNL                                     
REVDAT   3   10-JUN-20 6WLC    1       COMPND SOURCE REMARK DBREF               
REVDAT   3 2                   1       SEQADV SEQRES HELIX  SHEET               
REVDAT   3 3                   1       SITE   ATOM                              
REVDAT   2   06-MAY-20 6WLC    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   1   29-APR-20 6WLC    0                                                
JRNL        AUTH   Y.KIM,J.WOWER,N.MALTSEVA,C.CHANG,R.JEDRZEJCZAK,M.WILAMOWSKI, 
JRNL        AUTH 2 S.KANG,V.NICOLAESCU,G.RANDALL,K.MICHALSKA,A.JOACHIMIAK       
JRNL        TITL   TIPIRACIL BINDS TO URIDINE SITE AND INHIBITS NSP15           
JRNL        TITL 2 ENDORIBONUCLEASE NENDOU FROM SARS-COV-2.                     
JRNL        REF    COMMUN BIOL                   V.   4   193 2021              
JRNL        REFN                   ESSN 2399-3642                               
JRNL        PMID   33564093                                                     
JRNL        DOI    10.1038/S42003-021-01735-9                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.KIM,J.WOWER,N.MALTSEVA,C.CHANG,R.JEDRZEJCZAK,M.WILAMOWSKI, 
REMARK   1  AUTH 2 S.KANG,,N.NICOLAESCU,G.RANDALL,K.MICHALSKA,A.JOACHIMIAK,     
REMARK   1  AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
REMARK   1  AUTH 4 (CSGID)                                                      
REMARK   1  TITL   TIPIRACIL BINDS TO URIDINE SITE AND INHIBITS NSP15           
REMARK   1  TITL 2 ENDORIBONUCLEASE NENDOU FROM SARS-COV-2                      
REMARK   1  REF    BIORXIV                                    2020              
REMARK   1  REFN                                                                
REMARK   1  DOI    10.1101/2020.06.26.173872                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
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) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 129762                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6406                            
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 40.6300 -  5.6500    1.00     4244   204  0.1544 0.1847        
REMARK   3     2  5.6400 -  4.4800    1.00     4150   224  0.1334 0.1599        
REMARK   3     3  4.4800 -  3.9200    1.00     4156   216  0.1334 0.1510        
REMARK   3     4  3.9200 -  3.5600    1.00     4144   223  0.1550 0.1732        
REMARK   3     5  3.5600 -  3.3000    1.00     4077   256  0.1686 0.1945        
REMARK   3     6  3.3000 -  3.1100    1.00     4136   248  0.1773 0.2097        
REMARK   3     7  3.1100 -  2.9500    1.00     4137   204  0.1824 0.2043        
REMARK   3     8  2.9500 -  2.8200    1.00     4107   237  0.1910 0.2204        
REMARK   3     9  2.8200 -  2.7200    1.00     4130   216  0.1821 0.2067        
REMARK   3    10  2.7200 -  2.6200    1.00     4145   196  0.1809 0.1856        
REMARK   3    11  2.6200 -  2.5400    1.00     4132   193  0.1797 0.2092        
REMARK   3    12  2.5400 -  2.4700    1.00     4166   194  0.1787 0.1981        
REMARK   3    13  2.4700 -  2.4000    1.00     4150   198  0.1777 0.2204        
REMARK   3    14  2.4000 -  2.3400    1.00     4115   193  0.1769 0.1858        
REMARK   3    15  2.3400 -  2.2900    1.00     4086   224  0.1745 0.2142        
REMARK   3    16  2.2900 -  2.2400    1.00     4143   209  0.1810 0.2025        
REMARK   3    17  2.2400 -  2.2000    1.00     4148   193  0.1869 0.2160        
REMARK   3    18  2.2000 -  2.1600    1.00     4127   192  0.1910 0.2372        
REMARK   3    19  2.1600 -  2.1200    1.00     4145   192  0.2006 0.2209        
REMARK   3    20  2.1200 -  2.0800    1.00     4077   255  0.2078 0.2345        
REMARK   3    21  2.0800 -  2.0500    1.00     4114   200  0.2077 0.2559        
REMARK   3    22  2.0500 -  2.0200    1.00     4130   207  0.2133 0.2283        
REMARK   3    23  2.0200 -  1.9900    1.00     4136   186  0.2218 0.2502        
REMARK   3    24  1.9900 -  1.9600    1.00     4072   243  0.2340 0.2769        
REMARK   3    25  1.9600 -  1.9300    1.00     4129   227  0.2542 0.2886        
REMARK   3    26  1.9300 -  1.9100    1.00     4084   242  0.2666 0.3022        
REMARK   3    27  1.9100 -  1.8800    1.00     4028   231  0.2845 0.3090        
REMARK   3    28  1.8800 -  1.8600    0.99     4116   193  0.3082 0.3190        
REMARK   3    29  1.8600 -  1.8400    0.97     3954   239  0.3348 0.3427        
REMARK   3    30  1.8400 -  1.8200    0.94     3878   171  0.3524 0.3684        
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)     : 0.233            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.77                          
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      :  0.006           5946                                  
REMARK   3   ANGLE     :  0.762           8068                                  
REMARK   3   CHIRALITY :  0.057            917                                  
REMARK   3   PLANARITY :  0.005           1038                                  
REMARK   3   DIHEDRAL  : 19.102           2202                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 197 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  60.6565 -23.4994 -14.5239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2680 T22:   0.2532                                     
REMARK   3      T33:   0.4518 T12:   0.0237                                     
REMARK   3      T13:   0.0121 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2443 L22:   1.6673                                     
REMARK   3      L33:   1.1331 L12:   0.6311                                     
REMARK   3      L13:  -0.5173 L23:  -0.6836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0875 S12:  -0.0088 S13:   0.3807                       
REMARK   3      S21:   0.0640 S22:   0.0664 S23:   0.2953                       
REMARK   3      S31:  -0.1897 S32:  -0.1489 S33:  -0.1569                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 225 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  79.3562 -24.2578 -43.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5200 T22:   0.2282                                     
REMARK   3      T33:   0.3525 T12:  -0.0055                                     
REMARK   3      T13:  -0.0492 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4635 L22:   4.9275                                     
REMARK   3      L33:   6.7516 L12:   0.1418                                     
REMARK   3      L13:  -0.6752 L23:  -0.1552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2419 S12:   0.6921 S13:  -0.6218                       
REMARK   3      S21:  -0.7841 S22:   0.1189 S23:   0.1936                       
REMARK   3      S31:   1.1396 S32:  -0.0388 S33:   0.1612                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  87.0133 -24.4001 -33.3291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3961 T22:   0.2537                                     
REMARK   3      T33:   0.3999 T12:  -0.0056                                     
REMARK   3      T13:   0.0389 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4783 L22:   1.9214                                     
REMARK   3      L33:   1.4309 L12:  -1.1973                                     
REMARK   3      L13:  -0.1535 L23:  -0.1467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0322 S12:   0.0911 S13:  -0.0066                       
REMARK   3      S21:  -0.2804 S22:   0.0199 S23:  -0.0549                       
REMARK   3      S31:   0.1349 S32:   0.0682 S33:   0.0141                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 310 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  89.1195 -10.1401 -29.9023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3600 T22:   0.2766                                     
REMARK   3      T33:   0.5178 T12:   0.0177                                     
REMARK   3      T13:   0.0123 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2991 L22:   3.1567                                     
REMARK   3      L33:   2.6738 L12:   1.4659                                     
REMARK   3      L13:  -2.0420 L23:  -0.5843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1039 S12:  -0.1447 S13:   0.6285                       
REMARK   3      S21:  -0.0370 S22:   0.0716 S23:  -0.4015                       
REMARK   3      S31:   0.1212 S32:   0.2783 S33:  -0.1412                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 38 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  91.3470 -30.9709   7.7388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2429 T22:   0.2988                                     
REMARK   3      T33:   0.3299 T12:   0.0238                                     
REMARK   3      T13:  -0.0119 T23:  -0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6851 L22:   4.1834                                     
REMARK   3      L33:   5.3026 L12:   1.4750                                     
REMARK   3      L13:   0.7913 L23:   2.1765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0644 S12:   0.1015 S13:  -0.1060                       
REMARK   3      S21:   0.0197 S22:   0.1959 S23:  -0.3951                       
REMARK   3      S31:  -0.1734 S32:   0.3588 S33:  -0.1575                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 183 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2287 -16.1678  15.7649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2782 T22:   0.2345                                     
REMARK   3      T33:   0.3555 T12:  -0.0094                                     
REMARK   3      T13:  -0.0230 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9910 L22:   1.7041                                     
REMARK   3      L33:   1.2029 L12:  -0.4786                                     
REMARK   3      L13:  -0.4289 L23:   0.6955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:  -0.0311 S13:   0.2012                       
REMARK   3      S21:   0.0613 S22:   0.0506 S23:  -0.0019                       
REMARK   3      S31:  -0.0898 S32:   0.0665 S33:  -0.0434                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 184 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.6053 -15.3790  27.1295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4406 T22:   0.2994                                     
REMARK   3      T33:   0.4647 T12:   0.0051                                     
REMARK   3      T13:  -0.0123 T23:  -0.0771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7002 L22:   7.6063                                     
REMARK   3      L33:   4.4337 L12:   1.2574                                     
REMARK   3      L13:  -0.8609 L23:  -6.2095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2347 S12:  -0.2413 S13:   0.2167                       
REMARK   3      S21:   0.1330 S22:   0.0945 S23:   0.4931                       
REMARK   3      S31:  -0.0088 S32:   0.0726 S33:  -0.2332                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.1311 -28.0222  46.0494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8541 T22:   0.5493                                     
REMARK   3      T33:   0.4170 T12:  -0.0563                                     
REMARK   3      T13:   0.1570 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5874 L22:   3.9222                                     
REMARK   3      L33:   3.7258 L12:   1.0542                                     
REMARK   3      L13:   0.7431 L23:   0.7462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2400 S12:  -1.0418 S13:   0.0599                       
REMARK   3      S21:   1.4317 S22:  -0.2297 S23:   0.4963                       
REMARK   3      S31:   0.0991 S32:  -0.2396 S33:   0.0100                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 237 THROUGH 309 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6054 -34.2534  32.0287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4147 T22:   0.3342                                     
REMARK   3      T33:   0.3399 T12:  -0.0289                                     
REMARK   3      T13:   0.0643 T23:  -0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2398 L22:   4.6747                                     
REMARK   3      L33:   2.1821 L12:   1.2770                                     
REMARK   3      L13:  -0.5422 L23:  -0.3145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0347 S12:  -0.1786 S13:  -0.0429                       
REMARK   3      S21:   0.3791 S22:  -0.0333 S23:   0.0099                       
REMARK   3      S31:   0.0969 S32:  -0.0112 S33:  -0.0087                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 310 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0691 -22.0532  30.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4160 T22:   0.4592                                     
REMARK   3      T33:   0.6476 T12:  -0.0233                                     
REMARK   3      T13:   0.0811 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7480 L22:   5.2307                                     
REMARK   3      L33:   2.4340 L12:   3.3837                                     
REMARK   3      L13:  -1.3269 L23:  -1.7364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0981 S12:   0.3501 S13:   0.7513                       
REMARK   3      S21:   0.1546 S22:   0.4292 S23:   1.2301                       
REMARK   3      S31:   0.1514 S32:  -0.6421 S33:  -0.3095                       
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 6WLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248566.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
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 PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130237                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
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                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.14700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.87900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP                                      
REMARK 200 STARTING MODEL: PDBID 6W01                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16 %(W/V) PEG400, 100 MM TRIS PH 8.5,    
REMARK 280  200 MM SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.15200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.15200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.15200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33130 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 83110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       75.47850            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000     -130.73260            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      150.95700            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     VAL B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     SER B    -1                                                      
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     ASN A   0    CG   OD1  ND2                                       
REMARK 470     ASN B   0    CG   OD1  ND2                                       
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    MET A   1     -138.81     63.57                                   
REMARK 500    SER A   2      141.93   -170.70                                   
REMARK 500    SER A   2      113.89   -170.94                                   
REMARK 500    ASN A  29     -114.38     51.67                                   
REMARK 500    ASN A  29       52.96     34.41                                   
REMARK 500    LEU A 249       66.95     65.75                                   
REMARK 500    MET B   1     -137.53     65.15                                   
REMARK 500    ASN B  29     -118.89     48.34                                   
REMARK 500    LEU B 249       64.13     68.35                                   
REMARK 500    ASP B 297       78.32   -104.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue U5P A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue U5P B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6VWW   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN, APP FORM                                           
REMARK 900 RELATED ID: 6W01   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CITRATE                              
DBREF  6WLC A    2   347  UNP    P0DTD1   R1AB_SARS2    6453   6798             
DBREF  6WLC B    2   347  UNP    P0DTD1   R1AB_SARS2    6453   6798             
SEQADV 6WLC MET A  -22  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WLC HIS A  -21  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -20  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -19  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -18  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -17  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS A  -16  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A  -15  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A  -14  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY A  -13  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC VAL A  -12  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASP A  -11  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU A  -10  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY A   -9  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC THR A   -8  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLU A   -7  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN A   -6  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU A   -5  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC TYR A   -4  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC PHE A   -3  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLN A   -2  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER A   -1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN A    0  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET A    1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET B  -22  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WLC HIS B  -21  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -20  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -19  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -18  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -17  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC HIS B  -16  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B  -15  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B  -14  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY B  -13  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC VAL B  -12  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASP B  -11  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU B  -10  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLY B   -9  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC THR B   -8  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLU B   -7  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN B   -6  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC LEU B   -5  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC TYR B   -4  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC PHE B   -3  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC GLN B   -2  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC SER B   -1  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC ASN B    0  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WLC MET B    1  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  370  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  370  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET SER LEU          
SEQRES   3 A  370  GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS PHE          
SEQRES   4 A  370  ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE ASN          
SEQRES   5 A  370  ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL GLU          
SEQRES   6 A  370  LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL ALA          
SEQRES   7 A  370  PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL PRO          
SEQRES   8 A  370  GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE ALA          
SEQRES   9 A  370  ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA PRO          
SEQRES  10 A  370  ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR ASP          
SEQRES  11 A  370  ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO LEU          
SEQRES  12 A  370  THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL ASP          
SEQRES  13 A  370  LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR GLU          
SEQRES  14 A  370  GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO LYS          
SEQRES  15 A  370  GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU ALA          
SEQRES  16 A  370  VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP GLY          
SEQRES  17 A  370  VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN SER          
SEQRES  18 A  370  ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET GLU          
SEQRES  19 A  370  ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE GLU          
SEQRES  20 A  370  ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE VAL          
SEQRES  21 A  370  TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU HIS          
SEQRES  22 A  370  LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER PRO          
SEQRES  23 A  370  PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR VAL          
SEQRES  24 A  370  LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER SER          
SEQRES  25 A  370  LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP ASP          
SEQRES  26 A  370  PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL VAL          
SEQRES  27 A  370  SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU ILE          
SEQRES  28 A  370  SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU THR          
SEQRES  29 A  370  PHE TYR PRO LYS LEU GLN                                      
SEQRES   1 B  370  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  370  GLY THR GLU ASN LEU TYR PHE GLN SER ASN MET SER LEU          
SEQRES   3 B  370  GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS PHE          
SEQRES   4 B  370  ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE ASN          
SEQRES   5 B  370  ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL GLU          
SEQRES   6 B  370  LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL ALA          
SEQRES   7 B  370  PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL PRO          
SEQRES   8 B  370  GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE ALA          
SEQRES   9 B  370  ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA PRO          
SEQRES  10 B  370  ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR ASP          
SEQRES  11 B  370  ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO LEU          
SEQRES  12 B  370  THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL ASP          
SEQRES  13 B  370  LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR GLU          
SEQRES  14 B  370  GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO LYS          
SEQRES  15 B  370  GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU ALA          
SEQRES  16 B  370  VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP GLY          
SEQRES  17 B  370  VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN SER          
SEQRES  18 B  370  ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET GLU          
SEQRES  19 B  370  ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE GLU          
SEQRES  20 B  370  ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE VAL          
SEQRES  21 B  370  TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU HIS          
SEQRES  22 B  370  LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER PRO          
SEQRES  23 B  370  PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR VAL          
SEQRES  24 B  370  LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER SER          
SEQRES  25 B  370  LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP ASP          
SEQRES  26 B  370  PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL VAL          
SEQRES  27 B  370  SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU ILE          
SEQRES  28 B  370  SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU THR          
SEQRES  29 B  370  PHE TYR PRO LYS LEU GLN                                      
HET    U5P  A 401      21                                                       
HET    TRS  A 402       8                                                       
HET    EDO  A 403       4                                                       
HET    ACT  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    SO4  A 410       5                                                       
HET    U5P  B 401      21                                                       
HET    TRS  B 402       8                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    ACT  B 405       4                                                       
HET    EDO  B 406       4                                                       
HET    ACT  B 407       4                                                       
HET    ACT  B 408       4                                                       
HET    FMT  B 409       3                                                       
HET    FMT  B 410       3                                                       
HET    EDO  B 411       4                                                       
HETNAM     U5P URIDINE-5'-MONOPHOSPHATE                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FMT FORMIC ACID                                                      
HETSYN     TRS TRIS BUFFER                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  U5P    2(C9 H13 N2 O9 P)                                            
FORMUL   4  TRS    2(C4 H12 N O3 1+)                                            
FORMUL   5  EDO    10(C2 H6 O2)                                                 
FORMUL   6  ACT    4(C2 H3 O2 1-)                                               
FORMUL  12  SO4    O4 S 2-                                                      
FORMUL  21  FMT    2(C H2 O2)                                                   
FORMUL  24  HOH   *486(H2 O)                                                    
HELIX    1 AA1 SER A    2  GLY A   14  1                                  13    
HELIX    2 AA2 PRO A   51  LYS A   61  1                                  11    
HELIX    3 AA3 GLU A   69  LEU A   76  1                                   8    
HELIX    4 AA4 GLU A  114  ALA A  118  5                                   5    
HELIX    5 AA5 GLY A  130  ALA A  138  1                                   9    
HELIX    6 AA6 SER A  208  LEU A  217  1                                  10    
HELIX    7 AA7 ALA A  218  TYR A  226  1                                   9    
HELIX    8 AA8 ALA A  232  VAL A  237  1                                   6    
HELIX    9 AA9 LEU A  251  SER A  262  1                                  12    
HELIX   10 AB1 LEU A  299  LYS A  308  1                                  10    
HELIX   11 AB2 SER B    2  GLY B   14  1                                  13    
HELIX   12 AB3 PRO B   51  LYS B   61  1                                  11    
HELIX   13 AB4 GLU B   69  LEU B   76  1                                   8    
HELIX   14 AB5 GLU B  114  ALA B  118  5                                   5    
HELIX   15 AB6 GLY B  130  ALA B  138  1                                   9    
HELIX   16 AB7 SER B  208  LEU B  217  1                                  10    
HELIX   17 AB8 ALA B  218  TYR B  226  1                                   9    
HELIX   18 AB9 ALA B  232  VAL B  237  1                                   6    
HELIX   19 AC1 LEU B  251  SER B  262  1                                  12    
HELIX   20 AC2 LEU B  299  SER B  309  1                                  11    
SHEET    1 AA1 3 VAL A  25  ILE A  28  0                                        
SHEET    2 AA1 3 THR A  31  VAL A  36 -1  O  TYR A  33   N  SER A  26           
SHEET    3 AA1 3 VAL A  39  GLU A  45 -1  O  VAL A  39   N  VAL A  36           
SHEET    1 AA2 5 ILE A  80  ALA A  81  0                                        
SHEET    2 AA2 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80           
SHEET    3 AA2 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124           
SHEET    4 AA2 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145           
SHEET    5 AA2 5 SER A 155  VAL A 156 -1  N  SER A 155   O  TYR A 179           
SHEET    1 AA3 5 ILE A  80  ALA A  81  0                                        
SHEET    2 AA3 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80           
SHEET    3 AA3 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124           
SHEET    4 AA3 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145           
SHEET    5 AA3 5 VAL A 186  VAL A 187 -1  O  VAL A 186   N  VAL A 183           
SHEET    1 AA4 2 TRP A  87  ASP A  88  0                                        
SHEET    2 AA4 2 ALA A  93  PRO A  94 -1  O  ALA A  93   N  ASP A  88           
SHEET    1 AA5 2 THR A  99  ILE A 100  0                                        
SHEET    2 AA5 2 ASP A 107  ALA A 109  1  O  ILE A 108   N  THR A  99           
SHEET    1 AA6 2 ALA A 161  LEU A 163  0                                        
SHEET    2 AA6 2 VAL A 166  LEU A 168 -1  O  VAL A 166   N  LEU A 163           
SHEET    1 AA7 3 PHE A 264  GLU A 267  0                                        
SHEET    2 AA7 3 LYS A 277  ASP A 283 -1  O  THR A 282   N  GLU A 265           
SHEET    3 AA7 3 SER A 289  VAL A 295 -1  O  VAL A 295   N  LYS A 277           
SHEET    1 AA8 3 SER A 316  ILE A 323  0                                        
SHEET    2 AA8 3 THR A 326  LYS A 335 -1  O  PHE A 330   N  VAL A 319           
SHEET    3 AA8 3 HIS A 338  PRO A 344 -1  O  GLU A 340   N  TRP A 333           
SHEET    1 AA9 3 VAL B  25  ILE B  28  0                                        
SHEET    2 AA9 3 THR B  31  VAL B  36 -1  O  TYR B  33   N  SER B  26           
SHEET    3 AA9 3 VAL B  39  GLU B  45 -1  O  VAL B  39   N  VAL B  36           
SHEET    1 AB1 5 ILE B  80  ALA B  81  0                                        
SHEET    2 AB1 5 VAL B 122  ASP B 125  1  O  PHE B 123   N  ILE B  80           
SHEET    3 AB1 5 GLY B 141  THR B 145  1  O  VAL B 142   N  PHE B 124           
SHEET    4 AB1 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145           
SHEET    5 AB1 5 SER B 155  VAL B 156 -1  N  SER B 155   O  TYR B 179           
SHEET    1 AB2 5 ILE B  80  ALA B  81  0                                        
SHEET    2 AB2 5 VAL B 122  ASP B 125  1  O  PHE B 123   N  ILE B  80           
SHEET    3 AB2 5 GLY B 141  THR B 145  1  O  VAL B 142   N  PHE B 124           
SHEET    4 AB2 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145           
SHEET    5 AB2 5 VAL B 186  VAL B 187 -1  O  VAL B 186   N  VAL B 183           
SHEET    1 AB3 2 TRP B  87  ASP B  88  0                                        
SHEET    2 AB3 2 ALA B  93  PRO B  94 -1  O  ALA B  93   N  ASP B  88           
SHEET    1 AB4 2 THR B  99  ILE B 100  0                                        
SHEET    2 AB4 2 ASP B 107  ALA B 109  1  O  ILE B 108   N  THR B  99           
SHEET    1 AB5 2 ALA B 161  LEU B 163  0                                        
SHEET    2 AB5 2 VAL B 166  LEU B 168 -1  O  VAL B 166   N  LEU B 163           
SHEET    1 AB6 3 PHE B 264  GLU B 267  0                                        
SHEET    2 AB6 3 LYS B 277  ASP B 283 -1  O  THR B 282   N  GLU B 265           
SHEET    3 AB6 3 SER B 289  VAL B 295 -1  O  VAL B 295   N  LYS B 277           
SHEET    1 AB7 3 SER B 316  ILE B 323  0                                        
SHEET    2 AB7 3 THR B 326  LYS B 335 -1  O  PHE B 330   N  VAL B 319           
SHEET    3 AB7 3 HIS B 338  PRO B 344 -1  O  GLU B 340   N  TRP B 333           
SITE     1 AC1 10 HIS A 250  LYS A 290  VAL A 292  CYS A 293                    
SITE     2 AC1 10 SER A 294  TYR A 343  LEU A 346  HOH A 540                    
SITE     3 AC1 10 HOH A 646  HOH A 655                                          
SITE     1 AC2  5 PHE A  44  GLU A  45  ASP A  92  HOH A 509                    
SITE     2 AC2  5 HOH A 661                                                     
SITE     1 AC3  9 ASN A   0  ASN A  53  GLU A  57  CYS A 103                    
SITE     2 AC3  9 SER A 104  MET A 105  GLU B   4  PRO B  24                    
SITE     3 AC3  9 VAL B  25                                                     
SITE     1 AC4  2 GLU A 340  HOH A 646                                          
SITE     1 AC5  3 ASN A 200  LEU A 201  TYR A 279                               
SITE     1 AC6  5 ASN A  74  VAL A  78  ASP A  79  HOH A 511                    
SITE     2 AC6  5 HOH A 533                                                     
SITE     1 AC7  6 LEU A 312  SER A 313  VAL A 314  LYS A 335                    
SITE     2 AC7  6 ASP A 336  GLY A 337                                          
SITE     1 AC8  5 GLU A  69  VAL A  70  TYR A  89  LYS A  90                    
SITE     2 AC8  5 ASP A 273                                                     
SITE     1 AC9  4 ASN A  75  LEU A  76  LYS A 181  TYR A 325                    
SITE     1 AD1  7 GLU A 229  GLY A 230  TYR A 231  GLY A 337                    
SITE     2 AD1  7 HIS A 338  HOH A 513  HOH A 688                               
SITE     1 AD2  9 HIS B 250  LYS B 290  VAL B 292  CYS B 293                    
SITE     2 AD2  9 SER B 294  TYR B 343  LEU B 346  HOH B 592                    
SITE     3 AD2  9 HOH B 660                                                     
SITE     1 AD3  7 PHE B  44  GLU B  45  TRP B  59  ASP B  92                    
SITE     2 AD3  7 FMT B 410  EDO B 411  HOH B 543                               
SITE     1 AD4  8 LYS A 320  VAL A 321  THR A 322  GLU A 327                    
SITE     2 AD4  8 VAL B 149  LYS B 150  GLY B 151  HOH B 692                    
SITE     1 AD5  4 SER B 155  VAL B 156  GLU B 192  THR B 193                    
SITE     1 AD6  7 LEU B 312  SER B 313  VAL B 314  VAL B 315                    
SITE     2 AD6  7 LYS B 335  ASP B 336  GLY B 337                               
SITE     1 AD7  5 GLU B 192  LYS B 320  THR B 322  GLU B 327                    
SITE     2 AD7  5 HOH B 681                                                     
SITE     1 AD8  4 GLU B 146  LYS B 174  GLN B 176  ASN B 178                    
SITE     1 AD9  7 GLU A 192  GLY B 126  THR B 145  GLY B 147                    
SITE     2 AD9  7 SER B 148  VAL B 149  HOH B 571                               
SITE     1 AE1  2 GLU B  42  HOH B 643                                          
SITE     1 AE2  5 ASP B  92  TRS B 402  EDO B 411  HOH B 513                    
SITE     2 AE2  5 HOH B 537                                                     
SITE     1 AE3  3 GLU B  45  TRS B 402  FMT B 410                               
CRYST1  150.957  150.957  112.304  90.00  90.00 120.00 P 63         12          
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      0.006624  0.003825  0.000000        0.00000                         
SCALE2      0.000000  0.007649  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008904        0.00000                         
ATOM      1  N  AASN A   0      46.055 -31.384  -2.121  0.56 74.44           N  
ANISOU    1  N  AASN A   0     8134   9188  10962    308   1181    100       N  
ATOM      2  N  BASN A   0      54.569 -29.955   2.502  0.44 35.82           N  
ANISOU    2  N  BASN A   0     4303   4313   4995    -96   1093   -589       N  
ATOM      3  CA AASN A   0      47.039 -31.759  -1.112  0.56 67.29           C  
ANISOU    3  CA AASN A   0     7396   8303   9868    245   1204    -12       C  
ATOM      4  CA BASN A   0      53.212 -30.170   2.033  0.44 52.71           C  
ANISOU    4  CA BASN A   0     6315   6433   7280    -18   1156   -519       C  
ATOM      5  C  AASN A   0      48.291 -32.360  -1.756  0.56 67.28           C  
ANISOU    5  C  AASN A   0     7482   8338   9744    185   1024    -23       C  
ATOM      6  C  BASN A   0      53.191 -30.887   0.686  0.44 54.29           C  
ANISOU    6  C  BASN A   0     6406   6659   7564     15   1009   -410       C  
ATOM      7  O  AASN A   0      48.238 -33.389  -2.432  0.56 67.38           O  
ANISOU    7  O  AASN A   0     7454   8405   9742    143    897     47       O  
ATOM      8  O  BASN A   0      54.212 -31.399   0.232  0.44 64.76           O  
ANISOU    8  O  BASN A   0     7762   8021   8824    -22    872   -390       O  
ATOM      9  CB AASN A   0      46.429 -32.729  -0.114  0.56 70.09           C  
ANISOU    9  CB AASN A   0     7747   8717  10166    199   1280     -6       C  
ATOM     10  CB BASN A   0      52.469 -28.846   1.944  0.44 58.28           C  
ANISOU   10  CB BASN A   0     6992   7032   8121     56   1305   -560       C  
ATOM     11  N  AMET A   1      49.421 -31.700  -1.533  0.56 68.09           N  
ANISOU   11  N  AMET A   1     7705   8404   9761    178   1021   -112       N  
ATOM     12  N  BMET A   1      52.023 -30.895   0.054  0.44 56.96           N  
ANISOU   12  N  BMET A   1     6617   6975   8048     80   1042   -338       N  
ATOM     13  CA AMET A   1      50.680 -32.088  -2.148  0.56 62.19           C  
ANISOU   13  CA AMET A   1     7033   7680   8916    133    869   -122       C  
ATOM     14  CA BMET A   1      51.748 -31.651  -1.184  0.44 60.59           C  
ANISOU   14  CA BMET A   1     6973   7465   8584     97    912   -231       C  
ATOM     15  C  AMET A   1      51.289 -33.284  -1.414  0.56 56.82           C  
ANISOU   15  C  AMET A   1     6437   7070   8082     56    826   -142       C  
ATOM     16  C  BMET A   1      51.897 -33.140  -0.849  0.44 56.63           C  
ANISOU   16  C  BMET A   1     6490   7047   7979     32    843   -195       C  
ATOM     17  O  AMET A   1      51.129 -33.431  -0.199  0.56 52.07           O  
ANISOU   17  O  AMET A   1     5888   6489   7408     29    925   -188       O  
ATOM     18  O  BMET A   1      51.445 -33.568   0.224  0.44 56.40           O  
ANISOU   18  O  BMET A   1     6484   7051   7894      5    931   -212       O  
ATOM     19  CB AMET A   1      51.634 -30.891  -2.138  0.56 65.08           C  
ANISOU   19  CB AMET A   1     7485   7981   9262    150    887   -202       C  
ATOM     20  CB BMET A   1      52.607 -31.158  -2.333  0.44 61.53           C  
ANISOU   20  CB BMET A   1     7099   7551   8730    113    799   -220       C  
ATOM     21  CG AMET A   1      50.954 -29.565  -2.520  0.56 69.81           C  
ANISOU   21  CG AMET A   1     8015   8491  10017    234    979   -194       C  
ATOM     22  CG BMET A   1      51.850 -30.291  -3.332  0.44 60.57           C  
ANISOU   22  CG BMET A   1     6871   7368   8775    189    812   -163       C  
ATOM     23  SD AMET A   1      49.676 -29.003  -1.359  0.56 77.52           S  
ANISOU   23  SD AMET A   1     8954   9423  11075    283   1207   -226       S  
ATOM     24  SD BMET A   1      51.835 -30.959  -5.011  0.44 47.05           S  
ANISOU   24  SD BMET A   1     5077   5689   7112    186    636    -50       S  
ATOM     25  CE AMET A   1      48.431 -28.358  -2.475  0.56 74.36           C  
ANISOU   25  CE AMET A   1     8367   8971  10917    386   1223   -101       C  
ATOM     26  CE BMET A   1      51.275 -32.652  -4.721  0.44 47.37           C  
ANISOU   26  CE BMET A   1     5086   5818   7093    126    593      0       C  
ATOM     27  N  ASER A   2      51.995 -34.142  -2.161  0.56 53.15           N  
ANISOU   27  N  ASER A   2     5987   6638   7569     20    684   -102       N  
ATOM     28  N  BSER A   2      52.508 -33.944  -1.723  0.44 50.90           N  
ANISOU   28  N  BSER A   2     5760   6351   7228      8    699   -145       N  
ATOM     29  CA ASER A   2      52.458 -35.411  -1.604  0.56 44.26           C  
ANISOU   29  CA ASER A   2     4919   5571   6327    -44    639    -94       C  
ATOM     30  CA BSER A   2      52.481 -35.395  -1.563  0.44 44.76           C  
ANISOU   30  CA BSER A   2     4986   5635   6387    -44    641    -96       C  
ATOM     31  C  ASER A   2      53.423 -36.103  -2.562  0.56 39.48           C  
ANISOU   31  C  ASER A   2     4340   4976   5687    -67    497    -61       C  
ATOM     32  C  BSER A   2      53.418 -36.102  -2.538  0.44 39.67           C  
ANISOU   32  C  BSER A   2     4364   4999   5709    -67    499    -62       C  
ATOM     33  O  ASER A   2      53.215 -36.079  -3.778  0.56 38.20           O  
ANISOU   33  O  ASER A   2     4121   4793   5599    -49    428    -16       O  
ATOM     34  O  BSER A   2      53.199 -36.076  -3.754  0.44 38.82           O  
ANISOU   34  O  BSER A   2     4200   4873   5679    -48    431    -17       O  
ATOM     35  CB ASER A   2      51.264 -36.327  -1.310  0.56 47.20           C  
ANISOU   35  CB ASER A   2     5218   5980   6734    -60    679    -34       C  
ATOM     36  CB BSER A   2      51.052 -35.918  -1.745  0.44 46.86           C  
ANISOU   36  CB BSER A   2     5139   5917   6748    -35    676    -25       C  
ATOM     37  OG ASER A   2      51.162 -37.403  -2.232  0.56 39.65           O  
ANISOU   37  OG ASER A   2     4222   5045   5798    -89    568     38       O  
ATOM     38  OG BSER A   2      51.008 -37.334  -1.717  0.44 37.98           O  
ANISOU   38  OG BSER A   2     4019   4840   5573    -90    616     24       O  
ATOM     39  N   LEU A   3      54.462 -36.740  -2.004  1.00 37.05           N  
ANISOU   39  N   LEU A   3     4116   4697   5264   -110    458    -78       N  
ATOM     40  CA  LEU A   3      55.374 -37.537  -2.825  1.00 35.67           C  
ANISOU   40  CA  LEU A   3     3965   4525   5063   -127    346    -42       C  
ATOM     41  C   LEU A   3      54.622 -38.550  -3.680  1.00 33.26           C  
ANISOU   41  C   LEU A   3     3603   4222   4813   -140    300     26       C  
ATOM     42  O   LEU A   3      54.862 -38.670  -4.887  1.00 33.34           O  
ANISOU   42  O   LEU A   3     3601   4208   4858   -136    225     50       O  
ATOM     43  CB  LEU A   3      56.382 -38.270  -1.929  1.00 34.34           C  
ANISOU   43  CB  LEU A   3     3873   4394   4779   -169    323    -44       C  
ATOM     44  CG  LEU A   3      57.263 -39.309  -2.638  1.00 37.94           C  
ANISOU   44  CG  LEU A   3     4349   4846   5219   -182    231      5       C  
ATOM     45  CD1 LEU A   3      58.127 -38.620  -3.695  1.00 36.85           C  
ANISOU   45  CD1 LEU A   3     4216   4670   5114   -154    175    -12       C  
ATOM     46  CD2 LEU A   3      58.130 -40.084  -1.638  1.00 40.22           C  
ANISOU   46  CD2 LEU A   3     4695   5175   5412   -217    215     27       C  
ATOM     47  N   GLU A   4      53.709 -39.297  -3.058  1.00 31.64           N  
ANISOU   47  N   GLU A   4     3368   4046   4608   -166    345     56       N  
ATOM     48  CA  GLU A   4      52.988 -40.342  -3.775  1.00 35.93           C  
ANISOU   48  CA  GLU A   4     3864   4592   5195   -197    300    119       C  
ATOM     49  C   GLU A   4      52.071 -39.767  -4.847  1.00 35.48           C  
ANISOU   49  C   GLU A   4     3716   4520   5246   -178    276    148       C  
ATOM     50  O   GLU A   4      51.850 -40.420  -5.873  1.00 34.06           O  
ANISOU   50  O   GLU A   4     3518   4334   5090   -212    199    190       O  
ATOM     51  CB  GLU A   4      52.193 -41.193  -2.783  1.00 36.43           C  
ANISOU   51  CB  GLU A   4     3912   4691   5240   -233    362    148       C  
ATOM     52  CG  GLU A   4      53.080 -42.141  -1.959  1.00 42.78           C  
ANISOU   52  CG  GLU A   4     4803   5512   5939   -266    354    153       C  
ATOM     53  CD  GLU A   4      53.818 -41.472  -0.783  1.00 47.35           C  
ANISOU   53  CD  GLU A   4     5446   6116   6429   -256    404    102       C  
ATOM     54  OE1 GLU A   4      53.762 -40.234  -0.624  1.00 41.75           O  
ANISOU   54  OE1 GLU A   4     4731   5397   5734   -224    450     48       O  
ATOM     55  OE2 GLU A   4      54.452 -42.208   0.002  1.00 47.42           O  
ANISOU   55  OE2 GLU A   4     5517   6151   6351   -288    396    122       O  
ATOM     56  N   ASN A   5      51.526 -38.558  -4.630  1.00 31.68           N  
ANISOU   56  N   ASN A   5     3180   4028   4829   -128    342    130       N  
ATOM     57  CA  ASN A   5      50.717 -37.919  -5.662  1.00 32.74           C  
ANISOU   57  CA  ASN A   5     3217   4147   5075   -102    312    176       C  
ATOM     58  C   ASN A   5      51.575 -37.422  -6.823  1.00 32.06           C  
ANISOU   58  C   ASN A   5     3167   4030   4985    -88    224    169       C  
ATOM     59  O   ASN A   5      51.153 -37.491  -7.985  1.00 34.23           O  
ANISOU   59  O   ASN A   5     3392   4306   5309   -104    146    224       O  
ATOM     60  CB  ASN A   5      49.913 -36.764  -5.069  1.00 35.95           C  
ANISOU   60  CB  ASN A   5     3552   4537   5568    -41    424    167       C  
ATOM     61  CG  ASN A   5      49.142 -35.994  -6.131  1.00 44.92           C  
ANISOU   61  CG  ASN A   5     4577   5654   6834     -3    391    231       C  
ATOM     62  OD1 ASN A   5      49.483 -34.849  -6.459  1.00 37.20           O  
ANISOU   62  OD1 ASN A   5     3604   4633   5898     52    404    211       O  
ATOM     63  ND2 ASN A   5      48.124 -36.636  -6.706  1.00 37.28           N  
ANISOU   63  ND2 ASN A   5     3511   4721   5932    -38    340    317       N  
ATOM     64  N   VAL A   6      52.766 -36.882  -6.534  1.00 34.26           N  
ANISOU   64  N   VAL A   6     3530   4286   5203    -66    234    106       N  
ATOM     65  CA  VAL A   6      53.684 -36.525  -7.613  1.00 35.44           C  
ANISOU   65  CA  VAL A   6     3719   4406   5340    -59    156    101       C  
ATOM     66  C   VAL A   6      53.999 -37.752  -8.463  1.00 34.18           C  
ANISOU   66  C   VAL A   6     3595   4257   5136   -113     68    134       C  
ATOM     67  O   VAL A   6      53.968 -37.700  -9.701  1.00 34.59           O  
ANISOU   67  O   VAL A   6     3637   4296   5208   -126     -2    165       O  
ATOM     68  CB  VAL A   6      54.970 -35.882  -7.052  1.00 35.31           C  
ANISOU   68  CB  VAL A   6     3784   4370   5264    -40    181     32       C  
ATOM     69  CG1 VAL A   6      55.959 -35.624  -8.176  1.00 36.35           C  
ANISOU   69  CG1 VAL A   6     3953   4473   5384    -36    106     34       C  
ATOM     70  CG2 VAL A   6      54.636 -34.569  -6.334  1.00 35.98           C  
ANISOU   70  CG2 VAL A   6     3849   4427   5393      5    274    -11       C  
ATOM     71  N   ALA A   7      54.303 -38.883  -7.809  1.00 34.28           N  
ANISOU   71  N   ALA A   7     3655   4287   5083   -150     77    127       N  
ATOM     72  CA  ALA A   7      54.602 -40.101  -8.558  1.00 30.11           C  
ANISOU   72  CA  ALA A   7     3171   3750   4518   -200     15    152       C  
ATOM     73  C   ALA A   7      53.401 -40.556  -9.373  1.00 29.42           C  
ANISOU   73  C   ALA A   7     3023   3674   4479   -247    -30    204       C  
ATOM     74  O   ALA A   7      53.549 -41.029 -10.506  1.00 35.45           O  
ANISOU   74  O   ALA A   7     3821   4423   5227   -289    -97    220       O  
ATOM     75  CB  ALA A   7      55.050 -41.208  -7.601  1.00 31.60           C  
ANISOU   75  CB  ALA A   7     3413   3948   4645   -224     43    148       C  
ATOM     76  N   PHE A   8      52.200 -40.429  -8.816  1.00 30.40           N  
ANISOU   76  N   PHE A   8     3061   3830   4662   -248      9    234       N  
ATOM     77  CA  PHE A   8      51.019 -40.826  -9.571  1.00 32.43           C  
ANISOU   77  CA  PHE A   8     3243   4108   4973   -301    -43    298       C  
ATOM     78  C   PHE A   8      50.912 -40.032 -10.869  1.00 38.79           C  
ANISOU   78  C   PHE A   8     4016   4906   5814   -296   -118    327       C  
ATOM     79  O   PHE A   8      50.595 -40.588 -11.932  1.00 35.11           O  
ANISOU   79  O   PHE A   8     3556   4448   5336   -366   -204    364       O  
ATOM     80  CB  PHE A   8      49.763 -40.634  -8.711  1.00 34.65           C  
ANISOU   80  CB  PHE A   8     3413   4423   5330   -289     24    333       C  
ATOM     81  CG  PHE A   8      48.489 -40.856  -9.462  1.00 35.87           C  
ANISOU   81  CG  PHE A   8     3460   4607   5560   -341    -35    414       C  
ATOM     82  CD1 PHE A   8      47.889 -39.817 -10.158  1.00 36.73           C  
ANISOU   82  CD1 PHE A   8     3473   4725   5759   -308    -67    466       C  
ATOM     83  CD2 PHE A   8      47.879 -42.104  -9.473  1.00 38.42           C  
ANISOU   83  CD2 PHE A   8     3775   4950   5871   -429    -62    447       C  
ATOM     84  CE1 PHE A   8      46.715 -40.019 -10.858  1.00 42.41           C  
ANISOU   84  CE1 PHE A   8     4080   5483   6550   -363   -137    557       C  
ATOM     85  CE2 PHE A   8      46.706 -42.306 -10.170  1.00 41.07           C  
ANISOU   85  CE2 PHE A   8     4007   5322   6276   -492   -129    527       C  
ATOM     86  CZ  PHE A   8      46.125 -41.263 -10.867  1.00 47.02           C  
ANISOU   86  CZ  PHE A   8     4656   6095   7116   -460   -172    586       C  
ATOM     87  N   ASN A   9      51.149 -38.720 -10.799  1.00 33.97           N  
ANISOU   87  N   ASN A   9     3379   4280   5246   -220    -88    314       N  
ATOM     88  CA  ASN A   9      51.067 -37.901 -12.002  1.00 35.31           C  
ANISOU   88  CA  ASN A   9     3519   4443   5454   -210   -156    354       C  
ATOM     89  C   ASN A   9      52.138 -38.283 -13.015  1.00 35.87           C  
ANISOU   89  C   ASN A   9     3701   4491   5438   -248   -224    328       C  
ATOM     90  O   ASN A   9      51.866 -38.333 -14.222  1.00 40.21           O  
ANISOU   90  O   ASN A   9     4248   5050   5980   -296   -310    374       O  
ATOM     91  CB  ASN A   9      51.183 -36.417 -11.639  1.00 35.31           C  
ANISOU   91  CB  ASN A   9     3478   4415   5522   -118    -94    341       C  
ATOM     92  CG  ASN A   9      49.862 -35.832 -11.191  1.00 40.20           C  
ANISOU   92  CG  ASN A   9     3962   5049   6263    -79    -40    398       C  
ATOM     93  OD1 ASN A   9      49.196 -35.122 -11.945  1.00 40.87           O  
ANISOU   93  OD1 ASN A   9     3957   5135   6436    -59    -80    473       O  
ATOM     94  ND2 ASN A   9      49.464 -36.143  -9.956  1.00 37.62           N  
ANISOU   94  ND2 ASN A   9     3617   4733   5945    -69     54    370       N  
ATOM     95  N   VAL A  10      53.364 -38.534 -12.552  1.00 34.05           N  
ANISOU   95  N   VAL A  10     3567   4232   5140   -229   -186    261       N  
ATOM     96  CA  VAL A  10      54.431 -38.903 -13.480  1.00 32.57           C  
ANISOU   96  CA  VAL A  10     3480   4016   4880   -255   -228    238       C  
ATOM     97  C   VAL A  10      54.057 -40.185 -14.219  1.00 36.45           C  
ANISOU   97  C   VAL A  10     4014   4512   5326   -347   -283    257       C  
ATOM     98  O   VAL A  10      54.163 -40.267 -15.447  1.00 36.10           O  
ANISOU   98  O   VAL A  10     4012   4458   5244   -395   -345    272       O  
ATOM     99  CB  VAL A  10      55.769 -39.041 -12.733  1.00 37.31           C  
ANISOU   99  CB  VAL A  10     4156   4589   5432   -218   -174    177       C  
ATOM    100  CG1 VAL A  10      56.812 -39.704 -13.642  1.00 35.48           C  
ANISOU  100  CG1 VAL A  10     4022   4322   5136   -247   -200    160       C  
ATOM    101  CG2 VAL A  10      56.263 -37.650 -12.267  1.00 35.51           C  
ANISOU  101  CG2 VAL A  10     3905   4350   5236   -147   -135    151       C  
ATOM    102  N   VAL A  11      53.565 -41.186 -13.481  1.00 35.38           N  
ANISOU  102  N   VAL A  11     3870   4387   5187   -382   -257    259       N  
ATOM    103  CA  VAL A  11      53.239 -42.485 -14.074  1.00 35.23           C  
ANISOU  103  CA  VAL A  11     3902   4359   5124   -478   -298    269       C  
ATOM    104  C   VAL A  11      52.069 -42.377 -15.045  1.00 41.77           C  
ANISOU  104  C   VAL A  11     4669   5225   5975   -552   -385    329       C  
ATOM    105  O   VAL A  11      52.033 -43.069 -16.071  1.00 47.42           O  
ANISOU  105  O   VAL A  11     5455   5929   6633   -643   -444    330       O  
ATOM    106  CB  VAL A  11      52.947 -43.508 -12.956  1.00 40.46           C  
ANISOU  106  CB  VAL A  11     4562   5022   5788   -496   -244    265       C  
ATOM    107  CG1 VAL A  11      52.262 -44.745 -13.511  1.00 48.74           C  
ANISOU  107  CG1 VAL A  11     5641   6064   6815   -607   -286    285       C  
ATOM    108  CG2 VAL A  11      54.232 -43.887 -12.252  1.00 41.39           C  
ANISOU  108  CG2 VAL A  11     4761   5101   5865   -447   -182    220       C  
ATOM    109  N   ASN A  12      51.084 -41.533 -14.739  1.00 38.94           N  
ANISOU  109  N   ASN A  12     4180   4912   5703   -520   -393    384       N  
ATOM    110  CA  ASN A  12      49.855 -41.519 -15.519  1.00 39.62           C  
ANISOU  110  CA  ASN A  12     4180   5046   5827   -594   -483    464       C  
ATOM    111  C   ASN A  12      49.788 -40.388 -16.534  1.00 46.98           C  
ANISOU  111  C   ASN A  12     5075   5994   6781   -575   -551    513       C  
ATOM    112  O   ASN A  12      49.037 -40.494 -17.511  1.00 43.68           O  
ANISOU  112  O   ASN A  12     4622   5617   6359   -660   -654    581       O  
ATOM    113  CB  ASN A  12      48.643 -41.427 -14.589  1.00 45.49           C  
ANISOU  113  CB  ASN A  12     4780   5832   6672   -578   -447    518       C  
ATOM    114  CG  ASN A  12      48.374 -42.732 -13.869  1.00 52.04           C  
ANISOU  114  CG  ASN A  12     5637   6659   7478   -638   -411    498       C  
ATOM    115  OD1 ASN A  12      47.753 -43.632 -14.426  1.00 53.82           O  
ANISOU  115  OD1 ASN A  12     5867   6901   7683   -750   -478    529       O  
ATOM    116  ND2 ASN A  12      48.858 -42.848 -12.633  1.00 40.04           N  
ANISOU  116  ND2 ASN A  12     4141   5118   5954   -573   -307    449       N  
ATOM    117  N   LYS A  13      50.545 -39.317 -16.335  1.00 41.06           N  
ANISOU  117  N   LYS A  13     4332   5216   6052   -474   -503    487       N  
ATOM    118  CA  LYS A  13      50.421 -38.149 -17.188  1.00 39.29           C  
ANISOU  118  CA  LYS A  13     4060   5001   5866   -444   -557    545       C  
ATOM    119  C   LYS A  13      51.743 -37.717 -17.803  1.00 40.51           C  
ANISOU  119  C   LYS A  13     4332   5112   5950   -418   -552    493       C  
ATOM    120  O   LYS A  13      51.748 -36.795 -18.634  1.00 41.21           O  
ANISOU  120  O   LYS A  13     4399   5203   6055   -402   -600    544       O  
ATOM    121  CB  LYS A  13      49.808 -36.983 -16.397  1.00 38.31           C  
ANISOU  121  CB  LYS A  13     3802   4880   5875   -341   -495    586       C  
ATOM    122  CG  LYS A  13      48.319 -37.176 -16.067  1.00 49.13           C  
ANISOU  122  CG  LYS A  13     5024   6301   7344   -364   -510    671       C  
ATOM    123  CD  LYS A  13      47.475 -37.185 -17.338  1.00 58.14           C  
ANISOU  123  CD  LYS A  13     6098   7496   8498   -448   -648    783       C  
ATOM    124  CE  LYS A  13      46.000 -36.962 -17.037  1.00 62.77           C  
ANISOU  124  CE  LYS A  13     6495   8132   9223   -441   -660    896       C  
ATOM    125  NZ  LYS A  13      45.133 -37.009 -18.263  1.00 62.27           N  
ANISOU  125  NZ  LYS A  13     6353   8135   9172   -537   -814   1023       N  
ATOM    126  N   GLY A  14      52.859 -38.355 -17.427  1.00 37.15           N  
ANISOU  126  N   GLY A  14     4018   4644   5451   -411   -493    405       N  
ATOM    127  CA  GLY A  14      54.166 -38.032 -17.951  1.00 35.38           C  
ANISOU  127  CA  GLY A  14     3897   4378   5167   -386   -476    358       C  
ATOM    128  C   GLY A  14      54.880 -36.905 -17.231  1.00 41.44           C  
ANISOU  128  C   GLY A  14     4641   5117   5986   -281   -407    328       C  
ATOM    129  O   GLY A  14      56.073 -36.680 -17.490  1.00 41.41           O  
ANISOU  129  O   GLY A  14     4716   5078   5940   -258   -382    286       O  
ATOM    130  N   HIS A  15      54.196 -36.205 -16.332  1.00 38.36           N  
ANISOU  130  N   HIS A  15     4151   4738   5687   -223   -367    347       N  
ATOM    131  CA  HIS A  15      54.724 -35.054 -15.602  1.00 36.08           C  
ANISOU  131  CA  HIS A  15     3843   4416   5449   -135   -296    314       C  
ATOM    132  C   HIS A  15      53.656 -34.666 -14.583  1.00 38.43           C  
ANISOU  132  C   HIS A  15     4034   4728   5839    -93   -242    333       C  
ATOM    133  O   HIS A  15      52.595 -35.291 -14.516  1.00 37.53           O  
ANISOU  133  O   HIS A  15     3856   4652   5751   -130   -264    379       O  
ATOM    134  CB  HIS A  15      55.048 -33.890 -16.543  1.00 38.02           C  
ANISOU  134  CB  HIS A  15     4087   4637   5720   -105   -327    347       C  
ATOM    135  CG  HIS A  15      53.833 -33.230 -17.114  1.00 36.89           C  
ANISOU  135  CG  HIS A  15     3838   4515   5663    -99   -377    446       C  
ATOM    136  ND1 HIS A  15      53.581 -31.883 -16.966  1.00 39.72           N  
ANISOU  136  ND1 HIS A  15     4127   4841   6125    -22   -340    479       N  
ATOM    137  CD2 HIS A  15      52.776 -33.738 -17.795  1.00 42.06           C  
ANISOU  137  CD2 HIS A  15     4437   5220   6325   -162   -460    527       C  
ATOM    138  CE1 HIS A  15      52.430 -31.584 -17.544  1.00 42.54           C  
ANISOU  138  CE1 HIS A  15     4380   5226   6557    -27   -398    586       C  
ATOM    139  NE2 HIS A  15      51.921 -32.691 -18.054  1.00 42.40           N  
ANISOU  139  NE2 HIS A  15     4365   5266   6479   -116   -479    619       N  
ATOM    140  N   PHE A  16      53.928 -33.629 -13.792  1.00 36.03           N  
ANISOU  140  N   PHE A  16     3715   4390   5586    -20   -162    297       N  
ATOM    141  CA  PHE A  16      52.928 -33.188 -12.825  1.00 37.17           C  
ANISOU  141  CA  PHE A  16     3767   4535   5819     24    -86    308       C  
ATOM    142  C   PHE A  16      51.824 -32.427 -13.542  1.00 37.55           C  
ANISOU  142  C   PHE A  16     3700   4585   5983     52   -117    408       C  
ATOM    143  O   PHE A  16      52.083 -31.395 -14.174  1.00 41.26           O  
ANISOU  143  O   PHE A  16     4164   5018   6497     91   -131    435       O  
ATOM    144  CB  PHE A  16      53.508 -32.313 -11.715  1.00 35.36           C  
ANISOU  144  CB  PHE A  16     3571   4262   5603     83     20    230       C  
ATOM    145  CG  PHE A  16      52.504 -32.042 -10.624  1.00 35.74           C  
ANISOU  145  CG  PHE A  16     3547   4310   5725    120    120    227       C  
ATOM    146  CD1 PHE A  16      52.185 -33.038  -9.709  1.00 40.08           C  
ANISOU  146  CD1 PHE A  16     4102   4900   6228     86    156    204       C  
ATOM    147  CD2 PHE A  16      51.824 -30.830 -10.556  1.00 40.38           C  
ANISOU  147  CD2 PHE A  16     4057   4851   6435    190    187    256       C  
ATOM    148  CE1 PHE A  16      51.231 -32.816  -8.714  1.00 44.95           C  
ANISOU  148  CE1 PHE A  16     4653   5517   6909    117    261    203       C  
ATOM    149  CE2 PHE A  16      50.875 -30.596  -9.568  1.00 44.71           C  
ANISOU  149  CE2 PHE A  16     4538   5392   7059    228    300    253       C  
ATOM    150  CZ  PHE A  16      50.573 -31.594  -8.645  1.00 45.87           C  
ANISOU  150  CZ  PHE A  16     4695   5585   7149    189    338    225       C  
ATOM    151  N   ASP A  17      50.585 -32.915 -13.395  1.00 39.28           N  
ANISOU  151  N   ASP A  17     3818   4846   6260     32   -126    473       N  
ATOM    152  CA  ASP A  17      49.420 -32.365 -14.079  1.00 41.36           C  
ANISOU  152  CA  ASP A  17     3947   5126   6642     50   -170    593       C  
ATOM    153  C   ASP A  17      48.285 -32.037 -13.110  1.00 45.55           C  
ANISOU  153  C   ASP A  17     4352   5654   7300    107    -67    625       C  
ATOM    154  O   ASP A  17      47.150 -31.828 -13.548  1.00 44.23           O  
ANISOU  154  O   ASP A  17     4045   5514   7245    114   -103    741       O  
ATOM    155  CB  ASP A  17      48.947 -33.363 -15.150  1.00 51.58           C  
ANISOU  155  CB  ASP A  17     5226   6486   7885    -54   -309    667       C  
ATOM    156  CG  ASP A  17      47.928 -32.773 -16.117  1.00 71.53           C  
ANISOU  156  CG  ASP A  17     7622   9042  10513    -54   -395    809       C  
ATOM    157  OD1 ASP A  17      47.975 -31.553 -16.381  1.00 73.93           O  
ANISOU  157  OD1 ASP A  17     7886   9304  10902     23   -374    852       O  
ATOM    158  OD2 ASP A  17      47.068 -33.542 -16.602  1.00 70.87           O  
ANISOU  158  OD2 ASP A  17     7474   9024  10429   -137   -486    886       O  
ATOM    159  N   GLY A  18      48.544 -32.018 -11.802  1.00 41.97           N  
ANISOU  159  N   GLY A  18     3942   5174   6832    142     60    531       N  
ATOM    160  CA  GLY A  18      47.502 -31.676 -10.851  1.00 45.44           C  
ANISOU  160  CA  GLY A  18     4275   5604   7387    197    182    552       C  
ATOM    161  C   GLY A  18      46.403 -32.705 -10.677  1.00 45.67           C  
ANISOU  161  C   GLY A  18     4207   5700   7443    144    161    617       C  
ATOM    162  O   GLY A  18      45.335 -32.368 -10.164  1.00 51.48           O  
ANISOU  162  O   GLY A  18     4818   6434   8307    192    249    671       O  
ATOM    163  N   GLN A  19      46.625 -33.957 -11.077  1.00 38.89           N  
ANISOU  163  N   GLN A  19     3404   4896   6477     46     58    614       N  
ATOM    164  CA  GLN A  19      45.594 -34.983 -10.961  1.00 40.38           C  
ANISOU  164  CA  GLN A  19     3507   5147   6690    -21     30    677       C  
ATOM    165  C   GLN A  19      45.630 -35.612  -9.572  1.00 44.78           C  
ANISOU  165  C   GLN A  19     4110   5706   7200    -24    148    601       C  
ATOM    166  O   GLN A  19      46.685 -35.694  -8.938  1.00 41.22           O  
ANISOU  166  O   GLN A  19     3791   5228   6644    -16    196    496       O  
ATOM    167  CB  GLN A  19      45.791 -36.062 -12.029  1.00 48.50           C  
ANISOU  167  CB  GLN A  19     4588   6220   7622   -136   -126    704       C  
ATOM    168  CG  GLN A  19      45.763 -35.527 -13.451  1.00 59.32           C  
ANISOU  168  CG  GLN A  19     5928   7599   9011   -153   -253    783       C  
ATOM    169  CD  GLN A  19      44.427 -34.895 -13.798  1.00 70.72           C  
ANISOU  169  CD  GLN A  19     7179   9073  10617   -126   -277    925       C  
ATOM    170  OE1 GLN A  19      43.371 -35.418 -13.440  1.00 76.04           O  
ANISOU  170  OE1 GLN A  19     7738   9792  11361   -158   -267    987       O  
ATOM    171  NE2 GLN A  19      44.467 -33.761 -14.488  1.00 72.74           N  
ANISOU  171  NE2 GLN A  19     7391   9304  10942    -65   -307    986       N  
ATOM    172  N   GLN A  20      44.464 -36.056  -9.105  1.00 41.03           N  
ANISOU  172  N   GLN A  20     3518   5269   6804    -41    192    662       N  
ATOM    173  CA  GLN A  20      44.369 -36.755  -7.827  1.00 40.25           C  
ANISOU  173  CA  GLN A  20     3455   5180   6657    -57    300    606       C  
ATOM    174  C   GLN A  20      44.754 -38.220  -7.991  1.00 44.24           C  
ANISOU  174  C   GLN A  20     4048   5719   7040   -165    212    588       C  
ATOM    175  O   GLN A  20      44.413 -38.855  -8.990  1.00 46.20           O  
ANISOU  175  O   GLN A  20     4265   6000   7289   -243     86    652       O  
ATOM    176  CB  GLN A  20      42.953 -36.665  -7.264  1.00 45.46           C  
ANISOU  176  CB  GLN A  20     3951   5864   7459    -33    395    685       C  
ATOM    177  CG  GLN A  20      42.520 -35.260  -6.884  1.00 64.28           C  
ANISOU  177  CG  GLN A  20     6249   8196   9978     86    526    696       C  
ATOM    178  CD  GLN A  20      41.058 -35.189  -6.483  1.00 88.22           C  
ANISOU  178  CD  GLN A  20     9095  11250  13173    114    620    795       C  
ATOM    179  OE1 GLN A  20      40.288 -34.414  -7.048  1.00103.20           O  
ANISOU  179  OE1 GLN A  20    10840  13139  15232    171    615    899       O  
ATOM    180  NE2 GLN A  20      40.671 -35.996  -5.498  1.00 89.57           N  
ANISOU  180  NE2 GLN A  20     9271  11451  13312     76    708    772       N  
ATOM    181  N   GLY A  21      45.438 -38.761  -6.995  1.00 40.90           N  
ANISOU  181  N   GLY A  21     3739   5288   6513   -174    280    506       N  
ATOM    182  CA  GLY A  21      45.796 -40.169  -6.999  1.00 38.00           C  
ANISOU  182  CA  GLY A  21     3455   4939   6044   -265    221    493       C  
ATOM    183  C   GLY A  21      47.096 -40.391  -6.259  1.00 39.31           C  
ANISOU  183  C   GLY A  21     3774   5080   6083   -252    260    400       C  
ATOM    184  O   GLY A  21      47.810 -39.458  -5.912  1.00 36.49           O  
ANISOU  184  O   GLY A  21     3465   4695   5704   -187    308    341       O  
ATOM    185  N   GLU A  22      47.400 -41.662  -6.006  1.00 36.68           N  
ANISOU  185  N   GLU A  22     3512   4755   5670   -319    237    393       N  
ATOM    186  CA  GLU A  22      48.668 -41.997  -5.351  1.00 35.20           C  
ANISOU  186  CA  GLU A  22     3458   4549   5367   -311    258    327       C  
ATOM    187  C   GLU A  22      49.160 -43.342  -5.867  1.00 40.52           C  
ANISOU  187  C   GLU A  22     4209   5208   5978   -383    180    338       C  
ATOM    188  O   GLU A  22      48.358 -44.200  -6.234  1.00 37.49           O  
ANISOU  188  O   GLU A  22     3784   4835   5625   -452    146    388       O  
ATOM    189  CB  GLU A  22      48.514 -42.065  -3.818  1.00 41.34           C  
ANISOU  189  CB  GLU A  22     4251   5348   6109   -297    378    305       C  
ATOM    190  CG  GLU A  22      48.437 -40.729  -3.097  1.00 58.07           C  
ANISOU  190  CG  GLU A  22     6351   7462   8251   -225    480    260       C  
ATOM    191  CD  GLU A  22      47.011 -40.298  -2.805  1.00 77.21           C  
ANISOU  191  CD  GLU A  22     8645   9901  10790   -203    571    303       C  
ATOM    192  OE1 GLU A  22      46.111 -41.165  -2.822  1.00 80.80           O  
ANISOU  192  OE1 GLU A  22     9030  10384  11287   -253    566    366       O  
ATOM    193  OE2 GLU A  22      46.793 -39.092  -2.552  1.00 79.04           O  
ANISOU  193  OE2 GLU A  22     8841  10110  11079   -135    653    275       O  
ATOM    194  N   VAL A  23      50.479 -43.521  -5.875  1.00 34.68           N  
ANISOU  194  N   VAL A  23     3578   4440   5158   -369    158    295       N  
ATOM    195  CA  VAL A  23      51.083 -44.830  -6.127  1.00 32.35           C  
ANISOU  195  CA  VAL A  23     3369   4117   4807   -422    118    302       C  
ATOM    196  C   VAL A  23      52.117 -45.104  -5.044  1.00 39.10           C  
ANISOU  196  C   VAL A  23     4302   4970   5585   -395    164    279       C  
ATOM    197  O   VAL A  23      52.623 -44.172  -4.398  1.00 36.35           O  
ANISOU  197  O   VAL A  23     3963   4638   5210   -342    200    243       O  
ATOM    198  CB  VAL A  23      51.725 -44.908  -7.536  1.00 31.21           C  
ANISOU  198  CB  VAL A  23     3276   3932   4652   -437     32    290       C  
ATOM    199  CG1 VAL A  23      50.662 -44.772  -8.625  1.00 38.36           C  
ANISOU  199  CG1 VAL A  23     4109   4850   5616   -487    -31    326       C  
ATOM    200  CG2 VAL A  23      52.818 -43.875  -7.702  1.00 34.52           C  
ANISOU  200  CG2 VAL A  23     3730   4337   5047   -368     28    246       C  
ATOM    201  N   PRO A  24      52.456 -46.378  -4.817  1.00 39.87           N  
ANISOU  201  N   PRO A  24     4459   5044   5645   -435    160    304       N  
ATOM    202  CA  PRO A  24      53.468 -46.688  -3.803  1.00 34.60           C  
ANISOU  202  CA  PRO A  24     3858   4380   4908   -411    190    304       C  
ATOM    203  C   PRO A  24      54.845 -46.315  -4.311  1.00 34.62           C  
ANISOU  203  C   PRO A  24     3916   4354   4883   -368    149    276       C  
ATOM    204  O   PRO A  24      55.178 -46.568  -5.472  1.00 36.67           O  
ANISOU  204  O   PRO A  24     4201   4566   5165   -376    103    270       O  
ATOM    205  CB  PRO A  24      53.344 -48.207  -3.615  1.00 39.10           C  
ANISOU  205  CB  PRO A  24     4467   4920   5470   -465    197    355       C  
ATOM    206  CG  PRO A  24      52.028 -48.594  -4.302  1.00 41.67           C  
ANISOU  206  CG  PRO A  24     4735   5240   5858   -527    183    373       C  
ATOM    207  CD  PRO A  24      51.884 -47.605  -5.407  1.00 36.88           C  
ANISOU  207  CD  PRO A  24     4089   4634   5289   -509    132    341       C  
ATOM    208  N   VAL A  25      55.644 -45.713  -3.432  1.00 35.17           N  
ANISOU  208  N   VAL A  25     4008   4454   4902   -332    167    260       N  
ATOM    209  CA  VAL A  25      56.951 -45.166  -3.802  1.00 30.88           C  
ANISOU  209  CA  VAL A  25     3499   3893   4339   -292    130    235       C  
ATOM    210  C   VAL A  25      58.014 -45.696  -2.851  1.00 30.56           C  
ANISOU  210  C   VAL A  25     3505   3869   4239   -287    130    271       C  
ATOM    211  O   VAL A  25      57.785 -45.778  -1.640  1.00 34.85           O  
ANISOU  211  O   VAL A  25     4052   4461   4730   -305    164    288       O  
ATOM    212  CB  VAL A  25      56.925 -43.620  -3.765  1.00 35.73           C  
ANISOU  212  CB  VAL A  25     4085   4533   4959   -259    139    179       C  
ATOM    213  CG1 VAL A  25      58.325 -43.053  -3.925  1.00 34.69           C  
ANISOU  213  CG1 VAL A  25     3988   4392   4801   -228    104    159       C  
ATOM    214  CG2 VAL A  25      55.983 -43.081  -4.837  1.00 33.99           C  
ANISOU  214  CG2 VAL A  25     3810   4294   4811   -256    126    165       C  
ATOM    215  N   SER A  26      59.199 -46.017  -3.399  1.00 30.96           N  
ANISOU  215  N   SER A  26     3586   3881   4296   -264     93    288       N  
ATOM    216  CA  SER A  26      60.388 -46.346  -2.624  1.00 31.97           C  
ANISOU  216  CA  SER A  26     3739   4027   4383   -250     78    336       C  
ATOM    217  C   SER A  26      61.473 -45.336  -2.956  1.00 29.18           C  
ANISOU  217  C   SER A  26     3381   3680   4027   -217     43    304       C  
ATOM    218  O   SER A  26      61.684 -45.009  -4.125  1.00 32.32           O  
ANISOU  218  O   SER A  26     3777   4032   4472   -196     30    274       O  
ATOM    219  CB  SER A  26      60.930 -47.754  -2.940  1.00 34.28           C  
ANISOU  219  CB  SER A  26     4060   4258   4708   -244     78    405       C  
ATOM    220  OG  SER A  26      60.037 -48.747  -2.520  1.00 47.86           O  
ANISOU  220  OG  SER A  26     5789   5969   6428   -281    110    442       O  
ATOM    221  N   ILE A  27      62.185 -44.870  -1.939  1.00 29.19           N  
ANISOU  221  N   ILE A  27     3384   3738   3967   -223     25    316       N  
ATOM    222  CA  ILE A  27      63.363 -44.026  -2.145  1.00 27.93           C  
ANISOU  222  CA  ILE A  27     3218   3588   3806   -204    -15    301       C  
ATOM    223  C   ILE A  27      64.587 -44.772  -1.634  1.00 29.42           C  
ANISOU  223  C   ILE A  27     3404   3792   3983   -198    -52    392       C  
ATOM    224  O   ILE A  27      64.637 -45.159  -0.458  1.00 32.90           O  
ANISOU  224  O   ILE A  27     3854   4289   4359   -229    -62    443       O  
ATOM    225  CB  ILE A  27      63.218 -42.671  -1.440  1.00 34.16           C  
ANISOU  225  CB  ILE A  27     4011   4432   4537   -228    -12    234       C  
ATOM    226  CG1 ILE A  27      62.035 -41.893  -2.064  1.00 38.05           C  
ANISOU  226  CG1 ILE A  27     4490   4897   5070   -218     31    159       C  
ATOM    227  CG2 ILE A  27      64.515 -41.885  -1.518  1.00 34.40           C  
ANISOU  227  CG2 ILE A  27     4035   4475   4560   -224    -61    227       C  
ATOM    228  CD1 ILE A  27      61.817 -40.559  -1.451  1.00 47.16           C  
ANISOU  228  CD1 ILE A  27     5653   6080   6185   -233     57     87       C  
ATOM    229  N  AILE A  28      65.575 -44.991  -2.481  0.46 33.10           N  
ANISOU  229  N  AILE A  28     3855   4210   4512   -158    -69    422       N  
ATOM    230  N  BILE A  28      65.577 -44.939  -2.531  0.54 31.28           N  
ANISOU  230  N  BILE A  28     3624   3978   4283   -157    -69    418       N  
ATOM    231  CA AILE A  28      66.759 -45.657  -1.951  0.46 28.88           C  
ANISOU  231  CA AILE A  28     3299   3691   3983   -145   -103    524       C  
ATOM    232  CA BILE A  28      66.863 -45.597  -2.275  0.54 30.52           C  
ANISOU  232  CA BILE A  28     3504   3882   4210   -135    -99    516       C  
ATOM    233  C  AILE A  28      67.975 -44.951  -2.520  0.46 28.97           C  
ANISOU  233  C  AILE A  28     3276   3698   4035   -119   -135    524       C  
ATOM    234  C  BILE A  28      67.903 -45.014  -3.231  0.54 29.44           C  
ANISOU  234  C  BILE A  28     3341   3713   4133    -98   -113    503       C  
ATOM    235  O  AILE A  28      68.089 -44.790  -3.739  0.46 32.39           O  
ANISOU  235  O  AILE A  28     3711   4064   4531    -85   -108    485       O  
ATOM    236  O  BILE A  28      67.582 -44.649  -4.364  0.54 29.21           O  
ANISOU  236  O  BILE A  28     3326   3628   4143    -80    -84    438       O  
ATOM    237  CB AILE A  28      66.764 -47.176  -2.226  0.46 32.42           C  
ANISOU  237  CB AILE A  28     3755   4070   4491   -115    -68    604       C  
ATOM    238  CB BILE A  28      66.826 -47.134  -2.483  0.54 33.61           C  
ANISOU  238  CB BILE A  28     3906   4207   4657   -107    -64    596       C  
ATOM    239  CG1AILE A  28      67.996 -47.846  -1.617  0.46 38.04           C  
ANISOU  239  CG1AILE A  28     4431   4798   5226    -92   -100    731       C  
ATOM    240  CG1BILE A  28      65.506 -47.758  -2.055  0.54 29.25           C  
ANISOU  240  CG1BILE A  28     3388   3655   4072   -142    -29    585       C  
ATOM    241  CG2AILE A  28      66.662 -47.476  -3.683  0.46 37.29           C  
ANISOU  241  CG2AILE A  28     4392   4588   5188    -80    -22    564       C  
ATOM    242  CG2BILE A  28      68.000 -47.807  -1.762  0.54 37.83           C  
ANISOU  242  CG2BILE A  28     4405   4763   5206    -88    -97    723       C  
ATOM    243  CD1AILE A  28      67.843 -49.349  -1.473  0.46 44.40           C  
ANISOU  243  CD1AILE A  28     5251   5543   6077    -71    -61    822       C  
ATOM    244  CD1BILE A  28      65.396 -49.237  -2.429  0.54 33.29           C  
ANISOU  244  CD1BILE A  28     3922   4080   4648   -122     16    649       C  
ATOM    245  N  AASN A  29      68.851 -44.489  -1.630  0.46 30.28           N  
ANISOU  245  N  AASN A  29     3412   3938   4154   -147   -195    566       N  
ATOM    246  N  BASN A  29      69.174 -45.005  -2.790  0.54 32.41           N  
ANISOU  246  N  BASN A  29     3673   4124   4519    -90   -158    580       N  
ATOM    247  CA AASN A  29      69.893 -43.529  -1.972  0.46 37.38           C  
ANISOU  247  CA AASN A  29     4276   4852   5074   -145   -234    553       C  
ATOM    248  CA BASN A  29      70.347 -44.521  -3.532  0.54 34.96           C  
ANISOU  248  CA BASN A  29     3954   4424   4905    -58   -171    593       C  
ATOM    249  C  AASN A  29      69.266 -42.340  -2.686  0.46 34.84           C  
ANISOU  249  C  AASN A  29     3981   4506   4750   -152   -208    429       C  
ATOM    250  C  BASN A  29      70.097 -43.332  -4.449  0.54 35.29           C  
ANISOU  250  C  BASN A  29     4012   4444   4952    -60   -158    485       C  
ATOM    251  O  AASN A  29      68.445 -41.626  -2.098  0.46 33.60           O  
ANISOU  251  O  AASN A  29     3857   4385   4523   -194   -202    357       O  
ATOM    252  O  BASN A  29      70.450 -43.393  -5.639  0.54 27.33           O  
ANISOU  252  O  BASN A  29     3003   3366   4013    -19   -121    474       O  
ATOM    253  CB AASN A  29      70.980 -44.203  -2.807  0.46 36.03           C  
ANISOU  253  CB AASN A  29     4057   4621   5011    -82   -223    633       C  
ATOM    254  CB BASN A  29      70.971 -45.613  -4.412  0.54 44.63           C  
ANISOU  254  CB BASN A  29     5165   5558   6235      9   -119    661       C  
ATOM    255  CG AASN A  29      71.639 -45.344  -2.064  0.46 37.76           C  
ANISOU  255  CG AASN A  29     4237   4860   5251    -67   -246    773       C  
ATOM    256  CG BASN A  29      70.548 -46.994  -4.029  0.54 44.35           C  
ANISOU  256  CG BASN A  29     5150   5487   6214     23    -86    729       C  
ATOM    257  OD1AASN A  29      71.903 -45.237  -0.866  0.46 44.72           O  
ANISOU  257  OD1AASN A  29     5101   5831   6058   -117   -314    829       O  
ATOM    258  OD1BASN A  29      71.044 -47.550  -3.054  0.54 38.90           O  
ANISOU  258  OD1BASN A  29     4424   4839   5518     22   -121    835       O  
ATOM    259  ND2AASN A  29      71.890 -46.453  -2.761  0.46 38.42           N  
ANISOU  259  ND2AASN A  29     4312   4854   5433      0   -188    834       N  
ATOM    260  ND2BASN A  29      69.649 -47.579  -4.813  0.54 50.53           N  
ANISOU  260  ND2BASN A  29     5992   6190   7016     30    -22    676       N  
ATOM    261  N  AASN A  30      69.599 -42.152  -3.961  0.46 34.86           N  
ANISOU  261  N  AASN A  30     3973   4442   4830   -108   -183    407       N  
ATOM    262  N  BASN A  30      69.515 -42.254  -3.916  0.54 33.57           N  
ANISOU  262  N  BASN A  30     3812   4278   4664   -108   -181    409       N  
ATOM    263  CA AASN A  30      69.211 -40.963  -4.709  0.46 37.80           C  
ANISOU  263  CA AASN A  30     4362   4792   5210   -111   -169    311       C  
ATOM    264  CA BASN A  30      69.242 -41.034  -4.675  0.54 37.62           C  
ANISOU  264  CA BASN A  30     4338   4769   5186   -110   -170    316       C  
ATOM    265  C  AASN A  30      68.267 -41.280  -5.866  0.46 34.91           C  
ANISOU  265  C  AASN A  30     4026   4354   4883    -81   -118    269       C  
ATOM    266  C  BASN A  30      68.272 -41.280  -5.830  0.54 35.06           C  
ANISOU  266  C  BASN A  30     4045   4375   4901    -81   -118    270       C  
ATOM    267  O  AASN A  30      68.219 -40.545  -6.851  0.46 34.95           O  
ANISOU  267  O  AASN A  30     4037   4323   4918    -68   -106    221       O  
ATOM    268  O  BASN A  30      68.215 -40.495  -6.777  0.54 35.09           O  
ANISOU  268  O  BASN A  30     4054   4345   4933    -70   -108    220       O  
ATOM    269  CB AASN A  30      70.451 -40.233  -5.223  0.46 43.54           C  
ANISOU  269  CB AASN A  30     5052   5513   5979   -102   -193    320       C  
ATOM    270  CB BASN A  30      70.542 -40.404  -5.201  0.54 41.78           C  
ANISOU  270  CB BASN A  30     4825   5289   5760    -98   -194    334       C  
ATOM    271  CG AASN A  30      70.541 -38.809  -4.706  0.46 38.89           C  
ANISOU  271  CG AASN A  30     4468   4967   5342   -152   -226    255       C  
ATOM    272  CG BASN A  30      70.751 -38.974  -4.710  0.54 39.95           C  
ANISOU  272  CG BASN A  30     4593   5102   5483   -148   -230    274       C  
ATOM    273  OD1AASN A  30      69.622 -38.316  -4.055  0.46 35.83           O  
ANISOU  273  OD1AASN A  30     4117   4603   4893   -187   -216    194       O  
ATOM    274  OD1BASN A  30      69.838 -38.336  -4.190  0.54 34.47           O  
ANISOU  274  OD1BASN A  30     3937   4427   4732   -182   -220    203       O  
ATOM    275  ND2AASN A  30      71.637 -38.143  -5.007  0.46 37.35           N  
ANISOU  275  ND2AASN A  30     4237   4774   5179   -159   -254    268       N  
ATOM    276  ND2BASN A  30      71.956 -38.468  -4.890  0.54 43.30           N  
ANISOU  276  ND2BASN A  30     4975   5537   5940   -156   -264    303       N  
ATOM    277  N   THR A  31      67.494 -42.359  -5.765  1.00 32.82           N  
ANISOU  277  N   THR A  31     3782   4071   4616    -79    -91    292       N  
ATOM    278  CA  THR A  31      66.610 -42.768  -6.847  1.00 33.17           C  
ANISOU  278  CA  THR A  31     3858   4054   4691    -69    -54    260       C  
ATOM    279  C   THR A  31      65.201 -42.970  -6.304  1.00 35.83           C  
ANISOU  279  C   THR A  31     4207   4414   4992   -100    -42    236       C  
ATOM    280  O   THR A  31      65.024 -43.446  -5.178  1.00 32.38           O  
ANISOU  280  O   THR A  31     3767   4018   4516   -119    -44    270       O  
ATOM    281  CB  THR A  31      67.131 -44.065  -7.499  1.00 40.06           C  
ANISOU  281  CB  THR A  31     4749   4858   5612    -40    -21    314       C  
ATOM    282  OG1 THR A  31      68.464 -43.838  -7.981  1.00 42.33           O  
ANISOU  282  OG1 THR A  31     5015   5125   5944     -5    -18    342       O  
ATOM    283  CG2 THR A  31      66.233 -44.515  -8.662  1.00 40.00           C  
ANISOU  283  CG2 THR A  31     4791   4787   5620    -51     13    274       C  
ATOM    284  N   VAL A  32      64.200 -42.602  -7.103  1.00 31.59           N  
ANISOU  284  N   VAL A  32     3678   3854   4470   -108    -31    187       N  
ATOM    285  CA  VAL A  32      62.799 -42.801  -6.753  1.00 28.00           C  
ANISOU  285  CA  VAL A  32     3219   3418   4003   -136    -15    172       C  
ATOM    286  C   VAL A  32      62.258 -43.961  -7.580  1.00 31.42           C  
ANISOU  286  C   VAL A  32     3679   3797   4461   -152     -3    191       C  
ATOM    287  O   VAL A  32      62.404 -43.977  -8.812  1.00 31.84           O  
ANISOU  287  O   VAL A  32     3756   3803   4538   -150     -7    176       O  
ATOM    288  CB  VAL A  32      61.976 -41.526  -7.005  1.00 31.89           C  
ANISOU  288  CB  VAL A  32     3685   3925   4506   -136    -15    117       C  
ATOM    289  CG1 VAL A  32      60.514 -41.764  -6.635  1.00 30.56           C  
ANISOU  289  CG1 VAL A  32     3494   3776   4341   -161      9    115       C  
ATOM    290  CG2 VAL A  32      62.542 -40.358  -6.210  1.00 32.62           C  
ANISOU  290  CG2 VAL A  32     3768   4054   4572   -129    -17     86       C  
ATOM    291  N   TYR A  33      61.617 -44.921  -6.911  1.00 30.16           N  
ANISOU  291  N   TYR A  33     3524   3645   4290   -178     16    223       N  
ATOM    292  CA  TYR A  33      60.992 -46.061  -7.566  1.00 28.62           C  
ANISOU  292  CA  TYR A  33     3361   3398   4115   -210     30    237       C  
ATOM    293  C   TYR A  33      59.505 -46.072  -7.264  1.00 32.49           C  
ANISOU  293  C   TYR A  33     3819   3921   4604   -254     33    229       C  
ATOM    294  O   TYR A  33      59.056 -45.552  -6.238  1.00 35.09           O  
ANISOU  294  O   TYR A  33     4111   4308   4914   -252     46    228       O  
ATOM    295  CB  TYR A  33      61.580 -47.398  -7.081  1.00 30.45           C  
ANISOU  295  CB  TYR A  33     3626   3592   4352   -206     57    297       C  
ATOM    296  CG  TYR A  33      63.053 -47.534  -7.302  1.00 34.06           C  
ANISOU  296  CG  TYR A  33     4097   4013   4829   -158     63    325       C  
ATOM    297  CD1 TYR A  33      63.947 -47.013  -6.390  1.00 37.96           C  
ANISOU  297  CD1 TYR A  33     4556   4562   5306   -127     42    356       C  
ATOM    298  CD2 TYR A  33      63.554 -48.202  -8.414  1.00 33.23           C  
ANISOU  298  CD2 TYR A  33     4042   3821   4763   -147     94    323       C  
ATOM    299  CE1 TYR A  33      65.279 -47.131  -6.582  1.00 32.58           C  
ANISOU  299  CE1 TYR A  33     3868   3854   4657    -84     43    396       C  
ATOM    300  CE2 TYR A  33      64.918 -48.323  -8.615  1.00 39.02           C  
ANISOU  300  CE2 TYR A  33     4776   4518   5530    -94    114    357       C  
ATOM    301  CZ  TYR A  33      65.772 -47.779  -7.690  1.00 44.82           C  
ANISOU  301  CZ  TYR A  33     5455   5314   6259    -61     84    399       C  
ATOM    302  OH  TYR A  33      67.130 -47.870  -7.843  1.00 48.53           O  
ANISOU  302  OH  TYR A  33     5906   5759   6776    -10     98    447       O  
ATOM    303  N   THR A  34      58.751 -46.719  -8.146  1.00 30.24           N  
ANISOU  303  N   THR A  34     3554   3598   4339   -299     27    227       N  
ATOM    304  CA  THR A  34      57.364 -47.041  -7.854  1.00 27.87           C  
ANISOU  304  CA  THR A  34     3217   3323   4050   -350     31    239       C  
ATOM    305  C   THR A  34      57.121 -48.521  -8.111  1.00 32.45           C  
ANISOU  305  C   THR A  34     3849   3844   4635   -404     46    265       C  
ATOM    306  O   THR A  34      57.784 -49.148  -8.939  1.00 35.21           O  
ANISOU  306  O   THR A  34     4268   4124   4987   -410     50    258       O  
ATOM    307  CB  THR A  34      56.403 -46.181  -8.678  1.00 31.90           C  
ANISOU  307  CB  THR A  34     3677   3857   4586   -371     -5    216       C  
ATOM    308  OG1 THR A  34      55.072 -46.367  -8.182  1.00 35.81           O  
ANISOU  308  OG1 THR A  34     4112   4390   5104   -412      6    240       O  
ATOM    309  CG2 THR A  34      56.440 -46.577 -10.146  1.00 32.94           C  
ANISOU  309  CG2 THR A  34     3861   3938   4718   -414    -42    204       C  
ATOM    310  N   LYS A  35      56.172 -49.082  -7.378  1.00 32.69           N  
ANISOU  310  N   LYS A  35     3852   3899   4672   -445     65    295       N  
ATOM    311  CA  LYS A  35      55.895 -50.509  -7.454  1.00 34.07           C  
ANISOU  311  CA  LYS A  35     4076   4014   4856   -502     86    324       C  
ATOM    312  C   LYS A  35      54.829 -50.728  -8.516  1.00 45.75           C  
ANISOU  312  C   LYS A  35     5553   5478   6354   -586     50    306       C  
ATOM    313  O   LYS A  35      53.744 -50.140  -8.436  1.00 40.08           O  
ANISOU  313  O   LYS A  35     4753   4822   5655   -612     26    311       O  
ATOM    314  CB  LYS A  35      55.444 -51.050  -6.098  1.00 41.44           C  
ANISOU  314  CB  LYS A  35     4983   4980   5783   -512    127    374       C  
ATOM    315  CG  LYS A  35      55.131 -52.555  -6.099  1.00 49.52           C  
ANISOU  315  CG  LYS A  35     6058   5933   6824   -574    155    412       C  
ATOM    316  CD  LYS A  35      54.650 -53.046  -4.736  1.00 59.58           C  
ANISOU  316  CD  LYS A  35     7305   7245   8089   -587    197    470       C  
ATOM    317  CE  LYS A  35      55.809 -53.359  -3.818  1.00 64.86           C  
ANISOU  317  CE  LYS A  35     8008   7907   8730   -526    222    520       C  
ATOM    318  NZ  LYS A  35      55.353 -54.051  -2.580  1.00 73.53           N  
ANISOU  318  NZ  LYS A  35     9097   9030   9810   -552    262    588       N  
ATOM    319  N   VAL A  36      55.153 -51.538  -9.525  1.00 41.58           N  
ANISOU  319  N   VAL A  36     5112   4866   5820   -630     47    287       N  
ATOM    320  CA  VAL A  36      54.237 -51.880 -10.612  1.00 41.62           C  
ANISOU  320  CA  VAL A  36     5137   4853   5824   -733      3    268       C  
ATOM    321  C   VAL A  36      54.134 -53.399 -10.647  1.00 52.45           C  
ANISOU  321  C   VAL A  36     6594   6135   7200   -805     42    277       C  
ATOM    322  O   VAL A  36      55.103 -54.086 -11.001  1.00 38.86           O  
ANISOU  322  O   VAL A  36     4973   4320   5472   -787     89    260       O  
ATOM    323  CB  VAL A  36      54.707 -51.326 -11.964  1.00 42.96           C  
ANISOU  323  CB  VAL A  36     5357   5001   5965   -739    -37    221       C  
ATOM    324  CG1 VAL A  36      53.716 -51.670 -13.054  1.00 49.33           C  
ANISOU  324  CG1 VAL A  36     6188   5803   6754   -863    -97    208       C  
ATOM    325  CG2 VAL A  36      54.924 -49.812 -11.887  1.00 40.91           C  
ANISOU  325  CG2 VAL A  36     5019   4817   5710   -660    -67    216       C  
ATOM    326  N   ASP A  37      52.971 -53.922 -10.255  1.00 44.80           N  
ANISOU  326  N   ASP A  37     5582   5189   6252   -884     34    308       N  
ATOM    327  CA  ASP A  37      52.694 -55.358 -10.260  1.00 52.44           C  
ANISOU  327  CA  ASP A  37     6626   6071   7230   -969     70    320       C  
ATOM    328  C   ASP A  37      53.786 -56.147  -9.542  1.00 54.65           C  
ANISOU  328  C   ASP A  37     6973   6270   7522   -897    153    345       C  
ATOM    329  O   ASP A  37      54.331 -57.127 -10.056  1.00 53.08           O  
ANISOU  329  O   ASP A  37     6887   5955   7328   -921    199    327       O  
ATOM    330  CB  ASP A  37      52.487 -55.865 -11.686  1.00 68.47           C  
ANISOU  330  CB  ASP A  37     8753   8032   9231  -1079     36    267       C  
ATOM    331  CG  ASP A  37      51.228 -55.302 -12.322  1.00 83.31           C  
ANISOU  331  CG  ASP A  37    10554   9996  11103  -1176    -60    269       C  
ATOM    332  OD1 ASP A  37      51.339 -54.545 -13.310  1.00 89.21           O  
ANISOU  332  OD1 ASP A  37    11309  10771  11816  -1184   -119    237       O  
ATOM    333  OD2 ASP A  37      50.126 -55.598 -11.812  1.00 89.73           O  
ANISOU  333  OD2 ASP A  37    11289  10852  11951  -1243    -76    313       O  
ATOM    334  N   GLY A  38      54.107 -55.706  -8.333  1.00 47.52           N  
ANISOU  334  N   GLY A  38     6002   5429   6624   -809    174    390       N  
ATOM    335  CA  GLY A  38      55.000 -56.439  -7.471  1.00 43.94           C  
ANISOU  335  CA  GLY A  38     5588   4923   6185   -747    238    442       C  
ATOM    336  C   GLY A  38      56.486 -56.176  -7.656  1.00 41.56           C  
ANISOU  336  C   GLY A  38     5325   4584   5883   -647    258    437       C  
ATOM    337  O   GLY A  38      57.283 -56.727  -6.890  1.00 52.12           O  
ANISOU  337  O   GLY A  38     6677   5886   7239   -588    302    498       O  
ATOM    338  N   VAL A  39      56.896 -55.371  -8.643  1.00 40.17           N  
ANISOU  338  N   VAL A  39     5159   4413   5689   -627    227    377       N  
ATOM    339  CA  VAL A  39      58.312 -55.048  -8.815  1.00 40.15           C  
ANISOU  339  CA  VAL A  39     5179   4382   5694   -532    249    377       C  
ATOM    340  C   VAL A  39      58.498 -53.538  -8.872  1.00 39.61           C  
ANISOU  340  C   VAL A  39     5039   4413   5596   -485    194    347       C  
ATOM    341  O   VAL A  39      57.593 -52.784  -9.237  1.00 38.84           O  
ANISOU  341  O   VAL A  39     4900   4379   5480   -528    143    311       O  
ATOM    342  CB  VAL A  39      58.940 -55.696 -10.073  1.00 46.41           C  
ANISOU  342  CB  VAL A  39     6082   5050   6502   -546    295    333       C  
ATOM    343  CG1 VAL A  39      58.843 -57.220  -9.992  1.00 53.11           C  
ANISOU  343  CG1 VAL A  39     7014   5777   7390   -589    367    360       C  
ATOM    344  CG2 VAL A  39      58.306 -55.156 -11.343  1.00 43.20           C  
ANISOU  344  CG2 VAL A  39     5704   4657   6053   -622    246    255       C  
ATOM    345  N   ASP A  40      59.719 -53.113  -8.538  1.00 34.30           N  
ANISOU  345  N   ASP A  40     4352   3750   4931   -397    204    369       N  
ATOM    346  CA  ASP A  40      60.081 -51.699  -8.494  1.00 33.76           C  
ANISOU  346  CA  ASP A  40     4224   3764   4839   -350    160    344       C  
ATOM    347  C   ASP A  40      60.579 -51.221  -9.849  1.00 33.14           C  
ANISOU  347  C   ASP A  40     4185   3645   4760   -342    154    288       C  
ATOM    348  O   ASP A  40      61.404 -51.877 -10.486  1.00 35.78           O  
ANISOU  348  O   ASP A  40     4588   3890   5119   -324    203    287       O  
ATOM    349  CB  ASP A  40      61.152 -51.473  -7.430  1.00 34.09           C  
ANISOU  349  CB  ASP A  40     4228   3843   4883   -276    165    400       C  
ATOM    350  CG  ASP A  40      60.631 -51.766  -6.026  1.00 47.53           C  
ANISOU  350  CG  ASP A  40     5893   5604   6562   -290    165    455       C  
ATOM    351  OD1 ASP A  40      59.428 -51.496  -5.781  1.00 46.17           O  
ANISOU  351  OD1 ASP A  40     5692   5481   6368   -340    153    431       O  
ATOM    352  OD2 ASP A  40      61.408 -52.264  -5.183  1.00 48.49           O  
ANISOU  352  OD2 ASP A  40     6011   5724   6688   -254    179    528       O  
ATOM    353  N   VAL A  41      60.073 -50.071 -10.279  1.00 30.41           N  
ANISOU  353  N   VAL A  41     3800   3363   4392   -355    103    246       N  
ATOM    354  CA  VAL A  41      60.438 -49.445 -11.543  1.00 29.08           C  
ANISOU  354  CA  VAL A  41     3663   3173   4212   -354     88    199       C  
ATOM    355  C   VAL A  41      60.989 -48.067 -11.216  1.00 29.83           C  
ANISOU  355  C   VAL A  41     3693   3336   4305   -292     59    194       C  
ATOM    356  O   VAL A  41      60.354 -47.304 -10.480  1.00 32.99           O  
ANISOU  356  O   VAL A  41     4024   3811   4699   -288     29    197       O  
ATOM    357  CB  VAL A  41      59.224 -49.346 -12.490  1.00 32.02           C  
ANISOU  357  CB  VAL A  41     4051   3555   4560   -442     42    165       C  
ATOM    358  CG1 VAL A  41      59.629 -48.702 -13.816  1.00 34.67           C  
ANISOU  358  CG1 VAL A  41     4430   3873   4871   -447     24    125       C  
ATOM    359  CG2 VAL A  41      58.589 -50.746 -12.696  1.00 36.71           C  
ANISOU  359  CG2 VAL A  41     4711   4084   5153   -524     66    167       C  
ATOM    360  N   GLU A  42      62.166 -47.750 -11.754  1.00 30.50           N  
ANISOU  360  N   GLU A  42     3802   3389   4399   -245     78    186       N  
ATOM    361  CA  GLU A  42      62.783 -46.454 -11.501  1.00 30.63           C  
ANISOU  361  CA  GLU A  42     3763   3461   4416   -194     52    180       C  
ATOM    362  C   GLU A  42      62.038 -45.331 -12.212  1.00 37.97           C  
ANISOU  362  C   GLU A  42     4670   4426   5329   -218      6    142       C  
ATOM    363  O   GLU A  42      61.815 -45.381 -13.425  1.00 36.03           O  
ANISOU  363  O   GLU A  42     4474   4148   5070   -254     -2    118       O  
ATOM    364  CB  GLU A  42      64.253 -46.476 -11.946  1.00 31.55           C  
ANISOU  364  CB  GLU A  42     3902   3529   4556   -142     89    191       C  
ATOM    365  CG  GLU A  42      64.892 -45.095 -11.975  1.00 33.54           C  
ANISOU  365  CG  GLU A  42     4107   3827   4809   -106     60    178       C  
ATOM    366  CD  GLU A  42      66.359 -45.138 -12.389  1.00 49.18           C  
ANISOU  366  CD  GLU A  42     6097   5766   6825    -57    100    199       C  
ATOM    367  OE1 GLU A  42      67.050 -46.129 -12.065  1.00 42.11           O  
ANISOU  367  OE1 GLU A  42     5208   4827   5963    -29    144    246       O  
ATOM    368  OE2 GLU A  42      66.811 -44.187 -13.054  1.00 49.98           O  
ANISOU  368  OE2 GLU A  42     6192   5872   6927    -45     92    176       O  
ATOM    369  N   LEU A  43      61.678 -44.296 -11.456  1.00 32.05           N  
ANISOU  369  N   LEU A  43     3852   3743   4581   -199    -21    138       N  
ATOM    370  CA  LEU A  43      61.025 -43.125 -12.026  1.00 31.45           C  
ANISOU  370  CA  LEU A  43     3743   3698   4511   -206    -58    115       C  
ATOM    371  C   LEU A  43      61.953 -41.928 -12.172  1.00 33.65           C  
ANISOU  371  C   LEU A  43     4006   3983   4798   -160    -62     99       C  
ATOM    372  O   LEU A  43      61.717 -41.071 -13.038  1.00 35.97           O  
ANISOU  372  O   LEU A  43     4294   4276   5098   -162    -87     87       O  
ATOM    373  CB  LEU A  43      59.843 -42.704 -11.153  1.00 33.96           C  
ANISOU  373  CB  LEU A  43     3993   4070   4840   -216    -67    120       C  
ATOM    374  CG  LEU A  43      58.669 -43.645 -11.051  1.00 39.85           C  
ANISOU  374  CG  LEU A  43     4732   4821   5588   -270    -70    140       C  
ATOM    375  CD1 LEU A  43      57.579 -42.930 -10.285  1.00 42.03           C  
ANISOU  375  CD1 LEU A  43     4926   5152   5890   -266    -66    145       C  
ATOM    376  CD2 LEU A  43      58.223 -44.066 -12.451  1.00 40.35           C  
ANISOU  376  CD2 LEU A  43     4835   4852   5644   -328   -105    139       C  
ATOM    377  N   PHE A  44      62.978 -41.819 -11.328  1.00 29.06           N  
ANISOU  377  N   PHE A  44     3413   3411   4216   -124    -45    107       N  
ATOM    378  CA  PHE A  44      63.790 -40.603 -11.318  1.00 28.96           C  
ANISOU  378  CA  PHE A  44     3379   3410   4214    -92    -53     91       C  
ATOM    379  C   PHE A  44      65.085 -40.872 -10.577  1.00 32.01           C  
ANISOU  379  C   PHE A  44     3760   3803   4600    -68    -42    116       C  
ATOM    380  O   PHE A  44      65.056 -41.426  -9.477  1.00 36.00           O  
ANISOU  380  O   PHE A  44     4253   4338   5088    -74    -39    139       O  
ATOM    381  CB  PHE A  44      63.018 -39.459 -10.644  1.00 30.85           C  
ANISOU  381  CB  PHE A  44     3572   3692   4458    -91    -64     65       C  
ATOM    382  CG  PHE A  44      63.835 -38.195 -10.444  1.00 33.23           C  
ANISOU  382  CG  PHE A  44     3859   3999   4768    -68    -67     42       C  
ATOM    383  CD1 PHE A  44      63.966 -37.270 -11.473  1.00 32.87           C  
ANISOU  383  CD1 PHE A  44     3814   3926   4748    -57    -77     30       C  
ATOM    384  CD2 PHE A  44      64.423 -37.911  -9.214  1.00 32.22           C  
ANISOU  384  CD2 PHE A  44     3720   3906   4618    -70    -63     34       C  
ATOM    385  CE1 PHE A  44      64.698 -36.094 -11.287  1.00 32.10           C  
ANISOU  385  CE1 PHE A  44     3706   3826   4664    -44    -77      9       C  
ATOM    386  CE2 PHE A  44      65.153 -36.743  -9.020  1.00 30.41           C  
ANISOU  386  CE2 PHE A  44     3482   3679   4392    -66    -69      8       C  
ATOM    387  CZ  PHE A  44      65.299 -35.837 -10.059  1.00 28.01           C  
ANISOU  387  CZ  PHE A  44     3179   3339   4126    -51    -73     -6       C  
ATOM    388  N   GLU A  45      66.213 -40.482 -11.172  1.00 29.57           N  
ANISOU  388  N   GLU A  45     3455   3471   4311    -46    -37    120       N  
ATOM    389  CA  GLU A  45      67.514 -40.555 -10.522  1.00 30.08           C  
ANISOU  389  CA  GLU A  45     3492   3549   4388    -25    -36    156       C  
ATOM    390  C   GLU A  45      67.999 -39.130 -10.276  1.00 32.82           C  
ANISOU  390  C   GLU A  45     3809   3927   4736    -27    -63    130       C  
ATOM    391  O   GLU A  45      68.120 -38.346 -11.221  1.00 35.36           O  
ANISOU  391  O   GLU A  45     4138   4221   5076    -21    -59    106       O  
ATOM    392  CB  GLU A  45      68.540 -41.312 -11.368  1.00 36.55           C  
ANISOU  392  CB  GLU A  45     4331   4312   5246      4      3    192       C  
ATOM    393  CG  GLU A  45      69.887 -41.362 -10.658  1.00 41.41           C  
ANISOU  393  CG  GLU A  45     4894   4948   5890     28     -3    249       C  
ATOM    394  CD  GLU A  45      71.012 -41.975 -11.487  1.00 51.19           C  
ANISOU  394  CD  GLU A  45     6135   6127   7190     68     52    292       C  
ATOM    395  OE1 GLU A  45      70.874 -42.094 -12.726  1.00 50.13           O  
ANISOU  395  OE1 GLU A  45     6054   5932   7060     73     99    261       O  
ATOM    396  OE2 GLU A  45      72.041 -42.328 -10.876  1.00 57.83           O  
ANISOU  396  OE2 GLU A  45     6921   6981   8070     93     51    363       O  
ATOM    397  N   ASN A  46      68.264 -38.802  -9.015  1.00 30.51           N  
ANISOU  397  N   ASN A  46     3488   3688   4417    -44    -88    135       N  
ATOM    398  CA  ASN A  46      68.632 -37.438  -8.630  1.00 30.03           C  
ANISOU  398  CA  ASN A  46     3411   3652   4348    -62   -111     98       C  
ATOM    399  C   ASN A  46      70.090 -37.166  -8.982  1.00 33.81           C  
ANISOU  399  C   ASN A  46     3860   4123   4862    -54   -123    132       C  
ATOM    400  O   ASN A  46      70.995 -37.821  -8.455  1.00 34.00           O  
ANISOU  400  O   ASN A  46     3853   4173   4892    -53   -139    193       O  
ATOM    401  CB  ASN A  46      68.415 -37.254  -7.132  1.00 32.93           C  
ANISOU  401  CB  ASN A  46     3774   4080   4657   -100   -131     87       C  
ATOM    402  CG  ASN A  46      68.706 -35.848  -6.672  1.00 34.91           C  
ANISOU  402  CG  ASN A  46     4027   4348   4891   -134   -145     34       C  
ATOM    403  OD1 ASN A  46      68.678 -34.899  -7.465  1.00 31.95           O  
ANISOU  403  OD1 ASN A  46     3655   3932   4553   -122   -132     -2       O  
ATOM    404  ND2 ASN A  46      69.011 -35.704  -5.380  1.00 30.81           N  
ANISOU  404  ND2 ASN A  46     3511   3886   4308   -182   -171     32       N  
ATOM    405  N   LYS A  47      70.315 -36.205  -9.873  1.00 32.80           N  
ANISOU  405  N   LYS A  47     3735   3962   4764    -48   -114    103       N  
ATOM    406  CA  LYS A  47      71.644 -35.725 -10.237  1.00 34.39           C  
ANISOU  406  CA  LYS A  47     3904   4156   5005    -48   -121    130       C  
ATOM    407  C   LYS A  47      71.918 -34.323  -9.699  1.00 36.55           C  
ANISOU  407  C   LYS A  47     4168   4451   5268    -90   -150     88       C  
ATOM    408  O   LYS A  47      72.974 -33.750  -9.988  1.00 36.87           O  
ANISOU  408  O   LYS A  47     4179   4487   5344   -101   -159    105       O  
ATOM    409  CB  LYS A  47      71.814 -35.742 -11.765  1.00 38.08           C  
ANISOU  409  CB  LYS A  47     4393   4563   5514    -15    -78    134       C  
ATOM    410  CG  LYS A  47      71.712 -37.149 -12.390  1.00 41.35           C  
ANISOU  410  CG  LYS A  47     4833   4942   5937     17    -36    168       C  
ATOM    411  CD  LYS A  47      72.564 -38.167 -11.628  1.00 46.62           C  
ANISOU  411  CD  LYS A  47     5458   5628   6626     33    -35    236       C  
ATOM    412  CE  LYS A  47      74.055 -37.813 -11.597  1.00 65.98           C  
ANISOU  412  CE  LYS A  47     7845   8092   9133     40    -38    289       C  
ATOM    413  NZ  LYS A  47      74.856 -38.491 -12.651  1.00 68.52           N  
ANISOU  413  NZ  LYS A  47     8165   8352   9516     87     36    332       N  
ATOM    414  N   THR A  48      70.992 -33.768  -8.917  1.00 33.58           N  
ANISOU  414  N   THR A  48     3818   4092   4848   -117   -156     31       N  
ATOM    415  CA  THR A  48      71.122 -32.445  -8.332  1.00 31.31           C  
ANISOU  415  CA  THR A  48     3541   3809   4545   -163   -168    -24       C  
ATOM    416  C   THR A  48      71.795 -32.523  -6.964  1.00 34.77           C  
ANISOU  416  C   THR A  48     3969   4317   4927   -225   -215    -14       C  
ATOM    417  O   THR A  48      72.042 -33.600  -6.419  1.00 34.57           O  
ANISOU  417  O   THR A  48     3922   4337   4875   -225   -240     44       O  
ATOM    418  CB  THR A  48      69.747 -31.792  -8.188  1.00 31.35           C  
ANISOU  418  CB  THR A  48     3584   3787   4539   -157   -132    -91       C  
ATOM    419  OG1 THR A  48      69.127 -32.245  -6.973  1.00 31.51           O  
ANISOU  419  OG1 THR A  48     3622   3855   4496   -182   -130   -109       O  
ATOM    420  CG2 THR A  48      68.853 -32.138  -9.377  1.00 30.28           C  
ANISOU  420  CG2 THR A  48     3451   3609   4443   -102   -104    -77       C  
ATOM    421  N   THR A  49      72.057 -31.359  -6.377  1.00 31.45           N  
ANISOU  421  N   THR A  49     3568   3900   4480   -286   -229    -68       N  
ATOM    422  CA  THR A  49      72.540 -31.277  -5.004  1.00 33.47           C  
ANISOU  422  CA  THR A  49     3834   4226   4657   -368   -278    -74       C  
ATOM    423  C   THR A  49      71.409 -31.064  -3.988  1.00 35.21           C  
ANISOU  423  C   THR A  49     4120   4459   4798   -397   -244   -147       C  
ATOM    424  O   THR A  49      71.685 -30.819  -2.805  1.00 37.04           O  
ANISOU  424  O   THR A  49     4385   4745   4943   -481   -276   -171       O  
ATOM    425  CB  THR A  49      73.581 -30.163  -4.883  1.00 37.45           C  
ANISOU  425  CB  THR A  49     4331   4731   5168   -439   -314    -95       C  
ATOM    426  OG1 THR A  49      72.975 -28.918  -5.249  1.00 37.51           O  
ANISOU  426  OG1 THR A  49     4390   4663   5200   -440   -259   -184       O  
ATOM    427  CG2 THR A  49      74.755 -30.434  -5.829  1.00 34.67           C  
ANISOU  427  CG2 THR A  49     3901   4372   4898   -410   -340    -11       C  
ATOM    428  N   LEU A  50      70.153 -31.164  -4.418  1.00 31.94           N  
ANISOU  428  N   LEU A  50     3725   3999   4410   -337   -180   -178       N  
ATOM    429  CA  LEU A  50      68.963 -31.117  -3.573  1.00 32.29           C  
ANISOU  429  CA  LEU A  50     3818   4049   4400   -346   -128   -235       C  
ATOM    430  C   LEU A  50      68.611 -32.510  -3.050  1.00 33.22           C  
ANISOU  430  C   LEU A  50     3924   4226   4472   -336   -141   -176       C  
ATOM    431  O   LEU A  50      69.075 -33.524  -3.592  1.00 34.05           O  
ANISOU  431  O   LEU A  50     3984   4343   4611   -300   -176    -96       O  
ATOM    432  CB  LEU A  50      67.781 -30.573  -4.372  1.00 31.72           C  
ANISOU  432  CB  LEU A  50     3750   3902   4400   -282    -55   -275       C  
ATOM    433  CG  LEU A  50      67.845 -29.125  -4.848  1.00 43.93           C  
ANISOU  433  CG  LEU A  50     5316   5375   6002   -282    -22   -333       C  
ATOM    434  CD1 LEU A  50      66.687 -28.858  -5.793  1.00 41.40           C  
ANISOU  434  CD1 LEU A  50     4975   4989   5766   -205     33   -333       C  
ATOM    435  CD2 LEU A  50      67.800 -28.179  -3.673  1.00 48.53           C  
ANISOU  435  CD2 LEU A  50     5966   5952   6522   -353     16   -422       C  
ATOM    436  N   PRO A  51      67.784 -32.596  -1.998  1.00 31.39           N  
ANISOU  436  N   PRO A  51     3737   4023   4167   -366   -104   -215       N  
ATOM    437  CA  PRO A  51      67.271 -33.911  -1.568  1.00 32.88           C  
ANISOU  437  CA  PRO A  51     3916   4256   4322   -351   -104   -158       C  
ATOM    438  C   PRO A  51      66.492 -34.586  -2.685  1.00 32.06           C  
ANISOU  438  C   PRO A  51     3773   4105   4304   -271    -76   -125       C  
ATOM    439  O   PRO A  51      65.776 -33.928  -3.441  1.00 32.23           O  
ANISOU  439  O   PRO A  51     3788   4068   4389   -232    -32   -165       O  
ATOM    440  CB  PRO A  51      66.361 -33.573  -0.377  1.00 33.27           C  
ANISOU  440  CB  PRO A  51     4025   4328   4286   -396    -42   -224       C  
ATOM    441  CG  PRO A  51      66.920 -32.237   0.137  1.00 32.33           C  
ANISOU  441  CG  PRO A  51     3961   4202   4121   -465    -40   -306       C  
ATOM    442  CD  PRO A  51      67.362 -31.510  -1.092  1.00 33.87           C  
ANISOU  442  CD  PRO A  51     4120   4329   4422   -422    -51   -313       C  
ATOM    443  N   VAL A  52      66.627 -35.919  -2.771  1.00 29.41           N  
ANISOU  443  N   VAL A  52     3412   3792   3970   -252   -103    -46       N  
ATOM    444  CA  VAL A  52      66.059 -36.677  -3.887  1.00 32.20           C  
ANISOU  444  CA  VAL A  52     3739   4099   4395   -194    -86    -14       C  
ATOM    445  C   VAL A  52      64.555 -36.422  -4.044  1.00 31.11           C  
ANISOU  445  C   VAL A  52     3605   3936   4279   -175    -27    -58       C  
ATOM    446  O   VAL A  52      64.055 -36.257  -5.166  1.00 31.05           O  
ANISOU  446  O   VAL A  52     3577   3880   4339   -138    -16    -61       O  
ATOM    447  CB  VAL A  52      66.365 -38.184  -3.704  1.00 30.20           C  
ANISOU  447  CB  VAL A  52     3475   3868   4132   -187   -109     71       C  
ATOM    448  CG1 VAL A  52      65.898 -38.668  -2.331  1.00 30.47           C  
ANISOU  448  CG1 VAL A  52     3531   3961   4084   -229   -100     84       C  
ATOM    449  CG2 VAL A  52      65.709 -39.013  -4.812  1.00 32.66           C  
ANISOU  449  CG2 VAL A  52     3778   4126   4506   -145    -85     92       C  
ATOM    450  N   ASN A  53      63.800 -36.389  -2.939  1.00 30.50           N  
ANISOU  450  N   ASN A  53     3548   3892   4148   -203     14    -84       N  
ATOM    451  CA  ASN A  53      62.355 -36.221  -3.098  1.00 30.98           C  
ANISOU  451  CA  ASN A  53     3593   3929   4248   -180     77   -111       C  
ATOM    452  C   ASN A  53      61.993 -34.806  -3.527  1.00 34.79           C  
ANISOU  452  C   ASN A  53     4070   4363   4785   -156    116   -172       C  
ATOM    453  O   ASN A  53      60.950 -34.602  -4.167  1.00 33.57           O  
ANISOU  453  O   ASN A  53     3878   4175   4703   -119    148   -170       O  
ATOM    454  CB  ASN A  53      61.610 -36.564  -1.813  1.00 33.10           C  
ANISOU  454  CB  ASN A  53     3884   4243   4451   -212    129   -121       C  
ATOM    455  CG  ASN A  53      62.010 -35.662  -0.659  1.00 33.66           C  
ANISOU  455  CG  ASN A  53     4011   4341   4438   -261    156   -184       C  
ATOM    456  OD1 ASN A  53      63.201 -35.502  -0.364  1.00 32.98           O  
ANISOU  456  OD1 ASN A  53     3950   4281   4299   -298     97   -179       O  
ATOM    457  ND2 ASN A  53      61.014 -35.073   0.006  1.00 34.10           N  
ANISOU  457  ND2 ASN A  53     4085   4389   4481   -266    248   -241       N  
ATOM    458  N   VAL A  54      62.835 -33.827  -3.195  1.00 30.78           N  
ANISOU  458  N   VAL A  54     3596   3849   4251   -181    110   -218       N  
ATOM    459  CA  VAL A  54      62.589 -32.446  -3.618  1.00 33.28           C  
ANISOU  459  CA  VAL A  54     3913   4104   4627   -159    152   -274       C  
ATOM    460  C   VAL A  54      62.924 -32.275  -5.092  1.00 34.11           C  
ANISOU  460  C   VAL A  54     3982   4166   4813   -117    107   -238       C  
ATOM    461  O   VAL A  54      62.145 -31.694  -5.861  1.00 33.01           O  
ANISOU  461  O   VAL A  54     3812   3979   4753    -74    135   -237       O  
ATOM    462  CB  VAL A  54      63.408 -31.475  -2.745  1.00 33.63           C  
ANISOU  462  CB  VAL A  54     4019   4150   4610   -215    162   -342       C  
ATOM    463  CG1 VAL A  54      63.222 -30.023  -3.218  1.00 30.68           C  
ANISOU  463  CG1 VAL A  54     3652   3695   4309   -191    213   -399       C  
ATOM    464  CG2 VAL A  54      63.027 -31.622  -1.279  1.00 32.79           C  
ANISOU  464  CG2 VAL A  54     3965   4089   4404   -268    213   -383       C  
ATOM    465  N   ALA A  55      64.093 -32.783  -5.505  1.00 31.81           N  
ANISOU  465  N   ALA A  55     3691   3891   4503   -130     40   -199       N  
ATOM    466  CA  ALA A  55      64.466 -32.744  -6.913  1.00 34.26           C  
ANISOU  466  CA  ALA A  55     3979   4164   4876    -97      7   -164       C  
ATOM    467  C   ALA A  55      63.427 -33.443  -7.778  1.00 32.47           C  
ANISOU  467  C   ALA A  55     3723   3924   4689    -64      8   -124       C  
ATOM    468  O   ALA A  55      63.108 -32.973  -8.878  1.00 32.24           O  
ANISOU  468  O   ALA A  55     3676   3856   4716    -37      2   -111       O  
ATOM    469  CB  ALA A  55      65.845 -33.383  -7.114  1.00 31.37           C  
ANISOU  469  CB  ALA A  55     3614   3820   4487   -112    -47   -122       C  
ATOM    470  N   PHE A  56      62.894 -34.576  -7.295  1.00 28.23           N  
ANISOU  470  N   PHE A  56     3182   3424   4121    -74     11    -99       N  
ATOM    471  CA  PHE A  56      61.865 -35.307  -8.032  1.00 30.92           C  
ANISOU  471  CA  PHE A  56     3497   3757   4494    -61      7    -63       C  
ATOM    472  C   PHE A  56      60.642 -34.440  -8.282  1.00 28.59           C  
ANISOU  472  C   PHE A  56     3163   3441   4261    -37     39    -73       C  
ATOM    473  O   PHE A  56      60.107 -34.412  -9.395  1.00 30.56           O  
ANISOU  473  O   PHE A  56     3385   3670   4556    -24     13    -39       O  
ATOM    474  CB  PHE A  56      61.468 -36.554  -7.241  1.00 29.89           C  
ANISOU  474  CB  PHE A  56     3370   3665   4321    -84     15    -39       C  
ATOM    475  CG  PHE A  56      60.351 -37.356  -7.856  1.00 31.85           C  
ANISOU  475  CG  PHE A  56     3594   3910   4599    -88     11     -4       C  
ATOM    476  CD1 PHE A  56      60.448 -37.849  -9.152  1.00 31.51           C  
ANISOU  476  CD1 PHE A  56     3559   3839   4575    -91    -29     24       C  
ATOM    477  CD2 PHE A  56      59.233 -37.682  -7.099  1.00 32.02           C  
ANISOU  477  CD2 PHE A  56     3588   3957   4621    -99     48      0       C  
ATOM    478  CE1 PHE A  56      59.429 -38.641  -9.703  1.00 33.42           C  
ANISOU  478  CE1 PHE A  56     3785   4080   4833   -115    -42     55       C  
ATOM    479  CE2 PHE A  56      58.206 -38.472  -7.633  1.00 35.08           C  
ANISOU  479  CE2 PHE A  56     3945   4345   5037   -116     37     38       C  
ATOM    480  CZ  PHE A  56      58.302 -38.955  -8.928  1.00 33.72           C  
ANISOU  480  CZ  PHE A  56     3784   4147   4880   -129    -14     65       C  
ATOM    481  N   GLU A  57      60.191 -33.719  -7.257  1.00 31.60           N  
ANISOU  481  N   GLU A  57     3540   3824   4643    -34     99   -116       N  
ATOM    482  CA  GLU A  57      59.007 -32.878  -7.409  1.00 33.63           C  
ANISOU  482  CA  GLU A  57     3748   4052   4978      1    148   -118       C  
ATOM    483  C   GLU A  57      59.255 -31.703  -8.357  1.00 33.09           C  
ANISOU  483  C   GLU A  57     3670   3928   4974     32    137   -116       C  
ATOM    484  O   GLU A  57      58.391 -31.362  -9.179  1.00 31.21           O  
ANISOU  484  O   GLU A  57     3377   3669   4814     63    131    -72       O  
ATOM    485  CB  GLU A  57      58.560 -32.384  -6.037  1.00 33.85           C  
ANISOU  485  CB  GLU A  57     3790   4084   4988     -2    238   -173       C  
ATOM    486  CG  GLU A  57      57.290 -31.549  -6.084  1.00 37.79           C  
ANISOU  486  CG  GLU A  57     4229   4544   5586     44    314   -169       C  
ATOM    487  CD  GLU A  57      56.710 -31.291  -4.706  1.00 52.76           C  
ANISOU  487  CD  GLU A  57     6143   6444   7460     39    424   -223       C  
ATOM    488  OE1 GLU A  57      56.906 -32.140  -3.812  1.00 59.37           O  
ANISOU  488  OE1 GLU A  57     7019   7334   8204     -6    427   -237       O  
ATOM    489  OE2 GLU A  57      56.064 -30.236  -4.521  1.00 53.55           O  
ANISOU  489  OE2 GLU A  57     6221   6488   7636     80    515   -250       O  
ATOM    490  N   LEU A  58      60.419 -31.059  -8.254  1.00 32.41           N  
ANISOU  490  N   LEU A  58     3632   3821   4861     21    131   -156       N  
ATOM    491  CA  LEU A  58      60.716 -29.953  -9.159  1.00 33.15           C  
ANISOU  491  CA  LEU A  58     3721   3859   5017     48    123   -151       C  
ATOM    492  C   LEU A  58      60.815 -30.434 -10.601  1.00 33.46           C  
ANISOU  492  C   LEU A  58     3743   3900   5071     53     52    -84       C  
ATOM    493  O   LEU A  58      60.306 -29.779 -11.520  1.00 32.41           O  
ANISOU  493  O   LEU A  58     3577   3733   5004     81     42    -44       O  
ATOM    494  CB  LEU A  58      62.008 -29.263  -8.731  1.00 31.87           C  
ANISOU  494  CB  LEU A  58     3613   3677   4818     20    126   -204       C  
ATOM    495  CG  LEU A  58      61.960 -28.619  -7.340  1.00 38.09           C  
ANISOU  495  CG  LEU A  58     4439   4456   5576     -3    198   -282       C  
ATOM    496  CD1 LEU A  58      63.299 -27.957  -7.015  1.00 42.32           C  
ANISOU  496  CD1 LEU A  58     5029   4980   6071    -50    181   -330       C  
ATOM    497  CD2 LEU A  58      60.839 -27.624  -7.269  1.00 40.84           C  
ANISOU  497  CD2 LEU A  58     4764   4742   6012     43    283   -300       C  
ATOM    498  N   TRP A  59      61.460 -31.580 -10.817  1.00 29.35           N  
ANISOU  498  N   TRP A  59     3248   3416   4488     24      6    -68       N  
ATOM    499  CA  TRP A  59      61.520 -32.156 -12.154  1.00 30.47           C  
ANISOU  499  CA  TRP A  59     3393   3556   4627     18    -48    -16       C  
ATOM    500  C   TRP A  59      60.120 -32.433 -12.693  1.00 32.96           C  
ANISOU  500  C   TRP A  59     3661   3884   4980     21    -66     32       C  
ATOM    501  O   TRP A  59      59.804 -32.099 -13.844  1.00 31.92           O  
ANISOU  501  O   TRP A  59     3516   3738   4876     24   -104     78       O  
ATOM    502  CB  TRP A  59      62.357 -33.442 -12.129  1.00 29.96           C  
ANISOU  502  CB  TRP A  59     3368   3518   4498    -10    -69    -13       C  
ATOM    503  CG  TRP A  59      62.290 -34.176 -13.415  1.00 33.71           C  
ANISOU  503  CG  TRP A  59     3863   3985   4959    -26   -106     27       C  
ATOM    504  CD1 TRP A  59      62.870 -33.812 -14.606  1.00 39.29           C  
ANISOU  504  CD1 TRP A  59     4597   4665   5667    -26   -125     45       C  
ATOM    505  CD2 TRP A  59      61.587 -35.394 -13.663  1.00 33.50           C  
ANISOU  505  CD2 TRP A  59     3844   3978   4908    -55   -124     51       C  
ATOM    506  NE1 TRP A  59      62.566 -34.739 -15.573  1.00 38.81           N  
ANISOU  506  NE1 TRP A  59     4569   4606   5574    -57   -151     72       N  
ATOM    507  CE2 TRP A  59      61.785 -35.719 -15.021  1.00 39.39           C  
ANISOU  507  CE2 TRP A  59     4630   4704   5632    -77   -154     74       C  
ATOM    508  CE3 TRP A  59      60.810 -36.242 -12.868  1.00 37.04           C  
ANISOU  508  CE3 TRP A  59     4274   4454   5346    -71   -114     53       C  
ATOM    509  CZ2 TRP A  59      61.250 -36.865 -15.599  1.00 49.01           C  
ANISOU  509  CZ2 TRP A  59     5879   5927   6816   -122   -175     92       C  
ATOM    510  CZ3 TRP A  59      60.276 -37.388 -13.449  1.00 44.36           C  
ANISOU  510  CZ3 TRP A  59     5219   5384   6249   -111   -138     78       C  
ATOM    511  CH2 TRP A  59      60.496 -37.684 -14.802  1.00 52.12           C  
ANISOU  511  CH2 TRP A  59     6251   6345   7209   -140   -170     94       C  
ATOM    512  N   ALA A  60      59.256 -33.044 -11.874  1.00 32.28           N  
ANISOU  512  N   ALA A  60     3545   3828   4892     14    -43     30       N  
ATOM    513  CA  ALA A  60      57.913 -33.344 -12.359  1.00 29.99           C  
ANISOU  513  CA  ALA A  60     3195   3555   4644      8    -66     85       C  
ATOM    514  C   ALA A  60      57.138 -32.069 -12.681  1.00 30.75           C  
ANISOU  514  C   ALA A  60     3226   3623   4835     52    -50    117       C  
ATOM    515  O   ALA A  60      56.250 -32.089 -13.539  1.00 33.16           O  
ANISOU  515  O   ALA A  60     3476   3940   5182     46    -98    187       O  
ATOM    516  CB  ALA A  60      57.129 -34.182 -11.340  1.00 30.77           C  
ANISOU  516  CB  ALA A  60     3267   3691   4733     -8    -33     80       C  
ATOM    517  N   LYS A  61      57.456 -30.959 -12.014  1.00 32.05           N  
ANISOU  517  N   LYS A  61     3396   3747   5035     92     14     73       N  
ATOM    518  CA  LYS A  61      56.749 -29.699 -12.226  1.00 32.91           C  
ANISOU  518  CA  LYS A  61     3444   3810   5250    144     50    103       C  
ATOM    519  C   LYS A  61      57.468 -28.790 -13.226  1.00 32.91           C  
ANISOU  519  C   LYS A  61     3469   3764   5270    158     17    123       C  
ATOM    520  O   LYS A  61      57.147 -27.596 -13.320  1.00 34.57           O  
ANISOU  520  O   LYS A  61     3645   3918   5571    207     58    141       O  
ATOM    521  CB  LYS A  61      56.533 -28.994 -10.885  1.00 37.83           C  
ANISOU  521  CB  LYS A  61     4066   4400   5908    177    161     38       C  
ATOM    522  CG  LYS A  61      55.518 -29.731  -9.990  1.00 36.56           C  
ANISOU  522  CG  LYS A  61     3861   4280   5750    172    208     38       C  
ATOM    523  CD  LYS A  61      55.392 -29.105  -8.608  1.00 38.51           C  
ANISOU  523  CD  LYS A  61     4131   4497   6005    192    331    -39       C  
ATOM    524  CE  LYS A  61      54.269 -29.805  -7.800  1.00 36.67           C  
ANISOU  524  CE  LYS A  61     3845   4304   5784    190    388    -26       C  
ATOM    525  NZ  LYS A  61      54.141 -29.245  -6.412  1.00 39.75           N  
ANISOU  525  NZ  LYS A  61     4275   4666   6164    201    522   -110       N  
ATOM    526  N   ARG A  62      58.405 -29.341 -13.997  1.00 32.82           N  
ANISOU  526  N   ARG A  62     3516   3770   5183    119    -46    126       N  
ATOM    527  CA  ARG A  62      59.163 -28.546 -14.959  1.00 34.94           C  
ANISOU  527  CA  ARG A  62     3815   4000   5462    126    -72    146       C  
ATOM    528  C   ARG A  62      58.234 -27.931 -16.002  1.00 37.63           C  
ANISOU  528  C   ARG A  62     4094   4327   5876    149   -112    241       C  
ATOM    529  O   ARG A  62      57.160 -28.458 -16.302  1.00 32.79           O  
ANISOU  529  O   ARG A  62     3423   3755   5282    138   -153    303       O  
ATOM    530  CB  ARG A  62      60.225 -29.404 -15.653  1.00 33.38           C  
ANISOU  530  CB  ARG A  62     3687   3827   5170     79   -121    138       C  
ATOM    531  CG  ARG A  62      59.667 -30.515 -16.566  1.00 36.01           C  
ANISOU  531  CG  ARG A  62     4022   4204   5454     36   -188    191       C  
ATOM    532  CD  ARG A  62      60.731 -31.580 -16.862  1.00 36.41           C  
ANISOU  532  CD  ARG A  62     4151   4268   5414     -5   -200    160       C  
ATOM    533  NE  ARG A  62      60.223 -32.639 -17.736  1.00 39.86           N  
ANISOU  533  NE  ARG A  62     4612   4735   5797    -57   -252    196       N  
ATOM    534  CZ  ARG A  62      59.470 -33.663 -17.330  1.00 45.76           C  
ANISOU  534  CZ  ARG A  62     5344   5515   6527    -86   -263    196       C  
ATOM    535  NH1 ARG A  62      59.126 -33.780 -16.055  1.00 35.11           N  
ANISOU  535  NH1 ARG A  62     3954   4178   5208    -62   -222    167       N  
ATOM    536  NH2 ARG A  62      59.057 -34.579 -18.195  1.00 49.76           N  
ANISOU  536  NH2 ARG A  62     5885   6042   6980   -148   -312    223       N  
ATOM    537  N   ASN A  63      58.651 -26.789 -16.551  1.00 31.70           N  
ANISOU  537  N   ASN A  63     3352   3521   5172    176   -104    263       N  
ATOM    538  CA  ASN A  63      57.893 -26.159 -17.627  1.00 33.02           C  
ANISOU  538  CA  ASN A  63     3462   3676   5407    196   -152    372       C  
ATOM    539  C   ASN A  63      58.028 -26.989 -18.902  1.00 32.37           C  
ANISOU  539  C   ASN A  63     3416   3649   5233    133   -252    427       C  
ATOM    540  O   ASN A  63      59.149 -27.310 -19.319  1.00 34.95           O  
ANISOU  540  O   ASN A  63     3827   3976   5475     98   -261    388       O  
ATOM    541  CB  ASN A  63      58.408 -24.733 -17.855  1.00 32.97           C  
ANISOU  541  CB  ASN A  63     3467   3586   5472    239   -111    380       C  
ATOM    542  CG  ASN A  63      57.458 -23.893 -18.670  1.00 39.07           C  
ANISOU  542  CG  ASN A  63     4162   4333   6349    280   -140    503       C  
ATOM    543  OD1 ASN A  63      57.000 -24.316 -19.724  1.00 39.45           O  
ANISOU  543  OD1 ASN A  63     4188   4435   6366    248   -234    597       O  
ATOM    544  ND2 ASN A  63      57.159 -22.682 -18.186  1.00 41.42           N  
ANISOU  544  ND2 ASN A  63     4420   4545   6772    350    -58    508       N  
ATOM    545  N   ILE A  64      56.894 -27.359 -19.511  1.00 31.02           N  
ANISOU  545  N   ILE A  64     3182   3526   5077    112   -322    517       N  
ATOM    546  CA  ILE A  64      56.908 -28.207 -20.705  1.00 32.85           C  
ANISOU  546  CA  ILE A  64     3462   3814   5206     33   -418    564       C  
ATOM    547  C   ILE A  64      56.445 -27.435 -21.945  1.00 38.00           C  
ANISOU  547  C   ILE A  64     4082   4470   5888     27   -493    687       C  
ATOM    548  O   ILE A  64      56.031 -28.032 -22.933  1.00 37.72           O  
ANISOU  548  O   ILE A  64     4061   4491   5779    -46   -587    751       O  
ATOM    549  CB  ILE A  64      56.070 -29.488 -20.505  1.00 34.40           C  
ANISOU  549  CB  ILE A  64     3633   4075   5361    -22   -460    566       C  
ATOM    550  CG1 ILE A  64      54.618 -29.123 -20.184  1.00 42.62           C  
ANISOU  550  CG1 ILE A  64     4538   5136   6520     12   -474    650       C  
ATOM    551  CG2 ILE A  64      56.698 -30.393 -19.431  1.00 33.24           C  
ANISOU  551  CG2 ILE A  64     3539   3928   5163    -27   -394    453       C  
ATOM    552  CD1 ILE A  64      53.618 -30.145 -20.653  1.00 45.56           C  
ANISOU  552  CD1 ILE A  64     4871   5583   6855    -68   -565    712       C  
ATOM    553  N   LYS A  65      56.483 -26.127 -21.896  1.00 36.08           N  
ANISOU  553  N   LYS A  65     3797   4165   5747     97   -454    725       N  
ATOM    554  CA  LYS A  65      56.331 -25.293 -23.071  1.00 34.53           C  
ANISOU  554  CA  LYS A  65     3587   3959   5574     97   -516    842       C  
ATOM    555  C   LYS A  65      57.704 -24.825 -23.536  1.00 34.51           C  
ANISOU  555  C   LYS A  65     3690   3910   5512     90   -484    798       C  
ATOM    556  O   LYS A  65      58.694 -24.973 -22.813  1.00 36.82           O  
ANISOU  556  O   LYS A  65     4042   4170   5778     99   -408    683       O  
ATOM    557  CB  LYS A  65      55.446 -24.085 -22.745  1.00 37.56           C  
ANISOU  557  CB  LYS A  65     3850   4290   6133    187   -483    929       C  
ATOM    558  CG  LYS A  65      54.013 -24.452 -22.371  1.00 50.59           C  
ANISOU  558  CG  LYS A  65     5372   5987   7863    201   -512    998       C  
ATOM    559  CD  LYS A  65      53.364 -23.362 -21.533  1.00 74.25           C  
ANISOU  559  CD  LYS A  65     8261   8903  11045    312   -413   1026       C  
ATOM    560  CE  LYS A  65      53.951 -23.333 -20.124  1.00 86.71           C  
ANISOU  560  CE  LYS A  65     9889  10423  12632    351   -276    866       C  
ATOM    561  NZ  LYS A  65      53.339 -22.277 -19.265  1.00 94.07           N  
ANISOU  561  NZ  LYS A  65    10740  11267  13736    453   -157    874       N  
ATOM    562  N   PRO A  66      57.830 -24.282 -24.746  1.00 38.02           N  
ANISOU  562  N   PRO A  66     4158   4354   5932     67   -542    893       N  
ATOM    563  CA  PRO A  66      59.129 -23.707 -25.127  1.00 37.72           C  
ANISOU  563  CA  PRO A  66     4210   4264   5859     67   -496    856       C  
ATOM    564  C   PRO A  66      59.469 -22.572 -24.178  1.00 35.16           C  
ANISOU  564  C   PRO A  66     3851   3844   5664    151   -396    812       C  
ATOM    565  O   PRO A  66      58.627 -21.713 -23.894  1.00 39.61           O  
ANISOU  565  O   PRO A  66     4325   4364   6360    216   -380    878       O  
ATOM    566  CB  PRO A  66      58.898 -23.205 -26.560  1.00 37.96           C  
ANISOU  566  CB  PRO A  66     4253   4313   5857     32   -581    994       C  
ATOM    567  CG  PRO A  66      57.712 -24.005 -27.053  1.00 40.00           C  
ANISOU  567  CG  PRO A  66     4467   4663   6069    -26   -691   1075       C  
ATOM    568  CD  PRO A  66      56.849 -24.199 -25.848  1.00 38.59           C  
ANISOU  568  CD  PRO A  66     4182   4482   5998     29   -658   1044       C  
ATOM    569  N   VAL A  67      60.702 -22.581 -23.674  1.00 36.24           N  
ANISOU  569  N   VAL A  67     4058   3945   5766    146   -325    702       N  
ATOM    570  CA  VAL A  67      61.160 -21.531 -22.760  1.00 36.80           C  
ANISOU  570  CA  VAL A  67     4117   3925   5940    202   -232    643       C  
ATOM    571  C   VAL A  67      62.541 -21.071 -23.210  1.00 34.23           C  
ANISOU  571  C   VAL A  67     3869   3560   5576    176   -203    615       C  
ATOM    572  O   VAL A  67      63.249 -21.792 -23.931  1.00 33.80           O  
ANISOU  572  O   VAL A  67     3879   3553   5410    121   -233    610       O  
ATOM    573  CB  VAL A  67      61.192 -22.020 -21.291  1.00 32.38           C  
ANISOU  573  CB  VAL A  67     3547   3368   5388    215   -171    523       C  
ATOM    574  CG1 VAL A  67      59.762 -22.215 -20.726  1.00 34.84           C  
ANISOU  574  CG1 VAL A  67     3769   3700   5770    254   -173    555       C  
ATOM    575  CG2 VAL A  67      62.010 -23.311 -21.178  1.00 31.86           C  
ANISOU  575  CG2 VAL A  67     3544   3367   5193    156   -186    446       C  
ATOM    576  N   PRO A  68      62.955 -19.871 -22.798  1.00 32.46           N  
ANISOU  576  N   PRO A  68     3643   3244   5448    212   -136    597       N  
ATOM    577  CA  PRO A  68      64.311 -19.413 -23.123  1.00 37.53           C  
ANISOU  577  CA  PRO A  68     4350   3847   6063    181   -104    567       C  
ATOM    578  C   PRO A  68      65.364 -20.401 -22.642  1.00 34.57           C  
ANISOU  578  C   PRO A  68     4021   3522   5592    134    -89    464       C  
ATOM    579  O   PRO A  68      65.227 -21.027 -21.584  1.00 36.65           O  
ANISOU  579  O   PRO A  68     4269   3813   5842    136    -74    385       O  
ATOM    580  CB  PRO A  68      64.418 -18.078 -22.380  1.00 37.51           C  
ANISOU  580  CB  PRO A  68     4333   3733   6187    222    -26    537       C  
ATOM    581  CG  PRO A  68      62.995 -17.579 -22.316  1.00 36.20           C  
ANISOU  581  CG  PRO A  68     4092   3534   6128    288    -27    614       C  
ATOM    582  CD  PRO A  68      62.182 -18.841 -22.087  1.00 35.11           C  
ANISOU  582  CD  PRO A  68     3918   3497   5926    280    -80    607       C  
ATOM    583  N   GLU A  69      66.413 -20.556 -23.444  1.00 33.12           N  
ANISOU  583  N   GLU A  69     3891   3350   5343     93    -91    476       N  
ATOM    584  CA  GLU A  69      67.543 -21.352 -22.985  1.00 37.23           C  
ANISOU  584  CA  GLU A  69     4442   3904   5801     57    -64    392       C  
ATOM    585  C   GLU A  69      68.127 -20.736 -21.718  1.00 38.47           C  
ANISOU  585  C   GLU A  69     4582   4014   6022     60    -13    308       C  
ATOM    586  O   GLU A  69      68.106 -19.514 -21.527  1.00 37.25           O  
ANISOU  586  O   GLU A  69     4420   3781   5953     76     19    313       O  
ATOM    587  CB  GLU A  69      68.602 -21.457 -24.081  1.00 41.34           C  
ANISOU  587  CB  GLU A  69     5016   4431   6262     20    -54    426       C  
ATOM    588  CG  GLU A  69      68.152 -22.313 -25.254  1.00 42.48           C  
ANISOU  588  CG  GLU A  69     5202   4632   6306     -5    -98    485       C  
ATOM    589  CD  GLU A  69      69.263 -22.608 -26.232  1.00 45.34           C  
ANISOU  589  CD  GLU A  69     5629   5002   6596    -45    -64    500       C  
ATOM    590  OE1 GLU A  69      69.514 -21.745 -27.107  1.00 41.62           O  
ANISOU  590  OE1 GLU A  69     5183   4497   6134    -56    -57    567       O  
ATOM    591  OE2 GLU A  69      69.882 -23.708 -26.135  1.00 42.10           O  
ANISOU  591  OE2 GLU A  69     5246   4627   6123    -64    -37    448       O  
ATOM    592  N   VAL A  70      68.663 -21.603 -20.853  1.00 34.89           N  
ANISOU  592  N   VAL A  70     4127   3607   5523     40     -7    233       N  
ATOM    593  CA  VAL A  70      69.160 -21.163 -19.547  1.00 32.48           C  
ANISOU  593  CA  VAL A  70     3811   3275   5254     25     27    151       C  
ATOM    594  C   VAL A  70      70.260 -20.125 -19.702  1.00 31.43           C  
ANISOU  594  C   VAL A  70     3693   3083   5167     -6     58    147       C  
ATOM    595  O   VAL A  70      70.356 -19.186 -18.900  1.00 35.35           O  
ANISOU  595  O   VAL A  70     4192   3519   5720    -19     90     97       O  
ATOM    596  CB  VAL A  70      69.631 -22.384 -18.722  1.00 32.70           C  
ANISOU  596  CB  VAL A  70     3833   3377   5216      2     15     95       C  
ATOM    597  CG1 VAL A  70      70.447 -21.956 -17.505  1.00 36.15           C  
ANISOU  597  CG1 VAL A  70     4265   3802   5668    -37     34     22       C  
ATOM    598  CG2 VAL A  70      68.424 -23.221 -18.280  1.00 35.02           C  
ANISOU  598  CG2 VAL A  70     4110   3714   5481     29     -6     86       C  
ATOM    599  N   LYS A  71      71.103 -20.257 -20.732  1.00 34.14           N  
ANISOU  599  N   LYS A  71     4052   3436   5484    -26     58    197       N  
ATOM    600  CA  LYS A  71      72.164 -19.264 -20.907  1.00 35.97           C  
ANISOU  600  CA  LYS A  71     4291   3611   5765    -61     90    201       C  
ATOM    601  C   LYS A  71      71.586 -17.865 -21.121  1.00 36.67           C  
ANISOU  601  C   LYS A  71     4391   3602   5940    -42    113    229       C  
ATOM    602  O   LYS A  71      72.173 -16.870 -20.663  1.00 34.60           O  
ANISOU  602  O   LYS A  71     4135   3272   5738    -74    146    195       O  
ATOM    603  CB  LYS A  71      73.083 -19.657 -22.072  1.00 33.15           C  
ANISOU  603  CB  LYS A  71     3949   3279   5368    -80     99    260       C  
ATOM    604  CG  LYS A  71      72.394 -19.742 -23.440  1.00 35.03           C  
ANISOU  604  CG  LYS A  71     4221   3520   5570    -55     86    344       C  
ATOM    605  CD  LYS A  71      73.368 -20.113 -24.575  1.00 37.90           C  
ANISOU  605  CD  LYS A  71     4615   3902   5881    -82    115    392       C  
ATOM    606  CE  LYS A  71      72.601 -20.593 -25.805  1.00 39.06           C  
ANISOU  606  CE  LYS A  71     4812   4079   5950    -74     91    459       C  
ATOM    607  NZ  LYS A  71      73.474 -21.085 -26.921  1.00 39.39           N  
ANISOU  607  NZ  LYS A  71     4904   4141   5920   -103    135    494       N  
ATOM    608  N   ILE A  72      70.441 -17.761 -21.799  1.00 33.95           N  
ANISOU  608  N   ILE A  72     4045   3246   5606      8     94    296       N  
ATOM    609  CA  ILE A  72      69.826 -16.447 -21.983  1.00 32.51           C  
ANISOU  609  CA  ILE A  72     3863   2965   5524     39    121    339       C  
ATOM    610  C   ILE A  72      69.341 -15.904 -20.647  1.00 36.12           C  
ANISOU  610  C   ILE A  72     4310   3365   6049     54    162    254       C  
ATOM    611  O   ILE A  72      69.568 -14.735 -20.309  1.00 37.69           O  
ANISOU  611  O   ILE A  72     4528   3462   6331     44    215    230       O  
ATOM    612  CB  ILE A  72      68.666 -16.515 -22.996  1.00 35.86           C  
ANISOU  612  CB  ILE A  72     4273   3402   5949     88     80    449       C  
ATOM    613  CG1 ILE A  72      69.163 -16.847 -24.399  1.00 40.41           C  
ANISOU  613  CG1 ILE A  72     4883   4022   6451     60     49    534       C  
ATOM    614  CG2 ILE A  72      67.907 -15.193 -23.013  1.00 40.82           C  
ANISOU  614  CG2 ILE A  72     4884   3922   6705    137    112    502       C  
ATOM    615  CD1 ILE A  72      70.000 -15.778 -25.027  1.00 43.17           C  
ANISOU  615  CD1 ILE A  72     5259   4298   6847     38     87    579       C  
ATOM    616  N   LEU A  73      68.628 -16.734 -19.884  1.00 34.73           N  
ANISOU  616  N   LEU A  73     4112   3246   5836     73    148    208       N  
ATOM    617  CA  LEU A  73      68.130 -16.296 -18.587  1.00 33.43           C  
ANISOU  617  CA  LEU A  73     3950   3033   5721     84    199    121       C  
ATOM    618  C   LEU A  73      69.282 -15.909 -17.669  1.00 36.55           C  
ANISOU  618  C   LEU A  73     4382   3403   6102      9    228     22       C  
ATOM    619  O   LEU A  73      69.211 -14.888 -16.973  1.00 35.21           O  
ANISOU  619  O   LEU A  73     4242   3137   5998     -2    291    -38       O  
ATOM    620  CB  LEU A  73      67.272 -17.402 -17.949  1.00 34.36           C  
ANISOU  620  CB  LEU A  73     4038   3232   5785    107    177     93       C  
ATOM    621  CG  LEU A  73      66.077 -17.867 -18.779  1.00 35.79           C  
ANISOU  621  CG  LEU A  73     4175   3450   5976    165    136    191       C  
ATOM    622  CD1 LEU A  73      65.492 -19.137 -18.174  1.00 42.57           C  
ANISOU  622  CD1 LEU A  73     5010   4400   6765    167    107    158       C  
ATOM    623  CD2 LEU A  73      65.017 -16.754 -18.830  1.00 40.60           C  
ANISOU  623  CD2 LEU A  73     4753   3961   6713    232    184    241       C  
ATOM    624  N   ASN A  74      70.350 -16.719 -17.644  1.00 33.54           N  
ANISOU  624  N   ASN A  74     4000   3105   5640    -45    186      4       N  
ATOM    625  CA  ASN A  74      71.512 -16.369 -16.833  1.00 34.50           C  
ANISOU  625  CA  ASN A  74     4142   3216   5748   -128    195    -71       C  
ATOM    626  C   ASN A  74      72.100 -15.029 -17.263  1.00 35.61           C  
ANISOU  626  C   ASN A  74     4309   3250   5969   -159    234    -58       C  
ATOM    627  O   ASN A  74      72.456 -14.197 -16.423  1.00 36.46           O  
ANISOU  627  O   ASN A  74     4453   3292   6108   -216    271   -135       O  
ATOM    628  CB  ASN A  74      72.596 -17.442 -16.941  1.00 35.95           C  
ANISOU  628  CB  ASN A  74     4300   3505   5855   -170    144    -59       C  
ATOM    629  CG  ASN A  74      72.230 -18.732 -16.230  1.00 41.63           C  
ANISOU  629  CG  ASN A  74     5001   4320   6497   -158    110    -88       C  
ATOM    630  OD1 ASN A  74      71.289 -18.780 -15.441  1.00 39.37           O  
ANISOU  630  OD1 ASN A  74     4725   4029   6205   -137    125   -135       O  
ATOM    631  ND2 ASN A  74      73.014 -19.777 -16.481  1.00 36.78           N  
ANISOU  631  ND2 ASN A  74     4359   3788   5830   -173     74    -58       N  
ATOM    632  N   ASN A  75      72.284 -14.839 -18.572  1.00 34.62           N  
ANISOU  632  N   ASN A  75     4174   3110   5869   -134    227     40       N  
ATOM    633  CA  ASN A  75      72.883 -13.595 -19.066  1.00 33.88           C  
ANISOU  633  CA  ASN A  75     4104   2915   5853   -165    265     66       C  
ATOM    634  C   ASN A  75      72.025 -12.379 -18.731  1.00 36.93           C  
ANISOU  634  C   ASN A  75     4523   3169   6342   -132    330     46       C  
ATOM    635  O   ASN A  75      72.550 -11.265 -18.588  1.00 38.41           O  
ANISOU  635  O   ASN A  75     4746   3252   6597   -179    377     21       O  
ATOM    636  CB  ASN A  75      73.079 -13.675 -20.579  1.00 39.50           C  
ANISOU  636  CB  ASN A  75     4805   3640   6562   -138    249    185       C  
ATOM    637  CG  ASN A  75      74.174 -14.662 -20.986  1.00 34.94           C  
ANISOU  637  CG  ASN A  75     4206   3164   5906   -178    217    203       C  
ATOM    638  OD1 ASN A  75      74.887 -15.206 -20.145  1.00 35.69           O  
ANISOU  638  OD1 ASN A  75     4282   3316   5964   -226    201    138       O  
ATOM    639  ND2 ASN A  75      74.323 -14.863 -22.285  1.00 34.66           N  
ANISOU  639  ND2 ASN A  75     4174   3148   5846   -159    214    296       N  
ATOM    640  N   LEU A  76      70.711 -12.557 -18.649  1.00 38.49           N  
ANISOU  640  N   LEU A  76     4704   3359   6560    -51    340     65       N  
ATOM    641  CA  LEU A  76      69.833 -11.452 -18.289  1.00 43.57           C  
ANISOU  641  CA  LEU A  76     5369   3870   7317     -5    418     51       C  
ATOM    642  C   LEU A  76      69.695 -11.277 -16.783  1.00 43.74           C  
ANISOU  642  C   LEU A  76     5431   3857   7332    -41    474    -89       C  
ATOM    643  O   LEU A  76      68.921 -10.416 -16.349  1.00 47.18           O  
ANISOU  643  O   LEU A  76     5890   4174   7861      0    561   -118       O  
ATOM    644  CB  LEU A  76      68.448 -11.640 -18.913  1.00 37.78           C  
ANISOU  644  CB  LEU A  76     4586   3140   6630    101    410    152       C  
ATOM    645  CG  LEU A  76      68.368 -11.473 -20.431  1.00 44.85           C  
ANISOU  645  CG  LEU A  76     5456   4038   7546    136    366    303       C  
ATOM    646  CD1 LEU A  76      67.041 -12.029 -20.945  1.00 44.62           C  
ANISOU  646  CD1 LEU A  76     5368   4063   7524    217    323    399       C  
ATOM    647  CD2 LEU A  76      68.536 -10.009 -20.842  1.00 45.91           C  
ANISOU  647  CD2 LEU A  76     5618   4021   7804    144    430    351       C  
ATOM    648  N   GLY A  77      70.419 -12.065 -15.986  1.00 39.90           N  
ANISOU  648  N   GLY A  77     4953   3468   6738   -117    432   -172       N  
ATOM    649  CA  GLY A  77      70.395 -11.908 -14.545  1.00 43.39           C  
ANISOU  649  CA  GLY A  77     5447   3889   7149   -173    476   -305       C  
ATOM    650  C   GLY A  77      69.170 -12.466 -13.843  1.00 39.96           C  
ANISOU  650  C   GLY A  77     5002   3484   6698   -110    507   -338       C  
ATOM    651  O   GLY A  77      68.880 -12.042 -12.722  1.00 43.25           O  
ANISOU  651  O   GLY A  77     5476   3844   7114   -139    579   -445       O  
ATOM    652  N   VAL A  78      68.444 -13.400 -14.464  1.00 40.20           N  
ANISOU  652  N   VAL A  78     4965   3598   6710    -32    458   -252       N  
ATOM    653  CA  VAL A  78      67.259 -13.976 -13.831  1.00 37.47           C  
ANISOU  653  CA  VAL A  78     4597   3286   6355     26    485   -273       C  
ATOM    654  C   VAL A  78      67.674 -14.804 -12.622  1.00 40.75           C  
ANISOU  654  C   VAL A  78     5042   3794   6648    -48    463   -374       C  
ATOM    655  O   VAL A  78      68.565 -15.654 -12.713  1.00 39.22           O  
ANISOU  655  O   VAL A  78     4833   3705   6363   -100    378   -365       O  
ATOM    656  CB  VAL A  78      66.465 -14.825 -14.835  1.00 34.17           C  
ANISOU  656  CB  VAL A  78     4100   2943   5938    105    423   -153       C  
ATOM    657  CG1 VAL A  78      65.394 -15.629 -14.109  1.00 35.82           C  
ANISOU  657  CG1 VAL A  78     4278   3211   6121    145    437   -177       C  
ATOM    658  CG2 VAL A  78      65.826 -13.934 -15.912  1.00 37.89           C  
ANISOU  658  CG2 VAL A  78     4540   3322   6536    181    446    -41       C  
ATOM    659  N   ASP A  79      67.019 -14.566 -11.485  1.00 40.07           N  
ANISOU  659  N   ASP A  79     4996   3668   6560    -50    544   -465       N  
ATOM    660  CA  ASP A  79      67.271 -15.292 -10.240  1.00 37.58           C  
ANISOU  660  CA  ASP A  79     4719   3439   6123   -122    530   -559       C  
ATOM    661  C   ASP A  79      66.262 -16.400  -9.960  1.00 41.41           C  
ANISOU  661  C   ASP A  79     5154   4010   6569    -62    521   -535       C  
ATOM    662  O   ASP A  79      66.583 -17.349  -9.229  1.00 37.74           O  
ANISOU  662  O   ASP A  79     4698   3651   5991   -115    473   -571       O  
ATOM    663  CB  ASP A  79      67.225 -14.317  -9.056  1.00 41.29           C  
ANISOU  663  CB  ASP A  79     5287   3808   6593   -181    637   -691       C  
ATOM    664  CG  ASP A  79      68.301 -13.264  -9.139  1.00 48.31           C  
ANISOU  664  CG  ASP A  79     6237   4613   7504   -268    643   -733       C  
ATOM    665  OD1 ASP A  79      69.476 -13.651  -9.292  1.00 53.75           O  
ANISOU  665  OD1 ASP A  79     6914   5384   8124   -348    543   -718       O  
ATOM    666  OD2 ASP A  79      67.970 -12.055  -9.077  1.00 49.02           O  
ANISOU  666  OD2 ASP A  79     6382   4551   7692   -255    751   -775       O  
ATOM    667  N   ILE A  80      65.042 -16.278 -10.465  1.00 38.67           N  
ANISOU  667  N   ILE A  80     4754   3621   6319     40    567   -470       N  
ATOM    668  CA  ILE A  80      63.939 -17.122 -10.025  1.00 37.60           C  
ANISOU  668  CA  ILE A  80     4575   3546   6166     91    585   -460       C  
ATOM    669  C   ILE A  80      62.810 -16.961 -11.024  1.00 41.55           C  
ANISOU  669  C   ILE A  80     4989   4009   6789    199    596   -344       C  
ATOM    670  O   ILE A  80      62.738 -15.952 -11.734  1.00 39.10           O  
ANISOU  670  O   ILE A  80     4670   3599   6588    240    627   -296       O  
ATOM    671  CB  ILE A  80      63.515 -16.709  -8.584  1.00 36.07           C  
ANISOU  671  CB  ILE A  80     4453   3301   5952     63    704   -583       C  
ATOM    672  CG1 ILE A  80      62.649 -17.786  -7.911  1.00 41.24           C  
ANISOU  672  CG1 ILE A  80     5075   4046   6549     85    713   -587       C  
ATOM    673  CG2 ILE A  80      62.795 -15.333  -8.582  1.00 35.61           C  
ANISOU  673  CG2 ILE A  80     4414   3077   6040    126    844   -601       C  
ATOM    674  CD1 ILE A  80      62.530 -17.581  -6.387  1.00 37.95           C  
ANISOU  674  CD1 ILE A  80     4750   3609   6058     26    816   -719       C  
ATOM    675  N   ALA A  81      61.918 -17.943 -11.076  1.00 38.48           N  
ANISOU  675  N   ALA A  81     4532   3702   6385    241    567   -292       N  
ATOM    676  CA  ALA A  81      60.793 -17.937 -11.999  1.00 42.02           C  
ANISOU  676  CA  ALA A  81     4885   4140   6940    330    556   -170       C  
ATOM    677  C   ALA A  81      59.480 -17.790 -11.237  1.00 43.38           C  
ANISOU  677  C   ALA A  81     5015   4275   7193    393    665   -181       C  
ATOM    678  O   ALA A  81      59.330 -18.321 -10.131  1.00 39.01           O  
ANISOU  678  O   ALA A  81     4493   3762   6566    362    710   -266       O  
ATOM    679  CB  ALA A  81      60.765 -19.223 -12.829  1.00 40.89           C  
ANISOU  679  CB  ALA A  81     4689   4123   6723    320    428    -85       C  
ATOM    680  N   ALA A  82      58.528 -17.075 -11.835  1.00 39.32           N  
ANISOU  680  N   ALA A  82     4425   3684   6832    483    709    -86       N  
ATOM    681  CA  ALA A  82      57.202 -16.899 -11.248  1.00 42.36           C  
ANISOU  681  CA  ALA A  82     4745   4027   7324    558    821    -72       C  
ATOM    682  C   ALA A  82      56.343 -18.126 -11.543  1.00 39.62           C  
ANISOU  682  C   ALA A  82     4297   3806   6953    573    739     15       C  
ATOM    683  O   ALA A  82      55.891 -18.320 -12.677  1.00 45.15           O  
ANISOU  683  O   ALA A  82     4909   4544   7704    605    644    151       O  
ATOM    684  CB  ALA A  82      56.538 -15.638 -11.795  1.00 44.49           C  
ANISOU  684  CB  ALA A  82     4957   4161   7787    655    901     14       C  
ATOM    685  N   ASN A  83      56.136 -18.965 -10.529  1.00 40.62           N  
ANISOU  685  N   ASN A  83     4442   3998   6992    539    770    -61       N  
ATOM    686  CA  ASN A  83      55.115 -20.018 -10.573  1.00 43.28           C  
ANISOU  686  CA  ASN A  83     4680   4432   7331    557    730     11       C  
ATOM    687  C   ASN A  83      55.387 -21.077 -11.642  1.00 43.03           C  
ANISOU  687  C   ASN A  83     4617   4515   7216    513    556     95       C  
ATOM    688  O   ASN A  83      54.464 -21.625 -12.253  1.00 43.20           O  
ANISOU  688  O   ASN A  83     4536   4594   7284    535    495    205       O  
ATOM    689  CB  ASN A  83      53.740 -19.388 -10.751  1.00 45.75           C  
ANISOU  689  CB  ASN A  83     4871   4679   7833    660    814    110       C  
ATOM    690  CG  ASN A  83      53.478 -18.344  -9.697  1.00 49.18           C  
ANISOU  690  CG  ASN A  83     5349   4984   8354    707   1010     18       C  
ATOM    691  OD1 ASN A  83      53.834 -17.177  -9.858  1.00 60.43           O  
ANISOU  691  OD1 ASN A  83     6816   6286   9858    737   1075      0       O  
ATOM    692  ND2 ASN A  83      52.900 -18.770  -8.581  1.00 53.08           N  
ANISOU  692  ND2 ASN A  83     5847   5497   8825    705   1112    -50       N  
ATOM    693  N   THR A  84      56.662 -21.389 -11.851  1.00 37.63           N  
ANISOU  693  N   THR A  84     4023   3865   6409    443    482     43       N  
ATOM    694  CA  THR A  84      57.067 -22.458 -12.757  1.00 37.89           C  
ANISOU  694  CA  THR A  84     4053   3998   6348    394    341     98       C  
ATOM    695  C   THR A  84      58.469 -22.885 -12.347  1.00 35.35           C  
ANISOU  695  C   THR A  84     3835   3707   5891    321    313      2       C  
ATOM    696  O   THR A  84      59.118 -22.224 -11.533  1.00 40.86           O  
ANISOU  696  O   THR A  84     4601   4351   6575    303    383    -91       O  
ATOM    697  CB  THR A  84      57.010 -22.005 -14.230  1.00 44.74           C  
ANISOU  697  CB  THR A  84     4879   4848   7273    416    261    217       C  
ATOM    698  OG1 THR A  84      57.223 -23.123 -15.103  1.00 44.97           O  
ANISOU  698  OG1 THR A  84     4910   4974   7204    363    137    267       O  
ATOM    699  CG2 THR A  84      58.065 -20.926 -14.527  1.00 42.31           C  
ANISOU  699  CG2 THR A  84     4640   4457   6979    413    282    186       C  
ATOM    700  N   VAL A  85      58.925 -24.009 -12.909  1.00 34.93           N  
ANISOU  700  N   VAL A  85     3793   3738   5742    274    213     28       N  
ATOM    701  CA  VAL A  85      60.301 -24.480 -12.761  1.00 31.75           C  
ANISOU  701  CA  VAL A  85     3468   3367   5229    214    175    -31       C  
ATOM    702  C   VAL A  85      60.927 -24.511 -14.147  1.00 35.58           C  
ANISOU  702  C   VAL A  85     3962   3858   5699    202     95     34       C  
ATOM    703  O   VAL A  85      60.432 -25.210 -15.038  1.00 34.91           O  
ANISOU  703  O   VAL A  85     3846   3820   5600    198     30    107       O  
ATOM    704  CB  VAL A  85      60.386 -25.882 -12.124  1.00 36.59           C  
ANISOU  704  CB  VAL A  85     4094   4066   5742    172    147    -60       C  
ATOM    705  CG1 VAL A  85      61.841 -26.364 -12.084  1.00 33.24           C  
ANISOU  705  CG1 VAL A  85     3732   3672   5224    120    104    -97       C  
ATOM    706  CG2 VAL A  85      59.784 -25.895 -10.735  1.00 38.74           C  
ANISOU  706  CG2 VAL A  85     4366   4340   6012    176    229   -122       C  
ATOM    707  N   ILE A  86      62.022 -23.783 -14.330  1.00 33.46           N  
ANISOU  707  N   ILE A  86     3742   3545   5427    185    103      6       N  
ATOM    708  CA  ILE A  86      62.823 -23.925 -15.536  1.00 29.72           C  
ANISOU  708  CA  ILE A  86     3290   3083   4920    163     41     56       C  
ATOM    709  C   ILE A  86      63.825 -25.045 -15.269  1.00 33.05           C  
ANISOU  709  C   ILE A  86     3751   3568   5239    114     10     16       C  
ATOM    710  O   ILE A  86      64.762 -24.870 -14.483  1.00 35.03           O  
ANISOU  710  O   ILE A  86     4032   3813   5463     84     33    -48       O  
ATOM    711  CB  ILE A  86      63.540 -22.620 -15.911  1.00 33.39           C  
ANISOU  711  CB  ILE A  86     3781   3467   5439    167     68     56       C  
ATOM    712  CG1 ILE A  86      62.531 -21.480 -16.058  1.00 33.78           C  
ANISOU  712  CG1 ILE A  86     3789   3438   5609    226    113    100       C  
ATOM    713  CG2 ILE A  86      64.292 -22.806 -17.209  1.00 32.35           C  
ANISOU  713  CG2 ILE A  86     3671   3351   5269    145     12    115       C  
ATOM    714  CD1 ILE A  86      61.478 -21.759 -17.099  1.00 38.40           C  
ANISOU  714  CD1 ILE A  86     4313   4052   6224    258     56    215       C  
ATOM    715  N   TRP A  87      63.626 -26.201 -15.901  1.00 30.36           N  
ANISOU  715  N   TRP A  87     3408   3285   4844    100    -41     56       N  
ATOM    716  CA  TRP A  87      64.556 -27.310 -15.714  1.00 28.47           C  
ANISOU  716  CA  TRP A  87     3201   3092   4523     64    -58     30       C  
ATOM    717  C   TRP A  87      65.773 -27.122 -16.613  1.00 32.20           C  
ANISOU  717  C   TRP A  87     3708   3548   4979     47    -68     48       C  
ATOM    718  O   TRP A  87      65.636 -26.890 -17.818  1.00 33.48           O  
ANISOU  718  O   TRP A  87     3880   3694   5145     50    -89    103       O  
ATOM    719  CB  TRP A  87      63.882 -28.649 -16.013  1.00 31.16           C  
ANISOU  719  CB  TRP A  87     3538   3486   4816     53    -93     58       C  
ATOM    720  CG  TRP A  87      64.725 -29.833 -15.560  1.00 32.94           C  
ANISOU  720  CG  TRP A  87     3792   3749   4976     27    -94     30       C  
ATOM    721  CD1 TRP A  87      65.485 -30.653 -16.355  1.00 35.71           C  
ANISOU  721  CD1 TRP A  87     4179   4106   5281      9   -106     49       C  
ATOM    722  CD2 TRP A  87      64.907 -30.301 -14.210  1.00 30.04           C  
ANISOU  722  CD2 TRP A  87     3418   3410   4585     19    -75    -14       C  
ATOM    723  NE1 TRP A  87      66.117 -31.606 -15.587  1.00 32.88           N  
ANISOU  723  NE1 TRP A  87     3829   3775   4890     -1    -95     27       N  
ATOM    724  CE2 TRP A  87      65.770 -31.425 -14.271  1.00 35.59           C  
ANISOU  724  CE2 TRP A  87     4146   4138   5241      1    -84     -7       C  
ATOM    725  CE3 TRP A  87      64.395 -29.905 -12.964  1.00 32.37           C  
ANISOU  725  CE3 TRP A  87     3695   3711   4893     23    -45    -56       C  
ATOM    726  CZ2 TRP A  87      66.154 -32.145 -13.133  1.00 33.44           C  
ANISOU  726  CZ2 TRP A  87     3870   3900   4936    -11    -78    -26       C  
ATOM    727  CZ3 TRP A  87      64.771 -30.627 -11.827  1.00 32.65           C  
ANISOU  727  CZ3 TRP A  87     3741   3788   4879      0    -39    -85       C  
ATOM    728  CH2 TRP A  87      65.651 -31.733 -11.923  1.00 31.04           C  
ANISOU  728  CH2 TRP A  87     3551   3612   4630    -16    -62    -63       C  
ATOM    729  N   ASP A  88      66.965 -27.228 -16.026  1.00 32.20           N  
ANISOU  729  N   ASP A  88     3722   3555   4958     25    -54      9       N  
ATOM    730  CA  ASP A  88      68.221 -27.015 -16.755  1.00 31.37           C  
ANISOU  730  CA  ASP A  88     3636   3433   4849      8    -51     28       C  
ATOM    731  C   ASP A  88      68.695 -28.379 -17.246  1.00 35.07           C  
ANISOU  731  C   ASP A  88     4123   3940   5262      0    -59     49       C  
ATOM    732  O   ASP A  88      69.290 -29.152 -16.494  1.00 33.58           O  
ANISOU  732  O   ASP A  88     3925   3783   5052    -10    -55     31       O  
ATOM    733  CB  ASP A  88      69.247 -26.351 -15.841  1.00 32.91           C  
ANISOU  733  CB  ASP A  88     3824   3617   5064    -18    -35    -16       C  
ATOM    734  CG  ASP A  88      70.563 -26.048 -16.543  1.00 36.37           C  
ANISOU  734  CG  ASP A  88     4267   4038   5515    -37    -27      9       C  
ATOM    735  OD1 ASP A  88      70.861 -26.608 -17.619  1.00 37.79           O  
ANISOU  735  OD1 ASP A  88     4461   4222   5675    -28    -23     54       O  
ATOM    736  OD2 ASP A  88      71.310 -25.226 -15.995  1.00 38.81           O  
ANISOU  736  OD2 ASP A  88     4567   4326   5852    -67    -19    -18       O  
ATOM    737  N   TYR A  89      68.422 -28.685 -18.512  1.00 31.48           N  
ANISOU  737  N   TYR A  89     3699   3479   4784      0    -67     91       N  
ATOM    738  CA  TYR A  89      68.731 -30.018 -19.016  1.00 34.93           C  
ANISOU  738  CA  TYR A  89     4171   3937   5166    -11    -58    102       C  
ATOM    739  C   TYR A  89      70.242 -30.232 -19.212  1.00 39.85           C  
ANISOU  739  C   TYR A  89     4800   4549   5793    -14    -17    106       C  
ATOM    740  O   TYR A  89      70.694 -31.379 -19.251  1.00 38.21           O  
ANISOU  740  O   TYR A  89     4608   4350   5560    -13      8    108       O  
ATOM    741  CB  TYR A  89      67.970 -30.260 -20.323  1.00 33.19           C  
ANISOU  741  CB  TYR A  89     3996   3713   4902    -27    -79    140       C  
ATOM    742  CG  TYR A  89      66.494 -30.604 -20.145  1.00 33.95           C  
ANISOU  742  CG  TYR A  89     4076   3836   4988    -32   -124    148       C  
ATOM    743  CD1 TYR A  89      65.520 -29.605 -20.037  1.00 35.32           C  
ANISOU  743  CD1 TYR A  89     4206   4004   5211    -16   -153    172       C  
ATOM    744  CD2 TYR A  89      66.074 -31.929 -20.113  1.00 34.66           C  
ANISOU  744  CD2 TYR A  89     4191   3952   5028    -54   -131    138       C  
ATOM    745  CE1 TYR A  89      64.165 -29.928 -19.884  1.00 34.86           C  
ANISOU  745  CE1 TYR A  89     4115   3973   5156    -19   -192    191       C  
ATOM    746  CE2 TYR A  89      64.739 -32.254 -19.955  1.00 40.28           C  
ANISOU  746  CE2 TYR A  89     4880   4691   5735    -68   -174    151       C  
ATOM    747  CZ  TYR A  89      63.789 -31.259 -19.847  1.00 37.86           C  
ANISOU  747  CZ  TYR A  89     4516   4386   5481    -50   -206    181       C  
ATOM    748  OH  TYR A  89      62.465 -31.621 -19.705  1.00 40.36           O  
ANISOU  748  OH  TYR A  89     4796   4735   5806    -62   -246    206       O  
ATOM    749  N   LYS A  90      71.035 -29.165 -19.330  1.00 37.29           N  
ANISOU  749  N   LYS A  90     4458   4199   5510    -17     -3    113       N  
ATOM    750  CA  LYS A  90      72.487 -29.351 -19.403  1.00 37.17           C  
ANISOU  750  CA  LYS A  90     4428   4180   5515    -20     37    126       C  
ATOM    751  C   LYS A  90      73.058 -29.819 -18.067  1.00 40.39           C  
ANISOU  751  C   LYS A  90     4783   4622   5940    -22     26    109       C  
ATOM    752  O   LYS A  90      74.052 -30.543 -18.042  1.00 41.43           O  
ANISOU  752  O   LYS A  90     4893   4764   6085    -16     55    133       O  
ATOM    753  CB  LYS A  90      73.176 -28.051 -19.825  1.00 47.80           C  
ANISOU  753  CB  LYS A  90     5764   5492   6906    -33     51    141       C  
ATOM    754  CG  LYS A  90      72.663 -27.440 -21.120  1.00 57.99           C  
ANISOU  754  CG  LYS A  90     7104   6750   8180    -35     56    173       C  
ATOM    755  CD  LYS A  90      73.151 -28.202 -22.327  1.00 60.50           C  
ANISOU  755  CD  LYS A  90     7475   7063   8450    -39    104    202       C  
ATOM    756  CE  LYS A  90      72.881 -27.425 -23.605  1.00 59.64           C  
ANISOU  756  CE  LYS A  90     7416   6926   8317    -54    108    244       C  
ATOM    757  NZ  LYS A  90      71.424 -27.165 -23.812  1.00 53.00           N  
ANISOU  757  NZ  LYS A  90     6594   6093   7451    -56     44    257       N  
ATOM    758  N   ARG A  91      72.476 -29.378 -16.954  1.00 34.42           N  
ANISOU  758  N   ARG A  91     4006   3885   5188    -32    -12     73       N  
ATOM    759  CA  ARG A  91      72.920 -29.758 -15.619  1.00 35.74           C  
ANISOU  759  CA  ARG A  91     4133   4094   5352    -48    -33     59       C  
ATOM    760  C   ARG A  91      72.061 -30.862 -14.997  1.00 36.93           C  
ANISOU  760  C   ARG A  91     4293   4279   5462    -35    -47     50       C  
ATOM    761  O   ARG A  91      72.418 -31.364 -13.926  1.00 38.27           O  
ANISOU  761  O   ARG A  91     4434   4489   5619    -48    -66     51       O  
ATOM    762  CB  ARG A  91      72.930 -28.519 -14.693  1.00 33.52           C  
ANISOU  762  CB  ARG A  91     3838   3811   5088    -84    -56     17       C  
ATOM    763  CG  ARG A  91      74.076 -27.480 -14.966  1.00 34.31           C  
ANISOU  763  CG  ARG A  91     3917   3884   5234   -116    -50     27       C  
ATOM    764  CD  ARG A  91      73.807 -26.118 -14.239  1.00 37.68           C  
ANISOU  764  CD  ARG A  91     4358   4282   5676   -155    -60    -30       C  
ATOM    765  NE  ARG A  91      73.612 -26.359 -12.818  1.00 40.28           N  
ANISOU  765  NE  ARG A  91     4685   4658   5963   -189    -88    -72       N  
ATOM    766  CZ  ARG A  91      72.464 -26.246 -12.169  1.00 37.84           C  
ANISOU  766  CZ  ARG A  91     4407   4344   5627   -180    -80   -121       C  
ATOM    767  NH1 ARG A  91      72.430 -26.564 -10.886  1.00 39.00           N  
ANISOU  767  NH1 ARG A  91     4557   4540   5722   -218   -101   -154       N  
ATOM    768  NH2 ARG A  91      71.365 -25.795 -12.778  1.00 39.67           N  
ANISOU  768  NH2 ARG A  91     4663   4526   5885   -137    -49   -130       N  
ATOM    769  N  AASP A  92      70.962 -31.245 -15.645  0.53 34.90           N  
ANISOU  769  N  AASP A  92     4071   4007   5180    -18    -42     48       N  
ATOM    770  N  BASP A  92      70.974 -31.278 -15.655  0.47 34.45           N  
ANISOU  770  N  BASP A  92     4015   3952   5124    -18    -42     49       N  
ATOM    771  CA AASP A  92      69.989 -32.180 -15.080  0.53 30.01           C  
ANISOU  771  CA AASP A  92     3459   3415   4527    -13    -55     38       C  
ATOM    772  CA BASP A  92      69.980 -32.197 -15.078  0.47 30.29           C  
ANISOU  772  CA BASP A  92     3495   3451   4562    -13    -55     38       C  
ATOM    773  C  AASP A  92      69.561 -31.735 -13.684  0.53 33.38           C  
ANISOU  773  C  AASP A  92     3863   3872   4949    -28    -74      2       C  
ATOM    774  C  BASP A  92      69.557 -31.737 -13.682  0.47 33.24           C  
ANISOU  774  C  BASP A  92     3845   3855   4931    -28    -74      2       C  
ATOM    775  O  AASP A  92      69.568 -32.508 -12.723  0.53 33.60           O  
ANISOU  775  O  AASP A  92     3880   3938   4950    -36    -83      2       O  
ATOM    776  O  BASP A  92      69.556 -32.507 -12.717  0.47 33.63           O  
ANISOU  776  O  BASP A  92     3883   3942   4952    -36    -83      1       O  
ATOM    777  CB AASP A  92      70.552 -33.605 -15.058  0.53 33.52           C  
ANISOU  777  CB AASP A  92     3908   3871   4957     -4    -36     67       C  
ATOM    778  CB BASP A  92      70.503 -33.642 -15.042  0.47 32.94           C  
ANISOU  778  CB BASP A  92     3835   3798   4882     -4    -37     67       C  
ATOM    779  CG AASP A  92      69.475 -34.639 -14.923  0.53 33.91           C  
ANISOU  779  CG AASP A  92     3982   3931   4973     -4    -41     64       C  
ATOM    780  CG BASP A  92      70.666 -34.251 -16.429  0.47 40.09           C  
ANISOU  780  CG BASP A  92     4789   4666   5779      5      0     88       C  
ATOM    781  OD1AASP A  92      68.286 -34.264 -15.006  0.53 34.58           O  
ANISOU  781  OD1AASP A  92     4074   4019   5047    -11    -60     45       O  
ATOM    782  OD1BASP A  92      69.823 -33.985 -17.313  0.47 50.34           O  
ANISOU  782  OD1BASP A  92     6125   5947   7054     -5     -7     81       O  
ATOM    783  OD2AASP A  92      69.807 -35.825 -14.737  0.53 39.34           O  
ANISOU  783  OD2AASP A  92     4675   4619   5652      4    -22     86       O  
ATOM    784  OD2BASP A  92      71.638 -35.010 -16.635  0.47 57.84           O  
ANISOU  784  OD2BASP A  92     7036   6899   8042     20     41    115       O  
ATOM    785  N   ALA A  93      69.185 -30.461 -13.575  1.00 31.07           N  
ANISOU  785  N   ALA A  93     3569   3556   4680    -33    -72    -29       N  
ATOM    786  CA  ALA A  93      68.892 -29.864 -12.282  1.00 27.72           C  
ANISOU  786  CA  ALA A  93     3138   3146   4247    -54    -72    -76       C  
ATOM    787  C   ALA A  93      68.037 -28.619 -12.499  1.00 30.76           C  
ANISOU  787  C   ALA A  93     3530   3481   4675    -40    -49   -104       C  
ATOM    788  O   ALA A  93      67.959 -28.106 -13.619  1.00 32.00           O  
ANISOU  788  O   ALA A  93     3690   3598   4869    -20    -46    -75       O  
ATOM    789  CB  ALA A  93      70.192 -29.510 -11.533  1.00 30.50           C  
ANISOU  789  CB  ALA A  93     3480   3519   4592    -96    -88    -88       C  
ATOM    790  N   PRO A  94      67.373 -28.123 -11.461  1.00 32.23           N  
ANISOU  790  N   PRO A  94     3722   3665   4858    -48    -24   -153       N  
ATOM    791  CA  PRO A  94      66.641 -26.855 -11.621  1.00 33.63           C  
ANISOU  791  CA  PRO A  94     3902   3779   5096    -27     15   -175       C  
ATOM    792  C   PRO A  94      67.611 -25.749 -11.996  1.00 32.11           C  
ANISOU  792  C   PRO A  94     3725   3536   4939    -47     19   -185       C  
ATOM    793  O   PRO A  94      68.743 -25.705 -11.507  1.00 32.69           O  
ANISOU  793  O   PRO A  94     3809   3630   4983    -95      1   -206       O  
ATOM    794  CB  PRO A  94      66.027 -26.603 -10.238  1.00 32.63           C  
ANISOU  794  CB  PRO A  94     3791   3657   4949    -42     58   -240       C  
ATOM    795  CG  PRO A  94      66.091 -27.923  -9.520  1.00 36.45           C  
ANISOU  795  CG  PRO A  94     4273   4219   5358    -63     32   -233       C  
ATOM    796  CD  PRO A  94      67.311 -28.626 -10.075  1.00 32.02           C  
ANISOU  796  CD  PRO A  94     3704   3689   4775    -79    -22   -188       C  
ATOM    797  N   ALA A  95      67.161 -24.849 -12.875  1.00 31.49           N  
ANISOU  797  N   ALA A  95     3642   3393   4928    -13     39   -161       N  
ATOM    798  CA  ALA A  95      67.993 -23.706 -13.242  1.00 36.33           C  
ANISOU  798  CA  ALA A  95     4273   3947   5585    -33     51   -168       C  
ATOM    799  C   ALA A  95      68.148 -22.710 -12.100  1.00 40.98           C  
ANISOU  799  C   ALA A  95     4895   4492   6185    -72     95   -249       C  
ATOM    800  O   ALA A  95      69.143 -21.973 -12.067  1.00 34.82           O  
ANISOU  800  O   ALA A  95     4134   3680   5415   -119     95   -271       O  
ATOM    801  CB  ALA A  95      67.406 -23.003 -14.472  1.00 37.04           C  
ANISOU  801  CB  ALA A  95     4352   3977   5746     14     61   -108       C  
ATOM    802  N   HIS A  96      67.203 -22.687 -11.159  1.00 34.09           N  
ANISOU  802  N   HIS A  96     4033   3616   5304    -61    139   -298       N  
ATOM    803  CA  HIS A  96      67.193 -21.731 -10.061  1.00 41.08           C  
ANISOU  803  CA  HIS A  96     4969   4448   6191   -101    200   -388       C  
ATOM    804  C   HIS A  96      67.049 -22.461  -8.728  1.00 41.82           C  
ANISOU  804  C   HIS A  96     5086   4612   6192   -143    203   -444       C  
ATOM    805  O   HIS A  96      66.351 -23.471  -8.636  1.00 40.92           O  
ANISOU  805  O   HIS A  96     4941   4554   6050   -110    192   -413       O  
ATOM    806  CB  HIS A  96      66.047 -20.721 -10.280  1.00 35.31           C  
ANISOU  806  CB  HIS A  96     4237   3617   5562    -37    284   -392       C  
ATOM    807  CG  HIS A  96      66.110 -20.059 -11.625  1.00 37.35           C  
ANISOU  807  CG  HIS A  96     4469   3813   5908      6    273   -317       C  
ATOM    808  ND1 HIS A  96      65.172 -20.279 -12.614  1.00 37.11           N  
ANISOU  808  ND1 HIS A  96     4383   3781   5935     79    258   -227       N  
ATOM    809  CD2 HIS A  96      67.037 -19.229 -12.162  1.00 32.77           C  
ANISOU  809  CD2 HIS A  96     3910   3178   5361    -24    266   -310       C  
ATOM    810  CE1 HIS A  96      65.506 -19.589 -13.692  1.00 41.56           C  
ANISOU  810  CE1 HIS A  96     4942   4293   6557     95    244   -167       C  
ATOM    811  NE2 HIS A  96      66.636 -18.948 -13.446  1.00 35.53           N  
ANISOU  811  NE2 HIS A  96     4224   3494   5783     36    254   -217       N  
ATOM    812  N  AILE A  97      67.695 -21.918  -7.690  0.54 45.08           N  
ANISOU  812  N  AILE A  97     5558   5017   6552   -225    218   -524       N  
ATOM    813  N  BILE A  97      67.693 -21.923  -7.690  0.46 45.34           N  
ANISOU  813  N  BILE A  97     5591   5050   6584   -225    218   -524       N  
ATOM    814  CA AILE A  97      67.750 -22.615  -6.407  0.54 53.35           C  
ANISOU  814  CA AILE A  97     6637   6143   7489   -284    207   -569       C  
ATOM    815  CA BILE A  97      67.744 -22.643  -6.419  0.46 53.24           C  
ANISOU  815  CA BILE A  97     6622   6131   7475   -283    206   -567       C  
ATOM    816  C  AILE A  97      66.403 -22.585  -5.691  0.54 49.89           C  
ANISOU  816  C  AILE A  97     6223   5683   7051   -248    298   -616       C  
ATOM    817  C  BILE A  97      66.417 -22.574  -5.664  0.46 49.75           C  
ANISOU  817  C  BILE A  97     6206   5664   7030   -251    299   -618       C  
ATOM    818  O  AILE A  97      66.038 -23.545  -5.000  0.54 46.87           O  
ANISOU  818  O  AILE A  97     5838   5376   6595   -257    289   -613       O  
ATOM    819  O  BILE A  97      66.080 -23.499  -4.917  0.46 47.06           O  
ANISOU  819  O  BILE A  97     5868   5400   6613   -264    291   -620       O  
ATOM    820  CB AILE A  97      68.869 -22.022  -5.526  0.54 59.86           C  
ANISOU  820  CB AILE A  97     7524   6977   8244   -402    183   -637       C  
ATOM    821  CB BILE A  97      68.903 -22.122  -5.550  0.46 60.19           C  
ANISOU  821  CB BILE A  97     7561   7027   8283   -401    176   -630       C  
ATOM    822  CG1AILE A  97      68.949 -22.757  -4.184  0.54 59.38           C  
ANISOU  822  CG1AILE A  97     7500   7009   8053   -474    160   -672       C  
ATOM    823  CG1BILE A  97      69.284 -20.692  -5.941  0.46 62.38           C  
ANISOU  823  CG1BILE A  97     7875   7195   8633   -425    217   -673       C  
ATOM    824  CG2AILE A  97      68.665 -20.527  -5.316  0.54 62.72           C  
ANISOU  824  CG2AILE A  97     7957   7218   8655   -427    273   -724       C  
ATOM    825  CG2BILE A  97      70.110 -23.055  -5.658  0.46 63.70           C  
ANISOU  825  CG2BILE A  97     7957   7572   8675   -443     64   -562       C  
ATOM    826  CD1AILE A  97      69.138 -24.261  -4.313  0.54 61.75           C  
ANISOU  826  CD1AILE A  97     7734   7416   8313   -447     80   -582       C  
ATOM    827  CD1BILE A  97      68.737 -19.628  -5.002  0.46 63.20           C  
ANISOU  827  CD1BILE A  97     8073   7212   8727   -466    323   -789       C  
ATOM    828  N   SER A  98      65.644 -21.507  -5.840  1.00 38.83           N  
ANISOU  828  N   SER A  98     4841   4174   5739   -205    395   -652       N  
ATOM    829  CA  SER A  98      64.399 -21.317  -5.104  1.00 37.40           C  
ANISOU  829  CA  SER A  98     4681   3956   5574   -169    507   -701       C  
ATOM    830  C   SER A  98      63.217 -21.248  -6.060  1.00 35.56           C  
ANISOU  830  C   SER A  98     4365   3674   5470    -53    546   -624       C  
ATOM    831  O   SER A  98      63.373 -21.154  -7.282  1.00 38.99           O  
ANISOU  831  O   SER A  98     4746   4092   5977     -9    491   -545       O  
ATOM    832  CB  SER A  98      64.468 -20.042  -4.255  1.00 43.19           C  
ANISOU  832  CB  SER A  98     5515   4590   6305   -223    614   -818       C  
ATOM    833  OG  SER A  98      65.405 -20.204  -3.210  1.00 43.19           O  
ANISOU  833  OG  SER A  98     5594   4653   6163   -347    573   -889       O  
ATOM    834  N   THR A  99      62.011 -21.289  -5.492  1.00 35.59           N  
ANISOU  834  N   THR A  99     4359   3660   5505     -8    642   -643       N  
ATOM    835  CA  THR A  99      60.808 -21.261  -6.305  1.00 35.63           C  
ANISOU  835  CA  THR A  99     4269   3630   5638     97    673   -558       C  
ATOM    836  C   THR A  99      59.797 -20.292  -5.709  1.00 41.38           C  
ANISOU  836  C   THR A  99     5010   4250   6460    148    834   -608       C  
ATOM    837  O   THR A  99      59.920 -19.829  -4.569  1.00 41.11           O  
ANISOU  837  O   THR A  99     5071   4179   6370     97    931   -720       O  
ATOM    838  CB  THR A  99      60.182 -22.664  -6.450  1.00 40.91           C  
ANISOU  838  CB  THR A  99     4866   4406   6272    118    612   -486       C  
ATOM    839  OG1 THR A  99      59.980 -23.237  -5.154  1.00 40.82           O  
ANISOU  839  OG1 THR A  99     4900   4448   6163     73    660   -552       O  
ATOM    840  CG2 THR A  99      61.071 -23.580  -7.290  1.00 41.64           C  
ANISOU  840  CG2 THR A  99     4938   4580   6304     89    469   -422       C  
ATOM    841  N   ILE A 100      58.794 -19.976  -6.520  1.00 41.31           N  
ANISOU  841  N   ILE A 100     4908   4191   6598    247    866   -518       N  
ATOM    842  CA  ILE A 100      57.658 -19.165  -6.113  1.00 39.97           C  
ANISOU  842  CA  ILE A 100     4715   3918   6554    322   1025   -532       C  
ATOM    843  C   ILE A 100      56.413 -19.966  -6.452  1.00 45.83           C  
ANISOU  843  C   ILE A 100     5329   4721   7364    393   1013   -426       C  
ATOM    844  O   ILE A 100      56.105 -20.159  -7.633  1.00 44.73           O  
ANISOU  844  O   ILE A 100     5093   4605   7299    440    920   -303       O  
ATOM    845  CB  ILE A 100      57.627 -17.804  -6.814  1.00 42.70           C  
ANISOU  845  CB  ILE A 100     5052   4123   7049    382   1082   -504       C  
ATOM    846  CG1 ILE A 100      58.895 -17.005  -6.499  1.00 40.86           C  
ANISOU  846  CG1 ILE A 100     4947   3826   6750    298   1090   -610       C  
ATOM    847  CG2 ILE A 100      56.343 -17.048  -6.423  1.00 40.74           C  
ANISOU  847  CG2 ILE A 100     4760   3761   6957    478   1260   -499       C  
ATOM    848  CD1 ILE A 100      59.035 -15.730  -7.333  1.00 43.56           C  
ANISOU  848  CD1 ILE A 100     5285   4033   7234    347   1124   -570       C  
ATOM    849  N   GLY A 101      55.700 -20.431  -5.427  1.00 43.21           N  
ANISOU  849  N   GLY A 101     4999   4418   6999    391   1103   -470       N  
ATOM    850  CA  GLY A 101      54.427 -21.109  -5.643  1.00 43.50           C  
ANISOU  850  CA  GLY A 101     4908   4504   7116    454   1110   -371       C  
ATOM    851  C   GLY A 101      54.520 -22.446  -6.356  1.00 49.80           C  
ANISOU  851  C   GLY A 101     5644   5434   7844    422    941   -283       C  
ATOM    852  O   GLY A 101      53.595 -22.814  -7.087  1.00 51.62           O  
ANISOU  852  O   GLY A 101     5752   5695   8168    473    899   -167       O  
ATOM    853  N   VAL A 102      55.601 -23.194  -6.158  1.00 38.97           N  
ANISOU  853  N   VAL A 102     4352   4139   6314    336    844   -332       N  
ATOM    854  CA  VAL A 102      55.806 -24.482  -6.823  1.00 40.67           C  
ANISOU  854  CA  VAL A 102     4528   4465   6461    303    697   -260       C  
ATOM    855  C   VAL A 102      55.851 -25.635  -5.826  1.00 48.60           C  
ANISOU  855  C   VAL A 102     5569   5557   7338    244    695   -302       C  
ATOM    856  O   VAL A 102      55.214 -26.667  -6.032  1.00 49.15           O  
ANISOU  856  O   VAL A 102     5573   5696   7405    244    649   -237       O  
ATOM    857  CB  VAL A 102      57.084 -24.472  -7.693  1.00 47.28           C  
ANISOU  857  CB  VAL A 102     5410   5312   7242    265    577   -250       C  
ATOM    858  CG1 VAL A 102      57.295 -25.857  -8.310  1.00 41.66           C  
ANISOU  858  CG1 VAL A 102     4673   4701   6455    229    449   -188       C  
ATOM    859  CG2 VAL A 102      56.994 -23.404  -8.778  1.00 46.00           C  
ANISOU  859  CG2 VAL A 102     5208   5068   7201    320    570   -190       C  
ATOM    860  N   CYS A 103      56.631 -25.493  -4.757  1.00 42.31           N  
ANISOU  860  N   CYS A 103     4881   4763   6432    184    737   -406       N  
ATOM    861  CA  CYS A 103      57.038 -26.640  -3.955  1.00 49.14           C  
ANISOU  861  CA  CYS A 103     5792   5722   7155    114    696   -431       C  
ATOM    862  C   CYS A 103      57.320 -26.167  -2.539  1.00 50.28           C  
ANISOU  862  C   CYS A 103     6044   5851   7209     61    798   -545       C  
ATOM    863  O   CYS A 103      58.009 -25.162  -2.352  1.00 45.75           O  
ANISOU  863  O   CYS A 103     5544   5216   6624     36    827   -616       O  
ATOM    864  CB  CYS A 103      58.277 -27.304  -4.567  1.00 44.70           C  
ANISOU  864  CB  CYS A 103     5254   5215   6514     68    552   -403       C  
ATOM    865  SG  CYS A 103      59.197 -28.397  -3.452  1.00 49.92           S  
ANISOU  865  SG  CYS A 103     5992   5973   7002    -24    502   -439       S  
ATOM    866  N   SER A 104      56.795 -26.884  -1.545  1.00 43.14           N  
ANISOU  866  N   SER A 104     5156   5003   6233     34    851   -562       N  
ATOM    867  CA  SER A 104      56.854 -26.369  -0.181  1.00 44.34           C  
ANISOU  867  CA  SER A 104     5416   5135   6295    -19    970   -673       C  
ATOM    868  C   SER A 104      58.278 -26.332   0.358  1.00 48.28           C  
ANISOU  868  C   SER A 104     6026   5673   6644   -121    892   -734       C  
ATOM    869  O   SER A 104      58.611 -25.441   1.150  1.00 49.52           O  
ANISOU  869  O   SER A 104     6288   5784   6744   -175    972   -838       O  
ATOM    870  CB  SER A 104      55.953 -27.197   0.736  1.00 61.19           C  
ANISOU  870  CB  SER A 104     7542   7328   8380    -29   1045   -667       C  
ATOM    871  OG  SER A 104      54.624 -27.183   0.253  1.00 73.16           O  
ANISOU  871  OG  SER A 104     8941   8809  10047     62   1118   -603       O  
ATOM    872  N   MET A 105      59.138 -27.267  -0.065  1.00 39.46           N  
ANISOU  872  N   MET A 105     4888   4637   5468   -154    741   -671       N  
ATOM    873  CA  MET A 105      60.509 -27.261   0.433  1.00 44.95           C  
ANISOU  873  CA  MET A 105     5666   5378   6036   -250    659   -708       C  
ATOM    874  C   MET A 105      61.345 -26.128  -0.163  1.00 48.40           C  
ANISOU  874  C   MET A 105     6128   5742   6521   -258    634   -745       C  
ATOM    875  O   MET A 105      62.266 -25.647   0.501  1.00 50.27           O  
ANISOU  875  O   MET A 105     6452   5986   6662   -349    616   -812       O  
ATOM    876  CB  MET A 105      61.178 -28.617   0.168  1.00 44.67           C  
ANISOU  876  CB  MET A 105     5589   5440   5942   -270    520   -618       C  
ATOM    877  CG  MET A 105      60.965 -29.656   1.292  1.00 46.76           C  
ANISOU  877  CG  MET A 105     5887   5794   6086   -322    525   -606       C  
ATOM    878  SD  MET A 105      61.723 -29.134   2.853  1.00 51.71           S  
ANISOU  878  SD  MET A 105     6654   6460   6532   -453    547   -703       S  
ATOM    879  CE  MET A 105      63.351 -28.714   2.232  1.00 61.19           C  
ANISOU  879  CE  MET A 105     7854   7665   7731   -497    409   -688       C  
ATOM    880  N   THR A 106      61.074 -25.703  -1.407  1.00 40.64           N  
ANISOU  880  N   THR A 106     5070   4694   5679   -176    625   -696       N  
ATOM    881  CA  THR A 106      61.922 -24.704  -2.061  1.00 38.90           C  
ANISOU  881  CA  THR A 106     4868   4407   5506   -184    595   -716       C  
ATOM    882  C   THR A 106      61.283 -23.324  -2.215  1.00 40.64           C  
ANISOU  882  C   THR A 106     5104   4497   5838   -136    720   -769       C  
ATOM    883  O   THR A 106      61.997 -22.370  -2.565  1.00 39.20           O  
ANISOU  883  O   THR A 106     4958   4247   5688   -157    713   -801       O  
ATOM    884  CB  THR A 106      62.366 -25.175  -3.455  1.00 35.86           C  
ANISOU  884  CB  THR A 106     4400   4040   5185   -140    480   -616       C  
ATOM    885  OG1 THR A 106      61.221 -25.393  -4.281  1.00 39.99           O  
ANISOU  885  OG1 THR A 106     4837   4540   5817    -48    504   -547       O  
ATOM    886  CG2 THR A 106      63.183 -26.472  -3.370  1.00 41.70           C  
ANISOU  886  CG2 THR A 106     5127   4888   5828   -185    365   -563       C  
ATOM    887  N   ASP A 107      59.976 -23.192  -1.994  1.00 38.51           N  
ANISOU  887  N   ASP A 107     4804   4186   5642    -68    838   -771       N  
ATOM    888  CA  ASP A 107      59.304 -21.906  -2.158  1.00 42.63           C  
ANISOU  888  CA  ASP A 107     5329   4573   6296     -5    971   -806       C  
ATOM    889  C   ASP A 107      59.855 -20.879  -1.179  1.00 42.22           C  
ANISOU  889  C   ASP A 107     5415   4448   6176    -85   1064   -943       C  
ATOM    890  O   ASP A 107      60.024 -21.163   0.008  1.00 41.77           O  
ANISOU  890  O   ASP A 107     5450   4441   5981   -170   1099  -1022       O  
ATOM    891  CB  ASP A 107      57.800 -22.054  -1.919  1.00 45.36           C  
ANISOU  891  CB  ASP A 107     5608   4897   6731     78   1093   -779       C  
ATOM    892  CG  ASP A 107      57.033 -22.484  -3.151  1.00 47.43           C  
ANISOU  892  CG  ASP A 107     5723   5174   7124    173   1031   -642       C  
ATOM    893  OD1 ASP A 107      57.640 -22.759  -4.209  1.00 45.97           O  
ANISOU  893  OD1 ASP A 107     5497   5020   6948    174    895   -571       O  
ATOM    894  OD2 ASP A 107      55.793 -22.561  -3.047  1.00 48.54           O  
ANISOU  894  OD2 ASP A 107     5788   5298   7358    242   1121   -603       O  
ATOM    895  N   ILE A 108      60.113 -19.666  -1.669  1.00 40.61           N  
ANISOU  895  N   ILE A 108     5236   4125   6069    -66   1108   -970       N  
ATOM    896  CA  ILE A 108      60.287 -18.538  -0.767  1.00 41.09           C  
ANISOU  896  CA  ILE A 108     5431   4081   6102   -127   1242  -1107       C  
ATOM    897  C   ILE A 108      59.037 -17.682  -0.693  1.00 42.70           C  
ANISOU  897  C   ILE A 108     5621   4146   6459    -24   1438  -1128       C  
ATOM    898  O   ILE A 108      58.977 -16.765   0.143  1.00 45.06           O  
ANISOU  898  O   ILE A 108     6041   4339   6743    -65   1589  -1253       O  
ATOM    899  CB  ILE A 108      61.491 -17.659  -1.171  1.00 48.64           C  
ANISOU  899  CB  ILE A 108     6447   4977   7056   -194   1182  -1143       C  
ATOM    900  CG1 ILE A 108      61.213 -16.963  -2.506  1.00 48.40           C  
ANISOU  900  CG1 ILE A 108     6327   4847   7217    -84   1186  -1054       C  
ATOM    901  CG2 ILE A 108      62.765 -18.494  -1.240  1.00 44.30           C  
ANISOU  901  CG2 ILE A 108     5896   4564   6371   -290    996  -1111       C  
ATOM    902  CD1 ILE A 108      62.364 -16.135  -3.002  1.00 52.06           C  
ANISOU  902  CD1 ILE A 108     6838   5252   7690   -144   1128  -1074       C  
ATOM    903  N   ALA A 109      58.048 -17.939  -1.545  1.00 45.20           N  
ANISOU  903  N   ALA A 109     5793   4455   6925    103   1442  -1006       N  
ATOM    904  CA  ALA A 109      56.812 -17.167  -1.591  1.00 43.70           C  
ANISOU  904  CA  ALA A 109     5554   4137   6914    218   1621   -992       C  
ATOM    905  C   ALA A 109      55.820 -17.948  -2.434  1.00 49.54           C  
ANISOU  905  C   ALA A 109     6117   4942   7764    325   1562   -836       C  
ATOM    906  O   ALA A 109      56.206 -18.816  -3.217  1.00 45.72           O  
ANISOU  906  O   ALA A 109     5564   4568   7239    312   1386   -745       O  
ATOM    907  CB  ALA A 109      57.035 -15.770  -2.183  1.00 46.29           C  
ANISOU  907  CB  ALA A 109     5906   4302   7381    259   1685  -1003       C  
ATOM    908  N   LYS A 110      54.539 -17.629  -2.269  1.00 45.30           N  
ANISOU  908  N   LYS A 110     5508   4334   7371    425   1716   -805       N  
ATOM    909  CA  LYS A 110      53.526 -18.228  -3.127  1.00 51.26           C  
ANISOU  909  CA  LYS A 110     6082   5142   8254    523   1660   -644       C  
ATOM    910  C   LYS A 110      53.246 -17.398  -4.371  1.00 51.03           C  
ANISOU  910  C   LYS A 110     5951   5022   8416    621   1638   -527       C  
ATOM    911  O   LYS A 110      52.898 -17.961  -5.414  1.00 46.30           O  
ANISOU  911  O   LYS A 110     5221   4496   7874    661   1504   -384       O  
ATOM    912  CB  LYS A 110      52.228 -18.444  -2.341  1.00 58.84           C  
ANISOU  912  CB  LYS A 110     6985   6091   9280    581   1824   -643       C  
ATOM    913  CG  LYS A 110      52.416 -19.274  -1.084  1.00 66.90           C  
ANISOU  913  CG  LYS A 110     8108   7204  10108    484   1856   -749       C  
ATOM    914  CD  LYS A 110      51.090 -19.799  -0.559  1.00 80.98           C  
ANISOU  914  CD  LYS A 110     9797   9014  11956    543   1976   -707       C  
ATOM    915  CE  LYS A 110      50.027 -18.708  -0.525  1.00 87.56           C  
ANISOU  915  CE  LYS A 110    10565   9693  13009    665   2189   -688       C  
ATOM    916  NZ  LYS A 110      50.439 -17.519   0.277  1.00 90.40           N  
ANISOU  916  NZ  LYS A 110    11094   9905  13349    642   2371   -847       N  
ATOM    917  N   LYS A 111      53.412 -16.082  -4.295  1.00 44.63           N  
ANISOU  917  N   LYS A 111     5204   4052   7700    651   1762   -583       N  
ATOM    918  CA  LYS A 111      53.192 -15.176  -5.409  1.00 51.17           C  
ANISOU  918  CA  LYS A 111     5949   4778   8715    744   1754   -470       C  
ATOM    919  C   LYS A 111      54.385 -14.243  -5.548  1.00 53.88           C  
ANISOU  919  C   LYS A 111     6423   5028   9021    684   1745   -554       C  
ATOM    920  O   LYS A 111      55.024 -13.897  -4.548  1.00 49.79           O  
ANISOU  920  O   LYS A 111     6061   4465   8393    598   1830   -715       O  
ATOM    921  CB  LYS A 111      51.915 -14.341  -5.209  1.00 52.30           C  
ANISOU  921  CB  LYS A 111     6011   4782   9081    875   1960   -426       C  
ATOM    922  CG  LYS A 111      50.637 -15.167  -5.084  1.00 53.47           C  
ANISOU  922  CG  LYS A 111     6006   5012   9296    940   1985   -329       C  
ATOM    923  CD  LYS A 111      49.436 -14.271  -4.792  1.00 58.04           C  
ANISOU  923  CD  LYS A 111     6504   5442  10108   1074   2213   -289       C  
ATOM    924  CE  LYS A 111      48.171 -15.087  -4.564  1.00 60.79           C  
ANISOU  924  CE  LYS A 111     6696   5874  10527   1131   2250   -196       C  
ATOM    925  NZ  LYS A 111      47.025 -14.194  -4.190  1.00 68.46           N  
ANISOU  925  NZ  LYS A 111     7591   6700  11721   1257   2486   -157       N  
ATOM    926  N   PRO A 112      54.708 -13.811  -6.772  1.00 49.82           N  
ANISOU  926  N   PRO A 112     5853   4486   8592    718   1641   -445       N  
ATOM    927  CA  PRO A 112      55.865 -12.918  -6.955  1.00 49.42           C  
ANISOU  927  CA  PRO A 112     5920   4346   8513    657   1630   -515       C  
ATOM    928  C   PRO A 112      55.640 -11.511  -6.431  1.00 62.95           C  
ANISOU  928  C   PRO A 112     7712   5849  10356    698   1843   -596       C  
ATOM    929  O   PRO A 112      56.577 -10.705  -6.436  1.00 56.63           O  
ANISOU  929  O   PRO A 112     7025   4959   9533    635   1855   -673       O  
ATOM    930  CB  PRO A 112      56.081 -12.928  -8.478  1.00 50.93           C  
ANISOU  930  CB  PRO A 112     6011   4570   8768    695   1469   -352       C  
ATOM    931  CG  PRO A 112      54.762 -13.316  -9.054  1.00 58.85           C  
ANISOU  931  CG  PRO A 112     6843   5612   9904    806   1456   -193       C  
ATOM    932  CD  PRO A 112      54.121 -14.235  -8.056  1.00 58.77           C  
ANISOU  932  CD  PRO A 112     6820   5688   9822    793   1508   -251       C  
ATOM    933  N   THR A 113      54.435 -11.197  -5.964  1.00 55.29           N  
ANISOU  933  N   THR A 113     6687   4794   9527    800   2020   -583       N  
ATOM    934  CA  THR A 113      54.148  -9.904  -5.367  1.00 67.02           C  
ANISOU  934  CA  THR A 113     8258   6065  11142    844   2255   -672       C  
ATOM    935  C   THR A 113      54.583  -9.814  -3.910  1.00 63.42           C  
ANISOU  935  C   THR A 113     7993   5578  10526    730   2387   -894       C  
ATOM    936  O   THR A 113      54.514  -8.730  -3.333  1.00 60.74           O  
ANISOU  936  O   THR A 113     7763   5062  10252    734   2580   -998       O  
ATOM    937  CB  THR A 113      52.650  -9.607  -5.477  1.00 64.71           C  
ANISOU  937  CB  THR A 113     7817   5694  11078   1006   2402   -554       C  
ATOM    938  OG1 THR A 113      51.901 -10.753  -5.042  1.00 63.89           O  
ANISOU  938  OG1 THR A 113     7627   5730  10919   1018   2386   -530       O  
ATOM    939  CG2 THR A 113      52.287  -9.288  -6.921  1.00 60.85           C  
ANISOU  939  CG2 THR A 113     7164   5205  10751   1102   2283   -332       C  
ATOM    940  N   GLU A 114      55.028 -10.912  -3.302  1.00 60.72           N  
ANISOU  940  N   GLU A 114     7699   5407   9965    621   2282   -962       N  
ATOM    941  CA  GLU A 114      55.464 -10.842  -1.915  1.00 59.42           C  
ANISOU  941  CA  GLU A 114     7722   5227   9629    498   2390  -1163       C  
ATOM    942  C   GLU A 114      56.784 -10.070  -1.814  1.00 58.33           C  
ANISOU  942  C   GLU A 114     7745   5019   9399    370   2355  -1279       C  
ATOM    943  O   GLU A 114      57.571  -9.996  -2.765  1.00 62.02           O  
ANISOU  943  O   GLU A 114     8174   5516   9875    350   2194  -1204       O  
ATOM    944  CB  GLU A 114      55.568 -12.250  -1.315  1.00 55.23           C  
ANISOU  944  CB  GLU A 114     7188   4903   8895    417   2278  -1182       C  
ATOM    945  CG  GLU A 114      54.197 -12.925  -1.137  1.00 59.14           C  
ANISOU  945  CG  GLU A 114     7550   5445   9473    525   2358  -1100       C  
ATOM    946  CD  GLU A 114      54.281 -14.402  -0.769  1.00 67.90           C  
ANISOU  946  CD  GLU A 114     8632   6762  10403    456   2221  -1084       C  
ATOM    947  OE1 GLU A 114      53.729 -15.243  -1.516  1.00 67.77           O  
ANISOU  947  OE1 GLU A 114     8453   6849  10446    524   2107   -935       O  
ATOM    948  OE2 GLU A 114      54.899 -14.728   0.267  1.00 66.58           O  
ANISOU  948  OE2 GLU A 114     8610   6654  10033    328   2225  -1216       O  
ATOM    949  N  ATHR A 115      57.015  -9.491  -0.632  0.40 57.84           N  
ANISOU  949  N  ATHR A 115     7868   4864   9245    274   2514  -1466       N  
ATOM    950  N  BTHR A 115      57.009  -9.477  -0.636  0.60 57.86           N  
ANISOU  950  N  BTHR A 115     7871   4865   9250    276   2516  -1466       N  
ATOM    951  CA ATHR A 115      58.121  -8.554  -0.452  0.40 58.52           C  
ANISOU  951  CA ATHR A 115     8117   4848   9271    151   2520  -1588       C  
ATOM    952  CA BTHR A 115      58.127  -8.552  -0.457  0.60 58.37           C  
ANISOU  952  CA BTHR A 115     8098   4829   9252    150   2519  -1587       C  
ATOM    953  C  ATHR A 115      59.479  -9.216  -0.638  0.40 58.48           C  
ANISOU  953  C  ATHR A 115     8136   5011   9073      5   2272  -1588       C  
ATOM    954  C  BTHR A 115      59.473  -9.228  -0.678  0.60 58.62           C  
ANISOU  954  C  BTHR A 115     8148   5030   9095      9   2268  -1582       C  
ATOM    955  O  ATHR A 115      60.427  -8.562  -1.086  0.40 58.47           O  
ANISOU  955  O  ATHR A 115     8186   4953   9079    -62   2205  -1603       O  
ATOM    956  O  BTHR A 115      60.400  -8.606  -1.209  0.60 57.72           O  
ANISOU  956  O  BTHR A 115     8071   4864   8995    -49   2193  -1584       O  
ATOM    957  CB ATHR A 115      58.046  -7.920   0.934  0.40 60.33           C  
ANISOU  957  CB ATHR A 115     8546   4979   9400     54   2722  -1783       C  
ATOM    958  CB BTHR A 115      58.068  -7.931   0.939  0.60 60.49           C  
ANISOU  958  CB BTHR A 115     8567   5000   9416     51   2719  -1785       C  
ATOM    959  OG1ATHR A 115      58.345  -8.912   1.925  0.40 62.38           O  
ANISOU  959  OG1ATHR A 115     8886   5392   9423    -70   2668  -1879       O  
ATOM    960  OG1BTHR A 115      56.824  -7.238   1.099  0.60 63.72           O  
ANISOU  960  OG1BTHR A 115     8924   5310   9977    177   2909  -1731       O  
ATOM    961  CG2ATHR A 115      56.655  -7.374   1.184  0.40 63.21           C  
ANISOU  961  CG2ATHR A 115     8848   5257   9911    189   2922  -1727       C  
ATOM    962  CG2BTHR A 115      59.214  -6.949   1.150  0.60 54.80           C  
ANISOU  962  CG2BTHR A 115     8007   4206   8610    -99   2695  -1892       C  
ATOM    963  N   ILE A 116      59.602 -10.500  -0.293  1.00 57.97           N  
ANISOU  963  N   ILE A 116     8033   5147   8845    -45   2140  -1565       N  
ATOM    964  CA  ILE A 116      60.883 -11.184  -0.430  1.00 52.97           C  
ANISOU  964  CA  ILE A 116     7412   4673   8042   -174   1914  -1554       C  
ATOM    965  C   ILE A 116      61.317 -11.263  -1.887  1.00 50.55           C  
ANISOU  965  C   ILE A 116     6970   4396   7841   -109   1754  -1400       C  
ATOM    966  O   ILE A 116      62.511 -11.392  -2.171  1.00 53.56           O  
ANISOU  966  O   ILE A 116     7371   4846   8132   -209   1602  -1396       O  
ATOM    967  CB  ILE A 116      60.804 -12.582   0.220  1.00 60.16           C  
ANISOU  967  CB  ILE A 116     8298   5780   8779   -220   1822  -1545       C  
ATOM    968  CG1 ILE A 116      62.202 -13.131   0.513  1.00 65.47           C  
ANISOU  968  CG1 ILE A 116     9029   6594   9252   -384   1633  -1575       C  
ATOM    969  CG2 ILE A 116      60.024 -13.543  -0.658  1.00 48.28           C  
ANISOU  969  CG2 ILE A 116     6604   4371   7369    -81   1741  -1376       C  
ATOM    970  CD1 ILE A 116      62.195 -14.567   1.025  1.00 71.26           C  
ANISOU  970  CD1 ILE A 116     9722   7522   9830   -420   1524  -1537       C  
ATOM    971  N   CYS A 117      60.371 -11.169  -2.829  1.00 48.58           N  
ANISOU  971  N   CYS A 117     6582   4095   7781     53   1787  -1267       N  
ATOM    972  CA  CYS A 117      60.679 -11.251  -4.253  1.00 47.42           C  
ANISOU  972  CA  CYS A 117     6314   3979   7727    114   1642  -1113       C  
ATOM    973  C   CYS A 117      61.085  -9.920  -4.867  1.00 50.82           C  
ANISOU  973  C   CYS A 117     6783   4238   8288    126   1695  -1111       C  
ATOM    974  O   CYS A 117      61.645  -9.914  -5.970  1.00 52.10           O  
ANISOU  974  O   CYS A 117     6878   4429   8489    138   1566  -1005       O  
ATOM    975  CB  CYS A 117      59.476 -11.779  -5.034  1.00 58.66           C  
ANISOU  975  CB  CYS A 117     7567   5438   9283    269   1632   -956       C  
ATOM    976  SG  CYS A 117      58.935 -13.416  -4.560  1.00 58.40           S  
ANISOU  976  SG  CYS A 117     7464   5605   9123    266   1555   -926       S  
ATOM    977  N   ALA A 118      60.782  -8.799  -4.209  1.00 51.42           N  
ANISOU  977  N   ALA A 118     6969   4132   8438    124   1892  -1222       N  
ATOM    978  CA  ALA A 118      61.064  -7.487  -4.792  1.00 57.24           C  
ANISOU  978  CA  ALA A 118     7743   4684   9322    146   1962  -1214       C  
ATOM    979  C   ALA A 118      62.511  -7.326  -5.250  1.00 57.86           C  
ANISOU  979  C   ALA A 118     7868   4801   9315     21   1810  -1222       C  
ATOM    980  O   ALA A 118      62.720  -6.905  -6.399  1.00 54.15           O  
ANISOU  980  O   ALA A 118     7326   4286   8963     78   1752  -1103       O  
ATOM    981  CB  ALA A 118      60.652  -6.386  -3.801  1.00 57.13           C  
ANISOU  981  CB  ALA A 118     7876   4465   9367    133   2209  -1368       C  
ATOM    982  N   PRO A 119      63.539  -7.651  -4.451  1.00 55.84           N  
ANISOU  982  N   PRO A 119     7719   4635   8863   -148   1735  -1343       N  
ATOM    983  CA  PRO A 119      64.918  -7.484  -4.941  1.00 54.13           C  
ANISOU  983  CA  PRO A 119     7523   4457   8586   -262   1591  -1332       C  
ATOM    984  C   PRO A 119      65.369  -8.530  -5.962  1.00 55.08           C  
ANISOU  984  C   PRO A 119     7501   4754   8671   -232   1387  -1180       C  
ATOM    985  O   PRO A 119      66.402  -8.318  -6.610  1.00 48.54           O  
ANISOU  985  O   PRO A 119     6664   3940   7837   -293   1285  -1141       O  
ATOM    986  CB  PRO A 119      65.760  -7.569  -3.660  1.00 59.75           C  
ANISOU  986  CB  PRO A 119     8382   5220   9099   -454   1576  -1500       C  
ATOM    987  CG  PRO A 119      64.948  -8.350  -2.726  1.00 63.40           C  
ANISOU  987  CG  PRO A 119     8858   5763   9470   -434   1632  -1551       C  
ATOM    988  CD  PRO A 119      63.519  -7.993  -3.016  1.00 63.08           C  
ANISOU  988  CD  PRO A 119     8756   5600   9613   -255   1797  -1499       C  
ATOM    989  N   LEU A 120      64.649  -9.636  -6.137  1.00 46.57           N  
ANISOU  989  N   LEU A 120     6317   3804   7572   -145   1333  -1097       N  
ATOM    990  CA  LEU A 120      65.083 -10.661  -7.076  1.00 47.86           C  
ANISOU  990  CA  LEU A 120     6365   4126   7693   -125   1154   -967       C  
ATOM    991  C   LEU A 120      64.597 -10.339  -8.483  1.00 47.14           C  
ANISOU  991  C   LEU A 120     6168   3980   7764      2   1139   -812       C  
ATOM    992  O   LEU A 120      63.524  -9.757  -8.675  1.00 49.35           O  
ANISOU  992  O   LEU A 120     6415   4146   8189    114   1254   -772       O  
ATOM    993  CB  LEU A 120      64.559 -12.038  -6.656  1.00 45.11           C  
ANISOU  993  CB  LEU A 120     5959   3938   7243   -103   1097   -946       C  
ATOM    994  CG  LEU A 120      64.886 -12.496  -5.234  1.00 50.18           C  
ANISOU  994  CG  LEU A 120     6698   4654   7716   -221   1106  -1079       C  
ATOM    995  CD1 LEU A 120      64.124 -13.774  -4.906  1.00 46.64           C  
ANISOU  995  CD1 LEU A 120     6183   4337   7202   -172   1076  -1040       C  
ATOM    996  CD2 LEU A 120      66.380 -12.711  -5.074  1.00 51.46           C  
ANISOU  996  CD2 LEU A 120     6902   4902   7748   -365    974  -1110       C  
ATOM    997  N   THR A 121      65.394 -10.730  -9.474  1.00 40.38           N  
ANISOU  997  N   THR A 121     5255   3207   6882    -16    999   -719       N  
ATOM    998  CA  THR A 121      64.995 -10.601 -10.872  1.00 43.97           C  
ANISOU  998  CA  THR A 121     5612   3641   7454     89    959   -561       C  
ATOM    999  C   THR A 121      64.142 -11.814 -11.230  1.00 46.18           C  
ANISOU  999  C   THR A 121     5787   4053   7707    167    890   -468       C  
ATOM   1000  O   THR A 121      64.656 -12.920 -11.431  1.00 47.23           O  
ANISOU 1000  O   THR A 121     5889   4332   7723    126    769   -443       O  
ATOM   1001  CB  THR A 121      66.217 -10.464 -11.775  1.00 44.40           C  
ANISOU 1001  CB  THR A 121     5665   3721   7486     29    857   -507       C  
ATOM   1002  OG1 THR A 121      66.848  -9.198 -11.526  1.00 47.15           O  
ANISOU 1002  OG1 THR A 121     6102   3922   7888    -36    934   -580       O  
ATOM   1003  CG2 THR A 121      65.809 -10.531 -13.250  1.00 41.23           C  
ANISOU 1003  CG2 THR A 121     5167   3329   7168    125    799   -337       C  
ATOM   1004  N   VAL A 122      62.825 -11.596 -11.295  1.00 41.66           N  
ANISOU 1004  N   VAL A 122     5156   3421   7252    278    972   -414       N  
ATOM   1005  CA  VAL A 122      61.845 -12.660 -11.480  1.00 38.99           C  
ANISOU 1005  CA  VAL A 122     4718   3193   6901    346    924   -334       C  
ATOM   1006  C   VAL A 122      61.548 -12.815 -12.966  1.00 45.08           C  
ANISOU 1006  C   VAL A 122     5391   4000   7739    413    826   -162       C  
ATOM   1007  O   VAL A 122      61.317 -11.822 -13.670  1.00 44.60           O  
ANISOU 1007  O   VAL A 122     5308   3826   7811    471    864    -82       O  
ATOM   1008  CB  VAL A 122      60.553 -12.355 -10.698  1.00 40.95           C  
ANISOU 1008  CB  VAL A 122     4946   3366   7247    426   1070   -362       C  
ATOM   1009  CG1 VAL A 122      59.485 -13.395 -11.016  1.00 36.30           C  
ANISOU 1009  CG1 VAL A 122     4236   2888   6668    495   1015   -259       C  
ATOM   1010  CG2 VAL A 122      60.827 -12.295  -9.191  1.00 40.62           C  
ANISOU 1010  CG2 VAL A 122     5020   3303   7110    346   1170   -540       C  
ATOM   1011  N   PHE A 123      61.531 -14.063 -13.437  1.00 38.53           N  
ANISOU 1011  N   PHE A 123     4506   3321   6813    400    702   -103       N  
ATOM   1012  CA  PHE A 123      61.159 -14.376 -14.810  1.00 36.29           C  
ANISOU 1012  CA  PHE A 123     4138   3089   6561    447    602     54       C  
ATOM   1013  C   PHE A 123      59.646 -14.524 -14.910  1.00 40.57           C  
ANISOU 1013  C   PHE A 123     4575   3634   7205    541    627    147       C  
ATOM   1014  O   PHE A 123      59.064 -15.382 -14.238  1.00 41.62           O  
ANISOU 1014  O   PHE A 123     4680   3842   7292    542    633    111       O  
ATOM   1015  CB  PHE A 123      61.841 -15.662 -15.274  1.00 36.70           C  
ANISOU 1015  CB  PHE A 123     4192   3292   6461    382    470     67       C  
ATOM   1016  CG  PHE A 123      61.363 -16.143 -16.613  1.00 41.43           C  
ANISOU 1016  CG  PHE A 123     4720   3957   7066    414    367    214       C  
ATOM   1017  CD1 PHE A 123      61.718 -15.465 -17.777  1.00 45.89           C  
ANISOU 1017  CD1 PHE A 123     5286   4478   7672    421    331    310       C  
ATOM   1018  CD2 PHE A 123      60.536 -17.256 -16.714  1.00 43.02           C  
ANISOU 1018  CD2 PHE A 123     4860   4264   7224    426    308    260       C  
ATOM   1019  CE1 PHE A 123      61.275 -15.904 -19.022  1.00 45.73           C  
ANISOU 1019  CE1 PHE A 123     5213   4526   7637    435    232    447       C  
ATOM   1020  CE2 PHE A 123      60.088 -17.698 -17.955  1.00 48.34           C  
ANISOU 1020  CE2 PHE A 123     5479   5001   7888    435    206    392       C  
ATOM   1021  CZ  PHE A 123      60.469 -17.022 -19.113  1.00 47.54           C  
ANISOU 1021  CZ  PHE A 123     5387   4863   7815    437    166    484       C  
ATOM   1022  N   PHE A 124      59.028 -13.705 -15.760  1.00 42.20           N  
ANISOU 1022  N   PHE A 124     4717   3762   7554    617    639    276       N  
ATOM   1023  CA  PHE A 124      57.597 -13.723 -16.041  1.00 44.80           C  
ANISOU 1023  CA  PHE A 124     4923   4091   8007    711    649    401       C  
ATOM   1024  C   PHE A 124      57.343 -14.173 -17.477  1.00 52.38           C  
ANISOU 1024  C   PHE A 124     5808   5143   8950    713    497    570       C  
ATOM   1025  O   PHE A 124      58.097 -13.828 -18.391  1.00 43.22           O  
ANISOU 1025  O   PHE A 124     4687   3973   7760    682    434    620       O  
ATOM   1026  CB  PHE A 124      56.975 -12.336 -15.848  1.00 42.03           C  
ANISOU 1026  CB  PHE A 124     4545   3566   7858    806    792    436       C  
ATOM   1027  CG  PHE A 124      57.129 -11.775 -14.464  1.00 46.68           C  
ANISOU 1027  CG  PHE A 124     5222   4044   8469    800    962    267       C  
ATOM   1028  CD1 PHE A 124      56.201 -12.083 -13.474  1.00 50.71           C  
ANISOU 1028  CD1 PHE A 124     5696   4556   9016    842   1063    217       C  
ATOM   1029  CD2 PHE A 124      58.174 -10.901 -14.159  1.00 42.41           C  
ANISOU 1029  CD2 PHE A 124     4804   3395   7915    748   1026    160       C  
ATOM   1030  CE1 PHE A 124      56.314 -11.554 -12.198  1.00 45.73           C  
ANISOU 1030  CE1 PHE A 124     5162   3822   8392    829   1230     56       C  
ATOM   1031  CE2 PHE A 124      58.295 -10.358 -12.881  1.00 46.52           C  
ANISOU 1031  CE2 PHE A 124     5420   3811   8444    727   1183     -2       C  
ATOM   1032  CZ  PHE A 124      57.356 -10.691 -11.896  1.00 46.65           C  
ANISOU 1032  CZ  PHE A 124     5411   3830   8483    767   1288    -57       C  
ATOM   1033  N   ASP A 125      56.256 -14.908 -17.685  1.00 49.73           N  
ANISOU 1033  N   ASP A 125     5367   4896   8633    743    441    661       N  
ATOM   1034  CA  ASP A 125      55.942 -15.498 -18.985  1.00 44.56           C  
ANISOU 1034  CA  ASP A 125     4650   4347   7934    722    284    812       C  
ATOM   1035  C   ASP A 125      54.607 -14.927 -19.463  1.00 50.84           C  
ANISOU 1035  C   ASP A 125     5302   5107   8908    815    285    989       C  
ATOM   1036  O   ASP A 125      53.542 -15.312 -18.966  1.00 48.82           O  
ANISOU 1036  O   ASP A 125     4948   4882   8719    856    312   1017       O  
ATOM   1037  CB  ASP A 125      55.917 -17.029 -18.867  1.00 46.21           C  
ANISOU 1037  CB  ASP A 125     4863   4707   7986    649    194    768       C  
ATOM   1038  CG  ASP A 125      55.640 -17.731 -20.189  1.00 49.38           C  
ANISOU 1038  CG  ASP A 125     5226   5222   8316    604     33    902       C  
ATOM   1039  OD1 ASP A 125      55.373 -17.065 -21.207  1.00 50.41           O  
ANISOU 1039  OD1 ASP A 125     5312   5328   8512    630    -20   1046       O  
ATOM   1040  OD2 ASP A 125      55.691 -18.974 -20.205  1.00 50.30           O  
ANISOU 1040  OD2 ASP A 125     5361   5449   8301    537    -40    866       O  
ATOM   1041  N   GLY A 126      54.663 -14.017 -20.436  1.00 50.65           N  
ANISOU 1041  N   GLY A 126     5258   5021   8965    847    255   1119       N  
ATOM   1042  CA  GLY A 126      53.465 -13.367 -20.945  1.00 51.17           C  
ANISOU 1042  CA  GLY A 126     5180   5046   9217    941    251   1311       C  
ATOM   1043  C   GLY A 126      52.438 -14.310 -21.543  1.00 50.38           C  
ANISOU 1043  C   GLY A 126     4958   5092   9093    921    111   1449       C  
ATOM   1044  O   GLY A 126      51.298 -13.890 -21.769  1.00 57.70           O  
ANISOU 1044  O   GLY A 126     5737   5998  10187   1001    111   1610       O  
ATOM   1045  N   ARG A 127      52.804 -15.566 -21.808  1.00 44.14           N  
ANISOU 1045  N   ARG A 127     4221   4444   8106    815     -6   1395       N  
ATOM   1046  CA  ARG A 127      51.828 -16.539 -22.283  1.00 49.54           C  
ANISOU 1046  CA  ARG A 127     4802   5267   8755    778   -135   1505       C  
ATOM   1047  C   ARG A 127      50.878 -16.984 -21.177  1.00 54.37           C  
ANISOU 1047  C   ARG A 127     5320   5888   9449    822    -53   1462       C  
ATOM   1048  O   ARG A 127      49.794 -17.491 -21.476  1.00 65.17           O  
ANISOU 1048  O   ARG A 127     6557   7342  10861    820   -134   1588       O  
ATOM   1049  CB  ARG A 127      52.546 -17.755 -22.889  1.00 44.61           C  
ANISOU 1049  CB  ARG A 127     4282   4773   7895    646   -266   1447       C  
ATOM   1050  CG  ARG A 127      53.347 -17.398 -24.141  1.00 55.23           C  
ANISOU 1050  CG  ARG A 127     5709   6124   9152    595   -355   1515       C  
ATOM   1051  CD  ARG A 127      54.298 -18.509 -24.541  1.00 53.03           C  
ANISOU 1051  CD  ARG A 127     5562   5940   8646    477   -429   1414       C  
ATOM   1052  NE  ARG A 127      55.195 -18.877 -23.449  1.00 48.59           N  
ANISOU 1052  NE  ARG A 127     5092   5345   8024    468   -324   1214       N  
ATOM   1053  CZ  ARG A 127      56.187 -19.751 -23.572  1.00 47.05           C  
ANISOU 1053  CZ  ARG A 127     5012   5206   7659    386   -351   1107       C  
ATOM   1054  NH1 ARG A 127      56.414 -20.332 -24.747  1.00 41.57           N  
ANISOU 1054  NH1 ARG A 127     4368   4592   6833    304   -464   1168       N  
ATOM   1055  NH2 ARG A 127      56.951 -20.037 -22.530  1.00 44.74           N  
ANISOU 1055  NH2 ARG A 127     4786   4887   7328    382   -263    946       N  
ATOM   1056  N   VAL A 128      51.261 -16.801 -19.916  1.00 54.97           N  
ANISOU 1056  N   VAL A 128     5460   5883   9542    855    105   1292       N  
ATOM   1057  CA  VAL A 128      50.433 -17.157 -18.769  1.00 54.23           C  
ANISOU 1057  CA  VAL A 128     5297   5789   9520    897    209   1236       C  
ATOM   1058  C   VAL A 128      49.602 -15.938 -18.382  1.00 58.56           C  
ANISOU 1058  C   VAL A 128     5738   6199  10313   1031    355   1314       C  
ATOM   1059  O   VAL A 128      50.125 -14.817 -18.303  1.00 52.00           O  
ANISOU 1059  O   VAL A 128     4968   5231   9559   1082    453   1284       O  
ATOM   1060  CB  VAL A 128      51.311 -17.637 -17.598  1.00 51.26           C  
ANISOU 1060  CB  VAL A 128     5059   5404   9013    850    301   1012       C  
ATOM   1061  CG1 VAL A 128      50.479 -17.925 -16.360  1.00 52.62           C  
ANISOU 1061  CG1 VAL A 128     5173   5568   9253    892    427    950       C  
ATOM   1062  CG2 VAL A 128      52.142 -18.862 -18.004  1.00 54.41           C  
ANISOU 1062  CG2 VAL A 128     5554   5929   9189    729    166    948       C  
ATOM   1063  N   ASP A 129      48.300 -16.148 -18.159  1.00 56.54           N  
ANISOU 1063  N   ASP A 129     5320   5973  10190   1087    376   1420       N  
ATOM   1064  CA  ASP A 129      47.420 -15.039 -17.815  1.00 60.06           C  
ANISOU 1064  CA  ASP A 129     5645   6285  10891   1226    526   1511       C  
ATOM   1065  C   ASP A 129      47.918 -14.324 -16.567  1.00 51.54           C  
ANISOU 1065  C   ASP A 129     4682   5052   9849   1276    752   1320       C  
ATOM   1066  O   ASP A 129      48.313 -14.955 -15.585  1.00 54.46           O  
ANISOU 1066  O   ASP A 129     5151   5450  10091   1221    814   1140       O  
ATOM   1067  CB  ASP A 129      45.987 -15.527 -17.581  1.00 70.84           C  
ANISOU 1067  CB  ASP A 129     6826   7720  12370   1263    531   1626       C  
ATOM   1068  CG  ASP A 129      45.239 -15.795 -18.871  1.00 87.70           C  
ANISOU 1068  CG  ASP A 129     8835   9980  14508   1218    329   1848       C  
ATOM   1069  OD1 ASP A 129      44.956 -16.978 -19.162  1.00 96.10           O  
ANISOU 1069  OD1 ASP A 129     9842  11189  15480   1140    184   1887       O  
ATOM   1070  OD2 ASP A 129      44.937 -14.823 -19.595  1.00 98.49           O  
ANISOU 1070  OD2 ASP A 129    10163  11298  15962   1251    315   1981       O  
ATOM   1071  N   GLY A 130      47.900 -12.994 -16.613  1.00 53.64           N  
ANISOU 1071  N   GLY A 130     4955   5164  10262   1356    868   1354       N  
ATOM   1072  CA  GLY A 130      48.243 -12.177 -15.476  1.00 57.85           C  
ANISOU 1072  CA  GLY A 130     5604   5542  10833   1391   1090   1181       C  
ATOM   1073  C   GLY A 130      49.715 -11.836 -15.341  1.00 51.96           C  
ANISOU 1073  C   GLY A 130     5042   4717   9985   1341   1108   1026       C  
ATOM   1074  O   GLY A 130      50.049 -10.883 -14.627  1.00 55.48           O  
ANISOU 1074  O   GLY A 130     5589   5012  10480   1365   1280    909       O  
ATOM   1075  N   GLN A 131      50.606 -12.569 -16.010  1.00 51.95           N  
ANISOU 1075  N   GLN A 131     5115   4842   9783   1229    927   1008       N  
ATOM   1076  CA  GLN A 131      52.028 -12.367 -15.745  1.00 44.42           C  
ANISOU 1076  CA  GLN A 131     4347   3850   8682   1145    939    839       C  
ATOM   1077  C   GLN A 131      52.561 -11.082 -16.371  1.00 51.25           C  
ANISOU 1077  C   GLN A 131     5254   4572   9645   1180    971    891       C  
ATOM   1078  O   GLN A 131      53.487 -10.479 -15.815  1.00 53.47           O  
ANISOU 1078  O   GLN A 131     5675   4752   9888   1144   1065    743       O  
ATOM   1079  CB  GLN A 131      52.840 -13.590 -16.194  1.00 42.82           C  
ANISOU 1079  CB  GLN A 131     4206   3818   8244   1020    757    799       C  
ATOM   1080  CG  GLN A 131      52.496 -14.855 -15.381  1.00 47.50           C  
ANISOU 1080  CG  GLN A 131     4790   4534   8726    974    747    714       C  
ATOM   1081  CD  GLN A 131      53.715 -15.654 -14.906  1.00 65.51           C  
ANISOU 1081  CD  GLN A 131     7214   6889  10786    859    700    548       C  
ATOM   1082  OE1 GLN A 131      54.807 -15.569 -15.476  1.00 61.60           O  
ANISOU 1082  OE1 GLN A 131     6806   6404  10197    799    624    525       O  
ATOM   1083  NE2 GLN A 131      53.521 -16.440 -13.852  1.00 68.30           N  
ANISOU 1083  NE2 GLN A 131     7588   7299  11065    830    749    443       N  
ATOM   1084  N   VAL A 132      51.990 -10.615 -17.489  1.00 48.78           N  
ANISOU 1084  N   VAL A 132     4825   4246   9463   1245    897   1102       N  
ATOM   1085  CA  VAL A 132      52.427  -9.316 -18.004  1.00 50.48           C  
ANISOU 1085  CA  VAL A 132     5079   4306   9794   1289    950   1158       C  
ATOM   1086  C   VAL A 132      52.187  -8.238 -16.957  1.00 57.54           C  
ANISOU 1086  C   VAL A 132     6029   5044  10790   1334   1175   1046       C  
ATOM   1087  O   VAL A 132      53.067  -7.413 -16.681  1.00 53.74           O  
ANISOU 1087  O   VAL A 132     5680   4439  10301   1306   1263    935       O  
ATOM   1088  CB  VAL A 132      51.742  -8.978 -19.343  1.00 51.94           C  
ANISOU 1088  CB  VAL A 132     5139   4545  10050   1320    825   1404       C  
ATOM   1089  CG1 VAL A 132      51.987  -7.517 -19.712  1.00 56.00           C  
ANISOU 1089  CG1 VAL A 132     5697   4921  10660   1350    906   1448       C  
ATOM   1090  CG2 VAL A 132      52.283  -9.865 -20.440  1.00 53.72           C  
ANISOU 1090  CG2 VAL A 132     5369   4914  10127   1241    608   1486       C  
ATOM   1091  N   ASP A 133      51.010  -8.255 -16.324  1.00 53.12           N  
ANISOU 1091  N   ASP A 133     5377   4489  10316   1392   1275   1065       N  
ATOM   1092  CA  ASP A 133      50.701  -7.239 -15.321  1.00 57.76           C  
ANISOU 1092  CA  ASP A 133     6022   4930  10996   1431   1498    961       C  
ATOM   1093  C   ASP A 133      51.517  -7.424 -14.047  1.00 54.20           C  
ANISOU 1093  C   ASP A 133     5737   4420  10437   1371   1618    708       C  
ATOM   1094  O   ASP A 133      51.845  -6.437 -13.380  1.00 57.81           O  
ANISOU 1094  O   ASP A 133     6309   4736  10919   1362   1777    589       O  
ATOM   1095  CB  ASP A 133      49.210  -7.251 -15.004  1.00 69.79           C  
ANISOU 1095  CB  ASP A 133     7400   6475  12643   1507   1576   1059       C  
ATOM   1096  CG  ASP A 133      48.368  -6.825 -16.186  1.00 85.37           C  
ANISOU 1096  CG  ASP A 133     9215   8482  14740   1561   1481   1309       C  
ATOM   1097  OD1 ASP A 133      47.575  -7.649 -16.683  1.00 96.22           O  
ANISOU 1097  OD1 ASP A 133    10447   9995  16119   1567   1353   1448       O  
ATOM   1098  OD2 ASP A 133      48.524  -5.671 -16.637  1.00 91.76           O  
ANISOU 1098  OD2 ASP A 133    10046   9183  15638   1590   1527   1368       O  
ATOM   1099  N   LEU A 134      51.846  -8.666 -13.686  1.00 49.89           N  
ANISOU 1099  N   LEU A 134     5208   3982   9766   1322   1545    625       N  
ATOM   1100  CA  LEU A 134      52.773  -8.881 -12.579  1.00 56.28           C  
ANISOU 1100  CA  LEU A 134     6183   4748  10452   1246   1632    390       C  
ATOM   1101  C   LEU A 134      54.127  -8.245 -12.873  1.00 56.05           C  
ANISOU 1101  C   LEU A 134     6299   4650  10349   1165   1598    313       C  
ATOM   1102  O   LEU A 134      54.744  -7.637 -11.991  1.00 56.44           O  
ANISOU 1102  O   LEU A 134     6494   4583  10366   1115   1730    140       O  
ATOM   1103  CB  LEU A 134      52.929 -10.376 -12.304  1.00 55.49           C  
ANISOU 1103  CB  LEU A 134     6082   4854  10147   1156   1500    336       C  
ATOM   1104  CG  LEU A 134      51.654 -11.039 -11.767  1.00 57.64           C  
ANISOU 1104  CG  LEU A 134     6233   5187  10482   1219   1558    377       C  
ATOM   1105  CD1 LEU A 134      51.887 -12.528 -11.511  1.00 61.34           C  
ANISOU 1105  CD1 LEU A 134     6714   5854  10737   1119   1424    321       C  
ATOM   1106  CD2 LEU A 134      51.182 -10.318 -10.509  1.00 59.50           C  
ANISOU 1106  CD2 LEU A 134     6522   5266  10817   1274   1817    253       C  
ATOM   1107  N   PHE A 135      54.597  -8.364 -14.114  1.00 51.30           N  
ANISOU 1107  N   PHE A 135     5660   4119   9713   1141   1423    441       N  
ATOM   1108  CA  PHE A 135      55.839  -7.704 -14.507  1.00 55.30           C  
ANISOU 1108  CA  PHE A 135     6286   4560  10167   1070   1393    392       C  
ATOM   1109  C   PHE A 135      55.724  -6.182 -14.411  1.00 57.16           C  
ANISOU 1109  C   PHE A 135     6561   4586  10570   1127   1555    396       C  
ATOM   1110  O   PHE A 135      56.675  -5.506 -13.998  1.00 57.04           O  
ANISOU 1110  O   PHE A 135     6689   4470  10513   1054   1623    261       O  
ATOM   1111  CB  PHE A 135      56.225  -8.127 -15.924  1.00 50.22           C  
ANISOU 1111  CB  PHE A 135     5586   4036   9458   1041   1187    547       C  
ATOM   1112  CG  PHE A 135      57.421  -7.396 -16.474  1.00 53.21           C  
ANISOU 1112  CG  PHE A 135     6066   4344   9807    979   1159    530       C  
ATOM   1113  CD1 PHE A 135      58.706  -7.764 -16.106  1.00 52.76           C  
ANISOU 1113  CD1 PHE A 135     6134   4344   9569    850   1114    378       C  
ATOM   1114  CD2 PHE A 135      57.260  -6.349 -17.366  1.00 51.42           C  
ANISOU 1114  CD2 PHE A 135     5801   3996   9740   1048   1176    678       C  
ATOM   1115  CE1 PHE A 135      59.806  -7.087 -16.615  1.00 46.18           C  
ANISOU 1115  CE1 PHE A 135     5382   3448   8718    790   1092    369       C  
ATOM   1116  CE2 PHE A 135      58.351  -5.681 -17.876  1.00 49.91           C  
ANISOU 1116  CE2 PHE A 135     5701   3738   9523    987   1156    667       C  
ATOM   1117  CZ  PHE A 135      59.624  -6.057 -17.498  1.00 46.37           C  
ANISOU 1117  CZ  PHE A 135     5374   3349   8896    856   1115    509       C  
ATOM   1118  N   ARG A 136      54.572  -5.622 -14.796  1.00 52.08           N  
ANISOU 1118  N   ARG A 136     5797   3924  10066   1224   1596    548       N  
ATOM   1119  CA  ARG A 136      54.408  -4.171 -14.735  1.00 54.70           C  
ANISOU 1119  CA  ARG A 136     6164   4105  10514   1257   1735    558       C  
ATOM   1120  C   ARG A 136      54.497  -3.651 -13.305  1.00 60.09           C  
ANISOU 1120  C   ARG A 136     6979   4675  11180   1224   1938    348       C  
ATOM   1121  O   ARG A 136      54.842  -2.482 -13.091  1.00 60.35           O  
ANISOU 1121  O   ARG A 136     7105   4568  11259   1208   2052    289       O  
ATOM   1122  CB  ARG A 136      53.068  -3.755 -15.351  1.00 64.31           C  
ANISOU 1122  CB  ARG A 136     7212   5329  11893   1368   1744    767       C  
ATOM   1123  CG  ARG A 136      52.906  -4.035 -16.844  1.00 63.62           C  
ANISOU 1123  CG  ARG A 136     7002   5345  11826   1392   1547    993       C  
ATOM   1124  CD  ARG A 136      51.550  -3.506 -17.321  1.00 69.07           C  
ANISOU 1124  CD  ARG A 136     7529   6031  12682   1490   1573   1192       C  
ATOM   1125  NE  ARG A 136      51.397  -3.507 -18.776  1.00 62.77           N  
ANISOU 1125  NE  ARG A 136     6628   5315  11907   1503   1396   1415       N  
ATOM   1126  CZ  ARG A 136      51.970  -2.623 -19.589  1.00 70.28           C  
ANISOU 1126  CZ  ARG A 136     7618   6197  12886   1495   1369   1488       C  
ATOM   1127  NH1 ARG A 136      52.756  -1.667 -19.100  1.00 69.45           N  
ANISOU 1127  NH1 ARG A 136     7651   5939  12796   1474   1502   1354       N  
ATOM   1128  NH2 ARG A 136      51.770  -2.702 -20.898  1.00 75.61           N  
ANISOU 1128  NH2 ARG A 136     8202   6961  13566   1500   1204   1695       N  
ATOM   1129  N   ASN A 137      54.160  -4.486 -12.320  1.00 61.77           N  
ANISOU 1129  N   ASN A 137     7203   4946  11321   1210   1988    236       N  
ATOM   1130  CA  ASN A 137      54.188  -4.092 -10.916  1.00 66.26           C  
ANISOU 1130  CA  ASN A 137     7903   5424  11847   1168   2178     35       C  
ATOM   1131  C   ASN A 137      55.472  -4.492 -10.204  1.00 64.45           C  
ANISOU 1131  C   ASN A 137     7847   5204  11437   1032   2158   -174       C  
ATOM   1132  O   ASN A 137      55.767  -3.941  -9.138  1.00 71.83           O  
ANISOU 1132  O   ASN A 137     8927   6050  12315    965   2301   -349       O  
ATOM   1133  CB  ASN A 137      53.004  -4.712 -10.163  1.00 69.20           C  
ANISOU 1133  CB  ASN A 137     8195   5853  12245   1225   2264     34       C  
ATOM   1134  CG  ASN A 137      51.662  -4.243 -10.690  1.00 78.21           C  
ANISOU 1134  CG  ASN A 137     9167   6976  13574   1349   2308    231       C  
ATOM   1135  OD1 ASN A 137      51.463  -3.056 -10.945  1.00 75.35           O  
ANISOU 1135  OD1 ASN A 137     8806   6491  13334   1391   2398    287       O  
ATOM   1136  ND2 ASN A 137      50.733  -5.178 -10.855  1.00 89.62           N  
ANISOU 1136  ND2 ASN A 137    10462   8544  15047   1403   2243    341       N  
ATOM   1137  N   ALA A 138      56.231  -5.434 -10.758  1.00 58.28           N  
ANISOU 1137  N   ALA A 138     7054   4528  10562    983   1983   -157       N  
ATOM   1138  CA  ALA A 138      57.415  -5.937 -10.080  1.00 60.08           C  
ANISOU 1138  CA  ALA A 138     7428   4778  10621    849   1952   -344       C  
ATOM   1139  C   ALA A 138      58.559  -4.932 -10.153  1.00 63.82           C  
ANISOU 1139  C   ALA A 138     8037   5145  11067    754   1966   -423       C  
ATOM   1140  O   ALA A 138      58.680  -4.155 -11.104  1.00 58.84           O  
ANISOU 1140  O   ALA A 138     7369   4455  10532    791   1934   -302       O  
ATOM   1141  CB  ALA A 138      57.859  -7.264 -10.688  1.00 56.49           C  
ANISOU 1141  CB  ALA A 138     6906   4560   9999    790   1718   -275       C  
ATOM   1142  N  AARG A 139      59.410  -4.962  -9.129  0.67 62.99           N  
ANISOU 1142  N  AARG A 139     8091   5022  10820    620   2008   -625       N  
ATOM   1143  N  BARG A 139      59.404  -4.954  -9.125  0.34 63.80           N  
ANISOU 1143  N  BARG A 139     8193   5124  10923    620   2010   -626       N  
ATOM   1144  CA AARG A 139      60.563  -4.070  -9.077  0.67 64.28           C  
ANISOU 1144  CA AARG A 139     8389   5097  10939    504   2014   -716       C  
ATOM   1145  CA BARG A 139      60.559  -4.067  -9.085  0.34 64.63           C  
ANISOU 1145  CA BARG A 139     8432   5141  10985    504   2014   -715       C  
ATOM   1146  C  AARG A 139      61.673  -4.535 -10.014  0.67 60.40           C  
ANISOU 1146  C  AARG A 139     7869   4720  10360    430   1808   -646       C  
ATOM   1147  C  BARG A 139      61.653  -4.538 -10.038  0.34 60.30           C  
ANISOU 1147  C  BARG A 139     7853   4707  10350    433   1807   -641       C  
ATOM   1148  O  AARG A 139      62.294  -3.717 -10.705  0.67 57.60           O  
ANISOU 1148  O  AARG A 139     7541   4269  10077    411   1795   -601       O  
ATOM   1149  O  BARG A 139      62.241  -3.729 -10.767  0.34 59.57           O  
ANISOU 1149  O  BARG A 139     7781   4520  10334    420   1792   -590       O  
ATOM   1150  CB AARG A 139      61.080  -3.978  -7.641  0.67 67.01           C  
ANISOU 1150  CB AARG A 139     8907   5423  11131    362   2103   -945       C  
ATOM   1151  CB BARG A 139      61.095  -3.981  -7.657  0.34 67.71           C  
ANISOU 1151  CB BARG A 139     8995   5512  11220    362   2101   -943       C  
ATOM   1152  CG AARG A 139      62.235  -3.019  -7.465  0.67 72.40           C  
ANISOU 1152  CG AARG A 139     9732   6020  11759    225   2111  -1046       C  
ATOM   1153  CG BARG A 139      62.076  -2.854  -7.440  0.34 72.57           C  
ANISOU 1153  CG BARG A 139     9752   6022  11800    241   2137  -1041       C  
ATOM   1154  CD AARG A 139      62.375  -2.581  -6.017  0.67 78.39           C  
ANISOU 1154  CD AARG A 139    10658   6733  12394    108   2240  -1249       C  
ATOM   1155  CD BARG A 139      62.969  -3.127  -6.249  0.34 73.89           C  
ANISOU 1155  CD BARG A 139    10079   6229  11767     56   2132  -1248       C  
ATOM   1156  NE AARG A 139      63.418  -1.571  -5.864  0.67 75.09           N  
ANISOU 1156  NE AARG A 139    10370   6228  11933    -25   2247  -1336       N  
ATOM   1157  NE BARG A 139      62.259  -3.101  -4.975  0.34 76.16           N  
ANISOU 1157  NE BARG A 139    10447   6506  11985     45   2281  -1372       N  
ATOM   1158  CZ AARG A 139      63.236  -0.272  -6.071  0.67 74.51           C  
ANISOU 1158  CZ AARG A 139    10327   6010  11973     12   2357  -1312       C  
ATOM   1159  CZ BARG A 139      62.830  -3.383  -3.809  0.34 69.31           C  
ANISOU 1159  CZ BARG A 139     9721   5689  10926   -113   2288  -1548       C  
ATOM   1160  NH1AARG A 139      64.246   0.567  -5.913  0.67 76.41           N  
ANISOU 1160  NH1AARG A 139    10687   6180  12164   -122   2352  -1397       N  
ATOM   1161  NH1BARG A 139      64.114  -3.714  -3.766  0.34 63.18           N  
ANISOU 1161  NH1BARG A 139     9008   4981  10018   -273   2146  -1613       N  
ATOM   1162  NH2AARG A 139      62.047   0.188  -6.436  0.67 76.90           N  
ANISOU 1162  NH2AARG A 139    10536   6241  12443    178   2468  -1198       N  
ATOM   1163  NH2BARG A 139      62.122  -3.334  -2.689  0.34 69.39           N  
ANISOU 1163  NH2BARG A 139     9805   5687  10873   -119   2432  -1649       N  
ATOM   1164  N   ASN A 140      61.928  -5.839 -10.049  1.00 52.31           N  
ANISOU 1164  N   ASN A 140     6791   3913   9172    385   1649   -628       N  
ATOM   1165  CA  ASN A 140      62.983  -6.425 -10.864  1.00 50.53           C  
ANISOU 1165  CA  ASN A 140     6536   3827   8836    311   1456   -565       C  
ATOM   1166  C   ASN A 140      62.420  -7.628 -11.595  1.00 50.34           C  
ANISOU 1166  C   ASN A 140     6372   3978   8778    383   1322   -425       C  
ATOM   1167  O   ASN A 140      61.770  -8.474 -10.978  1.00 49.25           O  
ANISOU 1167  O   ASN A 140     6201   3931   8580    403   1327   -454       O  
ATOM   1168  CB  ASN A 140      64.165  -6.844  -9.994  1.00 51.23           C  
ANISOU 1168  CB  ASN A 140     6731   4004   8730    144   1396   -718       C  
ATOM   1169  CG  ASN A 140      64.869  -5.657  -9.389  1.00 55.98           C  
ANISOU 1169  CG  ASN A 140     7477   4444   9349     43   1501   -852       C  
ATOM   1170  OD1 ASN A 140      65.598  -4.953 -10.082  1.00 54.12           O  
ANISOU 1170  OD1 ASN A 140     7258   4137   9169      9   1474   -812       O  
ATOM   1171  ND2 ASN A 140      64.637  -5.410  -8.096  1.00 54.74           N  
ANISOU 1171  ND2 ASN A 140     7432   4224   9143    -13   1629  -1014       N  
ATOM   1172  N   GLY A 141      62.652  -7.707 -12.898  1.00 48.45           N  
ANISOU 1172  N   GLY A 141     6057   3781   8569    414   1208   -276       N  
ATOM   1173  CA  GLY A 141      62.035  -8.783 -13.644  1.00 43.94           C  
ANISOU 1173  CA  GLY A 141     5365   3361   7969    476   1088   -143       C  
ATOM   1174  C   GLY A 141      62.511  -8.863 -15.075  1.00 46.11           C  
ANISOU 1174  C   GLY A 141     5589   3688   8242    479    959      1       C  
ATOM   1175  O   GLY A 141      63.070  -7.907 -15.632  1.00 48.39           O  
ANISOU 1175  O   GLY A 141     5914   3872   8601    467    979     36       O  
ATOM   1176  N   VAL A 142      62.285 -10.038 -15.658  1.00 42.28           N  
ANISOU 1176  N   VAL A 142     5029   3366   7670    487    831     83       N  
ATOM   1177  CA  VAL A 142      62.420 -10.275 -17.088  1.00 41.00           C  
ANISOU 1177  CA  VAL A 142     4811   3270   7499    502    711    238       C  
ATOM   1178  C   VAL A 142      61.117 -10.883 -17.581  1.00 48.95           C  
ANISOU 1178  C   VAL A 142     5702   4349   8548    587    661    366       C  
ATOM   1179  O   VAL A 142      60.566 -11.784 -16.937  1.00 46.92           O  
ANISOU 1179  O   VAL A 142     5414   4179   8236    590    654    321       O  
ATOM   1180  CB  VAL A 142      63.614 -11.194 -17.409  1.00 39.80           C  
ANISOU 1180  CB  VAL A 142     4695   3251   7174    402    595    204       C  
ATOM   1181  CG1 VAL A 142      63.525 -11.673 -18.837  1.00 35.52           C  
ANISOU 1181  CG1 VAL A 142     4098   2796   6602    419    479    357       C  
ATOM   1182  CG2 VAL A 142      64.921 -10.419 -17.185  1.00 41.81           C  
ANISOU 1182  CG2 VAL A 142     5042   3429   7416    318    631    119       C  
ATOM   1183  N   LEU A 143      60.622 -10.382 -18.710  1.00 40.29           N  
ANISOU 1183  N   LEU A 143     4540   3218   7549    649    624    534       N  
ATOM   1184  CA  LEU A 143      59.341 -10.783 -19.276  1.00 42.53           C  
ANISOU 1184  CA  LEU A 143     4702   3562   7894    725    568    683       C  
ATOM   1185  C   LEU A 143      59.554 -11.254 -20.708  1.00 46.65           C  
ANISOU 1185  C   LEU A 143     5199   4190   8335    693    414    824       C  
ATOM   1186  O   LEU A 143      60.255 -10.589 -21.478  1.00 45.61           O  
ANISOU 1186  O   LEU A 143     5111   4008   8212    672    397    877       O  
ATOM   1187  CB  LEU A 143      58.360  -9.599 -19.262  1.00 40.01           C  
ANISOU 1187  CB  LEU A 143     4315   3088   7798    840    677    779       C  
ATOM   1188  CG  LEU A 143      57.040  -9.789 -20.011  1.00 47.13           C  
ANISOU 1188  CG  LEU A 143     5069   4040   8798    924    610    977       C  
ATOM   1189  CD1 LEU A 143      56.168 -10.816 -19.313  1.00 47.20           C  
ANISOU 1189  CD1 LEU A 143     5009   4152   8774    936    604    940       C  
ATOM   1190  CD2 LEU A 143      56.289  -8.468 -20.161  1.00 44.77           C  
ANISOU 1190  CD2 LEU A 143     4703   3570   8737   1041    717   1097       C  
ATOM   1191  N   ILE A 144      58.962 -12.392 -21.074  1.00 39.71           N  
ANISOU 1191  N   ILE A 144     4259   3456   7372    680    307    882       N  
ATOM   1192  CA  ILE A 144      58.880 -12.772 -22.482  1.00 38.20           C  
ANISOU 1192  CA  ILE A 144     4040   3359   7116    653    167   1034       C  
ATOM   1193  C   ILE A 144      57.424 -12.721 -22.930  1.00 45.03           C  
ANISOU 1193  C   ILE A 144     4771   4245   8093    726    121   1204       C  
ATOM   1194  O   ILE A 144      56.500 -12.996 -22.156  1.00 43.47           O  
ANISOU 1194  O   ILE A 144     4497   4054   7965    775    166   1186       O  
ATOM   1195  CB  ILE A 144      59.481 -14.157 -22.788  1.00 37.03           C  
ANISOU 1195  CB  ILE A 144     3943   3364   6763    557     64    977       C  
ATOM   1196  CG1 ILE A 144      58.787 -15.248 -21.975  1.00 41.74           C  
ANISOU 1196  CG1 ILE A 144     4495   4046   7316    555     56    911       C  
ATOM   1197  CG2 ILE A 144      61.012 -14.144 -22.559  1.00 37.32           C  
ANISOU 1197  CG2 ILE A 144     4095   3382   6702    487     98    846       C  
ATOM   1198  CD1 ILE A 144      59.147 -16.645 -22.409  1.00 41.64           C  
ANISOU 1198  CD1 ILE A 144     4521   4177   7124    471    -49    886       C  
ATOM   1199  N   THR A 145      57.220 -12.351 -24.191  1.00 44.11           N  
ANISOU 1199  N   THR A 145     4621   4144   7995    729     30   1380       N  
ATOM   1200  CA  THR A 145      55.896 -12.418 -24.798  1.00 45.45           C  
ANISOU 1200  CA  THR A 145     4655   4365   8250    777    -53   1570       C  
ATOM   1201  C   THR A 145      56.023 -12.889 -26.235  1.00 53.23           C  
ANISOU 1201  C   THR A 145     5657   5470   9099    698   -219   1703       C  
ATOM   1202  O   THR A 145      57.103 -12.863 -26.829  1.00 53.24           O  
ANISOU 1202  O   THR A 145     5768   5478   8980    631   -242   1669       O  
ATOM   1203  CB  THR A 145      55.160 -11.075 -24.799  1.00 47.85           C  
ANISOU 1203  CB  THR A 145     4866   4524   8792    896     29   1703       C  
ATOM   1204  OG1 THR A 145      55.882 -10.137 -25.614  1.00 49.55           O  
ANISOU 1204  OG1 THR A 145     5142   4659   9025    890     26   1777       O  
ATOM   1205  CG2 THR A 145      55.014 -10.543 -23.391  1.00 47.24           C  
ANISOU 1205  CG2 THR A 145     4789   4312   8849    971    214   1565       C  
ATOM   1206  N   GLU A 146      54.890 -13.304 -26.793  1.00 49.87           N  
ANISOU 1206  N   GLU A 146     5119   5138   8692    702   -331   1859       N  
ATOM   1207  CA  GLU A 146      54.831 -13.677 -28.194  1.00 51.59           C  
ANISOU 1207  CA  GLU A 146     5350   5470   8783    620   -496   2006       C  
ATOM   1208  C   GLU A 146      54.467 -12.514 -29.104  1.00 56.48           C  
ANISOU 1208  C   GLU A 146     5908   6027   9526    672   -533   2223       C  
ATOM   1209  O   GLU A 146      54.678 -12.609 -30.317  1.00 62.97           O  
ANISOU 1209  O   GLU A 146     6773   6925  10227    596   -656   2338       O  
ATOM   1210  CB  GLU A 146      53.826 -14.814 -28.385  1.00 51.35           C  
ANISOU 1210  CB  GLU A 146     5237   5588   8684    568   -621   2065       C  
ATOM   1211  CG  GLU A 146      54.237 -16.109 -27.719  1.00 44.43           C  
ANISOU 1211  CG  GLU A 146     4436   4789   7655    497   -609   1871       C  
ATOM   1212  CD  GLU A 146      53.165 -17.183 -27.854  1.00 59.26           C  
ANISOU 1212  CD  GLU A 146     6229   6801   9486    445   -724   1932       C  
ATOM   1213  OE1 GLU A 146      51.966 -16.831 -27.852  1.00 61.13           O  
ANISOU 1213  OE1 GLU A 146     6310   7042   9875    505   -757   2083       O  
ATOM   1214  OE2 GLU A 146      53.519 -18.370 -27.986  1.00 54.45           O  
ANISOU 1214  OE2 GLU A 146     5704   6289   8696    343   -780   1837       O  
ATOM   1215  N   GLY A 147      53.936 -11.424 -28.553  1.00 56.89           N  
ANISOU 1215  N   GLY A 147     5865   5938   9811    797   -424   2283       N  
ATOM   1216  CA  GLY A 147      53.550 -10.272 -29.344  1.00 61.71           C  
ANISOU 1216  CA  GLY A 147     6407   6473  10568    863   -447   2502       C  
ATOM   1217  C   GLY A 147      53.796  -8.962 -28.625  1.00 61.22           C  
ANISOU 1217  C   GLY A 147     6347   6199  10714    978   -262   2462       C  
ATOM   1218  O   GLY A 147      54.524  -8.925 -27.628  1.00 64.25           O  
ANISOU 1218  O   GLY A 147     6822   6504  11087    979   -127   2247       O  
ATOM   1219  N   SER A 148      53.188  -7.884 -29.114  1.00 60.03           N  
ANISOU 1219  N   SER A 148     6123   6004  10681   1027   -240   2603       N  
ATOM   1220  CA  SER A 148      53.428  -6.560 -28.559  1.00 60.89           C  
ANISOU 1220  CA  SER A 148     6259   5932  10944   1105    -58   2542       C  
ATOM   1221  C   SER A 148      52.832  -6.425 -27.162  1.00 64.81           C  
ANISOU 1221  C   SER A 148     6704   6345  11576   1185    107   2409       C  
ATOM   1222  O   SER A 148      51.816  -7.043 -26.829  1.00 66.03           O  
ANISOU 1222  O   SER A 148     6747   6583  11761   1206     81   2439       O  
ATOM   1223  CB  SER A 148      52.836  -5.483 -29.471  1.00 70.80           C  
ANISOU 1223  CB  SER A 148     7438   7167  12294   1138    -82   2741       C  
ATOM   1224  OG  SER A 148      53.425  -5.522 -30.759  1.00 81.38           O  
ANISOU 1224  OG  SER A 148     8842   8580  13501   1059   -222   2860       O  
ATOM   1225  N   VAL A 149      53.478  -5.598 -26.343  1.00 63.59           N  
ANISOU 1225  N   VAL A 149     6639   6025  11496   1221    283   2258       N  
ATOM   1226  CA  VAL A 149      52.974  -5.197 -25.034  1.00 62.08           C  
ANISOU 1226  CA  VAL A 149     6427   5729  11434   1293    469   2130       C  
ATOM   1227  C   VAL A 149      52.769  -3.690 -25.066  1.00 68.59           C  
ANISOU 1227  C   VAL A 149     7242   6403  12415   1358    600   2180       C  
ATOM   1228  O   VAL A 149      53.683  -2.947 -25.444  1.00 59.55           O  
ANISOU 1228  O   VAL A 149     6196   5171  11258   1333    624   2165       O  
ATOM   1229  CB  VAL A 149      53.943  -5.589 -23.903  1.00 63.18           C  
ANISOU 1229  CB  VAL A 149     6698   5802  11504   1260    569   1882       C  
ATOM   1230  CG1 VAL A 149      53.430  -5.076 -22.563  1.00 61.13           C  
ANISOU 1230  CG1 VAL A 149     6436   5429  11363   1323    771   1747       C  
ATOM   1231  CG2 VAL A 149      54.145  -7.094 -23.870  1.00 61.05           C  
ANISOU 1231  CG2 VAL A 149     6432   5675  11091   1201    443   1838       C  
ATOM   1232  N   LYS A 150      51.576  -3.241 -24.672  1.00 66.66           N  
ANISOU 1232  N   LYS A 150     6880   6126  12323   1438    689   2244       N  
ATOM   1233  CA  LYS A 150      51.241  -1.827 -24.776  1.00 69.69           C  
ANISOU 1233  CA  LYS A 150     7237   6371  12872   1507    811   2319       C  
ATOM   1234  C   LYS A 150      52.209  -0.984 -23.955  1.00 65.42           C  
ANISOU 1234  C   LYS A 150     6852   5652  12354   1503    987   2124       C  
ATOM   1235  O   LYS A 150      52.424  -1.243 -22.767  1.00 71.62           O  
ANISOU 1235  O   LYS A 150     7708   6385  13117   1496   1106   1926       O  
ATOM   1236  CB  LYS A 150      49.798  -1.580 -24.322  1.00 70.04           C  
ANISOU 1236  CB  LYS A 150     7128   6402  13080   1593    900   2402       C  
ATOM   1237  CG  LYS A 150      49.308  -0.173 -24.625  1.00 82.88           C  
ANISOU 1237  CG  LYS A 150     8699   7902  14892   1669   1003   2528       C  
ATOM   1238  CD  LYS A 150      47.890   0.074 -24.119  1.00 93.48           C  
ANISOU 1238  CD  LYS A 150     9890   9220  16410   1757   1109   2610       C  
ATOM   1239  CE  LYS A 150      47.881   0.716 -22.734  1.00 97.42           C  
ANISOU 1239  CE  LYS A 150    10463   9544  17006   1808   1364   2420       C  
ATOM   1240  NZ  LYS A 150      46.503   1.115 -22.301  1.00 94.83           N  
ANISOU 1240  NZ  LYS A 150     9989   9172  16869   1900   1490   2517       N  
ATOM   1241  N   GLY A 151      52.812   0.006 -24.607  1.00 62.38           N  
ANISOU 1241  N   GLY A 151     6523   5178  11999   1497    998   2180       N  
ATOM   1242  CA  GLY A 151      53.675   0.962 -23.946  1.00 69.15           C  
ANISOU 1242  CA  GLY A 151     7522   5860  12892   1486   1161   2018       C  
ATOM   1243  C   GLY A 151      55.083   0.493 -23.660  1.00 77.25           C  
ANISOU 1243  C   GLY A 151     8707   6884  13760   1387   1137   1839       C  
ATOM   1244  O   GLY A 151      55.814   1.197 -22.956  1.00 84.90           O  
ANISOU 1244  O   GLY A 151     9800   7714  14744   1360   1272   1679       O  
ATOM   1245  N   LEU A 152      55.494  -0.666 -24.177  1.00 62.17           N  
ANISOU 1245  N   LEU A 152     6800   5120  11700   1325    970   1860       N  
ATOM   1246  CA  LEU A 152      56.844  -1.174 -23.960  1.00 64.85           C  
ANISOU 1246  CA  LEU A 152     7280   5464  11897   1228    942   1705       C  
ATOM   1247  C   LEU A 152      57.515  -1.490 -25.288  1.00 66.60           C  
ANISOU 1247  C   LEU A 152     7519   5775  12012   1167    775   1838       C  
ATOM   1248  O   LEU A 152      56.930  -2.173 -26.135  1.00 63.14           O  
ANISOU 1248  O   LEU A 152     6988   5476  11526   1172    627   1997       O  
ATOM   1249  CB  LEU A 152      56.826  -2.425 -23.081  1.00 62.24           C  
ANISOU 1249  CB  LEU A 152     6958   5216  11475   1201    928   1564       C  
ATOM   1250  CG  LEU A 152      56.344  -2.180 -21.653  1.00 63.25           C  
ANISOU 1250  CG  LEU A 152     7101   5255  11675   1240   1105   1401       C  
ATOM   1251  CD1 LEU A 152      56.426  -3.441 -20.833  1.00 66.82           C  
ANISOU 1251  CD1 LEU A 152     7571   5794  12023   1205   1083   1263       C  
ATOM   1252  CD2 LEU A 152      57.161  -1.064 -21.020  1.00 70.93           C  
ANISOU 1252  CD2 LEU A 152     8211   6057  12682   1206   1258   1251       C  
ATOM   1253  N   GLN A 153      58.745  -0.999 -25.461  1.00 55.86           N  
ANISOU 1253  N   GLN A 153     6281   4337  10607   1100    800   1770       N  
ATOM   1254  CA  GLN A 153      59.545  -1.369 -26.622  1.00 54.26           C  
ANISOU 1254  CA  GLN A 153     6117   4215  10284   1028    661   1869       C  
ATOM   1255  C   GLN A 153      60.145  -2.751 -26.404  1.00 54.55           C  
ANISOU 1255  C   GLN A 153     6197   4358  10172    956    577   1773       C  
ATOM   1256  O   GLN A 153      60.763  -2.987 -25.364  1.00 49.60           O  
ANISOU 1256  O   GLN A 153     5645   3679   9522    918    659   1577       O  
ATOM   1257  CB  GLN A 153      60.664  -0.365 -26.865  1.00 59.56           C  
ANISOU 1257  CB  GLN A 153     6899   4766  10966    975    726   1832       C  
ATOM   1258  CG  GLN A 153      60.161   0.977 -27.350  1.00 81.31           C  
ANISOU 1258  CG  GLN A 153     9615   7423  13858   1040    785   1961       C  
ATOM   1259  CD  GLN A 153      58.971   0.831 -28.282  1.00 92.07           C  
ANISOU 1259  CD  GLN A 153    10838   8891  15252   1106    674   2190       C  
ATOM   1260  OE1 GLN A 153      57.839   1.143 -27.911  1.00100.62           O  
ANISOU 1260  OE1 GLN A 153    11820   9952  16459   1193    729   2236       O  
ATOM   1261  NE2 GLN A 153      59.220   0.347 -29.496  1.00 93.03           N  
ANISOU 1261  NE2 GLN A 153    10956   9133  15258   1056    518   2337       N  
ATOM   1262  N   PRO A 154      59.978  -3.677 -27.345  1.00 53.87           N  
ANISOU 1262  N   PRO A 154     6068   4421   9979    929    416   1906       N  
ATOM   1263  CA  PRO A 154      60.528  -5.022 -27.188  1.00 49.21           C  
ANISOU 1263  CA  PRO A 154     5525   3998   9176    833    332   1777       C  
ATOM   1264  C   PRO A 154      61.943  -5.140 -27.729  1.00 52.46           C  
ANISOU 1264  C   PRO A 154     6052   4449   9432    721    301   1718       C  
ATOM   1265  O   PRO A 154      62.377  -4.382 -28.597  1.00 48.95           O  
ANISOU 1265  O   PRO A 154     5639   3945   9016    709    294   1833       O  
ATOM   1266  CB  PRO A 154      59.568  -5.877 -28.026  1.00 49.43           C  
ANISOU 1266  CB  PRO A 154     5456   4191   9132    841    176   1940       C  
ATOM   1267  CG  PRO A 154      59.170  -4.949 -29.136  1.00 54.14           C  
ANISOU 1267  CG  PRO A 154     6005   4729   9837    889    134   2182       C  
ATOM   1268  CD  PRO A 154      59.107  -3.569 -28.532  1.00 57.75           C  
ANISOU 1268  CD  PRO A 154     6464   5005  10474    959    297   2139       C  
ATOM   1269  N   SER A 155      62.661  -6.119 -27.191  1.00 47.84           N  
ANISOU 1269  N   SER A 155     5524   3966   8688    640    287   1542       N  
ATOM   1270  CA  SER A 155      63.909  -6.599 -27.768  1.00 49.20           C  
ANISOU 1270  CA  SER A 155     5783   4223   8689    533    238   1496       C  
ATOM   1271  C   SER A 155      63.634  -7.969 -28.373  1.00 44.42           C  
ANISOU 1271  C   SER A 155     5160   3812   7907    490    108   1529       C  
ATOM   1272  O   SER A 155      63.163  -8.871 -27.673  1.00 44.92           O  
ANISOU 1272  O   SER A 155     5190   3953   7924    495     90   1442       O  
ATOM   1273  CB  SER A 155      65.014  -6.679 -26.715  1.00 51.16           C  
ANISOU 1273  CB  SER A 155     6106   4436   8898    470    321   1281       C  
ATOM   1274  OG  SER A 155      66.083  -7.504 -27.160  1.00 46.39           O  
ANISOU 1274  OG  SER A 155     5557   3950   8118    374    265   1231       O  
ATOM   1275  N   VAL A 156      63.903  -8.113 -29.668  1.00 40.78           N  
ANISOU 1275  N   VAL A 156     4728   3423   7343    442     23   1655       N  
ATOM   1276  CA  VAL A 156      63.627  -9.368 -30.362  1.00 44.38           C  
ANISOU 1276  CA  VAL A 156     5186   4054   7623    388    -98   1692       C  
ATOM   1277  C   VAL A 156      64.657 -10.406 -29.939  1.00 46.78           C  
ANISOU 1277  C   VAL A 156     5561   4438   7775    310    -81   1513       C  
ATOM   1278  O   VAL A 156      65.866 -10.208 -30.113  1.00 42.41           O  
ANISOU 1278  O   VAL A 156     5081   3859   7176    257    -33   1457       O  
ATOM   1279  CB  VAL A 156      63.639  -9.158 -31.881  1.00 47.79           C  
ANISOU 1279  CB  VAL A 156     5647   4534   7978    348   -184   1877       C  
ATOM   1280  CG1 VAL A 156      63.486 -10.490 -32.586  1.00 48.04           C  
ANISOU 1280  CG1 VAL A 156     5708   4740   7804    270   -296   1888       C  
ATOM   1281  CG2 VAL A 156      62.514  -8.213 -32.288  1.00 48.42           C  
ANISOU 1281  CG2 VAL A 156     5636   4547   8214    430   -217   2079       C  
ATOM   1282  N   GLY A 157      64.183 -11.529 -29.393  1.00 43.81           N  
ANISOU 1282  N   GLY A 157     5158   4159   7330    305   -119   1433       N  
ATOM   1283  CA  GLY A 157      65.076 -12.554 -28.896  1.00 39.52           C  
ANISOU 1283  CA  GLY A 157     4669   3685   6662    244   -100   1272       C  
ATOM   1284  C   GLY A 157      65.556 -13.493 -29.985  1.00 40.21           C  
ANISOU 1284  C   GLY A 157     4823   3890   6566    165   -166   1303       C  
ATOM   1285  O   GLY A 157      65.309 -13.284 -31.177  1.00 39.67           O  
ANISOU 1285  O   GLY A 157     4774   3850   6448    142   -227   1444       O  
ATOM   1286  N   PRO A 158      66.272 -14.544 -29.600  1.00 40.32           N  
ANISOU 1286  N   PRO A 158     4878   3970   6473    118   -150   1173       N  
ATOM   1287  CA  PRO A 158      66.742 -15.516 -30.595  1.00 40.27           C  
ANISOU 1287  CA  PRO A 158     4945   4062   6292     44   -190   1186       C  
ATOM   1288  C   PRO A 158      65.566 -16.239 -31.234  1.00 44.19           C  
ANISOU 1288  C   PRO A 158     5428   4654   6708     27   -297   1272       C  
ATOM   1289  O   PRO A 158      64.430 -16.203 -30.748  1.00 42.81           O  
ANISOU 1289  O   PRO A 158     5172   4483   6610     74   -340   1305       O  
ATOM   1290  CB  PRO A 158      67.621 -16.473 -29.783  1.00 46.37           C  
ANISOU 1290  CB  PRO A 158     5742   4868   7010     19   -138   1027       C  
ATOM   1291  CG  PRO A 158      67.121 -16.355 -28.390  1.00 45.74           C  
ANISOU 1291  CG  PRO A 158     5591   4750   7036     74   -116    945       C  
ATOM   1292  CD  PRO A 158      66.621 -14.935 -28.223  1.00 40.34           C  
ANISOU 1292  CD  PRO A 158     4862   3959   6507    130    -92   1015       C  
ATOM   1293  N   LYS A 159      65.848 -16.886 -32.367  1.00 40.43           N  
ANISOU 1293  N   LYS A 159     5035   4254   6071    -49   -337   1313       N  
ATOM   1294  CA  LYS A 159      64.800 -17.631 -33.062  1.00 46.34           C  
ANISOU 1294  CA  LYS A 159     5788   5101   6717    -93   -449   1391       C  
ATOM   1295  C   LYS A 159      64.458 -18.925 -32.338  1.00 43.84           C  
ANISOU 1295  C   LYS A 159     5459   4848   6349   -105   -463   1278       C  
ATOM   1296  O   LYS A 159      63.317 -19.395 -32.427  1.00 40.34           O  
ANISOU 1296  O   LYS A 159     4972   4467   5887   -117   -554   1331       O  
ATOM   1297  CB  LYS A 159      65.220 -17.928 -34.502  1.00 43.01           C  
ANISOU 1297  CB  LYS A 159     5481   4738   6121   -186   -480   1459       C  
ATOM   1298  CG  LYS A 159      65.242 -16.690 -35.420  1.00 51.94           C  
ANISOU 1298  CG  LYS A 159     6622   5827   7285   -184   -499   1617       C  
ATOM   1299  CD  LYS A 159      65.862 -17.011 -36.770  1.00 56.40           C  
ANISOU 1299  CD  LYS A 159     7321   6447   7661   -284   -504   1661       C  
ATOM   1300  CE  LYS A 159      65.879 -15.787 -37.677  1.00 66.75           C  
ANISOU 1300  CE  LYS A 159     8644   7720   9000   -287   -525   1829       C  
ATOM   1301  NZ  LYS A 159      66.593 -16.079 -38.945  1.00 73.67           N  
ANISOU 1301  NZ  LYS A 159     9663   8646   9683   -388   -508   1861       N  
ATOM   1302  N   GLN A 160      65.419 -19.507 -31.623  1.00 39.80           N  
ANISOU 1302  N   GLN A 160     4979   4322   5821   -104   -378   1132       N  
ATOM   1303  CA  GLN A 160      65.262 -20.815 -31.003  1.00 40.02           C  
ANISOU 1303  CA  GLN A 160     5011   4407   5789   -122   -381   1026       C  
ATOM   1304  C   GLN A 160      64.901 -20.698 -29.522  1.00 40.70           C  
ANISOU 1304  C   GLN A 160     5002   4456   6005    -50   -351    950       C  
ATOM   1305  O   GLN A 160      65.149 -19.681 -28.865  1.00 44.26           O  
ANISOU 1305  O   GLN A 160     5407   4828   6582      6   -298    939       O  
ATOM   1306  CB  GLN A 160      66.535 -21.659 -31.162  1.00 38.06           C  
ANISOU 1306  CB  GLN A 160     4855   4169   5438   -166   -304    925       C  
ATOM   1307  CG  GLN A 160      67.719 -21.261 -30.258  1.00 39.84           C  
ANISOU 1307  CG  GLN A 160     5057   4328   5751   -124   -203    835       C  
ATOM   1308  CD  GLN A 160      68.582 -20.145 -30.860  1.00 40.49           C  
ANISOU 1308  CD  GLN A 160     5165   4351   5868   -127   -154    889       C  
ATOM   1309  OE1 GLN A 160      68.109 -19.348 -31.672  1.00 40.85           O  
ANISOU 1309  OE1 GLN A 160     5218   4384   5920   -132   -196   1003       O  
ATOM   1310  NE2 GLN A 160      69.851 -20.092 -30.454  1.00 39.97           N  
ANISOU 1310  NE2 GLN A 160     5106   4250   5830   -126    -67    816       N  
ATOM   1311  N   ALA A 161      64.292 -21.766 -29.010  1.00 37.68           N  
ANISOU 1311  N   ALA A 161     4601   4131   5586    -61   -382    897       N  
ATOM   1312  CA  ALA A 161      63.998 -21.901 -27.594  1.00 33.87           C  
ANISOU 1312  CA  ALA A 161     4046   3629   5195     -7   -348    813       C  
ATOM   1313  C   ALA A 161      64.101 -23.374 -27.236  1.00 35.25           C  
ANISOU 1313  C   ALA A 161     4254   3865   5274    -45   -349    724       C  
ATOM   1314  O   ALA A 161      64.291 -24.233 -28.101  1.00 38.74           O  
ANISOU 1314  O   ALA A 161     4773   4355   5591   -111   -374    728       O  
ATOM   1315  CB  ALA A 161      62.615 -21.338 -27.242  1.00 37.84           C  
ANISOU 1315  CB  ALA A 161     4447   4123   5809     45   -393    890       C  
ATOM   1316  N   SER A 162      63.991 -23.664 -25.945  1.00 32.96           N  
ANISOU 1316  N   SER A 162     3915   3567   5042     -8   -314    640       N  
ATOM   1317  CA  SER A 162      64.161 -25.019 -25.439  1.00 33.76           C  
ANISOU 1317  CA  SER A 162     4042   3714   5071    -35   -304    556       C  
ATOM   1318  C   SER A 162      62.798 -25.617 -25.125  1.00 33.18           C  
ANISOU 1318  C   SER A 162     3914   3689   5005    -38   -364    579       C  
ATOM   1319  O   SER A 162      62.021 -25.035 -24.365  1.00 36.19           O  
ANISOU 1319  O   SER A 162     4210   4050   5489     13   -361    594       O  
ATOM   1320  CB  SER A 162      65.041 -25.034 -24.186  1.00 36.64           C  
ANISOU 1320  CB  SER A 162     4394   4048   5482     -4   -229    455       C  
ATOM   1321  OG  SER A 162      65.187 -26.343 -23.669  1.00 37.32           O  
ANISOU 1321  OG  SER A 162     4498   4174   5507    -24   -221    388       O  
ATOM   1322  N   LEU A 163      62.522 -26.792 -25.675  1.00 33.59           N  
ANISOU 1322  N   LEU A 163     4014   3797   4950   -102   -407    578       N  
ATOM   1323  CA  LEU A 163      61.280 -27.500 -25.379  1.00 35.74           C  
ANISOU 1323  CA  LEU A 163     4236   4122   5224   -120   -466    596       C  
ATOM   1324  C   LEU A 163      61.646 -28.890 -24.873  1.00 35.64           C  
ANISOU 1324  C   LEU A 163     4272   4129   5139   -152   -434    503       C  
ATOM   1325  O   LEU A 163      62.153 -29.716 -25.640  1.00 37.54           O  
ANISOU 1325  O   LEU A 163     4609   4383   5271   -213   -433    482       O  
ATOM   1326  CB  LEU A 163      60.375 -27.573 -26.610  1.00 33.71           C  
ANISOU 1326  CB  LEU A 163     3986   3915   4906   -184   -569    704       C  
ATOM   1327  CG  LEU A 163      59.081 -28.379 -26.415  1.00 34.98           C  
ANISOU 1327  CG  LEU A 163     4091   4138   5063   -223   -642    733       C  
ATOM   1328  CD1 LEU A 163      58.225 -27.795 -25.314  1.00 40.93           C  
ANISOU 1328  CD1 LEU A 163     4710   4876   5965   -142   -626    753       C  
ATOM   1329  CD2 LEU A 163      58.278 -28.467 -27.720  1.00 35.63           C  
ANISOU 1329  CD2 LEU A 163     4188   4282   5069   -309   -761    847       C  
ATOM   1330  N   ASN A 164      61.412 -29.136 -23.581  1.00 30.35           N  
ANISOU 1330  N   ASN A 164     3544   3456   4531   -110   -400    448       N  
ATOM   1331  CA  ASN A 164      61.757 -30.421 -22.967  1.00 35.06           C  
ANISOU 1331  CA  ASN A 164     4177   4067   5075   -132   -367    370       C  
ATOM   1332  C   ASN A 164      63.212 -30.798 -23.242  1.00 38.02           C  
ANISOU 1332  C   ASN A 164     4639   4414   5394   -141   -306    317       C  
ATOM   1333  O   ASN A 164      63.542 -31.950 -23.512  1.00 32.87           O  
ANISOU 1333  O   ASN A 164     4055   3769   4667   -182   -290    283       O  
ATOM   1334  CB  ASN A 164      60.802 -31.507 -23.448  1.00 32.74           C  
ANISOU 1334  CB  ASN A 164     3902   3823   4715   -202   -431    394       C  
ATOM   1335  CG  ASN A 164      59.371 -31.112 -23.260  1.00 37.69           C  
ANISOU 1335  CG  ASN A 164     4427   4483   5411   -195   -494    465       C  
ATOM   1336  OD1 ASN A 164      59.013 -30.591 -22.207  1.00 35.86           O  
ANISOU 1336  OD1 ASN A 164     4111   4238   5277   -130   -460    455       O  
ATOM   1337  ND2 ASN A 164      58.545 -31.306 -24.285  1.00 38.38           N  
ANISOU 1337  ND2 ASN A 164     4518   4614   5450   -263   -584    542       N  
ATOM   1338  N   GLY A 165      64.096 -29.810 -23.181  1.00 38.67           N  
ANISOU 1338  N   GLY A 165     4715   4458   5520   -102   -265    313       N  
ATOM   1339  CA  GLY A 165      65.509 -30.056 -23.374  1.00 40.50           C  
ANISOU 1339  CA  GLY A 165     5004   4663   5720   -104   -202    274       C  
ATOM   1340  C   GLY A 165      65.972 -30.084 -24.810  1.00 40.64           C  
ANISOU 1340  C   GLY A 165     5107   4674   5662   -148   -197    307       C  
ATOM   1341  O   GLY A 165      67.172 -30.234 -25.046  1.00 40.43           O  
ANISOU 1341  O   GLY A 165     5123   4621   5618   -145   -130    282       O  
ATOM   1342  N   VAL A 166      65.065 -29.952 -25.771  1.00 34.05           N  
ANISOU 1342  N   VAL A 166     4295   3864   4778   -191   -264    368       N  
ATOM   1343  CA  VAL A 166      65.390 -29.937 -27.196  1.00 34.13           C  
ANISOU 1343  CA  VAL A 166     4400   3874   4694   -248   -266    406       C  
ATOM   1344  C   VAL A 166      65.389 -28.492 -27.648  1.00 37.54           C  
ANISOU 1344  C   VAL A 166     4800   4289   5176   -225   -289    480       C  
ATOM   1345  O   VAL A 166      64.341 -27.831 -27.612  1.00 37.03           O  
ANISOU 1345  O   VAL A 166     4668   4240   5160   -213   -361    546       O  
ATOM   1346  CB  VAL A 166      64.368 -30.741 -28.017  1.00 36.64           C  
ANISOU 1346  CB  VAL A 166     4774   4240   4908   -331   -340    435       C  
ATOM   1347  CG1 VAL A 166      64.751 -30.760 -29.499  1.00 36.42           C  
ANISOU 1347  CG1 VAL A 166     4866   4214   4758   -404   -337    466       C  
ATOM   1348  CG2 VAL A 166      64.214 -32.139 -27.455  1.00 38.86           C  
ANISOU 1348  CG2 VAL A 166     5079   4528   5157   -353   -319    364       C  
ATOM   1349  N   THR A 167      66.536 -27.996 -28.107  1.00 36.57           N  
ANISOU 1349  N   THR A 167     4718   4129   5046   -218   -224    478       N  
ATOM   1350  CA  THR A 167      66.581 -26.635 -28.623  1.00 37.91           C  
ANISOU 1350  CA  THR A 167     4868   4275   5261   -202   -241    554       C  
ATOM   1351  C   THR A 167      66.181 -26.645 -30.090  1.00 40.16           C  
ANISOU 1351  C   THR A 167     5235   4592   5432   -274   -293    633       C  
ATOM   1352  O   THR A 167      66.744 -27.400 -30.890  1.00 42.22           O  
ANISOU 1352  O   THR A 167     5602   4861   5577   -332   -253    606       O  
ATOM   1353  CB  THR A 167      67.963 -26.010 -28.447  1.00 39.95           C  
ANISOU 1353  CB  THR A 167     5129   4481   5571   -172   -152    526       C  
ATOM   1354  OG1 THR A 167      68.270 -25.950 -27.052  1.00 41.57           O  
ANISOU 1354  OG1 THR A 167     5258   4666   5871   -120   -121    460       O  
ATOM   1355  CG2 THR A 167      67.944 -24.592 -28.995  1.00 37.29           C  
ANISOU 1355  CG2 THR A 167     4774   4109   5283   -160   -168    609       C  
ATOM   1356  N   LEU A 168      65.198 -25.819 -30.438  1.00 37.06           N  
ANISOU 1356  N   LEU A 168     4795   4215   5073   -273   -379    733       N  
ATOM   1357  CA  LEU A 168      64.653 -25.863 -31.784  1.00 35.97           C  
ANISOU 1357  CA  LEU A 168     4726   4124   4816   -354   -456    824       C  
ATOM   1358  C   LEU A 168      64.055 -24.511 -32.164  1.00 41.14           C  
ANISOU 1358  C   LEU A 168     5316   4769   5548   -326   -521    955       C  
ATOM   1359  O   LEU A 168      63.669 -23.713 -31.308  1.00 38.10           O  
ANISOU 1359  O   LEU A 168     4819   4346   5311   -246   -522    975       O  
ATOM   1360  CB  LEU A 168      63.605 -26.973 -31.888  1.00 36.09           C  
ANISOU 1360  CB  LEU A 168     4756   4206   4752   -420   -537    819       C  
ATOM   1361  CG  LEU A 168      62.419 -26.881 -30.919  1.00 45.68           C  
ANISOU 1361  CG  LEU A 168     5837   5439   6080   -372   -602    843       C  
ATOM   1362  CD1 LEU A 168      61.290 -26.080 -31.545  1.00 42.90           C  
ANISOU 1362  CD1 LEU A 168     5419   5125   5756   -386   -719    992       C  
ATOM   1363  CD2 LEU A 168      61.903 -28.276 -30.493  1.00 44.95           C  
ANISOU 1363  CD2 LEU A 168     5759   5388   5933   -418   -621    772       C  
ATOM   1364  N   ILE A 169      63.984 -24.275 -33.470  1.00 39.64           N  
ANISOU 1364  N   ILE A 169     5201   4610   5250   -397   -571   1048       N  
ATOM   1365  CA  ILE A 169      63.219 -23.179 -34.048  1.00 41.47           C  
ANISOU 1365  CA  ILE A 169     5377   4850   5529   -389   -660   1204       C  
ATOM   1366  C   ILE A 169      61.835 -23.733 -34.371  1.00 46.61           C  
ANISOU 1366  C   ILE A 169     5995   5587   6127   -450   -797   1280       C  
ATOM   1367  O   ILE A 169      61.696 -24.624 -35.214  1.00 43.06           O  
ANISOU 1367  O   ILE A 169     5650   5204   5508   -561   -846   1277       O  
ATOM   1368  CB  ILE A 169      63.912 -22.616 -35.293  1.00 36.68           C  
ANISOU 1368  CB  ILE A 169     4872   4237   4826   -441   -645   1276       C  
ATOM   1369  CG1 ILE A 169      65.305 -22.083 -34.909  1.00 46.06           C  
ANISOU 1369  CG1 ILE A 169     6079   5341   6082   -384   -507   1201       C  
ATOM   1370  CG2 ILE A 169      63.055 -21.528 -35.957  1.00 38.16           C  
ANISOU 1370  CG2 ILE A 169     5002   4440   5058   -438   -751   1460       C  
ATOM   1371  CD1 ILE A 169      66.075 -21.457 -36.060  1.00 45.53           C  
ANISOU 1371  CD1 ILE A 169     6105   5259   5937   -428   -472   1271       C  
ATOM   1372  N   GLY A 170      60.816 -23.224 -33.684  1.00 44.43           N  
ANISOU 1372  N   GLY A 170     5574   5307   5999   -382   -851   1346       N  
ATOM   1373  CA  GLY A 170      59.509 -23.863 -33.726  1.00 38.66           C  
ANISOU 1373  CA  GLY A 170     4784   4658   5248   -431   -970   1404       C  
ATOM   1374  C   GLY A 170      58.793 -23.635 -35.043  1.00 45.21           C  
ANISOU 1374  C   GLY A 170     5633   5564   5979   -524  -1111   1571       C  
ATOM   1375  O   GLY A 170      58.831 -22.548 -35.619  1.00 43.26           O  
ANISOU 1375  O   GLY A 170     5366   5296   5774   -498  -1135   1696       O  
ATOM   1376  N   GLU A 171      58.113 -24.681 -35.517  1.00 42.73           N  
ANISOU 1376  N   GLU A 171     5362   5343   5532   -640  -1210   1578       N  
ATOM   1377  CA  GLU A 171      57.224 -24.573 -36.666  1.00 47.84           C  
ANISOU 1377  CA  GLU A 171     6011   6084   6083   -747  -1373   1745       C  
ATOM   1378  C   GLU A 171      55.769 -24.785 -36.294  1.00 45.10           C  
ANISOU 1378  C   GLU A 171     5508   5803   5824   -753  -1498   1840       C  
ATOM   1379  O   GLU A 171      54.897 -24.081 -36.804  1.00 47.69           O  
ANISOU 1379  O   GLU A 171     5735   6178   6206   -759  -1621   2030       O  
ATOM   1380  CB  GLU A 171      57.628 -25.576 -37.751  1.00 50.97           C  
ANISOU 1380  CB  GLU A 171     6605   6541   6218   -912  -1401   1690       C  
ATOM   1381  CG  GLU A 171      59.098 -25.491 -38.145  1.00 51.48           C  
ANISOU 1381  CG  GLU A 171     6827   6542   6192   -910  -1260   1591       C  
ATOM   1382  CD  GLU A 171      59.478 -26.483 -39.234  1.00 66.10           C  
ANISOU 1382  CD  GLU A 171     8886   8444   7787  -1073  -1265   1531       C  
ATOM   1383  OE1 GLU A 171      58.659 -27.375 -39.554  1.00 66.06           O  
ANISOU 1383  OE1 GLU A 171     8915   8517   7669  -1194  -1370   1536       O  
ATOM   1384  OE2 GLU A 171      60.600 -26.372 -39.773  1.00 67.63           O  
ANISOU 1384  OE2 GLU A 171     9212   8595   7890  -1086  -1156   1478       O  
ATOM   1385  N   ALA A 172      55.493 -25.738 -35.409  1.00 39.99           N  
ANISOU 1385  N   ALA A 172     4832   5160   5202   -750  -1466   1723       N  
ATOM   1386  CA  ALA A 172      54.156 -25.941 -34.864  1.00 50.21           C  
ANISOU 1386  CA  ALA A 172     5962   6507   6609   -740  -1557   1800       C  
ATOM   1387  C   ALA A 172      53.925 -25.135 -33.597  1.00 47.62           C  
ANISOU 1387  C   ALA A 172     5468   6098   6528   -566  -1467   1800       C  
ATOM   1388  O   ALA A 172      52.790 -25.055 -33.124  1.00 49.62           O  
ANISOU 1388  O   ALA A 172     5560   6382   6911   -532  -1525   1888       O  
ATOM   1389  CB  ALA A 172      53.920 -27.432 -34.570  1.00 48.07           C  
ANISOU 1389  CB  ALA A 172     5751   6282   6233   -838  -1568   1676       C  
ATOM   1390  N   VAL A 173      54.980 -24.548 -33.039  1.00 41.35           N  
ANISOU 1390  N   VAL A 173     4712   5200   5798   -463  -1321   1702       N  
ATOM   1391  CA  VAL A 173      54.909 -23.761 -31.816  1.00 44.80           C  
ANISOU 1391  CA  VAL A 173     5025   5549   6449   -310  -1216   1676       C  
ATOM   1392  C   VAL A 173      55.842 -22.569 -32.001  1.00 50.44           C  
ANISOU 1392  C   VAL A 173     5778   6171   7216   -236  -1135   1689       C  
ATOM   1393  O   VAL A 173      56.806 -22.634 -32.768  1.00 44.23           O  
ANISOU 1393  O   VAL A 173     5130   5382   6293   -296  -1119   1656       O  
ATOM   1394  CB  VAL A 173      55.289 -24.608 -30.573  1.00 47.07           C  
ANISOU 1394  CB  VAL A 173     5331   5805   6748   -278  -1107   1489       C  
ATOM   1395  CG1 VAL A 173      56.780 -24.995 -30.588  1.00 39.73           C  
ANISOU 1395  CG1 VAL A 173     4562   4832   5703   -298  -1005   1335       C  
ATOM   1396  CG2 VAL A 173      54.903 -23.892 -29.284  1.00 59.65           C  
ANISOU 1396  CG2 VAL A 173     6788   7326   8552   -141  -1017   1475       C  
ATOM   1397  N   LYS A 174      55.522 -21.456 -31.340  1.00 41.23           N  
ANISOU 1397  N   LYS A 174     4490   4925   6252   -111  -1079   1745       N  
ATOM   1398  CA  LYS A 174      56.321 -20.236 -31.444  1.00 42.62           C  
ANISOU 1398  CA  LYS A 174     4692   4999   6502    -40   -998   1763       C  
ATOM   1399  C   LYS A 174      57.471 -20.302 -30.448  1.00 44.52           C  
ANISOU 1399  C   LYS A 174     5002   5159   6755      6   -848   1569       C  
ATOM   1400  O   LYS A 174      57.258 -20.587 -29.263  1.00 43.15           O  
ANISOU 1400  O   LYS A 174     4774   4960   6661     60   -781   1470       O  
ATOM   1401  CB  LYS A 174      55.450 -19.007 -31.184  1.00 50.67           C  
ANISOU 1401  CB  LYS A 174     5558   5955   7740     72   -994   1910       C  
ATOM   1402  CG  LYS A 174      56.019 -17.701 -31.700  1.00 65.59           C  
ANISOU 1402  CG  LYS A 174     7470   7753   9696    121   -956   1994       C  
ATOM   1403  CD  LYS A 174      54.896 -16.711 -31.955  1.00 73.54           C  
ANISOU 1403  CD  LYS A 174     8325   8735  10883    197  -1011   2207       C  
ATOM   1404  CE  LYS A 174      55.416 -15.287 -32.054  1.00 83.88           C  
ANISOU 1404  CE  LYS A 174     9638   9910  12321    282   -926   2267       C  
ATOM   1405  NZ  LYS A 174      56.510 -15.147 -33.055  1.00 89.92           N  
ANISOU 1405  NZ  LYS A 174    10550  10684  12931    203   -942   2268       N  
ATOM   1406  N   THR A 175      58.696 -20.080 -30.935  1.00 41.90           N  
ANISOU 1406  N   THR A 175     4788   4793   6338    -22   -798   1519       N  
ATOM   1407  CA  THR A 175      59.881 -20.084 -30.078  1.00 36.72           C  
ANISOU 1407  CA  THR A 175     4191   4066   5694     11   -668   1354       C  
ATOM   1408  C   THR A 175      60.570 -18.727 -30.057  1.00 42.61           C  
ANISOU 1408  C   THR A 175     4941   4703   6545     73   -590   1378       C  
ATOM   1409  O   THR A 175      61.561 -18.553 -29.331  1.00 43.15           O  
ANISOU 1409  O   THR A 175     5047   4708   6639     97   -488   1254       O  
ATOM   1410  CB  THR A 175      60.885 -21.171 -30.519  1.00 36.58           C  
ANISOU 1410  CB  THR A 175     4310   4098   5492    -78   -654   1250       C  
ATOM   1411  OG1 THR A 175      61.179 -21.032 -31.918  1.00 39.56           O  
ANISOU 1411  OG1 THR A 175     4772   4508   5750   -152   -707   1341       O  
ATOM   1412  CG2 THR A 175      60.321 -22.578 -30.257  1.00 39.30           C  
ANISOU 1412  CG2 THR A 175     4658   4525   5749   -133   -700   1188       C  
ATOM   1413  N   GLN A 176      60.051 -17.765 -30.810  1.00 44.88           N  
ANISOU 1413  N   GLN A 176     5184   4967   6899     95   -641   1541       N  
ATOM   1414  CA  GLN A 176      60.614 -16.430 -30.958  1.00 50.99           C  
ANISOU 1414  CA  GLN A 176     5965   5632   7776    146   -575   1591       C  
ATOM   1415  C   GLN A 176      59.894 -15.495 -29.992  1.00 51.14           C  
ANISOU 1415  C   GLN A 176     5868   5552   8012    259   -515   1613       C  
ATOM   1416  O   GLN A 176      58.700 -15.232 -30.158  1.00 49.67           O  
ANISOU 1416  O   GLN A 176     5576   5380   7917    300   -577   1749       O  
ATOM   1417  CB  GLN A 176      60.421 -15.969 -32.399  1.00 55.97           C  
ANISOU 1417  CB  GLN A 176     6621   6297   8349    102   -668   1772       C  
ATOM   1418  CG  GLN A 176      60.651 -14.515 -32.614  1.00 66.91           C  
ANISOU 1418  CG  GLN A 176     7986   7568   9870    164   -619   1870       C  
ATOM   1419  CD  GLN A 176      62.098 -14.241 -32.817  1.00 50.93           C  
ANISOU 1419  CD  GLN A 176     6075   5493   7784    130   -532   1786       C  
ATOM   1420  OE1 GLN A 176      62.630 -14.454 -33.906  1.00 62.65           O  
ANISOU 1420  OE1 GLN A 176     7651   7031   9123     50   -570   1835       O  
ATOM   1421  NE2 GLN A 176      62.763 -13.789 -31.769  1.00 62.00           N  
ANISOU 1421  NE2 GLN A 176     7474   6795   9290    180   -414   1658       N  
ATOM   1422  N   PHE A 177      60.604 -14.996 -28.984  1.00 40.24           N  
ANISOU 1422  N   PHE A 177     4505   4070   6714    305   -391   1484       N  
ATOM   1423  CA  PHE A 177      59.988 -14.151 -27.970  1.00 39.31           C  
ANISOU 1423  CA  PHE A 177     4300   3845   6792    405   -308   1475       C  
ATOM   1424  C   PHE A 177      60.489 -12.720 -28.076  1.00 44.54           C  
ANISOU 1424  C   PHE A 177     4979   4365   7578    451   -227   1517       C  
ATOM   1425  O   PHE A 177      61.617 -12.475 -28.508  1.00 40.67           O  
ANISOU 1425  O   PHE A 177     4580   3853   7020    402   -205   1485       O  
ATOM   1426  CB  PHE A 177      60.289 -14.665 -26.561  1.00 42.34           C  
ANISOU 1426  CB  PHE A 177     4696   4215   7176    414   -221   1283       C  
ATOM   1427  CG  PHE A 177      59.972 -16.114 -26.367  1.00 43.70           C  
ANISOU 1427  CG  PHE A 177     4866   4515   7224    364   -284   1224       C  
ATOM   1428  CD1 PHE A 177      58.725 -16.618 -26.709  1.00 49.04           C  
ANISOU 1428  CD1 PHE A 177     5458   5270   7907    368   -374   1331       C  
ATOM   1429  CD2 PHE A 177      60.927 -16.977 -25.855  1.00 39.20           C  
ANISOU 1429  CD2 PHE A 177     4374   3984   6536    309   -255   1070       C  
ATOM   1430  CE1 PHE A 177      58.433 -17.971 -26.532  1.00 42.29           C  
ANISOU 1430  CE1 PHE A 177     4606   4525   6937    313   -430   1273       C  
ATOM   1431  CE2 PHE A 177      60.652 -18.331 -25.676  1.00 43.18           C  
ANISOU 1431  CE2 PHE A 177     4881   4594   6931    264   -305   1017       C  
ATOM   1432  CZ  PHE A 177      59.404 -18.823 -26.014  1.00 40.71           C  
ANISOU 1432  CZ  PHE A 177     4494   4352   6621    264   -390   1114       C  
ATOM   1433  N   ASN A 178      59.630 -11.784 -27.674  1.00 39.93           N  
ANISOU 1433  N   ASN A 178     4306   3680   7186    548   -176   1592       N  
ATOM   1434  CA  ASN A 178      60.064 -10.455 -27.281  1.00 47.22           C  
ANISOU 1434  CA  ASN A 178     5249   4434   8258    603    -55   1574       C  
ATOM   1435  C   ASN A 178      60.547 -10.496 -25.838  1.00 45.70           C  
ANISOU 1435  C   ASN A 178     5096   4178   8090    608     67   1364       C  
ATOM   1436  O   ASN A 178      59.977 -11.202 -25.000  1.00 43.73           O  
ANISOU 1436  O   ASN A 178     4806   3978   7833    624     78   1285       O  
ATOM   1437  CB  ASN A 178      58.917  -9.440 -27.402  1.00 45.17           C  
ANISOU 1437  CB  ASN A 178     4878   4076   8208    712    -31   1741       C  
ATOM   1438  CG  ASN A 178      58.542  -9.129 -28.839  1.00 51.11           C  
ANISOU 1438  CG  ASN A 178     5595   4871   8954    705   -149   1971       C  
ATOM   1439  OD1 ASN A 178      59.378  -9.136 -29.737  1.00 53.38           O  
ANISOU 1439  OD1 ASN A 178     5969   5195   9119    631   -200   2001       O  
ATOM   1440  ND2 ASN A 178      57.271  -8.823 -29.057  1.00 51.41           N  
ANISOU 1440  ND2 ASN A 178     5501   4904   9129    783   -189   2144       N  
ATOM   1441  N   TYR A 179      61.594  -9.727 -25.543  1.00 42.81           N  
ANISOU 1441  N   TYR A 179     4810   3704   7750    587    155   1277       N  
ATOM   1442  CA  TYR A 179      62.159  -9.646 -24.201  1.00 39.85           C  
ANISOU 1442  CA  TYR A 179     4486   3266   7388    573    264   1082       C  
ATOM   1443  C   TYR A 179      62.033  -8.239 -23.641  1.00 42.83           C  
ANISOU 1443  C   TYR A 179     4870   3451   7952    635    398   1069       C  
ATOM   1444  O   TYR A 179      62.194  -7.251 -24.371  1.00 44.95           O  
ANISOU 1444  O   TYR A 179     5147   3623   8309    656    414   1179       O  
ATOM   1445  CB  TYR A 179      63.638 -10.040 -24.191  1.00 41.90           C  
ANISOU 1445  CB  TYR A 179     4844   3571   7507    471    254    966       C  
ATOM   1446  CG  TYR A 179      63.876 -11.524 -24.201  1.00 35.57           C  
ANISOU 1446  CG  TYR A 179     4051   2934   6532    412    172    907       C  
ATOM   1447  CD1 TYR A 179      63.816 -12.248 -25.382  1.00 41.73           C  
ANISOU 1447  CD1 TYR A 179     4828   3826   7200    380     65   1010       C  
ATOM   1448  CD2 TYR A 179      64.179 -12.206 -23.025  1.00 35.03           C  
ANISOU 1448  CD2 TYR A 179     4002   2902   6406    383    204    747       C  
ATOM   1449  CE1 TYR A 179      64.045 -13.627 -25.388  1.00 39.11           C  
ANISOU 1449  CE1 TYR A 179     4515   3628   6715    325      4    949       C  
ATOM   1450  CE2 TYR A 179      64.417 -13.568 -23.028  1.00 36.50           C  
ANISOU 1450  CE2 TYR A 179     4198   3226   6446    334    136    700       C  
ATOM   1451  CZ  TYR A 179      64.338 -14.268 -24.211  1.00 40.09           C  
ANISOU 1451  CZ  TYR A 179     4651   3778   6804    308     42    799       C  
ATOM   1452  OH  TYR A 179      64.563 -15.624 -24.206  1.00 43.23           O  
ANISOU 1452  OH  TYR A 179     5065   4295   7064    260    -11    746       O  
ATOM   1453  N   TYR A 180      61.768  -8.161 -22.333  1.00 45.26           N  
ANISOU 1453  N   TYR A 180     5184   3698   8314    658    501    931       N  
ATOM   1454  CA  TYR A 180      61.687  -6.906 -21.596  1.00 47.26           C  
ANISOU 1454  CA  TYR A 180     5468   3758   8731    705    653    876       C  
ATOM   1455  C   TYR A 180      62.350  -7.125 -20.249  1.00 47.21           C  
ANISOU 1455  C   TYR A 180     5547   3739   8653    637    730    655       C  
ATOM   1456  O   TYR A 180      62.327  -8.231 -19.716  1.00 44.31           O  
ANISOU 1456  O   TYR A 180     5174   3501   8162    601    683    572       O  
ATOM   1457  CB  TYR A 180      60.236  -6.432 -21.376  1.00 46.10           C  
ANISOU 1457  CB  TYR A 180     5220   3526   8768    833    726    971       C  
ATOM   1458  CG  TYR A 180      59.371  -6.526 -22.606  1.00 51.26           C  
ANISOU 1458  CG  TYR A 180     5761   4243   9473    895    616   1204       C  
ATOM   1459  CD1 TYR A 180      58.861  -7.760 -23.026  1.00 52.90           C  
ANISOU 1459  CD1 TYR A 180     5901   4635   9562    875    480   1263       C  
ATOM   1460  CD2 TYR A 180      59.054  -5.393 -23.346  1.00 46.52           C  
ANISOU 1460  CD2 TYR A 180     5124   3516   9037    966    645   1369       C  
ATOM   1461  CE1 TYR A 180      58.072  -7.857 -24.158  1.00 52.78           C  
ANISOU 1461  CE1 TYR A 180     5788   4688   9578    911    366   1478       C  
ATOM   1462  CE2 TYR A 180      58.253  -5.480 -24.480  1.00 55.22           C  
ANISOU 1462  CE2 TYR A 180     6117   4686  10176   1014    529   1598       C  
ATOM   1463  CZ  TYR A 180      57.767  -6.719 -24.877  1.00 55.64           C  
ANISOU 1463  CZ  TYR A 180     6108   4934  10097    980    385   1649       C  
ATOM   1464  OH  TYR A 180      56.986  -6.835 -25.999  1.00 52.36           O  
ANISOU 1464  OH  TYR A 180     5592   4599   9701   1006    256   1874       O  
ATOM   1465  N   LYS A 181      62.936  -6.067 -19.699  1.00 41.01           N  
ANISOU 1465  N   LYS A 181     4844   2796   7942    612    845    563       N  
ATOM   1466  CA  LYS A 181      63.639  -6.167 -18.426  1.00 47.20           C  
ANISOU 1466  CA  LYS A 181     5722   3565   8647    526    911    355       C  
ATOM   1467  C   LYS A 181      63.434  -4.893 -17.621  1.00 43.15           C  
ANISOU 1467  C   LYS A 181     5273   2840   8284    552   1084    273       C  
ATOM   1468  O   LYS A 181      63.472  -3.790 -18.171  1.00 52.26           O  
ANISOU 1468  O   LYS A 181     6439   3846   9572    587   1142    351       O  
ATOM   1469  CB  LYS A 181      65.140  -6.407 -18.622  1.00 50.41           C  
ANISOU 1469  CB  LYS A 181     6199   4038   8918    400    839    291       C  
ATOM   1470  CG  LYS A 181      65.896  -6.592 -17.319  1.00 44.15           C  
ANISOU 1470  CG  LYS A 181     5491   3254   8032    298    880     93       C  
ATOM   1471  CD  LYS A 181      67.383  -6.854 -17.545  1.00 50.01           C  
ANISOU 1471  CD  LYS A 181     6277   4068   8655    176    801     52       C  
ATOM   1472  CE  LYS A 181      68.037  -7.298 -16.245  1.00 56.23           C  
ANISOU 1472  CE  LYS A 181     7126   4909   9329     72    808   -122       C  
ATOM   1473  NZ  LYS A 181      69.509  -7.392 -16.339  1.00 65.82           N  
ANISOU 1473  NZ  LYS A 181     8375   6177  10458    -50    744   -160       N  
ATOM   1474  N   LYS A 182      63.225  -5.059 -16.318  1.00 50.90           N  
ANISOU 1474  N   LYS A 182     6303   3803   9234    530   1173    113       N  
ATOM   1475  CA  LYS A 182      63.099  -3.965 -15.367  1.00 50.66           C  
ANISOU 1475  CA  LYS A 182     6362   3574   9311    531   1354     -6       C  
ATOM   1476  C   LYS A 182      64.155  -4.117 -14.284  1.00 48.48           C  
ANISOU 1476  C   LYS A 182     6213   3323   8886    381   1366   -212       C  
ATOM   1477  O   LYS A 182      64.397  -5.224 -13.795  1.00 51.07           O  
ANISOU 1477  O   LYS A 182     6535   3816   9053    322   1282   -278       O  
ATOM   1478  CB  LYS A 182      61.713  -3.939 -14.712  1.00 56.75           C  
ANISOU 1478  CB  LYS A 182     7083   4286  10192    646   1477     -9       C  
ATOM   1479  CG  LYS A 182      60.618  -3.360 -15.575  1.00 67.20           C  
ANISOU 1479  CG  LYS A 182     8290   5535  11707    794   1509    187       C  
ATOM   1480  CD  LYS A 182      59.267  -3.501 -14.890  1.00 68.20           C  
ANISOU 1480  CD  LYS A 182     8346   5672  11897    889   1608    188       C  
ATOM   1481  CE  LYS A 182      59.109  -2.492 -13.773  1.00 61.49           C  
ANISOU 1481  CE  LYS A 182     7598   4687  11079    873   1801     41       C  
ATOM   1482  NZ  LYS A 182      57.773  -2.623 -13.120  1.00 67.17           N  
ANISOU 1482  NZ  LYS A 182     8242   5413  11866    965   1911     50       N  
ATOM   1483  N   VAL A 183      64.784  -3.005 -13.910  1.00 48.28           N  
ANISOU 1483  N   VAL A 183     6299   3131   8914    313   1466   -306       N  
ATOM   1484  CA  VAL A 183      65.736  -2.981 -12.807  1.00 53.01           C  
ANISOU 1484  CA  VAL A 183     7026   3735   9382    157   1486   -503       C  
ATOM   1485  C   VAL A 183      65.328  -1.847 -11.884  1.00 52.42           C  
ANISOU 1485  C   VAL A 183     7065   3438   9413    157   1692   -630       C  
ATOM   1486  O   VAL A 183      65.238  -0.693 -12.321  1.00 54.37           O  
ANISOU 1486  O   VAL A 183     7324   3569   9764    194   1758   -571       O  
ATOM   1487  CB  VAL A 183      67.188  -2.802 -13.288  1.00 61.57           C  
ANISOU 1487  CB  VAL A 183     8148   4852  10393     28   1385   -505       C  
ATOM   1488  CG1 VAL A 183      68.143  -2.745 -12.101  1.00 60.21           C  
ANISOU 1488  CG1 VAL A 183     8100   4688  10090   -145   1396   -699       C  
ATOM   1489  CG2 VAL A 183      67.584  -3.934 -14.229  1.00 58.02           C  
ANISOU 1489  CG2 VAL A 183     7593   4610   9843     34   1204   -382       C  
ATOM   1490  N   ASP A 184      65.055  -2.176 -10.622  1.00 57.26           N  
ANISOU 1490  N   ASP A 184     7750   4071   9936    111   1765   -785       N  
ATOM   1491  CA  ASP A 184      64.629  -1.201  -9.612  1.00 58.38           C  
ANISOU 1491  CA  ASP A 184     7997   4098  10086     96   1936   -907       C  
ATOM   1492  C   ASP A 184      63.456  -0.356 -10.105  1.00 62.82           C  
ANISOU 1492  C   ASP A 184     8482   4562  10826    261   2048   -778       C  
ATOM   1493  O   ASP A 184      63.447   0.873  -9.988  1.00 62.78           O  
ANISOU 1493  O   ASP A 184     8542   4424  10888    257   2159   -801       O  
ATOM   1494  CB  ASP A 184      65.793  -0.309  -9.181  1.00 65.66           C  
ANISOU 1494  CB  ASP A 184     9064   4946  10938    -69   1951  -1032       C  
ATOM   1495  CG  ASP A 184      66.921  -1.097  -8.554  1.00 76.76           C  
ANISOU 1495  CG  ASP A 184    10543   6459  12164   -249   1842  -1162       C  
ATOM   1496  OD1 ASP A 184      66.647  -2.131  -7.909  1.00 81.34           O  
ANISOU 1496  OD1 ASP A 184    11116   7141  12647   -261   1818  -1224       O  
ATOM   1497  OD2 ASP A 184      68.088  -0.684  -8.711  1.00 86.64           O  
ANISOU 1497  OD2 ASP A 184    11849   7696  13372   -381   1776  -1194       O  
ATOM   1498  N   GLY A 185      62.453  -1.031 -10.664  1.00 57.00           N  
ANISOU 1498  N   GLY A 185     7598   3893  10165    403   2015   -635       N  
ATOM   1499  CA  GLY A 185      61.243  -0.376 -11.118  1.00 60.46           C  
ANISOU 1499  CA  GLY A 185     7936   4264  10771    558   2105   -494       C  
ATOM   1500  C   GLY A 185      61.356   0.356 -12.435  1.00 64.00           C  
ANISOU 1500  C   GLY A 185     8314   4661  11340    617   2051   -317       C  
ATOM   1501  O   GLY A 185      60.368   0.956 -12.873  1.00 64.76           O  
ANISOU 1501  O   GLY A 185     8320   4702  11582    741   2117   -185       O  
ATOM   1502  N   VAL A 186      62.514   0.316 -13.090  1.00 63.02           N  
ANISOU 1502  N   VAL A 186     8224   4558  11163    531   1932   -301       N  
ATOM   1503  CA  VAL A 186      62.762   1.079 -14.306  1.00 61.69           C  
ANISOU 1503  CA  VAL A 186     8011   4337  11091    567   1886   -144       C  
ATOM   1504  C   VAL A 186      62.919   0.112 -15.470  1.00 57.72           C  
ANISOU 1504  C   VAL A 186     7399   3966  10567    597   1707     15       C  
ATOM   1505  O   VAL A 186      63.745  -0.811 -15.415  1.00 56.28           O  
ANISOU 1505  O   VAL A 186     7242   3874  10266    507   1604    -46       O  
ATOM   1506  CB  VAL A 186      64.005   1.978 -14.165  1.00 67.76           C  
ANISOU 1506  CB  VAL A 186     8915   5008  11822    434   1909   -246       C  
ATOM   1507  CG1 VAL A 186      64.376   2.580 -15.507  1.00 66.13           C  
ANISOU 1507  CG1 VAL A 186     8660   4770  11696    461   1840    -76       C  
ATOM   1508  CG2 VAL A 186      63.750   3.075 -13.142  1.00 66.00           C  
ANISOU 1508  CG2 VAL A 186     8802   4642  11634    412   2091   -382       C  
ATOM   1509  N   VAL A 187      62.136   0.328 -16.527  1.00 49.50           N  
ANISOU 1509  N   VAL A 187     6236   2936   9636    715   1670    221       N  
ATOM   1510  CA  VAL A 187      62.258  -0.495 -17.722  1.00 56.19           C  
ANISOU 1510  CA  VAL A 187     6989   3907  10455    737   1500    384       C  
ATOM   1511  C   VAL A 187      63.605  -0.224 -18.378  1.00 56.48           C  
ANISOU 1511  C   VAL A 187     7095   3927  10439    634   1428    390       C  
ATOM   1512  O   VAL A 187      64.010   0.932 -18.549  1.00 56.16           O  
ANISOU 1512  O   VAL A 187     7112   3770  10455    610   1493    390       O  
ATOM   1513  CB  VAL A 187      61.095  -0.224 -18.689  1.00 64.76           C  
ANISOU 1513  CB  VAL A 187     7933   5011  11660    872   1472    608       C  
ATOM   1514  CG1 VAL A 187      61.274  -1.040 -19.960  1.00 60.58           C  
ANISOU 1514  CG1 VAL A 187     7326   4614  11079    875   1290    777       C  
ATOM   1515  CG2 VAL A 187      59.748  -0.543 -18.020  1.00 59.63           C  
ANISOU 1515  CG2 VAL A 187     7199   4387  11070    967   1544    610       C  
ATOM   1516  N   GLN A 188      64.317  -1.289 -18.720  1.00 53.14           N  
ANISOU 1516  N   GLN A 188     6666   3614   9909    570   1301    392       N  
ATOM   1517  CA  GLN A 188      65.626  -1.176 -19.344  1.00 56.77           C  
ANISOU 1517  CA  GLN A 188     7179   4095  10298    462   1226    399       C  
ATOM   1518  C   GLN A 188      65.507  -1.185 -20.861  1.00 56.07           C  
ANISOU 1518  C   GLN A 188     7011   4058  10235    516   1123    621       C  
ATOM   1519  O   GLN A 188      64.627  -1.836 -21.430  1.00 59.29           O  
ANISOU 1519  O   GLN A 188     7320   4573  10636    598   1045    750       O  
ATOM   1520  CB  GLN A 188      66.532  -2.333 -18.914  1.00 57.65           C  
ANISOU 1520  CB  GLN A 188     7314   4396  10193    343   1120    277       C  
ATOM   1521  CG  GLN A 188      66.698  -2.467 -17.422  1.00 63.28           C  
ANISOU 1521  CG  GLN A 188     8106   5094  10846    272   1194     67       C  
ATOM   1522  CD  GLN A 188      67.323  -1.238 -16.810  1.00 68.56           C  
ANISOU 1522  CD  GLN A 188     8894   5569  11588    193   1317    -51       C  
ATOM   1523  OE1 GLN A 188      66.625  -0.343 -16.329  1.00 71.47           O  
ANISOU 1523  OE1 GLN A 188     9299   5777  12078    251   1459    -85       O  
ATOM   1524  NE2 GLN A 188      68.649  -1.183 -16.829  1.00 70.20           N  
ANISOU 1524  NE2 GLN A 188     9157   5811  11705     54   1261   -111       N  
ATOM   1525  N   GLN A 189      66.406  -0.453 -21.515  1.00 51.33           N  
ANISOU 1525  N   GLN A 189     6460   3384   9659    458   1122    667       N  
ATOM   1526  CA  GLN A 189      66.657  -0.632 -22.940  1.00 50.31           C  
ANISOU 1526  CA  GLN A 189     6284   3342   9490    462   1008    850       C  
ATOM   1527  C   GLN A 189      67.713  -1.723 -23.081  1.00 49.37           C  
ANISOU 1527  C   GLN A 189     6181   3415   9162    349    894    781       C  
ATOM   1528  O   GLN A 189      68.881  -1.505 -22.747  1.00 51.24           O  
ANISOU 1528  O   GLN A 189     6488   3631   9350    238    913    673       O  
ATOM   1529  CB  GLN A 189      67.134   0.660 -23.596  1.00 54.52           C  
ANISOU 1529  CB  GLN A 189     6859   3752  10106    446   1056    928       C  
ATOM   1530  CG  GLN A 189      66.115   1.784 -23.601  1.00 72.45           C  
ANISOU 1530  CG  GLN A 189     9099   5919  12511    551   1145    997       C  
ATOM   1531  CD  GLN A 189      66.443   2.845 -24.636  1.00 92.38           C  
ANISOU 1531  CD  GLN A 189    11635   8374  15092    552   1148   1135       C  
ATOM   1532  OE1 GLN A 189      67.085   2.561 -25.651  1.00 94.89           O  
ANISOU 1532  OE1 GLN A 189    11952   8760  15343    506   1056   1241       O  
ATOM   1533  NE2 GLN A 189      66.007   4.076 -24.384  1.00 99.60           N  
ANISOU 1533  NE2 GLN A 189    12564   9151  16129    601   1262   1135       N  
ATOM   1534  N   LEU A 190      67.310  -2.883 -23.569  1.00 42.38           N  
ANISOU 1534  N   LEU A 190     5230   2712   8161    374    780    846       N  
ATOM   1535  CA  LEU A 190      68.263  -3.981 -23.715  1.00 40.73           C  
ANISOU 1535  CA  LEU A 190     5033   2677   7764    280    686    786       C  
ATOM   1536  C   LEU A 190      69.222  -3.683 -24.869  1.00 46.06           C  
ANISOU 1536  C   LEU A 190     5734   3362   8404    222    648    885       C  
ATOM   1537  O   LEU A 190      68.825  -3.070 -25.863  1.00 43.66           O  
ANISOU 1537  O   LEU A 190     5412   3001   8174    274    641   1050       O  
ATOM   1538  CB  LEU A 190      67.525  -5.301 -23.955  1.00 43.74           C  
ANISOU 1538  CB  LEU A 190     5348   3234   8036    320    585    828       C  
ATOM   1539  CG  LEU A 190      66.763  -5.863 -22.748  1.00 52.85           C  
ANISOU 1539  CG  LEU A 190     6478   4416   9187    355    614    711       C  
ATOM   1540  CD1 LEU A 190      65.813  -6.965 -23.178  1.00 52.93           C  
ANISOU 1540  CD1 LEU A 190     6411   4573   9128    408    518    795       C  
ATOM   1541  CD2 LEU A 190      67.742  -6.388 -21.683  1.00 47.02           C  
ANISOU 1541  CD2 LEU A 190     5795   3730   8341    255    624    523       C  
ATOM   1542  N   PRO A 191      70.486  -4.094 -24.766  1.00 45.60           N  
ANISOU 1542  N   PRO A 191     5712   3374   8240    116    626    799       N  
ATOM   1543  CA  PRO A 191      71.475  -3.717 -25.787  1.00 49.67           C  
ANISOU 1543  CA  PRO A 191     6254   3884   8736     57    614    884       C  
ATOM   1544  C   PRO A 191      71.286  -4.488 -27.086  1.00 49.92           C  
ANISOU 1544  C   PRO A 191     6257   4052   8660     79    523   1028       C  
ATOM   1545  O   PRO A 191      70.751  -5.600 -27.112  1.00 49.11           O  
ANISOU 1545  O   PRO A 191     6119   4083   8456    106    454   1024       O  
ATOM   1546  CB  PRO A 191      72.813  -4.086 -25.134  1.00 49.50           C  
ANISOU 1546  CB  PRO A 191     6260   3914   8634    -60    617    742       C  
ATOM   1547  CG  PRO A 191      72.455  -5.269 -24.242  1.00 49.64           C  
ANISOU 1547  CG  PRO A 191     6249   4056   8554    -50    574    632       C  
ATOM   1548  CD  PRO A 191      71.067  -4.943 -23.710  1.00 44.66           C  
ANISOU 1548  CD  PRO A 191     5604   3348   8017     47    611    631       C  
ATOM   1549  N   GLU A 192      71.752  -3.877 -28.178  1.00 47.27           N  
ANISOU 1549  N   GLU A 192     5944   3676   8339     58    527   1154       N  
ATOM   1550  CA  GLU A 192      71.950  -4.614 -29.421  1.00 44.94           C  
ANISOU 1550  CA  GLU A 192     5650   3515   7909     40    454   1265       C  
ATOM   1551  C   GLU A 192      72.808  -5.834 -29.146  1.00 46.99           C  
ANISOU 1551  C   GLU A 192     5913   3918   8023    -27    426   1150       C  
ATOM   1552  O   GLU A 192      73.797  -5.745 -28.417  1.00 41.78           O  
ANISOU 1552  O   GLU A 192     5264   3235   7375    -93    470   1032       O  
ATOM   1553  CB  GLU A 192      72.653  -3.744 -30.466  1.00 46.19           C  
ANISOU 1553  CB  GLU A 192     5849   3606   8096      0    485   1386       C  
ATOM   1554  CG  GLU A 192      71.792  -2.720 -31.127  1.00 57.52           C  
ANISOU 1554  CG  GLU A 192     7278   4930   9647     70    490   1555       C  
ATOM   1555  CD  GLU A 192      72.455  -2.139 -32.355  1.00 56.94           C  
ANISOU 1555  CD  GLU A 192     7247   4833   9555     24    500   1696       C  
ATOM   1556  OE1 GLU A 192      73.566  -2.602 -32.731  1.00 49.58           O  
ANISOU 1556  OE1 GLU A 192     6347   3979   8512    -60    507   1659       O  
ATOM   1557  OE2 GLU A 192      71.864  -1.218 -32.944  1.00 55.72           O  
ANISOU 1557  OE2 GLU A 192     7090   4580   9502     75    507   1851       O  
ATOM   1558  N   THR A 193      72.439  -6.973 -29.735  1.00 37.36           N  
ANISOU 1558  N   THR A 193     4684   2842   6670    -15    353   1189       N  
ATOM   1559  CA  THR A 193      73.148  -8.204 -29.418  1.00 39.15           C  
ANISOU 1559  CA  THR A 193     4910   3194   6772    -64    336   1081       C  
ATOM   1560  C   THR A 193      73.098  -9.160 -30.607  1.00 43.23           C  
ANISOU 1560  C   THR A 193     5451   3837   7138    -76    282   1165       C  
ATOM   1561  O   THR A 193      72.127  -9.171 -31.374  1.00 38.84           O  
ANISOU 1561  O   THR A 193     4898   3305   6554    -38    227   1281       O  
ATOM   1562  CB  THR A 193      72.555  -8.851 -28.147  1.00 38.97           C  
ANISOU 1562  CB  THR A 193     4850   3204   6752    -32    318    956       C  
ATOM   1563  OG1 THR A 193      73.321 -10.010 -27.776  1.00 37.60           O  
ANISOU 1563  OG1 THR A 193     4672   3142   6472    -79    304    858       O  
ATOM   1564  CG2 THR A 193      71.059  -9.252 -28.341  1.00 38.76           C  
ANISOU 1564  CG2 THR A 193     4792   3220   6715     45    255   1024       C  
ATOM   1565  N   TYR A 194      74.189  -9.912 -30.793  1.00 39.33           N  
ANISOU 1565  N   TYR A 194     4976   3418   6551   -135    305   1112       N  
ATOM   1566  CA  TYR A 194      74.145 -11.135 -31.575  1.00 36.58           C  
ANISOU 1566  CA  TYR A 194     4657   3196   6046   -149    269   1134       C  
ATOM   1567  C   TYR A 194      73.561 -12.251 -30.718  1.00 36.18           C  
ANISOU 1567  C   TYR A 194     4574   3222   5951   -121    224   1035       C  
ATOM   1568  O   TYR A 194      73.442 -12.126 -29.500  1.00 37.28           O  
ANISOU 1568  O   TYR A 194     4669   3326   6167   -102    231    941       O  
ATOM   1569  CB  TYR A 194      75.543 -11.530 -32.080  1.00 36.65           C  
ANISOU 1569  CB  TYR A 194     4696   3244   5988   -212    332   1116       C  
ATOM   1570  CG  TYR A 194      76.165 -10.552 -33.049  1.00 37.09           C  
ANISOU 1570  CG  TYR A 194     4789   3236   6067   -248    382   1222       C  
ATOM   1571  CD1 TYR A 194      75.862 -10.592 -34.401  1.00 35.15           C  
ANISOU 1571  CD1 TYR A 194     4608   3027   5721   -261    366   1346       C  
ATOM   1572  CD2 TYR A 194      77.080  -9.599 -32.611  1.00 35.66           C  
ANISOU 1572  CD2 TYR A 194     4584   2962   6002   -281    445   1199       C  
ATOM   1573  CE1 TYR A 194      76.427  -9.700 -35.289  1.00 39.60           C  
ANISOU 1573  CE1 TYR A 194     5210   3535   6301   -297    415   1450       C  
ATOM   1574  CE2 TYR A 194      77.659  -8.696 -33.493  1.00 40.39           C  
ANISOU 1574  CE2 TYR A 194     5217   3501   6630   -318    496   1299       C  
ATOM   1575  CZ  TYR A 194      77.330  -8.745 -34.830  1.00 37.00           C  
ANISOU 1575  CZ  TYR A 194     4850   3107   6100   -322    484   1427       C  
ATOM   1576  OH  TYR A 194      77.909  -7.849 -35.700  1.00 39.27           O  
ANISOU 1576  OH  TYR A 194     5175   3334   6410   -360    538   1534       O  
ATOM   1577  N   PHE A 195      73.185 -13.354 -31.362  1.00 36.07           N  
ANISOU 1577  N   PHE A 195     4590   3310   5804   -127    181   1056       N  
ATOM   1578  CA  PHE A 195      72.736 -14.548 -30.659  1.00 37.17           C  
ANISOU 1578  CA  PHE A 195     4707   3527   5889   -111    145    966       C  
ATOM   1579  C   PHE A 195      73.511 -15.761 -31.141  1.00 34.25           C  
ANISOU 1579  C   PHE A 195     4380   3241   5391   -153    172    928       C  
ATOM   1580  O   PHE A 195      73.757 -15.907 -32.340  1.00 40.17           O  
ANISOU 1580  O   PHE A 195     5196   4019   6048   -188    185    999       O  
ATOM   1581  CB  PHE A 195      71.237 -14.808 -30.860  1.00 39.71           C  
ANISOU 1581  CB  PHE A 195     5017   3886   6185    -74     59   1025       C  
ATOM   1582  CG  PHE A 195      70.370 -13.762 -30.242  1.00 40.31           C  
ANISOU 1582  CG  PHE A 195     5036   3876   6403    -16     46   1056       C  
ATOM   1583  CD1 PHE A 195      70.299 -13.636 -28.864  1.00 41.52           C  
ANISOU 1583  CD1 PHE A 195     5141   3987   6647     14     75    947       C  
ATOM   1584  CD2 PHE A 195      69.621 -12.915 -31.030  1.00 38.95           C  
ANISOU 1584  CD2 PHE A 195     4860   3664   6274      8     10   1197       C  
ATOM   1585  CE1 PHE A 195      69.492 -12.675 -28.292  1.00 39.54           C  
ANISOU 1585  CE1 PHE A 195     4847   3645   6530     70     85    967       C  
ATOM   1586  CE2 PHE A 195      68.813 -11.945 -30.460  1.00 41.50           C  
ANISOU 1586  CE2 PHE A 195     5126   3894   6748     73     15   1231       C  
ATOM   1587  CZ  PHE A 195      68.754 -11.826 -29.090  1.00 37.97           C  
ANISOU 1587  CZ  PHE A 195     4639   3396   6392    105     61   1110       C  
ATOM   1588  N   THR A 196      73.886 -16.630 -30.205  1.00 33.90           N  
ANISOU 1588  N   THR A 196     4305   3235   5343   -149    186    819       N  
ATOM   1589  CA  THR A 196      74.416 -17.924 -30.601  1.00 33.68           C  
ANISOU 1589  CA  THR A 196     4314   3280   5202   -174    214    784       C  
ATOM   1590  C   THR A 196      73.279 -18.785 -31.135  1.00 39.56           C  
ANISOU 1590  C   THR A 196     5104   4090   5839   -173    148    809       C  
ATOM   1591  O   THR A 196      72.101 -18.505 -30.906  1.00 39.03           O  
ANISOU 1591  O   THR A 196     5010   4021   5799   -146     74    839       O  
ATOM   1592  CB  THR A 196      75.123 -18.634 -29.438  1.00 36.68           C  
ANISOU 1592  CB  THR A 196     4640   3680   5617   -168    243    678       C  
ATOM   1593  OG1 THR A 196      74.243 -18.705 -28.317  1.00 36.17           O  
ANISOU 1593  OG1 THR A 196     4528   3619   5598   -134    186    625       O  
ATOM   1594  CG2 THR A 196      76.411 -17.875 -29.037  1.00 33.83           C  
ANISOU 1594  CG2 THR A 196     4235   3270   5349   -191    304    663       C  
ATOM   1595  N   GLN A 197      73.648 -19.834 -31.872  1.00 37.66           N  
ANISOU 1595  N   GLN A 197     4931   3901   5477   -207    180    798       N  
ATOM   1596  CA  GLN A 197      72.689 -20.607 -32.653  1.00 38.94           C  
ANISOU 1596  CA  GLN A 197     5161   4123   5510   -235    122    829       C  
ATOM   1597  C   GLN A 197      72.299 -21.926 -31.996  1.00 39.16           C  
ANISOU 1597  C   GLN A 197     5181   4199   5498   -226    103    743       C  
ATOM   1598  O   GLN A 197      71.326 -22.554 -32.438  1.00 41.42           O  
ANISOU 1598  O   GLN A 197     5511   4535   5693   -253     37    762       O  
ATOM   1599  CB  GLN A 197      73.257 -20.860 -34.058  1.00 34.75           C  
ANISOU 1599  CB  GLN A 197     4742   3611   4851   -294    177    876       C  
ATOM   1600  CG  GLN A 197      73.499 -19.566 -34.867  1.00 38.13           C  
ANISOU 1600  CG  GLN A 197     5190   3998   5301   -311    187    983       C  
ATOM   1601  CD  GLN A 197      72.188 -18.883 -35.255  1.00 48.97           C  
ANISOU 1601  CD  GLN A 197     6557   5379   6671   -310     71   1089       C  
ATOM   1602  OE1 GLN A 197      71.213 -19.545 -35.623  1.00 47.38           O  
ANISOU 1602  OE1 GLN A 197     6390   5240   6373   -337     -9   1110       O  
ATOM   1603  NE2 GLN A 197      72.156 -17.558 -35.154  1.00 46.53           N  
ANISOU 1603  NE2 GLN A 197     6198   5004   6477   -280     62   1162       N  
ATOM   1604  N   SER A 198      73.031 -22.359 -30.967  1.00 35.74           N  
ANISOU 1604  N   SER A 198     4101   4654   4822   -318    222    810       N  
ATOM   1605  CA  SER A 198      72.625 -23.482 -30.116  1.00 40.83           C  
ANISOU 1605  CA  SER A 198     4827   5352   5334   -469    416   1110       C  
ATOM   1606  C   SER A 198      72.541 -24.800 -30.888  1.00 36.62           C  
ANISOU 1606  C   SER A 198     4566   4382   4966   -682    389   1312       C  
ATOM   1607  O   SER A 198      71.726 -25.669 -30.563  1.00 42.15           O  
ANISOU 1607  O   SER A 198     5272   5021   5720   -948    536   1532       O  
ATOM   1608  CB  SER A 198      71.290 -23.193 -29.423  1.00 43.12           C  
ANISOU 1608  CB  SER A 198     4786   5970   5627   -626    605   1103       C  
ATOM   1609  OG  SER A 198      71.384 -22.091 -28.544  1.00 47.80           O  
ANISOU 1609  OG  SER A 198     5169   6958   6034   -412    681    884       O  
ATOM   1610  N   ARG A 199      73.384 -24.979 -31.897  1.00 36.01           N  
ANISOU 1610  N   ARG A 199     4718   3990   4974   -586    225   1224       N  
ATOM   1611  CA  ARG A 199      73.400 -26.222 -32.658  1.00 43.38           C  
ANISOU 1611  CA  ARG A 199     5950   4471   6060   -758    207   1327       C  
ATOM   1612  C   ARG A 199      74.349 -27.234 -32.007  1.00 50.40           C  
ANISOU 1612  C   ARG A 199     7147   5163   6840   -583    314   1613       C  
ATOM   1613  O   ARG A 199      75.065 -26.924 -31.055  1.00 43.88           O  
ANISOU 1613  O   ARG A 199     6280   4613   5778   -322    355   1730       O  
ATOM   1614  CB  ARG A 199      73.787 -25.932 -34.108  1.00 39.68           C  
ANISOU 1614  CB  ARG A 199     5574   3803   5699   -726      7   1066       C  
ATOM   1615  CG  ARG A 199      72.737 -25.110 -34.836  1.00 47.72           C  
ANISOU 1615  CG  ARG A 199     6310   4983   6840   -908   -129    871       C  
ATOM   1616  CD  ARG A 199      73.203 -24.603 -36.189  1.00 46.53           C  
ANISOU 1616  CD  ARG A 199     6232   4746   6701   -832   -330    664       C  
ATOM   1617  NE  ARG A 199      74.188 -23.532 -36.084  1.00 41.05           N  
ANISOU 1617  NE  ARG A 199     5477   4209   5910   -523   -360    598       N  
ATOM   1618  CZ  ARG A 199      74.555 -22.762 -37.105  1.00 40.78           C  
ANISOU 1618  CZ  ARG A 199     5431   4186   5878   -445   -503    472       C  
ATOM   1619  NH1 ARG A 199      74.004 -22.941 -38.300  1.00 42.91           N  
ANISOU 1619  NH1 ARG A 199     5747   4377   6181   -622   -649    396       N  
ATOM   1620  NH2 ARG A 199      75.468 -21.806 -36.935  1.00 37.04           N  
ANISOU 1620  NH2 ARG A 199     4893   3823   5357   -216   -506    430       N  
ATOM   1621  N   ASN A 200      74.332 -28.471 -32.509  1.00 53.20           N  
ANISOU 1621  N   ASN A 200     7807   5031   7373   -726    348   1725       N  
ATOM   1622  CA  ASN A 200      75.232 -29.506 -32.003  1.00 48.31           C  
ANISOU 1622  CA  ASN A 200     7505   4126   6724   -510    444   2029       C  
ATOM   1623  C   ASN A 200      76.007 -30.136 -33.161  1.00 54.08           C  
ANISOU 1623  C   ASN A 200     8545   4375   7629   -387    369   1854       C  
ATOM   1624  O   ASN A 200      75.676 -29.955 -34.338  1.00 52.98           O  
ANISOU 1624  O   ASN A 200     8414   4109   7608   -559    260   1523       O  
ATOM   1625  CB  ASN A 200      74.484 -30.569 -31.179  1.00 58.87           C  
ANISOU 1625  CB  ASN A 200     8964   5268   8135   -768    646   2431       C  
ATOM   1626  CG  ASN A 200      73.430 -31.305 -31.974  1.00 75.82           C  
ANISOU 1626  CG  ASN A 200    11205   6992  10609  -1238    666   2332       C  
ATOM   1627  OD1 ASN A 200      73.743 -32.156 -32.809  1.00 85.74           O  
ANISOU 1627  OD1 ASN A 200    12704   7806  12068  -1254    559   2181       O  
ATOM   1628  ND2 ASN A 200      72.166 -31.007 -31.693  1.00 70.18           N  
ANISOU 1628  ND2 ASN A 200    10190   6548   9928  -1608    731   2341       N  
ATOM   1629  N   LEU A 201      77.073 -30.862 -32.804  1.00 58.52           N  
ANISOU 1629  N   LEU A 201     9302   4765   8168    -60    396   2045       N  
ATOM   1630  CA  LEU A 201      78.033 -31.336 -33.802  1.00 71.17           C  
ANISOU 1630  CA  LEU A 201    11037   6110   9893    158    311   1797       C  
ATOM   1631  C   LEU A 201      77.391 -32.302 -34.788  1.00 76.48           C  
ANISOU 1631  C   LEU A 201    11881   6323  10854   -135    311   1591       C  
ATOM   1632  O   LEU A 201      77.473 -32.111 -36.008  1.00 89.71           O  
ANISOU 1632  O   LEU A 201    13598   7916  12572   -172    258   1222       O  
ATOM   1633  CB  LEU A 201      79.220 -32.014 -33.115  1.00 72.63           C  
ANISOU 1633  CB  LEU A 201    11277   6292  10029    542    311   2023       C  
ATOM   1634  CG  LEU A 201      80.456 -31.179 -32.810  1.00 64.73           C  
ANISOU 1634  CG  LEU A 201    10082   5707   8804    940    248   2007       C  
ATOM   1635  CD1 LEU A 201      81.648 -32.094 -32.625  1.00 77.62           C  
ANISOU 1635  CD1 LEU A 201    11780   7213  10500   1284    235   2120       C  
ATOM   1636  CD2 LEU A 201      80.698 -30.183 -33.923  1.00 66.89           C  
ANISOU 1636  CD2 LEU A 201    10258   6094   9063    956    197   1641       C  
ATOM   1637  N   GLN A 202      76.751 -33.351 -34.273  1.00 72.01           N  
ANISOU 1637  N   GLN A 202    11421   5477  10463   -358    368   1821       N  
ATOM   1638  CA  GLN A 202      76.349 -34.470 -35.119  1.00 85.95           C  
ANISOU 1638  CA  GLN A 202    13361   6750  12546   -578    364   1628       C  
ATOM   1639  C   GLN A 202      75.235 -34.081 -36.083  1.00 93.52           C  
ANISOU 1639  C   GLN A 202    14216   7733  13584   -990    326   1281       C  
ATOM   1640  O   GLN A 202      75.181 -34.582 -37.213  1.00104.75           O  
ANISOU 1640  O   GLN A 202    15768   8894  15139  -1092    277    918       O  
ATOM   1641  CB  GLN A 202      75.908 -35.635 -34.245  1.00 87.58           C  
ANISOU 1641  CB  GLN A 202    13703   6646  12928   -747    416   2004       C  
ATOM   1642  CG  GLN A 202      76.946 -36.048 -33.224  1.00100.74           C  
ANISOU 1642  CG  GLN A 202    15490   8330  14458   -352    435   2372       C  
ATOM   1643  CD  GLN A 202      76.439 -37.134 -32.307  1.00119.43           C  
ANISOU 1643  CD  GLN A 202    18037  10412  16929   -553    490   2792       C  
ATOM   1644  OE1 GLN A 202      75.266 -37.147 -31.934  1.00133.41           O  
ANISOU 1644  OE1 GLN A 202    19750  12233  18705   -990    545   2936       O  
ATOM   1645  NE2 GLN A 202      77.316 -38.062 -31.945  1.00122.43           N  
ANISOU 1645  NE2 GLN A 202    18631  10493  17393   -244    484   3004       N  
ATOM   1646  N   GLU A 203      74.335 -33.199 -35.656  1.00 80.27           N  
ANISOU 1646  N   GLU A 203    12304   6400  11795  -1233    339   1366       N  
ATOM   1647  CA  GLU A 203      73.196 -32.793 -36.465  1.00 74.77           C  
ANISOU 1647  CA  GLU A 203    11455   5816  11137  -1642    257   1063       C  
ATOM   1648  C   GLU A 203      73.300 -31.337 -36.900  1.00 57.98           C  
ANISOU 1648  C   GLU A 203     9174   4110   8747  -1568     94    886       C  
ATOM   1649  O   GLU A 203      72.280 -30.656 -37.034  1.00 59.88           O  
ANISOU 1649  O   GLU A 203     9148   4631   8972  -1869    -22    820       O  
ATOM   1650  CB  GLU A 203      71.897 -33.017 -35.698  1.00 79.15           C  
ANISOU 1650  CB  GLU A 203    11803   6447  11826  -2045    373   1286       C  
ATOM   1651  CG  GLU A 203      71.895 -34.266 -34.832  1.00 86.34           C  
ANISOU 1651  CG  GLU A 203    12831   7005  12969  -2071    535   1667       C  
ATOM   1652  CD  GLU A 203      70.734 -34.291 -33.859  1.00 92.61           C  
ANISOU 1652  CD  GLU A 203    13396   7999  13791  -2402    754   1947       C  
ATOM   1653  OE1 GLU A 203      70.092 -35.355 -33.717  1.00105.65           O  
ANISOU 1653  OE1 GLU A 203    15056   9357  15728  -2675    835   2067       O  
ATOM   1654  OE2 GLU A 203      70.461 -33.239 -33.240  1.00 93.04           O  
ANISOU 1654  OE2 GLU A 203    13278   8524  13550  -2411    826   2026       O  
ATOM   1655  N   PHE A 204      74.520 -30.844 -37.124  1.00 53.21           N  
ANISOU 1655  N   PHE A 204     8678   3567   7974  -1163     58    829       N  
ATOM   1656  CA  PHE A 204      74.692 -29.447 -37.483  1.00 48.91           C  
ANISOU 1656  CA  PHE A 204     7904   3451   7230  -1040    -95    695       C  
ATOM   1657  C   PHE A 204      74.042 -29.172 -38.831  1.00 57.56           C  
ANISOU 1657  C   PHE A 204     8954   4601   8314  -1304   -294    365       C  
ATOM   1658  O   PHE A 204      74.279 -29.888 -39.805  1.00 65.74           O  
ANISOU 1658  O   PHE A 204    10263   5352   9364  -1365   -321    121       O  
ATOM   1659  CB  PHE A 204      76.176 -29.076 -37.524  1.00 46.14           C  
ANISOU 1659  CB  PHE A 204     7630   3171   6730   -573    -66    686       C  
ATOM   1660  CG  PHE A 204      76.425 -27.616 -37.714  1.00 48.17           C  
ANISOU 1660  CG  PHE A 204     7587   3887   6828   -433   -182    594       C  
ATOM   1661  CD1 PHE A 204      76.383 -27.044 -38.976  1.00 48.04           C  
ANISOU 1661  CD1 PHE A 204     7547   3966   6742   -495   -322    348       C  
ATOM   1662  CD2 PHE A 204      76.707 -26.803 -36.627  1.00 52.21           C  
ANISOU 1662  CD2 PHE A 204     7856   4729   7252   -250   -149    755       C  
ATOM   1663  CE1 PHE A 204      76.610 -25.697 -39.151  1.00 45.97           C  
ANISOU 1663  CE1 PHE A 204     7033   4052   6383   -377   -414    320       C  
ATOM   1664  CE2 PHE A 204      76.940 -25.447 -36.796  1.00 48.95           C  
ANISOU 1664  CE2 PHE A 204     7192   4649   6758   -146   -245    647       C  
ATOM   1665  CZ  PHE A 204      76.887 -24.897 -38.057  1.00 52.45           C  
ANISOU 1665  CZ  PHE A 204     7624   5114   7191   -210   -370    457       C  
ATOM   1666  N   LYS A 205      73.218 -28.130 -38.878  1.00 52.90           N  
ANISOU 1666  N   LYS A 205     7995   4421   7683  -1425   -431    349       N  
ATOM   1667  CA  LYS A 205      72.532 -27.742 -40.091  1.00 57.69           C  
ANISOU 1667  CA  LYS A 205     8494   5182   8244  -1645   -665    111       C  
ATOM   1668  C   LYS A 205      72.867 -26.297 -40.431  1.00 52.96           C  
ANISOU 1668  C   LYS A 205     7664   4966   7492  -1387   -784    106       C  
ATOM   1669  O   LYS A 205      72.722 -25.410 -39.575  1.00 49.12           O  
ANISOU 1669  O   LYS A 205     6898   4724   7043  -1246   -741    260       O  
ATOM   1670  CB  LYS A 205      71.011 -27.914 -39.947  1.00 55.36           C  
ANISOU 1670  CB  LYS A 205     7921   4999   8112  -2073   -752    129       C  
ATOM   1671  CG  LYS A 205      70.593 -29.348 -39.636  1.00 57.68           C  
ANISOU 1671  CG  LYS A 205     8418   4894   8604  -2389   -610    146       C  
ATOM   1672  CD  LYS A 205      69.126 -29.556 -39.882  1.00 64.61           C  
ANISOU 1672  CD  LYS A 205     8974   5957   9619  -2804   -706     59       C  
ATOM   1673  CE  LYS A 205      68.687 -30.940 -39.421  1.00 75.12           C  
ANISOU 1673  CE  LYS A 205    10421   6928  11193  -3052   -490    105       C  
ATOM   1674  NZ  LYS A 205      69.672 -31.999 -39.792  1.00 85.25           N  
ANISOU 1674  NZ  LYS A 205    12161   7708  12523  -2893   -384    -16       N  
ATOM   1675  N   PRO A 206      73.321 -26.021 -41.648  1.00 52.13           N  
ANISOU 1675  N   PRO A 206     7684   4911   7213  -1326   -915    -66       N  
ATOM   1676  CA  PRO A 206      73.626 -24.639 -42.024  1.00 46.76           C  
ANISOU 1676  CA  PRO A 206     6804   4543   6419  -1113  -1018    -10       C  
ATOM   1677  C   PRO A 206      72.368 -23.787 -42.034  1.00 49.79           C  
ANISOU 1677  C   PRO A 206     6805   5215   6900  -1248  -1205     66       C  
ATOM   1678  O   PRO A 206      71.267 -24.266 -42.310  1.00 54.47           O  
ANISOU 1678  O   PRO A 206     7288   5850   7557  -1554  -1338      2       O  
ATOM   1679  CB  PRO A 206      74.215 -24.780 -43.432  1.00 46.46           C  
ANISOU 1679  CB  PRO A 206     7013   4504   6134  -1100  -1101   -192       C  
ATOM   1680  CG  PRO A 206      73.593 -26.016 -43.958  1.00 46.55           C  
ANISOU 1680  CG  PRO A 206     7232   4312   6142  -1419  -1163   -415       C  
ATOM   1681  CD  PRO A 206      73.497 -26.950 -42.774  1.00 50.46           C  
ANISOU 1681  CD  PRO A 206     7804   4479   6890  -1477   -968   -331       C  
ATOM   1682  N   ARG A 207      72.543 -22.499 -41.727  1.00 48.64           N  
ANISOU 1682  N   ARG A 207     6431   5256   6795  -1013  -1215    192       N  
ATOM   1683  CA  ARG A 207      71.421 -21.570 -41.649  1.00 50.00           C  
ANISOU 1683  CA  ARG A 207     6214   5671   7114  -1036  -1364    278       C  
ATOM   1684  C   ARG A 207      71.587 -20.356 -42.557  1.00 55.01           C  
ANISOU 1684  C   ARG A 207     6765   6449   7687   -867  -1540    365       C  
ATOM   1685  O   ARG A 207      70.808 -19.405 -42.443  1.00 50.78           O  
ANISOU 1685  O   ARG A 207     5906   6066   7320   -782  -1649    471       O  
ATOM   1686  CB  ARG A 207      71.201 -21.131 -40.195  1.00 48.15           C  
ANISOU 1686  CB  ARG A 207     5743   5484   7066   -908  -1177    350       C  
ATOM   1687  CG  ARG A 207      70.500 -22.217 -39.356  1.00 53.82           C  
ANISOU 1687  CG  ARG A 207     6420   6164   7864  -1148  -1040    358       C  
ATOM   1688  CD  ARG A 207      70.357 -21.861 -37.881  1.00 44.82           C  
ANISOU 1688  CD  ARG A 207     5079   5142   6807  -1021   -816    429       C  
ATOM   1689  NE  ARG A 207      69.756 -22.978 -37.163  1.00 48.34           N  
ANISOU 1689  NE  ARG A 207     5524   5550   7292  -1280   -660    506       N  
ATOM   1690  CZ  ARG A 207      69.665 -23.080 -35.841  1.00 50.64           C  
ANISOU 1690  CZ  ARG A 207     5723   5950   7567  -1238   -420    608       C  
ATOM   1691  NH1 ARG A 207      70.137 -22.117 -35.061  1.00 47.95           N  
ANISOU 1691  NH1 ARG A 207     5280   5780   7160   -941   -326    575       N  
ATOM   1692  NH2 ARG A 207      69.093 -24.151 -35.295  1.00 43.21           N  
ANISOU 1692  NH2 ARG A 207     4800   4953   6663  -1518   -270    740       N  
ATOM   1693  N   SER A 208      72.570 -20.367 -43.455  1.00 51.04           N  
ANISOU 1693  N   SER A 208     6538   5899   6957   -804  -1551    346       N  
ATOM   1694  CA  SER A 208      72.726 -19.330 -44.465  1.00 50.37           C  
ANISOU 1694  CA  SER A 208     6418   5956   6764   -695  -1712    491       C  
ATOM   1695  C   SER A 208      73.450 -19.934 -45.656  1.00 54.47           C  
ANISOU 1695  C   SER A 208     7267   6505   6923   -771  -1732    398       C  
ATOM   1696  O   SER A 208      74.048 -21.008 -45.564  1.00 45.74           O  
ANISOU 1696  O   SER A 208     6419   5243   5718   -828  -1576    204       O  
ATOM   1697  CB  SER A 208      73.520 -18.136 -43.936  1.00 48.53           C  
ANISOU 1697  CB  SER A 208     6112   5638   6689   -437  -1580    624       C  
ATOM   1698  OG  SER A 208      74.873 -18.517 -43.752  1.00 48.42           O  
ANISOU 1698  OG  SER A 208     6337   5501   6560   -366  -1366    545       O  
ATOM   1699  N   GLN A 209      73.429 -19.206 -46.775  1.00 52.29           N  
ANISOU 1699  N   GLN A 209     6988   6433   6446   -741  -1906    554       N  
ATOM   1700  CA  GLN A 209      74.159 -19.660 -47.954  1.00 51.30           C  
ANISOU 1700  CA  GLN A 209     7170   6416   5908   -795  -1892    464       C  
ATOM   1701  C   GLN A 209      75.656 -19.717 -47.687  1.00 50.43           C  
ANISOU 1701  C   GLN A 209     7248   6145   5769   -625  -1574    426       C  
ATOM   1702  O   GLN A 209      76.343 -20.629 -48.164  1.00 57.49           O  
ANISOU 1702  O   GLN A 209     8411   7013   6419   -650  -1439    208       O  
ATOM   1703  CB  GLN A 209      73.873 -18.751 -49.149  1.00 53.28           C  
ANISOU 1703  CB  GLN A 209     7366   6972   5906   -779  -2128    724       C  
ATOM   1704  CG  GLN A 209      74.486 -19.267 -50.435  1.00 58.55           C  
ANISOU 1704  CG  GLN A 209     8344   7854   6048   -862  -2116    606       C  
ATOM   1705  CD  GLN A 209      73.889 -20.597 -50.863  1.00 62.60           C  
ANISOU 1705  CD  GLN A 209     9014   8433   6338  -1125  -2244    214       C  
ATOM   1706  OE1 GLN A 209      72.668 -20.763 -50.888  1.00 70.03           O  
ANISOU 1706  OE1 GLN A 209     9764   9499   7346  -1308  -2530    181       O  
ATOM   1707  NE2 GLN A 209      74.747 -21.554 -51.197  1.00 58.41           N  
ANISOU 1707  NE2 GLN A 209     8815   7805   5572  -1149  -2025   -104       N  
ATOM   1708  N   MET A 210      76.185 -18.754 -46.930  1.00 44.37           N  
ANISOU 1708  N   MET A 210     6323   5274   5260   -449  -1452    608       N  
ATOM   1709  CA  MET A 210      77.605 -18.793 -46.601  1.00 44.79           C  
ANISOU 1709  CA  MET A 210     6477   5227   5313   -310  -1176    568       C  
ATOM   1710  C   MET A 210      77.953 -20.060 -45.826  1.00 50.82           C  
ANISOU 1710  C   MET A 210     7369   5813   6127   -287  -1016    322       C  
ATOM   1711  O   MET A 210      79.005 -20.667 -46.056  1.00 48.46           O  
ANISOU 1711  O   MET A 210     7242   5484   5686   -192   -825    205       O  
ATOM   1712  CB  MET A 210      78.009 -17.547 -45.807  1.00 43.19           C  
ANISOU 1712  CB  MET A 210     6057   4936   5419   -184  -1110    750       C  
ATOM   1713  CG  MET A 210      79.496 -17.515 -45.441  1.00 42.51           C  
ANISOU 1713  CG  MET A 210     5997   4809   5347    -73   -859    710       C  
ATOM   1714  SD  MET A 210      79.944 -16.209 -44.276  1.00 47.23           S  
ANISOU 1714  SD  MET A 210     6334   5278   6335      6   -801    794       S  
ATOM   1715  CE  MET A 210      79.501 -14.742 -45.216  1.00 49.61           C  
ANISOU 1715  CE  MET A 210     6567   5557   6724    -44   -936   1117       C  
ATOM   1716  N   GLU A 211      77.069 -20.488 -44.918  1.00 46.59           N  
ANISOU 1716  N   GLU A 211     6742   5161   5798   -360  -1076    266       N  
ATOM   1717  CA  GLU A 211      77.332 -21.701 -44.150  1.00 48.51           C  
ANISOU 1717  CA  GLU A 211     7127   5200   6106   -343   -926    115       C  
ATOM   1718  C   GLU A 211      77.217 -22.946 -45.021  1.00 50.74           C  
ANISOU 1718  C   GLU A 211     7703   5383   6191   -478   -932   -110       C  
ATOM   1719  O   GLU A 211      77.986 -23.900 -44.853  1.00 48.33           O  
ANISOU 1719  O   GLU A 211     7612   4876   5875   -370   -749   -240       O  
ATOM   1720  CB  GLU A 211      76.382 -21.782 -42.953  1.00 43.17           C  
ANISOU 1720  CB  GLU A 211     6268   4460   5676   -417   -958    163       C  
ATOM   1721  CG  GLU A 211      76.716 -20.790 -41.859  1.00 46.45           C  
ANISOU 1721  CG  GLU A 211     6453   4933   6265   -249   -885    279       C  
ATOM   1722  CD  GLU A 211      76.004 -21.081 -40.558  1.00 46.75           C  
ANISOU 1722  CD  GLU A 211     6354   4948   6462   -287   -834    297       C  
ATOM   1723  OE1 GLU A 211      74.969 -21.785 -40.587  1.00 49.56           O  
ANISOU 1723  OE1 GLU A 211     6707   5267   6855   -489   -889    275       O  
ATOM   1724  OE2 GLU A 211      76.484 -20.603 -39.507  1.00 43.64           O  
ANISOU 1724  OE2 GLU A 211     5843   4604   6134   -140   -733    325       O  
ATOM   1725  N   ILE A 212      76.259 -22.960 -45.952  1.00 47.47           N  
ANISOU 1725  N   ILE A 212     7298   5107   5630   -702  -1152   -176       N  
ATOM   1726  CA  ILE A 212      76.202 -24.041 -46.933  1.00 49.22           C  
ANISOU 1726  CA  ILE A 212     7819   5271   5610   -859  -1176   -467       C  
ATOM   1727  C   ILE A 212      77.515 -24.111 -47.706  1.00 55.06           C  
ANISOU 1727  C   ILE A 212     8775   6067   6076   -657   -981   -566       C  
ATOM   1728  O   ILE A 212      78.107 -25.186 -47.869  1.00 50.41           O  
ANISOU 1728  O   ILE A 212     8460   5258   5436   -594   -805   -825       O  
ATOM   1729  CB  ILE A 212      74.999 -23.851 -47.877  1.00 53.50           C  
ANISOU 1729  CB  ILE A 212     8280   6079   5969  -1138  -1499   -514       C  
ATOM   1730  CG1 ILE A 212      73.681 -24.027 -47.116  1.00 50.79           C  
ANISOU 1730  CG1 ILE A 212     7692   5682   5923  -1363  -1655   -470       C  
ATOM   1731  CG2 ILE A 212      75.080 -24.821 -49.062  1.00 56.81           C  
ANISOU 1731  CG2 ILE A 212     9031   6517   6038  -1306  -1537   -881       C  
ATOM   1732  CD1 ILE A 212      72.450 -23.938 -47.991  1.00 59.50           C  
ANISOU 1732  CD1 ILE A 212     8645   7085   6877  -1650  -2007   -527       C  
ATOM   1733  N   ASP A 213      78.000 -22.956 -48.174  1.00 50.43           N  
ANISOU 1733  N   ASP A 213     8057   5761   5342   -542   -985   -349       N  
ATOM   1734  CA  ASP A 213      79.258 -22.919 -48.917  1.00 52.76           C  
ANISOU 1734  CA  ASP A 213     8494   6185   5369   -370   -763   -401       C  
ATOM   1735  C   ASP A 213      80.424 -23.397 -48.060  1.00 51.35           C  
ANISOU 1735  C   ASP A 213     8331   5782   5398   -110   -473   -448       C  
ATOM   1736  O   ASP A 213      81.289 -24.143 -48.538  1.00 48.68           O  
ANISOU 1736  O   ASP A 213     8188   5407   4902     36   -256   -666       O  
ATOM   1737  CB  ASP A 213      79.524 -21.504 -49.431  1.00 54.08           C  
ANISOU 1737  CB  ASP A 213     8481   6655   5410   -337   -805    -71       C  
ATOM   1738  CG  ASP A 213      78.609 -21.115 -50.571  1.00 55.71           C  
ANISOU 1738  CG  ASP A 213     8716   7162   5288   -527  -1078      7       C  
ATOM   1739  OD1 ASP A 213      77.888 -21.993 -51.088  1.00 58.15           O  
ANISOU 1739  OD1 ASP A 213     9190   7505   5400   -704  -1228   -269       O  
ATOM   1740  OD2 ASP A 213      78.605 -19.924 -50.946  1.00 59.69           O  
ANISOU 1740  OD2 ASP A 213     9075   7865   5740   -508  -1157    356       O  
ATOM   1741  N   PHE A 214      80.462 -22.980 -46.790  1.00 46.95           N  
ANISOU 1741  N   PHE A 214     7554   5106   5179    -26   -469   -259       N  
ATOM   1742  CA  PHE A 214      81.556 -23.389 -45.912  1.00 48.58           C  
ANISOU 1742  CA  PHE A 214     7729   5173   5556    232   -247   -261       C  
ATOM   1743  C   PHE A 214      81.622 -24.901 -45.779  1.00 46.56           C  
ANISOU 1743  C   PHE A 214     7748   4600   5344    307   -138   -495       C  
ATOM   1744  O   PHE A 214      82.708 -25.490 -45.804  1.00 45.81           O  
ANISOU 1744  O   PHE A 214     7734   4430   5240    571     82   -588       O  
ATOM   1745  CB  PHE A 214      81.406 -22.758 -44.529  1.00 47.02           C  
ANISOU 1745  CB  PHE A 214     7272   4945   5649    268   -305    -58       C  
ATOM   1746  CG  PHE A 214      82.460 -23.205 -43.549  1.00 51.96           C  
ANISOU 1746  CG  PHE A 214     7840   5495   6409    528   -138    -35       C  
ATOM   1747  CD1 PHE A 214      83.684 -22.561 -43.489  1.00 44.76           C  
ANISOU 1747  CD1 PHE A 214     6732   4783   5492    695    -20     37       C  
ATOM   1748  CD2 PHE A 214      82.234 -24.288 -42.701  1.00 48.98           C  
ANISOU 1748  CD2 PHE A 214     7587   4862   6163    598   -108    -54       C  
ATOM   1749  CE1 PHE A 214      84.664 -22.976 -42.591  1.00 42.91           C  
ANISOU 1749  CE1 PHE A 214     6390   4550   5364    950     90     68       C  
ATOM   1750  CE2 PHE A 214      83.204 -24.707 -41.805  1.00 44.02           C  
ANISOU 1750  CE2 PHE A 214     6894   4202   5628    876     12     26       C  
ATOM   1751  CZ  PHE A 214      84.422 -24.056 -41.746  1.00 47.63           C  
ANISOU 1751  CZ  PHE A 214     7121   4914   6062   1066     94     76       C  
ATOM   1752  N   LEU A 215      80.469 -25.547 -45.635  1.00 46.76           N  
ANISOU 1752  N   LEU A 215     7901   4413   5452     79   -280   -584       N  
ATOM   1753  CA  LEU A 215      80.468 -26.993 -45.470  1.00 48.60           C  
ANISOU 1753  CA  LEU A 215     8426   4241   5798    108   -172   -787       C  
ATOM   1754  C   LEU A 215      80.763 -27.708 -46.781  1.00 52.84           C  
ANISOU 1754  C   LEU A 215     9270   4726   6081    104    -84  -1157       C  
ATOM   1755  O   LEU A 215      81.412 -28.763 -46.779  1.00 56.35           O  
ANISOU 1755  O   LEU A 215     9956   4846   6611    312    120  -1350       O  
ATOM   1756  CB  LEU A 215      79.130 -27.442 -44.887  1.00 54.01           C  
ANISOU 1756  CB  LEU A 215     9125   4714   6681   -199   -332   -756       C  
ATOM   1757  CG  LEU A 215      78.931 -26.996 -43.439  1.00 51.74           C  
ANISOU 1757  CG  LEU A 215     8581   4450   6627   -144   -339   -434       C  
ATOM   1758  CD1 LEU A 215      77.504 -27.262 -42.997  1.00 55.63           C  
ANISOU 1758  CD1 LEU A 215     9014   4848   7274   -489   -478   -389       C  
ATOM   1759  CD2 LEU A 215      79.937 -27.704 -42.530  1.00 50.73           C  
ANISOU 1759  CD2 LEU A 215     8543   4086   6646    179   -133   -322       C  
ATOM   1760  N   GLU A 216      80.323 -27.144 -47.905  1.00 53.18           N  
ANISOU 1760  N   GLU A 216     9313   5095   5797   -100   -228  -1258       N  
ATOM   1761  CA  GLU A 216      80.459 -27.841 -49.181  1.00 65.62           C  
ANISOU 1761  CA  GLU A 216    11200   6685   7046   -153   -166  -1668       C  
ATOM   1762  C   GLU A 216      81.831 -27.623 -49.809  1.00 65.60           C  
ANISOU 1762  C   GLU A 216    11211   6915   6798    171    117  -1726       C  
ATOM   1763  O   GLU A 216      82.426 -28.567 -50.339  1.00 69.06           O  
ANISOU 1763  O   GLU A 216    11919   7182   7137    334    337  -2089       O  
ATOM   1764  CB  GLU A 216      79.354 -27.398 -50.143  1.00 74.78           C  
ANISOU 1764  CB  GLU A 216    12352   8174   7888   -520   -472  -1744       C  
ATOM   1765  CG  GLU A 216      78.125 -28.306 -50.136  1.00 98.48           C  
ANISOU 1765  CG  GLU A 216    15504  10904  11010   -888   -682  -2003       C  
ATOM   1766  CD  GLU A 216      76.869 -27.636 -50.690  1.00112.41           C  
ANISOU 1766  CD  GLU A 216    17078  13058  12575  -1241  -1064  -1926       C  
ATOM   1767  OE1 GLU A 216      76.987 -26.631 -51.427  1.00115.73           O  
ANISOU 1767  OE1 GLU A 216    17370  13953  12650  -1195  -1164  -1750       O  
ATOM   1768  OE2 GLU A 216      75.757 -28.117 -50.379  1.00115.10           O  
ANISOU 1768  OE2 GLU A 216    17376  13238  13120  -1564  -1265  -2009       O  
ATOM   1769  N   LEU A 217      82.353 -26.399 -49.755  1.00 58.76           N  
ANISOU 1769  N   LEU A 217    10049   6419   5858    264    137  -1389       N  
ATOM   1770  CA  LEU A 217      83.569 -26.056 -50.480  1.00 62.10           C  
ANISOU 1770  CA  LEU A 217    10427   7157   6010    489    406  -1406       C  
ATOM   1771  C   LEU A 217      84.825 -26.461 -49.709  1.00 59.85           C  
ANISOU 1771  C   LEU A 217    10031   6706   6002    880    695  -1381       C  
ATOM   1772  O   LEU A 217      84.818 -26.623 -48.484  1.00 62.42           O  
ANISOU 1772  O   LEU A 217    10240   6768   6711    979    646  -1212       O  
ATOM   1773  CB  LEU A 217      83.623 -24.553 -50.764  1.00 62.44           C  
ANISOU 1773  CB  LEU A 217    10193   7629   5904    381    318  -1019       C  
ATOM   1774  CG  LEU A 217      82.502 -23.944 -51.603  1.00 59.77           C  
ANISOU 1774  CG  LEU A 217     9899   7549   5263     64     20   -931       C  
ATOM   1775  CD1 LEU A 217      82.619 -22.426 -51.623  1.00 62.94           C  
ANISOU 1775  CD1 LEU A 217    10016   8226   5671     18    -48   -461       C  
ATOM   1776  CD2 LEU A 217      82.543 -24.505 -53.010  1.00 58.77           C  
ANISOU 1776  CD2 LEU A 217    10064   7679   4588     -1     89  -1268       C  
ATOM   1777  N   ALA A 218      85.922 -26.608 -50.452  1.00 62.43           N  
ANISOU 1777  N   ALA A 218    10368   7253   6101   1116   1001  -1537       N  
ATOM   1778  CA  ALA A 218      87.236 -26.723 -49.840  1.00 57.50           C  
ANISOU 1778  CA  ALA A 218     9509   6633   5706   1504   1266  -1448       C  
ATOM   1779  C   ALA A 218      87.627 -25.397 -49.184  1.00 63.70           C  
ANISOU 1779  C   ALA A 218     9866   7705   6634   1446   1192  -1014       C  
ATOM   1780  O   ALA A 218      87.040 -24.344 -49.451  1.00 65.96           O  
ANISOU 1780  O   ALA A 218    10066   8197   6799   1148   1012   -797       O  
ATOM   1781  CB  ALA A 218      88.280 -27.138 -50.876  1.00 59.82           C  
ANISOU 1781  CB  ALA A 218     9862   7162   5706   1763   1641  -1735       C  
ATOM   1782  N   MET A 219      88.644 -25.463 -48.314  1.00 66.28           N  
ANISOU 1782  N   MET A 219     9916   8030   7237   1742   1324   -895       N  
ATOM   1783  CA  MET A 219      89.025 -24.305 -47.504  1.00 55.71           C  
ANISOU 1783  CA  MET A 219     8171   6906   6089   1666   1227   -553       C  
ATOM   1784  C   MET A 219      89.438 -23.124 -48.380  1.00 56.39           C  
ANISOU 1784  C   MET A 219     8064   7414   5947   1469   1328   -397       C  
ATOM   1785  O   MET A 219      88.927 -22.008 -48.221  1.00 55.33           O  
ANISOU 1785  O   MET A 219     7816   7343   5864   1185   1136   -152       O  
ATOM   1786  CB  MET A 219      90.153 -24.690 -46.539  1.00 60.85           C  
ANISOU 1786  CB  MET A 219     8538   7570   7012   2033   1344   -495       C  
ATOM   1787  CG  MET A 219      90.644 -23.545 -45.635  1.00 54.09           C  
ANISOU 1787  CG  MET A 219     7241   6964   6348   1936   1228   -217       C  
ATOM   1788  SD  MET A 219      91.991 -23.973 -44.485  1.00 59.58           S  
ANISOU 1788  SD  MET A 219     7532   7799   7308   2358   1296   -140       S  
ATOM   1789  CE  MET A 219      93.335 -24.399 -45.592  1.00 61.09           C  
ANISOU 1789  CE  MET A 219     7555   8293   7365   2673   1714   -299       C  
ATOM   1790  N   ASP A 220      90.357 -23.353 -49.323  1.00 57.05           N  
ANISOU 1790  N   ASP A 220     8113   7777   5787   1624   1652   -524       N  
ATOM   1791  CA  ASP A 220      90.841 -22.251 -50.149  1.00 65.92           C  
ANISOU 1791  CA  ASP A 220     9038   9324   6684   1424   1799   -313       C  
ATOM   1792  C   ASP A 220      89.760 -21.724 -51.084  1.00 65.60           C  
ANISOU 1792  C   ASP A 220     9274   9345   6307   1093   1633   -226       C  
ATOM   1793  O   ASP A 220      89.710 -20.516 -51.343  1.00 68.15           O  
ANISOU 1793  O   ASP A 220     9446   9852   6596    839   1580    110       O  
ATOM   1794  CB  ASP A 220      92.073 -22.684 -50.943  1.00 78.04           C  
ANISOU 1794  CB  ASP A 220    10448  11203   8000   1679   2232   -475       C  
ATOM   1795  CG  ASP A 220      93.215 -23.124 -50.047  1.00 95.76           C  
ANISOU 1795  CG  ASP A 220    12330  13461  10595   2042   2381   -510       C  
ATOM   1796  OD1 ASP A 220      93.746 -24.237 -50.262  1.00103.92           O  
ANISOU 1796  OD1 ASP A 220    13441  14447  11596   2432   2620   -805       O  
ATOM   1797  OD2 ASP A 220      93.563 -22.368 -49.111  1.00 94.08           O  
ANISOU 1797  OD2 ASP A 220    11753  13299  10696   1952   2243   -258       O  
ATOM   1798  N   GLU A 221      88.894 -22.602 -51.600  1.00 68.31           N  
ANISOU 1798  N   GLU A 221    10010   9529   6414   1084   1534   -513       N  
ATOM   1799  CA  GLU A 221      87.776 -22.138 -52.416  1.00 67.34           C  
ANISOU 1799  CA  GLU A 221    10112   9508   5965    776   1300   -424       C  
ATOM   1800  C   GLU A 221      86.873 -21.199 -51.629  1.00 56.48           C  
ANISOU 1800  C   GLU A 221     8607   7944   4908    557    945    -95       C  
ATOM   1801  O   GLU A 221      86.457 -20.151 -52.138  1.00 57.86           O  
ANISOU 1801  O   GLU A 221     8739   8296   4949    340    819    220       O  
ATOM   1802  CB  GLU A 221      86.965 -23.323 -52.934  1.00 71.58           C  
ANISOU 1802  CB  GLU A 221    11055   9881   6259    770   1205   -852       C  
ATOM   1803  CG  GLU A 221      87.664 -24.184 -53.961  1.00 88.61           C  
ANISOU 1803  CG  GLU A 221    13416  12246   8005    955   1547  -1251       C  
ATOM   1804  CD  GLU A 221      86.813 -25.368 -54.384  1.00110.48           C  
ANISOU 1804  CD  GLU A 221    16611  14769  10599    903   1424  -1743       C  
ATOM   1805  OE1 GLU A 221      86.049 -25.889 -53.540  1.00114.21           O  
ANISOU 1805  OE1 GLU A 221    17172  14779  11445    847   1182  -1813       O  
ATOM   1806  OE2 GLU A 221      86.901 -25.774 -55.563  1.00124.52           O  
ANISOU 1806  OE2 GLU A 221    18632  16828  11852    889   1575  -2072       O  
ATOM   1807  N   PHE A 222      86.558 -21.560 -50.384  1.00 52.54           N  
ANISOU 1807  N   PHE A 222     8050   7087   4826    633    796   -152       N  
ATOM   1808  CA  PHE A 222      85.653 -20.742 -49.580  1.00 52.61           C  
ANISOU 1808  CA  PHE A 222     7936   6924   5129    458    493     89       C  
ATOM   1809  C   PHE A 222      86.275 -19.391 -49.245  1.00 55.97           C  
ANISOU 1809  C   PHE A 222     8040   7465   5759    388    536    421       C  
ATOM   1810  O   PHE A 222      85.624 -18.348 -49.368  1.00 51.47           O  
ANISOU 1810  O   PHE A 222     7419   6887   5250    200    355    684       O  
ATOM   1811  CB  PHE A 222      85.274 -21.480 -48.298  1.00 47.90           C  
ANISOU 1811  CB  PHE A 222     7344   5981   4875    560    382    -46       C  
ATOM   1812  CG  PHE A 222      84.427 -20.664 -47.370  1.00 48.56           C  
ANISOU 1812  CG  PHE A 222     7269   5930   5251    418    130    153       C  
ATOM   1813  CD1 PHE A 222      83.052 -20.655 -47.504  1.00 48.39           C  
ANISOU 1813  CD1 PHE A 222     7360   5817   5210    236   -124    158       C  
ATOM   1814  CD2 PHE A 222      85.005 -19.895 -46.369  1.00 48.28           C  
ANISOU 1814  CD2 PHE A 222     6946   5891   5507    467    148    301       C  
ATOM   1815  CE1 PHE A 222      82.262 -19.901 -46.658  1.00 47.42           C  
ANISOU 1815  CE1 PHE A 222     7062   5591   5365    148   -317    315       C  
ATOM   1816  CE2 PHE A 222      84.220 -19.124 -45.523  1.00 46.05           C  
ANISOU 1816  CE2 PHE A 222     6532   5488   5478    356    -53    419       C  
ATOM   1817  CZ  PHE A 222      82.844 -19.132 -45.668  1.00 46.39           C  
ANISOU 1817  CZ  PHE A 222     6686   5430   5511    219   -268    430       C  
ATOM   1818  N   ILE A 223      87.529 -19.397 -48.790  1.00 52.18           N  
ANISOU 1818  N   ILE A 223     7325   7073   5428    541    764    408       N  
ATOM   1819  CA  ILE A 223      88.184 -18.153 -48.405  1.00 51.91           C  
ANISOU 1819  CA  ILE A 223     6964   7125   5636    421    804    671       C  
ATOM   1820  C   ILE A 223      88.299 -17.217 -49.600  1.00 59.34           C  
ANISOU 1820  C   ILE A 223     7915   8292   6341    214    903    955       C  
ATOM   1821  O   ILE A 223      88.168 -15.994 -49.461  1.00 58.76           O  
ANISOU 1821  O   ILE A 223     7705   8138   6481     14    814   1245       O  
ATOM   1822  CB  ILE A 223      89.553 -18.471 -47.771  1.00 52.66           C  
ANISOU 1822  CB  ILE A 223     6761   7351   5897    618   1019    573       C  
ATOM   1823  CG1 ILE A 223      89.352 -19.074 -46.377  1.00 48.90           C  
ANISOU 1823  CG1 ILE A 223     6239   6648   5692    786    850    426       C  
ATOM   1824  CG2 ILE A 223      90.435 -17.234 -47.708  1.00 50.21           C  
ANISOU 1824  CG2 ILE A 223     6093   7213   5769    429   1124    808       C  
ATOM   1825  CD1 ILE A 223      90.638 -19.558 -45.731  1.00 48.46           C  
ANISOU 1825  CD1 ILE A 223     5890   6755   5766   1045   1007    342       C  
ATOM   1826  N   GLU A 224      88.509 -17.771 -50.793  1.00 61.13           N  
ANISOU 1826  N   GLU A 224     8326   8788   6114    260   1093    882       N  
ATOM   1827  CA  GLU A 224      88.566 -16.943 -51.992  1.00 61.04           C  
ANISOU 1827  CA  GLU A 224     8358   9055   5779     64   1192   1202       C  
ATOM   1828  C   GLU A 224      87.200 -16.359 -52.315  1.00 64.73           C  
ANISOU 1828  C   GLU A 224     9021   9394   6179   -104    849   1427       C  
ATOM   1829  O   GLU A 224      87.087 -15.163 -52.608  1.00 62.83           O  
ANISOU 1829  O   GLU A 224     8704   9151   6016   -284    799   1847       O  
ATOM   1830  CB  GLU A 224      89.091 -17.760 -53.170  1.00 73.01           C  
ANISOU 1830  CB  GLU A 224    10040  10957   6745    175   1490   1011       C  
ATOM   1831  CG  GLU A 224      89.225 -16.971 -54.458  1.00 91.06           C  
ANISOU 1831  CG  GLU A 224    12379  13628   8590    -23   1635   1373       C  
ATOM   1832  CD  GLU A 224      88.822 -17.778 -55.677  1.00109.11           C  
ANISOU 1832  CD  GLU A 224    15015  16239  10202     23   1682   1144       C  
ATOM   1833  OE1 GLU A 224      87.809 -17.424 -56.320  1.00114.80           O  
ANISOU 1833  OE1 GLU A 224    15952  17040  10627   -135   1410   1338       O  
ATOM   1834  OE2 GLU A 224      89.515 -18.771 -55.989  1.00113.92           O  
ANISOU 1834  OE2 GLU A 224    15675  17032  10577    232   1981    749       O  
ATOM   1835  N   ARG A 225      86.149 -17.182 -52.245  1.00 59.85           N  
ANISOU 1835  N   ARG A 225     8632   8650   5459    -47    606   1170       N  
ATOM   1836  CA  ARG A 225      84.824 -16.734 -52.659  1.00 65.17           C  
ANISOU 1836  CA  ARG A 225     9443   9292   6025   -184    265   1365       C  
ATOM   1837  C   ARG A 225      84.322 -15.587 -51.791  1.00 61.39           C  
ANISOU 1837  C   ARG A 225     8765   8500   6060   -254     59   1657       C  
ATOM   1838  O   ARG A 225      83.715 -14.635 -52.296  1.00 59.48           O  
ANISOU 1838  O   ARG A 225     8531   8271   5796   -357   -109   2034       O  
ATOM   1839  CB  ARG A 225      83.837 -17.899 -52.619  1.00 66.06           C  
ANISOU 1839  CB  ARG A 225     9774   9324   6003   -151     52    986       C  
ATOM   1840  CG  ARG A 225      82.382 -17.476 -52.794  1.00 65.06           C  
ANISOU 1840  CG  ARG A 225     9684   9165   5871   -282   -348   1158       C  
ATOM   1841  CD  ARG A 225      81.480 -18.678 -52.960  1.00 69.34           C  
ANISOU 1841  CD  ARG A 225    10427   9700   6218   -326   -537    764       C  
ATOM   1842  NE  ARG A 225      81.892 -19.487 -54.102  1.00 77.34           N  
ANISOU 1842  NE  ARG A 225    11700  11026   6661   -337   -385    494       N  
ATOM   1843  CZ  ARG A 225      81.268 -20.588 -54.500  1.00 81.82           C  
ANISOU 1843  CZ  ARG A 225    12497  11618   6974   -415   -509     79       C  
ATOM   1844  NH1 ARG A 225      80.196 -21.015 -53.846  1.00 87.15           N  
ANISOU 1844  NH1 ARG A 225    13147  12032   7936   -515   -786    -60       N  
ATOM   1845  NH2 ARG A 225      81.716 -21.262 -55.553  1.00 81.30           N  
ANISOU 1845  NH2 ARG A 225    12680  11842   6370   -412   -340   -220       N  
ATOM   1846  N   TYR A 226      84.553 -15.661 -50.482  1.00 56.05           N  
ANISOU 1846  N   TYR A 226     8633   6795   5870    845    710   1282       N  
ATOM   1847  CA  TYR A 226      84.101 -14.629 -49.563  1.00 57.57           C  
ANISOU 1847  CA  TYR A 226     8716   6864   6293    750    686   1352       C  
ATOM   1848  C   TYR A 226      85.198 -13.624 -49.229  1.00 57.36           C  
ANISOU 1848  C   TYR A 226     8613   6720   6463    704    888   1523       C  
ATOM   1849  O   TYR A 226      85.023 -12.809 -48.317  1.00 56.82           O  
ANISOU 1849  O   TYR A 226     8445   6525   6621    611    878   1554       O  
ATOM   1850  CB  TYR A 226      83.517 -15.279 -48.301  1.00 52.43           C  
ANISOU 1850  CB  TYR A 226     7973   6148   5801    615    536   1162       C  
ATOM   1851  CG  TYR A 226      82.205 -15.973 -48.619  1.00 55.11           C  
ANISOU 1851  CG  TYR A 226     8360   6580   6000    649    326   1026       C  
ATOM   1852  CD1 TYR A 226      82.175 -17.310 -49.001  1.00 46.52           C  
ANISOU 1852  CD1 TYR A 226     7336   5566   4774    667    248    859       C  
ATOM   1853  CD2 TYR A 226      81.002 -15.268 -48.604  1.00 53.13           C  
ANISOU 1853  CD2 TYR A 226     8087   6341   5760    670    205   1065       C  
ATOM   1854  CE1 TYR A 226      80.978 -17.934 -49.327  1.00 56.16           C  
ANISOU 1854  CE1 TYR A 226     8587   6861   5890    689     46    725       C  
ATOM   1855  CE2 TYR A 226      79.805 -15.884 -48.926  1.00 55.76           C  
ANISOU 1855  CE2 TYR A 226     8442   6764   5980    698      8    941       C  
ATOM   1856  CZ  TYR A 226      79.799 -17.217 -49.282  1.00 55.28           C  
ANISOU 1856  CZ  TYR A 226     8436   6768   5800    700    -75    767       C  
ATOM   1857  OH  TYR A 226      78.611 -17.828 -49.606  1.00 58.09           O  
ANISOU 1857  OH  TYR A 226     8799   7202   6071    716   -282    632       O  
ATOM   1858  N   LYS A 227      86.308 -13.651 -49.968  1.00 57.58           N  
ANISOU 1858  N   LYS A 227     8680   6785   6413    770   1072   1633       N  
ATOM   1859  CA  LYS A 227      87.377 -12.656 -49.873  1.00 58.80           C  
ANISOU 1859  CA  LYS A 227     8757   6833   6752    736   1281   1823       C  
ATOM   1860  C   LYS A 227      87.844 -12.479 -48.426  1.00 53.18           C  
ANISOU 1860  C   LYS A 227     7887   5966   6353    563   1274   1740       C  
ATOM   1861  O   LYS A 227      87.834 -11.383 -47.866  1.00 54.84           O  
ANISOU 1861  O   LYS A 227     8013   6042   6781    495   1302   1826       O  
ATOM   1862  CB  LYS A 227      86.920 -11.321 -50.474  1.00 63.94           C  
ANISOU 1862  CB  LYS A 227     9440   7452   7402    812   1336   2045       C  
ATOM   1863  CG  LYS A 227      86.216 -11.430 -51.831  1.00 72.24           C  
ANISOU 1863  CG  LYS A 227    10652   8676   8121   1003   1299   2118       C  
ATOM   1864  CD  LYS A 227      87.173 -11.248 -53.003  1.00 87.49           C  
ANISOU 1864  CD  LYS A 227    12658  10688   9896   1138   1526   2319       C  
ATOM   1865  CE  LYS A 227      86.422 -10.966 -54.312  1.00 91.93           C  
ANISOU 1865  CE  LYS A 227    13375  11409  10145   1347   1500   2446       C  
ATOM   1866  NZ  LYS A 227      85.618 -12.131 -54.792  1.00 95.86           N  
ANISOU 1866  NZ  LYS A 227    13985  12085  10351   1435   1294   2229       N  
ATOM   1867  N   LEU A 228      88.259 -13.589 -47.818  1.00 51.78           N  
ANISOU 1867  N   LEU A 228     7673   5808   6193    502   1231   1565       N  
ATOM   1868  CA  LEU A 228      88.626 -13.597 -46.410  1.00 50.05           C  
ANISOU 1868  CA  LEU A 228     7315   5474   6227    359   1195   1460       C  
ATOM   1869  C   LEU A 228      90.133 -13.695 -46.182  1.00 52.38           C  
ANISOU 1869  C   LEU A 228     7516   5729   6657    313   1357   1494       C  
ATOM   1870  O   LEU A 228      90.561 -13.928 -45.045  1.00 44.43           O  
ANISOU 1870  O   LEU A 228     6397   4657   5826    212   1319   1384       O  
ATOM   1871  CB  LEU A 228      87.901 -14.736 -45.688  1.00 42.76           C  
ANISOU 1871  CB  LEU A 228     6401   4588   5257    319   1016   1245       C  
ATOM   1872  CG  LEU A 228      86.406 -14.502 -45.460  1.00 45.65           C  
ANISOU 1872  CG  LEU A 228     6793   4958   5592    318    842   1196       C  
ATOM   1873  CD1 LEU A 228      85.682 -15.797 -45.038  1.00 47.19           C  
ANISOU 1873  CD1 LEU A 228     7010   5208   5712    294    685   1004       C  
ATOM   1874  CD2 LEU A 228      86.214 -13.442 -44.404  1.00 52.19           C  
ANISOU 1874  CD2 LEU A 228     7514   5659   6657    233    822   1220       C  
ATOM   1875  N   GLU A 229      90.944 -13.500 -47.222  1.00 52.57           N  
ANISOU 1875  N   GLU A 229     7573   5799   6602    394   1538   1650       N  
ATOM   1876  CA  GLU A 229      92.396 -13.541 -47.067  1.00 58.85           C  
ANISOU 1876  CA  GLU A 229     8257   6562   7541    354   1706   1700       C  
ATOM   1877  C   GLU A 229      92.852 -12.530 -46.020  1.00 58.41           C  
ANISOU 1877  C   GLU A 229     8032   6341   7818    214   1722   1726       C  
ATOM   1878  O   GLU A 229      92.408 -11.380 -46.013  1.00 55.71           O  
ANISOU 1878  O   GLU A 229     7677   5901   7590    190   1724   1831       O  
ATOM   1879  CB  GLU A 229      93.086 -13.250 -48.403  1.00 61.53           C  
ANISOU 1879  CB  GLU A 229     8652   6971   7757    471   1921   1908       C  
ATOM   1880  CG  GLU A 229      92.649 -14.137 -49.563  1.00 75.75           C  
ANISOU 1880  CG  GLU A 229    10635   8946   9202    636   1907   1885       C  
ATOM   1881  CD  GLU A 229      91.366 -13.660 -50.227  1.00 88.69           C  
ANISOU 1881  CD  GLU A 229    12404  10631  10664    721   1806   1940       C  
ATOM   1882  OE1 GLU A 229      90.730 -12.721 -49.703  1.00 92.01           O  
ANISOU 1882  OE1 GLU A 229    12776  10943  11240    650   1735   1982       O  
ATOM   1883  OE2 GLU A 229      90.995 -14.226 -51.277  1.00 94.06           O  
ANISOU 1883  OE2 GLU A 229    13235  11460  11045    870   1792   1932       O  
ATOM   1884  N   GLY A 230      93.728 -12.968 -45.120  1.00 58.26           N  
ANISOU 1884  N   GLY A 230     7886   6290   7958    130   1724   1619       N  
ATOM   1885  CA  GLY A 230      94.245 -12.086 -44.098  1.00 53.88           C  
ANISOU 1885  CA  GLY A 230     7164   5590   7718      2   1721   1610       C  
ATOM   1886  C   GLY A 230      93.448 -12.047 -42.811  1.00 51.42           C  
ANISOU 1886  C   GLY A 230     6821   5221   7495    -74   1519   1434       C  
ATOM   1887  O   GLY A 230      93.851 -11.344 -41.874  1.00 51.72           O  
ANISOU 1887  O   GLY A 230     6725   5144   7783   -172   1493   1392       O  
ATOM   1888  N   TYR A 231      92.327 -12.762 -42.730  1.00 42.00           N  
ANISOU 1888  N   TYR A 231     5742   4105   6112    -28   1376   1328       N  
ATOM   1889  CA  TYR A 231      91.565 -12.836 -41.492  1.00 43.65           C  
ANISOU 1889  CA  TYR A 231     5918   4278   6389    -86   1201   1170       C  
ATOM   1890  C   TYR A 231      91.834 -14.109 -40.715  1.00 42.19           C  
ANISOU 1890  C   TYR A 231     5707   4162   6160    -97   1129   1009       C  
ATOM   1891  O   TYR A 231      91.126 -14.383 -39.740  1.00 43.31           O  
ANISOU 1891  O   TYR A 231     5840   4301   6314   -124    991    885       O  
ATOM   1892  CB  TYR A 231      90.069 -12.704 -41.776  1.00 45.33           C  
ANISOU 1892  CB  TYR A 231     6246   4517   6462    -37   1088   1169       C  
ATOM   1893  CG  TYR A 231      89.725 -11.318 -42.249  1.00 48.51           C  
ANISOU 1893  CG  TYR A 231     6657   4827   6946    -27   1137   1319       C  
ATOM   1894  CD1 TYR A 231      89.663 -10.256 -41.353  1.00 50.72           C  
ANISOU 1894  CD1 TYR A 231     6844   4968   7458   -100   1101   1301       C  
ATOM   1895  CD2 TYR A 231      89.507 -11.058 -43.594  1.00 49.98           C  
ANISOU 1895  CD2 TYR A 231     6948   5062   6979     66   1224   1480       C  
ATOM   1896  CE1 TYR A 231      89.358  -8.963 -41.784  1.00 50.89           C  
ANISOU 1896  CE1 TYR A 231     6877   4882   7578    -88   1152   1445       C  
ATOM   1897  CE2 TYR A 231      89.201  -9.770 -44.033  1.00 54.66           C  
ANISOU 1897  CE2 TYR A 231     7552   5563   7654     87   1279   1641       C  
ATOM   1898  CZ  TYR A 231      89.129  -8.732 -43.123  1.00 51.54           C  
ANISOU 1898  CZ  TYR A 231     7062   5009   7510      5   1246   1625       C  
ATOM   1899  OH  TYR A 231      88.832  -7.460 -43.560  1.00 64.86           O  
ANISOU 1899  OH  TYR A 231     8764   6584   9296     30   1306   1788       O  
ATOM   1900  N   ALA A 232      92.816 -14.905 -41.142  1.00 44.94           N  
ANISOU 1900  N   ALA A 232     6048   4574   6454    -65   1228   1018       N  
ATOM   1901  CA  ALA A 232      93.265 -16.091 -40.405  1.00 44.65           C  
ANISOU 1901  CA  ALA A 232     5976   4590   6401    -68   1181    883       C  
ATOM   1902  C   ALA A 232      92.150 -17.118 -40.188  1.00 40.13           C  
ANISOU 1902  C   ALA A 232     5509   4073   5666    -36   1046    770       C  
ATOM   1903  O   ALA A 232      92.130 -17.817 -39.166  1.00 40.46           O  
ANISOU 1903  O   ALA A 232     5510   4121   5742    -58    964    655       O  
ATOM   1904  CB  ALA A 232      93.887 -15.701 -39.061  1.00 46.23           C  
ANISOU 1904  CB  ALA A 232     6017   4727   6822   -149   1134    805       C  
ATOM   1905  N   PHE A 233      91.220 -17.244 -41.143  1.00 41.31           N  
ANISOU 1905  N   PHE A 233     5789   4263   5643     20   1021    804       N  
ATOM   1906  CA  PHE A 233      90.192 -18.275 -41.013  1.00 40.54           C  
ANISOU 1906  CA  PHE A 233     5778   4210   5416     40    894    693       C  
ATOM   1907  C   PHE A 233      90.801 -19.670 -41.015  1.00 43.51           C  
ANISOU 1907  C   PHE A 233     6179   4630   5722     75    917    609       C  
ATOM   1908  O   PHE A 233      90.293 -20.564 -40.334  1.00 41.82           O  
ANISOU 1908  O   PHE A 233     5974   4415   5500     60    821    503       O  
ATOM   1909  CB  PHE A 233      89.155 -18.146 -42.127  1.00 47.58           C  
ANISOU 1909  CB  PHE A 233     6794   5147   6138     99    853    735       C  
ATOM   1910  CG  PHE A 233      87.938 -17.364 -41.721  1.00 49.13           C  
ANISOU 1910  CG  PHE A 233     6979   5307   6380     66    741    741       C  
ATOM   1911  CD1 PHE A 233      88.067 -16.202 -40.977  1.00 57.56           C  
ANISOU 1911  CD1 PHE A 233     7951   6293   7626     11    754    788       C  
ATOM   1912  CD2 PHE A 233      86.665 -17.794 -42.069  1.00 54.20           C  
ANISOU 1912  CD2 PHE A 233     7700   5995   6899     93    619    690       C  
ATOM   1913  CE1 PHE A 233      86.951 -15.477 -40.590  1.00 60.85           C  
ANISOU 1913  CE1 PHE A 233     8360   6676   8085     -4    658    790       C  
ATOM   1914  CE2 PHE A 233      85.544 -17.070 -41.690  1.00 48.14           C  
ANISOU 1914  CE2 PHE A 233     6909   5203   6180     72    522    702       C  
ATOM   1915  CZ  PHE A 233      85.690 -15.913 -40.950  1.00 54.93           C  
ANISOU 1915  CZ  PHE A 233     7683   5983   7206     30    547    754       C  
ATOM   1916  N   GLU A 234      91.899 -19.866 -41.752  1.00 46.38           N  
ANISOU 1916  N   GLU A 234     6549   5029   6045    128   1054    664       N  
ATOM   1917  CA  GLU A 234      92.569 -21.164 -41.767  1.00 48.63           C  
ANISOU 1917  CA  GLU A 234     6856   5349   6272    175   1088    586       C  
ATOM   1918  C   GLU A 234      92.863 -21.640 -40.351  1.00 51.06           C  
ANISOU 1918  C   GLU A 234     7061   5620   6718    122   1029    501       C  
ATOM   1919  O   GLU A 234      92.723 -22.828 -40.039  1.00 53.68           O  
ANISOU 1919  O   GLU A 234     7434   5958   7005    146    980    408       O  
ATOM   1920  CB  GLU A 234      93.864 -21.071 -42.580  1.00 49.03           C  
ANISOU 1920  CB  GLU A 234     6886   5440   6302    238   1265    676       C  
ATOM   1921  CG  GLU A 234      93.681 -20.629 -44.023  1.00 58.00           C  
ANISOU 1921  CG  GLU A 234     8131   6632   7275    318   1348    780       C  
ATOM   1922  CD  GLU A 234      93.766 -19.115 -44.204  1.00 72.07           C  
ANISOU 1922  CD  GLU A 234     9847   8375   9162    277   1419    937       C  
ATOM   1923  OE1 GLU A 234      93.553 -18.362 -43.227  1.00 63.41           O  
ANISOU 1923  OE1 GLU A 234     8648   7197   8248    179   1353    933       O  
ATOM   1924  OE2 GLU A 234      94.055 -18.682 -45.339  1.00 75.15           O  
ANISOU 1924  OE2 GLU A 234    10291   8811   9450    354   1547   1067       O  
ATOM   1925  N   HIS A 235      93.252 -20.710 -39.476  1.00 44.38           N  
ANISOU 1925  N   HIS A 235     6084   4735   6044     57   1028    530       N  
ATOM   1926  CA  HIS A 235      93.549 -21.003 -38.079  1.00 42.02           C  
ANISOU 1926  CA  HIS A 235     5682   4419   5864     22    964    453       C  
ATOM   1927  C   HIS A 235      92.274 -20.975 -37.236  1.00 38.06           C  
ANISOU 1927  C   HIS A 235     5202   3894   5365    -15    824    392       C  
ATOM   1928  O   HIS A 235      91.900 -21.979 -36.616  1.00 39.35           O  
ANISOU 1928  O   HIS A 235     5388   4067   5496      0    762    321       O  
ATOM   1929  CB  HIS A 235      94.590 -19.987 -37.582  1.00 38.44           C  
ANISOU 1929  CB  HIS A 235     5074   3939   5591    -25   1018    494       C  
ATOM   1930  CG  HIS A 235      94.902 -20.067 -36.121  1.00 45.81           C  
ANISOU 1930  CG  HIS A 235     5894   4870   6643    -52    935    408       C  
ATOM   1931  ND1 HIS A 235      95.928 -20.842 -35.616  1.00 43.60           N  
ANISOU 1931  ND1 HIS A 235     5539   4632   6397    -15    960    368       N  
ATOM   1932  CD2 HIS A 235      94.359 -19.424 -35.061  1.00 43.84           C  
ANISOU 1932  CD2 HIS A 235     5591   4590   6475    -96    828    355       C  
ATOM   1933  CE1 HIS A 235      95.983 -20.692 -34.303  1.00 44.96           C  
ANISOU 1933  CE1 HIS A 235     5620   4807   6655    -33    864    295       C  
ATOM   1934  NE2 HIS A 235      95.040 -19.836 -33.941  1.00 44.20           N  
ANISOU 1934  NE2 HIS A 235     5539   4669   6587    -81    785    281       N  
ATOM   1935  N   ILE A 236      91.558 -19.846 -37.260  1.00 38.20           N  
ANISOU 1935  N   ILE A 236     5214   3878   5422    -56    784    431       N  
ATOM   1936  CA  ILE A 236      90.474 -19.606 -36.303  1.00 36.06           C  
ANISOU 1936  CA  ILE A 236     4931   3588   5184    -87    665    380       C  
ATOM   1937  C   ILE A 236      89.308 -20.564 -36.532  1.00 37.90           C  
ANISOU 1937  C   ILE A 236     5263   3843   5296    -68    593    341       C  
ATOM   1938  O   ILE A 236      88.744 -21.117 -35.580  1.00 37.87           O  
ANISOU 1938  O   ILE A 236     5240   3841   5308    -75    522    285       O  
ATOM   1939  CB  ILE A 236      89.991 -18.144 -36.391  1.00 37.15           C  
ANISOU 1939  CB  ILE A 236     5044   3676   5395   -122    649    434       C  
ATOM   1940  CG1 ILE A 236      91.107 -17.156 -36.042  1.00 33.64           C  
ANISOU 1940  CG1 ILE A 236     4483   3183   5115   -158    707    458       C  
ATOM   1941  CG2 ILE A 236      88.768 -17.946 -35.507  1.00 34.10           C  
ANISOU 1941  CG2 ILE A 236     4655   3281   5021   -134    534    383       C  
ATOM   1942  CD1 ILE A 236      90.768 -15.710 -36.427  1.00 46.41           C  
ANISOU 1942  CD1 ILE A 236     6092   4724   6817   -188    722    535       C  
ATOM   1943  N   VAL A 237      88.875 -20.714 -37.778  1.00 37.33           N  
ANISOU 1943  N   VAL A 237     5290   3786   5106    -42    606    372       N  
ATOM   1944  CA  VAL A 237      87.663 -21.471 -38.070  1.00 38.25           C  
ANISOU 1944  CA  VAL A 237     5488   3916   5130    -37    515    325       C  
ATOM   1945  C   VAL A 237      87.975 -22.907 -38.477  1.00 40.83           C  
ANISOU 1945  C   VAL A 237     5883   4253   5377     -1    531    261       C  
ATOM   1946  O   VAL A 237      87.336 -23.841 -38.000  1.00 42.60           O  
ANISOU 1946  O   VAL A 237     6119   4458   5609    -16    464    197       O  
ATOM   1947  CB  VAL A 237      86.809 -20.757 -39.143  1.00 40.47           C  
ANISOU 1947  CB  VAL A 237     5837   4215   5323    -21    483    376       C  
ATOM   1948  CG1 VAL A 237      85.537 -21.551 -39.381  1.00 40.55           C  
ANISOU 1948  CG1 VAL A 237     5906   4242   5260    -23    369    310       C  
ATOM   1949  CG2 VAL A 237      86.472 -19.324 -38.704  1.00 37.13           C  
ANISOU 1949  CG2 VAL A 237     5350   3762   4998    -49    470    441       C  
ATOM   1950  N   TYR A 238      88.936 -23.106 -39.379  1.00 40.70           N  
ANISOU 1950  N   TYR A 238     5912   4262   5290     51    627    282       N  
ATOM   1951  CA  TYR A 238      89.216 -24.466 -39.852  1.00 37.26           C  
ANISOU 1951  CA  TYR A 238     5555   3829   4772    100    642    209       C  
ATOM   1952  C   TYR A 238      90.035 -25.282 -38.859  1.00 41.14           C  
ANISOU 1952  C   TYR A 238     5985   4294   5353    104    678    174       C  
ATOM   1953  O   TYR A 238      89.898 -26.514 -38.818  1.00 42.56           O  
ANISOU 1953  O   TYR A 238     6217   4442   5510    126    654    102       O  
ATOM   1954  CB  TYR A 238      89.941 -24.408 -41.196  1.00 39.91           C  
ANISOU 1954  CB  TYR A 238     5968   4214   4980    178    742    243       C  
ATOM   1955  CG  TYR A 238      89.061 -23.946 -42.331  1.00 48.61           C  
ANISOU 1955  CG  TYR A 238     7166   5359   5944    207    694    263       C  
ATOM   1956  CD1 TYR A 238      88.318 -24.862 -43.072  1.00 45.14           C  
ANISOU 1956  CD1 TYR A 238     6841   4934   5376    245    608    162       C  
ATOM   1957  CD2 TYR A 238      88.964 -22.597 -42.661  1.00 47.25           C  
ANISOU 1957  CD2 TYR A 238     6969   5208   5775    202    728    378       C  
ATOM   1958  CE1 TYR A 238      87.507 -24.449 -44.112  1.00 49.50           C  
ANISOU 1958  CE1 TYR A 238     7477   5543   5787    285    546    171       C  
ATOM   1959  CE2 TYR A 238      88.153 -22.172 -43.702  1.00 45.82           C  
ANISOU 1959  CE2 TYR A 238     6878   5077   5456    248    682    408       C  
ATOM   1960  CZ  TYR A 238      87.429 -23.105 -44.423  1.00 51.55           C  
ANISOU 1960  CZ  TYR A 238     7713   5838   6034    293    586    301       C  
ATOM   1961  OH  TYR A 238      86.619 -22.692 -45.450  1.00 50.36           O  
ANISOU 1961  OH  TYR A 238     7648   5754   5733    351    522    322       O  
ATOM   1962  N   GLY A 239      90.877 -24.633 -38.070  1.00 42.77           N  
ANISOU 1962  N   GLY A 239     6079   4507   5665     89    729    220       N  
ATOM   1963  CA  GLY A 239      91.763 -25.324 -37.143  1.00 41.94           C  
ANISOU 1963  CA  GLY A 239     5904   4397   5633    111    761    195       C  
ATOM   1964  C   GLY A 239      93.085 -25.715 -37.781  1.00 41.86           C  
ANISOU 1964  C   GLY A 239     5895   4415   5596    179    880    210       C  
ATOM   1965  O   GLY A 239      93.180 -26.003 -38.970  1.00 43.36           O  
ANISOU 1965  O   GLY A 239     6178   4620   5675    228    934    209       O  
ATOM   1966  N   ASP A 240      94.129 -25.725 -36.958  1.00 40.56           N  
ANISOU 1966  N   ASP A 240     5616   4266   5527    193    921    219       N  
ATOM   1967  CA  ASP A 240      95.487 -26.087 -37.364  1.00 40.77           C  
ANISOU 1967  CA  ASP A 240     5605   4327   5558    261   1038    238       C  
ATOM   1968  C   ASP A 240      95.892 -27.310 -36.545  1.00 40.10           C  
ANISOU 1968  C   ASP A 240     5505   4232   5499    318   1026    188       C  
ATOM   1969  O   ASP A 240      96.079 -27.213 -35.329  1.00 40.31           O  
ANISOU 1969  O   ASP A 240     5432   4268   5614    304    974    182       O  
ATOM   1970  CB  ASP A 240      96.446 -24.907 -37.139  1.00 44.63           C  
ANISOU 1970  CB  ASP A 240     5945   4846   6168    227   1097    303       C  
ATOM   1971  CG  ASP A 240      97.880 -25.196 -37.582  1.00 47.95           C  
ANISOU 1971  CG  ASP A 240     6297   5310   6613    294   1230    337       C  
ATOM   1972  OD1 ASP A 240      98.195 -26.347 -37.963  1.00 46.99           O  
ANISOU 1972  OD1 ASP A 240     6246   5198   6409    381   1278    305       O  
ATOM   1973  OD2 ASP A 240      98.705 -24.254 -37.543  1.00 46.54           O  
ANISOU 1973  OD2 ASP A 240     5985   5148   6550    259   1290    396       O  
ATOM   1974  N   PHE A 241      96.020 -28.462 -37.206  1.00 40.62           N  
ANISOU 1974  N   PHE A 241     5674   4277   5481    392   1070    150       N  
ATOM   1975  CA  PHE A 241      96.314 -29.718 -36.528  1.00 42.10           C  
ANISOU 1975  CA  PHE A 241     5869   4433   5695    456   1064    110       C  
ATOM   1976  C   PHE A 241      97.741 -30.178 -36.786  1.00 44.69           C  
ANISOU 1976  C   PHE A 241     6146   4801   6033    556   1180    124       C  
ATOM   1977  O   PHE A 241      98.038 -31.374 -36.671  1.00 42.29           O  
ANISOU 1977  O   PHE A 241     5889   4460   5718    638   1202     88       O  
ATOM   1978  CB  PHE A 241      95.311 -30.796 -36.955  1.00 40.64           C  
ANISOU 1978  CB  PHE A 241     5836   4164   5441    465   1014     42       C  
ATOM   1979  CG  PHE A 241      93.874 -30.417 -36.695  1.00 37.65           C  
ANISOU 1979  CG  PHE A 241     5489   3749   5065    369    900     32       C  
ATOM   1980  CD1 PHE A 241      93.200 -29.552 -37.556  1.00 43.72           C  
ANISOU 1980  CD1 PHE A 241     6303   4542   5767    319    873     37       C  
ATOM   1981  CD2 PHE A 241      93.198 -30.908 -35.583  1.00 38.84           C  
ANISOU 1981  CD2 PHE A 241     5619   3851   5286    340    830     31       C  
ATOM   1982  CE1 PHE A 241      91.879 -29.191 -37.311  1.00 48.59           C  
ANISOU 1982  CE1 PHE A 241     6935   5133   6394    239    768     30       C  
ATOM   1983  CE2 PHE A 241      91.872 -30.547 -35.333  1.00 49.49           C  
ANISOU 1983  CE2 PHE A 241     6982   5176   6648    257    737     30       C  
ATOM   1984  CZ  PHE A 241      91.217 -29.687 -36.192  1.00 42.33           C  
ANISOU 1984  CZ  PHE A 241     6111   4293   5681    206    702     24       C  
ATOM   1985  N   SER A 242      98.634 -29.249 -37.128  1.00 40.19           N  
ANISOU 1985  N   SER A 242     5473   4299   5498    551   1259    181       N  
ATOM   1986  CA  SER A 242      99.982 -29.616 -37.539  1.00 45.51           C  
ANISOU 1986  CA  SER A 242     6088   5022   6183    647   1387    204       C  
ATOM   1987  C   SER A 242     100.959 -29.697 -36.375  1.00 42.96           C  
ANISOU 1987  C   SER A 242     5596   4740   5986    676   1378    217       C  
ATOM   1988  O   SER A 242     102.007 -30.331 -36.512  1.00 47.74           O  
ANISOU 1988  O   SER A 242     6154   5379   6605    776   1466    225       O  
ATOM   1989  CB  SER A 242     100.505 -28.622 -38.586  1.00 50.69           C  
ANISOU 1989  CB  SER A 242     6704   5732   6822    635   1500    277       C  
ATOM   1990  OG  SER A 242     100.698 -27.339 -38.021  1.00 49.29           O  
ANISOU 1990  OG  SER A 242     6378   5575   6776    537   1474    331       O  
ATOM   1991  N   HIS A 243     100.643 -29.090 -35.236  1.00 40.90           N  
ANISOU 1991  N   HIS A 243     5245   4486   5809    603   1269    214       N  
ATOM   1992  CA  HIS A 243     101.528 -29.076 -34.080  1.00 42.90           C  
ANISOU 1992  CA  HIS A 243     5334   4796   6168    636   1234    214       C  
ATOM   1993  C   HIS A 243     100.861 -29.780 -32.910  1.00 45.66           C  
ANISOU 1993  C   HIS A 243     5725   5122   6501    662   1126    182       C  
ATOM   1994  O   HIS A 243      99.660 -30.058 -32.928  1.00 42.67           O  
ANISOU 1994  O   HIS A 243     5475   4677   6059    624   1074    166       O  
ATOM   1995  CB  HIS A 243     101.905 -27.644 -33.693  1.00 44.30           C  
ANISOU 1995  CB  HIS A 243     5347   5016   6467    543   1200    230       C  
ATOM   1996  CG  HIS A 243     102.458 -26.858 -34.836  1.00 62.86           C  
ANISOU 1996  CG  HIS A 243     7655   7376   8854    506   1321    289       C  
ATOM   1997  ND1 HIS A 243     103.606 -27.231 -35.498  1.00 66.41           N  
ANISOU 1997  ND1 HIS A 243     8042   7871   9321    584   1457    330       N  
ATOM   1998  CD2 HIS A 243     102.002 -25.749 -35.462  1.00 67.44           C  
ANISOU 1998  CD2 HIS A 243     8249   7924   9449    412   1340    330       C  
ATOM   1999  CE1 HIS A 243     103.848 -26.371 -36.471  1.00 70.36           C  
ANISOU 1999  CE1 HIS A 243     8515   8372   9846    537   1562    400       C  
ATOM   2000  NE2 HIS A 243     102.889 -25.463 -36.472  1.00 69.10           N  
ANISOU 2000  NE2 HIS A 243     8405   8162   9687    433   1492    405       N  
ATOM   2001  N   SER A 244     101.669 -30.069 -31.886  1.00 43.27           N  
ANISOU 2001  N   SER A 244     5302   4882   6257    734   1095    181       N  
ATOM   2002  CA  SER A 244     101.156 -30.782 -30.721  1.00 44.68           C  
ANISOU 2002  CA  SER A 244     5513   5052   6409    787   1010    175       C  
ATOM   2003  C   SER A 244     100.023 -30.008 -30.058  1.00 40.80           C  
ANISOU 2003  C   SER A 244     5040   4552   5909    694    903    160       C  
ATOM   2004  O   SER A 244      99.057 -30.610 -29.577  1.00 40.51           O  
ANISOU 2004  O   SER A 244     5100   4469   5823    704    863    170       O  
ATOM   2005  CB  SER A 244     102.277 -31.051 -29.719  1.00 43.92           C  
ANISOU 2005  CB  SER A 244     5270   5052   6365    892    984    179       C  
ATOM   2006  OG  SER A 244     102.765 -29.835 -29.193  1.00 50.87           O  
ANISOU 2006  OG  SER A 244     5985   6016   7328    834    915    150       O  
ATOM   2007  N   GLN A 245     100.117 -28.676 -30.014  1.00 35.45           N  
ANISOU 2007  N   GLN A 245     4266   3912   5291    606    863    139       N  
ATOM   2008  CA  GLN A 245      98.992 -27.878 -29.539  1.00 35.61           C  
ANISOU 2008  CA  GLN A 245     4315   3914   5300    522    773    120       C  
ATOM   2009  C   GLN A 245      98.108 -27.515 -30.725  1.00 35.47           C  
ANISOU 2009  C   GLN A 245     4413   3818   5246    433    812    135       C  
ATOM   2010  O   GLN A 245      98.577 -26.952 -31.722  1.00 38.23           O  
ANISOU 2010  O   GLN A 245     4744   4161   5623    393    882    152       O  
ATOM   2011  CB  GLN A 245      99.442 -26.609 -28.798  1.00 41.68           C  
ANISOU 2011  CB  GLN A 245     4931   4747   6160    479    693     75       C  
ATOM   2012  CG  GLN A 245      98.660 -26.373 -27.484  1.00 62.51           C  
ANISOU 2012  CG  GLN A 245     7568   7421   8762    495    574     39       C  
ATOM   2013  CD  GLN A 245      98.159 -24.935 -27.275  1.00 76.33           C  
ANISOU 2013  CD  GLN A 245     9275   9160  10568    399    500    -10       C  
ATOM   2014  OE1 GLN A 245      98.248 -24.085 -28.161  1.00 79.60           O  
ANISOU 2014  OE1 GLN A 245     9673   9520  11053    308    540     -4       O  
ATOM   2015  NE2 GLN A 245      97.623 -24.672 -26.088  1.00 75.84           N  
ANISOU 2015  NE2 GLN A 245     9199   9146  10470    434    400    -55       N  
ATOM   2016  N   LEU A 246      96.830 -27.856 -30.611  1.00 36.09           N  
ANISOU 2016  N   LEU A 246     4605   3846   5263    409    769    137       N  
ATOM   2017  CA  LEU A 246      95.852 -27.571 -31.646  1.00 35.06           C  
ANISOU 2017  CA  LEU A 246     4583   3651   5086    334    780    143       C  
ATOM   2018  C   LEU A 246      95.647 -26.062 -31.766  1.00 37.95           C  
ANISOU 2018  C   LEU A 246     4890   4028   5500    248    748    144       C  
ATOM   2019  O   LEU A 246      95.372 -25.382 -30.777  1.00 40.92           O  
ANISOU 2019  O   LEU A 246     5199   4430   5919    227    670    122       O  
ATOM   2020  CB  LEU A 246      94.542 -28.284 -31.303  1.00 36.34           C  
ANISOU 2020  CB  LEU A 246     4845   3761   5202    326    728    142       C  
ATOM   2021  CG  LEU A 246      93.504 -28.565 -32.391  1.00 49.07           C  
ANISOU 2021  CG  LEU A 246     6586   5301   6756    276    729    134       C  
ATOM   2022  CD1 LEU A 246      92.540 -29.670 -31.939  1.00 44.01           C  
ANISOU 2022  CD1 LEU A 246     6016   4596   6110    284    695    134       C  
ATOM   2023  CD2 LEU A 246      92.728 -27.308 -32.738  1.00 47.04           C  
ANISOU 2023  CD2 LEU A 246     6326   5051   6497    192    683    139       C  
ATOM   2024  N   GLY A 247      95.790 -25.537 -32.982  1.00 37.97           N  
ANISOU 2024  N   GLY A 247     4922   4010   5493    211    813    171       N  
ATOM   2025  CA  GLY A 247      95.647 -24.109 -33.216  1.00 39.06           C  
ANISOU 2025  CA  GLY A 247     5010   4138   5692    134    801    191       C  
ATOM   2026  C   GLY A 247      94.225 -23.754 -33.598  1.00 41.91           C  
ANISOU 2026  C   GLY A 247     5474   4457   5992     85    750    199       C  
ATOM   2027  O   GLY A 247      93.616 -24.416 -34.441  1.00 39.94           O  
ANISOU 2027  O   GLY A 247     5344   4188   5646     98    766    205       O  
ATOM   2028  N   GLY A 248      93.701 -22.702 -32.966  1.00 36.97           N  
ANISOU 2028  N   GLY A 248     4798   3821   5428     35    680    189       N  
ATOM   2029  CA  GLY A 248      92.390 -22.174 -33.330  1.00 34.60           C  
ANISOU 2029  CA  GLY A 248     4574   3487   5087     -8    632    205       C  
ATOM   2030  C   GLY A 248      91.246 -23.131 -33.031  1.00 35.12           C  
ANISOU 2030  C   GLY A 248     4721   3549   5074      8    573    182       C  
ATOM   2031  O   GLY A 248      91.183 -23.776 -31.970  1.00 37.24           O  
ANISOU 2031  O   GLY A 248     4962   3838   5351     40    538    154       O  
ATOM   2032  N   LEU A 249      90.329 -23.221 -34.002  1.00 37.82           N  
ANISOU 2032  N   LEU A 249     5160   3867   5344    -12    564    200       N  
ATOM   2033  CA  LEU A 249      89.102 -24.018 -33.939  1.00 36.12           C  
ANISOU 2033  CA  LEU A 249     5012   3634   5078    -18    502    180       C  
ATOM   2034  C   LEU A 249      88.138 -23.482 -32.867  1.00 39.40           C  
ANISOU 2034  C   LEU A 249     5377   4056   5539    -40    428    178       C  
ATOM   2035  O   LEU A 249      87.816 -24.145 -31.885  1.00 37.27           O  
ANISOU 2035  O   LEU A 249     5084   3794   5283    -20    404    167       O  
ATOM   2036  CB  LEU A 249      89.413 -25.506 -33.717  1.00 39.78           C  
ANISOU 2036  CB  LEU A 249     5510   4084   5523     23    524    152       C  
ATOM   2037  CG  LEU A 249      88.307 -26.471 -34.161  1.00 41.70           C  
ANISOU 2037  CG  LEU A 249     5838   4280   5725      6    480    126       C  
ATOM   2038  CD1 LEU A 249      88.191 -26.550 -35.685  1.00 43.52           C  
ANISOU 2038  CD1 LEU A 249     6166   4501   5867      6    487    104       C  
ATOM   2039  CD2 LEU A 249      88.544 -27.868 -33.576  1.00 44.52           C  
ANISOU 2039  CD2 LEU A 249     6209   4598   6109     43    500    110       C  
ATOM   2040  N   HIS A 250      87.619 -22.272 -33.119  1.00 34.79           N  
ANISOU 2040  N   HIS A 250     4780   3466   4971    -70    399    198       N  
ATOM   2041  CA  HIS A 250      86.796 -21.550 -32.146  1.00 34.77           C  
ANISOU 2041  CA  HIS A 250     4725   3472   5013    -78    338    192       C  
ATOM   2042  C   HIS A 250      85.341 -21.386 -32.558  1.00 37.94           C  
ANISOU 2042  C   HIS A 250     5165   3865   5385   -100    282    211       C  
ATOM   2043  O   HIS A 250      84.554 -20.823 -31.790  1.00 37.31           O  
ANISOU 2043  O   HIS A 250     5043   3797   5338    -96    238    210       O  
ATOM   2044  CB  HIS A 250      87.421 -20.170 -31.888  1.00 33.94           C  
ANISOU 2044  CB  HIS A 250     4555   3357   4985    -86    344    189       C  
ATOM   2045  CG  HIS A 250      88.793 -20.269 -31.302  1.00 34.83           C  
ANISOU 2045  CG  HIS A 250     4598   3487   5148    -67    378    156       C  
ATOM   2046  ND1 HIS A 250      89.020 -20.796 -30.050  1.00 36.50           N  
ANISOU 2046  ND1 HIS A 250     4761   3746   5364    -22    349    113       N  
ATOM   2047  CD2 HIS A 250      90.011 -19.946 -31.802  1.00 37.21           C  
ANISOU 2047  CD2 HIS A 250     4862   3775   5500    -79    438    167       C  
ATOM   2048  CE1 HIS A 250      90.318 -20.780 -29.796  1.00 40.24           C  
ANISOU 2048  CE1 HIS A 250     5167   4237   5885     -6    375     86       C  
ATOM   2049  NE2 HIS A 250      90.942 -20.268 -30.844  1.00 35.82           N  
ANISOU 2049  NE2 HIS A 250     4606   3638   5365    -47    432    119       N  
ATOM   2050  N  ALEU A 251      84.965 -21.840 -33.745  0.38 35.95           N  
ANISOU 2050  N  ALEU A 251     4990   3602   5069   -114    277    221       N  
ATOM   2051  N  BLEU A 251      84.965 -21.858 -33.740  0.62 35.98           N  
ANISOU 2051  N  BLEU A 251     4993   3605   5073   -114    277    221       N  
ATOM   2052  CA ALEU A 251      83.598 -21.740 -34.236  0.38 37.87           C  
ANISOU 2052  CA ALEU A 251     5260   3846   5284   -134    208    231       C  
ATOM   2053  CA BLEU A 251      83.608 -21.747 -34.256  0.62 37.72           C  
ANISOU 2053  CA BLEU A 251     5241   3826   5264   -134    209    231       C  
ATOM   2054  C  ALEU A 251      83.019 -23.133 -34.393  0.38 39.98           C  
ANISOU 2054  C  ALEU A 251     5560   4100   5530   -149    177    197       C  
ATOM   2055  C  BLEU A 251      83.017 -23.138 -34.403  0.62 40.19           C  
ANISOU 2055  C  BLEU A 251     5587   4126   5556   -150    177    197       C  
ATOM   2056  O  ALEU A 251      83.663 -24.007 -34.980  0.38 41.29           O  
ANISOU 2056  O  ALEU A 251     5784   4249   5656   -141    209    168       O  
ATOM   2057  O  BLEU A 251      83.653 -24.017 -34.990  0.62 41.49           O  
ANISOU 2057  O  BLEU A 251     5810   4274   5680   -141    208    168       O  
ATOM   2058  CB ALEU A 251      83.545 -21.008 -35.573  0.38 41.45           C  
ANISOU 2058  CB ALEU A 251     5772   4302   5674   -128    207    265       C  
ATOM   2059  CB BLEU A 251      83.596 -21.040 -35.611  0.62 41.42           C  
ANISOU 2059  CB BLEU A 251     5772   4299   5668   -128    210    264       C  
ATOM   2060  CG ALEU A 251      83.137 -19.550 -35.453  0.38 45.51           C  
ANISOU 2060  CG ALEU A 251     6250   4809   6232   -124    191    312       C  
ATOM   2061  CG BLEU A 251      83.433 -19.528 -35.595  0.62 44.13           C  
ANISOU 2061  CG BLEU A 251     6083   4633   6053   -122    210    316       C  
ATOM   2062  CD1ALEU A 251      84.307 -18.721 -34.943  0.38 51.43           C  
ANISOU 2062  CD1ALEU A 251     6950   5531   7060   -123    258    325       C  
ATOM   2063  CD1BLEU A 251      82.064 -19.135 -35.029  0.62 35.36           C  
ANISOU 2063  CD1BLEU A 251     4930   3531   4976   -126    130    317       C  
ATOM   2064  CD2ALEU A 251      82.626 -19.045 -36.790  0.38 49.21           C  
ANISOU 2064  CD2ALEU A 251     6786   5291   6620   -106    169    360       C  
ATOM   2065  CD2BLEU A 251      84.561 -18.878 -34.806  0.62 47.85           C  
ANISOU 2065  CD2BLEU A 251     6490   5078   6612   -123    269    316       C  
ATOM   2066  N   LEU A 252      81.796 -23.329 -33.892  1.00 33.90           N  
ANISOU 2066  N   LEU A 252     4749   3331   4801   -172    119    201       N  
ATOM   2067  CA  LEU A 252      81.198 -24.661 -33.920  1.00 33.16           C  
ANISOU 2067  CA  LEU A 252     4666   3203   4730   -202     91    173       C  
ATOM   2068  C   LEU A 252      81.137 -25.224 -35.341  1.00 39.14           C  
ANISOU 2068  C   LEU A 252     5512   3941   5418   -215     50    119       C  
ATOM   2069  O   LEU A 252      81.445 -26.403 -35.554  1.00 39.90           O  
ANISOU 2069  O   LEU A 252     5653   3989   5520   -221     62     72       O  
ATOM   2070  CB  LEU A 252      79.806 -24.628 -33.282  1.00 33.78           C  
ANISOU 2070  CB  LEU A 252     4667   3290   4878   -229     39    199       C  
ATOM   2071  CG  LEU A 252      79.167 -26.024 -33.201  1.00 41.52           C  
ANISOU 2071  CG  LEU A 252     5637   4214   5926   -275     19    180       C  
ATOM   2072  CD1 LEU A 252      80.016 -26.947 -32.323  1.00 46.36           C  
ANISOU 2072  CD1 LEU A 252     6251   4790   6573   -250    102    198       C  
ATOM   2073  CD2 LEU A 252      77.752 -25.951 -32.671  1.00 42.46           C  
ANISOU 2073  CD2 LEU A 252     5659   4345   6128   -307    -24    219       C  
ATOM   2074  N   ILE A 253      80.786 -24.397 -36.336  1.00 36.92           N  
ANISOU 2074  N   ILE A 253     5266   3697   5064   -205      4    123       N  
ATOM   2075  CA  ILE A 253      80.715 -24.916 -37.706  1.00 40.42           C  
ANISOU 2075  CA  ILE A 253     5803   4144   5411   -195    -44     63       C  
ATOM   2076  C   ILE A 253      82.052 -25.520 -38.149  1.00 38.47           C  
ANISOU 2076  C   ILE A 253     5634   3879   5102   -156     40     33       C  
ATOM   2077  O   ILE A 253      82.081 -26.484 -38.923  1.00 40.71           O  
ANISOU 2077  O   ILE A 253     5994   4141   5334   -146     11    -47       O  
ATOM   2078  CB  ILE A 253      80.220 -23.825 -38.686  1.00 38.24           C  
ANISOU 2078  CB  ILE A 253     5556   3929   5043   -164    -96     94       C  
ATOM   2079  CG1 ILE A 253      79.860 -24.448 -40.040  1.00 41.22           C  
ANISOU 2079  CG1 ILE A 253     6026   4330   5306   -143   -179     15       C  
ATOM   2080  CG2 ILE A 253      81.250 -22.691 -38.864  1.00 37.09           C  
ANISOU 2080  CG2 ILE A 253     5431   3807   4854   -117      0    172       C  
ATOM   2081  CD1 ILE A 253      79.125 -23.505 -40.985  1.00 41.59           C  
ANISOU 2081  CD1 ILE A 253     6097   4452   5253   -101   -256     48       C  
ATOM   2082  N   GLY A 254      83.172 -24.998 -37.654  1.00 38.61           N  
ANISOU 2082  N   GLY A 254     5628   3907   5135   -129    140     85       N  
ATOM   2083  CA  GLY A 254      84.457 -25.565 -38.034  1.00 36.20           C  
ANISOU 2083  CA  GLY A 254     5378   3594   4784    -85    227     65       C  
ATOM   2084  C   GLY A 254      84.677 -26.934 -37.413  1.00 40.39           C  
ANISOU 2084  C   GLY A 254     5908   4063   5377    -92    240     14       C  
ATOM   2085  O   GLY A 254      85.242 -27.833 -38.044  1.00 39.40           O  
ANISOU 2085  O   GLY A 254     5858   3912   5202    -56    269    -43       O  
ATOM   2086  N   LEU A 255      84.230 -27.106 -36.166  1.00 38.01           N  
ANISOU 2086  N   LEU A 255     5525   3736   5180   -125    227     40       N  
ATOM   2087  CA  LEU A 255      84.219 -28.427 -35.554  1.00 41.46           C  
ANISOU 2087  CA  LEU A 255     5960   4102   5689   -132    238     14       C  
ATOM   2088  C   LEU A 255      83.303 -29.372 -36.317  1.00 41.40           C  
ANISOU 2088  C   LEU A 255     6010   4030   5690   -171    159    -64       C  
ATOM   2089  O   LEU A 255      83.645 -30.538 -36.530  1.00 39.11           O  
ANISOU 2089  O   LEU A 255     5775   3665   5420   -158    176   -120       O  
ATOM   2090  CB  LEU A 255      83.776 -28.332 -34.095  1.00 42.74           C  
ANISOU 2090  CB  LEU A 255     6025   4268   5948   -148    245     77       C  
ATOM   2091  CG  LEU A 255      84.759 -27.797 -33.052  1.00 41.19           C  
ANISOU 2091  CG  LEU A 255     5769   4122   5761    -98    312    126       C  
ATOM   2092  CD1 LEU A 255      84.831 -26.272 -33.075  1.00 39.88           C  
ANISOU 2092  CD1 LEU A 255     5563   4021   5569   -100    299    148       C  
ATOM   2093  CD2 LEU A 255      84.350 -28.293 -31.672  1.00 44.21           C  
ANISOU 2093  CD2 LEU A 255     6086   4496   6216    -87    325    176       C  
ATOM   2094  N   ALA A 256      82.131 -28.883 -36.734  1.00 41.54           N  
ANISOU 2094  N   ALA A 256     6009   4071   5701   -216     64    -75       N  
ATOM   2095  CA  ALA A 256      81.195 -29.725 -37.478  1.00 47.48           C  
ANISOU 2095  CA  ALA A 256     6799   4768   6475   -260    -37   -167       C  
ATOM   2096  C   ALA A 256      81.821 -30.234 -38.769  1.00 44.98           C  
ANISOU 2096  C   ALA A 256     6608   4443   6038   -209    -46   -268       C  
ATOM   2097  O   ALA A 256      81.691 -31.420 -39.108  1.00 44.31           O  
ANISOU 2097  O   ALA A 256     6574   4268   5993   -224    -83   -366       O  
ATOM   2098  CB  ALA A 256      79.906 -28.949 -37.769  1.00 40.20           C  
ANISOU 2098  CB  ALA A 256     5824   3899   5552   -302   -144   -159       C  
ATOM   2099  N   LYS A 257      82.522 -29.358 -39.494  1.00 45.61           N  
ANISOU 2099  N   LYS A 257     6740   4613   5976   -143     -5   -244       N  
ATOM   2100  CA  LYS A 257      83.130 -29.766 -40.757  1.00 47.45           C  
ANISOU 2100  CA  LYS A 257     7098   4863   6067    -72      2   -329       C  
ATOM   2101  C   LYS A 257      84.216 -30.812 -40.529  1.00 50.23           C  
ANISOU 2101  C   LYS A 257     7492   5144   6448    -30     96   -364       C  
ATOM   2102  O   LYS A 257      84.296 -31.813 -41.253  1.00 49.42           O  
ANISOU 2102  O   LYS A 257     7482   4988   6306      1     66   -482       O  
ATOM   2103  CB  LYS A 257      83.698 -28.547 -41.488  1.00 44.16           C  
ANISOU 2103  CB  LYS A 257     6715   4558   5505     -3     57   -258       C  
ATOM   2104  CG  LYS A 257      84.170 -28.835 -42.920  1.00 44.63           C  
ANISOU 2104  CG  LYS A 257     6909   4668   5381     92     65   -332       C  
ATOM   2105  CD  LYS A 257      84.714 -27.563 -43.574  1.00 48.43           C  
ANISOU 2105  CD  LYS A 257     7411   5257   5733    160    145   -222       C  
ATOM   2106  CE  LYS A 257      85.283 -27.821 -44.967  1.00 48.99           C  
ANISOU 2106  CE  LYS A 257     7617   5397   5599    279    182   -272       C  
ATOM   2107  NZ  LYS A 257      84.235 -28.134 -45.980  1.00 49.00           N  
ANISOU 2107  NZ  LYS A 257     7707   5440   5473    309     27   -387       N  
ATOM   2108  N   ARG A 258      85.059 -30.601 -39.518  1.00 47.60           N  
ANISOU 2108  N   ARG A 258     7092   4811   6184    -20    203   -272       N  
ATOM   2109  CA  ARG A 258      86.099 -31.579 -39.209  1.00 47.79           C  
ANISOU 2109  CA  ARG A 258     7142   4774   6242     30    292   -292       C  
ATOM   2110  C   ARG A 258      85.493 -32.901 -38.767  1.00 48.28           C  
ANISOU 2110  C   ARG A 258     7211   4702   6430    -13    244   -355       C  
ATOM   2111  O   ARG A 258      85.968 -33.975 -39.158  1.00 49.98           O  
ANISOU 2111  O   ARG A 258     7505   4839   6647     32    267   -436       O  
ATOM   2112  CB  ARG A 258      87.012 -31.027 -38.119  1.00 46.43           C  
ANISOU 2112  CB  ARG A 258     6876   4642   6125     49    391   -182       C  
ATOM   2113  CG  ARG A 258      88.029 -32.019 -37.599  1.00 54.57           C  
ANISOU 2113  CG  ARG A 258     7910   5618   7207    107    476   -184       C  
ATOM   2114  CD  ARG A 258      89.374 -31.738 -38.193  1.00 54.67           C  
ANISOU 2114  CD  ARG A 258     7944   5697   7131    193    578   -173       C  
ATOM   2115  NE  ARG A 258      90.383 -32.714 -37.800  1.00 50.84           N  
ANISOU 2115  NE  ARG A 258     7463   5167   6688    266    659   -180       N  
ATOM   2116  CZ  ARG A 258      91.502 -32.909 -38.487  1.00 54.83           C  
ANISOU 2116  CZ  ARG A 258     8007   5705   7121    358    751   -198       C  
ATOM   2117  NH1 ARG A 258      91.716 -32.199 -39.584  1.00 55.55           N  
ANISOU 2117  NH1 ARG A 258     8140   5874   7090    384    779   -202       N  
ATOM   2118  NH2 ARG A 258      92.394 -33.810 -38.093  1.00 49.27           N  
ANISOU 2118  NH2 ARG A 258     7298   4959   6461    434    822   -202       N  
ATOM   2119  N   PHE A 259      84.425 -32.838 -37.965  1.00 47.30           N  
ANISOU 2119  N   PHE A 259     7003   4545   6424    -99    183   -313       N  
ATOM   2120  CA  PHE A 259      83.861 -34.040 -37.355  1.00 50.72           C  
ANISOU 2120  CA  PHE A 259     7416   4840   7014   -149    162   -334       C  
ATOM   2121  C   PHE A 259      83.276 -34.990 -38.396  1.00 57.67           C  
ANISOU 2121  C   PHE A 259     8383   5622   7909   -176     65   -487       C  
ATOM   2122  O   PHE A 259      83.383 -36.217 -38.258  1.00 55.82           O  
ANISOU 2122  O   PHE A 259     8183   5245   7781   -179     79   -539       O  
ATOM   2123  CB  PHE A 259      82.799 -33.641 -36.326  1.00 49.67           C  
ANISOU 2123  CB  PHE A 259     7163   4713   6996   -228    131   -241       C  
ATOM   2124  CG  PHE A 259      82.194 -34.807 -35.598  1.00 64.09           C  
ANISOU 2124  CG  PHE A 259     8950   6398   9003   -282    134   -224       C  
ATOM   2125  CD1 PHE A 259      82.902 -35.457 -34.594  1.00 70.58           C  
ANISOU 2125  CD1 PHE A 259     9756   7166   9895   -234    241   -141       C  
ATOM   2126  CD2 PHE A 259      80.918 -35.249 -35.909  1.00 62.51           C  
ANISOU 2126  CD2 PHE A 259     8719   6118   8913   -378     31   -281       C  
ATOM   2127  CE1 PHE A 259      82.351 -36.537 -33.920  1.00 75.87           C  
ANISOU 2127  CE1 PHE A 259    10392   7696  10741   -276    262    -99       C  
ATOM   2128  CE2 PHE A 259      80.357 -36.324 -35.236  1.00 75.63           C  
ANISOU 2128  CE2 PHE A 259    10331   7632  10771   -437     48   -249       C  
ATOM   2129  CZ  PHE A 259      81.075 -36.970 -34.243  1.00 73.91           C  
ANISOU 2129  CZ  PHE A 259    10109   7352  10620   -384    172   -150       C  
ATOM   2130  N   LYS A 260      82.644 -34.452 -39.441  1.00 61.95           N  
ANISOU 2130  N   LYS A 260     8961   6232   8347   -190    -41   -565       N  
ATOM   2131  CA  LYS A 260      82.056 -35.321 -40.458  1.00 69.80           C  
ANISOU 2131  CA  LYS A 260    10034   7144   9342   -210   -160   -737       C  
ATOM   2132  C   LYS A 260      83.116 -36.100 -41.225  1.00 69.82           C  
ANISOU 2132  C   LYS A 260    10173   7105   9250   -108   -109   -845       C  
ATOM   2133  O   LYS A 260      82.816 -37.163 -41.779  1.00 73.35           O  
ANISOU 2133  O   LYS A 260    10690   7431   9748   -119   -185   -999       O  
ATOM   2134  CB  LYS A 260      81.182 -34.508 -41.420  1.00 74.19           C  
ANISOU 2134  CB  LYS A 260    10599   7810   9779   -224   -293   -795       C  
ATOM   2135  CG  LYS A 260      81.940 -33.565 -42.339  1.00 86.30           C  
ANISOU 2135  CG  LYS A 260    12217   9498  11074   -113   -252   -781       C  
ATOM   2136  CD  LYS A 260      81.033 -32.947 -43.411  1.00 95.17           C  
ANISOU 2136  CD  LYS A 260    13370  10724  12067   -106   -396   -849       C  
ATOM   2137  CE  LYS A 260      79.937 -32.070 -42.808  1.00 97.17           C  
ANISOU 2137  CE  LYS A 260    13490  11023  12407   -190   -461   -751       C  
ATOM   2138  NZ  LYS A 260      79.162 -31.318 -43.846  1.00 93.48           N  
ANISOU 2138  NZ  LYS A 260    13048  10677  11794   -158   -591   -791       N  
ATOM   2139  N   GLU A 261      84.348 -35.609 -41.245  1.00 59.42           N  
ANISOU 2139  N   GLU A 261     8886   5878   7811    -10     20   -772       N  
ATOM   2140  CA  GLU A 261      85.449 -36.291 -41.905  1.00 69.13           C  
ANISOU 2140  CA  GLU A 261    10233   7085   8948    105     94   -854       C  
ATOM   2141  C   GLU A 261      86.317 -37.092 -40.942  1.00 65.25           C  
ANISOU 2141  C   GLU A 261     9717   6493   8584    135    214   -793       C  
ATOM   2142  O   GLU A 261      86.827 -38.150 -41.320  1.00 62.30           O  
ANISOU 2142  O   GLU A 261     9434   6017   8220    201    241   -895       O  
ATOM   2143  CB  GLU A 261      86.313 -35.265 -42.652  1.00 85.61           C  
ANISOU 2143  CB  GLU A 261    12361   9343  10822    206    173   -805       C  
ATOM   2144  CG  GLU A 261      87.818 -35.389 -42.435  1.00 98.50           C  
ANISOU 2144  CG  GLU A 261    14003  11000  12423    309    339   -742       C  
ATOM   2145  CD  GLU A 261      88.549 -34.063 -42.610  1.00107.92           C  
ANISOU 2145  CD  GLU A 261    15154  12354  13499    355    435   -614       C  
ATOM   2146  OE1 GLU A 261      87.870 -33.017 -42.719  1.00114.55           O  
ANISOU 2146  OE1 GLU A 261    15952  13271  14300    301    378   -558       O  
ATOM   2147  OE2 GLU A 261      89.801 -34.066 -42.633  1.00106.97           O  
ANISOU 2147  OE2 GLU A 261    15031  12272  13339    443    569   -567       O  
ATOM   2148  N   SER A 262      86.462 -36.640 -39.694  1.00 55.70           N  
ANISOU 2148  N   SER A 262     8389   5306   7468    100    280   -636       N  
ATOM   2149  CA  SER A 262      87.456 -37.174 -38.781  1.00 53.04           C  
ANISOU 2149  CA  SER A 262     8023   4923   7208    159    401   -555       C  
ATOM   2150  C   SER A 262      87.021 -36.954 -37.336  1.00 47.20           C  
ANISOU 2150  C   SER A 262     7157   4173   6604     93    416   -415       C  
ATOM   2151  O   SER A 262      86.727 -35.812 -36.965  1.00 55.09           O  
ANISOU 2151  O   SER A 262     8076   5287   7567     55    400   -335       O  
ATOM   2152  CB  SER A 262      88.799 -36.491 -39.041  1.00 61.71           C  
ANISOU 2152  CB  SER A 262     9123   6156   8170    264    511   -505       C  
ATOM   2153  OG  SER A 262      89.833 -37.086 -38.288  1.00 67.84           O  
ANISOU 2153  OG  SER A 262     9872   6895   9009    339    617   -446       O  
ATOM   2154  N   PRO A 263      86.978 -37.991 -36.508  1.00 49.82           N  
ANISOU 2154  N   PRO A 263     7473   4371   7085     91    451   -377       N  
ATOM   2155  CA  PRO A 263      86.434 -37.833 -35.156  1.00 53.04           C  
ANISOU 2155  CA  PRO A 263     7768   4776   7607     40    468   -238       C  
ATOM   2156  C   PRO A 263      87.436 -37.227 -34.184  1.00 54.99           C  
ANISOU 2156  C   PRO A 263     7944   5144   7804    121    559   -115       C  
ATOM   2157  O   PRO A 263      88.653 -37.294 -34.365  1.00 49.03           O  
ANISOU 2157  O   PRO A 263     7216   4431   6980    218    628   -123       O  
ATOM   2158  CB  PRO A 263      86.092 -39.269 -34.755  1.00 60.63           C  
ANISOU 2158  CB  PRO A 263     8752   5537   8746     24    485   -239       C  
ATOM   2159  CG  PRO A 263      87.118 -40.089 -35.486  1.00 56.44           C  
ANISOU 2159  CG  PRO A 263     8334   4936   8176    122    530   -337       C  
ATOM   2160  CD  PRO A 263      87.312 -39.398 -36.810  1.00 54.90           C  
ANISOU 2160  CD  PRO A 263     8206   4846   7806    138    476   -462       C  
ATOM   2161  N   PHE A 264      86.896 -36.625 -33.130  1.00 44.01           N  
ANISOU 2161  N   PHE A 264     6454   3816   6451     84    554     -7       N  
ATOM   2162  CA  PHE A 264      87.734 -36.099 -32.067  1.00 45.28           C  
ANISOU 2162  CA  PHE A 264     6541   4089   6574    161    619     96       C  
ATOM   2163  C   PHE A 264      86.947 -36.120 -30.766  1.00 49.15           C  
ANISOU 2163  C   PHE A 264     6950   4580   7144    140    627    213       C  
ATOM   2164  O   PHE A 264      85.726 -36.294 -30.751  1.00 45.60           O  
ANISOU 2164  O   PHE A 264     6483   4065   6777     52    584    222       O  
ATOM   2165  CB  PHE A 264      88.250 -34.696 -32.395  1.00 45.15           C  
ANISOU 2165  CB  PHE A 264     6489   4227   6439    167    604     80       C  
ATOM   2166  CG  PHE A 264      87.181 -33.745 -32.847  1.00 40.12           C  
ANISOU 2166  CG  PHE A 264     5836   3631   5776     74    523     55       C  
ATOM   2167  CD1 PHE A 264      86.422 -33.042 -31.926  1.00 47.96           C  
ANISOU 2167  CD1 PHE A 264     6744   4681   6798     37    495    126       C  
ATOM   2168  CD2 PHE A 264      86.924 -33.566 -34.201  1.00 48.28           C  
ANISOU 2168  CD2 PHE A 264     6943   4656   6746     39    474    -39       C  
ATOM   2169  CE1 PHE A 264      85.431 -32.166 -32.346  1.00 53.26           C  
ANISOU 2169  CE1 PHE A 264     7396   5389   7450    -37    422    107       C  
ATOM   2170  CE2 PHE A 264      85.937 -32.693 -34.628  1.00 54.30           C  
ANISOU 2170  CE2 PHE A 264     7689   5463   7479    -32    394    -53       C  
ATOM   2171  CZ  PHE A 264      85.190 -31.992 -33.700  1.00 54.28           C  
ANISOU 2171  CZ  PHE A 264     7595   5507   7522    -73    369     22       C  
ATOM   2172  N   GLU A 265      87.673 -35.964 -29.665  1.00 37.58           N  
ANISOU 2172  N   GLU A 265     5428   3199   5652    232    682    303       N  
ATOM   2173  CA  GLU A 265      87.106 -36.013 -28.326  1.00 40.89           C  
ANISOU 2173  CA  GLU A 265     5777   3646   6114    253    708    427       C  
ATOM   2174  C   GLU A 265      87.029 -34.606 -27.762  1.00 44.48           C  
ANISOU 2174  C   GLU A 265     6153   4266   6480    257    671    442       C  
ATOM   2175  O   GLU A 265      87.990 -33.834 -27.885  1.00 44.65           O  
ANISOU 2175  O   GLU A 265     6157   4389   6419    299    660    397       O  
ATOM   2176  CB  GLU A 265      87.950 -36.905 -27.420  1.00 46.32           C  
ANISOU 2176  CB  GLU A 265     6465   4317   6819    379    791    519       C  
ATOM   2177  CG  GLU A 265      87.936 -38.348 -27.884  1.00 68.85           C  
ANISOU 2177  CG  GLU A 265     9396   6976   9786    379    835    514       C  
ATOM   2178  CD  GLU A 265      86.857 -39.169 -27.218  1.00 78.74           C  
ANISOU 2178  CD  GLU A 265    10632   8105  11179    341    873    625       C  
ATOM   2179  OE1 GLU A 265      86.173 -38.628 -26.320  1.00 72.74           O  
ANISOU 2179  OE1 GLU A 265     9797   7434  10406    334    879    721       O  
ATOM   2180  OE2 GLU A 265      86.702 -40.354 -27.590  1.00 84.71           O  
ANISOU 2180  OE2 GLU A 265    11448   8671  12065    321    904    618       O  
ATOM   2181  N   LEU A 266      85.877 -34.274 -27.164  1.00 37.40           N  
ANISOU 2181  N   LEU A 266     5206   3390   5615    212    655    501       N  
ATOM   2182  CA  LEU A 266      85.650 -32.991 -26.498  1.00 38.70           C  
ANISOU 2182  CA  LEU A 266     5299   3699   5706    227    621    514       C  
ATOM   2183  C   LEU A 266      85.289 -33.284 -25.051  1.00 48.51           C  
ANISOU 2183  C   LEU A 266     6489   4990   6952    309    676    641       C  
ATOM   2184  O   LEU A 266      84.226 -33.851 -24.779  1.00 51.24           O  
ANISOU 2184  O   LEU A 266     6818   5266   7383    269    708    720       O  
ATOM   2185  CB  LEU A 266      84.531 -32.199 -27.165  1.00 43.41           C  
ANISOU 2185  CB  LEU A 266     5883   4294   6319    118    554    468       C  
ATOM   2186  CG  LEU A 266      84.612 -31.634 -28.580  1.00 46.79           C  
ANISOU 2186  CG  LEU A 266     6357   4704   6716     45    491    358       C  
ATOM   2187  CD1 LEU A 266      83.342 -30.850 -28.850  1.00 51.42           C  
ANISOU 2187  CD1 LEU A 266     6908   5311   7318    -34    427    350       C  
ATOM   2188  CD2 LEU A 266      85.828 -30.742 -28.767  1.00 44.85           C  
ANISOU 2188  CD2 LEU A 266     6110   4548   6384     92    489    310       C  
ATOM   2189  N  AGLU A 267      86.170 -32.934 -24.121  0.71 36.73           N  
ANISOU 2189  N  AGLU A 267     4965   3620   5369    428    689    664       N  
ATOM   2190  N  BGLU A 267      86.172 -32.899 -24.132  0.29 36.71           N  
ANISOU 2190  N  BGLU A 267     4962   3620   5365    427    687    661       N  
ATOM   2191  CA AGLU A 267      85.858 -33.079 -22.705  0.71 37.01           C  
ANISOU 2191  CA AGLU A 267     4956   3738   5366    534    737    782       C  
ATOM   2192  CA BGLU A 267      85.917 -33.020 -22.700  0.29 38.98           C  
ANISOU 2192  CA BGLU A 267     5206   3996   5610    537    733    776       C  
ATOM   2193  C  AGLU A 267      85.220 -31.776 -22.242  0.71 41.91           C  
ANISOU 2193  C  AGLU A 267     5522   4480   5923    528    686    752       C  
ATOM   2194  C  BGLU A 267      85.214 -31.740 -22.261  0.29 40.30           C  
ANISOU 2194  C  BGLU A 267     5317   4277   5718    526    684    749       C  
ATOM   2195  O  AGLU A 267      85.853 -30.714 -22.281  0.71 34.60           O  
ANISOU 2195  O  AGLU A 267     4575   3646   4926    544    620    654       O  
ATOM   2196  O  BGLU A 267      85.797 -30.653 -22.325  0.29 34.61           O  
ANISOU 2196  O  BGLU A 267     4576   3646   4929    537    617    649       O  
ATOM   2197  CB AGLU A 267      87.099 -33.423 -21.880  0.71 43.36           C  
ANISOU 2197  CB AGLU A 267     5756   4627   6092    687    763    815       C  
ATOM   2198  CB BGLU A 267      87.224 -33.233 -21.936  0.29 46.59           C  
ANISOU 2198  CB BGLU A 267     6161   5052   6489    685    749    793       C  
ATOM   2199  CG AGLU A 267      86.990 -33.088 -20.389  0.71 53.84           C  
ANISOU 2199  CG AGLU A 267     7035   6111   7312    827    778    896       C  
ATOM   2200  CG BGLU A 267      87.297 -34.491 -21.076  0.29 60.69           C  
ANISOU 2200  CG BGLU A 267     7963   6805   8290    799    843    945       C  
ATOM   2201  CD AGLU A 267      86.175 -34.096 -19.582  0.71 69.48           C  
ANISOU 2201  CD AGLU A 267     9021   8050   9330    886    886   1077       C  
ATOM   2202  CD BGLU A 267      86.543 -34.360 -19.759  0.29 68.22           C  
ANISOU 2202  CD BGLU A 267     8875   7863   9181    892    888   1068       C  
ATOM   2203  OE1AGLU A 267      85.940 -35.220 -20.082  0.71 71.42           O  
ANISOU 2203  OE1AGLU A 267     9306   8130   9702    831    949   1143       O  
ATOM   2204  OE1BGLU A 267      85.670 -35.213 -19.479  0.29 71.68           O  
ANISOU 2204  OE1BGLU A 267     9320   8210   9704    882    978   1207       O  
ATOM   2205  OE2AGLU A 267      85.777 -33.764 -18.435  0.71 67.90           O  
ANISOU 2205  OE2AGLU A 267     8783   7981   9036    994    911   1154       O  
ATOM   2206  OE2BGLU A 267      86.825 -33.406 -19.001  0.29 69.01           O  
ANISOU 2206  OE2BGLU A 267     8933   8135   9152    980    836   1026       O  
ATOM   2207  N   ASP A 268      83.950 -31.861 -21.850  1.00 38.43           N  
ANISOU 2207  N   ASP A 268     5051   4027   5524    502    721    836       N  
ATOM   2208  CA  ASP A 268      83.144 -30.707 -21.439  1.00 34.82           C  
ANISOU 2208  CA  ASP A 268     4542   3670   5019    501    685    817       C  
ATOM   2209  C   ASP A 268      83.355 -30.525 -19.938  1.00 43.60           C  
ANISOU 2209  C   ASP A 268     5622   4934   6012    669    723    885       C  
ATOM   2210  O   ASP A 268      82.577 -31.009 -19.116  1.00 37.60           O  
ANISOU 2210  O   ASP A 268     4836   4197   5254    729    806   1020       O  
ATOM   2211  CB  ASP A 268      81.681 -30.976 -21.793  1.00 40.15           C  
ANISOU 2211  CB  ASP A 268     5187   4260   5807    397    710    878       C  
ATOM   2212  CG  ASP A 268      80.765 -29.778 -21.577  1.00 42.87           C  
ANISOU 2212  CG  ASP A 268     5477   4694   6119    388    671    852       C  
ATOM   2213  OD1 ASP A 268      81.218 -28.698 -21.135  1.00 42.55           O  
ANISOU 2213  OD1 ASP A 268     5429   4769   5970    460    624    779       O  
ATOM   2214  OD2 ASP A 268      79.556 -29.924 -21.873  1.00 47.79           O  
ANISOU 2214  OD2 ASP A 268     6058   5262   6839    305    684    899       O  
ATOM   2215  N   PHE A 269      84.445 -29.828 -19.563  1.00 36.81           N  
ANISOU 2215  N   PHE A 269     4759   4183   5044    755    661    792       N  
ATOM   2216  CA  PHE A 269      84.867 -29.925 -18.163  1.00 36.84           C  
ANISOU 2216  CA  PHE A 269     4746   4334   4919    938    687    849       C  
ATOM   2217  C   PHE A 269      84.106 -28.980 -17.233  1.00 34.07           C  
ANISOU 2217  C   PHE A 269     4356   4118   4472   1019    675    844       C  
ATOM   2218  O   PHE A 269      84.186 -29.158 -16.010  1.00 39.41           O  
ANISOU 2218  O   PHE A 269     5024   4925   5025   1188    713    915       O  
ATOM   2219  CB  PHE A 269      86.397 -29.738 -18.010  1.00 36.56           C  
ANISOU 2219  CB  PHE A 269     4709   4371   4812   1016    619    753       C  
ATOM   2220  CG  PHE A 269      86.947 -28.469 -18.617  1.00 37.08           C  
ANISOU 2220  CG  PHE A 269     4751   4453   4887    942    508    577       C  
ATOM   2221  CD1 PHE A 269      87.489 -28.474 -19.894  1.00 40.69           C  
ANISOU 2221  CD1 PHE A 269     5225   4798   5437    816    486    510       C  
ATOM   2222  CD2 PHE A 269      86.956 -27.284 -17.899  1.00 43.38           C  
ANISOU 2222  CD2 PHE A 269     5509   5374   5601   1006    432    480       C  
ATOM   2223  CE1 PHE A 269      88.013 -27.312 -20.456  1.00 38.36           C  
ANISOU 2223  CE1 PHE A 269     4902   4509   5164    748    404    374       C  
ATOM   2224  CE2 PHE A 269      87.470 -26.112 -18.456  1.00 44.60           C  
ANISOU 2224  CE2 PHE A 269     5635   5516   5794    930    337    326       C  
ATOM   2225  CZ  PHE A 269      87.998 -26.129 -19.740  1.00 39.18           C  
ANISOU 2225  CZ  PHE A 269     4961   4714   5213    798    330    286       C  
ATOM   2226  N   ILE A 270      83.331 -28.039 -17.767  1.00 32.84           N  
ANISOU 2226  N   ILE A 270     4181   3935   4361    919    630    770       N  
ATOM   2227  CA  ILE A 270      82.346 -27.280 -16.991  1.00 35.38           C  
ANISOU 2227  CA  ILE A 270     4468   4359   4618    988    642    785       C  
ATOM   2228  C   ILE A 270      80.984 -27.500 -17.643  1.00 40.34           C  
ANISOU 2228  C   ILE A 270     5071   4883   5373    863    695    865       C  
ATOM   2229  O   ILE A 270      80.558 -26.684 -18.479  1.00 37.84           O  
ANISOU 2229  O   ILE A 270     4744   4514   5118    753    629    776       O  
ATOM   2230  CB  ILE A 270      82.658 -25.772 -16.945  1.00 39.71           C  
ANISOU 2230  CB  ILE A 270     5002   4976   5108   1002    528    608       C  
ATOM   2231  CG1 ILE A 270      84.134 -25.501 -16.673  1.00 48.69           C  
ANISOU 2231  CG1 ILE A 270     6146   6176   6178   1069    444    490       C  
ATOM   2232  CG2 ILE A 270      81.797 -25.077 -15.893  1.00 41.54           C  
ANISOU 2232  CG2 ILE A 270     5208   5338   5240   1128    546    617       C  
ATOM   2233  CD1 ILE A 270      84.499 -24.038 -16.903  1.00 48.71           C  
ANISOU 2233  CD1 ILE A 270     6130   6189   6190   1034    326    306       C  
ATOM   2234  N   PRO A 271      80.279 -28.563 -17.309  1.00 34.86           N  
ANISOU 2234  N   PRO A 271     4359   4154   4732    874    809   1034       N  
ATOM   2235  CA  PRO A 271      79.085 -28.921 -18.084  1.00 37.35           C  
ANISOU 2235  CA  PRO A 271     4637   4346   5209    728    842   1098       C  
ATOM   2236  C   PRO A 271      77.854 -28.133 -17.672  1.00 33.90           C  
ANISOU 2236  C   PRO A 271     4131   3987   4761    752    864   1126       C  
ATOM   2237  O   PRO A 271      77.072 -28.552 -16.815  1.00 40.33           O  
ANISOU 2237  O   PRO A 271     4896   4857   5573    830    977   1277       O  
ATOM   2238  CB  PRO A 271      78.925 -30.421 -17.806  1.00 41.17           C  
ANISOU 2238  CB  PRO A 271     5119   4747   5778    733    962   1272       C  
ATOM   2239  CG  PRO A 271      79.536 -30.617 -16.448  1.00 42.99           C  
ANISOU 2239  CG  PRO A 271     5366   5121   5850    938   1028   1355       C  
ATOM   2240  CD  PRO A 271      80.676 -29.625 -16.366  1.00 36.13           C  
ANISOU 2240  CD  PRO A 271     4534   4357   4836   1006    907   1178       C  
ATOM   2241  N   MET A 272      77.684 -26.973 -18.293  1.00 37.56           N  
ANISOU 2241  N   MET A 272     4592   4456   5224    693    763    989       N  
ATOM   2242  CA  MET A 272      76.524 -26.125 -18.073  1.00 37.03           C  
ANISOU 2242  CA  MET A 272     4460   4448   5160    710    769    996       C  
ATOM   2243  C   MET A 272      76.203 -25.429 -19.383  1.00 33.65           C  
ANISOU 2243  C   MET A 272     4031   3929   4824    564    665    888       C  
ATOM   2244  O   MET A 272      76.978 -25.465 -20.340  1.00 41.87           O  
ANISOU 2244  O   MET A 272     5130   4886   5895    472    591    800       O  
ATOM   2245  CB  MET A 272      76.788 -25.087 -16.982  1.00 40.12           C  
ANISOU 2245  CB  MET A 272     4860   5001   5382    884    754    928       C  
ATOM   2246  CG  MET A 272      78.017 -24.250 -17.281  1.00 44.30           C  
ANISOU 2246  CG  MET A 272     5451   5532   5848    885    631    747       C  
ATOM   2247  SD  MET A 272      78.409 -23.135 -15.927  1.00 46.25           S  
ANISOU 2247  SD  MET A 272     5707   5958   5907   1093    593    639       S  
ATOM   2248  CE  MET A 272      77.110 -21.917 -16.112  1.00 52.22           C  
ANISOU 2248  CE  MET A 272     6419   6720   6705   1083    576    596       C  
ATOM   2249  N   ASP A 273      75.059 -24.765 -19.407  1.00 31.91           N  
ANISOU 2249  N   ASP A 273     3746   3740   4640    558    664    902       N  
ATOM   2250  CA  ASP A 273      74.682 -23.980 -20.567  1.00 32.20           C  
ANISOU 2250  CA  ASP A 273     3780   3712   4744    449    564    811       C  
ATOM   2251  C   ASP A 273      75.394 -22.632 -20.483  1.00 38.15           C  
ANISOU 2251  C   ASP A 273     4584   4511   5400    514    485    670       C  
ATOM   2252  O   ASP A 273      75.241 -21.916 -19.489  1.00 40.58           O  
ANISOU 2252  O   ASP A 273     4876   4922   5620    646    505    650       O  
ATOM   2253  CB  ASP A 273      73.173 -23.781 -20.580  1.00 33.38           C  
ANISOU 2253  CB  ASP A 273     3826   3881   4976    432    593    885       C  
ATOM   2254  CG  ASP A 273      72.636 -23.433 -21.958  1.00 41.87           C  
ANISOU 2254  CG  ASP A 273     4886   4871   6150    298    492    829       C  
ATOM   2255  OD1 ASP A 273      73.315 -23.742 -22.961  1.00 40.77           O  
ANISOU 2255  OD1 ASP A 273     4816   4641   6034    200    425    764       O  
ATOM   2256  OD2 ASP A 273      71.518 -22.875 -22.033  1.00 39.06           O  
ANISOU 2256  OD2 ASP A 273     4449   4549   5842    303    484    854       O  
ATOM   2257  N   SER A 274      76.163 -22.281 -21.505  1.00 34.24           N  
ANISOU 2257  N   SER A 274     4148   3936   4926    427    400    573       N  
ATOM   2258  CA  SER A 274      76.738 -20.934 -21.520  1.00 37.39           C  
ANISOU 2258  CA  SER A 274     4580   4350   5276    467    329    449       C  
ATOM   2259  C   SER A 274      77.018 -20.508 -22.954  1.00 33.83           C  
ANISOU 2259  C   SER A 274     4170   3796   4889    347    254    392       C  
ATOM   2260  O   SER A 274      77.184 -21.335 -23.851  1.00 37.38           O  
ANISOU 2260  O   SER A 274     4644   4176   5383    250    251    419       O  
ATOM   2261  CB  SER A 274      78.005 -20.834 -20.656  1.00 44.60           C  
ANISOU 2261  CB  SER A 274     5529   5320   6096    561    323    379       C  
ATOM   2262  OG  SER A 274      78.979 -21.769 -21.047  1.00 45.22           O  
ANISOU 2262  OG  SER A 274     5646   5352   6184    507    330    390       O  
ATOM   2263  N   THR A 275      77.051 -19.187 -23.148  1.00 32.97           N  
ANISOU 2263  N   THR A 275     4070   3675   4781    365    200    315       N  
ATOM   2264  CA  THR A 275      77.262 -18.609 -24.477  1.00 28.89           C  
ANISOU 2264  CA  THR A 275     3592   3068   4316    273    141    281       C  
ATOM   2265  C   THR A 275      78.573 -19.073 -25.113  1.00 29.76           C  
ANISOU 2265  C   THR A 275     3759   3125   4423    210    136    250       C  
ATOM   2266  O   THR A 275      78.626 -19.389 -26.311  1.00 33.77           O  
ANISOU 2266  O   THR A 275     4302   3573   4956    124    119    268       O  
ATOM   2267  CB  THR A 275      77.232 -17.089 -24.352  1.00 32.38           C  
ANISOU 2267  CB  THR A 275     4036   3496   4771    323     99    210       C  
ATOM   2268  OG1 THR A 275      75.892 -16.685 -24.033  1.00 35.76           O  
ANISOU 2268  OG1 THR A 275     4412   3966   5210    377    106    248       O  
ATOM   2269  CG2 THR A 275      77.715 -16.429 -25.634  1.00 33.78           C  
ANISOU 2269  CG2 THR A 275     4260   3578   4997    243     56    188       C  
ATOM   2270  N   VAL A 276      79.653 -19.062 -24.353  1.00 32.72           N  
ANISOU 2270  N   VAL A 276     4140   3530   4762    261    144    196       N  
ATOM   2271  CA  VAL A 276      80.929 -19.619 -24.791  1.00 33.82           C  
ANISOU 2271  CA  VAL A 276     4314   3635   4900    219    151    174       C  
ATOM   2272  C   VAL A 276      81.111 -20.950 -24.071  1.00 31.43           C  
ANISOU 2272  C   VAL A 276     4006   3382   4555    259    203    226       C  
ATOM   2273  O   VAL A 276      80.862 -21.041 -22.861  1.00 31.97           O  
ANISOU 2273  O   VAL A 276     4043   3533   4572    357    225    239       O  
ATOM   2274  CB  VAL A 276      82.098 -18.656 -24.484  1.00 35.89           C  
ANISOU 2274  CB  VAL A 276     4570   3892   5175    245    116     76       C  
ATOM   2275  CG1 VAL A 276      83.458 -19.311 -24.831  1.00 35.21           C  
ANISOU 2275  CG1 VAL A 276     4499   3789   5092    213    134     62       C  
ATOM   2276  CG2 VAL A 276      81.930 -17.330 -25.220  1.00 33.13           C  
ANISOU 2276  CG2 VAL A 276     4227   3468   4891    202     79     43       C  
ATOM   2277  N   LYS A 277      81.516 -21.987 -24.805  1.00 31.88           N  
ANISOU 2277  N   LYS A 277     4098   3387   4628    198    228    260       N  
ATOM   2278  CA  LYS A 277      81.783 -23.300 -24.219  1.00 34.61           C  
ANISOU 2278  CA  LYS A 277     4446   3753   4952    235    283    317       C  
ATOM   2279  C   LYS A 277      83.275 -23.599 -24.304  1.00 35.66           C  
ANISOU 2279  C   LYS A 277     4602   3881   5066    251    286    273       C  
ATOM   2280  O   LYS A 277      83.926 -23.271 -25.297  1.00 40.43           O  
ANISOU 2280  O   LYS A 277     5232   4432   5696    189    266    228       O  
ATOM   2281  CB  LYS A 277      80.987 -24.408 -24.918  1.00 35.29           C  
ANISOU 2281  CB  LYS A 277     4548   3767   5092    160    311    388       C  
ATOM   2282  CG  LYS A 277      79.471 -24.410 -24.615  1.00 37.37           C  
ANISOU 2282  CG  LYS A 277     4759   4046   5394    152    322    455       C  
ATOM   2283  CD  LYS A 277      79.156 -24.747 -23.145  1.00 37.26           C  
ANISOU 2283  CD  LYS A 277     4698   4116   5344    260    390    530       C  
ATOM   2284  CE  LYS A 277      79.704 -26.113 -22.734  1.00 34.65           C  
ANISOU 2284  CE  LYS A 277     4386   3762   5017    287    458    601       C  
ATOM   2285  NZ  LYS A 277      79.477 -26.388 -21.263  1.00 37.65           N  
ANISOU 2285  NZ  LYS A 277     4728   4242   5337    418    535    692       N  
ATOM   2286  N   ASN A 278      83.818 -24.224 -23.265  1.00 34.25           N  
ANISOU 2286  N   ASN A 278     4408   3766   4839    344    317    296       N  
ATOM   2287  CA  ASN A 278      85.240 -24.545 -23.220  1.00 33.65           C  
ANISOU 2287  CA  ASN A 278     4336   3703   4747    377    317    258       C  
ATOM   2288  C   ASN A 278      85.422 -26.048 -23.200  1.00 31.52           C  
ANISOU 2288  C   ASN A 278     4098   3400   4480    396    382    341       C  
ATOM   2289  O   ASN A 278      84.837 -26.729 -22.354  1.00 35.74           O  
ANISOU 2289  O   ASN A 278     4624   3966   4990    460    429    427       O  
ATOM   2290  CB  ASN A 278      85.887 -23.921 -22.002  1.00 30.77           C  
ANISOU 2290  CB  ASN A 278     3923   3449   4318    488    277    198       C  
ATOM   2291  CG  ASN A 278      85.647 -22.431 -21.965  1.00 57.26           C  
ANISOU 2291  CG  ASN A 278     7251   6814   7691    471    210    105       C  
ATOM   2292  OD1 ASN A 278      86.293 -21.680 -22.687  1.00 44.50           O  
ANISOU 2292  OD1 ASN A 278     5625   5144   6136    403    174     36       O  
ATOM   2293  ND2 ASN A 278      84.648 -22.007 -21.195  1.00 66.57           N  
ANISOU 2293  ND2 ASN A 278     8418   8049   8828    531    206    115       N  
ATOM   2294  N   TYR A 279      86.276 -26.552 -24.096  1.00 32.10           N  
ANISOU 2294  N   TYR A 279     4204   3409   4583    353    395    321       N  
ATOM   2295  CA  TYR A 279      86.491 -27.983 -24.227  1.00 33.26           C  
ANISOU 2295  CA  TYR A 279     4391   3497   4750    369    456    386       C  
ATOM   2296  C   TYR A 279      87.973 -28.301 -24.179  1.00 33.77           C  
ANISOU 2296  C   TYR A 279     4449   3589   4795    431    466    356       C  
ATOM   2297  O   TYR A 279      88.797 -27.567 -24.733  1.00 33.57           O  
ANISOU 2297  O   TYR A 279     4404   3575   4776    402    435    280       O  
ATOM   2298  CB  TYR A 279      85.934 -28.526 -25.550  1.00 34.06           C  
ANISOU 2298  CB  TYR A 279     4551   3475   4913    259    466    385       C  
ATOM   2299  CG  TYR A 279      84.456 -28.305 -25.734  1.00 34.69           C  
ANISOU 2299  CG  TYR A 279     4624   3525   5030    189    446    412       C  
ATOM   2300  CD1 TYR A 279      83.530 -29.039 -25.000  1.00 39.71           C  
ANISOU 2300  CD1 TYR A 279     5238   4148   5703    207    488    505       C  
ATOM   2301  CD2 TYR A 279      83.982 -27.374 -26.647  1.00 34.70           C  
ANISOU 2301  CD2 TYR A 279     4632   3514   5037    111    391    357       C  
ATOM   2302  CE1 TYR A 279      82.172 -28.852 -25.168  1.00 36.32           C  
ANISOU 2302  CE1 TYR A 279     4780   3695   5325    141    472    533       C  
ATOM   2303  CE2 TYR A 279      82.609 -27.173 -26.815  1.00 34.71           C  
ANISOU 2303  CE2 TYR A 279     4614   3497   5076     56    365    382       C  
ATOM   2304  CZ  TYR A 279      81.721 -27.930 -26.079  1.00 40.47           C  
ANISOU 2304  CZ  TYR A 279     5309   4216   5852     67    403    465       C  
ATOM   2305  OH  TYR A 279      80.370 -27.750 -26.230  1.00 40.94           O  
ANISOU 2305  OH  TYR A 279     5327   4262   5965     11    380    494       O  
ATOM   2306  N   PHE A 280      88.289 -29.417 -23.539  1.00 31.93           N  
ANISOU 2306  N   PHE A 280     4226   3358   4548    518    517    428       N  
ATOM   2307  CA  PHE A 280      89.596 -30.048 -23.655  1.00 29.82           C  
ANISOU 2307  CA  PHE A 280     3961   3092   4277    580    541    418       C  
ATOM   2308  C   PHE A 280      89.513 -30.981 -24.863  1.00 35.69           C  
ANISOU 2308  C   PHE A 280     4780   3694   5085    508    588    425       C  
ATOM   2309  O   PHE A 280      88.864 -32.034 -24.804  1.00 35.85           O  
ANISOU 2309  O   PHE A 280     4846   3627   5148    506    636    497       O  
ATOM   2310  CB  PHE A 280      89.920 -30.775 -22.349  1.00 33.31           C  
ANISOU 2310  CB  PHE A 280     4382   3609   4665    727    571    501       C  
ATOM   2311  CG  PHE A 280      91.354 -31.250 -22.214  1.00 33.78           C  
ANISOU 2311  CG  PHE A 280     4418   3709   4708    823    579    488       C  
ATOM   2312  CD1 PHE A 280      92.126 -31.597 -23.320  1.00 36.21           C  
ANISOU 2312  CD1 PHE A 280     4749   3940   5070    778    603    446       C  
ATOM   2313  CD2 PHE A 280      91.925 -31.350 -20.953  1.00 39.47           C  
ANISOU 2313  CD2 PHE A 280     5089   4561   5348    976    561    521       C  
ATOM   2314  CE1 PHE A 280      93.449 -32.046 -23.159  1.00 42.31           C  
ANISOU 2314  CE1 PHE A 280     5485   4758   5833    878    616    441       C  
ATOM   2315  CE2 PHE A 280      93.237 -31.795 -20.784  1.00 47.25           C  
ANISOU 2315  CE2 PHE A 280     6038   5596   6319   1076    558    512       C  
ATOM   2316  CZ  PHE A 280      93.998 -32.143 -21.889  1.00 45.11           C  
ANISOU 2316  CZ  PHE A 280     5779   5240   6119   1024    589    474       C  
ATOM   2317  N   ILE A 281      90.139 -30.591 -25.973  1.00 34.35           N  
ANISOU 2317  N   ILE A 281     4624   3499   4927    451    578    348       N  
ATOM   2318  CA  ILE A 281      89.945 -31.269 -27.250  1.00 35.47           C  
ANISOU 2318  CA  ILE A 281     4850   3522   5106    384    607    326       C  
ATOM   2319  C   ILE A 281      91.172 -32.100 -27.593  1.00 38.76           C  
ANISOU 2319  C   ILE A 281     5287   3913   5525    456    661    317       C  
ATOM   2320  O   ILE A 281      92.314 -31.651 -27.420  1.00 35.24           O  
ANISOU 2320  O   ILE A 281     4780   3551   5059    510    663    293       O  
ATOM   2321  CB  ILE A 281      89.625 -30.280 -28.385  1.00 40.46           C  
ANISOU 2321  CB  ILE A 281     5499   4145   5728    285    569    260       C  
ATOM   2322  CG1 ILE A 281      89.483 -31.041 -29.701  1.00 41.54           C  
ANISOU 2322  CG1 ILE A 281     5731   4179   5875    241    590    224       C  
ATOM   2323  CG2 ILE A 281      90.700 -29.207 -28.511  1.00 37.38           C  
ANISOU 2323  CG2 ILE A 281     5045   3836   5319    297    560    218       C  
ATOM   2324  CD1 ILE A 281      89.052 -30.165 -30.860  1.00 47.26           C  
ANISOU 2324  CD1 ILE A 281     6486   4903   6568    161    553    174       C  
ATOM   2325  N   THR A 282      90.929 -33.322 -28.077  1.00 34.84           N  
ANISOU 2325  N   THR A 282     4873   3297   5070    456    703    330       N  
ATOM   2326  CA  THR A 282      91.980 -34.210 -28.579  1.00 34.70           C  
ANISOU 2326  CA  THR A 282     4894   3230   5058    527    761    312       C  
ATOM   2327  C   THR A 282      91.583 -34.690 -29.967  1.00 39.23           C  
ANISOU 2327  C   THR A 282     5571   3687   5646    460    767    240       C  
ATOM   2328  O   THR A 282      90.548 -35.347 -30.121  1.00 38.37           O  
ANISOU 2328  O   THR A 282     5518   3466   5592    405    751    242       O  
ATOM   2329  CB  THR A 282      92.185 -35.399 -27.645  1.00 34.24           C  
ANISOU 2329  CB  THR A 282     4844   3128   5039    631    811    397       C  
ATOM   2330  OG1 THR A 282      92.529 -34.920 -26.343  1.00 38.71           O  
ANISOU 2330  OG1 THR A 282     5318   3826   5562    711    794    458       O  
ATOM   2331  CG2 THR A 282      93.318 -36.315 -28.158  1.00 37.10           C  
ANISOU 2331  CG2 THR A 282     5245   3437   5413    721    874    376       C  
ATOM   2332  N   ASP A 283      92.396 -34.367 -30.972  1.00 37.84           N  
ANISOU 2332  N   ASP A 283     5414   3540   5423    471    789    175       N  
ATOM   2333  CA  ASP A 283      92.103 -34.780 -32.341  1.00 39.03           C  
ANISOU 2333  CA  ASP A 283     5672   3604   5552    433    791     94       C  
ATOM   2334  C   ASP A 283      92.581 -36.206 -32.563  1.00 39.70           C  
ANISOU 2334  C   ASP A 283     5832   3576   5674    514    848     72       C  
ATOM   2335  O   ASP A 283      93.772 -36.493 -32.415  1.00 40.88           O  
ANISOU 2335  O   ASP A 283     5956   3762   5814    618    914     88       O  
ATOM   2336  CB  ASP A 283      92.766 -33.856 -33.352  1.00 40.68           C  
ANISOU 2336  CB  ASP A 283     5878   3898   5682    429    810     50       C  
ATOM   2337  CG  ASP A 283      92.383 -34.207 -34.770  1.00 50.34           C  
ANISOU 2337  CG  ASP A 283     7220   5057   6848    408    804    -37       C  
ATOM   2338  OD1 ASP A 283      91.188 -34.064 -35.117  1.00 50.76           O  
ANISOU 2338  OD1 ASP A 283     7317   5071   6899    324    728    -69       O  
ATOM   2339  OD2 ASP A 283      93.265 -34.643 -35.527  1.00 48.48           O  
ANISOU 2339  OD2 ASP A 283     7034   4819   6566    486    872    -77       O  
ATOM   2340  N   ALA A 284      91.663 -37.096 -32.945  1.00 40.45           N  
ANISOU 2340  N   ALA A 284     6016   3528   5825    468    821     29       N  
ATOM   2341  CA  ALA A 284      92.011 -38.510 -33.010  1.00 43.34           C  
ANISOU 2341  CA  ALA A 284     6456   3754   6259    542    872     11       C  
ATOM   2342  C   ALA A 284      92.957 -38.822 -34.167  1.00 49.45           C  
ANISOU 2342  C   ALA A 284     7307   4523   6961    621    921    -86       C  
ATOM   2343  O   ALA A 284      93.796 -39.722 -34.048  1.00 46.35           O  
ANISOU 2343  O   ALA A 284     6941   4072   6599    732    991    -81       O  
ATOM   2344  CB  ALA A 284      90.743 -39.365 -33.114  1.00 44.70           C  
ANISOU 2344  CB  ALA A 284     6690   3752   6542    457    822    -20       C  
ATOM   2345  N   GLN A 285      92.843 -38.106 -35.286  1.00 42.00           N  
ANISOU 2345  N   GLN A 285     6401   3642   5914    582    892   -167       N  
ATOM   2346  CA  GLN A 285      93.668 -38.435 -36.448  1.00 45.46           C  
ANISOU 2346  CA  GLN A 285     6924   4083   6266    671    949   -258       C  
ATOM   2347  C   GLN A 285      95.127 -38.040 -36.235  1.00 44.68           C  
ANISOU 2347  C   GLN A 285     6742   4109   6126    777   1050   -194       C  
ATOM   2348  O   GLN A 285      96.038 -38.796 -36.598  1.00 41.90           O  
ANISOU 2348  O   GLN A 285     6431   3727   5762    895   1130   -226       O  
ATOM   2349  CB  GLN A 285      93.115 -37.757 -37.705  1.00 46.04           C  
ANISOU 2349  CB  GLN A 285     7065   4208   6222    617    896   -346       C  
ATOM   2350  CG  GLN A 285      93.900 -38.090 -38.983  1.00 51.05           C  
ANISOU 2350  CG  GLN A 285     7801   4861   6736    727    962   -441       C  
ATOM   2351  CD  GLN A 285      93.820 -39.561 -39.368  1.00 58.74           C  
ANISOU 2351  CD  GLN A 285     8899   5665   7754    789    958   -560       C  
ATOM   2352  OE1 GLN A 285      92.734 -40.132 -39.454  1.00 65.64           O  
ANISOU 2352  OE1 GLN A 285     9835   6410   8697    710    860   -639       O  
ATOM   2353  NE2 GLN A 285      94.976 -40.183 -39.594  1.00 55.96           N  
ANISOU 2353  NE2 GLN A 285     8577   5307   7378    930   1065   -577       N  
ATOM   2354  N   THR A 286      95.375 -36.865 -35.648  1.00 41.74           N  
ANISOU 2354  N   THR A 286     6244   3872   5744    738   1045   -110       N  
ATOM   2355  CA  THR A 286      96.724 -36.318 -35.595  1.00 41.72           C  
ANISOU 2355  CA  THR A 286     6142   3993   5717    815   1127    -63       C  
ATOM   2356  C   THR A 286      97.370 -36.366 -34.220  1.00 40.71           C  
ANISOU 2356  C   THR A 286     5888   3914   5668    865   1135     23       C  
ATOM   2357  O   THR A 286      98.600 -36.330 -34.136  1.00 43.99           O  
ANISOU 2357  O   THR A 286     6221   4406   6087    956   1204     49       O  
ATOM   2358  CB  THR A 286      96.729 -34.859 -36.072  1.00 41.79           C  
ANISOU 2358  CB  THR A 286     6091   4121   5668    742   1120    -43       C  
ATOM   2359  OG1 THR A 286      96.001 -34.053 -35.133  1.00 41.89           O  
ANISOU 2359  OG1 THR A 286     6025   4162   5729    644   1035      6       O  
ATOM   2360  CG2 THR A 286      96.078 -34.747 -37.447  1.00 39.56           C  
ANISOU 2360  CG2 THR A 286     5935   3815   5282    711   1108   -117       C  
ATOM   2361  N   GLY A 287      96.590 -36.435 -33.149  1.00 37.14           N  
ANISOU 2361  N   GLY A 287     5411   3432   5271    818   1066     70       N  
ATOM   2362  CA  GLY A 287      97.160 -36.257 -31.834  1.00 37.65           C  
ANISOU 2362  CA  GLY A 287     5352   3579   5376    872   1059    150       C  
ATOM   2363  C   GLY A 287      97.328 -34.816 -31.402  1.00 36.40           C  
ANISOU 2363  C   GLY A 287     5067   3559   5206    811   1012    169       C  
ATOM   2364  O   GLY A 287      97.799 -34.576 -30.283  1.00 42.23           O  
ANISOU 2364  O   GLY A 287     5696   4381   5967    859    985    214       O  
ATOM   2365  N   SER A 288      96.960 -33.850 -32.245  1.00 38.96           N  
ANISOU 2365  N   SER A 288     5403   3906   5495    715    997    133       N  
ATOM   2366  CA  SER A 288      96.927 -32.456 -31.817  1.00 37.71           C  
ANISOU 2366  CA  SER A 288     5136   3843   5348    643    945    148       C  
ATOM   2367  C   SER A 288      95.840 -32.279 -30.755  1.00 40.63           C  
ANISOU 2367  C   SER A 288     5500   4205   5732    596    859    173       C  
ATOM   2368  O   SER A 288      94.749 -32.850 -30.870  1.00 39.66           O  
ANISOU 2368  O   SER A 288     5471   3992   5604    558    837    172       O  
ATOM   2369  CB  SER A 288      96.660 -31.551 -33.021  1.00 41.59           C  
ANISOU 2369  CB  SER A 288     5663   4339   5802    560    959    123       C  
ATOM   2370  OG  SER A 288      97.064 -30.218 -32.761  1.00 43.11           O  
ANISOU 2370  OG  SER A 288     5734   4614   6033    511    941    141       O  
ATOM   2371  N   SER A 289      96.149 -31.523 -29.698  1.00 35.91           N  
ANISOU 2371  N   SER A 289     4785   3702   5156    606    810    190       N  
ATOM   2372  CA  SER A 289      95.218 -31.367 -28.576  1.00 38.69           C  
ANISOU 2372  CA  SER A 289     5126   4069   5504    593    740    217       C  
ATOM   2373  C   SER A 289      95.357 -29.984 -27.935  1.00 38.37           C  
ANISOU 2373  C   SER A 289     4975   4129   5475    560    671    192       C  
ATOM   2374  O   SER A 289      96.341 -29.270 -28.145  1.00 36.53           O  
ANISOU 2374  O   SER A 289     4652   3952   5276    555    674    160       O  
ATOM   2375  CB  SER A 289      95.429 -32.468 -27.517  1.00 37.37           C  
ANISOU 2375  CB  SER A 289     4957   3907   5334    711    753    275       C  
ATOM   2376  OG  SER A 289      96.693 -32.368 -26.876  1.00 39.57           O  
ANISOU 2376  OG  SER A 289     5127   4291   5616    810    749    275       O  
ATOM   2377  N   LYS A 290      94.351 -29.603 -27.144  1.00 32.67           N  
ANISOU 2377  N   LYS A 290     4255   3422   4734    536    611    203       N  
ATOM   2378  CA  LYS A 290      94.398 -28.318 -26.451  1.00 36.13           C  
ANISOU 2378  CA  LYS A 290     4600   3945   5182    516    536    161       C  
ATOM   2379  C   LYS A 290      93.523 -28.383 -25.206  1.00 36.72           C  
ANISOU 2379  C   LYS A 290     4679   4065   5210    564    488    189       C  
ATOM   2380  O   LYS A 290      92.381 -28.849 -25.274  1.00 36.35           O  
ANISOU 2380  O   LYS A 290     4708   3956   5147    535    507    237       O  
ATOM   2381  CB  LYS A 290      93.953 -27.172 -27.377  1.00 35.87           C  
ANISOU 2381  CB  LYS A 290     4577   3871   5180    397    524    127       C  
ATOM   2382  CG  LYS A 290      93.951 -25.789 -26.708  1.00 36.39           C  
ANISOU 2382  CG  LYS A 290     4554   3994   5280    370    446     73       C  
ATOM   2383  CD  LYS A 290      94.086 -24.639 -27.741  1.00 40.14           C  
ANISOU 2383  CD  LYS A 290     5010   4421   5819    269    458     52       C  
ATOM   2384  CE  LYS A 290      92.905 -24.623 -28.724  1.00 37.43           C  
ANISOU 2384  CE  LYS A 290     4779   4002   5441    199    481     88       C  
ATOM   2385  NZ  LYS A 290      93.163 -23.704 -29.877  1.00 40.53           N  
ANISOU 2385  NZ  LYS A 290     5169   4353   5876    127    517     95       N  
ATOM   2386  N  ACYS A 291      94.065 -27.911 -24.075  0.66 34.16           N  
ANISOU 2386  N  ACYS A 291     4264   3852   4864    643    426    156       N  
ATOM   2387  N  BCYS A 291      94.063 -27.909 -24.081  0.34 34.96           N  
ANISOU 2387  N  BCYS A 291     4366   3953   4965    642    426    156       N  
ATOM   2388  CA ACYS A 291      93.384 -28.048 -22.785  0.66 35.64           C  
ANISOU 2388  CA ACYS A 291     4454   4111   4977    728    392    189       C  
ATOM   2389  CA BCYS A 291      93.387 -28.055 -22.795  0.34 36.47           C  
ANISOU 2389  CA BCYS A 291     4559   4215   5082    728    392    190       C  
ATOM   2390  C  ACYS A 291      92.152 -27.156 -22.691  0.66 37.21           C  
ANISOU 2390  C  ACYS A 291     4674   4296   5167    659    357    171       C  
ATOM   2391  C  BCYS A 291      92.156 -27.160 -22.694  0.34 36.86           C  
ANISOU 2391  C  BCYS A 291     4629   4252   5123    659    357    171       C  
ATOM   2392  O  ACYS A 291      91.122 -27.566 -22.142  0.66 37.52           O  
ANISOU 2392  O  ACYS A 291     4757   4337   5162    690    378    240       O  
ATOM   2393  O  BCYS A 291      91.122 -27.579 -22.159  0.34 38.00           O  
ANISOU 2393  O  BCYS A 291     4819   4397   5224    689    379    240       O  
ATOM   2394  CB ACYS A 291      94.344 -27.721 -21.641  0.66 41.00           C  
ANISOU 2394  CB ACYS A 291     5032   4931   5613    847    318    136       C  
ATOM   2395  CB BCYS A 291      94.365 -27.747 -21.664  0.34 41.53           C  
ANISOU 2395  CB BCYS A 291     5101   4997   5682    847    320    137       C  
ATOM   2396  SG ACYS A 291      95.715 -28.855 -21.457  0.66 39.56           S  
ANISOU 2396  SG ACYS A 291     4811   4795   5424    972    351    175       S  
ATOM   2397  SG BCYS A 291      95.227 -26.186 -21.899  0.34 53.89           S  
ANISOU 2397  SG BCYS A 291     6547   6597   7333    771    228     -8       S  
ATOM   2398  N   VAL A 292      92.248 -25.919 -23.167  1.00 31.22           N  
ANISOU 2398  N   VAL A 292     3876   3525   4460    573    309     88       N  
ATOM   2399  CA  VAL A 292      91.127 -24.970 -23.128  1.00 32.72           C  
ANISOU 2399  CA  VAL A 292     4083   3698   4652    514    274     66       C  
ATOM   2400  C   VAL A 292      90.923 -24.448 -24.541  1.00 37.89           C  
ANISOU 2400  C   VAL A 292     4770   4248   5377    384    297     58       C  
ATOM   2401  O   VAL A 292      91.667 -23.570 -25.006  1.00 39.91           O  
ANISOU 2401  O   VAL A 292     4974   4489   5699    335    277      0       O  
ATOM   2402  CB  VAL A 292      91.345 -23.814 -22.148  1.00 37.78           C  
ANISOU 2402  CB  VAL A 292     4648   4425   5281    561    181    -33       C  
ATOM   2403  CG1 VAL A 292      90.126 -22.883 -22.172  1.00 36.39           C  
ANISOU 2403  CG1 VAL A 292     4499   4218   5111    511    157    -50       C  
ATOM   2404  CG2 VAL A 292      91.580 -24.344 -20.738  1.00 38.12           C  
ANISOU 2404  CG2 VAL A 292     4666   4598   5222    717    152    -27       C  
ATOM   2405  N   CYS A 293      89.922 -24.987 -25.224  1.00 31.41           N  
ANISOU 2405  N   CYS A 293     4030   3356   4548    332    339    120       N  
ATOM   2406  CA  CYS A 293      89.521 -24.535 -26.550  1.00 31.52           C  
ANISOU 2406  CA  CYS A 293     4089   3289   4599    229    352    119       C  
ATOM   2407  C   CYS A 293      88.140 -23.907 -26.407  1.00 36.25           C  
ANISOU 2407  C   CYS A 293     4704   3877   5192    195    316    130       C  
ATOM   2408  O   CYS A 293      87.137 -24.611 -26.250  1.00 36.66           O  
ANISOU 2408  O   CYS A 293     4791   3915   5223    197    329    182       O  
ATOM   2409  CB  CYS A 293      89.505 -25.693 -27.546  1.00 35.05           C  
ANISOU 2409  CB  CYS A 293     4614   3667   5037    204    411    160       C  
ATOM   2410  SG  CYS A 293      89.342 -25.149 -29.271  1.00 44.70           S  
ANISOU 2410  SG  CYS A 293     5895   4820   6268    110    427    150       S  
ATOM   2411  N   SER A 294      88.088 -22.588 -26.462  1.00 31.83           N  
ANISOU 2411  N   SER A 294     4110   3317   4666    165    274     83       N  
ATOM   2412  CA  SER A 294      86.816 -21.880 -26.340  1.00 29.50           C  
ANISOU 2412  CA  SER A 294     3823   3014   4370    146    240     90       C  
ATOM   2413  C   SER A 294      86.084 -21.912 -27.674  1.00 34.42           C  
ANISOU 2413  C   SER A 294     4508   3567   5002     67    254    131       C  
ATOM   2414  O   SER A 294      86.663 -21.602 -28.717  1.00 36.56           O  
ANISOU 2414  O   SER A 294     4802   3796   5293     21    272    128       O  
ATOM   2415  CB  SER A 294      87.062 -20.440 -25.893  1.00 29.95           C  
ANISOU 2415  CB  SER A 294     3827   3082   4473    153    187     17       C  
ATOM   2416  OG  SER A 294      87.601 -20.415 -24.579  1.00 38.94           O  
ANISOU 2416  OG  SER A 294     4909   4301   5584    241    152    -41       O  
ATOM   2417  N   VAL A 295      84.811 -22.285 -27.638  1.00 32.10           N  
ANISOU 2417  N   VAL A 295     4236   3269   4692     58    244    171       N  
ATOM   2418  CA  VAL A 295      84.029 -22.563 -28.835  1.00 32.40           C  
ANISOU 2418  CA  VAL A 295     4328   3255   4728     -7    238    200       C  
ATOM   2419  C   VAL A 295      82.703 -21.828 -28.723  1.00 33.77           C  
ANISOU 2419  C   VAL A 295     4479   3437   4915    -17    195    217       C  
ATOM   2420  O   VAL A 295      82.019 -21.922 -27.698  1.00 33.70           O  
ANISOU 2420  O   VAL A 295     4427   3470   4908     24    194    236       O  
ATOM   2421  CB  VAL A 295      83.793 -24.073 -29.025  1.00 37.18           C  
ANISOU 2421  CB  VAL A 295     4970   3831   5326    -18    264    228       C  
ATOM   2422  CG1 VAL A 295      82.858 -24.328 -30.190  1.00 39.40           C  
ANISOU 2422  CG1 VAL A 295     5297   4065   5607    -83    231    233       C  
ATOM   2423  CG2 VAL A 295      85.131 -24.797 -29.255  1.00 31.68           C  
ANISOU 2423  CG2 VAL A 295     4302   3121   4616      3    312    211       C  
ATOM   2424  N   ILE A 296      82.349 -21.096 -29.772  1.00 35.35           N  
ANISOU 2424  N   ILE A 296     4707   3606   5117    -57    167    221       N  
ATOM   2425  CA  ILE A 296      81.083 -20.381 -29.842  1.00 37.30           C  
ANISOU 2425  CA  ILE A 296     4933   3859   5379    -60    122    241       C  
ATOM   2426  C   ILE A 296      80.387 -20.749 -31.152  1.00 33.36           C  
ANISOU 2426  C   ILE A 296     4482   3336   4857   -110     88    262       C  
ATOM   2427  O   ILE A 296      81.047 -20.927 -32.182  1.00 37.76           O  
ANISOU 2427  O   ILE A 296     5100   3869   5376   -131    100    254       O  
ATOM   2428  CB  ILE A 296      81.320 -18.853 -29.710  1.00 36.17           C  
ANISOU 2428  CB  ILE A 296     4772   3705   5266    -38    109    222       C  
ATOM   2429  CG1 ILE A 296      80.013 -18.111 -29.452  1.00 31.11           C  
ANISOU 2429  CG1 ILE A 296     4098   3079   4645    -12     69    240       C  
ATOM   2430  CG2 ILE A 296      82.079 -18.285 -30.932  1.00 35.48           C  
ANISOU 2430  CG2 ILE A 296     4734   3567   5180    -72    124    233       C  
ATOM   2431  CD1 ILE A 296      80.229 -16.621 -29.167  1.00 33.64           C  
ANISOU 2431  CD1 ILE A 296     4402   3368   5013     21     56    210       C  
ATOM   2432  N   ASP A 297      79.055 -20.892 -31.106  1.00 36.21           N  
ANISOU 2432  N   ASP A 297     4807   3713   5238   -120     44    285       N  
ATOM   2433  CA  ASP A 297      78.269 -21.189 -32.302  1.00 37.26           C  
ANISOU 2433  CA  ASP A 297     4970   3836   5352   -162    -16    288       C  
ATOM   2434  C   ASP A 297      77.564 -19.910 -32.740  1.00 38.87           C  
ANISOU 2434  C   ASP A 297     5161   4057   5550   -139    -62    314       C  
ATOM   2435  O   ASP A 297      76.402 -19.674 -32.434  1.00 38.19           O  
ANISOU 2435  O   ASP A 297     5011   3999   5501   -130   -102    336       O  
ATOM   2436  CB  ASP A 297      77.263 -22.320 -32.053  1.00 38.13           C  
ANISOU 2436  CB  ASP A 297     5033   3943   5512   -200    -42    294       C  
ATOM   2437  CG  ASP A 297      76.444 -22.658 -33.308  1.00 42.52           C  
ANISOU 2437  CG  ASP A 297     5610   4491   6054   -245   -131    270       C  
ATOM   2438  OD1 ASP A 297      76.893 -22.325 -34.424  1.00 43.81           O  
ANISOU 2438  OD1 ASP A 297     5853   4656   6138   -236   -157    246       O  
ATOM   2439  OD2 ASP A 297      75.342 -23.246 -33.179  1.00 42.26           O  
ANISOU 2439  OD2 ASP A 297     5508   4457   6092   -283   -176    275       O  
ATOM   2440  N   LEU A 298      78.301 -19.065 -33.443  1.00 37.99           N  
ANISOU 2440  N   LEU A 298     5106   3927   5402   -123    -47    322       N  
ATOM   2441  CA  LEU A 298      77.713 -17.937 -34.142  1.00 36.17           C  
ANISOU 2441  CA  LEU A 298     4886   3699   5157    -95    -87    362       C  
ATOM   2442  C   LEU A 298      77.402 -18.357 -35.563  1.00 37.88           C  
ANISOU 2442  C   LEU A 298     5167   3935   5289   -106   -140    367       C  
ATOM   2443  O   LEU A 298      78.113 -19.175 -36.150  1.00 40.07           O  
ANISOU 2443  O   LEU A 298     5507   4207   5510   -126   -120    338       O  
ATOM   2444  CB  LEU A 298      78.669 -16.739 -34.163  1.00 33.51           C  
ANISOU 2444  CB  LEU A 298     4573   3317   4843    -70    -32    385       C  
ATOM   2445  CG  LEU A 298      78.889 -16.023 -32.837  1.00 39.15           C  
ANISOU 2445  CG  LEU A 298     5225   4010   5639    -45     -7    358       C  
ATOM   2446  CD1 LEU A 298      80.080 -15.072 -32.956  1.00 35.90           C  
ANISOU 2446  CD1 LEU A 298     4832   3532   5275    -44     46    362       C  
ATOM   2447  CD2 LEU A 298      77.617 -15.266 -32.426  1.00 40.77           C  
ANISOU 2447  CD2 LEU A 298     5381   4230   5881      0    -53    376       C  
ATOM   2448  N   LEU A 299      76.346 -17.775 -36.122  1.00 36.46           N  
ANISOU 2448  N   LEU A 299     4974   3786   5092    -79   -212    400       N  
ATOM   2449  CA  LEU A 299      76.145 -17.867 -37.560  1.00 37.78           C  
ANISOU 2449  CA  LEU A 299     5214   3987   5152    -60   -270    409       C  
ATOM   2450  C   LEU A 299      77.399 -17.350 -38.249  1.00 38.46           C  
ANISOU 2450  C   LEU A 299     5391   4048   5174    -32   -186    450       C  
ATOM   2451  O   LEU A 299      77.938 -16.305 -37.872  1.00 39.82           O  
ANISOU 2451  O   LEU A 299     5554   4175   5403    -12   -118    503       O  
ATOM   2452  CB  LEU A 299      74.923 -17.048 -37.980  1.00 38.71           C  
ANISOU 2452  CB  LEU A 299     5299   4148   5263    -13   -354    457       C  
ATOM   2453  CG  LEU A 299      74.535 -17.090 -39.454  1.00 42.17           C  
ANISOU 2453  CG  LEU A 299     5806   4646   5570     29   -438    466       C  
ATOM   2454  CD1 LEU A 299      73.724 -18.353 -39.726  1.00 46.69           C  
ANISOU 2454  CD1 LEU A 299     6346   5262   6133    -19   -550    374       C  
ATOM   2455  CD2 LEU A 299      73.761 -15.833 -39.833  1.00 47.17           C  
ANISOU 2455  CD2 LEU A 299     6424   5306   6191    108   -480    553       C  
ATOM   2456  N   LEU A 300      77.892 -18.095 -39.237  1.00 38.80           N  
ANISOU 2456  N   LEU A 300     5518   4116   5109    -28   -185    423       N  
ATOM   2457  CA  LEU A 300      79.183 -17.735 -39.825  1.00 41.17           C  
ANISOU 2457  CA  LEU A 300     5891   4397   5353      1    -79    471       C  
ATOM   2458  C   LEU A 300      79.177 -16.305 -40.360  1.00 39.78           C  
ANISOU 2458  C   LEU A 300     5737   4212   5167     59    -46    586       C  
ATOM   2459  O   LEU A 300      80.175 -15.583 -40.230  1.00 40.48           O  
ANISOU 2459  O   LEU A 300     5827   4244   5311     60     61    647       O  
ATOM   2460  CB  LEU A 300      79.549 -18.720 -40.929  1.00 42.57           C  
ANISOU 2460  CB  LEU A 300     6165   4620   5390     22    -88    424       C  
ATOM   2461  CG  LEU A 300      80.984 -18.599 -41.429  1.00 43.33           C  
ANISOU 2461  CG  LEU A 300     6324   4705   5436     52     44    469       C  
ATOM   2462  CD1 LEU A 300      81.957 -18.680 -40.270  1.00 40.74           C  
ANISOU 2462  CD1 LEU A 300     5927   4312   5242     -1    131    455       C  
ATOM   2463  CD2 LEU A 300      81.248 -19.695 -42.433  1.00 45.96           C  
ANISOU 2463  CD2 LEU A 300     6753   5088   5621     87     29    400       C  
ATOM   2464  N   ASP A 301      78.057 -15.878 -40.956  1.00 40.78           N  
ANISOU 2464  N   ASP A 301     5873   4387   5236    108   -137    621       N  
ATOM   2465  CA  ASP A 301      77.943 -14.513 -41.460  1.00 40.63           C  
ANISOU 2465  CA  ASP A 301     5876   4350   5211    176   -106    746       C  
ATOM   2466  C   ASP A 301      78.128 -13.497 -40.341  1.00 39.82           C  
ANISOU 2466  C   ASP A 301     5698   4149   5284    151    -50    777       C  
ATOM   2467  O   ASP A 301      78.698 -12.419 -40.557  1.00 40.58           O  
ANISOU 2467  O   ASP A 301     5813   4176   5428    179     34    874       O  
ATOM   2468  CB  ASP A 301      76.580 -14.294 -42.131  1.00 44.15           C  
ANISOU 2468  CB  ASP A 301     6326   4874   5575    241   -234    768       C  
ATOM   2469  CG  ASP A 301      76.178 -15.433 -43.057  1.00 52.93           C  
ANISOU 2469  CG  ASP A 301     7492   6088   6531    257   -335    687       C  
ATOM   2470  OD1 ASP A 301      76.124 -16.590 -42.590  1.00 44.86           O  
ANISOU 2470  OD1 ASP A 301     6438   5066   5542    183   -376    568       O  
ATOM   2471  OD2 ASP A 301      75.888 -15.164 -44.243  1.00 53.42           O  
ANISOU 2471  OD2 ASP A 301     7630   6229   6440    349   -380    740       O  
ATOM   2472  N   ASP A 302      77.618 -13.811 -39.146  1.00 41.58           N  
ANISOU 2472  N   ASP A 302     5834   4361   5603    106    -95    695       N  
ATOM   2473  CA  ASP A 302      77.761 -12.906 -38.009  1.00 39.62           C  
ANISOU 2473  CA  ASP A 302     5520   4031   5504     97    -56    695       C  
ATOM   2474  C   ASP A 302      79.209 -12.831 -37.548  1.00 44.44           C  
ANISOU 2474  C   ASP A 302     6127   4571   6186     51     46    676       C  
ATOM   2475  O   ASP A 302      79.718 -11.743 -37.246  1.00 38.99           O  
ANISOU 2475  O   ASP A 302     5419   3790   5605     55    101    712       O  
ATOM   2476  CB  ASP A 302      76.874 -13.358 -36.845  1.00 41.83           C  
ANISOU 2476  CB  ASP A 302     5712   4340   5842     78   -119    615       C  
ATOM   2477  CG  ASP A 302      75.399 -13.007 -37.037  1.00 46.11           C  
ANISOU 2477  CG  ASP A 302     6216   4931   6374    129   -210    645       C  
ATOM   2478  OD1 ASP A 302      75.087 -12.076 -37.806  1.00 44.34           O  
ANISOU 2478  OD1 ASP A 302     6026   4694   6126    192   -222    730       O  
ATOM   2479  OD2 ASP A 302      74.554 -13.673 -36.395  1.00 46.95           O  
ANISOU 2479  OD2 ASP A 302     6248   5087   6503    111   -264    593       O  
ATOM   2480  N   PHE A 303      79.886 -13.976 -37.475  1.00 38.05           N  
ANISOU 2480  N   PHE A 303     5329   3796   5332      8     68    615       N  
ATOM   2481  CA  PHE A 303      81.294 -13.954 -37.091  1.00 37.98           C  
ANISOU 2481  CA  PHE A 303     5306   3735   5390    -28    159    599       C  
ATOM   2482  C   PHE A 303      82.136 -13.189 -38.112  1.00 38.17           C  
ANISOU 2482  C   PHE A 303     5377   3714   5411    -11    252    704       C  
ATOM   2483  O   PHE A 303      83.058 -12.455 -37.743  1.00 37.55           O  
ANISOU 2483  O   PHE A 303     5257   3552   5457    -37    323    722       O  
ATOM   2484  CB  PHE A 303      81.803 -15.388 -36.914  1.00 38.06           C  
ANISOU 2484  CB  PHE A 303     5323   3795   5343    -60    166    525       C  
ATOM   2485  CG  PHE A 303      83.256 -15.460 -36.542  1.00 38.61           C  
ANISOU 2485  CG  PHE A 303     5365   3829   5475    -87    253    507       C  
ATOM   2486  CD1 PHE A 303      83.675 -15.107 -35.264  1.00 43.37           C  
ANISOU 2486  CD1 PHE A 303     5887   4394   6197   -108    254    451       C  
ATOM   2487  CD2 PHE A 303      84.198 -15.873 -37.466  1.00 42.75           C  
ANISOU 2487  CD2 PHE A 303     5940   4367   5936    -82    330    542       C  
ATOM   2488  CE1 PHE A 303      85.013 -15.162 -34.924  1.00 43.89           C  
ANISOU 2488  CE1 PHE A 303     5912   4436   6329   -132    318    427       C  
ATOM   2489  CE2 PHE A 303      85.532 -15.937 -37.135  1.00 48.54           C  
ANISOU 2489  CE2 PHE A 303     6629   5073   6739   -106    411    531       C  
ATOM   2490  CZ  PHE A 303      85.941 -15.580 -35.865  1.00 46.96           C  
ANISOU 2490  CZ  PHE A 303     6337   4835   6670   -135    399    472       C  
ATOM   2491  N   VAL A 304      81.817 -13.321 -39.402  1.00 37.16           N  
ANISOU 2491  N   VAL A 304     5333   3640   5147     38    251    777       N  
ATOM   2492  CA  VAL A 304      82.548 -12.569 -40.421  1.00 36.17           C  
ANISOU 2492  CA  VAL A 304     5256   3482   5003     73    356    906       C  
ATOM   2493  C   VAL A 304      82.332 -11.072 -40.239  1.00 45.63           C  
ANISOU 2493  C   VAL A 304     6425   4576   6337     88    380    996       C  
ATOM   2494  O   VAL A 304      83.274 -10.275 -40.361  1.00 41.24           O  
ANISOU 2494  O   VAL A 304     5850   3927   5894     70    489   1075       O  
ATOM   2495  CB  VAL A 304      82.133 -13.026 -41.830  1.00 38.91           C  
ANISOU 2495  CB  VAL A 304     5710   3931   5142    149    339    962       C  
ATOM   2496  CG1 VAL A 304      82.610 -12.009 -42.887  1.00 39.76           C  
ANISOU 2496  CG1 VAL A 304     5872   4011   5222    214    451   1136       C  
ATOM   2497  CG2 VAL A 304      82.673 -14.408 -42.112  1.00 42.37           C  
ANISOU 2497  CG2 VAL A 304     6187   4442   5469    138    346    876       C  
ATOM   2498  N   GLU A 305      81.088 -10.659 -39.971  1.00 42.58           N  
ANISOU 2498  N   GLU A 305     6028   4194   5955    122    283    987       N  
ATOM   2499  CA  GLU A 305      80.820  -9.245 -39.714  1.00 38.91           C  
ANISOU 2499  CA  GLU A 305     5538   3617   5631    146    300   1058       C  
ATOM   2500  C   GLU A 305      81.649  -8.737 -38.539  1.00 37.50           C  
ANISOU 2500  C   GLU A 305     5276   3319   5655     75    341    986       C  
ATOM   2501  O   GLU A 305      82.259  -7.662 -38.609  1.00 41.39           O  
ANISOU 2501  O   GLU A 305     5751   3681   6293     64    419   1058       O  
ATOM   2502  CB  GLU A 305      79.329  -9.024 -39.442  1.00 39.23           C  
ANISOU 2502  CB  GLU A 305     5563   3695   5648    199    184   1036       C  
ATOM   2503  CG  GLU A 305      78.963  -7.552 -39.251  1.00 44.36           C  
ANISOU 2503  CG  GLU A 305     6198   4223   6436    245    199   1113       C  
ATOM   2504  CD  GLU A 305      77.459  -7.322 -39.130  1.00 46.36           C  
ANISOU 2504  CD  GLU A 305     6435   4528   6653    319     91   1109       C  
ATOM   2505  OE1 GLU A 305      76.871  -7.658 -38.079  1.00 45.83           O  
ANISOU 2505  OE1 GLU A 305     6299   4490   6625    302     23    993       O  
ATOM   2506  OE2 GLU A 305      76.870  -6.802 -40.095  1.00 50.97           O  
ANISOU 2506  OE2 GLU A 305     7069   5132   7165    405     78   1232       O  
ATOM   2507  N   ILE A 306      81.691  -9.511 -37.451  1.00 39.00           N  
ANISOU 2507  N   ILE A 306     5409   3549   5859     31    287    841       N  
ATOM   2508  CA  ILE A 306      82.404  -9.080 -36.249  1.00 39.41           C  
ANISOU 2508  CA  ILE A 306     5382   3514   6080    -19    298    746       C  
ATOM   2509  C   ILE A 306      83.885  -8.888 -36.541  1.00 39.42           C  
ANISOU 2509  C   ILE A 306     5360   3445   6174    -75    404    783       C  
ATOM   2510  O   ILE A 306      84.460  -7.833 -36.241  1.00 39.82           O  
ANISOU 2510  O   ILE A 306     5362   3362   6407   -105    443    792       O  
ATOM   2511  CB  ILE A 306      82.189 -10.083 -35.101  1.00 40.37           C  
ANISOU 2511  CB  ILE A 306     5457   3719   6161    -35    228    604       C  
ATOM   2512  CG1 ILE A 306      80.745 -10.026 -34.578  1.00 38.91           C  
ANISOU 2512  CG1 ILE A 306     5263   3581   5941     18    139    571       C  
ATOM   2513  CG2 ILE A 306      83.202  -9.829 -33.988  1.00 37.70           C  
ANISOU 2513  CG2 ILE A 306     5044   3321   5960    -78    240    501       C  
ATOM   2514  CD1 ILE A 306      80.325 -11.335 -33.881  1.00 41.25           C  
ANISOU 2514  CD1 ILE A 306     5534   3991   6148     10     89    487       C  
ATOM   2515  N   ILE A 307      84.530  -9.901 -37.133  1.00 37.19           N  
ANISOU 2515  N   ILE A 307     5104   3246   5780    -90    452    800       N  
ATOM   2516  CA  ILE A 307      85.975  -9.806 -37.324  1.00 40.78           C  
ANISOU 2516  CA  ILE A 307     5515   3649   6330   -140    558    830       C  
ATOM   2517  C   ILE A 307      86.321  -8.770 -38.388  1.00 40.05           C  
ANISOU 2517  C   ILE A 307     5449   3466   6303   -128    669   1002       C  
ATOM   2518  O   ILE A 307      87.345  -8.080 -38.286  1.00 42.00           O  
ANISOU 2518  O   ILE A 307     5624   3601   6733   -182    753   1037       O  
ATOM   2519  CB  ILE A 307      86.560 -11.200 -37.641  1.00 41.66           C  
ANISOU 2519  CB  ILE A 307     5649   3877   6303   -143    586    800       C  
ATOM   2520  CG1 ILE A 307      88.082 -11.174 -37.527  1.00 40.69           C  
ANISOU 2520  CG1 ILE A 307     5448   3712   6302   -195    683    803       C  
ATOM   2521  CG2 ILE A 307      86.148 -11.679 -39.025  1.00 43.29           C  
ANISOU 2521  CG2 ILE A 307     5966   4166   6315    -81    619    900       C  
ATOM   2522  CD1 ILE A 307      88.695 -12.574 -37.542  1.00 40.73           C  
ANISOU 2522  CD1 ILE A 307     5457   3823   6194   -190    700    744       C  
ATOM   2523  N   LYS A 308      85.459  -8.578 -39.383  1.00 40.54           N  
ANISOU 2523  N   LYS A 308     5604   3564   6233    -54    671   1117       N  
ATOM   2524  CA  LYS A 308      85.721  -7.534 -40.362  1.00 43.75           C  
ANISOU 2524  CA  LYS A 308     6042   3883   6698    -24    785   1304       C  
ATOM   2525  C   LYS A 308      85.430  -6.134 -39.832  1.00 45.74           C  
ANISOU 2525  C   LYS A 308     6250   3963   7166    -38    774   1328       C  
ATOM   2526  O   LYS A 308      85.662  -5.162 -40.548  1.00 42.37           O  
ANISOU 2526  O   LYS A 308     5841   3430   6829    -18    877   1494       O  
ATOM   2527  CB  LYS A 308      84.907  -7.771 -41.631  1.00 51.21           C  
ANISOU 2527  CB  LYS A 308     7108   4940   7411     82    783   1424       C  
ATOM   2528  CG  LYS A 308      85.459  -8.873 -42.524  1.00 54.62           C  
ANISOU 2528  CG  LYS A 308     7601   5508   7644    114    841   1446       C  
ATOM   2529  CD  LYS A 308      84.618  -8.979 -43.783  1.00 63.92           C  
ANISOU 2529  CD  LYS A 308     8901   6797   8588    234    822   1551       C  
ATOM   2530  CE  LYS A 308      85.233  -9.918 -44.800  1.00 71.56           C  
ANISOU 2530  CE  LYS A 308     9945   7893   9352    287    896   1582       C  
ATOM   2531  NZ  LYS A 308      84.349 -10.059 -45.998  1.00 80.24           N  
ANISOU 2531  NZ  LYS A 308    11168   9120  10199    418    847   1656       N  
ATOM   2532  N   SER A 309      84.943  -6.004 -38.602  1.00 40.65           N  
ANISOU 2532  N   SER A 309     5552   3284   6609    -63    661   1170       N  
ATOM   2533  CA  SER A 309      84.620  -4.697 -38.046  1.00 42.96           C  
ANISOU 2533  CA  SER A 309     5809   3409   7103    -64    640   1165       C  
ATOM   2534  C   SER A 309      85.617  -4.263 -36.978  1.00 47.15           C  
ANISOU 2534  C   SER A 309     6229   3814   7873   -158    640   1037       C  
ATOM   2535  O   SER A 309      85.333  -3.335 -36.213  1.00 43.39           O  
ANISOU 2535  O   SER A 309     5717   3206   7564   -161    588    962       O  
ATOM   2536  CB  SER A 309      83.196  -4.708 -37.494  1.00 44.72           C  
ANISOU 2536  CB  SER A 309     6059   3688   7245      5    510   1085       C  
ATOM   2537  OG  SER A 309      82.282  -5.095 -38.508  1.00 52.66           O  
ANISOU 2537  OG  SER A 309     7152   4814   8044     88    494   1194       O  
ATOM   2538  N   GLN A 310      86.795  -4.890 -36.934  1.00 41.88           N  
ANISOU 2538  N   GLN A 310     4950   3692   7271     -8    728   1393       N  
ATOM   2539  CA  GLN A 310      87.809  -4.578 -35.936  1.00 41.78           C  
ANISOU 2539  CA  GLN A 310     4837   3613   7424      5    788   1133       C  
ATOM   2540  C   GLN A 310      88.989  -3.841 -36.559  1.00 43.88           C  
ANISOU 2540  C   GLN A 310     5049   3768   7857    -26    948   1116       C  
ATOM   2541  O   GLN A 310      89.320  -4.019 -37.736  1.00 45.32           O  
ANISOU 2541  O   GLN A 310     5318   3952   7952    -55   1003   1254       O  
ATOM   2542  CB  GLN A 310      88.309  -5.848 -35.227  1.00 37.13           C  
ANISOU 2542  CB  GLN A 310     4306   3154   6650     18    677    949       C  
ATOM   2543  CG  GLN A 310      87.196  -6.708 -34.607  1.00 38.08           C  
ANISOU 2543  CG  GLN A 310     4508   3381   6580     36    533    950       C  
ATOM   2544  CD  GLN A 310      86.233  -5.897 -33.744  1.00 44.28           C  
ANISOU 2544  CD  GLN A 310     5202   4102   7521     47    534    930       C  
ATOM   2545  OE1 GLN A 310      86.652  -5.037 -32.969  1.00 42.08           O  
ANISOU 2545  OE1 GLN A 310     4814   3725   7448     39    612    783       O  
ATOM   2546  NE2 GLN A 310      84.932  -6.160 -33.891  1.00 37.94           N  
ANISOU 2546  NE2 GLN A 310     4440   3352   6624     52    466   1075       N  
ATOM   2547  N   ASP A 311      89.600  -2.976 -35.754  1.00 42.13           N  
ANISOU 2547  N   ASP A 311     4692   3445   7869    -43   1038    937       N  
ATOM   2548  CA  ASP A 311      90.866  -2.354 -36.105  1.00 42.51           C  
ANISOU 2548  CA  ASP A 311     4664   3404   8085    -92   1190    856       C  
ATOM   2549  C   ASP A 311      91.995  -3.349 -35.856  1.00 40.80           C  
ANISOU 2549  C   ASP A 311     4427   3313   7764    -94   1126    694       C  
ATOM   2550  O   ASP A 311      92.039  -3.998 -34.804  1.00 42.62           O  
ANISOU 2550  O   ASP A 311     4626   3654   7912    -72    990    544       O  
ATOM   2551  CB  ASP A 311      91.064  -1.089 -35.277  1.00 42.57           C  
ANISOU 2551  CB  ASP A 311     4539   3267   8370   -142   1315    705       C  
ATOM   2552  CG  ASP A 311      92.420  -0.440 -35.509  1.00 51.88           C  
ANISOU 2552  CG  ASP A 311     5619   4365   9728   -222   1473    583       C  
ATOM   2553  OD1 ASP A 311      93.423  -0.935 -34.959  1.00 49.50           O  
ANISOU 2553  OD1 ASP A 311     5231   4173   9403   -259   1412    388       O  
ATOM   2554  OD2 ASP A 311      92.474   0.575 -36.230  1.00 51.03           O  
ANISOU 2554  OD2 ASP A 311     5510   4084   9793   -249   1662    692       O  
ATOM   2555  N   LEU A 312      92.908  -3.471 -36.819  1.00 45.31           N  
ANISOU 2555  N   LEU A 312     5013   3859   8343   -114   1235    738       N  
ATOM   2556  CA  LEU A 312      93.925  -4.521 -36.791  1.00 45.23           C  
ANISOU 2556  CA  LEU A 312     4986   3954   8246    -87   1204    639       C  
ATOM   2557  C   LEU A 312      95.333  -3.978 -36.574  1.00 50.89           C  
ANISOU 2557  C   LEU A 312     5510   4637   9189   -134   1314    478       C  
ATOM   2558  O   LEU A 312      96.314  -4.651 -36.916  1.00 49.63           O  
ANISOU 2558  O   LEU A 312     5314   4524   9021   -110   1359    448       O  
ATOM   2559  CB  LEU A 312      93.870  -5.333 -38.085  1.00 44.27           C  
ANISOU 2559  CB  LEU A 312     5051   3840   7930    -81   1262    808       C  
ATOM   2560  CG  LEU A 312      92.500  -5.882 -38.492  1.00 41.80           C  
ANISOU 2560  CG  LEU A 312     4932   3583   7368    -77   1157    983       C  
ATOM   2561  CD1 LEU A 312      92.574  -6.630 -39.815  1.00 47.06           C  
ANISOU 2561  CD1 LEU A 312     5799   4258   7822   -124   1240   1123       C  
ATOM   2562  CD2 LEU A 312      91.944  -6.767 -37.397  1.00 46.16           C  
ANISOU 2562  CD2 LEU A 312     5496   4256   7784    -18    975    889       C  
ATOM   2563  N   SER A 313      95.461  -2.791 -35.991  1.00 45.53           N  
ANISOU 2563  N   SER A 313     4700   3877   8723   -209   1373    368       N  
ATOM   2564  CA  SER A 313      96.736  -2.082 -35.993  1.00 49.86           C  
ANISOU 2564  CA  SER A 313     5070   4375   9499   -296   1513    231       C  
ATOM   2565  C   SER A 313      97.599  -2.343 -34.759  1.00 52.94           C  
ANISOU 2565  C   SER A 313     5256   4920   9940   -330   1385      5       C  
ATOM   2566  O   SER A 313      98.681  -1.761 -34.650  1.00 51.66           O  
ANISOU 2566  O   SER A 313     4910   4750   9968   -426   1479   -126       O  
ATOM   2567  CB  SER A 313      96.487  -0.578 -36.122  1.00 52.14           C  
ANISOU 2567  CB  SER A 313     5340   4471  10001   -391   1691    230       C  
ATOM   2568  OG  SER A 313      95.789  -0.125 -34.980  1.00 51.65           O  
ANISOU 2568  OG  SER A 313     5251   4405   9969   -422   1614    122       O  
ATOM   2569  N   VAL A 314      97.172  -3.211 -33.848  1.00 50.19           N  
ANISOU 2569  N   VAL A 314     4932   4722   9418   -264   1172    -35       N  
ATOM   2570  CA  VAL A 314      97.837  -3.411 -32.566  1.00 47.79           C  
ANISOU 2570  CA  VAL A 314     4449   4585   9126   -307   1014   -225       C  
ATOM   2571  C   VAL A 314      98.099  -4.906 -32.373  1.00 49.78           C  
ANISOU 2571  C   VAL A 314     4713   5004   9199   -163    851   -169       C  
ATOM   2572  O   VAL A 314      97.346  -5.749 -32.870  1.00 48.08           O  
ANISOU 2572  O   VAL A 314     4694   4771   8804    -54    830    -26       O  
ATOM   2573  CB  VAL A 314      96.971  -2.799 -31.434  1.00 63.27           C  
ANISOU 2573  CB  VAL A 314     6445   6535  11059   -393    937   -343       C  
ATOM   2574  CG1 VAL A 314      96.926  -3.670 -30.195  1.00 62.09           C  
ANISOU 2574  CG1 VAL A 314     6274   6588  10729   -366    693   -434       C  
ATOM   2575  CG2 VAL A 314      97.417  -1.351 -31.117  1.00 57.46           C  
ANISOU 2575  CG2 VAL A 314     5584   5692  10555   -584   1090   -511       C  
ATOM   2576  N   VAL A 315      99.198  -5.237 -31.679  1.00 45.22           N  
ANISOU 2576  N   VAL A 315     3916   4588   8676   -168    746   -273       N  
ATOM   2577  CA  VAL A 315      99.601  -6.640 -31.531  1.00 42.66           C  
ANISOU 2577  CA  VAL A 315     3578   4403   8229     -7    625   -194       C  
ATOM   2578  C   VAL A 315      98.494  -7.466 -30.878  1.00 48.11           C  
ANISOU 2578  C   VAL A 315     4469   5148   8661     75    458   -150       C  
ATOM   2579  O   VAL A 315      98.134  -8.547 -31.365  1.00 47.58           O  
ANISOU 2579  O   VAL A 315     4568   5065   8445    210    468    -19       O  
ATOM   2580  CB  VAL A 315     100.916  -6.747 -30.737  1.00 49.66           C  
ANISOU 2580  CB  VAL A 315     4154   5483   9233    -27    505   -292       C  
ATOM   2581  CG1 VAL A 315     101.237  -8.216 -30.446  1.00 48.55           C  
ANISOU 2581  CG1 VAL A 315     3999   5476   8972    170    373   -181       C  
ATOM   2582  CG2 VAL A 315     102.055  -6.103 -31.513  1.00 56.34           C  
ANISOU 2582  CG2 VAL A 315     4794   6273  10342    -96    696   -321       C  
ATOM   2583  N   SER A 316      97.957  -6.989 -29.753  1.00 44.04           N  
ANISOU 2583  N   SER A 316     3955   4693   8087    -22    325   -272       N  
ATOM   2584  CA  SER A 316      96.949  -7.745 -29.019  1.00 41.21           C  
ANISOU 2584  CA  SER A 316     3776   4390   7490     40    173   -250       C  
ATOM   2585  C   SER A 316      96.049  -6.796 -28.243  1.00 45.07           C  
ANISOU 2585  C   SER A 316     4327   4830   7968   -104    157   -375       C  
ATOM   2586  O   SER A 316      96.506  -5.782 -27.711  1.00 45.24           O  
ANISOU 2586  O   SER A 316     4207   4859   8124   -262    177   -530       O  
ATOM   2587  CB  SER A 316      97.584  -8.755 -28.053  1.00 47.50           C  
ANISOU 2587  CB  SER A 316     4483   5393   8174    124    -33   -260       C  
ATOM   2588  OG  SER A 316      98.386  -8.097 -27.082  1.00 55.56           O  
ANISOU 2588  OG  SER A 316     5276   6557   9278    -14   -149   -413       O  
ATOM   2589  N   LYS A 317      94.770  -7.145 -28.164  1.00 41.08           N  
ANISOU 2589  N   LYS A 317     4034   4269   7308    -60    138   -315       N  
ATOM   2590  CA  LYS A 317      93.843  -6.355 -27.371  1.00 42.53           C  
ANISOU 2590  CA  LYS A 317     4282   4391   7488   -176    146   -426       C  
ATOM   2591  C   LYS A 317      92.587  -7.179 -27.148  1.00 43.53           C  
ANISOU 2591  C   LYS A 317     4617   4517   7404    -94     77   -347       C  
ATOM   2592  O   LYS A 317      92.369  -8.204 -27.801  1.00 39.00           O  
ANISOU 2592  O   LYS A 317     4151   3963   6702     32     56   -201       O  
ATOM   2593  CB  LYS A 317      93.511  -5.017 -28.046  1.00 46.35           C  
ANISOU 2593  CB  LYS A 317     4745   4674   8190   -262    358   -422       C  
ATOM   2594  CG  LYS A 317      92.622  -5.129 -29.283  1.00 43.47           C  
ANISOU 2594  CG  LYS A 317     4514   4182   7820   -163    464   -208       C  
ATOM   2595  CD  LYS A 317      91.959  -3.778 -29.577  1.00 47.29           C  
ANISOU 2595  CD  LYS A 317     4997   4469   8503   -236    648   -191       C  
ATOM   2596  CE  LYS A 317      91.112  -3.798 -30.846  1.00 49.83           C  
ANISOU 2596  CE  LYS A 317     5423   4692   8820   -150    730     56       C  
ATOM   2597  NZ  LYS A 317      90.643  -2.413 -31.205  1.00 45.38           N  
ANISOU 2597  NZ  LYS A 317     4826   3924   8491   -196    925    111       N  
ATOM   2598  N   VAL A 318      91.767  -6.707 -26.211  1.00 39.44           N  
ANISOU 2598  N   VAL A 318     4163   3968   6855   -185     68   -458       N  
ATOM   2599  CA  VAL A 318      90.484  -7.322 -25.891  1.00 40.06           C  
ANISOU 2599  CA  VAL A 318     4424   4033   6762   -137     28   -409       C  
ATOM   2600  C   VAL A 318      89.399  -6.616 -26.692  1.00 43.22           C  
ANISOU 2600  C   VAL A 318     4870   4260   7290   -132    189   -298       C  
ATOM   2601  O   VAL A 318      89.321  -5.383 -26.685  1.00 42.89           O  
ANISOU 2601  O   VAL A 318     4752   4086   7457   -218    332   -355       O  
ATOM   2602  CB  VAL A 318      90.195  -7.229 -24.383  1.00 55.59           C  
ANISOU 2602  CB  VAL A 318     6438   6060   8623   -245    -53   -592       C  
ATOM   2603  CG1 VAL A 318      88.783  -7.729 -24.076  1.00 48.39           C  
ANISOU 2603  CG1 VAL A 318     5709   5105   7572   -209    -51   -551       C  
ATOM   2604  CG2 VAL A 318      91.244  -8.000 -23.577  1.00 55.59           C  
ANISOU 2604  CG2 VAL A 318     6388   6266   8470   -241   -251   -658       C  
ATOM   2605  N   VAL A 319      88.568  -7.398 -27.378  1.00 34.63           N  
ANISOU 2605  N   VAL A 319     3905   3176   6078    -39    170   -131       N  
ATOM   2606  CA  VAL A 319      87.431  -6.911 -28.152  1.00 36.46           C  
ANISOU 2606  CA  VAL A 319     4169   3293   6393    -24    275     22       C  
ATOM   2607  C   VAL A 319      86.155  -7.368 -27.449  1.00 39.75           C  
ANISOU 2607  C   VAL A 319     4695   3725   6682    -23    230     12       C  
ATOM   2608  O   VAL A 319      86.027  -8.549 -27.097  1.00 39.27           O  
ANISOU 2608  O   VAL A 319     4753   3777   6392     11    112      0       O  
ATOM   2609  CB  VAL A 319      87.493  -7.438 -29.600  1.00 39.62           C  
ANISOU 2609  CB  VAL A 319     4616   3710   6729     41    284    229       C  
ATOM   2610  CG1 VAL A 319      86.156  -7.315 -30.282  1.00 39.24           C  
ANISOU 2610  CG1 VAL A 319     4620   3618   6670     52    317    415       C  
ATOM   2611  CG2 VAL A 319      88.567  -6.677 -30.403  1.00 43.61           C  
ANISOU 2611  CG2 VAL A 319     5006   4148   7416     25    391    254       C  
ATOM   2612  N   LYS A 320      85.221  -6.434 -27.233  1.00 36.75           N  
ANISOU 2612  N   LYS A 320     4277   3219   6468    -58    347     20       N  
ATOM   2613  CA  LYS A 320      83.959  -6.716 -26.551  1.00 40.44           C  
ANISOU 2613  CA  LYS A 320     4820   3678   6866    -64    343      5       C  
ATOM   2614  C   LYS A 320      82.830  -6.853 -27.566  1.00 41.23           C  
ANISOU 2614  C   LYS A 320     4918   3770   6978     -6    358    248       C  
ATOM   2615  O   LYS A 320      82.625  -5.964 -28.404  1.00 40.21           O  
ANISOU 2615  O   LYS A 320     4685   3544   7049     18    458    403       O  
ATOM   2616  CB  LYS A 320      83.606  -5.612 -25.554  1.00 44.32           C  
ANISOU 2616  CB  LYS A 320     5264   4025   7551   -145    494   -152       C  
ATOM   2617  CG  LYS A 320      84.607  -5.411 -24.426  1.00 51.05           C  
ANISOU 2617  CG  LYS A 320     6127   4908   8361   -256    471   -412       C  
ATOM   2618  CD  LYS A 320      84.669  -6.615 -23.505  1.00 57.34           C  
ANISOU 2618  CD  LYS A 320     7060   5867   8861   -269    297   -514       C  
ATOM   2619  CE  LYS A 320      85.593  -6.354 -22.319  1.00 68.76           C  
ANISOU 2619  CE  LYS A 320     8508   7372  10248   -403    252   -754       C  
ATOM   2620  NZ  LYS A 320      85.163  -5.182 -21.511  1.00 74.51           N  
ANISOU 2620  NZ  LYS A 320     9234   7940  11136   -549    444   -928       N  
ATOM   2621  N   VAL A 321      82.079  -7.945 -27.469  1.00 36.17           N  
ANISOU 2621  N   VAL A 321     4389   3235   6119      5    260    288       N  
ATOM   2622  CA  VAL A 321      80.961  -8.217 -28.371  1.00 38.46           C  
ANISOU 2622  CA  VAL A 321     4674   3566   6374     24    241    512       C  
ATOM   2623  C   VAL A 321      79.769  -8.642 -27.526  1.00 39.96           C  
ANISOU 2623  C   VAL A 321     4912   3774   6498      0    237    460       C  
ATOM   2624  O   VAL A 321      79.854  -9.628 -26.790  1.00 37.48           O  
ANISOU 2624  O   VAL A 321     4742   3535   5965    -24    164    324       O  
ATOM   2625  CB  VAL A 321      81.295  -9.317 -29.395  1.00 34.66           C  
ANISOU 2625  CB  VAL A 321     4304   3218   5649     25    132    626       C  
ATOM   2626  CG1 VAL A 321      80.202  -9.398 -30.460  1.00 39.33           C  
ANISOU 2626  CG1 VAL A 321     4869   3871   6206      2    106    872       C  
ATOM   2627  CG2 VAL A 321      82.684  -9.099 -30.018  1.00 35.01           C  
ANISOU 2627  CG2 VAL A 321     4327   3243   5731     45    151    620       C  
ATOM   2628  N   THR A 322      78.652  -7.931 -27.652  1.00 35.43           N  
ANISOU 2628  N   THR A 322     4213   3128   6120     12    325    584       N  
ATOM   2629  CA  THR A 322      77.446  -8.336 -26.937  1.00 30.52           C  
ANISOU 2629  CA  THR A 322     3615   2522   5459    -14    342    551       C  
ATOM   2630  C   THR A 322      76.798  -9.519 -27.660  1.00 33.28           C  
ANISOU 2630  C   THR A 322     4040   3049   5557    -46    204    691       C  
ATOM   2631  O   THR A 322      76.414  -9.418 -28.832  1.00 36.63           O  
ANISOU 2631  O   THR A 322     4377   3543   5997    -44    154    927       O  
ATOM   2632  CB  THR A 322      76.464  -7.173 -26.799  1.00 40.56           C  
ANISOU 2632  CB  THR A 322     4702   3647   7063     23    508    646       C  
ATOM   2633  OG1 THR A 322      77.090  -6.100 -26.078  1.00 39.03           O  
ANISOU 2633  OG1 THR A 322     4476   3267   7086     21    673    480       O  
ATOM   2634  CG2 THR A 322      75.222  -7.624 -26.024  1.00 39.00           C  
ANISOU 2634  CG2 THR A 322     4517   3462   6839     -8    547    599       C  
ATOM   2635  N   ILE A 323      76.670 -10.640 -26.953  1.00 35.89           N  
ANISOU 2635  N   ILE A 323     4544   3453   5641    -94    148    546       N  
ATOM   2636  CA  ILE A 323      76.134 -11.881 -27.503  1.00 31.09           C  
ANISOU 2636  CA  ILE A 323     4053   2997   4762   -155     45    627       C  
ATOM   2637  C   ILE A 323      75.230 -12.501 -26.449  1.00 32.36           C  
ANISOU 2637  C   ILE A 323     4302   3165   4830   -206     77    499       C  
ATOM   2638  O   ILE A 323      75.604 -12.574 -25.272  1.00 33.45           O  
ANISOU 2638  O   ILE A 323     4541   3230   4937   -199    122    293       O  
ATOM   2639  CB  ILE A 323      77.265 -12.867 -27.884  1.00 33.37           C  
ANISOU 2639  CB  ILE A 323     4531   3354   4795   -157    -34    576       C  
ATOM   2640  CG1 ILE A 323      78.339 -12.174 -28.754  1.00 37.49           C  
ANISOU 2640  CG1 ILE A 323     4971   3840   5434   -106    -31    659       C  
ATOM   2641  CG2 ILE A 323      76.688 -14.076 -28.609  1.00 34.12           C  
ANISOU 2641  CG2 ILE A 323     4762   3583   4618   -248    -99    665       C  
ATOM   2642  CD1 ILE A 323      79.483 -13.111 -29.184  1.00 36.28           C  
ANISOU 2642  CD1 ILE A 323     4981   3735   5070    -96    -74    620       C  
ATOM   2643  N   ASP A 324      74.045 -12.948 -26.867  1.00 34.20           N  
ANISOU 2643  N   ASP A 324     4495   3494   5004   -274     51    621       N  
ATOM   2644  CA  ASP A 324      73.057 -13.493 -25.933  1.00 29.97           C  
ANISOU 2644  CA  ASP A 324     4022   2961   4406   -335    105    511       C  
ATOM   2645  C   ASP A 324      72.850 -12.543 -24.755  1.00 34.72           C  
ANISOU 2645  C   ASP A 324     4542   3394   5256   -290    256    375       C  
ATOM   2646  O   ASP A 324      72.678 -12.970 -23.610  1.00 36.94           O  
ANISOU 2646  O   ASP A 324     4969   3626   5441   -329    320    182       O  
ATOM   2647  CB  ASP A 324      73.470 -14.882 -25.435  1.00 29.93           C  
ANISOU 2647  CB  ASP A 324     4308   3002   4060   -386     63    352       C  
ATOM   2648  CG  ASP A 324      73.584 -15.902 -26.543  1.00 37.20           C  
ANISOU 2648  CG  ASP A 324     5347   4059   4728   -457    -32    459       C  
ATOM   2649  OD1 ASP A 324      72.962 -15.717 -27.619  1.00 35.08           O  
ANISOU 2649  OD1 ASP A 324     4942   3894   4492   -519    -83    653       O  
ATOM   2650  OD2 ASP A 324      74.290 -16.931 -26.324  1.00 39.12           O  
ANISOU 2650  OD2 ASP A 324     5832   4306   4727   -458    -46    353       O  
ATOM   2651  N   TYR A 325      72.905 -11.236 -25.043  1.00 38.71           N  
ANISOU 2651  N   TYR A 325     4836   3797   6077   -217    334    473       N  
ATOM   2652  CA  TYR A 325      72.684 -10.129 -24.115  1.00 38.01           C  
ANISOU 2652  CA  TYR A 325     4649   3515   6278   -183    527    367       C  
ATOM   2653  C   TYR A 325      73.823  -9.907 -23.124  1.00 41.07           C  
ANISOU 2653  C   TYR A 325     5193   3802   6610   -197    571    112       C  
ATOM   2654  O   TYR A 325      73.710  -9.010 -22.289  1.00 47.25           O  
ANISOU 2654  O   TYR A 325     5937   4418   7598   -208    750    -16       O  
ATOM   2655  CB  TYR A 325      71.379 -10.274 -23.310  1.00 37.29           C  
ANISOU 2655  CB  TYR A 325     4528   3381   6260   -228    656    312       C  
ATOM   2656  CG  TYR A 325      70.131 -10.227 -24.159  1.00 38.49           C  
ANISOU 2656  CG  TYR A 325     4448   3625   6553   -216    637    576       C  
ATOM   2657  CD1 TYR A 325      69.737  -9.042 -24.788  1.00 42.33           C  
ANISOU 2657  CD1 TYR A 325     4652   4034   7397   -117    716    803       C  
ATOM   2658  CD2 TYR A 325      69.328 -11.352 -24.314  1.00 35.95           C  
ANISOU 2658  CD2 TYR A 325     4178   3469   6012   -310    544    609       C  
ATOM   2659  CE1 TYR A 325      68.587  -8.988 -25.562  1.00 42.91           C  
ANISOU 2659  CE1 TYR A 325     4480   4223   7603   -102    672   1082       C  
ATOM   2660  CE2 TYR A 325      68.167 -11.308 -25.090  1.00 39.13           C  
ANISOU 2660  CE2 TYR A 325     4338   3994   6535   -325    503    860       C  
ATOM   2661  CZ  TYR A 325      67.808 -10.122 -25.712  1.00 41.82           C  
ANISOU 2661  CZ  TYR A 325     4378   4282   7229   -215    552   1107       C  
ATOM   2662  OH  TYR A 325      66.668 -10.070 -26.480  1.00 43.84           O  
ANISOU 2662  OH  TYR A 325     4364   4687   7605   -225    484   1390       O  
ATOM   2663  N   THR A 326      74.919 -10.664 -23.191  1.00 38.09           N  
ANISOU 2663  N   THR A 326     4981   3521   5970   -206    424     38       N  
ATOM   2664  CA  THR A 326      76.042 -10.435 -22.288  1.00 40.22           C  
ANISOU 2664  CA  THR A 326     5360   3736   6186   -227    431   -176       C  
ATOM   2665  C   THR A 326      77.266  -9.979 -23.085  1.00 38.52           C  
ANISOU 2665  C   THR A 326     5067   3535   6032   -175    362   -111       C  
ATOM   2666  O   THR A 326      77.371 -10.216 -24.292  1.00 37.17           O  
ANISOU 2666  O   THR A 326     4840   3441   5842   -127    280     79       O  
ATOM   2667  CB  THR A 326      76.346 -11.708 -21.463  1.00 37.14           C  
ANISOU 2667  CB  THR A 326     5217   3440   5453   -271    329   -322       C  
ATOM   2668  OG1 THR A 326      77.069 -11.359 -20.275  1.00 49.50           O  
ANISOU 2668  OG1 THR A 326     6873   4955   6982   -327    357   -538       O  
ATOM   2669  CG2 THR A 326      77.157 -12.704 -22.259  1.00 36.91           C  
ANISOU 2669  CG2 THR A 326     5273   3545   5205   -220    163   -228       C  
ATOM   2670  N   GLU A 327      78.194  -9.295 -22.410  1.00 36.71           N  
ANISOU 2670  N   GLU A 327     4841   3235   5873   -206    405   -275       N  
ATOM   2671  CA  GLU A 327      79.430  -8.849 -23.060  1.00 33.48           C  
ANISOU 2671  CA  GLU A 327     4353   2839   5530   -173    353   -242       C  
ATOM   2672  C   GLU A 327      80.454  -9.981 -23.043  1.00 36.39           C  
ANISOU 2672  C   GLU A 327     4848   3359   5619   -152    173   -277       C  
ATOM   2673  O   GLU A 327      80.969 -10.344 -21.983  1.00 42.84           O  
ANISOU 2673  O   GLU A 327     5773   4221   6284   -199    116   -444       O  
ATOM   2674  CB  GLU A 327      79.996  -7.609 -22.370  1.00 48.48           C  
ANISOU 2674  CB  GLU A 327     6185   4604   7630   -243    486   -409       C  
ATOM   2675  CG  GLU A 327      79.392  -6.284 -22.836  1.00 77.23           C  
ANISOU 2675  CG  GLU A 327     9660   8059  11625   -220    695   -312       C  
ATOM   2676  CD  GLU A 327      80.370  -5.114 -22.701  1.00102.11           C  
ANISOU 2676  CD  GLU A 327    12737  11092  14970   -279    810   -428       C  
ATOM   2677  OE1 GLU A 327      81.345  -5.237 -21.927  1.00106.48           O  
ANISOU 2677  OE1 GLU A 327    13366  11710  15384   -377    741   -633       O  
ATOM   2678  OE2 GLU A 327      80.171  -4.078 -23.377  1.00108.66           O  
ANISOU 2678  OE2 GLU A 327    13429  11771  16086   -234    967   -304       O  
ATOM   2679  N   ILE A 328      80.759 -10.538 -24.215  1.00 35.19           N  
ANISOU 2679  N   ILE A 328     4686   3283   5400    -85     93   -110       N  
ATOM   2680  CA  ILE A 328      81.777 -11.582 -24.355  1.00 36.05           C  
ANISOU 2680  CA  ILE A 328     4897   3505   5295    -41    -34   -115       C  
ATOM   2681  C   ILE A 328      83.097 -10.921 -24.733  1.00 39.79           C  
ANISOU 2681  C   ILE A 328     5245   3969   5905    -18    -40   -126       C  
ATOM   2682  O   ILE A 328      83.148 -10.124 -25.675  1.00 36.86           O  
ANISOU 2682  O   ILE A 328     4750   3534   5722     -8     32    -19       O  
ATOM   2683  CB  ILE A 328      81.374 -12.620 -25.416  1.00 33.49           C  
ANISOU 2683  CB  ILE A 328     4664   3250   4809     -7    -74     51       C  
ATOM   2684  CG1 ILE A 328      80.066 -13.306 -25.021  1.00 36.73           C  
ANISOU 2684  CG1 ILE A 328     5191   3682   5081    -53    -65     50       C  
ATOM   2685  CG2 ILE A 328      82.507 -13.644 -25.630  1.00 35.59           C  
ANISOU 2685  CG2 ILE A 328     5033   3590   4900     57   -150     54       C  
ATOM   2686  CD1 ILE A 328      80.176 -14.133 -23.730  1.00 36.77           C  
ANISOU 2686  CD1 ILE A 328     5371   3714   4884    -62   -106   -107       C  
ATOM   2687  N   SER A 329      84.165 -11.261 -24.019  1.00 39.65           N  
ANISOU 2687  N   SER A 329     5250   4021   5792    -13   -127   -242       N  
ATOM   2688  CA  SER A 329      85.495 -10.759 -24.348  1.00 37.62           C  
ANISOU 2688  CA  SER A 329     4856   3782   5657      0   -144   -257       C  
ATOM   2689  C   SER A 329      86.185 -11.699 -25.333  1.00 41.69           C  
ANISOU 2689  C   SER A 329     5400   4360   6082    103   -188   -122       C  
ATOM   2690  O   SER A 329      86.267 -12.908 -25.096  1.00 39.75           O  
ANISOU 2690  O   SER A 329     5288   4186   5628    164   -262   -100       O  
ATOM   2691  CB  SER A 329      86.343 -10.607 -23.087  1.00 36.51           C  
ANISOU 2691  CB  SER A 329     4688   3713   5470    -62   -229   -436       C  
ATOM   2692  OG  SER A 329      85.829  -9.597 -22.261  1.00 43.98           O  
ANISOU 2692  OG  SER A 329     5617   4577   6518   -189   -142   -584       O  
ATOM   2693  N   PHE A 330      86.669 -11.137 -26.438  1.00 38.07           N  
ANISOU 2693  N   PHE A 330     4831   3853   5781    117   -116    -31       N  
ATOM   2694  CA  PHE A 330      87.482 -11.847 -27.420  1.00 36.75           C  
ANISOU 2694  CA  PHE A 330     4679   3718   5566    195   -112     77       C  
ATOM   2695  C   PHE A 330      88.914 -11.327 -27.354  1.00 39.20           C  
ANISOU 2695  C   PHE A 330     4815   4049   6031    205   -115     13       C  
ATOM   2696  O   PHE A 330      89.137 -10.130 -27.168  1.00 38.34           O  
ANISOU 2696  O   PHE A 330     4566   3888   6112    128    -69    -64       O  
ATOM   2697  CB  PHE A 330      86.973 -11.634 -28.852  1.00 35.00           C  
ANISOU 2697  CB  PHE A 330     4478   3433   5386    181    -15    241       C  
ATOM   2698  CG  PHE A 330      85.712 -12.386 -29.203  1.00 34.33           C  
ANISOU 2698  CG  PHE A 330     4556   3369   5116    160    -24    337       C  
ATOM   2699  CD1 PHE A 330      84.480 -11.989 -28.698  1.00 35.25           C  
ANISOU 2699  CD1 PHE A 330     4673   3469   5253    110    -32    327       C  
ATOM   2700  CD2 PHE A 330      85.751 -13.428 -30.114  1.00 39.43           C  
ANISOU 2700  CD2 PHE A 330     5350   4047   5587    171     -1    438       C  
ATOM   2701  CE1 PHE A 330      83.319 -12.656 -29.052  1.00 35.19           C  
ANISOU 2701  CE1 PHE A 330     4784   3501   5088     72    -46    419       C  
ATOM   2702  CE2 PHE A 330      84.594 -14.105 -30.479  1.00 43.21           C  
ANISOU 2702  CE2 PHE A 330     5976   4561   5882    111     -9    516       C  
ATOM   2703  CZ  PHE A 330      83.376 -13.715 -29.945  1.00 40.36           C  
ANISOU 2703  CZ  PHE A 330     5586   4208   5542     61    -45    510       C  
ATOM   2704  N   MET A 331      89.879 -12.213 -27.544  1.00 34.19           N  
ANISOU 2704  N   MET A 331     4181   3478   5332    296   -148     50       N  
ATOM   2705  CA  MET A 331      91.270 -11.805 -27.698  1.00 35.27           C  
ANISOU 2705  CA  MET A 331     4124   3643   5636    313   -138     21       C  
ATOM   2706  C   MET A 331      91.574 -11.665 -29.182  1.00 41.23           C  
ANISOU 2706  C   MET A 331     4869   4309   6488    331     13    140       C  
ATOM   2707  O   MET A 331      91.359 -12.602 -29.954  1.00 41.42           O  
ANISOU 2707  O   MET A 331     5046   4312   6382    389     70    250       O  
ATOM   2708  CB  MET A 331      92.219 -12.824 -27.061  1.00 39.70           C  
ANISOU 2708  CB  MET A 331     4654   4323   6108    421   -246     20       C  
ATOM   2709  CG  MET A 331      92.191 -12.836 -25.548  1.00 55.74           C  
ANISOU 2709  CG  MET A 331     6667   6470   8042    381   -415    -95       C  
ATOM   2710  SD  MET A 331      92.689 -11.250 -24.835  1.00 65.40           S  
ANISOU 2710  SD  MET A 331     7669   7728   9452    198   -448   -278       S  
ATOM   2711  CE  MET A 331      94.141 -10.837 -25.812  1.00 49.70           C  
ANISOU 2711  CE  MET A 331     5434   5742   7709    229   -366   -233       C  
ATOM   2712  N   LEU A 332      92.068 -10.497 -29.578  1.00 37.52           N  
ANISOU 2712  N   LEU A 332     4241   3781   6235    262     94    110       N  
ATOM   2713  CA  LEU A 332      92.436 -10.225 -30.961  1.00 35.18           C  
ANISOU 2713  CA  LEU A 332     3934   3394   6038    260    249    217       C  
ATOM   2714  C   LEU A 332      93.942 -10.029 -31.024  1.00 41.01           C  
ANISOU 2714  C   LEU A 332     4473   4160   6948    281    288    164       C  
ATOM   2715  O   LEU A 332      94.479  -9.123 -30.372  1.00 42.94           O  
ANISOU 2715  O   LEU A 332     4535   4431   7350    206    259     40       O  
ATOM   2716  CB  LEU A 332      91.715  -8.984 -31.493  1.00 38.65           C  
ANISOU 2716  CB  LEU A 332     4362   3721   6604    168    342    258       C  
ATOM   2717  CG  LEU A 332      92.164  -8.553 -32.892  1.00 41.75           C  
ANISOU 2717  CG  LEU A 332     4745   4020   7100    148    503    372       C  
ATOM   2718  CD1 LEU A 332      91.797  -9.634 -33.919  1.00 37.79           C  
ANISOU 2718  CD1 LEU A 332     4445   3526   6387    181    540    520       C  
ATOM   2719  CD2 LEU A 332      91.548  -7.201 -33.277  1.00 40.40           C  
ANISOU 2719  CD2 LEU A 332     4535   3729   7087     72    594    427       C  
ATOM   2720  N   TRP A 333      94.615 -10.886 -31.791  1.00 40.30           N  
ANISOU 2720  N   TRP A 333     4417   4064   6833    368    371    249       N  
ATOM   2721  CA  TRP A 333      96.047 -10.801 -32.033  1.00 39.34           C  
ANISOU 2721  CA  TRP A 333     4095   3958   6896    402    444    226       C  
ATOM   2722  C   TRP A 333      96.285 -10.523 -33.509  1.00 43.81           C  
ANISOU 2722  C   TRP A 333     4716   4391   7540    369    664    316       C  
ATOM   2723  O   TRP A 333      95.751 -11.234 -34.370  1.00 43.09           O  
ANISOU 2723  O   TRP A 333     4847   4238   7287    388    752    425       O  
ATOM   2724  CB  TRP A 333      96.754 -12.096 -31.636  1.00 41.44           C  
ANISOU 2724  CB  TRP A 333     4337   4311   7099    554    391    260       C  
ATOM   2725  CG  TRP A 333      96.784 -12.340 -30.167  1.00 47.37           C  
ANISOU 2725  CG  TRP A 333     5002   5215   7782    585    166    187       C  
ATOM   2726  CD1 TRP A 333      95.773 -12.846 -29.393  1.00 44.46           C  
ANISOU 2726  CD1 TRP A 333     4809   4886   7198    595     37    177       C  
ATOM   2727  CD2 TRP A 333      97.889 -12.105 -29.287  1.00 45.66           C  
ANISOU 2727  CD2 TRP A 333     4506   5145   7696    591     38    117       C  
ATOM   2728  NE1 TRP A 333      96.188 -12.935 -28.081  1.00 46.17           N  
ANISOU 2728  NE1 TRP A 333     4896   5259   7390    607   -158    107       N  
ATOM   2729  CE2 TRP A 333      97.479 -12.487 -27.990  1.00 44.46           C  
ANISOU 2729  CE2 TRP A 333     4394   5124   7376    600   -176     75       C  
ATOM   2730  CE3 TRP A 333      99.182 -11.603 -29.466  1.00 50.88           C  
ANISOU 2730  CE3 TRP A 333     4882   5855   8595    574     80     87       C  
ATOM   2731  CZ2 TRP A 333      98.318 -12.380 -26.882  1.00 47.96           C  
ANISOU 2731  CZ2 TRP A 333     4607   5758   7856    583   -368     15       C  
ATOM   2732  CZ3 TRP A 333     100.016 -11.504 -28.367  1.00 55.55           C  
ANISOU 2732  CZ3 TRP A 333     5219   6645   9244    559   -113     26       C  
ATOM   2733  CH2 TRP A 333      99.582 -11.890 -27.091  1.00 54.01           C  
ANISOU 2733  CH2 TRP A 333     5077   6593   8853    560   -345     -4       C  
ATOM   2734  N   CYS A 334      97.116  -9.518 -33.794  1.00 42.43           N  
ANISOU 2734  N   CYS A 334     4351   4174   7595    300    759    264       N  
ATOM   2735  CA  CYS A 334      97.386  -9.083 -35.155  1.00 44.95           C  
ANISOU 2735  CA  CYS A 334     4722   4358   7999    248    980    342       C  
ATOM   2736  C   CYS A 334      98.884  -8.942 -35.383  1.00 48.64           C  
ANISOU 2736  C   CYS A 334     4962   4824   8696    263   1102    290       C  
ATOM   2737  O   CYS A 334      99.662  -8.727 -34.451  1.00 47.51           O  
ANISOU 2737  O   CYS A 334     4568   4791   8691    269    997    181       O  
ATOM   2738  CB  CYS A 334      96.714  -7.750 -35.462  1.00 44.02           C  
ANISOU 2738  CB  CYS A 334     4626   4143   7958    125   1028    353       C  
ATOM   2739  SG  CYS A 334      94.902  -7.832 -35.395  1.00 46.64           S  
ANISOU 2739  SG  CYS A 334     5190   4468   8062    110    916    455       S  
ATOM   2740  N   LYS A 335      99.276  -9.042 -36.651  1.00 45.62           N  
ANISOU 2740  N   LYS A 335     4666   4323   8347    251   1328    371       N  
ATOM   2741  CA  LYS A 335     100.661  -8.813 -37.038  1.00 52.86           C  
ANISOU 2741  CA  LYS A 335     5370   5208   9506    251   1495    328       C  
ATOM   2742  C   LYS A 335     100.679  -8.195 -38.427  1.00 56.54           C  
ANISOU 2742  C   LYS A 335     5971   5503  10007    146   1746    398       C  
ATOM   2743  O   LYS A 335     100.063  -8.730 -39.354  1.00 51.33           O  
ANISOU 2743  O   LYS A 335     5589   4765   9147    136   1844    514       O  
ATOM   2744  CB  LYS A 335     101.478 -10.111 -37.016  1.00 57.95           C  
ANISOU 2744  CB  LYS A 335     5959   5895  10164    406   1546    362       C  
ATOM   2745  CG  LYS A 335     102.921  -9.918 -37.472  1.00 65.40           C  
ANISOU 2745  CG  LYS A 335     6657   6802  11389    417   1745    331       C  
ATOM   2746  CD  LYS A 335     103.692 -11.235 -37.485  1.00 75.21           C  
ANISOU 2746  CD  LYS A 335     7840   8060  12676    600   1830    393       C  
ATOM   2747  CE  LYS A 335     104.093 -11.664 -36.080  1.00 85.01           C  
ANISOU 2747  CE  LYS A 335     8820   9508  13974    724   1565    369       C  
ATOM   2748  NZ  LYS A 335     105.580 -11.664 -35.906  1.00 96.06           N  
ANISOU 2748  NZ  LYS A 335     9830  10982  15685    796   1626    356       N  
ATOM   2749  N   ASP A 336     101.371  -7.064 -38.551  1.00 58.71           N  
ANISOU 2749  N   ASP A 336     6060   5726  10520     49   1850    325       N  
ATOM   2750  CA  ASP A 336     101.546  -6.366 -39.826  1.00 61.17           C  
ANISOU 2750  CA  ASP A 336     6480   5867  10894    -57   2106    389       C  
ATOM   2751  C   ASP A 336     100.211  -6.110 -40.525  1.00 61.40           C  
ANISOU 2751  C   ASP A 336     6815   5818  10697   -116   2099    536       C  
ATOM   2752  O   ASP A 336     100.088  -6.253 -41.743  1.00 66.60           O  
ANISOU 2752  O   ASP A 336     7689   6374  11243   -169   2274    655       O  
ATOM   2753  CB  ASP A 336     102.500  -7.135 -40.739  1.00 64.33           C  
ANISOU 2753  CB  ASP A 336     6903   6199  11342    -16   2349    421       C  
ATOM   2754  CG  ASP A 336     103.894  -7.269 -40.145  1.00 76.78           C  
ANISOU 2754  CG  ASP A 336     8122   7855  13196     46   2376    305       C  
ATOM   2755  OD1 ASP A 336     104.356  -6.310 -39.488  1.00 77.13           O  
ANISOU 2755  OD1 ASP A 336     7909   7954  13442    -30   2308    189       O  
ATOM   2756  OD2 ASP A 336     104.523  -8.338 -40.326  1.00 83.88           O  
ANISOU 2756  OD2 ASP A 336     8992   8761  14117    166   2471    334       O  
ATOM   2757  N   GLY A 337      99.194  -5.739 -39.746  1.00 57.69           N  
ANISOU 2757  N   GLY A 337     6360   5404  10155   -116   1894    536       N  
ATOM   2758  CA  GLY A 337      97.911  -5.380 -40.316  1.00 49.33           C  
ANISOU 2758  CA  GLY A 337     5528   4288   8926   -163   1867    695       C  
ATOM   2759  C   GLY A 337      96.994  -6.532 -40.669  1.00 56.49           C  
ANISOU 2759  C   GLY A 337     6682   5263   9519   -127   1776    814       C  
ATOM   2760  O   GLY A 337      95.915  -6.289 -41.225  1.00 53.83           O  
ANISOU 2760  O   GLY A 337     6519   4909   9026   -180   1739    969       O  
ATOM   2761  N   HIS A 338      97.381  -7.773 -40.373  1.00 53.85           N  
ANISOU 2761  N   HIS A 338     6364   5005   9093    -45   1746    756       N  
ATOM   2762  CA  HIS A 338      96.534  -8.940 -40.588  1.00 55.70           C  
ANISOU 2762  CA  HIS A 338     6839   5297   9027    -26   1676    837       C  
ATOM   2763  C   HIS A 338      96.194  -9.600 -39.256  1.00 51.16           C  
ANISOU 2763  C   HIS A 338     6191   4845   8404     81   1459    749       C  
ATOM   2764  O   HIS A 338      96.940  -9.485 -38.281  1.00 47.57           O  
ANISOU 2764  O   HIS A 338     5505   4443   8128    154   1391    625       O  
ATOM   2765  CB  HIS A 338      97.211  -9.982 -41.491  1.00 60.42           C  
ANISOU 2765  CB  HIS A 338     7591   5837   9528    -26   1886    857       C  
ATOM   2766  CG  HIS A 338      97.669  -9.442 -42.809  1.00 86.18           C  
ANISOU 2766  CG  HIS A 338    10950   8974  12821   -143   2130    929       C  
ATOM   2767  ND1 HIS A 338      96.797  -8.950 -43.757  1.00 92.63           N  
ANISOU 2767  ND1 HIS A 338    11975   9762  13458   -280   2143   1084       N  
ATOM   2768  CD2 HIS A 338      98.907  -9.332 -43.345  1.00 94.55           C  
ANISOU 2768  CD2 HIS A 338    11927   9931  14066   -149   2374    878       C  
ATOM   2769  CE1 HIS A 338      97.480  -8.554 -44.816  1.00 95.28           C  
ANISOU 2769  CE1 HIS A 338    12377   9978  13845   -371   2384   1123       C  
ATOM   2770  NE2 HIS A 338      98.762  -8.774 -44.592  1.00 93.91           N  
ANISOU 2770  NE2 HIS A 338    12033   9750  13900   -296   2542    989       N  
ATOM   2771  N   VAL A 339      95.068 -10.317 -39.230  1.00 46.70           N  
ANISOU 2771  N   VAL A 339     5828   4338   7580     73   1349    818       N  
ATOM   2772  CA  VAL A 339      94.718 -11.117 -38.060  1.00 38.30           C  
ANISOU 2772  CA  VAL A 339     4748   3376   6430    168   1173    745       C  
ATOM   2773  C   VAL A 339      95.686 -12.278 -37.899  1.00 42.96           C  
ANISOU 2773  C   VAL A 339     5330   3970   7024    281   1256    694       C  
ATOM   2774  O   VAL A 339      96.021 -12.971 -38.869  1.00 42.55           O  
ANISOU 2774  O   VAL A 339     5439   3840   6887    264   1451    746       O  
ATOM   2775  CB  VAL A 339      93.282 -11.656 -38.169  1.00 44.75           C  
ANISOU 2775  CB  VAL A 339     5792   4245   6968    115   1067    831       C  
ATOM   2776  CG1 VAL A 339      92.921 -12.403 -36.895  1.00 40.81           C  
ANISOU 2776  CG1 VAL A 339     5280   3837   6391    208    900    746       C  
ATOM   2777  CG2 VAL A 339      92.307 -10.528 -38.436  1.00 41.71           C  
ANISOU 2777  CG2 VAL A 339     5392   3852   6602     24   1002    926       C  
ATOM   2778  N   GLU A 340      96.123 -12.517 -36.662  1.00 41.69           N  
ANISOU 2778  N   GLU A 340     4990   3895   6957    395   1117    603       N  
ATOM   2779  CA  GLU A 340      96.779 -13.778 -36.319  1.00 43.46           C  
ANISOU 2779  CA  GLU A 340     5221   4138   7156    538   1153    597       C  
ATOM   2780  C   GLU A 340      95.812 -14.770 -35.683  1.00 46.37           C  
ANISOU 2780  C   GLU A 340     5780   4561   7276    582   1025    611       C  
ATOM   2781  O   GLU A 340      95.731 -15.928 -36.113  1.00 43.98           O  
ANISOU 2781  O   GLU A 340     5687   4201   6822    622   1150    660       O  
ATOM   2782  CB  GLU A 340      97.965 -13.539 -35.382  1.00 49.67           C  
ANISOU 2782  CB  GLU A 340     5677   5007   8187    642   1073    521       C  
ATOM   2783  CG  GLU A 340      99.113 -12.809 -36.036  1.00 73.54           C  
ANISOU 2783  CG  GLU A 340     8500   7971  11470    609   1241    501       C  
ATOM   2784  CD  GLU A 340     100.455 -13.237 -35.485  1.00 85.24           C  
ANISOU 2784  CD  GLU A 340     9702   9522  13162    751   1244    482       C  
ATOM   2785  OE1 GLU A 340     100.587 -13.344 -34.246  1.00 90.21           O  
ANISOU 2785  OE1 GLU A 340    10166  10304  13806    817   1015    442       O  
ATOM   2786  OE2 GLU A 340     101.371 -13.482 -36.299  1.00 88.08           O  
ANISOU 2786  OE2 GLU A 340    10007   9790  13671    792   1478    516       O  
ATOM   2787  N   THR A 341      95.087 -14.345 -34.650  1.00 40.75           N  
ANISOU 2787  N   THR A 341     5014   3945   6525    564    805    559       N  
ATOM   2788  CA  THR A 341      93.943 -15.111 -34.175  1.00 39.71           C  
ANISOU 2788  CA  THR A 341     5090   3852   6146    563    700    572       C  
ATOM   2789  C   THR A 341      92.940 -14.180 -33.504  1.00 41.10           C  
ANISOU 2789  C   THR A 341     5218   4086   6311    476    529    527       C  
ATOM   2790  O   THR A 341      93.227 -13.017 -33.204  1.00 39.74           O  
ANISOU 2790  O   THR A 341     4849   3923   6327    435    486    471       O  
ATOM   2791  CB  THR A 341      94.353 -16.231 -33.214  1.00 45.01           C  
ANISOU 2791  CB  THR A 341     5762   4574   6765    719    636    556       C  
ATOM   2792  OG1 THR A 341      93.211 -17.045 -32.938  1.00 45.67           O  
ANISOU 2792  OG1 THR A 341     6093   4666   6593    697    585    571       O  
ATOM   2793  CG2 THR A 341      94.868 -15.656 -31.907  1.00 39.37           C  
ANISOU 2793  CG2 THR A 341     4789   3981   6191    770    437    475       C  
ATOM   2794  N   PHE A 342      91.761 -14.741 -33.237  1.00 40.55           N  
ANISOU 2794  N   PHE A 342     5336   4044   6027    445    456    546       N  
ATOM   2795  CA  PHE A 342      90.623 -14.004 -32.701  1.00 36.54           C  
ANISOU 2795  CA  PHE A 342     4814   3571   5498    365    332    522       C  
ATOM   2796  C   PHE A 342      89.738 -15.050 -32.045  1.00 40.76           C  
ANISOU 2796  C   PHE A 342     5530   4154   5804    382    252    509       C  
ATOM   2797  O   PHE A 342      89.139 -15.860 -32.754  1.00 42.78           O  
ANISOU 2797  O   PHE A 342     5994   4392   5868    335    321    579       O  
ATOM   2798  CB  PHE A 342      89.897 -13.273 -33.828  1.00 36.86           C  
ANISOU 2798  CB  PHE A 342     4901   3564   5541    248    400    629       C  
ATOM   2799  CG  PHE A 342      88.729 -12.430 -33.386  1.00 40.88           C  
ANISOU 2799  CG  PHE A 342     5362   4088   6083    186    306    638       C  
ATOM   2800  CD1 PHE A 342      88.892 -11.417 -32.451  1.00 40.12           C  
ANISOU 2800  CD1 PHE A 342     5083   3977   6183    196    256    536       C  
ATOM   2801  CD2 PHE A 342      87.482 -12.608 -33.965  1.00 41.89           C  
ANISOU 2801  CD2 PHE A 342     5619   4240   6057    105    288    754       C  
ATOM   2802  CE1 PHE A 342      87.811 -10.616 -32.070  1.00 39.37           C  
ANISOU 2802  CE1 PHE A 342     4948   3860   6151    147    220    547       C  
ATOM   2803  CE2 PHE A 342      86.396 -11.814 -33.594  1.00 43.45           C  
ANISOU 2803  CE2 PHE A 342     5741   4443   6326     67    222    788       C  
ATOM   2804  CZ  PHE A 342      86.562 -10.820 -32.646  1.00 39.36           C  
ANISOU 2804  CZ  PHE A 342     5052   3877   6025    100    206    684       C  
ATOM   2805  N   TYR A 343      89.685 -15.078 -30.716  1.00 36.90           N  
ANISOU 2805  N   TYR A 343     4981   3724   5314    429    122    414       N  
ATOM   2806  CA  TYR A 343      88.933 -16.143 -30.060  1.00 35.78           C  
ANISOU 2806  CA  TYR A 343     5028   3616   4952    451     66    400       C  
ATOM   2807  C   TYR A 343      88.179 -15.629 -28.845  1.00 39.04           C  
ANISOU 2807  C   TYR A 343     5399   4076   5360    409    -63    305       C  
ATOM   2808  O   TYR A 343      88.636 -14.700 -28.166  1.00 38.42           O  
ANISOU 2808  O   TYR A 343     5140   4019   5437    398   -126    220       O  
ATOM   2809  CB  TYR A 343      89.851 -17.308 -29.635  1.00 36.07           C  
ANISOU 2809  CB  TYR A 343     5117   3663   4924    593     78    404       C  
ATOM   2810  CG  TYR A 343      90.980 -16.939 -28.694  1.00 38.82           C  
ANISOU 2810  CG  TYR A 343     5241   4082   5425    684    -30    348       C  
ATOM   2811  CD1 TYR A 343      90.808 -16.981 -27.314  1.00 42.11           C  
ANISOU 2811  CD1 TYR A 343     5639   4587   5773    697   -191    273       C  
ATOM   2812  CD2 TYR A 343      92.228 -16.566 -29.187  1.00 43.08           C  
ANISOU 2812  CD2 TYR A 343     5588   4615   6165    736     30    370       C  
ATOM   2813  CE1 TYR A 343      91.850 -16.655 -26.452  1.00 42.19           C  
ANISOU 2813  CE1 TYR A 343     5442   4698   5890    747   -314    228       C  
ATOM   2814  CE2 TYR A 343      93.271 -16.244 -28.335  1.00 41.27           C  
ANISOU 2814  CE2 TYR A 343     5128   4484   6070    796    -86    324       C  
ATOM   2815  CZ  TYR A 343      93.076 -16.294 -26.970  1.00 44.28           C  
ANISOU 2815  CZ  TYR A 343     5493   4974   6359    795   -271    257       C  
ATOM   2816  OH  TYR A 343      94.111 -15.978 -26.124  1.00 54.72           O  
ANISOU 2816  OH  TYR A 343     6582   6427   7782    822   -411    218       O  
ATOM   2817  N   PRO A 344      87.027 -16.226 -28.536  1.00 42.68           N  
ANISOU 2817  N   PRO A 344     6032   4547   5639    366    -85    305       N  
ATOM   2818  CA  PRO A 344      86.298 -15.836 -27.326  1.00 40.46           C  
ANISOU 2818  CA  PRO A 344     5734   4294   5344    323   -176    204       C  
ATOM   2819  C   PRO A 344      86.970 -16.422 -26.102  1.00 41.01           C  
ANISOU 2819  C   PRO A 344     5827   4422   5334    404   -270    126       C  
ATOM   2820  O   PRO A 344      87.624 -17.466 -26.167  1.00 40.38           O  
ANISOU 2820  O   PRO A 344     5833   4353   5158    509   -260    179       O  
ATOM   2821  CB  PRO A 344      84.910 -16.449 -27.540  1.00 42.01           C  
ANISOU 2821  CB  PRO A 344     6111   4486   5366    250   -148    244       C  
ATOM   2822  CG  PRO A 344      85.205 -17.719 -28.299  1.00 41.77           C  
ANISOU 2822  CG  PRO A 344     6262   4445   5164    287    -74    321       C  
ATOM   2823  CD  PRO A 344      86.379 -17.364 -29.221  1.00 45.78           C  
ANISOU 2823  CD  PRO A 344     6655   4922   5816    337    -10    379       C  
ATOM   2824  N   LYS A 345      86.817 -15.737 -24.977  1.00 46.05           N  
ANISOU 2824  N   LYS A 345     6392   5092   6011    351   -352      8       N  
ATOM   2825  CA  LYS A 345      87.410 -16.188 -23.728  1.00 53.02           C  
ANISOU 2825  CA  LYS A 345     7296   6059   6791    397   -472    -59       C  
ATOM   2826  C   LYS A 345      86.359 -16.832 -22.829  1.00 61.54           C  
ANISOU 2826  C   LYS A 345     8583   7139   7659    359   -495   -108       C  
ATOM   2827  O   LYS A 345      85.194 -16.416 -22.812  1.00 52.85           O  
ANISOU 2827  O   LYS A 345     7530   5985   6565    260   -436   -152       O  
ATOM   2828  CB  LYS A 345      88.091 -15.036 -22.986  1.00 53.32           C  
ANISOU 2828  CB  LYS A 345     7134   6152   6974    323   -550   -178       C  
ATOM   2829  CG  LYS A 345      89.560 -14.869 -23.345  1.00 62.87           C  
ANISOU 2829  CG  LYS A 345     8144   7422   8323    392   -588   -139       C  
ATOM   2830  CD  LYS A 345      90.294 -13.984 -22.344  1.00 68.25           C  
ANISOU 2830  CD  LYS A 345     8651   8204   9076    293   -702   -273       C  
ATOM   2831  CE  LYS A 345      89.894 -12.531 -22.508  1.00 70.79           C  
ANISOU 2831  CE  LYS A 345     8876   8435   9585    139   -602   -386       C  
ATOM   2832  NZ  LYS A 345      90.550 -11.639 -21.505  1.00 75.78           N  
ANISOU 2832  NZ  LYS A 345     9370   9153  10268     -8   -683   -550       N  
ATOM   2833  N   LEU A 346      86.789 -17.860 -22.095  1.00 66.30           N  
ANISOU 2833  N   LEU A 346     9304   7800   8088    448   -571    -86       N  
ATOM   2834  CA  LEU A 346      86.031 -18.448 -20.999  1.00 75.78           C  
ANISOU 2834  CA  LEU A 346    10704   9013   9075    411   -609   -144       C  
ATOM   2835  C   LEU A 346      85.464 -17.350 -20.111  1.00 69.58           C  
ANISOU 2835  C   LEU A 346     9867   8235   8336    255   -633   -304       C  
ATOM   2836  O   LEU A 346      86.211 -16.583 -19.499  1.00 66.32           O  
ANISOU 2836  O   LEU A 346     9312   7893   7995    205   -723   -384       O  
ATOM   2837  CB  LEU A 346      86.941 -19.388 -20.202  1.00 82.73           C  
ANISOU 2837  CB  LEU A 346    11647   9979   9808    537   -723    -83       C  
ATOM   2838  CG  LEU A 346      86.694 -19.678 -18.716  1.00 90.91           C  
ANISOU 2838  CG  LEU A 346    12824  11083  10634    491   -833   -152       C  
ATOM   2839  CD1 LEU A 346      85.385 -20.421 -18.480  1.00 99.05           C  
ANISOU 2839  CD1 LEU A 346    14132  12024  11478    444   -728   -178       C  
ATOM   2840  CD2 LEU A 346      87.865 -20.461 -18.143  1.00 89.95           C  
ANISOU 2840  CD2 LEU A 346    12686  11072  10419    644   -973    -32       C  
ATOM   2841  N   GLN A 347      84.134 -17.263 -20.058  1.00 70.73           N  
ANISOU 2841  N   GLN A 347    10123   8303   8447    164   -536   -353       N  
ATOM   2842  CA  GLN A 347      83.441 -16.106 -19.486  1.00 78.45           C  
ANISOU 2842  CA  GLN A 347    11037   9235   9537     20   -482   -493       C  
ATOM   2843  C   GLN A 347      83.847 -15.774 -18.049  1.00 90.71           C  
ANISOU 2843  C   GLN A 347    12622  10851  10992    -70   -569   -641       C  
ATOM   2844  O   GLN A 347      83.695 -16.585 -17.139  1.00 99.93           O  
ANISOU 2844  O   GLN A 347    13980  12063  11926    -74   -626   -665       O  
ATOM   2845  CB  GLN A 347      81.924 -16.324 -19.547  1.00 77.51           C  
ANISOU 2845  CB  GLN A 347    11040   9033   9378    -43   -362   -502       C  
ATOM   2846  CG  GLN A 347      81.324 -16.159 -20.940  1.00 66.37           C  
ANISOU 2846  CG  GLN A 347     9538   7573   8108    -27   -276   -376       C  
ATOM   2847  CD  GLN A 347      79.974 -16.849 -21.081  1.00 56.91           C  
ANISOU 2847  CD  GLN A 347     8476   6348   6798    -76   -200   -346       C  
ATOM   2848  OE1 GLN A 347      79.798 -17.702 -21.940  1.00 43.22           O  
ANISOU 2848  OE1 GLN A 347     6822   4635   4963    -48   -189   -237       O  
ATOM   2849  NE2 GLN A 347      79.020 -16.488 -20.223  1.00 63.98           N  
ANISOU 2849  NE2 GLN A 347     9404   7195   7711   -167   -128   -453       N  
TER    2850      GLN A 347                                                      
ATOM   2851  N  AASN B   0      94.774 -18.402   1.771  0.59 63.60           N  
ANISOU 2851  N  AASN B   0     9570   6847   7746  -2096    256    567       N  
ATOM   2852  N  BASN B   0      86.248 -21.188  -2.093  0.41 41.17           N  
ANISOU 2852  N  BASN B   0     7006   4256   4380   -195   -942   1234       N  
ATOM   2853  CA AASN B   0      94.874 -19.835   1.517  0.59 58.54           C  
ANISOU 2853  CA AASN B   0     8578   6612   7052  -1970    358    429       C  
ATOM   2854  CA BASN B   0      87.418 -20.512  -1.581  0.41 56.81           C  
ANISOU 2854  CA BASN B   0     9092   6066   6425   -440   -782   1238       C  
ATOM   2855  C  AASN B   0      93.813 -20.617   2.295  0.59 62.70           C  
ANISOU 2855  C  AASN B   0     8954   7155   7714  -1503    197    353       C  
ATOM   2856  C  BASN B   0      87.885 -21.114  -0.273  0.41 50.76           C  
ANISOU 2856  C  BASN B   0     7993   5402   5891   -382   -608    960       C  
ATOM   2857  O  AASN B   0      94.133 -21.427   3.167  0.59 58.65           O  
ANISOU 2857  O  AASN B   0     8130   6823   7329  -1365    221    150       O  
ATOM   2858  O  BASN B   0      87.269 -22.054   0.250  0.41 48.64           O  
ANISOU 2858  O  BASN B   0     7447   5310   5726   -160   -606    791       O  
ATOM   2859  CB AASN B   0      96.265 -20.335   1.864  0.59 57.98           C  
ANISOU 2859  CB AASN B   0     8137   6845   7046  -2186    555    173       C  
ATOM   2860  CB BASN B   0      87.137 -19.020  -1.395  0.41 59.33           C  
ANISOU 2860  CB BASN B   0     9762   5932   6848   -368   -993   1421       C  
ATOM   2861  N  AMET B   1      92.547 -20.369   1.969  0.59 60.71           N  
ANISOU 2861  N  AMET B   1     8925   6718   7424  -1273     25    522       N  
ATOM   2862  N  BMET B   1      88.964 -20.557   0.265  0.41 58.34           N  
ANISOU 2862  N  BMET B   1     8995   6249   6921   -601   -477    922       N  
ATOM   2863  CA AMET B   1      91.421 -21.029   2.618  0.59 60.61           C  
ANISOU 2863  CA AMET B   1     8776   6730   7521   -874   -107    450       C  
ATOM   2864  CA BMET B   1      89.633 -21.036   1.490  0.41 62.60           C  
ANISOU 2864  CA BMET B   1     9249   6895   7642   -595   -333    678       C  
ATOM   2865  C  AMET B   1      91.082 -22.313   1.866  0.59 54.42           C  
ANISOU 2865  C  AMET B   1     7823   6235   6620   -793    -56    433       C  
ATOM   2866  C  BMET B   1      90.205 -22.431   1.195  0.41 52.27           C  
ANISOU 2866  C  BMET B   1     7648   5957   6254   -680   -151    540       C  
ATOM   2867  O  AMET B   1      90.907 -22.288   0.644  0.59 54.17           O  
ANISOU 2867  O  AMET B   1     7941   6250   6389   -907    -51    577       O  
ATOM   2868  O  BMET B   1      90.801 -22.638   0.124  0.41 57.31           O  
ANISOU 2868  O  BMET B   1     8328   6748   6697   -926    -30    595       O  
ATOM   2869  CB AMET B   1      90.214 -20.090   2.650  0.59 69.17           C  
ANISOU 2869  CB AMET B   1    10132   7492   8660   -653   -327    587       C  
ATOM   2870  CB BMET B   1      88.698 -20.949   2.681  0.41 69.19           C  
ANISOU 2870  CB BMET B   1     9986   7614   8689   -259   -461    555       C  
ATOM   2871  CG AMET B   1      89.008 -20.607   3.420  0.59 70.54           C  
ANISOU 2871  CG AMET B   1    10139   7701   8961   -270   -442    473       C  
ATOM   2872  CG BMET B   1      89.057 -19.860   3.677  0.41 73.22           C  
ANISOU 2872  CG BMET B   1    10607   7851   9361   -283   -489    488       C  
ATOM   2873  SD AMET B   1      89.300 -20.789   5.196  0.59 75.74           S  
ANISOU 2873  SD AMET B   1    10571   8400   9804   -174   -389    211       S  
ATOM   2874  SD BMET B   1      88.932 -20.385   5.400  0.41 70.58           S  
ANISOU 2874  SD BMET B   1     9982   7634   9199    -92   -449    207       S  
ATOM   2875  CE AMET B   1      89.956 -19.170   5.601  0.59 76.84           C  
ANISOU 2875  CE AMET B   1    10978   8180  10038   -353   -425    216       C  
ATOM   2876  CE BMET B   1      89.845 -21.922   5.321  0.41 71.36           C  
ANISOU 2876  CE BMET B   1     9781   8122   9211   -228   -274    128       C  
ATOM   2877  N  ASER B   2      90.989 -23.429   2.589  0.59 47.33           N  
ANISOU 2877  N  ASER B   2     6640   5516   5827   -614    -28    260       N  
ATOM   2878  N  BSER B   2      90.079 -23.394   2.114  0.41 46.42           N  
ANISOU 2878  N  BSER B   2     6627   5355   5654   -496   -123    355       N  
ATOM   2879  CA ASER B   2      90.810 -24.714   1.924  0.59 42.28           C  
ANISOU 2879  CA ASER B   2     5835   5121   5108   -566     37    203       C  
ATOM   2880  CA BSER B   2      90.791 -24.660   1.955  0.41 42.93           C  
ANISOU 2880  CA BSER B   2     5926   5192   5194   -564     31    208       C  
ATOM   2881  C  ASER B   2      90.398 -25.778   2.925  0.59 36.53           C  
ANISOU 2881  C  ASER B   2     4882   4473   4527   -332      8     63       C  
ATOM   2882  C  BSER B   2      90.348 -25.751   2.920  0.41 37.42           C  
ANISOU 2882  C  BSER B   2     5002   4579   4638   -326      3     68       C  
ATOM   2883  O  ASER B   2      90.555 -25.622   4.138  0.59 37.95           O  
ANISOU 2883  O  ASER B   2     4998   4586   4834   -254    -26     -7       O  
ATOM   2884  O  BSER B   2      90.440 -25.581   4.136  0.41 39.14           O  
ANISOU 2884  O  BSER B   2     5162   4725   4984   -240    -36      1       O  
ATOM   2885  CB ASER B   2      92.090 -25.156   1.234  0.59 47.03           C  
ANISOU 2885  CB ASER B   2     6309   5934   5624   -827    233    111       C  
ATOM   2886  CB BSER B   2      92.297 -24.428   2.113  0.41 45.37           C  
ANISOU 2886  CB BSER B   2     6141   5571   5527   -823    183    114       C  
ATOM   2887  OG ASER B   2      93.037 -25.578   2.200  0.59 40.74           O  
ANISOU 2887  OG ASER B   2     5267   5218   4996   -822    295    -70       O  
ATOM   2888  OG BSER B   2      92.997 -25.653   2.286  0.41 40.27           O  
ANISOU 2888  OG BSER B   2     5193   5160   4950   -798    288    -78       O  
ATOM   2889  N   LEU B   3      89.909 -26.893   2.381  1.00 34.43           N  
ANISOU 2889  N   LEU B   3     4512   4353   4216   -253     27     20       N  
ATOM   2890  CA  LEU B   3      89.536 -28.032   3.214  1.00 35.40           C  
ANISOU 2890  CA  LEU B   3     4458   4533   4460    -81     13    -90       C  
ATOM   2891  C   LEU B   3      90.714 -28.518   4.048  1.00 33.63           C  
ANISOU 2891  C   LEU B   3     4068   4355   4352   -107     71   -209       C  
ATOM   2892  O   LEU B   3      90.575 -28.776   5.249  1.00 33.22           O  
ANISOU 2892  O   LEU B   3     3966   4260   4395     10      9   -238       O  
ATOM   2893  CB  LEU B   3      89.011 -29.165   2.327  1.00 33.81           C  
ANISOU 2893  CB  LEU B   3     4187   4464   4196    -54     42   -139       C  
ATOM   2894  CG  LEU B   3      88.837 -30.526   2.997  1.00 40.74           C  
ANISOU 2894  CG  LEU B   3     4908   5374   5198     62     52   -251       C  
ATOM   2895  CD1 LEU B   3      87.767 -30.430   4.067  1.00 41.68           C  
ANISOU 2895  CD1 LEU B   3     5045   5412   5377    199    -38   -210       C  
ATOM   2896  CD2 LEU B   3      88.471 -31.576   1.944  1.00 41.96           C  
ANISOU 2896  CD2 LEU B   3     5012   5638   5293     40     97   -333       C  
ATOM   2897  N   GLU B   4      91.887 -28.644   3.421  1.00 32.54           N  
ANISOU 2897  N   GLU B   4     3837   4329   4196   -264    184   -289       N  
ATOM   2898  CA  GLU B   4      93.063 -29.137   4.129  1.00 40.40           C  
ANISOU 2898  CA  GLU B   4     4625   5397   5328   -259    207   -432       C  
ATOM   2899  C   GLU B   4      93.520 -28.162   5.209  1.00 36.33           C  
ANISOU 2899  C   GLU B   4     4139   4799   4868   -300    140   -415       C  
ATOM   2900  O   GLU B   4      94.052 -28.591   6.239  1.00 35.93           O  
ANISOU 2900  O   GLU B   4     3953   4773   4924   -211     67   -494       O  
ATOM   2901  CB  GLU B   4      94.192 -29.421   3.125  1.00 38.46           C  
ANISOU 2901  CB  GLU B   4     4222   5332   5059   -426    366   -574       C  
ATOM   2902  CG  GLU B   4      93.957 -30.681   2.238  1.00 41.70           C  
ANISOU 2902  CG  GLU B   4     4542   5846   5455   -356    435   -685       C  
ATOM   2903  CD  GLU B   4      92.916 -30.503   1.104  1.00 54.69           C  
ANISOU 2903  CD  GLU B   4     6384   7504   6893   -426    461   -575       C  
ATOM   2904  OE1 GLU B   4      92.256 -29.437   1.006  1.00 45.00           O  
ANISOU 2904  OE1 GLU B   4     5374   6177   5546   -483    395   -386       O  
ATOM   2905  OE2 GLU B   4      92.770 -31.446   0.293  1.00 54.83           O  
ANISOU 2905  OE2 GLU B   4     6334   7627   6871   -414    530   -694       O  
ATOM   2906  N   ASN B   5      93.322 -26.853   4.995  1.00 34.06           N  
ANISOU 2906  N   ASN B   5     4044   4395   4504   -433    142   -314       N  
ATOM   2907  CA  ASN B   5      93.673 -25.868   6.015  1.00 33.28           C  
ANISOU 2907  CA  ASN B   5     3998   4186   4462   -483     79   -328       C  
ATOM   2908  C   ASN B   5      92.693 -25.892   7.178  1.00 35.92           C  
ANISOU 2908  C   ASN B   5     4396   4420   4833   -270    -46   -309       C  
ATOM   2909  O   ASN B   5      93.097 -25.738   8.336  1.00 34.54           O  
ANISOU 2909  O   ASN B   5     4168   4249   4708   -251   -110   -388       O  
ATOM   2910  CB  ASN B   5      93.740 -24.469   5.396  1.00 35.28           C  
ANISOU 2910  CB  ASN B   5     4478   4286   4642   -698    114   -227       C  
ATOM   2911  CG  ASN B   5      94.047 -23.381   6.426  1.00 40.45           C  
ANISOU 2911  CG  ASN B   5     5214   4783   5373   -765     48   -271       C  
ATOM   2912  OD1 ASN B   5      93.174 -22.578   6.771  1.00 38.23           O  
ANISOU 2912  OD1 ASN B   5     5141   4281   5104   -670    -43   -205       O  
ATOM   2913  ND2 ASN B   5      95.295 -23.344   6.914  1.00 40.43           N  
ANISOU 2913  ND2 ASN B   5     5028   4901   5432   -923     86   -415       N  
ATOM   2914  N   VAL B   6      91.396 -26.047   6.896  1.00 34.16           N  
ANISOU 2914  N   VAL B   6     4276   4134   4568   -128    -79   -226       N  
ATOM   2915  CA  VAL B   6      90.432 -26.208   7.983  1.00 34.02           C  
ANISOU 2915  CA  VAL B   6     4272   4082   4572     50   -153   -246       C  
ATOM   2916  C   VAL B   6      90.809 -27.404   8.848  1.00 33.42           C  
ANISOU 2916  C   VAL B   6     4045   4131   4520    112   -170   -305       C  
ATOM   2917  O   VAL B   6      90.814 -27.325  10.086  1.00 32.37           O  
ANISOU 2917  O   VAL B   6     3915   4006   4380    151   -227   -350       O  
ATOM   2918  CB  VAL B   6      89.004 -26.345   7.420  1.00 32.74           C  
ANISOU 2918  CB  VAL B   6     4172   3892   4377    181   -175   -182       C  
ATOM   2919  CG1 VAL B   6      88.047 -26.698   8.541  1.00 34.84           C  
ANISOU 2919  CG1 VAL B   6     4394   4187   4655    322   -202   -242       C  
ATOM   2920  CG2 VAL B   6      88.580 -25.040   6.761  1.00 35.16           C  
ANISOU 2920  CG2 VAL B   6     4663   4026   4670    171   -227   -104       C  
ATOM   2921  N   ALA B   7      91.169 -28.522   8.209  1.00 33.48           N  
ANISOU 2921  N   ALA B   7     3941   4230   4551    120   -134   -310       N  
ATOM   2922  CA  ALA B   7      91.545 -29.714   8.960  1.00 37.72           C  
ANISOU 2922  CA  ALA B   7     4372   4825   5136    203   -188   -341       C  
ATOM   2923  C   ALA B   7      92.830 -29.500   9.751  1.00 32.51           C  
ANISOU 2923  C   ALA B   7     3614   4216   4524    166   -262   -414       C  
ATOM   2924  O   ALA B   7      92.957 -29.996  10.878  1.00 33.41           O  
ANISOU 2924  O   ALA B   7     3719   4346   4628    242   -373   -405       O  
ATOM   2925  CB  ALA B   7      91.691 -30.897   8.011  1.00 35.95           C  
ANISOU 2925  CB  ALA B   7     4053   4642   4963    235   -139   -368       C  
ATOM   2926  N   PHE B   8      93.800 -28.777   9.180  1.00 34.21           N  
ANISOU 2926  N   PHE B   8     3753   4474   4773     27   -208   -485       N  
ATOM   2927  CA  PHE B   8      95.006 -28.450   9.937  1.00 37.07           C  
ANISOU 2927  CA  PHE B   8     3985   4913   5188    -35   -286   -587       C  
ATOM   2928  C   PHE B   8      94.660 -27.718  11.229  1.00 39.75           C  
ANISOU 2928  C   PHE B   8     4449   5199   5454    -32   -384   -578       C  
ATOM   2929  O   PHE B   8      95.203 -28.029  12.298  1.00 36.53           O  
ANISOU 2929  O   PHE B   8     3971   4868   5040     16   -522   -621       O  
ATOM   2930  CB  PHE B   8      95.960 -27.608   9.086  1.00 33.56           C  
ANISOU 2930  CB  PHE B   8     3454   4525   4771   -258   -172   -673       C  
ATOM   2931  CG  PHE B   8      97.187 -27.145   9.835  1.00 32.01           C  
ANISOU 2931  CG  PHE B   8     3092   4431   4637   -363   -246   -813       C  
ATOM   2932  CD1 PHE B   8      97.193 -25.945  10.525  1.00 38.21           C  
ANISOU 2932  CD1 PHE B   8     4002   5134   5380   -495   -284   -830       C  
ATOM   2933  CD2 PHE B   8      98.338 -27.920   9.850  1.00 39.95           C  
ANISOU 2933  CD2 PHE B   8     3798   5619   5763   -320   -294   -958       C  
ATOM   2934  CE1 PHE B   8      98.326 -25.523  11.221  1.00 39.86           C  
ANISOU 2934  CE1 PHE B   8     4044   5460   5642   -618   -364   -984       C  
ATOM   2935  CE2 PHE B   8      99.468 -27.507  10.543  1.00 42.00           C  
ANISOU 2935  CE2 PHE B   8     3860   6010   6087   -413   -389  -1110       C  
ATOM   2936  CZ  PHE B   8      99.464 -26.310  11.227  1.00 47.69           C  
ANISOU 2936  CZ  PHE B   8     4711   6668   6742   -580   -423  -1121       C  
ATOM   2937  N   ASN B   9      93.763 -26.736  11.151  1.00 35.53           N  
ANISOU 2937  N   ASN B   9     4102   4538   4861    -74   -329   -537       N  
ATOM   2938  CA  ASN B   9      93.382 -25.996  12.349  1.00 37.29           C  
ANISOU 2938  CA  ASN B   9     4437   4714   5020    -67   -395   -585       C  
ATOM   2939  C   ASN B   9      92.663 -26.887  13.358  1.00 33.09           C  
ANISOU 2939  C   ASN B   9     3933   4248   4392     73   -459   -546       C  
ATOM   2940  O   ASN B   9      92.913 -26.787  14.565  1.00 39.59           O  
ANISOU 2940  O   ASN B   9     4772   5141   5129     63   -553   -603       O  
ATOM   2941  CB  ASN B   9      92.506 -24.796  11.973  1.00 34.37           C  
ANISOU 2941  CB  ASN B   9     4251   4159   4650    -92   -333   -575       C  
ATOM   2942  CG  ASN B   9      93.331 -23.585  11.554  1.00 35.46           C  
ANISOU 2942  CG  ASN B   9     4443   4184   4845   -295   -307   -625       C  
ATOM   2943  OD1 ASN B   9      93.544 -22.665  12.336  1.00 37.50           O  
ANISOU 2943  OD1 ASN B   9     4773   4364   5110   -371   -349   -735       O  
ATOM   2944  ND2 ASN B   9      93.807 -23.593  10.320  1.00 39.29           N  
ANISOU 2944  ND2 ASN B   9     4905   4667   5357   -416   -226   -556       N  
ATOM   2945  N   VAL B  10      91.753 -27.744  12.895  1.00 33.62           N  
ANISOU 2945  N   VAL B  10     4021   4303   4450    171   -407   -450       N  
ATOM   2946  CA  VAL B  10      91.049 -28.628  13.824  1.00 33.20           C  
ANISOU 2946  CA  VAL B  10     4016   4306   4290    244   -441   -397       C  
ATOM   2947  C   VAL B  10      92.050 -29.502  14.578  1.00 38.91           C  
ANISOU 2947  C   VAL B  10     4684   5108   4992    264   -591   -364       C  
ATOM   2948  O   VAL B  10      92.005 -29.615  15.809  1.00 38.83           O  
ANISOU 2948  O   VAL B  10     4752   5167   4835    254   -679   -351       O  
ATOM   2949  CB  VAL B  10      90.002 -29.472  13.078  1.00 35.20           C  
ANISOU 2949  CB  VAL B  10     4280   4532   4563    303   -357   -315       C  
ATOM   2950  CG1 VAL B  10      89.502 -30.603  13.973  1.00 42.43           C  
ANISOU 2950  CG1 VAL B  10     5253   5493   5375    320   -387   -235       C  
ATOM   2951  CG2 VAL B  10      88.809 -28.572  12.612  1.00 35.05           C  
ANISOU 2951  CG2 VAL B  10     4310   4463   4542    324   -263   -356       C  
ATOM   2952  N   VAL B  11      93.001 -30.087  13.852  1.00 39.31           N  
ANISOU 2952  N   VAL B  11     4595   5161   5181    299   -633   -366       N  
ATOM   2953  CA  VAL B  11      93.954 -31.016  14.459  1.00 38.52           C  
ANISOU 2953  CA  VAL B  11     4415   5110   5112    382   -818   -342       C  
ATOM   2954  C   VAL B  11      94.901 -30.300  15.416  1.00 41.45           C  
ANISOU 2954  C   VAL B  11     4729   5592   5428    327   -963   -432       C  
ATOM   2955  O   VAL B  11      95.270 -30.843  16.465  1.00 53.74           O  
ANISOU 2955  O   VAL B  11     6318   7206   6894    387  -1161   -377       O  
ATOM   2956  CB  VAL B  11      94.718 -31.760  13.347  1.00 43.25           C  
ANISOU 2956  CB  VAL B  11     4829   5693   5912    456   -807   -390       C  
ATOM   2957  CG1 VAL B  11      95.907 -32.503  13.912  1.00 51.83           C  
ANISOU 2957  CG1 VAL B  11     5772   6829   7091    582  -1032   -420       C  
ATOM   2958  CG2 VAL B  11      93.767 -32.704  12.635  1.00 45.24           C  
ANISOU 2958  CG2 VAL B  11     5162   5836   6191    514   -710   -307       C  
ATOM   2959  N   ASN B  12      95.315 -29.080  15.082  1.00 40.54           N  
ANISOU 2959  N   ASN B  12     4547   5501   5354    196   -885   -565       N  
ATOM   2960  CA  ASN B  12      96.351 -28.395  15.848  1.00 39.88           C  
ANISOU 2960  CA  ASN B  12     4367   5534   5251    109  -1019   -695       C  
ATOM   2961  C   ASN B  12      95.821 -27.425  16.893  1.00 48.24           C  
ANISOU 2961  C   ASN B  12     5600   6599   6130     13  -1026   -751       C  
ATOM   2962  O   ASN B  12      96.503 -27.192  17.898  1.00 46.59           O  
ANISOU 2962  O   ASN B  12     5356   6516   5830    -32  -1194   -835       O  
ATOM   2963  CB  ASN B  12      97.285 -27.637  14.902  1.00 44.42           C  
ANISOU 2963  CB  ASN B  12     4757   6136   5986    -36   -925   -837       C  
ATOM   2964  CG  ASN B  12      98.216 -28.565  14.157  1.00 55.12           C  
ANISOU 2964  CG  ASN B  12     5852   7578   7513     48   -954   -880       C  
ATOM   2965  OD1 ASN B  12      99.272 -28.923  14.666  1.00 58.83           O  
ANISOU 2965  OD1 ASN B  12     6111   8190   8051    105  -1139   -975       O  
ATOM   2966  ND2 ASN B  12      97.815 -28.986  12.957  1.00 45.16           N  
ANISOU 2966  ND2 ASN B  12     4589   6246   6323     74   -786   -834       N  
ATOM   2967  N   LYS B  13      94.632 -26.852  16.690  1.00 42.09           N  
ANISOU 2967  N   LYS B  13     4989   5702   5302     -8   -860   -736       N  
ATOM   2968  CA  LYS B  13      94.098 -25.824  17.577  1.00 42.34           C  
ANISOU 2968  CA  LYS B  13     5164   5723   5202    -83   -834   -855       C  
ATOM   2969  C   LYS B  13      92.736 -26.171  18.166  1.00 40.79           C  
ANISOU 2969  C   LYS B  13     5119   5540   4841    -11   -758   -801       C  
ATOM   2970  O   LYS B  13      92.211 -25.387  18.967  1.00 41.16           O  
ANISOU 2970  O   LYS B  13     5266   5606   4766    -57   -716   -941       O  
ATOM   2971  CB  LYS B  13      93.991 -24.480  16.837  1.00 45.36           C  
ANISOU 2971  CB  LYS B  13     5591   5930   5715   -183   -709   -961       C  
ATOM   2972  CG  LYS B  13      95.265 -24.051  16.103  1.00 54.12           C  
ANISOU 2972  CG  LYS B  13     6559   7028   6976   -330   -722  -1016       C  
ATOM   2973  CD  LYS B  13      96.439 -23.866  17.043  1.00 58.36           C  
ANISOU 2973  CD  LYS B  13     6972   7730   7473   -438   -884  -1162       C  
ATOM   2974  CE  LYS B  13      96.367 -22.550  17.796  1.00 64.27           C  
ANISOU 2974  CE  LYS B  13     7852   8401   8167   -583   -885  -1352       C  
ATOM   2975  NZ  LYS B  13      97.624 -22.291  18.572  1.00 67.62           N  
ANISOU 2975  NZ  LYS B  13     8125   9005   8562   -734  -1051  -1525       N  
ATOM   2976  N   GLY B  14      92.135 -27.299  17.779  1.00 37.54           N  
ANISOU 2976  N   GLY B  14     4714   5122   4427     82   -720   -636       N  
ATOM   2977  CA  GLY B  14      90.847 -27.708  18.299  1.00 41.58           C  
ANISOU 2977  CA  GLY B  14     5338   5676   4783    102   -622   -593       C  
ATOM   2978  C   GLY B  14      89.653 -27.119  17.575  1.00 46.86           C  
ANISOU 2978  C   GLY B  14     6013   6248   5544    146   -443   -657       C  
ATOM   2979  O   GLY B  14      88.511 -27.499  17.876  1.00 38.82           O  
ANISOU 2979  O   GLY B  14     5030   5293   4427    158   -338   -651       O  
ATOM   2980  N   HIS B  15      89.883 -26.215  16.627  1.00 40.52           N  
ANISOU 2980  N   HIS B  15     5174   5300   4920    161   -417   -714       N  
ATOM   2981  CA  HIS B  15      88.835 -25.489  15.907  1.00 39.32           C  
ANISOU 2981  CA  HIS B  15     5046   5024   4871    236   -311   -768       C  
ATOM   2982  C   HIS B  15      89.525 -24.577  14.900  1.00 39.18           C  
ANISOU 2982  C   HIS B  15     5044   4827   5015    200   -336   -766       C  
ATOM   2983  O   HIS B  15      90.757 -24.542  14.852  1.00 37.53           O  
ANISOU 2983  O   HIS B  15     4796   4633   4832     93   -398   -758       O  
ATOM   2984  CB  HIS B  15      87.958 -24.669  16.855  1.00 38.07           C  
ANISOU 2984  CB  HIS B  15     4940   4890   4633    265   -248   -966       C  
ATOM   2985  CG  HIS B  15      88.640 -23.451  17.402  1.00 42.09           C  
ANISOU 2985  CG  HIS B  15     5519   5312   5160    199   -300  -1140       C  
ATOM   2986  ND1 HIS B  15      88.111 -22.181  17.286  1.00 43.10           N  
ANISOU 2986  ND1 HIS B  15     5712   5253   5409    266   -268  -1311       N  
ATOM   2987  CD2 HIS B  15      89.815 -23.308  18.062  1.00 40.08           C  
ANISOU 2987  CD2 HIS B  15     5276   5120   4833     70   -399  -1184       C  
ATOM   2988  CE1 HIS B  15      88.932 -21.310  17.850  1.00 46.70           C  
ANISOU 2988  CE1 HIS B  15     6238   5639   5865    156   -325  -1456       C  
ATOM   2989  NE2 HIS B  15      89.973 -21.969  18.330  1.00 43.20           N  
ANISOU 2989  NE2 HIS B  15     5748   5369   5296     26   -403  -1388       N  
ATOM   2990  N   PHE B  16      88.774 -23.832  14.099  1.00 37.05           N  
ANISOU 2990  N   PHE B  16     4832   4395   4849    273   -298   -772       N  
ATOM   2991  CA  PHE B  16      89.406 -22.941  13.134  1.00 37.40           C  
ANISOU 2991  CA  PHE B  16     4955   4246   5009    195   -321   -729       C  
ATOM   2992  C   PHE B  16      89.935 -21.713  13.861  1.00 40.41           C  
ANISOU 2992  C   PHE B  16     5435   4497   5422    101   -357   -888       C  
ATOM   2993  O   PHE B  16      89.185 -21.004  14.540  1.00 41.09           O  
ANISOU 2993  O   PHE B  16     5591   4500   5520    194   -355  -1044       O  
ATOM   2994  CB  PHE B  16      88.460 -22.526  12.006  1.00 36.09           C  
ANISOU 2994  CB  PHE B  16     4868   3921   4924    307   -320   -644       C  
ATOM   2995  CG  PHE B  16      89.169 -21.780  10.902  1.00 37.91           C  
ANISOU 2995  CG  PHE B  16     5223   3966   5215    175   -340   -534       C  
ATOM   2996  CD1 PHE B  16      89.937 -22.472   9.969  1.00 42.35           C  
ANISOU 2996  CD1 PHE B  16     5720   4634   5738     46   -297   -408       C  
ATOM   2997  CD2 PHE B  16      89.138 -20.396  10.843  1.00 44.37           C  
ANISOU 2997  CD2 PHE B  16     6234   4501   6122    151   -392   -571       C  
ATOM   2998  CE1 PHE B  16      90.622 -21.788   8.973  1.00 45.40           C  
ANISOU 2998  CE1 PHE B  16     6227   4891   6133   -137   -280   -312       C  
ATOM   2999  CE2 PHE B  16      89.818 -19.710   9.847  1.00 46.19           C  
ANISOU 2999  CE2 PHE B  16     6625   4549   6377    -31   -400   -438       C  
ATOM   3000  CZ  PHE B  16      90.555 -20.407   8.909  1.00 42.04           C  
ANISOU 3000  CZ  PHE B  16     6028   4177   5771   -194   -331   -305       C  
ATOM   3001  N   ASP B  17      91.233 -21.458  13.704  1.00 37.97           N  
ANISOU 3001  N   ASP B  17     5113   4178   5138    -94   -381   -884       N  
ATOM   3002  CA  ASP B  17      91.915 -20.370  14.396  1.00 43.52           C  
ANISOU 3002  CA  ASP B  17     5891   4774   5870   -242   -418  -1053       C  
ATOM   3003  C   ASP B  17      92.731 -19.526  13.421  1.00 50.63           C  
ANISOU 3003  C   ASP B  17     6885   5473   6878   -455   -401   -992       C  
ATOM   3004  O   ASP B  17      93.604 -18.762  13.844  1.00 45.67           O  
ANISOU 3004  O   ASP B  17     6284   4783   6284   -659   -422  -1123       O  
ATOM   3005  CB  ASP B  17      92.791 -20.946  15.518  1.00 53.98           C  
ANISOU 3005  CB  ASP B  17     7072   6359   7081   -324   -482  -1156       C  
ATOM   3006  CG  ASP B  17      93.362 -19.884  16.442  1.00 66.37           C  
ANISOU 3006  CG  ASP B  17     8704   7868   8646   -474   -535  -1383       C  
ATOM   3007  OD1 ASP B  17      92.580 -19.105  17.032  1.00 63.59           O  
ANISOU 3007  OD1 ASP B  17     8489   7380   8293   -403   -518  -1539       O  
ATOM   3008  OD2 ASP B  17      94.603 -19.842  16.588  1.00 64.43           O  
ANISOU 3008  OD2 ASP B  17     8348   7725   8406   -664   -594  -1438       O  
ATOM   3009  N   GLY B  18      92.460 -19.646  12.122  1.00 47.43           N  
ANISOU 3009  N   GLY B  18     6538   4979   6503   -444   -358   -800       N  
ATOM   3010  CA  GLY B  18      93.161 -18.843  11.137  1.00 47.25           C  
ANISOU 3010  CA  GLY B  18     6651   4771   6532   -689   -320   -709       C  
ATOM   3011  C   GLY B  18      94.647 -19.115  11.005  1.00 49.10           C  
ANISOU 3011  C   GLY B  18     6702   5203   6750   -971   -260   -754       C  
ATOM   3012  O   GLY B  18      95.377 -18.256  10.507  1.00 47.90           O  
ANISOU 3012  O   GLY B  18     6656   4910   6635  -1258   -209   -744       O  
ATOM   3013  N   GLN B  19      95.121 -20.291  11.422  1.00 42.03           N  
ANISOU 3013  N   GLN B  19     5533   4626   5811   -903   -269   -808       N  
ATOM   3014  CA  GLN B  19      96.541 -20.608  11.320  1.00 39.50           C  
ANISOU 3014  CA  GLN B  19     4971   4526   5510  -1120   -235   -896       C  
ATOM   3015  C   GLN B  19      96.855 -21.159   9.936  1.00 42.55           C  
ANISOU 3015  C   GLN B  19     5277   5010   5880  -1206   -106   -778       C  
ATOM   3016  O   GLN B  19      96.013 -21.789   9.294  1.00 43.84           O  
ANISOU 3016  O   GLN B  19     5496   5166   5996  -1028    -83   -641       O  
ATOM   3017  CB  GLN B  19      96.948 -21.629  12.384  1.00 42.62           C  
ANISOU 3017  CB  GLN B  19     5116   5195   5882   -971   -350  -1007       C  
ATOM   3018  CG  GLN B  19      96.716 -21.160  13.808  1.00 53.50           C  
ANISOU 3018  CG  GLN B  19     6567   6548   7213   -920   -472  -1142       C  
ATOM   3019  CD  GLN B  19      97.517 -19.914  14.150  1.00 67.10           C  
ANISOU 3019  CD  GLN B  19     8331   8175   8989  -1204   -481  -1314       C  
ATOM   3020  OE1 GLN B  19      98.701 -19.812  13.831  1.00 74.55           O  
ANISOU 3020  OE1 GLN B  19     9091   9243   9992  -1438   -456  -1393       O  
ATOM   3021  NE2 GLN B  19      96.866 -18.954  14.793  1.00 64.53           N  
ANISOU 3021  NE2 GLN B  19     8234   7631   8656  -1194   -508  -1403       N  
ATOM   3022  N   GLN B  20      98.082 -20.932   9.474  1.00 44.00           N  
ANISOU 3022  N   GLN B  20     5310   5316   6092  -1502    -10   -862       N  
ATOM   3023  CA  GLN B  20      98.468 -21.489   8.185  1.00 50.61           C  
ANISOU 3023  CA  GLN B  20     6038   6304   6887  -1612    146   -804       C  
ATOM   3024  C   GLN B  20      98.918 -22.937   8.343  1.00 44.62           C  
ANISOU 3024  C   GLN B  20     4927   5849   6177  -1409    118   -915       C  
ATOM   3025  O   GLN B  20      99.474 -23.333   9.370  1.00 49.15           O  
ANISOU 3025  O   GLN B  20     5286   6562   6827  -1309    -12  -1059       O  
ATOM   3026  CB  GLN B  20      99.572 -20.653   7.533  1.00 57.47           C  
ANISOU 3026  CB  GLN B  20     6880   7207   7751  -2054    305   -866       C  
ATOM   3027  CG  GLN B  20      99.068 -19.327   6.979  1.00 71.81           C  
ANISOU 3027  CG  GLN B  20     9123   8662   9501  -2274    347   -682       C  
ATOM   3028  CD  GLN B  20      99.791 -18.909   5.715  1.00 89.75           C  
ANISOU 3028  CD  GLN B  20    11448  10987  11665  -2701    565   -616       C  
ATOM   3029  OE1 GLN B  20      99.185 -18.797   4.646  1.00 99.86           O  
ANISOU 3029  OE1 GLN B  20    12988  12154  12800  -2738    625   -392       O  
ATOM   3030  NE2 GLN B  20     101.095 -18.678   5.828  1.00 90.00           N  
ANISOU 3030  NE2 GLN B  20    11226  11221  11747  -3046    685   -818       N  
ATOM   3031  N   GLY B  21      98.657 -23.732   7.311  1.00 44.84           N  
ANISOU 3031  N   GLY B  21     4917   5963   6156  -1340    220   -848       N  
ATOM   3032  CA  GLY B  21      99.056 -25.127   7.337  1.00 44.78           C  
ANISOU 3032  CA  GLY B  21     4604   6184   6226  -1134    196   -964       C  
ATOM   3033  C   GLY B  21      98.057 -26.022   6.638  1.00 46.77           C  
ANISOU 3033  C   GLY B  21     4955   6399   6418   -929    222   -844       C  
ATOM   3034  O   GLY B  21      96.929 -25.605   6.347  1.00 42.31           O  
ANISOU 3034  O   GLY B  21     4675   5647   5752   -892    215   -666       O  
ATOM   3035  N   GLU B  22      98.459 -27.261   6.363  1.00 43.96           N  
ANISOU 3035  N   GLU B  22     4351   6212   6141   -784    238   -963       N  
ATOM   3036  CA  GLU B  22      97.610 -28.215   5.668  1.00 39.40           C  
ANISOU 3036  CA  GLU B  22     3841   5610   5521   -616    270   -896       C  
ATOM   3037  C   GLU B  22      97.881 -29.615   6.204  1.00 43.33           C  
ANISOU 3037  C   GLU B  22     4121   6166   6175   -340    153  -1008       C  
ATOM   3038  O   GLU B  22      99.012 -29.936   6.568  1.00 42.25           O  
ANISOU 3038  O   GLU B  22     3703   6170   6180   -309    106  -1189       O  
ATOM   3039  CB  GLU B  22      97.863 -28.185   4.154  1.00 48.65           C  
ANISOU 3039  CB  GLU B  22     4992   6911   6582   -826    492   -943       C  
ATOM   3040  CG  GLU B  22      97.288 -26.987   3.425  1.00 65.42           C  
ANISOU 3040  CG  GLU B  22     7434   8917   8508  -1065    572   -749       C  
ATOM   3041  CD  GLU B  22      98.352 -26.167   2.710  1.00 83.73           C  
ANISOU 3041  CD  GLU B  22     9702  11369  10742  -1452    767   -820       C  
ATOM   3042  OE1 GLU B  22      98.399 -24.937   2.930  1.00 83.78           O  
ANISOU 3042  OE1 GLU B  22     9910  11220  10702  -1658    755   -704       O  
ATOM   3043  OE2 GLU B  22      99.142 -26.755   1.933  1.00 95.28           O  
ANISOU 3043  OE2 GLU B  22    10923  13089  12189  -1567    945  -1010       O  
ATOM   3044  N   VAL B  23      96.836 -30.440   6.250  1.00 40.07           N  
ANISOU 3044  N   VAL B  23     3842   5634   5747   -142     90   -904       N  
ATOM   3045  CA  VAL B  23      96.995 -31.880   6.481  1.00 43.51           C  
ANISOU 3045  CA  VAL B  23     4136   6066   6330     98     -3   -988       C  
ATOM   3046  C   VAL B  23      96.247 -32.646   5.396  1.00 43.87           C  
ANISOU 3046  C   VAL B  23     4251   6083   6334    129    108   -993       C  
ATOM   3047  O   VAL B  23      95.259 -32.137   4.848  1.00 41.02           O  
ANISOU 3047  O   VAL B  23     4097   5677   5813     31    178   -863       O  
ATOM   3048  CB  VAL B  23      96.500 -32.299   7.877  1.00 41.72           C  
ANISOU 3048  CB  VAL B  23     4025   5699   6129    286   -222   -856       C  
ATOM   3049  CG1 VAL B  23      97.364 -31.686   8.962  1.00 45.40           C  
ANISOU 3049  CG1 VAL B  23     4394   6230   6625    266   -360   -892       C  
ATOM   3050  CG2 VAL B  23      95.047 -31.924   8.068  1.00 36.55           C  
ANISOU 3050  CG2 VAL B  23     3651   4915   5322    264   -208   -665       C  
ATOM   3051  N   PRO B  24      96.667 -33.866   5.062  1.00 45.79           N  
ANISOU 3051  N   PRO B  24     4326   6345   6727    278    107  -1158       N  
ATOM   3052  CA  PRO B  24      95.919 -34.657   4.073  1.00 39.58           C  
ANISOU 3052  CA  PRO B  24     3614   5524   5901    297    204  -1196       C  
ATOM   3053  C   PRO B  24      94.583 -35.101   4.635  1.00 40.00           C  
ANISOU 3053  C   PRO B  24     3905   5378   5915    395     91   -999       C  
ATOM   3054  O   PRO B  24      94.482 -35.488   5.802  1.00 39.45           O  
ANISOU 3054  O   PRO B  24     3888   5175   5927    531    -76   -900       O  
ATOM   3055  CB  PRO B  24      96.828 -35.864   3.810  1.00 40.69           C  
ANISOU 3055  CB  PRO B  24     3502   5691   6270    468    201  -1461       C  
ATOM   3056  CG  PRO B  24      98.113 -35.588   4.533  1.00 48.58           C  
ANISOU 3056  CG  PRO B  24     4253   6786   7419    527    109  -1569       C  
ATOM   3057  CD  PRO B  24      97.812 -34.608   5.613  1.00 44.58           C  
ANISOU 3057  CD  PRO B  24     3909   6226   6805    460    -16  -1333       C  
ATOM   3058  N   VAL B  25      93.557 -35.075   3.780  1.00 35.54           N  
ANISOU 3058  N   VAL B  25     3478   4818   5209    306    182   -952       N  
ATOM   3059  CA  VAL B  25      92.176 -35.331   4.178  1.00 33.27           C  
ANISOU 3059  CA  VAL B  25     3378   4400   4863    343    110   -792       C  
ATOM   3060  C   VAL B  25      91.540 -36.329   3.222  1.00 36.08           C  
ANISOU 3060  C   VAL B  25     3749   4741   5217    340    173   -896       C  
ATOM   3061  O   VAL B  25      91.779 -36.279   2.011  1.00 36.57           O  
ANISOU 3061  O   VAL B  25     3754   4945   5197    244    297  -1030       O  
ATOM   3062  CB  VAL B  25      91.367 -34.022   4.196  1.00 40.62           C  
ANISOU 3062  CB  VAL B  25     4455   5364   5617    238    116   -629       C  
ATOM   3063  CG1 VAL B  25      89.874 -34.300   4.394  1.00 38.52           C  
ANISOU 3063  CG1 VAL B  25     4313   5028   5296    269     70   -530       C  
ATOM   3064  CG2 VAL B  25      91.918 -33.104   5.273  1.00 36.56           C  
ANISOU 3064  CG2 VAL B  25     3945   4827   5118    238     46   -556       C  
ATOM   3065  N   SER B  26      90.723 -37.235   3.768  1.00 35.37           N  
ANISOU 3065  N   SER B  26     3749   4492   5197    411     95   -840       N  
ATOM   3066  CA  SER B  26      89.889 -38.155   2.999  1.00 35.04           C  
ANISOU 3066  CA  SER B  26     3748   4414   5153    374    138   -929       C  
ATOM   3067  C   SER B  26      88.431 -37.877   3.326  1.00 31.58           C  
ANISOU 3067  C   SER B  26     3432   3970   4598    304    106   -776       C  
ATOM   3068  O   SER B  26      88.069 -37.759   4.498  1.00 35.44           O  
ANISOU 3068  O   SER B  26     3991   4374   5102    332     36   -631       O  
ATOM   3069  CB  SER B  26      90.218 -39.632   3.314  1.00 34.58           C  
ANISOU 3069  CB  SER B  26     3683   4135   5319    493     81  -1034       C  
ATOM   3070  OG  SER B  26      91.495 -39.960   2.858  1.00 53.42           O  
ANISOU 3070  OG  SER B  26     5904   6550   7844    590    114  -1245       O  
ATOM   3071  N   ILE B  27      87.596 -37.783   2.298  1.00 33.19           N  
ANISOU 3071  N   ILE B  27     3644   4292   4676    210    153   -830       N  
ATOM   3072  CA  ILE B  27      86.147 -37.671   2.458  1.00 28.75           C  
ANISOU 3072  CA  ILE B  27     3130   3758   4034    154    116   -750       C  
ATOM   3073  C   ILE B  27      85.505 -38.981   2.016  1.00 29.54           C  
ANISOU 3073  C   ILE B  27     3229   3795   4199     86    137   -886       C  
ATOM   3074  O   ILE B  27      85.681 -39.405   0.868  1.00 33.60           O  
ANISOU 3074  O   ILE B  27     3706   4380   4678     39    185  -1057       O  
ATOM   3075  CB  ILE B  27      85.570 -36.519   1.621  1.00 34.77           C  
ANISOU 3075  CB  ILE B  27     3897   4707   4607    113     98   -705       C  
ATOM   3076  CG1 ILE B  27      86.256 -35.190   1.954  1.00 44.06           C  
ANISOU 3076  CG1 ILE B  27     5111   5897   5732    150     81   -581       C  
ATOM   3077  CG2 ILE B  27      84.061 -36.461   1.804  1.00 33.09           C  
ANISOU 3077  CG2 ILE B  27     3670   4548   4356     94     39   -671       C  
ATOM   3078  CD1 ILE B  27      85.964 -34.704   3.317  1.00 44.85           C  
ANISOU 3078  CD1 ILE B  27     5237   5913   5892    219     31   -467       C  
ATOM   3079  N  AILE B  28      84.765 -39.622   2.912  0.52 31.28           N  
ANISOU 3079  N  AILE B  28     3499   3889   4496     46    115   -824       N  
ATOM   3080  N  BILE B  28      84.710 -39.583   2.904  0.48 31.03           N  
ANISOU 3080  N  BILE B  28     3466   3866   4457     43    114   -821       N  
ATOM   3081  CA AILE B  28      84.077 -40.867   2.580  0.52 33.28           C  
ANISOU 3081  CA AILE B  28     3773   4048   4823    -67    138   -946       C  
ATOM   3082  CA BILE B  28      83.930 -40.780   2.581  0.48 31.72           C  
ANISOU 3082  CA BILE B  28     3570   3874   4608    -77    137   -939       C  
ATOM   3083  C  AILE B  28      82.661 -40.778   3.116  0.52 31.16           C  
ANISOU 3083  C  AILE B  28     3490   3856   4495   -191    139   -878       C  
ATOM   3084  C  BILE B  28      82.897 -40.993   3.680  0.48 32.87           C  
ANISOU 3084  C  BILE B  28     3760   3969   4760   -180    137   -820       C  
ATOM   3085  O  AILE B  28      82.464 -40.571   4.319  0.52 29.52           O  
ANISOU 3085  O  AILE B  28     3332   3597   4290   -197    138   -730       O  
ATOM   3086  O  BILE B  28      83.137 -40.634   4.837  0.48 31.85           O  
ANISOU 3086  O  BILE B  28     3692   3782   4628   -134    119   -659       O  
ATOM   3087  CB AILE B  28      84.801 -42.101   3.140  0.52 36.95           C  
ANISOU 3087  CB AILE B  28     4341   4206   5494    -25    121   -966       C  
ATOM   3088  CB BILE B  28      84.840 -42.017   2.411  0.48 37.81           C  
ANISOU 3088  CB BILE B  28     4396   4404   5566    -32    146  -1068       C  
ATOM   3089  CG1AILE B  28      86.224 -42.152   2.585  0.52 34.90           C  
ANISOU 3089  CG1AILE B  28     4022   3916   5322    128    124  -1094       C  
ATOM   3090  CG1BILE B  28      84.034 -43.254   1.975  0.48 37.79           C  
ANISOU 3090  CG1BILE B  28     4436   4280   5642   -183    172  -1220       C  
ATOM   3091  CG2AILE B  28      84.045 -43.367   2.771  0.52 39.66           C  
ANISOU 3091  CG2AILE B  28     4740   4404   5926   -174    147  -1100       C  
ATOM   3092  CG2BILE B  28      85.615 -42.295   3.686  0.48 39.97           C  
ANISOU 3092  CG2BILE B  28     4766   4446   5973     79     79   -914       C  
ATOM   3093  CD1AILE B  28      87.017 -43.334   3.030  0.52 34.75           C  
ANISOU 3093  CD1AILE B  28     4075   3581   5547    241     64  -1147       C  
ATOM   3094  CD1BILE B  28      84.881 -44.491   1.751  0.48 45.47           C  
ANISOU 3094  CD1BILE B  28     5478   4963   6836   -113    167  -1383       C  
ATOM   3095  N  AASN B  29      81.682 -40.951   2.227  0.52 32.91           N  
ANISOU 3095  N  AASN B  29     3624   4229   4651   -304    145  -1013       N  
ATOM   3096  N  BASN B  29      81.738 -41.563   3.327  0.48 33.18           N  
ANISOU 3096  N  BASN B  29     3756   4064   4788   -346    168   -918       N  
ATOM   3097  CA AASN B  29      80.284 -40.695   2.541  0.52 35.56           C  
ANISOU 3097  CA AASN B  29     3859   4725   4929   -410    143  -1006       C  
ATOM   3098  CA BASN B  29      80.718 -41.967   4.304  0.48 36.12           C  
ANISOU 3098  CA BASN B  29     4152   4406   5166   -516    213   -847       C  
ATOM   3099  C  AASN B  29      80.165 -39.333   3.213  0.52 39.94           C  
ANISOU 3099  C  AASN B  29     4367   5403   5405   -281    110   -863       C  
ATOM   3100  C  BASN B  29      80.132 -40.771   5.047  0.48 39.36           C  
ANISOU 3100  C  BASN B  29     4469   5026   5459   -475    221   -746       C  
ATOM   3101  O  AASN B  29      80.548 -38.314   2.626  0.52 39.26           O  
ANISOU 3101  O  AASN B  29     4266   5417   5235   -149     45   -832       O  
ATOM   3102  O  BASN B  29      79.777 -40.876   6.229  0.48 29.17           O  
ANISOU 3102  O  BASN B  29     3234   3703   4147   -570    276   -643       O  
ATOM   3103  CB AASN B  29      79.724 -41.832   3.398  0.52 35.28           C  
ANISOU 3103  CB AASN B  29     3888   4520   4995   -603    214  -1000       C  
ATOM   3104  CB BASN B  29      81.272 -42.980   5.311  0.48 43.88           C  
ANISOU 3104  CB BASN B  29     5347   5062   6263   -564    216   -724       C  
ATOM   3105  CG AASN B  29      79.714 -43.158   2.654  0.52 47.27           C  
ANISOU 3105  CG AASN B  29     5463   5881   6617   -742    235  -1174       C  
ATOM   3106  CG BASN B  29      81.879 -44.181   4.641  0.48 40.94           C  
ANISOU 3106  CG BASN B  29     5073   4422   6058   -559    191   -850       C  
ATOM   3107  OD1AASN B  29      79.420 -43.200   1.459  0.52 50.95           O  
ANISOU 3107  OD1AASN B  29     5830   6501   7029   -772    209  -1356       O  
ATOM   3108  OD1BASN B  29      82.964 -44.633   5.006  0.48 45.04           O  
ANISOU 3108  OD1BASN B  29     5721   4689   6702   -418    123   -787       O  
ATOM   3109  ND2AASN B  29      80.050 -44.243   3.348  0.52 45.21           N  
ANISOU 3109  ND2AASN B  29     5384   5297   6496   -828    266  -1118       N  
ATOM   3110  ND2BASN B  29      81.182 -44.705   3.642  0.48 33.72           N  
ANISOU 3110  ND2BASN B  29     4084   3568   5160   -699    230  -1057       N  
ATOM   3111  N  AASN B  30      79.677 -39.309   4.449  0.52 38.64           N  
ANISOU 3111  N  AASN B  30     4205   5218   5258   -336    162   -783       N  
ATOM   3112  N  BASN B  30      80.040 -39.629   4.358  0.48 38.09           N  
ANISOU 3112  N  BASN B  30     4186   5072   5216   -340    164   -782       N  
ATOM   3113  CA AASN B  30      79.472 -38.077   5.198  0.52 36.16           C  
ANISOU 3113  CA AASN B  30     3839   5015   4884   -222    148   -702       C  
ATOM   3114  CA BASN B  30      79.597 -38.371   4.963  0.48 37.86           C  
ANISOU 3114  CA BASN B  30     4072   5198   5113   -242    147   -718       C  
ATOM   3115  C  AASN B  30      80.520 -37.876   6.286  0.52 34.85           C  
ANISOU 3115  C  AASN B  30     3826   4692   4725   -156    162   -554       C  
ATOM   3116  C  BASN B  30      80.464 -37.997   6.162  0.48 34.85           C  
ANISOU 3116  C  BASN B  30     3819   4691   4730   -170    164   -568       C  
ATOM   3117  O  AASN B  30      80.241 -37.241   7.307  0.52 34.39           O  
ANISOU 3117  O  AASN B  30     3756   4693   4616   -140    193   -506       O  
ATOM   3118  O  BASN B  30      80.006 -37.353   7.106  0.48 38.22           O  
ANISOU 3118  O  BASN B  30     4212   5203   5106   -162    197   -534       O  
ATOM   3119  CB AASN B  30      78.074 -38.062   5.819  0.52 39.84           C  
ANISOU 3119  CB AASN B  30     4150   5654   5333   -338    215   -778       C  
ATOM   3120  CB BASN B  30      78.119 -38.442   5.358  0.48 38.63           C  
ANISOU 3120  CB BASN B  30     4005   5478   5197   -372    202   -809       C  
ATOM   3121  CG AASN B  30      77.112 -37.131   5.089  0.52 40.01           C  
ANISOU 3121  CG AASN B  30     3952   5919   5329   -224    123   -894       C  
ATOM   3122  CG BASN B  30      77.401 -37.126   5.145  0.48 43.08           C  
ANISOU 3122  CG BASN B  30     4390   6262   5717   -211    124   -862       C  
ATOM   3123  OD1AASN B  30      77.511 -36.103   4.541  0.52 39.25           O  
ANISOU 3123  OD1AASN B  30     3877   5836   5201    -27      6   -847       O  
ATOM   3124  OD1BASN B  30      77.908 -36.230   4.465  0.48 40.17           O  
ANISOU 3124  OD1BASN B  30     4056   5892   5315    -31     10   -815       O  
ATOM   3125  ND2AASN B  30      75.841 -37.491   5.085  0.52 41.19           N  
ANISOU 3125  ND2AASN B  30     3896   6259   5497   -355    162  -1045       N  
ATOM   3126  ND2BASN B  30      76.222 -36.997   5.731  0.48 34.99           N  
ANISOU 3126  ND2BASN B  30     3175   5419   4699   -278    185   -967       N  
ATOM   3127  N   THR B  31      81.728 -38.409   6.113  1.00 33.06           N  
ANISOU 3127  N   THR B  31     3719   4283   4559   -114    135   -510       N  
ATOM   3128  CA  THR B  31      82.694 -38.283   7.193  1.00 32.10           C  
ANISOU 3128  CA  THR B  31     3717   4035   4446    -49    111   -379       C  
ATOM   3129  C   THR B  31      84.000 -37.721   6.647  1.00 36.31           C  
ANISOU 3129  C   THR B  31     4247   4538   5010     98     52   -381       C  
ATOM   3130  O   THR B  31      84.388 -38.019   5.516  1.00 35.97           O  
ANISOU 3130  O   THR B  31     4166   4495   5007    115     54   -479       O  
ATOM   3131  CB  THR B  31      82.924 -39.642   7.877  1.00 40.96           C  
ANISOU 3131  CB  THR B  31     4992   4936   5636   -148    111   -306       C  
ATOM   3132  OG1 THR B  31      81.666 -40.141   8.356  1.00 41.58           O  
ANISOU 3132  OG1 THR B  31     5076   5062   5661   -356    201   -306       O  
ATOM   3133  CG2 THR B  31      83.885 -39.513   9.050  1.00 43.76           C  
ANISOU 3133  CG2 THR B  31     5475   5183   5970    -71     37   -154       C  
ATOM   3134  N   VAL B  32      84.655 -36.890   7.455  1.00 31.87           N  
ANISOU 3134  N   VAL B  32     3717   3979   4414    175     15   -299       N  
ATOM   3135  CA  VAL B  32      85.969 -36.327   7.149  1.00 30.62           C  
ANISOU 3135  CA  VAL B  32     3540   3806   4289    271    -27   -306       C  
ATOM   3136  C   VAL B  32      87.015 -37.041   7.989  1.00 31.93           C  
ANISOU 3136  C   VAL B  32     3762   3829   4539    325   -100   -254       C  
ATOM   3137  O   VAL B  32      86.888 -37.107   9.219  1.00 33.64           O  
ANISOU 3137  O   VAL B  32     4070   4007   4703    307   -144   -146       O  
ATOM   3138  CB  VAL B  32      86.010 -34.817   7.440  1.00 31.48           C  
ANISOU 3138  CB  VAL B  32     3640   4005   4316    308    -40   -271       C  
ATOM   3139  CG1 VAL B  32      87.375 -34.243   7.034  1.00 32.22           C  
ANISOU 3139  CG1 VAL B  32     3706   4096   4441    343    -60   -292       C  
ATOM   3140  CG2 VAL B  32      84.866 -34.123   6.752  1.00 33.53           C  
ANISOU 3140  CG2 VAL B  32     3859   4370   4512    302    -22   -303       C  
ATOM   3141  N   TYR B  33      88.062 -37.542   7.335  1.00 33.60           N  
ANISOU 3141  N   TYR B  33     3914   3982   4871    396   -123   -342       N  
ATOM   3142  CA  TYR B  33      89.188 -38.179   7.989  1.00 32.18           C  
ANISOU 3142  CA  TYR B  33     3741   3671   4813    506   -237   -324       C  
ATOM   3143  C   TYR B  33      90.467 -37.430   7.662  1.00 38.66           C  
ANISOU 3143  C   TYR B  33     4411   4599   5678    575   -248   -418       C  
ATOM   3144  O   TYR B  33      90.580 -36.753   6.633  1.00 37.63           O  
ANISOU 3144  O   TYR B  33     4192   4604   5503    517   -142   -514       O  
ATOM   3145  CB  TYR B  33      89.383 -39.638   7.543  1.00 31.15           C  
ANISOU 3145  CB  TYR B  33     3631   3348   4855    563   -266   -406       C  
ATOM   3146  CG  TYR B  33      88.183 -40.521   7.731  1.00 36.74           C  
ANISOU 3146  CG  TYR B  33     4493   3924   5544    444   -239   -337       C  
ATOM   3147  CD1 TYR B  33      87.139 -40.493   6.820  1.00 39.63           C  
ANISOU 3147  CD1 TYR B  33     4821   4389   5847    316   -116   -428       C  
ATOM   3148  CD2 TYR B  33      88.114 -41.420   8.798  1.00 39.91           C  
ANISOU 3148  CD2 TYR B  33     5081   4100   5981    438   -349   -180       C  
ATOM   3149  CE1 TYR B  33      86.042 -41.314   6.975  1.00 38.68           C  
ANISOU 3149  CE1 TYR B  33     4806   4172   5721    168    -80   -397       C  
ATOM   3150  CE2 TYR B  33      87.015 -42.248   8.967  1.00 38.31           C  
ANISOU 3150  CE2 TYR B  33     5031   3772   5754    267   -298   -116       C  
ATOM   3151  CZ  TYR B  33      85.978 -42.176   8.047  1.00 47.83           C  
ANISOU 3151  CZ  TYR B  33     6153   5105   6918    125   -152   -244       C  
ATOM   3152  OH  TYR B  33      84.873 -42.971   8.176  1.00 52.08           O  
ANISOU 3152  OH  TYR B  33     6800   5552   7438    -82    -87   -217       O  
ATOM   3153  N   THR B  34      91.452 -37.601   8.531  1.00 36.68           N  
ANISOU 3153  N   THR B  34     4134   4296   5507    682   -387   -389       N  
ATOM   3154  CA  THR B  34      92.803 -37.178   8.220  1.00 35.02           C  
ANISOU 3154  CA  THR B  34     3724   4191   5391    747   -405   -528       C  
ATOM   3155  C   THR B  34      93.763 -38.319   8.515  1.00 41.93           C  
ANISOU 3155  C   THR B  34     4518   4931   6483    943   -565   -600       C  
ATOM   3156  O   THR B  34      93.517 -39.158   9.387  1.00 41.06           O  
ANISOU 3156  O   THR B  34     4568   4627   6406   1026   -722   -458       O  
ATOM   3157  CB  THR B  34      93.194 -35.918   8.998  1.00 44.28           C  
ANISOU 3157  CB  THR B  34     4880   5486   6457    690   -448   -469       C  
ATOM   3158  OG1 THR B  34      94.450 -35.445   8.511  1.00 42.90           O  
ANISOU 3158  OG1 THR B  34     4484   5446   6370    688   -422   -633       O  
ATOM   3159  CG2 THR B  34      93.319 -36.214  10.485  1.00 40.10           C  
ANISOU 3159  CG2 THR B  34     4459   4880   5898    766   -645   -330       C  
ATOM   3160  N  ALYS B  35      94.854 -38.347   7.758  0.57 42.92           N  
ANISOU 3160  N  ALYS B  35     4396   5158   6755   1013   -523   -826       N  
ATOM   3161  N  BLYS B  35      94.867 -38.356   7.772  0.43 42.47           N  
ANISOU 3161  N  BLYS B  35     4337   5099   6700   1016   -527   -826       N  
ATOM   3162  CA ALYS B  35      95.852 -39.389   7.910  0.57 44.59           C  
ANISOU 3162  CA ALYS B  35     4465   5252   7224   1251   -684   -959       C  
ATOM   3163  CA BLYS B  35      95.844 -39.430   7.905  0.43 45.23           C  
ANISOU 3163  CA BLYS B  35     4550   5326   7311   1255   -686   -960       C  
ATOM   3164  C  ALYS B  35      96.790 -39.013   9.051  0.57 51.06           C  
ANISOU 3164  C  ALYS B  35     5194   6128   8078   1358   -907   -902       C  
ATOM   3165  C  BLYS B  35      96.853 -39.071   8.991  0.43 50.60           C  
ANISOU 3165  C  BLYS B  35     5117   6068   8038   1370   -907   -922       C  
ATOM   3166  O  ALYS B  35      97.314 -37.894   9.097  0.57 49.58           O  
ANISOU 3166  O  ALYS B  35     4862   6170   7808   1243   -850   -957       O  
ATOM   3167  O  BLYS B  35      97.513 -38.029   8.916  0.43 52.69           O  
ANISOU 3167  O  BLYS B  35     5196   6571   8252   1272   -843  -1015       O  
ATOM   3168  CB ALYS B  35      96.624 -39.579   6.603  0.57 49.61           C  
ANISOU 3168  CB ALYS B  35     4822   6025   8005   1278   -520  -1290       C  
ATOM   3169  CB BLYS B  35      96.552 -39.696   6.577  0.43 48.79           C  
ANISOU 3169  CB BLYS B  35     4734   5896   7909   1286   -521  -1288       C  
ATOM   3170  CG ALYS B  35      97.352 -40.911   6.495  0.57 43.21           C  
ANISOU 3170  CG ALYS B  35     3876   5031   7508   1560   -654  -1489       C  
ATOM   3171  CG BLYS B  35      95.775 -40.577   5.606  0.43 47.65           C  
ANISOU 3171  CG BLYS B  35     4688   5624   7793   1262   -392  -1384       C  
ATOM   3172  CD ALYS B  35      98.310 -40.959   5.307  0.57 54.76           C  
ANISOU 3172  CD ALYS B  35     4986   6709   9110   1585   -469  -1886       C  
ATOM   3173  CD BLYS B  35      96.272 -42.026   5.562  0.43 49.27           C  
ANISOU 3173  CD BLYS B  35     4838   5572   8309   1528   -526  -1555       C  
ATOM   3174  CE ALYS B  35      97.613 -41.345   4.012  0.57 55.75           C  
ANISOU 3174  CE ALYS B  35     5173   6845   9163   1455   -224  -2038       C  
ATOM   3175  CE BLYS B  35      95.516 -42.833   4.501  0.43 47.10           C  
ANISOU 3175  CE BLYS B  35     4653   5188   8055   1462   -372  -1705       C  
ATOM   3176  NZ ALYS B  35      98.592 -41.823   2.991  0.57 67.11           N  
ANISOU 3176  NZ ALYS B  35     6371   8433  10695   1466    -90  -2385       N  
ATOM   3177  NZ BLYS B  35      95.786 -44.293   4.552  0.43 63.88           N  
ANISOU 3177  NZ BLYS B  35     6811   6965  10497   1711   -520  -1845       N  
ATOM   3178  N   VAL B  36      96.964 -39.930   9.997  1.00 50.61           N  
ANISOU 3178  N   VAL B  36     5252   5853   8126   1557  -1179   -776       N  
ATOM   3179  CA  VAL B  36      97.897 -39.754  11.104  1.00 51.50           C  
ANISOU 3179  CA  VAL B  36     5281   6016   8271   1696  -1458   -724       C  
ATOM   3180  C   VAL B  36      98.743 -41.013  11.151  1.00 64.81           C  
ANISOU 3180  C   VAL B  36     6854   7499  10273   2030  -1709   -830       C  
ATOM   3181  O   VAL B  36      98.234 -42.101  11.458  1.00 64.57           O  
ANISOU 3181  O   VAL B  36     7098   7150  10285   2122  -1833   -664       O  
ATOM   3182  CB  VAL B  36      97.194 -39.509  12.447  1.00 49.57           C  
ANISOU 3182  CB  VAL B  36     5358   5710   7768   1602  -1602   -402       C  
ATOM   3183  CG1 VAL B  36      98.214 -39.421  13.567  1.00 53.82           C  
ANISOU 3183  CG1 VAL B  36     5815   6314   8320   1755  -1932   -358       C  
ATOM   3184  CG2 VAL B  36      96.330 -38.263  12.388  1.00 48.14           C  
ANISOU 3184  CG2 VAL B  36     5264   5706   7319   1317  -1359   -346       C  
ATOM   3185  N   ASP B  37     100.023 -40.875  10.820  1.00 70.58           N  
ANISOU 3185  N   ASP B  37     7257   8431  11131   2095  -1696  -1082       N  
ATOM   3186  CA  ASP B  37     100.972 -41.977  10.897  1.00 66.58           C  
ANISOU 3186  CA  ASP B  37     6672   7794  10831   2327  -1868  -1182       C  
ATOM   3187  C   ASP B  37     100.460 -43.201  10.143  1.00 60.04           C  
ANISOU 3187  C   ASP B  37     5985   6676  10150   2410  -1792  -1236       C  
ATOM   3188  O   ASP B  37     100.478 -44.330  10.643  1.00 69.22           O  
ANISOU 3188  O   ASP B  37     7347   7534  11420   2586  -2011  -1109       O  
ATOM   3189  CB  ASP B  37     101.293 -42.311  12.353  1.00 82.05           C  
ANISOU 3189  CB  ASP B  37     8808   9632  12737   2469  -2237   -924       C  
ATOM   3190  CG  ASP B  37     102.453 -41.497  12.891  1.00 95.27           C  
ANISOU 3190  CG  ASP B  37    10199  11610  14391   2478  -2353  -1034       C  
ATOM   3191  OD1 ASP B  37     103.615 -41.857  12.594  1.00102.43           O  
ANISOU 3191  OD1 ASP B  37    10823  12599  15498   2626  -2401  -1276       O  
ATOM   3192  OD2 ASP B  37     102.206 -40.490  13.589  1.00 97.93           O  
ANISOU 3192  OD2 ASP B  37    10584  12109  14514   2327  -2392   -905       O  
ATOM   3193  N   GLY B  38      99.992 -42.961   8.923  1.00 58.03           N  
ANISOU 3193  N   GLY B  38     5641   6520   9890   2264  -1481  -1427       N  
ATOM   3194  CA  GLY B  38      99.617 -44.026   8.022  1.00 63.92           C  
ANISOU 3194  CA  GLY B  38     6459   7057  10771   2310  -1372  -1565       C  
ATOM   3195  C   GLY B  38      98.180 -44.502   8.105  1.00 56.16           C  
ANISOU 3195  C   GLY B  38     5838   5780   9722   2230  -1354  -1347       C  
ATOM   3196  O   GLY B  38      97.777 -45.327   7.275  1.00 65.18           O  
ANISOU 3196  O   GLY B  38     7041   6761  10965   2226  -1238  -1488       O  
ATOM   3197  N   VAL B  39      97.390 -44.036   9.078  1.00 46.55           N  
ANISOU 3197  N   VAL B  39     5585   5866   6236   1582   -401   -815       N  
ATOM   3198  CA  VAL B  39      96.011 -44.497   9.197  1.00 45.63           C  
ANISOU 3198  CA  VAL B  39     5653   5636   6050   1527   -354   -724       C  
ATOM   3199  C   VAL B  39      95.065 -43.308   9.301  1.00 43.27           C  
ANISOU 3199  C   VAL B  39     5349   5352   5741   1374   -344   -683       C  
ATOM   3200  O   VAL B  39      95.438 -42.207   9.709  1.00 43.41           O  
ANISOU 3200  O   VAL B  39     5258   5451   5786   1344   -398   -712       O  
ATOM   3201  CB  VAL B  39      95.795 -45.461  10.393  1.00 41.07           C  
ANISOU 3201  CB  VAL B  39     5235   4971   5398   1677   -406   -671       C  
ATOM   3202  CG1 VAL B  39      96.712 -46.699  10.273  1.00 52.27           C  
ANISOU 3202  CG1 VAL B  39     6673   6361   6824   1844   -415   -707       C  
ATOM   3203  CG2 VAL B  39      96.006 -44.746  11.714  1.00 41.97           C  
ANISOU 3203  CG2 VAL B  39     5330   5138   5479   1739   -517   -668       C  
ATOM   3204  N   ASP B  40      93.813 -43.561   8.934  1.00 34.41           N  
ANISOU 3204  N   ASP B  40     4344   4145   4584   1280   -276   -622       N  
ATOM   3205  CA  ASP B  40      92.786 -42.530   8.895  1.00 32.35           C  
ANISOU 3205  CA  ASP B  40     4087   3889   4317   1136   -258   -583       C  
ATOM   3206  C   ASP B  40      92.151 -42.356  10.264  1.00 38.17           C  
ANISOU 3206  C   ASP B  40     4915   4587   5002   1169   -310   -530       C  
ATOM   3207  O   ASP B  40      91.807 -43.336  10.932  1.00 39.31           O  
ANISOU 3207  O   ASP B  40     5194   4643   5096   1254   -307   -489       O  
ATOM   3208  CB  ASP B  40      91.735 -42.899   7.851  1.00 39.70           C  
ANISOU 3208  CB  ASP B  40     5090   4756   5240   1028   -169   -558       C  
ATOM   3209  CG  ASP B  40      92.314 -42.932   6.449  1.00 51.27           C  
ANISOU 3209  CG  ASP B  40     6473   6267   6740    989   -114   -610       C  
ATOM   3210  OD1 ASP B  40      93.090 -42.015   6.128  1.00 54.61           O  
ANISOU 3210  OD1 ASP B  40     6766   6781   7203    960   -122   -648       O  
ATOM   3211  OD2 ASP B  40      92.004 -43.866   5.675  1.00 56.72           O  
ANISOU 3211  OD2 ASP B  40     7232   6899   7420    984    -56   -618       O  
ATOM   3212  N   VAL B  41      92.010 -41.104  10.686  1.00 31.77           N  
ANISOU 3212  N   VAL B  41     4036   3835   4201   1104   -349   -530       N  
ATOM   3213  CA  VAL B  41      91.367 -40.751  11.944  1.00 30.56           C  
ANISOU 3213  CA  VAL B  41     3961   3654   3997   1120   -392   -486       C  
ATOM   3214  C   VAL B  41      90.192 -39.840  11.629  1.00 39.06           C  
ANISOU 3214  C   VAL B  41     5040   4719   5083    966   -347   -451       C  
ATOM   3215  O   VAL B  41      90.356 -38.837  10.928  1.00 38.27           O  
ANISOU 3215  O   VAL B  41     4828   4682   5032    873   -339   -478       O  
ATOM   3216  CB  VAL B  41      92.341 -40.051  12.909  1.00 34.11           C  
ANISOU 3216  CB  VAL B  41     4324   4189   4446   1202   -498   -533       C  
ATOM   3217  CG1 VAL B  41      91.641 -39.743  14.224  1.00 37.08           C  
ANISOU 3217  CG1 VAL B  41     4802   4534   4754   1227   -538   -486       C  
ATOM   3218  CG2 VAL B  41      93.586 -40.916  13.131  1.00 39.91           C  
ANISOU 3218  CG2 VAL B  41     5033   4951   5180   1365   -556   -581       C  
ATOM   3219  N   GLU B  42      89.020 -40.174  12.168  1.00 34.59           N  
ANISOU 3219  N   GLU B  42     4601   4068   4474    945   -313   -391       N  
ATOM   3220  CA  GLU B  42      87.813 -39.380  11.937  1.00 34.44           C  
ANISOU 3220  CA  GLU B  42     4586   4034   4468    811   -274   -362       C  
ATOM   3221  C   GLU B  42      87.901 -38.025  12.635  1.00 37.15           C  
ANISOU 3221  C   GLU B  42     4861   4439   4815    784   -330   -370       C  
ATOM   3222  O   GLU B  42      88.107 -37.948  13.850  1.00 38.06           O  
ANISOU 3222  O   GLU B  42     5018   4557   4887    864   -383   -364       O  
ATOM   3223  CB  GLU B  42      86.580 -40.143  12.432  1.00 39.39           C  
ANISOU 3223  CB  GLU B  42     5356   4551   5060    800   -216   -307       C  
ATOM   3224  CG  GLU B  42      85.302 -39.316  12.467  1.00 42.00           C  
ANISOU 3224  CG  GLU B  42     5687   4865   5404    682   -185   -281       C  
ATOM   3225  CD  GLU B  42      84.083 -40.147  12.862  1.00 58.65           C  
ANISOU 3225  CD  GLU B  42     7923   6864   7499    660   -111   -241       C  
ATOM   3226  OE1 GLU B  42      83.948 -41.292  12.367  1.00 53.62           O  
ANISOU 3226  OE1 GLU B  42     7346   6159   6869    670    -58   -243       O  
ATOM   3227  OE2 GLU B  42      83.270 -39.659  13.675  1.00 68.59           O  
ANISOU 3227  OE2 GLU B  42     9221   8098   8743    630    -96   -212       O  
ATOM   3228  N   LEU B  43      87.727 -36.952  11.869  1.00 31.94           N  
ANISOU 3228  N   LEU B  43     4108   3826   4202    675   -318   -384       N  
ATOM   3229  CA  LEU B  43      87.648 -35.608  12.436  1.00 36.61           C  
ANISOU 3229  CA  LEU B  43     4643   4461   4808    631   -356   -392       C  
ATOM   3230  C   LEU B  43      86.224 -35.089  12.552  1.00 40.69           C  
ANISOU 3230  C   LEU B  43     5212   4931   5318    543   -320   -346       C  
ATOM   3231  O   LEU B  43      85.965 -34.201  13.376  1.00 37.13           O  
ANISOU 3231  O   LEU B  43     4756   4492   4861    529   -349   -343       O  
ATOM   3232  CB  LEU B  43      88.436 -34.609  11.581  1.00 35.34           C  
ANISOU 3232  CB  LEU B  43     4345   4374   4710    569   -359   -436       C  
ATOM   3233  CG  LEU B  43      89.927 -34.788  11.401  1.00 44.12           C  
ANISOU 3233  CG  LEU B  43     5359   5549   5855    634   -391   -501       C  
ATOM   3234  CD1 LEU B  43      90.437 -33.611  10.585  1.00 42.50           C  
ANISOU 3234  CD1 LEU B  43     5030   5399   5719    541   -366   -536       C  
ATOM   3235  CD2 LEU B  43      90.607 -34.864  12.760  1.00 46.03           C  
ANISOU 3235  CD2 LEU B  43     5598   5819   6072    746   -482   -535       C  
ATOM   3236  N   PHE B  44      85.303 -35.581  11.721  1.00 34.39           N  
ANISOU 3236  N   PHE B  44     4455   4084   4526    482   -258   -320       N  
ATOM   3237  CA  PHE B  44      83.977 -34.964  11.679  1.00 34.05           C  
ANISOU 3237  CA  PHE B  44     4432   4011   4494    395   -229   -291       C  
ATOM   3238  C   PHE B  44      82.989 -35.879  10.972  1.00 37.25           C  
ANISOU 3238  C   PHE B  44     4894   4355   4904    354   -171   -277       C  
ATOM   3239  O   PHE B  44      83.259 -36.335   9.858  1.00 36.79           O  
ANISOU 3239  O   PHE B  44     4814   4309   4857    340   -154   -297       O  
ATOM   3240  CB  PHE B  44      84.054 -33.621  10.953  1.00 32.29           C  
ANISOU 3240  CB  PHE B  44     4115   3844   4311    318   -240   -302       C  
ATOM   3241  CG  PHE B  44      82.723 -32.941  10.777  1.00 32.88           C  
ANISOU 3241  CG  PHE B  44     4200   3893   4401    239   -219   -276       C  
ATOM   3242  CD1 PHE B  44      82.161 -32.220  11.824  1.00 32.39           C  
ANISOU 3242  CD1 PHE B  44     4153   3817   4336    232   -233   -263       C  
ATOM   3243  CD2 PHE B  44      82.038 -33.010   9.567  1.00 34.71           C  
ANISOU 3243  CD2 PHE B  44     4424   4118   4645    179   -190   -272       C  
ATOM   3244  CE1 PHE B  44      80.925 -31.586  11.668  1.00 31.35           C  
ANISOU 3244  CE1 PHE B  44     4023   3663   4226    167   -213   -245       C  
ATOM   3245  CE2 PHE B  44      80.803 -32.366   9.407  1.00 32.57           C  
ANISOU 3245  CE2 PHE B  44     4154   3829   4391    119   -183   -255       C  
ATOM   3246  CZ  PHE B  44      80.247 -31.671  10.464  1.00 30.57           C  
ANISOU 3246  CZ  PHE B  44     3909   3560   4146    113   -192   -242       C  
ATOM   3247  N   GLU B  45      81.850 -36.148  11.600  1.00 36.45           N  
ANISOU 3247  N   GLU B  45     4863   4190   4798    333   -136   -252       N  
ATOM   3248  CA  GLU B  45      80.768 -36.902  10.984  1.00 34.79           C  
ANISOU 3248  CA  GLU B  45     4690   3920   4610    278    -80   -254       C  
ATOM   3249  C   GLU B  45      79.617 -35.944  10.727  1.00 33.27           C  
ANISOU 3249  C   GLU B  45     4453   3737   4451    191    -78   -253       C  
ATOM   3250  O   GLU B  45      79.111 -35.313  11.666  1.00 36.83           O  
ANISOU 3250  O   GLU B  45     4915   4177   4903    185    -76   -234       O  
ATOM   3251  CB  GLU B  45      80.300 -38.060  11.865  1.00 38.91           C  
ANISOU 3251  CB  GLU B  45     5323   4346   5114    315    -23   -234       C  
ATOM   3252  CG  GLU B  45      79.170 -38.838  11.207  1.00 45.33           C  
ANISOU 3252  CG  GLU B  45     6161   5093   5970    244     41   -253       C  
ATOM   3253  CD  GLU B  45      78.520 -39.869  12.120  1.00 56.56           C  
ANISOU 3253  CD  GLU B  45     7696   6404   7390    258    122   -231       C  
ATOM   3254  OE1 GLU B  45      78.862 -39.922  13.320  1.00 59.53           O  
ANISOU 3254  OE1 GLU B  45     8146   6754   7717    330    129   -192       O  
ATOM   3255  OE2 GLU B  45      77.652 -40.618  11.623  1.00 63.58           O  
ANISOU 3255  OE2 GLU B  45     8603   7229   8326    196    183   -258       O  
ATOM   3256  N   ASN B  46      79.208 -35.831   9.463  1.00 32.72           N  
ANISOU 3256  N   ASN B  46     4337   3690   4405    134    -80   -275       N  
ATOM   3257  CA  ASN B  46      78.204 -34.841   9.079  1.00 32.04           C  
ANISOU 3257  CA  ASN B  46     4201   3623   4348     68    -94   -276       C  
ATOM   3258  C   ASN B  46      76.810 -35.361   9.410  1.00 34.96           C  
ANISOU 3258  C   ASN B  46     4599   3929   4755     26    -50   -288       C  
ATOM   3259  O   ASN B  46      76.376 -36.368   8.846  1.00 34.02           O  
ANISOU 3259  O   ASN B  46     4499   3772   4654      4    -20   -320       O  
ATOM   3260  CB  ASN B  46      78.329 -34.537   7.591  1.00 32.42           C  
ANISOU 3260  CB  ASN B  46     4203   3723   4393     40   -120   -296       C  
ATOM   3261  CG  ASN B  46      77.306 -33.533   7.108  1.00 33.32           C  
ANISOU 3261  CG  ASN B  46     4274   3858   4527    -10   -144   -296       C  
ATOM   3262  OD1 ASN B  46      76.838 -32.685   7.870  1.00 33.12           O  
ANISOU 3262  OD1 ASN B  46     4234   3829   4523    -21   -151   -276       O  
ATOM   3263  ND2 ASN B  46      76.944 -33.632   5.821  1.00 31.44           N  
ANISOU 3263  ND2 ASN B  46     4021   3645   4281    -34   -162   -321       N  
ATOM   3264  N   LYS B  47      76.117 -34.682  10.330  1.00 34.90           N  
ANISOU 3264  N   LYS B  47     4589   3907   4766     11    -39   -271       N  
ATOM   3265  CA  LYS B  47      74.719 -34.966  10.638  1.00 36.30           C  
ANISOU 3265  CA  LYS B  47     4770   4028   4993    -39     11   -289       C  
ATOM   3266  C   LYS B  47      73.781 -33.896  10.090  1.00 39.02           C  
ANISOU 3266  C   LYS B  47     5034   4413   5379    -87    -26   -307       C  
ATOM   3267  O   LYS B  47      72.586 -33.931  10.387  1.00 38.59           O  
ANISOU 3267  O   LYS B  47     4960   4323   5379   -128     10   -330       O  
ATOM   3268  CB  LYS B  47      74.515 -35.106  12.151  1.00 40.17           C  
ANISOU 3268  CB  LYS B  47     5328   4462   5473    -16     68   -260       C  
ATOM   3269  CG  LYS B  47      75.396 -36.172  12.820  1.00 46.94           C  
ANISOU 3269  CG  LYS B  47     6285   5273   6278     52    102   -235       C  
ATOM   3270  CD  LYS B  47      75.322 -37.504  12.092  1.00 53.11           C  
ANISOU 3270  CD  LYS B  47     7096   6002   7079     37    142   -262       C  
ATOM   3271  CE  LYS B  47      73.949 -38.143  12.198  1.00 64.42           C  
ANISOU 3271  CE  LYS B  47     8542   7354   8580    -34    227   -290       C  
ATOM   3272  NZ  LYS B  47      73.657 -38.615  13.575  1.00 68.91           N  
ANISOU 3272  NZ  LYS B  47     9214   7837   9133    -11    319   -253       N  
ATOM   3273  N   THR B  48      74.292 -32.951   9.295  1.00 35.91           N  
ANISOU 3273  N   THR B  48     4594   4086   4963    -79    -90   -298       N  
ATOM   3274  CA  THR B  48      73.471 -31.877   8.751  1.00 33.77           C  
ANISOU 3274  CA  THR B  48     4261   3849   4720   -106   -131   -306       C  
ATOM   3275  C   THR B  48      72.941 -32.262   7.369  1.00 34.07           C  
ANISOU 3275  C   THR B  48     4268   3910   4766   -129   -164   -348       C  
ATOM   3276  O   THR B  48      73.290 -33.306   6.804  1.00 36.91           O  
ANISOU 3276  O   THR B  48     4653   4261   5109   -129   -152   -374       O  
ATOM   3277  CB  THR B  48      74.271 -30.583   8.642  1.00 36.08           C  
ANISOU 3277  CB  THR B  48     4538   4190   4983    -84   -174   -268       C  
ATOM   3278  OG1 THR B  48      75.020 -30.612   7.419  1.00 33.54           O  
ANISOU 3278  OG1 THR B  48     4212   3910   4624    -75   -203   -267       O  
ATOM   3279  CG2 THR B  48      75.231 -30.426   9.810  1.00 31.65           C  
ANISOU 3279  CG2 THR B  48     4008   3618   4398    -51   -158   -241       C  
ATOM   3280  N   THR B  49      72.116 -31.388   6.797  1.00 33.31           N  
ANISOU 3280  N   THR B  49     4120   3846   4690   -140   -211   -360       N  
ATOM   3281  CA  THR B  49      71.656 -31.542   5.420  1.00 35.57           C  
ANISOU 3281  CA  THR B  49     4380   4170   4966   -145   -264   -401       C  
ATOM   3282  C   THR B  49      72.550 -30.806   4.405  1.00 34.16           C  
ANISOU 3282  C   THR B  49     4220   4045   4712   -112   -308   -364       C  
ATOM   3283  O   THR B  49      72.222 -30.774   3.213  1.00 33.52           O  
ANISOU 3283  O   THR B  49     4134   4002   4601   -102   -358   -389       O  
ATOM   3284  CB  THR B  49      70.196 -31.076   5.302  1.00 38.55           C  
ANISOU 3284  CB  THR B  49     4691   4553   5403   -162   -299   -443       C  
ATOM   3285  OG1 THR B  49      70.080 -29.712   5.722  1.00 39.45           O  
ANISOU 3285  OG1 THR B  49     4788   4679   5520   -140   -319   -398       O  
ATOM   3286  CG2 THR B  49      69.290 -31.948   6.204  1.00 35.98           C  
ANISOU 3286  CG2 THR B  49     4342   4168   5161   -207   -233   -492       C  
ATOM   3287  N   LEU B  50      73.672 -30.249   4.844  1.00 33.23           N  
ANISOU 3287  N   LEU B  50     4129   3931   4567    -94   -287   -310       N  
ATOM   3288  CA  LEU B  50      74.657 -29.599   3.981  1.00 32.66           C  
ANISOU 3288  CA  LEU B  50     4076   3898   4435    -73   -301   -274       C  
ATOM   3289  C   LEU B  50      75.671 -30.618   3.466  1.00 32.39           C  
ANISOU 3289  C   LEU B  50     4072   3874   4361    -64   -274   -289       C  
ATOM   3290  O   LEU B  50      75.812 -31.705   4.041  1.00 33.30           O  
ANISOU 3290  O   LEU B  50     4199   3958   4496    -67   -244   -314       O  
ATOM   3291  CB  LEU B  50      75.386 -28.499   4.761  1.00 29.60           C  
ANISOU 3291  CB  LEU B  50     3686   3505   4057    -68   -284   -225       C  
ATOM   3292  CG  LEU B  50      74.576 -27.276   5.190  1.00 38.91           C  
ANISOU 3292  CG  LEU B  50     4842   4672   5269    -70   -305   -205       C  
ATOM   3293  CD1 LEU B  50      75.393 -26.392   6.109  1.00 36.10           C  
ANISOU 3293  CD1 LEU B  50     4486   4303   4929    -71   -282   -173       C  
ATOM   3294  CD2 LEU B  50      74.149 -26.506   3.973  1.00 41.49           C  
ANISOU 3294  CD2 LEU B  50     5178   5024   5564    -54   -347   -188       C  
ATOM   3295  N   PRO B  51      76.399 -30.309   2.379  1.00 31.97           N  
ANISOU 3295  N   PRO B  51     4040   3858   4251    -50   -277   -273       N  
ATOM   3296  CA  PRO B  51      77.490 -31.206   1.956  1.00 30.81           C  
ANISOU 3296  CA  PRO B  51     3915   3721   4071    -38   -242   -288       C  
ATOM   3297  C   PRO B  51      78.518 -31.360   3.064  1.00 28.99           C  
ANISOU 3297  C   PRO B  51     3672   3473   3869    -27   -206   -274       C  
ATOM   3298  O   PRO B  51      78.795 -30.424   3.821  1.00 32.76           O  
ANISOU 3298  O   PRO B  51     4128   3948   4371    -31   -205   -244       O  
ATOM   3299  CB  PRO B  51      78.094 -30.505   0.730  1.00 31.13           C  
ANISOU 3299  CB  PRO B  51     3978   3802   4046    -26   -236   -263       C  
ATOM   3300  CG  PRO B  51      76.955 -29.598   0.219  1.00 35.87           C  
ANISOU 3300  CG  PRO B  51     4586   4413   4631    -24   -289   -247       C  
ATOM   3301  CD  PRO B  51      76.206 -29.175   1.452  1.00 33.44           C  
ANISOU 3301  CD  PRO B  51     4238   4073   4395    -39   -305   -241       C  
ATOM   3302  N   VAL B  52      79.097 -32.564   3.138  1.00 28.35           N  
ANISOU 3302  N   VAL B  52     3608   3380   3784     -8   -181   -303       N  
ATOM   3303  CA  VAL B  52      80.005 -32.912   4.234  1.00 31.92           C  
ANISOU 3303  CA  VAL B  52     4054   3816   4257     20   -160   -298       C  
ATOM   3304  C   VAL B  52      81.124 -31.878   4.400  1.00 28.88           C  
ANISOU 3304  C   VAL B  52     3631   3467   3876     27   -154   -274       C  
ATOM   3305  O   VAL B  52      81.446 -31.467   5.519  1.00 30.57           O  
ANISOU 3305  O   VAL B  52     3825   3674   4117     38   -163   -265       O  
ATOM   3306  CB  VAL B  52      80.573 -34.333   4.023  1.00 33.36           C  
ANISOU 3306  CB  VAL B  52     4267   3982   4427     53   -134   -331       C  
ATOM   3307  CG1 VAL B  52      81.221 -34.473   2.621  1.00 30.17           C  
ANISOU 3307  CG1 VAL B  52     3862   3619   3980     57   -118   -349       C  
ATOM   3308  CG2 VAL B  52      81.575 -34.688   5.126  1.00 35.20           C  
ANISOU 3308  CG2 VAL B  52     4497   4204   4673    103   -125   -326       C  
ATOM   3309  N   ASN B  53      81.759 -31.454   3.308  1.00 30.21           N  
ANISOU 3309  N   ASN B  53     3788   3671   4018     19   -134   -270       N  
ATOM   3310  CA  ASN B  53      82.916 -30.567   3.474  1.00 29.40           C  
ANISOU 3310  CA  ASN B  53     3640   3594   3936     16   -111   -260       C  
ATOM   3311  C   ASN B  53      82.502 -29.163   3.912  1.00 34.44           C  
ANISOU 3311  C   ASN B  53     4262   4224   4601    -17   -125   -227       C  
ATOM   3312  O   ASN B  53      83.273 -28.468   4.587  1.00 33.06           O  
ANISOU 3312  O   ASN B  53     4043   4055   4465    -22   -119   -231       O  
ATOM   3313  CB  ASN B  53      83.732 -30.477   2.184  1.00 34.03           C  
ANISOU 3313  CB  ASN B  53     4225   4213   4491     10    -62   -264       C  
ATOM   3314  CG  ASN B  53      82.937 -29.904   1.030  1.00 36.45           C  
ANISOU 3314  CG  ASN B  53     4580   4523   4746    -14    -59   -234       C  
ATOM   3315  OD1 ASN B  53      81.852 -30.392   0.712  1.00 33.30           O  
ANISOU 3315  OD1 ASN B  53     4219   4114   4318     -9    -97   -241       O  
ATOM   3316  ND2 ASN B  53      83.471 -28.856   0.399  1.00 33.90           N  
ANISOU 3316  ND2 ASN B  53     4256   4212   4414    -36    -14   -204       N  
ATOM   3317  N   VAL B  54      81.295 -28.742   3.543  1.00 30.70           N  
ANISOU 3317  N   VAL B  54     3819   3734   4110    -34   -148   -204       N  
ATOM   3318  CA  VAL B  54      80.780 -27.442   3.966  1.00 34.67           C  
ANISOU 3318  CA  VAL B  54     4313   4220   4639    -57   -162   -173       C  
ATOM   3319  C   VAL B  54      80.419 -27.470   5.445  1.00 32.84           C  
ANISOU 3319  C   VAL B  54     4065   3965   4449    -50   -188   -184       C  
ATOM   3320  O   VAL B  54      80.802 -26.576   6.212  1.00 30.99           O  
ANISOU 3320  O   VAL B  54     3803   3723   4248    -60   -188   -180       O  
ATOM   3321  CB  VAL B  54      79.571 -27.066   3.094  1.00 33.26           C  
ANISOU 3321  CB  VAL B  54     4171   4036   4428    -61   -187   -151       C  
ATOM   3322  CG1 VAL B  54      78.932 -25.761   3.589  1.00 30.45           C  
ANISOU 3322  CG1 VAL B  54     3809   3655   4105    -73   -205   -120       C  
ATOM   3323  CG2 VAL B  54      80.014 -26.966   1.623  1.00 32.07           C  
ANISOU 3323  CG2 VAL B  54     4057   3911   4217    -57   -159   -135       C  
ATOM   3324  N   ALA B  55      79.685 -28.508   5.866  1.00 33.10           N  
ANISOU 3324  N   ALA B  55     4118   3980   4478    -35   -203   -202       N  
ATOM   3325  CA  ALA B  55      79.310 -28.654   7.268  1.00 31.38           C  
ANISOU 3325  CA  ALA B  55     3903   3734   4286    -24   -212   -208       C  
ATOM   3326  C   ALA B  55      80.535 -28.682   8.161  1.00 30.79           C  
ANISOU 3326  C   ALA B  55     3811   3671   4217      5   -212   -222       C  
ATOM   3327  O   ALA B  55      80.521 -28.129   9.269  1.00 31.78           O  
ANISOU 3327  O   ALA B  55     3931   3786   4359     12   -226   -223       O  
ATOM   3328  CB  ALA B  55      78.492 -29.935   7.460  1.00 31.35           C  
ANISOU 3328  CB  ALA B  55     3933   3699   4278    -16   -204   -226       C  
ATOM   3329  N   PHE B  56      81.588 -29.373   7.710  1.00 29.50           N  
ANISOU 3329  N   PHE B  56     3638   3532   4039     28   -200   -240       N  
ATOM   3330  CA  PHE B  56      82.851 -29.443   8.441  1.00 29.13           C  
ANISOU 3330  CA  PHE B  56     3558   3508   4002     66   -212   -266       C  
ATOM   3331  C   PHE B  56      83.432 -28.051   8.668  1.00 30.76           C  
ANISOU 3331  C   PHE B  56     3708   3734   4245     37   -217   -272       C  
ATOM   3332  O   PHE B  56      83.853 -27.706   9.779  1.00 30.50           O  
ANISOU 3332  O   PHE B  56     3654   3706   4227     58   -247   -296       O  
ATOM   3333  CB  PHE B  56      83.832 -30.302   7.637  1.00 30.41           C  
ANISOU 3333  CB  PHE B  56     3706   3697   4152     92   -191   -288       C  
ATOM   3334  CG  PHE B  56      85.210 -30.418   8.239  1.00 31.19           C  
ANISOU 3334  CG  PHE B  56     3753   3830   4270    139   -208   -327       C  
ATOM   3335  CD1 PHE B  56      85.385 -30.848   9.540  1.00 31.32           C  
ANISOU 3335  CD1 PHE B  56     3787   3838   4276    200   -249   -341       C  
ATOM   3336  CD2 PHE B  56      86.335 -30.141   7.477  1.00 35.24           C  
ANISOU 3336  CD2 PHE B  56     4200   4383   4809    128   -180   -354       C  
ATOM   3337  CE1 PHE B  56      86.667 -30.996  10.090  1.00 37.18           C  
ANISOU 3337  CE1 PHE B  56     4475   4619   5032    260   -282   -387       C  
ATOM   3338  CE2 PHE B  56      87.623 -30.288   8.014  1.00 36.80           C  
ANISOU 3338  CE2 PHE B  56     4329   4619   5036    175   -202   -405       C  
ATOM   3339  CZ  PHE B  56      87.783 -30.711   9.324  1.00 33.49           C  
ANISOU 3339  CZ  PHE B  56     3922   4198   4605    245   -262   -425       C  
ATOM   3340  N   GLU B  57      83.444 -27.227   7.628  1.00 31.89           N  
ANISOU 3340  N   GLU B  57     3835   3883   4400    -11   -187   -254       N  
ATOM   3341  CA  GLU B  57      84.018 -25.893   7.773  1.00 31.54           C  
ANISOU 3341  CA  GLU B  57     3741   3841   4401    -48   -176   -261       C  
ATOM   3342  C   GLU B  57      83.175 -25.017   8.706  1.00 32.61           C  
ANISOU 3342  C   GLU B  57     3891   3945   4554    -61   -203   -250       C  
ATOM   3343  O   GLU B  57      83.722 -24.290   9.547  1.00 31.93           O  
ANISOU 3343  O   GLU B  57     3766   3861   4505    -68   -219   -281       O  
ATOM   3344  CB  GLU B  57      84.169 -25.252   6.394  1.00 34.40           C  
ANISOU 3344  CB  GLU B  57     4107   4202   4762    -92   -121   -232       C  
ATOM   3345  CG  GLU B  57      84.766 -23.846   6.428  1.00 36.74           C  
ANISOU 3345  CG  GLU B  57     4362   4484   5113   -141    -88   -236       C  
ATOM   3346  CD  GLU B  57      85.051 -23.301   5.036  1.00 45.13           C  
ANISOU 3346  CD  GLU B  57     5444   5538   6165   -178    -13   -201       C  
ATOM   3347  OE1 GLU B  57      85.170 -24.109   4.095  1.00 49.85           O  
ANISOU 3347  OE1 GLU B  57     6067   6158   6715   -161     10   -192       O  
ATOM   3348  OE2 GLU B  57      85.159 -22.067   4.884  1.00 46.27           O  
ANISOU 3348  OE2 GLU B  57     5587   5647   6345   -223     27   -183       O  
ATOM   3349  N   LEU B  58      81.845 -25.082   8.593  1.00 31.87           N  
ANISOU 3349  N   LEU B  58     3848   3824   4439    -64   -211   -215       N  
ATOM   3350  CA  LEU B  58      81.000 -24.297   9.492  1.00 32.89           C  
ANISOU 3350  CA  LEU B  58     3987   3921   4587    -71   -230   -209       C  
ATOM   3351  C   LEU B  58      81.161 -24.755  10.937  1.00 35.68           C  
ANISOU 3351  C   LEU B  58     4347   4277   4934    -33   -258   -240       C  
ATOM   3352  O   LEU B  58      81.212 -23.934  11.860  1.00 32.57           O  
ANISOU 3352  O   LEU B  58     3942   3873   4560    -36   -274   -259       O  
ATOM   3353  CB  LEU B  58      79.530 -24.392   9.069  1.00 30.10           C  
ANISOU 3353  CB  LEU B  58     3673   3544   4221    -75   -232   -177       C  
ATOM   3354  CG  LEU B  58      79.138 -23.857   7.685  1.00 43.19           C  
ANISOU 3354  CG  LEU B  58     5341   5200   5868    -95   -220   -142       C  
ATOM   3355  CD1 LEU B  58      77.616 -23.888   7.482  1.00 44.68           C  
ANISOU 3355  CD1 LEU B  58     5551   5371   6054    -88   -243   -129       C  
ATOM   3356  CD2 LEU B  58      79.665 -22.473   7.472  1.00 42.03           C  
ANISOU 3356  CD2 LEU B  58     5182   5036   5749   -122   -198   -125       C  
ATOM   3357  N   TRP B  59      81.244 -26.063  11.153  1.00 27.67           N  
ANISOU 3357  N   TRP B  59     3360   3270   3884      8   -263   -247       N  
ATOM   3358  CA  TRP B  59      81.494 -26.571  12.497  1.00 32.18           C  
ANISOU 3358  CA  TRP B  59     3956   3839   4430     61   -288   -270       C  
ATOM   3359  C   TRP B  59      82.836 -26.079  13.029  1.00 33.25           C  
ANISOU 3359  C   TRP B  59     4038   4013   4582     81   -323   -317       C  
ATOM   3360  O   TRP B  59      82.942 -25.630  14.180  1.00 33.39           O  
ANISOU 3360  O   TRP B  59     4061   4033   4593    104   -355   -344       O  
ATOM   3361  CB  TRP B  59      81.453 -28.100  12.484  1.00 30.49           C  
ANISOU 3361  CB  TRP B  59     3792   3617   4177    106   -277   -263       C  
ATOM   3362  CG  TRP B  59      81.914 -28.689  13.784  1.00 32.60           C  
ANISOU 3362  CG  TRP B  59     4100   3882   4403    178   -303   -280       C  
ATOM   3363  CD1 TRP B  59      81.224 -28.697  14.981  1.00 37.69           C  
ANISOU 3363  CD1 TRP B  59     4807   4495   5018    203   -300   -271       C  
ATOM   3364  CD2 TRP B  59      83.150 -29.359  14.032  1.00 35.89           C  
ANISOU 3364  CD2 TRP B  59     4507   4332   4799    245   -336   -310       C  
ATOM   3365  NE1 TRP B  59      81.972 -29.327  15.947  1.00 40.14           N  
ANISOU 3365  NE1 TRP B  59     5160   4815   5276    287   -333   -288       N  
ATOM   3366  CE2 TRP B  59      83.155 -29.742  15.394  1.00 43.84           C  
ANISOU 3366  CE2 TRP B  59     5580   5325   5752    318   -362   -313       C  
ATOM   3367  CE3 TRP B  59      84.264 -29.661  13.245  1.00 38.40           C  
ANISOU 3367  CE3 TRP B  59     4765   4690   5135    258   -345   -336       C  
ATOM   3368  CZ2 TRP B  59      84.221 -30.417  15.976  1.00 46.33           C  
ANISOU 3368  CZ2 TRP B  59     5906   5667   6028    411   -409   -341       C  
ATOM   3369  CZ3 TRP B  59      85.325 -30.347  13.827  1.00 49.48           C  
ANISOU 3369  CZ3 TRP B  59     6165   6121   6513    345   -387   -369       C  
ATOM   3370  CH2 TRP B  59      85.295 -30.713  15.179  1.00 50.37           C  
ANISOU 3370  CH2 TRP B  59     6347   6222   6569    425   -426   -371       C  
ATOM   3371  N   ALA B  60      83.885 -26.170  12.209  1.00 30.46           N  
ANISOU 3371  N   ALA B  60     3628   3694   4250     73   -316   -337       N  
ATOM   3372  CA  ALA B  60      85.193 -25.704  12.662  1.00 31.67           C  
ANISOU 3372  CA  ALA B  60     3708   3889   4438     86   -348   -398       C  
ATOM   3373  C   ALA B  60      85.175 -24.214  12.980  1.00 34.31           C  
ANISOU 3373  C   ALA B  60     4004   4210   4822     31   -349   -419       C  
ATOM   3374  O   ALA B  60      85.930 -23.749  13.842  1.00 33.43           O  
ANISOU 3374  O   ALA B  60     3845   4124   4734     46   -393   -482       O  
ATOM   3375  CB  ALA B  60      86.254 -25.993  11.606  1.00 33.94           C  
ANISOU 3375  CB  ALA B  60     3931   4209   4754     75   -320   -419       C  
ATOM   3376  N   LYS B  61      84.330 -23.457  12.300  1.00 34.60           N  
ANISOU 3376  N   LYS B  61     4062   4208   4878    -28   -307   -373       N  
ATOM   3377  CA  LYS B  61      84.244 -22.017  12.496  1.00 33.63           C  
ANISOU 3377  CA  LYS B  61     3914   4057   4806    -81   -296   -385       C  
ATOM   3378  C   LYS B  61      83.171 -21.618  13.503  1.00 36.25           C  
ANISOU 3378  C   LYS B  61     4298   4356   5120    -67   -319   -376       C  
ATOM   3379  O   LYS B  61      82.788 -20.444  13.543  1.00 34.59           O  
ANISOU 3379  O   LYS B  61     4085   4109   4949   -108   -302   -373       O  
ATOM   3380  CB  LYS B  61      83.999 -21.329  11.146  1.00 33.54           C  
ANISOU 3380  CB  LYS B  61     3906   4016   4823   -141   -233   -336       C  
ATOM   3381  CG  LYS B  61      85.256 -21.366  10.261  1.00 37.93           C  
ANISOU 3381  CG  LYS B  61     4400   4598   5412   -168   -192   -359       C  
ATOM   3382  CD  LYS B  61      85.040 -20.782   8.871  1.00 36.92           C  
ANISOU 3382  CD  LYS B  61     4301   4438   5290   -217   -119   -301       C  
ATOM   3383  CE  LYS B  61      86.354 -20.761   8.093  1.00 39.50           C  
ANISOU 3383  CE  LYS B  61     4567   4788   5656   -251    -58   -330       C  
ATOM   3384  NZ  LYS B  61      86.205 -20.255   6.697  1.00 37.05           N  
ANISOU 3384  NZ  LYS B  61     4302   4442   5331   -290     25   -267       N  
ATOM   3385  N   ARG B  62      82.711 -22.550  14.333  1.00 31.96           N  
ANISOU 3385  N   ARG B  62     3805   3819   4518     -9   -347   -373       N  
ATOM   3386  CA  ARG B  62      81.627 -22.266  15.271  1.00 30.53           C  
ANISOU 3386  CA  ARG B  62     3679   3605   4315      4   -351   -362       C  
ATOM   3387  C   ARG B  62      82.077 -21.267  16.332  1.00 34.56           C  
ANISOU 3387  C   ARG B  62     4169   4118   4846      5   -385   -422       C  
ATOM   3388  O   ARG B  62      83.261 -21.173  16.679  1.00 31.36           O  
ANISOU 3388  O   ARG B  62     3712   3751   4453     19   -425   -484       O  
ATOM   3389  CB  ARG B  62      81.153 -23.560  15.942  1.00 34.15           C  
ANISOU 3389  CB  ARG B  62     4207   4063   4705     66   -355   -346       C  
ATOM   3390  CG  ARG B  62      82.216 -24.184  16.863  1.00 34.88           C  
ANISOU 3390  CG  ARG B  62     4306   4195   4753    137   -407   -392       C  
ATOM   3391  CD  ARG B  62      81.896 -25.639  17.199  1.00 41.40           C  
ANISOU 3391  CD  ARG B  62     5211   5008   5509    200   -395   -360       C  
ATOM   3392  NE  ARG B  62      82.901 -26.222  18.083  1.00 40.97           N  
ANISOU 3392  NE  ARG B  62     5176   4990   5402    287   -453   -399       N  
ATOM   3393  CZ  ARG B  62      84.078 -26.716  17.685  1.00 46.63           C  
ANISOU 3393  CZ  ARG B  62     5842   5751   6126    321   -489   -429       C  
ATOM   3394  NH1 ARG B  62      84.433 -26.694  16.402  1.00 34.28           N  
ANISOU 3394  NH1 ARG B  62     4208   4199   4619    268   -462   -423       N  
ATOM   3395  NH2 ARG B  62      84.919 -27.220  18.577  1.00 44.49           N  
ANISOU 3395  NH2 ARG B  62     5590   5514   5802    415   -553   -468       N  
ATOM   3396  N   ASN B  63      81.117 -20.499  16.849  1.00 33.31           N  
ANISOU 3396  N   ASN B  63     4042   3919   4694     -9   -370   -414       N  
ATOM   3397  CA  ASN B  63      81.431 -19.538  17.902  1.00 34.49           C  
ANISOU 3397  CA  ASN B  63     4181   4064   4858     -8   -401   -478       C  
ATOM   3398  C   ASN B  63      81.719 -20.289  19.204  1.00 31.43           C  
ANISOU 3398  C   ASN B  63     3840   3711   4391     71   -451   -516       C  
ATOM   3399  O   ASN B  63      80.901 -21.107  19.647  1.00 35.95           O  
ANISOU 3399  O   ASN B  63     4490   4270   4901    113   -430   -476       O  
ATOM   3400  CB  ASN B  63      80.253 -18.563  18.085  1.00 33.77           C  
ANISOU 3400  CB  ASN B  63     4121   3918   4794    -36   -367   -457       C  
ATOM   3401  CG  ASN B  63      80.628 -17.338  18.889  1.00 40.23           C  
ANISOU 3401  CG  ASN B  63     4918   4720   5648    -53   -388   -527       C  
ATOM   3402  OD1 ASN B  63      81.229 -17.442  19.952  1.00 39.31           O  
ANISOU 3402  OD1 ASN B  63     4807   4636   5494    -14   -438   -593       O  
ATOM   3403  ND2 ASN B  63      80.289 -16.157  18.368  1.00 43.08           N  
ANISOU 3403  ND2 ASN B  63     5261   5027   6079   -107   -353   -516       N  
ATOM   3404  N   ILE B  64      82.878 -20.013  19.812  1.00 32.15           N  
ANISOU 3404  N   ILE B  64     3887   3845   4485     92   -513   -597       N  
ATOM   3405  CA  ILE B  64      83.348 -20.714  21.013  1.00 36.41           C  
ANISOU 3405  CA  ILE B  64     4471   4426   4937    185   -579   -641       C  
ATOM   3406  C   ILE B  64      83.324 -19.809  22.248  1.00 39.52           C  
ANISOU 3406  C   ILE B  64     4886   4820   5311    203   -620   -713       C  
ATOM   3407  O   ILE B  64      83.993 -20.093  23.244  1.00 39.00           O  
ANISOU 3407  O   ILE B  64     4839   4800   5179    280   -696   -776       O  
ATOM   3408  CB  ILE B  64      84.752 -21.325  20.815  1.00 35.75           C  
ANISOU 3408  CB  ILE B  64     4320   4407   4857    224   -640   -691       C  
ATOM   3409  CG1 ILE B  64      85.801 -20.234  20.553  1.00 38.58           C  
ANISOU 3409  CG1 ILE B  64     4554   4788   5315    163   -669   -780       C  
ATOM   3410  CG2 ILE B  64      84.728 -22.381  19.706  1.00 35.78           C  
ANISOU 3410  CG2 ILE B  64     4322   4409   4862    222   -597   -621       C  
ATOM   3411  CD1 ILE B  64      87.247 -20.687  20.800  1.00 41.23           C  
ANISOU 3411  CD1 ILE B  64     4809   5201   5657    219   -752   -868       C  
ATOM   3412  N   LYS B  65      82.590 -18.721  22.198  1.00 35.98           N  
ANISOU 3412  N   LYS B  65     4436   4321   4914    141   -576   -709       N  
ATOM   3413  CA  LYS B  65      82.297 -17.935  23.382  1.00 37.97           C  
ANISOU 3413  CA  LYS B  65     4729   4560   5137    160   -599   -768       C  
ATOM   3414  C   LYS B  65      80.869 -18.223  23.815  1.00 37.03           C  
ANISOU 3414  C   LYS B  65     4714   4397   4960    183   -534   -701       C  
ATOM   3415  O   LYS B  65      80.105 -18.828  23.057  1.00 36.67           O  
ANISOU 3415  O   LYS B  65     4685   4324   4924    165   -472   -617       O  
ATOM   3416  CB  LYS B  65      82.468 -16.438  23.075  1.00 37.80           C  
ANISOU 3416  CB  LYS B  65     4634   4502   5225     74   -587   -821       C  
ATOM   3417  CG  LYS B  65      83.851 -16.077  22.554  1.00 47.50           C  
ANISOU 3417  CG  LYS B  65     5748   5764   6535     31   -627   -892       C  
ATOM   3418  CD  LYS B  65      83.927 -14.583  22.254  1.00 64.05           C  
ANISOU 3418  CD  LYS B  65     7788   7802   8745    -62   -592   -937       C  
ATOM   3419  CE  LYS B  65      82.931 -14.211  21.157  1.00 76.21           C  
ANISOU 3419  CE  LYS B  65     9352   9269  10334   -118   -498   -831       C  
ATOM   3420  NZ  LYS B  65      82.650 -12.747  21.098  1.00 76.24           N  
ANISOU 3420  NZ  LYS B  65     9346   9196  10425   -184   -457   -857       N  
ATOM   3421  N   PRO B  66      80.467 -17.838  25.031  1.00 35.15           N  
ANISOU 3421  N   PRO B  66     4545   4150   4662    224   -541   -741       N  
ATOM   3422  CA  PRO B  66      79.056 -18.009  25.401  1.00 36.98           C  
ANISOU 3422  CA  PRO B  66     4863   4331   4856    234   -459   -682       C  
ATOM   3423  C   PRO B  66      78.184 -17.268  24.406  1.00 34.63           C  
ANISOU 3423  C   PRO B  66     4512   3979   4666    153   -394   -638       C  
ATOM   3424  O   PRO B  66      78.440 -16.107  24.087  1.00 36.49           O  
ANISOU 3424  O   PRO B  66     4687   4194   4983    101   -405   -677       O  
ATOM   3425  CB  PRO B  66      78.973 -17.394  26.803  1.00 35.85           C  
ANISOU 3425  CB  PRO B  66     4786   4190   4645    280   -482   -755       C  
ATOM   3426  CG  PRO B  66      80.402 -17.488  27.336  1.00 36.30           C  
ANISOU 3426  CG  PRO B  66     4821   4316   4656    332   -596   -841       C  
ATOM   3427  CD  PRO B  66      81.244 -17.210  26.124  1.00 34.16           C  
ANISOU 3427  CD  PRO B  66     4420   4059   4501    261   -622   -851       C  
ATOM   3428  N   VAL B  67      77.170 -17.956  23.883  1.00 35.75           N  
ANISOU 3428  N   VAL B  67     4678   4095   4812    145   -326   -560       N  
ATOM   3429  CA  VAL B  67      76.218 -17.327  22.965  1.00 33.40           C  
ANISOU 3429  CA  VAL B  67     4335   3751   4605     88   -274   -520       C  
ATOM   3430  C   VAL B  67      74.810 -17.642  23.451  1.00 37.60           C  
ANISOU 3430  C   VAL B  67     4921   4247   5118    105   -198   -489       C  
ATOM   3431  O   VAL B  67      74.603 -18.613  24.200  1.00 33.56           O  
ANISOU 3431  O   VAL B  67     4483   3743   4526    149   -170   -478       O  
ATOM   3432  CB  VAL B  67      76.421 -17.806  21.505  1.00 33.03           C  
ANISOU 3432  CB  VAL B  67     4230   3713   4606     50   -275   -465       C  
ATOM   3433  CG1 VAL B  67      77.724 -17.210  20.859  1.00 33.63           C  
ANISOU 3433  CG1 VAL B  67     4238   3811   4729     15   -326   -496       C  
ATOM   3434  CG2 VAL B  67      76.434 -19.324  21.435  1.00 31.29           C  
ANISOU 3434  CG2 VAL B  67     4047   3518   4323     84   -265   -427       C  
ATOM   3435  N   PRO B  68      73.815 -16.845  23.037  1.00 33.36           N  
ANISOU 3435  N   PRO B  68     4351   3668   4658     73   -157   -477       N  
ATOM   3436  CA  PRO B  68      72.427 -17.151  23.404  1.00 33.32           C  
ANISOU 3436  CA  PRO B  68     4373   3632   4655     83    -78   -457       C  
ATOM   3437  C   PRO B  68      72.047 -18.557  22.981  1.00 32.35           C  
ANISOU 3437  C   PRO B  68     4261   3519   4512     84    -42   -408       C  
ATOM   3438  O   PRO B  68      72.451 -19.025  21.917  1.00 32.73           O  
ANISOU 3438  O   PRO B  68     4267   3588   4582     62    -74   -377       O  
ATOM   3439  CB  PRO B  68      71.618 -16.114  22.617  1.00 35.38           C  
ANISOU 3439  CB  PRO B  68     4568   3856   5018     52    -66   -448       C  
ATOM   3440  CG  PRO B  68      72.570 -14.962  22.440  1.00 34.78           C  
ANISOU 3440  CG  PRO B  68     4468   3773   4972     34   -122   -480       C  
ATOM   3441  CD  PRO B  68      73.905 -15.614  22.225  1.00 33.37           C  
ANISOU 3441  CD  PRO B  68     4289   3643   4749     31   -177   -482       C  
ATOM   3442  N   GLU B  69      71.245 -19.221  23.815  1.00 32.88           N  
ANISOU 3442  N   GLU B  69     4389   3566   4539    105     35   -403       N  
ATOM   3443  CA  GLU B  69      70.692 -20.500  23.402  1.00 38.91           C  
ANISOU 3443  CA  GLU B  69     5158   4320   5305     93     89   -364       C  
ATOM   3444  C   GLU B  69      69.856 -20.316  22.140  1.00 42.00           C  
ANISOU 3444  C   GLU B  69     5451   4705   5803     47     91   -349       C  
ATOM   3445  O   GLU B  69      69.234 -19.270  21.922  1.00 34.31           O  
ANISOU 3445  O   GLU B  69     4423   3716   4896     36     88   -366       O  
ATOM   3446  CB  GLU B  69      69.856 -21.101  24.522  1.00 39.91           C  
ANISOU 3446  CB  GLU B  69     5366   4410   5386    114    195   -365       C  
ATOM   3447  CG  GLU B  69      70.703 -21.618  25.659  1.00 43.14           C  
ANISOU 3447  CG  GLU B  69     5897   4829   5665    175    190   -366       C  
ATOM   3448  CD  GLU B  69      69.913 -22.449  26.628  1.00 49.04           C  
ANISOU 3448  CD  GLU B  69     6747   5531   6356    196    314   -349       C  
ATOM   3449  OE1 GLU B  69      69.191 -21.852  27.461  1.00 42.99           O  
ANISOU 3449  OE1 GLU B  69     6010   4740   5584    204    381   -375       O  
ATOM   3450  OE2 GLU B  69      70.004 -23.700  26.551  1.00 43.59           O  
ANISOU 3450  OE2 GLU B  69     6111   4823   5628    204    353   -309       O  
ATOM   3451  N   VAL B  70      69.862 -21.346  21.294  1.00 39.39           N  
ANISOU 3451  N   VAL B  70     5100   4384   5482     27     90   -321       N  
ATOM   3452  CA  VAL B  70      69.193 -21.262  19.997  1.00 39.04           C  
ANISOU 3452  CA  VAL B  70     4966   4345   5523     -7     71   -312       C  
ATOM   3453  C   VAL B  70      67.701 -20.980  20.151  1.00 32.43           C  
ANISOU 3453  C   VAL B  70     4081   3479   4763    -20    134   -336       C  
ATOM   3454  O   VAL B  70      67.110 -20.263  19.325  1.00 37.87           O  
ANISOU 3454  O   VAL B  70     4692   4172   5524    -26     99   -343       O  
ATOM   3455  CB  VAL B  70      69.457 -22.553  19.205  1.00 38.83           C  
ANISOU 3455  CB  VAL B  70     4938   4333   5484    -23     65   -290       C  
ATOM   3456  CG1 VAL B  70      68.557 -22.630  17.985  1.00 43.92           C  
ANISOU 3456  CG1 VAL B  70     5497   4984   6209    -54     52   -295       C  
ATOM   3457  CG2 VAL B  70      70.912 -22.603  18.789  1.00 34.83           C  
ANISOU 3457  CG2 VAL B  70     4449   3862   4924     -9     -8   -273       C  
ATOM   3458  N   LYS B  71      67.067 -21.501  21.213  1.00 32.29           N  
ANISOU 3458  N   LYS B  71     4109   3428   4729    -18    232   -351       N  
ATOM   3459  CA  LYS B  71      65.645 -21.222  21.401  1.00 36.33           C  
ANISOU 3459  CA  LYS B  71     4563   3914   5328    -32    304   -384       C  
ATOM   3460  C   LYS B  71      65.386 -19.720  21.554  1.00 35.28           C  
ANISOU 3460  C   LYS B  71     4394   3778   5233     -9    272   -406       C  
ATOM   3461  O   LYS B  71      64.372 -19.204  21.061  1.00 35.10           O  
ANISOU 3461  O   LYS B  71     4282   3751   5304    -12    273   -430       O  
ATOM   3462  CB  LYS B  71      65.094 -21.998  22.601  1.00 35.96           C  
ANISOU 3462  CB  LYS B  71     4586   3825   5251    -37    434   -394       C  
ATOM   3463  CG  LYS B  71      65.653 -21.594  23.966  1.00 38.58           C  
ANISOU 3463  CG  LYS B  71     5032   4144   5482      7    464   -392       C  
ATOM   3464  CD  LYS B  71      65.121 -22.490  25.105  1.00 39.02           C  
ANISOU 3464  CD  LYS B  71     5183   4153   5491      9    607   -390       C  
ATOM   3465  CE  LYS B  71      66.007 -22.408  26.349  1.00 44.80           C  
ANISOU 3465  CE  LYS B  71     6060   4883   6079     69    610   -378       C  
ATOM   3466  NZ  LYS B  71      65.557 -23.345  27.431  1.00 41.82           N  
ANISOU 3466  NZ  LYS B  71     5804   4453   5634     81    756   -362       N  
ATOM   3467  N   ILE B  72      66.302 -18.996  22.202  1.00 33.34           N  
ANISOU 3467  N   ILE B  72     4213   3535   4922     18    238   -405       N  
ATOM   3468  CA  ILE B  72      66.132 -17.543  22.335  1.00 35.78           C  
ANISOU 3468  CA  ILE B  72     4496   3829   5270     38    211   -429       C  
ATOM   3469  C   ILE B  72      66.269 -16.871  20.975  1.00 38.76           C  
ANISOU 3469  C   ILE B  72     4801   4218   5707     33    123   -409       C  
ATOM   3470  O   ILE B  72      65.459 -16.020  20.596  1.00 34.50           O  
ANISOU 3470  O   ILE B  72     4202   3661   5244     48    115   -422       O  
ATOM   3471  CB  ILE B  72      67.145 -16.963  23.341  1.00 37.00           C  
ANISOU 3471  CB  ILE B  72     4734   3981   5342     62    192   -445       C  
ATOM   3472  CG1 ILE B  72      66.934 -17.578  24.722  1.00 35.38           C  
ANISOU 3472  CG1 ILE B  72     4620   3762   5060     82    280   -462       C  
ATOM   3473  CG2 ILE B  72      67.028 -15.435  23.389  1.00 36.27           C  
ANISOU 3473  CG2 ILE B  72     4617   3864   5302     75    164   -474       C  
ATOM   3474  CD1 ILE B  72      65.596 -17.222  25.342  1.00 42.13           C  
ANISOU 3474  CD1 ILE B  72     5457   4581   5969     87    382   -495       C  
ATOM   3475  N   LEU B  73      67.295 -17.246  20.217  1.00 32.43           N  
ANISOU 3475  N   LEU B  73     4009   3446   4867     20     58   -376       N  
ATOM   3476  CA  LEU B  73      67.481 -16.660  18.891  1.00 33.96           C  
ANISOU 3476  CA  LEU B  73     4155   3648   5101     18    -14   -349       C  
ATOM   3477  C   LEU B  73      66.294 -16.960  17.985  1.00 36.07           C  
ANISOU 3477  C   LEU B  73     4347   3924   5436     21    -17   -348       C  
ATOM   3478  O   LEU B  73      65.810 -16.071  17.268  1.00 33.72           O  
ANISOU 3478  O   LEU B  73     4007   3616   5191     46    -58   -343       O  
ATOM   3479  CB  LEU B  73      68.782 -17.182  18.261  1.00 33.76           C  
ANISOU 3479  CB  LEU B  73     4153   3654   5020      0    -64   -318       C  
ATOM   3480  CG  LEU B  73      70.094 -16.883  18.999  1.00 39.01           C  
ANISOU 3480  CG  LEU B  73     4873   4323   5628      0    -81   -330       C  
ATOM   3481  CD1 LEU B  73      71.267 -17.525  18.261  1.00 38.10           C  
ANISOU 3481  CD1 LEU B  73     4760   4244   5473    -16   -125   -305       C  
ATOM   3482  CD2 LEU B  73      70.326 -15.387  19.160  1.00 37.91           C  
ANISOU 3482  CD2 LEU B  73     4732   4149   5523      3    -99   -347       C  
ATOM   3483  N   ASN B  74      65.810 -18.212  17.997  1.00 31.66           N  
ANISOU 3483  N   ASN B  74     3770   3379   4878      0     22   -359       N  
ATOM   3484  CA  ASN B  74      64.628 -18.548  17.213  1.00 34.63           C  
ANISOU 3484  CA  ASN B  74     4061   3768   5330     -2     17   -381       C  
ATOM   3485  C   ASN B  74      63.436 -17.698  17.638  1.00 35.36           C  
ANISOU 3485  C   ASN B  74     4096   3836   5503     25     48   -420       C  
ATOM   3486  O   ASN B  74      62.690 -17.183  16.796  1.00 33.77           O  
ANISOU 3486  O   ASN B  74     3820   3645   5366     55     -4   -432       O  
ATOM   3487  CB  ASN B  74      64.283 -20.037  17.373  1.00 35.37           C  
ANISOU 3487  CB  ASN B  74     4148   3867   5424    -40     77   -399       C  
ATOM   3488  CG  ASN B  74      65.250 -20.945  16.651  1.00 41.70           C  
ANISOU 3488  CG  ASN B  74     4984   4694   6164    -59     36   -367       C  
ATOM   3489  OD1 ASN B  74      66.044 -20.496  15.820  1.00 40.87           O  
ANISOU 3489  OD1 ASN B  74     4890   4613   6027    -45    -42   -334       O  
ATOM   3490  ND2 ASN B  74      65.182 -22.242  16.955  1.00 38.83           N  
ANISOU 3490  ND2 ASN B  74     4644   4321   5788    -90     97   -376       N  
ATOM   3491  N   ASN B  75      63.232 -17.556  18.944  1.00 32.20           N  
ANISOU 3491  N   ASN B  75     3732   3406   5098     23    133   -444       N  
ATOM   3492  CA  ASN B  75      62.062 -16.827  19.422  1.00 31.62           C  
ANISOU 3492  CA  ASN B  75     3601   3308   5106     49    179   -490       C  
ATOM   3493  C   ASN B  75      62.109 -15.363  19.018  1.00 42.51           C  
ANISOU 3493  C   ASN B  75     4968   4671   6511     98    110   -480       C  
ATOM   3494  O   ASN B  75      61.056 -14.733  18.864  1.00 38.01           O  
ANISOU 3494  O   ASN B  75     4324   4091   6027    135    109   -513       O  
ATOM   3495  CB  ASN B  75      61.955 -16.932  20.938  1.00 35.32           C  
ANISOU 3495  CB  ASN B  75     4132   3745   5543     40    291   -514       C  
ATOM   3496  CG  ASN B  75      61.515 -18.310  21.401  1.00 36.81           C  
ANISOU 3496  CG  ASN B  75     4327   3930   5730     -2    392   -529       C  
ATOM   3497  OD1 ASN B  75      61.154 -19.175  20.599  1.00 36.57           O  
ANISOU 3497  OD1 ASN B  75     4236   3918   5742    -32    380   -535       O  
ATOM   3498  ND2 ASN B  75      61.524 -18.507  22.700  1.00 34.94           N  
ANISOU 3498  ND2 ASN B  75     4172   3663   5442     -5    495   -539       N  
ATOM   3499  N   LEU B  76      63.307 -14.808  18.862  1.00 36.53           N  
ANISOU 3499  N   LEU B  76     4281   3907   5690    100     57   -439       N  
ATOM   3500  CA  LEU B  76      63.474 -13.419  18.452  1.00 40.54           C  
ANISOU 3500  CA  LEU B  76     4797   4384   6223    140      4   -422       C  
ATOM   3501  C   LEU B  76      63.503 -13.242  16.939  1.00 42.29           C  
ANISOU 3501  C   LEU B  76     4988   4623   6457    163    -85   -381       C  
ATOM   3502  O   LEU B  76      63.713 -12.121  16.469  1.00 44.54           O  
ANISOU 3502  O   LEU B  76     5296   4873   6755    198   -126   -354       O  
ATOM   3503  CB  LEU B  76      64.759 -12.839  19.054  1.00 33.25           C  
ANISOU 3503  CB  LEU B  76     3961   3436   5236    123      1   -410       C  
ATOM   3504  CG  LEU B  76      64.741 -12.690  20.579  1.00 36.81           C  
ANISOU 3504  CG  LEU B  76     4459   3866   5664    121     75   -457       C  
ATOM   3505  CD1 LEU B  76      66.131 -12.325  21.112  1.00 35.76           C  
ANISOU 3505  CD1 LEU B  76     4402   3724   5461    102     53   -458       C  
ATOM   3506  CD2 LEU B  76      63.721 -11.633  20.978  1.00 36.94           C  
ANISOU 3506  CD2 LEU B  76     4444   3837   5755    163    108   -494       C  
ATOM   3507  N   GLY B  77      63.304 -14.311  16.170  1.00 38.50           N  
ANISOU 3507  N   GLY B  77     4468   4190   5969    146   -111   -375       N  
ATOM   3508  CA  GLY B  77      63.241 -14.205  14.723  1.00 40.65           C  
ANISOU 3508  CA  GLY B  77     4718   4486   6242    177   -198   -342       C  
ATOM   3509  C   GLY B  77      64.567 -14.076  14.006  1.00 38.70           C  
ANISOU 3509  C   GLY B  77     4545   4240   5920    161   -238   -281       C  
ATOM   3510  O   GLY B  77      64.588 -13.623  12.860  1.00 39.86           O  
ANISOU 3510  O   GLY B  77     4700   4389   6056    199   -301   -243       O  
ATOM   3511  N   VAL B  78      65.676 -14.488  14.625  1.00 35.71           N  
ANISOU 3511  N   VAL B  78     4220   3862   5486    111   -203   -272       N  
ATOM   3512  CA  VAL B  78      66.985 -14.367  13.989  1.00 33.25           C  
ANISOU 3512  CA  VAL B  78     3964   3553   5116     90   -230   -225       C  
ATOM   3513  C   VAL B  78      67.086 -15.316  12.795  1.00 39.37           C  
ANISOU 3513  C   VAL B  78     4725   4377   5856     85   -273   -202       C  
ATOM   3514  O   VAL B  78      66.815 -16.518  12.904  1.00 38.89           O  
ANISOU 3514  O   VAL B  78     4636   4353   5788     62   -260   -228       O  
ATOM   3515  CB  VAL B  78      68.093 -14.641  15.015  1.00 34.68           C  
ANISOU 3515  CB  VAL B  78     4189   3732   5255     46   -192   -239       C  
ATOM   3516  CG1 VAL B  78      69.455 -14.792  14.315  1.00 32.98           C  
ANISOU 3516  CG1 VAL B  78     4008   3533   4991     18   -215   -204       C  
ATOM   3517  CG2 VAL B  78      68.133 -13.518  16.056  1.00 33.79           C  
ANISOU 3517  CG2 VAL B  78     4101   3569   5170     54   -162   -266       C  
ATOM   3518  N   ASP B  79      67.499 -14.781  11.646  1.00 35.92           N  
ANISOU 3518  N   ASP B  79     4318   3936   5393    106   -316   -154       N  
ATOM   3519  CA  ASP B  79      67.655 -15.554  10.413  1.00 37.95           C  
ANISOU 3519  CA  ASP B  79     4576   4239   5603    110   -359   -132       C  
ATOM   3520  C   ASP B  79      69.095 -15.963  10.123  1.00 37.93           C  
ANISOU 3520  C   ASP B  79     4622   4249   5540     66   -342   -103       C  
ATOM   3521  O   ASP B  79      69.324 -16.958   9.428  1.00 33.49           O  
ANISOU 3521  O   ASP B  79     4057   3731   4937     54   -359   -101       O  
ATOM   3522  CB  ASP B  79      67.149 -14.735   9.217  1.00 39.05           C  
ANISOU 3522  CB  ASP B  79     4732   4369   5737    175   -417    -94       C  
ATOM   3523  CG  ASP B  79      65.675 -14.417   9.310  1.00 47.30           C  
ANISOU 3523  CG  ASP B  79     5714   5414   6845    234   -452   -131       C  
ATOM   3524  OD1 ASP B  79      64.893 -15.359   9.554  1.00 52.07           O  
ANISOU 3524  OD1 ASP B  79     6243   6058   7481    222   -456   -189       O  
ATOM   3525  OD2 ASP B  79      65.301 -13.223   9.161  1.00 41.64           O  
ANISOU 3525  OD2 ASP B  79     5018   4651   6151    292   -469   -106       O  
ATOM   3526  N   ILE B  80      70.065 -15.205  10.613  1.00 34.40           N  
ANISOU 3526  N   ILE B  80     4212   3764   5093     41   -308    -88       N  
ATOM   3527  CA  ILE B  80      71.441 -15.319  10.135  1.00 32.41           C  
ANISOU 3527  CA  ILE B  80     3996   3520   4799      5   -292    -62       C  
ATOM   3528  C   ILE B  80      72.319 -14.558  11.116  1.00 35.72           C  
ANISOU 3528  C   ILE B  80     4427   3899   5244    -30   -255    -80       C  
ATOM   3529  O   ILE B  80      71.834 -13.646  11.796  1.00 34.93           O  
ANISOU 3529  O   ILE B  80     4329   3753   5189    -16   -244    -95       O  
ATOM   3530  CB  ILE B  80      71.539 -14.760   8.698  1.00 34.13           C  
ANISOU 3530  CB  ILE B  80     4257   3725   4986     32   -310     -3       C  
ATOM   3531  CG1 ILE B  80      72.877 -15.113   8.025  1.00 33.77           C  
ANISOU 3531  CG1 ILE B  80     4241   3697   4894     -6   -283     21       C  
ATOM   3532  CG2 ILE B  80      71.276 -13.250   8.677  1.00 32.77           C  
ANISOU 3532  CG2 ILE B  80     4122   3479   4850     60   -299     27       C  
ATOM   3533  CD1 ILE B  80      72.834 -14.877   6.500  1.00 33.11           C  
ANISOU 3533  CD1 ILE B  80     4212   3612   4755     29   -296     80       C  
ATOM   3534  N   ALA B  81      73.606 -14.908  11.205  1.00 32.93           N  
ANISOU 3534  N   ALA B  81     4078   3565   4870    -71   -237    -89       N  
ATOM   3535  CA  ALA B  81      74.532 -14.233  12.109  1.00 33.76           C  
ANISOU 3535  CA  ALA B  81     4182   3642   5004   -105   -212   -124       C  
ATOM   3536  C   ALA B  81      75.569 -13.438  11.326  1.00 36.23           C  
ANISOU 3536  C   ALA B  81     4513   3920   5331   -140   -181    -98       C  
ATOM   3537  O   ALA B  81      75.964 -13.822  10.222  1.00 36.13           O  
ANISOU 3537  O   ALA B  81     4514   3928   5287   -145   -173    -59       O  
ATOM   3538  CB  ALA B  81      75.244 -15.231  13.031  1.00 33.42           C  
ANISOU 3538  CB  ALA B  81     4116   3649   4934   -120   -219   -173       C  
ATOM   3539  N   ALA B  82      76.022 -12.324  11.913  1.00 35.71           N  
ANISOU 3539  N   ALA B  82     4451   3798   5319   -169   -154   -126       N  
ATOM   3540  CA  ALA B  82      77.060 -11.503  11.298  1.00 33.00           C  
ANISOU 3540  CA  ALA B  82     4121   3407   5008   -217   -105   -112       C  
ATOM   3541  C   ALA B  82      78.444 -12.075  11.631  1.00 34.69           C  
ANISOU 3541  C   ALA B  82     4284   3670   5227   -265    -99   -168       C  
ATOM   3542  O   ALA B  82      78.901 -12.001  12.780  1.00 37.19           O  
ANISOU 3542  O   ALA B  82     4564   3998   5569   -282   -117   -242       O  
ATOM   3543  CB  ALA B  82      76.938 -10.057  11.777  1.00 37.10           C  
ANISOU 3543  CB  ALA B  82     4664   3836   5597   -232    -74   -128       C  
ATOM   3544  N   ASN B  83      79.105 -12.663  10.626  1.00 35.61           N  
ANISOU 3544  N   ASN B  83     4397   3819   5315   -280    -77   -137       N  
ATOM   3545  CA  ASN B  83      80.531 -13.033  10.695  1.00 36.48           C  
ANISOU 3545  CA  ASN B  83     4451   3966   5445   -327    -58   -188       C  
ATOM   3546  C   ASN B  83      80.845 -14.021  11.817  1.00 34.20           C  
ANISOU 3546  C   ASN B  83     4111   3749   5134   -306   -118   -258       C  
ATOM   3547  O   ASN B  83      81.900 -13.954  12.449  1.00 40.21           O  
ANISOU 3547  O   ASN B  83     4815   4531   5932   -335   -126   -332       O  
ATOM   3548  CB  ASN B  83      81.399 -11.778  10.804  1.00 42.67           C  
ANISOU 3548  CB  ASN B  83     5217   4681   6314   -394      1   -224       C  
ATOM   3549  CG  ASN B  83      81.163 -10.844   9.643  1.00 48.70           C  
ANISOU 3549  CG  ASN B  83     6052   5361   7090   -410     76   -144       C  
ATOM   3550  OD1 ASN B  83      80.222 -10.055   9.655  1.00 49.38           O  
ANISOU 3550  OD1 ASN B  83     6196   5383   7183   -382     76   -104       O  
ATOM   3551  ND2 ASN B  83      81.977 -10.968   8.604  1.00 50.20           N  
ANISOU 3551  ND2 ASN B  83     6247   5551   7276   -444    142   -114       N  
ATOM   3552  N   THR B  84      79.929 -14.954  12.059  1.00 33.48           N  
ANISOU 3552  N   THR B  84     4041   3696   4983   -253   -162   -237       N  
ATOM   3553  CA  THR B  84      80.183 -16.072  12.957  1.00 32.87           C  
ANISOU 3553  CA  THR B  84     3941   3681   4867   -222   -208   -283       C  
ATOM   3554  C   THR B  84      79.217 -17.178  12.571  1.00 37.50           C  
ANISOU 3554  C   THR B  84     4560   4293   5395   -180   -222   -236       C  
ATOM   3555  O   THR B  84      78.326 -16.983  11.740  1.00 38.67           O  
ANISOU 3555  O   THR B  84     4737   4419   5538   -174   -210   -183       O  
ATOM   3556  CB  THR B  84      80.014 -15.678  14.435  1.00 40.70           C  
ANISOU 3556  CB  THR B  84     4931   4664   5868   -207   -239   -343       C  
ATOM   3557  OG1 THR B  84      80.411 -16.768  15.279  1.00 42.49           O  
ANISOU 3557  OG1 THR B  84     5151   4949   6044   -167   -281   -383       O  
ATOM   3558  CG2 THR B  84      78.561 -15.316  14.742  1.00 38.24           C  
ANISOU 3558  CG2 THR B  84     4665   4312   5551   -182   -235   -312       C  
ATOM   3559  N   VAL B  85      79.396 -18.341  13.189  1.00 33.79           N  
ANISOU 3559  N   VAL B  85     4087   3869   4882   -148   -250   -261       N  
ATOM   3560  CA  VAL B  85      78.470 -19.466  13.046  1.00 31.78           C  
ANISOU 3560  CA  VAL B  85     3863   3630   4583   -116   -256   -232       C  
ATOM   3561  C   VAL B  85      77.980 -19.827  14.436  1.00 33.00           C  
ANISOU 3561  C   VAL B  85     4041   3783   4714    -83   -269   -261       C  
ATOM   3562  O   VAL B  85      78.786 -20.148  15.318  1.00 32.98           O  
ANISOU 3562  O   VAL B  85     4038   3804   4688    -61   -291   -302       O  
ATOM   3563  CB  VAL B  85      79.128 -20.693  12.396  1.00 31.70           C  
ANISOU 3563  CB  VAL B  85     3845   3662   4536   -105   -258   -226       C  
ATOM   3564  CG1 VAL B  85      78.197 -21.935  12.528  1.00 31.72           C  
ANISOU 3564  CG1 VAL B  85     3882   3671   4500    -75   -259   -212       C  
ATOM   3565  CG2 VAL B  85      79.501 -20.418  10.956  1.00 35.23           C  
ANISOU 3565  CG2 VAL B  85     4283   4112   4992   -133   -233   -194       C  
ATOM   3566  N   ILE B  86      76.670 -19.778  14.636  1.00 33.21           N  
ANISOU 3566  N   ILE B  86     4090   3782   4745    -74   -254   -243       N  
ATOM   3567  CA  ILE B  86      76.071 -20.259  15.872  1.00 30.13           C  
ANISOU 3567  CA  ILE B  86     3735   3384   4327    -45   -244   -262       C  
ATOM   3568  C   ILE B  86      75.774 -21.737  15.645  1.00 31.12           C  
ANISOU 3568  C   ILE B  86     3883   3524   4417    -28   -230   -244       C  
ATOM   3569  O   ILE B  86      74.899 -22.085  14.845  1.00 32.56           O  
ANISOU 3569  O   ILE B  86     4054   3698   4618    -42   -215   -222       O  
ATOM   3570  CB  ILE B  86      74.802 -19.474  16.241  1.00 31.82           C  
ANISOU 3570  CB  ILE B  86     3954   3558   4577    -46   -221   -261       C  
ATOM   3571  CG1 ILE B  86      75.104 -17.965  16.380  1.00 30.76           C  
ANISOU 3571  CG1 ILE B  86     3804   3397   4486    -63   -231   -278       C  
ATOM   3572  CG2 ILE B  86      74.225 -20.005  17.554  1.00 36.38           C  
ANISOU 3572  CG2 ILE B  86     4576   4126   5122    -18   -192   -282       C  
ATOM   3573  CD1 ILE B  86      76.229 -17.662  17.335  1.00 36.78           C  
ANISOU 3573  CD1 ILE B  86     4572   4173   5230    -60   -253   -330       C  
ATOM   3574  N   TRP B  87      76.538 -22.610  16.299  1.00 31.02           N  
ANISOU 3574  N   TRP B  87     3901   3531   4353      4   -238   -259       N  
ATOM   3575  CA  TRP B  87      76.328 -24.043  16.112  1.00 31.38           C  
ANISOU 3575  CA  TRP B  87     3979   3577   4367     21   -216   -242       C  
ATOM   3576  C   TRP B  87      75.210 -24.518  17.026  1.00 31.19           C  
ANISOU 3576  C   TRP B  87     4008   3515   4330     33   -165   -239       C  
ATOM   3577  O   TRP B  87      75.206 -24.216  18.223  1.00 34.54           O  
ANISOU 3577  O   TRP B  87     4474   3928   4724     61   -156   -254       O  
ATOM   3578  CB  TRP B  87      77.613 -24.824  16.396  1.00 29.78           C  
ANISOU 3578  CB  TRP B  87     3795   3404   4114     63   -244   -255       C  
ATOM   3579  CG  TRP B  87      77.533 -26.282  15.952  1.00 31.29           C  
ANISOU 3579  CG  TRP B  87     4019   3588   4281     79   -220   -235       C  
ATOM   3580  CD1 TRP B  87      77.342 -27.368  16.752  1.00 33.29           C  
ANISOU 3580  CD1 TRP B  87     4348   3814   4486    121   -190   -227       C  
ATOM   3581  CD2 TRP B  87      77.633 -26.783  14.608  1.00 34.74           C  
ANISOU 3581  CD2 TRP B  87     4424   4038   4737     53   -219   -223       C  
ATOM   3582  NE1 TRP B  87      77.303 -28.516  15.994  1.00 33.31           N  
ANISOU 3582  NE1 TRP B  87     4363   3804   4488    118   -167   -213       N  
ATOM   3583  CE2 TRP B  87      77.491 -28.191  14.676  1.00 31.42           C  
ANISOU 3583  CE2 TRP B  87     4055   3594   4288     78   -189   -215       C  
ATOM   3584  CE3 TRP B  87      77.836 -26.179  13.357  1.00 33.73           C  
ANISOU 3584  CE3 TRP B  87     4240   3934   4643     15   -234   -218       C  
ATOM   3585  CZ2 TRP B  87      77.558 -29.009  13.542  1.00 33.12           C  
ANISOU 3585  CZ2 TRP B  87     4259   3814   4510     64   -181   -212       C  
ATOM   3586  CZ3 TRP B  87      77.914 -26.980  12.235  1.00 30.77           C  
ANISOU 3586  CZ3 TRP B  87     3860   3569   4263      7   -227   -210       C  
ATOM   3587  CH2 TRP B  87      77.759 -28.390  12.331  1.00 31.47           C  
ANISOU 3587  CH2 TRP B  87     3992   3638   4327     29   -203   -212       C  
ATOM   3588  N   ASP B  88      74.270 -25.277  16.466  1.00 32.93           N  
ANISOU 3588  N   ASP B  88     4225   3713   4574     10   -126   -225       N  
ATOM   3589  CA  ASP B  88      73.120 -25.779  17.211  1.00 36.20           C  
ANISOU 3589  CA  ASP B  88     4677   4083   4996      7    -56   -226       C  
ATOM   3590  C   ASP B  88      73.465 -27.180  17.700  1.00 36.46           C  
ANISOU 3590  C   ASP B  88     4787   4094   4973     38    -18   -215       C  
ATOM   3591  O   ASP B  88      73.384 -28.146  16.946  1.00 34.11           O  
ANISOU 3591  O   ASP B  88     4486   3787   4688     22     -4   -209       O  
ATOM   3592  CB  ASP B  88      71.889 -25.763  16.314  1.00 32.59           C  
ANISOU 3592  CB  ASP B  88     4158   3614   4611    -38    -37   -233       C  
ATOM   3593  CG  ASP B  88      70.618 -26.195  17.034  1.00 39.60           C  
ANISOU 3593  CG  ASP B  88     5061   4455   5531    -54     47   -248       C  
ATOM   3594  OD1 ASP B  88      70.692 -26.875  18.085  1.00 43.22           O  
ANISOU 3594  OD1 ASP B  88     5599   4879   5944    -33    108   -240       O  
ATOM   3595  OD2 ASP B  88      69.540 -25.852  16.519  1.00 40.35           O  
ANISOU 3595  OD2 ASP B  88     5088   4546   5698    -84     54   -268       O  
ATOM   3596  N   TYR B  89      73.849 -27.302  18.969  1.00 34.73           N  
ANISOU 3596  N   TYR B  89     4648   3862   4688     88     -2   -212       N  
ATOM   3597  CA  TYR B  89      74.296 -28.598  19.463  1.00 37.37           C  
ANISOU 3597  CA  TYR B  89     5074   4170   4956    135     28   -192       C  
ATOM   3598  C   TYR B  89      73.140 -29.569  19.684  1.00 44.22           C  
ANISOU 3598  C   TYR B  89     5992   4966   5844    108    137   -179       C  
ATOM   3599  O   TYR B  89      73.378 -30.770  19.787  1.00 42.39           O  
ANISOU 3599  O   TYR B  89     5833   4696   5576    134    176   -159       O  
ATOM   3600  CB  TYR B  89      75.094 -28.429  20.760  1.00 39.33           C  
ANISOU 3600  CB  TYR B  89     5404   4429   5111    214      1   -195       C  
ATOM   3601  CG  TYR B  89      76.511 -27.908  20.548  1.00 34.41           C  
ANISOU 3601  CG  TYR B  89     4733   3873   4466    249   -106   -219       C  
ATOM   3602  CD1 TYR B  89      76.761 -26.547  20.399  1.00 33.48           C  
ANISOU 3602  CD1 TYR B  89     4538   3795   4390    220   -159   -252       C  
ATOM   3603  CD2 TYR B  89      77.594 -28.785  20.492  1.00 35.81           C  
ANISOU 3603  CD2 TYR B  89     4942   4071   4595    310   -146   -216       C  
ATOM   3604  CE1 TYR B  89      78.069 -26.076  20.215  1.00 31.19           C  
ANISOU 3604  CE1 TYR B  89     4196   3561   4096    241   -244   -285       C  
ATOM   3605  CE2 TYR B  89      78.889 -28.328  20.299  1.00 37.67           C  
ANISOU 3605  CE2 TYR B  89     5117   4371   4826    339   -238   -251       C  
ATOM   3606  CZ  TYR B  89      79.124 -26.979  20.165  1.00 35.99           C  
ANISOU 3606  CZ  TYR B  89     4821   4195   4660    299   -283   -287       C  
ATOM   3607  OH  TYR B  89      80.417 -26.529  19.981  1.00 38.34           O  
ANISOU 3607  OH  TYR B  89     5048   4551   4967    317   -362   -332       O  
ATOM   3608  N   LYS B  90      71.902 -29.086  19.772  1.00 38.61           N  
ANISOU 3608  N   LYS B  90     5242   4230   5196     57    194   -194       N  
ATOM   3609  CA  LYS B  90      70.771 -30.007  19.881  1.00 42.02           C  
ANISOU 3609  CA  LYS B  90     5699   4594   5672     16    306   -195       C  
ATOM   3610  C   LYS B  90      70.520 -30.717  18.558  1.00 43.41           C  
ANISOU 3610  C   LYS B  90     5807   4769   5916    -35    296   -211       C  
ATOM   3611  O   LYS B  90      70.125 -31.884  18.536  1.00 45.47           O  
ANISOU 3611  O   LYS B  90     6111   4971   6194    -57    375   -211       O  
ATOM   3612  CB  LYS B  90      69.509 -29.259  20.317  1.00 44.33           C  
ANISOU 3612  CB  LYS B  90     5948   4867   6027    -24    369   -220       C  
ATOM   3613  CG  LYS B  90      69.645 -28.453  21.601  1.00 57.25           C  
ANISOU 3613  CG  LYS B  90     7650   6505   7600     22    383   -214       C  
ATOM   3614  CD  LYS B  90      69.301 -29.240  22.847  1.00 61.83           C  
ANISOU 3614  CD  LYS B  90     8363   7014   8116     48    506   -191       C  
ATOM   3615  CE  LYS B  90      69.206 -28.311  24.062  1.00 64.69           C  
ANISOU 3615  CE  LYS B  90     8779   7380   8419     89    525   -198       C  
ATOM   3616  NZ  LYS B  90      70.417 -27.441  24.214  1.00 54.26           N  
ANISOU 3616  NZ  LYS B  90     7458   6128   7030    147    393   -204       N  
ATOM   3617  N   ARG B  91      70.724 -30.020  17.448  1.00 32.88           N  
ANISOU 3617  N   ARG B  91     4376   3497   4620    -54    205   -228       N  
ATOM   3618  CA  ARG B  91      70.538 -30.583  16.117  1.00 33.96           C  
ANISOU 3618  CA  ARG B  91     4451   3646   4807    -93    179   -249       C  
ATOM   3619  C   ARG B  91      71.846 -31.036  15.481  1.00 39.57           C  
ANISOU 3619  C   ARG B  91     5184   4389   5462    -58    116   -232       C  
ATOM   3620  O   ARG B  91      71.811 -31.636  14.404  1.00 39.68           O  
ANISOU 3620  O   ARG B  91     5164   4410   5502    -84     99   -250       O  
ATOM   3621  CB  ARG B  91      69.855 -29.550  15.195  1.00 35.53           C  
ANISOU 3621  CB  ARG B  91     4538   3890   5072   -126    120   -277       C  
ATOM   3622  CG  ARG B  91      68.376 -29.245  15.511  1.00 39.44           C  
ANISOU 3622  CG  ARG B  91     4978   4358   5651   -166    177   -313       C  
ATOM   3623  CD  ARG B  91      67.909 -27.978  14.755  1.00 40.20           C  
ANISOU 3623  CD  ARG B  91     4977   4504   5792   -168     99   -330       C  
ATOM   3624  NE  ARG B  91      68.195 -28.102  13.330  1.00 46.72           N  
ANISOU 3624  NE  ARG B  91     5760   5374   6618   -172     19   -338       N  
ATOM   3625  CZ  ARG B  91      69.068 -27.367  12.654  1.00 39.28           C  
ANISOU 3625  CZ  ARG B  91     4818   4477   5631   -144    -59   -308       C  
ATOM   3626  NH1 ARG B  91      69.244 -27.619  11.364  1.00 40.86           N  
ANISOU 3626  NH1 ARG B  91     4992   4712   5822   -147   -115   -316       N  
ATOM   3627  NH2 ARG B  91      69.739 -26.366  13.243  1.00 36.84           N  
ANISOU 3627  NH2 ARG B  91     4533   4176   5288   -116    -76   -276       N  
ATOM   3628  N   ASP B  92      72.991 -30.755  16.110  1.00 35.80           N  
ANISOU 3628  N   ASP B  92     4755   3935   4913      0     79   -206       N  
ATOM   3629  CA  ASP B  92      74.294 -31.077  15.531  1.00 33.49           C  
ANISOU 3629  CA  ASP B  92     4465   3680   4578     37     19   -199       C  
ATOM   3630  C   ASP B  92      74.420 -30.471  14.132  1.00 33.65           C  
ANISOU 3630  C   ASP B  92     4396   3755   4636      1    -41   -213       C  
ATOM   3631  O   ASP B  92      74.777 -31.151  13.163  1.00 35.91           O  
ANISOU 3631  O   ASP B  92     4671   4052   4922     -4    -54   -220       O  
ATOM   3632  CB  ASP B  92      74.494 -32.605  15.507  1.00 43.39           C  
ANISOU 3632  CB  ASP B  92     5791   4885   5810     57     67   -192       C  
ATOM   3633  CG  ASP B  92      75.948 -33.018  15.477  1.00 65.99           C  
ANISOU 3633  CG  ASP B  92     8685   7777   8612    126     17   -181       C  
ATOM   3634  OD1 ASP B  92      76.837 -32.137  15.490  1.00 70.26           O  
ANISOU 3634  OD1 ASP B  92     9183   8379   9133    151    -52   -185       O  
ATOM   3635  OD2 ASP B  92      76.201 -34.243  15.443  1.00 76.58           O  
ANISOU 3635  OD2 ASP B  92    10090   9075   9933    154     52   -174       O  
ATOM   3636  N   ALA B  93      74.077 -29.184  14.017  1.00 29.41           N  
ANISOU 3636  N   ALA B  93     3803   3244   4127    -19    -73   -216       N  
ATOM   3637  CA  ALA B  93      74.008 -28.542  12.714  1.00 29.14           C  
ANISOU 3637  CA  ALA B  93     3702   3250   4122    -47   -120   -220       C  
ATOM   3638  C   ALA B  93      74.065 -27.034  12.913  1.00 31.45           C  
ANISOU 3638  C   ALA B  93     3960   3561   4427    -48   -152   -212       C  
ATOM   3639  O   ALA B  93      73.837 -26.549  14.025  1.00 32.32           O  
ANISOU 3639  O   ALA B  93     4090   3653   4538    -37   -134   -213       O  
ATOM   3640  CB  ALA B  93      72.727 -28.948  11.965  1.00 31.26           C  
ANISOU 3640  CB  ALA B  93     3934   3503   4440    -86   -105   -245       C  
ATOM   3641  N   PRO B  94      74.363 -26.268  11.861  1.00 35.82           N  
ANISOU 3641  N   PRO B  94     4475   4147   4989    -59   -193   -203       N  
ATOM   3642  CA  PRO B  94      74.340 -24.802  11.997  1.00 36.20           C  
ANISOU 3642  CA  PRO B  94     4499   4197   5058    -63   -213   -193       C  
ATOM   3643  C   PRO B  94      72.953 -24.337  12.403  1.00 32.55           C  
ANISOU 3643  C   PRO B  94     4020   3708   4641    -70   -198   -203       C  
ATOM   3644  O   PRO B  94      71.946 -24.876  11.943  1.00 30.82           O  
ANISOU 3644  O   PRO B  94     3780   3483   4448    -82   -191   -217       O  
ATOM   3645  CB  PRO B  94      74.703 -24.299  10.592  1.00 35.23           C  
ANISOU 3645  CB  PRO B  94     4354   4100   4931    -72   -243   -175       C  
ATOM   3646  CG  PRO B  94      75.422 -25.450   9.942  1.00 38.64           C  
ANISOU 3646  CG  PRO B  94     4799   4556   5327    -68   -241   -179       C  
ATOM   3647  CD  PRO B  94      74.736 -26.685  10.499  1.00 33.77           C  
ANISOU 3647  CD  PRO B  94     4202   3915   4713    -66   -214   -200       C  
ATOM   3648  N   ALA B  95      72.896 -23.325  13.271  1.00 30.27           N  
ANISOU 3648  N   ALA B  95     3734   3403   4367    -64   -194   -204       N  
ATOM   3649  CA  ALA B  95      71.575 -22.804  13.627  1.00 34.86           C  
ANISOU 3649  CA  ALA B  95     4290   3957   4996    -66   -176   -217       C  
ATOM   3650  C   ALA B  95      70.899 -22.117  12.448  1.00 37.57           C  
ANISOU 3650  C   ALA B  95     4590   4310   5375    -66   -215   -208       C  
ATOM   3651  O   ALA B  95      69.662 -22.056  12.407  1.00 35.16           O  
ANISOU 3651  O   ALA B  95     4247   3995   5118    -64   -210   -229       O  
ATOM   3652  CB  ALA B  95      71.674 -21.840  14.812  1.00 32.57           C  
ANISOU 3652  CB  ALA B  95     4019   3645   4710    -55   -160   -226       C  
ATOM   3653  N   HIS B  96      71.682 -21.629  11.481  1.00 34.66           N  
ANISOU 3653  N   HIS B  96     4226   3959   4982    -63   -251   -180       N  
ATOM   3654  CA  HIS B  96      71.193 -20.824  10.367  1.00 36.38           C  
ANISOU 3654  CA  HIS B  96     4429   4181   5213    -47   -290   -160       C  
ATOM   3655  C   HIS B  96      71.738 -21.371   9.054  1.00 34.22           C  
ANISOU 3655  C   HIS B  96     4169   3941   4893    -47   -315   -142       C  
ATOM   3656  O   HIS B  96      72.890 -21.791   8.989  1.00 42.11           O  
ANISOU 3656  O   HIS B  96     5190   4954   5856    -62   -299   -133       O  
ATOM   3657  CB  HIS B  96      71.606 -19.358  10.583  1.00 31.94           C  
ANISOU 3657  CB  HIS B  96     3882   3587   4665    -40   -289   -135       C  
ATOM   3658  CG  HIS B  96      71.189 -18.843  11.926  1.00 31.68           C  
ANISOU 3658  CG  HIS B  96     3844   3523   4670    -39   -262   -161       C  
ATOM   3659  ND1 HIS B  96      72.091 -18.538  12.922  1.00 35.16           N  
ANISOU 3659  ND1 HIS B  96     4307   3951   5101    -53   -240   -173       N  
ATOM   3660  CD2 HIS B  96      69.956 -18.686  12.468  1.00 33.08           C  
ANISOU 3660  CD2 HIS B  96     3994   3684   4893    -24   -251   -186       C  
ATOM   3661  CE1 HIS B  96      71.432 -18.162  14.006  1.00 36.05           C  
ANISOU 3661  CE1 HIS B  96     4419   4038   5242    -43   -217   -200       C  
ATOM   3662  NE2 HIS B  96      70.135 -18.250  13.759  1.00 32.74           N  
ANISOU 3662  NE2 HIS B  96     3968   3614   4858    -28   -216   -206       N  
ATOM   3663  N  AILE B  97      70.910 -21.337   8.008  0.44 43.46           N  
ANISOU 3663  N  AILE B  97     5324   5128   6061    -25   -357   -142       N  
ATOM   3664  N  BILE B  97      70.911 -21.331   8.007  0.56 43.13           N  
ANISOU 3664  N  BILE B  97     5283   5086   6019    -24   -357   -141       N  
ATOM   3665  CA AILE B  97      71.265 -22.011   6.761  0.44 51.03           C  
ANISOU 3665  CA AILE B  97     6301   6122   6965    -20   -382   -136       C  
ATOM   3666  CA BILE B  97      71.266 -22.003   6.760  0.56 51.23           C  
ANISOU 3666  CA BILE B  97     6327   6148   6991    -20   -382   -135       C  
ATOM   3667  C  AILE B  97      72.324 -21.241   5.976  0.44 46.94           C  
ANISOU 3667  C  AILE B  97     5833   5604   6399    -13   -376    -83       C  
ATOM   3668  C  BILE B  97      72.357 -21.243   6.014  0.56 47.23           C  
ANISOU 3668  C  BILE B  97     5870   5640   6436    -14   -374    -83       C  
ATOM   3669  O  AILE B  97      73.153 -21.850   5.288  0.44 41.80           O  
ANISOU 3669  O  AILE B  97     5206   4978   5699    -22   -365    -76       O  
ATOM   3670  O  BILE B  97      73.235 -21.853   5.389  0.56 41.63           O  
ANISOU 3670  O  BILE B  97     5184   4955   5680    -26   -360    -76       O  
ATOM   3671  CB AILE B  97      70.004 -22.249   5.910  0.44 57.57           C  
ANISOU 3671  CB AILE B  97     7098   6976   7801      9   -440   -165       C  
ATOM   3672  CB BILE B  97      70.013 -22.200   5.885  0.56 57.65           C  
ANISOU 3672  CB BILE B  97     7109   6986   7810     10   -441   -163       C  
ATOM   3673  CG1AILE B  97      70.338 -23.100   4.684  0.44 59.39           C  
ANISOU 3673  CG1AILE B  97     7351   7246   7967     14   -467   -174       C  
ATOM   3674  CG1BILE B  97      68.947 -21.155   6.231  0.56 57.89           C  
ANISOU 3674  CG1BILE B  97     7107   6994   7894     43   -466   -166       C  
ATOM   3675  CG2AILE B  97      69.371 -20.929   5.493  0.44 57.94           C  
ANISOU 3675  CG2AILE B  97     7148   7011   7856     58   -482   -137       C  
ATOM   3676  CG2BILE B  97      69.468 -23.621   6.034  0.56 60.28           C  
ANISOU 3676  CG2BILE B  97     7402   7334   8166    -16   -435   -226       C  
ATOM   3677  CD1AILE B  97      70.951 -24.448   5.026  0.44 63.29           C  
ANISOU 3677  CD1AILE B  97     7846   7745   8455    -26   -425   -202       C  
ATOM   3678  CD1BILE B  97      68.963 -19.933   5.331  0.56 56.97           C  
ANISOU 3678  CD1BILE B  97     7033   6871   7742     96   -506   -114       C  
ATOM   3679  N   SER B  98      72.319 -19.913   6.049  1.00 38.43           N  
ANISOU 3679  N   SER B  98     4774   4492   5337      1   -372    -47       N  
ATOM   3680  CA  SER B  98      73.273 -19.086   5.318  1.00 35.46           C  
ANISOU 3680  CA  SER B  98     4450   4098   4925      0   -347      5       C  
ATOM   3681  C   SER B  98      74.225 -18.382   6.272  1.00 33.34           C  
ANISOU 3681  C   SER B  98     4179   3792   4697    -38   -296      7       C  
ATOM   3682  O   SER B  98      74.039 -18.373   7.492  1.00 34.63           O  
ANISOU 3682  O   SER B  98     4310   3943   4906    -51   -291    -26       O  
ATOM   3683  CB  SER B  98      72.549 -18.054   4.448  1.00 39.66           C  
ANISOU 3683  CB  SER B  98     5023   4607   5438     53   -380     48       C  
ATOM   3684  OG  SER B  98      71.855 -18.729   3.419  1.00 41.96           O  
ANISOU 3684  OG  SER B  98     5320   4945   5678     94   -438     38       O  
ATOM   3685  N   THR B  99      75.277 -17.798   5.701  1.00 31.45           N  
ANISOU 3685  N   THR B  99     3975   3535   4441    -58   -253     41       N  
ATOM   3686  CA  THR B  99      76.253 -17.089   6.509  1.00 29.46           C  
ANISOU 3686  CA  THR B  99     3709   3248   4238   -101   -206     29       C  
ATOM   3687  C   THR B  99      76.602 -15.743   5.881  1.00 33.10           C  
ANISOU 3687  C   THR B  99     4221   3647   4708   -109   -161     79       C  
ATOM   3688  O   THR B  99      76.235 -15.428   4.746  1.00 36.42           O  
ANISOU 3688  O   THR B  99     4702   4056   5082    -75   -161    133       O  
ATOM   3689  CB  THR B  99      77.537 -17.912   6.703  1.00 35.55           C  
ANISOU 3689  CB  THR B  99     4448   4057   5002   -137   -179     -4       C  
ATOM   3690  OG1 THR B  99      78.045 -18.298   5.423  1.00 36.23           O  
ANISOU 3690  OG1 THR B  99     4564   4166   5036   -137   -155     26       O  
ATOM   3691  CG2 THR B  99      77.260 -19.165   7.546  1.00 35.38           C  
ANISOU 3691  CG2 THR B  99     4391   4078   4975   -126   -214    -50       C  
ATOM   3692  N   ILE B 100      77.349 -14.957   6.654  1.00 32.90           N  
ANISOU 3692  N   ILE B 100     4176   3580   4744   -154   -119     57       N  
ATOM   3693  CA  ILE B 100      77.850 -13.655   6.246  1.00 31.16           C  
ANISOU 3693  CA  ILE B 100     4000   3285   4555   -180    -55     93       C  
ATOM   3694  C   ILE B 100      79.327 -13.642   6.605  1.00 35.93           C  
ANISOU 3694  C   ILE B 100     4556   3892   5205   -250      1     47       C  
ATOM   3695  O   ILE B 100      79.673 -13.673   7.791  1.00 37.36           O  
ANISOU 3695  O   ILE B 100     4677   4084   5436   -275    -17    -20       O  
ATOM   3696  CB  ILE B 100      77.118 -12.507   6.943  1.00 35.20           C  
ANISOU 3696  CB  ILE B 100     4528   3727   5121   -165    -63     94       C  
ATOM   3697  CG1 ILE B 100      75.635 -12.516   6.561  1.00 37.51           C  
ANISOU 3697  CG1 ILE B 100     4851   4022   5377    -87   -124    130       C  
ATOM   3698  CG2 ILE B 100      77.768 -11.165   6.576  1.00 35.59           C  
ANISOU 3698  CG2 ILE B 100     4627   3682   5213   -203     19    126       C  
ATOM   3699  CD1 ILE B 100      74.780 -11.571   7.406  1.00 38.69           C  
ANISOU 3699  CD1 ILE B 100     5000   4115   5585    -62   -139    117       C  
ATOM   3700  N   GLY B 101      80.192 -13.630   5.592  1.00 35.31           N  
ANISOU 3700  N   GLY B 101     4501   3808   5107   -279     68     77       N  
ATOM   3701  CA  GLY B 101      81.630 -13.553   5.816  1.00 36.64           C  
ANISOU 3701  CA  GLY B 101     4610   3978   5334   -349    131     25       C  
ATOM   3702  C   GLY B 101      82.264 -14.751   6.506  1.00 43.43           C  
ANISOU 3702  C   GLY B 101     5382   4923   6196   -352     86    -48       C  
ATOM   3703  O   GLY B 101      83.272 -14.585   7.201  1.00 43.65           O  
ANISOU 3703  O   GLY B 101     5336   4958   6292   -398    103   -119       O  
ATOM   3704  N   VAL B 102      81.727 -15.961   6.318  1.00 35.16           N  
ANISOU 3704  N   VAL B 102     4340   3939   5078   -302     30    -39       N  
ATOM   3705  CA  VAL B 102      82.224 -17.161   6.990  1.00 35.56           C  
ANISOU 3705  CA  VAL B 102     4327   4061   5124   -290    -14   -100       C  
ATOM   3706  C   VAL B 102      82.786 -18.180   6.000  1.00 40.55           C  
ANISOU 3706  C   VAL B 102     4959   4742   5705   -281     10    -90       C  
ATOM   3707  O   VAL B 102      83.883 -18.710   6.195  1.00 41.91           O  
ANISOU 3707  O   VAL B 102     5069   4952   5901   -296     24   -141       O  
ATOM   3708  CB  VAL B 102      81.129 -17.813   7.865  1.00 39.72           C  
ANISOU 3708  CB  VAL B 102     4859   4609   5622   -241    -92   -111       C  
ATOM   3709  CG1 VAL B 102      81.657 -19.111   8.478  1.00 40.37           C  
ANISOU 3709  CG1 VAL B 102     4899   4753   5686   -219   -128   -160       C  
ATOM   3710  CG2 VAL B 102      80.675 -16.854   8.960  1.00 39.96           C  
ANISOU 3710  CG2 VAL B 102     4885   4597   5702   -247   -111   -133       C  
ATOM   3711  N   CYS B 103      82.031 -18.493   4.952  1.00 38.78           N  
ANISOU 3711  N   CYS B 103     4803   4521   5411   -250      8    -32       N  
ATOM   3712  CA  CYS B 103      82.285 -19.677   4.140  1.00 37.67           C  
ANISOU 3712  CA  CYS B 103     4671   4433   5210   -228     11    -32       C  
ATOM   3713  C   CYS B 103      81.772 -19.426   2.730  1.00 38.73           C  
ANISOU 3713  C   CYS B 103     4892   4552   5272   -209     38     34       C  
ATOM   3714  O   CYS B 103      80.614 -19.034   2.553  1.00 39.89           O  
ANISOU 3714  O   CYS B 103     5089   4678   5391   -176     -5     71       O  
ATOM   3715  CB  CYS B 103      81.610 -20.906   4.754  1.00 42.02           C  
ANISOU 3715  CB  CYS B 103     5207   5024   5736   -186    -64    -62       C  
ATOM   3716  SG  CYS B 103      81.438 -22.349   3.640  1.00 44.94           S  
ANISOU 3716  SG  CYS B 103     5611   5442   6024   -152    -73    -58       S  
ATOM   3717  N   SER B 104      82.634 -19.645   1.731  1.00 35.34           N  
ANISOU 3717  N   SER B 104     4480   4136   4809   -222    108     45       N  
ATOM   3718  CA  SER B 104      82.285 -19.276   0.362  1.00 38.78           C  
ANISOU 3718  CA  SER B 104     5017   4554   5162   -200    145    112       C  
ATOM   3719  C   SER B 104      81.131 -20.096  -0.209  1.00 41.23           C  
ANISOU 3719  C   SER B 104     5376   4904   5386   -137     62    122       C  
ATOM   3720  O   SER B 104      80.498 -19.646  -1.170  1.00 39.20           O  
ANISOU 3720  O   SER B 104     5208   4632   5054    -98     56    176       O  
ATOM   3721  CB  SER B 104      83.509 -19.393  -0.552  1.00 48.52           C  
ANISOU 3721  CB  SER B 104     6263   5796   6377   -230    253    116       C  
ATOM   3722  OG  SER B 104      83.901 -20.748  -0.706  1.00 60.04           O  
ANISOU 3722  OG  SER B 104     7684   7321   7808   -213    235     68       O  
ATOM   3723  N   MET B 105      80.833 -21.279   0.340  1.00 37.59           N  
ANISOU 3723  N   MET B 105     4862   4489   4931   -122     -3     68       N  
ATOM   3724  CA  MET B 105      79.682 -22.021  -0.173  1.00 37.27           C  
ANISOU 3724  CA  MET B 105     4856   4479   4826    -73    -79     64       C  
ATOM   3725  C   MET B 105      78.360 -21.537   0.415  1.00 38.65           C  
ANISOU 3725  C   MET B 105     5025   4633   5028    -50   -154     70       C  
ATOM   3726  O   MET B 105      77.321 -21.695  -0.226  1.00 38.57           O  
ANISOU 3726  O   MET B 105     5049   4638   4966     -5   -214     75       O  
ATOM   3727  CB  MET B 105      79.825 -23.525   0.095  1.00 34.17           C  
ANISOU 3727  CB  MET B 105     4419   4131   4434    -70   -106      3       C  
ATOM   3728  CG  MET B 105      80.509 -24.304  -1.040  1.00 41.53           C  
ANISOU 3728  CG  MET B 105     5386   5098   5295    -60    -65     -7       C  
ATOM   3729  SD  MET B 105      79.660 -24.203  -2.631  1.00 42.86           S  
ANISOU 3729  SD  MET B 105     5659   5285   5342     -9    -95     26       S  
ATOM   3730  CE  MET B 105      77.984 -24.661  -2.165  1.00 47.11           C  
ANISOU 3730  CE  MET B 105     6170   5833   5898     20   -217    -12       C  
ATOM   3731  N   THR B 106      78.363 -20.985   1.631  1.00 34.39           N  
ANISOU 3731  N   THR B 106     4436   4061   4569    -75   -154     60       N  
ATOM   3732  CA  THR B 106      77.120 -20.603   2.293  1.00 34.54           C  
ANISOU 3732  CA  THR B 106     4441   4062   4622    -53   -214     56       C  
ATOM   3733  C   THR B 106      76.932 -19.098   2.429  1.00 37.65           C  
ANISOU 3733  C   THR B 106     4863   4397   5045    -51   -196    101       C  
ATOM   3734  O   THR B 106      75.820 -18.661   2.755  1.00 33.75           O  
ANISOU 3734  O   THR B 106     4366   3886   4573    -20   -246    104       O  
ATOM   3735  CB  THR B 106      77.035 -21.229   3.690  1.00 33.73           C  
ANISOU 3735  CB  THR B 106     4270   3964   4581    -73   -232      4       C  
ATOM   3736  OG1 THR B 106      78.168 -20.823   4.457  1.00 33.46           O  
ANISOU 3736  OG1 THR B 106     4207   3914   4592   -110   -186     -6       O  
ATOM   3737  CG2 THR B 106      76.994 -22.780   3.585  1.00 36.56           C  
ANISOU 3737  CG2 THR B 106     4612   4366   4914    -67   -251    -39       C  
ATOM   3738  N   ASP B 107      77.972 -18.300   2.198  1.00 34.40           N  
ANISOU 3738  N   ASP B 107     4476   3949   4644    -84   -121    132       N  
ATOM   3739  CA  ASP B 107      77.846 -16.855   2.344  1.00 37.11           C  
ANISOU 3739  CA  ASP B 107     4856   4222   5024    -88    -91    173       C  
ATOM   3740  C   ASP B 107      76.824 -16.300   1.369  1.00 36.95           C  
ANISOU 3740  C   ASP B 107     4918   4181   4939    -20   -126    232       C  
ATOM   3741  O   ASP B 107      76.846 -16.615   0.179  1.00 35.87           O  
ANISOU 3741  O   ASP B 107     4846   4070   4715     13   -124    264       O  
ATOM   3742  CB  ASP B 107      79.185 -16.166   2.090  1.00 36.98           C  
ANISOU 3742  CB  ASP B 107     4855   4163   5033   -144     14    192       C  
ATOM   3743  CG  ASP B 107      80.088 -16.149   3.306  1.00 40.47           C  
ANISOU 3743  CG  ASP B 107     5207   4604   5566   -206     38    128       C  
ATOM   3744  OD1 ASP B 107      79.704 -16.681   4.374  1.00 40.80           O  
ANISOU 3744  OD1 ASP B 107     5189   4674   5637   -198    -25     78       O  
ATOM   3745  OD2 ASP B 107      81.203 -15.596   3.172  1.00 44.29           O  
ANISOU 3745  OD2 ASP B 107     5682   5056   6091   -260    122    125       O  
ATOM   3746  N   ILE B 108      75.948 -15.430   1.861  1.00 33.56           N  
ANISOU 3746  N   ILE B 108     4494   3708   4550      9   -160    245       N  
ATOM   3747  CA  ILE B 108      75.166 -14.595   0.956  1.00 35.59           C  
ANISOU 3747  CA  ILE B 108     4841   3928   4752     83   -184    310       C  
ATOM   3748  C   ILE B 108      75.774 -13.213   0.802  1.00 39.11           C  
ANISOU 3748  C   ILE B 108     5362   4277   5221     64    -94    372       C  
ATOM   3749  O   ILE B 108      75.319 -12.442  -0.058  1.00 38.41           O  
ANISOU 3749  O   ILE B 108     5376   4143   5075    130    -94    442       O  
ATOM   3750  CB  ILE B 108      73.705 -14.468   1.424  1.00 38.10           C  
ANISOU 3750  CB  ILE B 108     5123   4254   5099    144   -280    287       C  
ATOM   3751  CG1 ILE B 108      73.640 -13.783   2.784  1.00 44.73           C  
ANISOU 3751  CG1 ILE B 108     5909   5042   6043    108   -259    260       C  
ATOM   3752  CG2 ILE B 108      73.052 -15.851   1.483  1.00 41.68           C  
ANISOU 3752  CG2 ILE B 108     5504   4794   5538    155   -356    222       C  
ATOM   3753  CD1 ILE B 108      72.234 -13.522   3.234  1.00 40.33           C  
ANISOU 3753  CD1 ILE B 108     5317   4484   5522    169   -334    238       C  
ATOM   3754  N   ALA B 109      76.794 -12.889   1.594  1.00 34.29           N  
ANISOU 3754  N   ALA B 109     4706   3631   4692    -21    -17    344       N  
ATOM   3755  CA  ALA B 109      77.437 -11.584   1.647  1.00 36.24           C  
ANISOU 3755  CA  ALA B 109     5004   3776   4991    -61     80    382       C  
ATOM   3756  C   ALA B 109      78.715 -11.738   2.455  1.00 40.62           C  
ANISOU 3756  C   ALA B 109     5471   4333   5629   -162    145    317       C  
ATOM   3757  O   ALA B 109      78.878 -12.704   3.209  1.00 37.50           O  
ANISOU 3757  O   ALA B 109     4982   4012   5255   -183     97    246       O  
ATOM   3758  CB  ALA B 109      76.525 -10.529   2.287  1.00 38.45           C  
ANISOU 3758  CB  ALA B 109     5299   3985   5325    -24     48    392       C  
ATOM   3759  N   LYS B 110      79.622 -10.779   2.284  1.00 40.99           N  
ANISOU 3759  N   LYS B 110     5552   4297   5724   -222    256    337       N  
ATOM   3760  CA  LYS B 110      80.806 -10.711   3.129  1.00 37.12           C  
ANISOU 3760  CA  LYS B 110     4966   3803   5335   -318    312    260       C  
ATOM   3761  C   LYS B 110      80.594  -9.836   4.357  1.00 40.05           C  
ANISOU 3761  C   LYS B 110     5297   4116   5804   -344    296    212       C  
ATOM   3762  O   LYS B 110      81.192 -10.098   5.407  1.00 41.08           O  
ANISOU 3762  O   LYS B 110     5325   4280   6002   -394    278    122       O  
ATOM   3763  CB  LYS B 110      82.000 -10.198   2.315  1.00 45.46           C  
ANISOU 3763  CB  LYS B 110     6060   4802   6411   -386    454    287       C  
ATOM   3764  CG  LYS B 110      82.386 -11.154   1.201  1.00 56.41           C  
ANISOU 3764  CG  LYS B 110     7475   6254   7703   -368    480    317       C  
ATOM   3765  CD  LYS B 110      83.703 -10.784   0.545  1.00 78.69           C  
ANISOU 3765  CD  LYS B 110    10309   9030  10559   -448    635    324       C  
ATOM   3766  CE  LYS B 110      84.161 -11.893  -0.401  1.00 89.74           C  
ANISOU 3766  CE  LYS B 110    11716  10511  11871   -431    657    332       C  
ATOM   3767  NZ  LYS B 110      85.354 -11.500  -1.204  1.00 96.19           N  
ANISOU 3767  NZ  LYS B 110    12560  11277  12710   -503    827    350       N  
ATOM   3768  N   LYS B 111      79.752  -8.811   4.253  1.00 36.75           N  
ANISOU 3768  N   LYS B 111     4961   3614   5390   -302    298    266       N  
ATOM   3769  CA  LYS B 111      79.455  -7.914   5.356  1.00 39.56           C  
ANISOU 3769  CA  LYS B 111     5291   3905   5834   -318    287    223       C  
ATOM   3770  C   LYS B 111      77.952  -7.735   5.487  1.00 35.92           C  
ANISOU 3770  C   LYS B 111     4872   3439   5338   -221    200    258       C  
ATOM   3771  O   LYS B 111      77.234  -7.731   4.483  1.00 38.84           O  
ANISOU 3771  O   LYS B 111     5325   3804   5629   -144    180    337       O  
ATOM   3772  CB  LYS B 111      80.110  -6.540   5.147  1.00 39.08           C  
ANISOU 3772  CB  LYS B 111     5289   3710   5849   -380    409    244       C  
ATOM   3773  CG  LYS B 111      81.618  -6.608   4.902  1.00 49.35           C  
ANISOU 3773  CG  LYS B 111     6543   5006   7202   -484    514    206       C  
ATOM   3774  CD  LYS B 111      82.213  -5.214   4.709  1.00 54.59           C  
ANISOU 3774  CD  LYS B 111     7264   5521   7955   -556    651    222       C  
ATOM   3775  CE  LYS B 111      83.626  -5.279   4.142  1.00 61.74           C  
ANISOU 3775  CE  LYS B 111     8137   6416   8906   -656    779    201       C  
ATOM   3776  NZ  LYS B 111      84.124  -3.909   3.796  1.00 68.91           N  
ANISOU 3776  NZ  LYS B 111     9122   7161   9899   -728    935    230       N  
ATOM   3777  N   PRO B 112      77.450  -7.550   6.712  1.00 39.47           N  
ANISOU 3777  N   PRO B 112     5264   3889   5845   -217    149    194       N  
ATOM   3778  CA  PRO B 112      75.994  -7.411   6.897  1.00 43.12           C  
ANISOU 3778  CA  PRO B 112     5747   4350   6286   -125     72    215       C  
ATOM   3779  C   PRO B 112      75.423  -6.122   6.319  1.00 50.94           C  
ANISOU 3779  C   PRO B 112     6845   5226   7285    -72    106    289       C  
ATOM   3780  O   PRO B 112      74.196  -5.993   6.253  1.00 51.02           O  
ANISOU 3780  O   PRO B 112     6874   5238   7274     20     39    313       O  
ATOM   3781  CB  PRO B 112      75.820  -7.449   8.424  1.00 44.43           C  
ANISOU 3781  CB  PRO B 112     5831   4535   6517   -149     36    122       C  
ATOM   3782  CG  PRO B 112      77.188  -7.735   8.999  1.00 50.28           C  
ANISOU 3782  CG  PRO B 112     6508   5301   7297   -242     74     51       C  
ATOM   3783  CD  PRO B 112      78.192  -7.354   7.966  1.00 42.62           C  
ANISOU 3783  CD  PRO B 112     5581   4283   6330   -292    163     96       C  
ATOM   3784  N   THR B 113      76.262  -5.175   5.900  1.00 51.89           N  
ANISOU 3784  N   THR B 113     7033   5243   7440   -123    211    324       N  
ATOM   3785  CA  THR B 113      75.777  -3.945   5.283  1.00 57.48           C  
ANISOU 3785  CA  THR B 113     7866   5826   8149    -66    256    407       C  
ATOM   3786  C   THR B 113      75.340  -4.134   3.841  1.00 58.65           C  
ANISOU 3786  C   THR B 113     8120   5983   8180     24    242    514       C  
ATOM   3787  O   THR B 113      74.724  -3.223   3.277  1.00 54.45           O  
ANISOU 3787  O   THR B 113     7703   5360   7625    106    253    592       O  
ATOM   3788  CB  THR B 113      76.852  -2.861   5.324  1.00 55.96           C  
ANISOU 3788  CB  THR B 113     7719   5504   8041   -160    391    408       C  
ATOM   3789  OG1 THR B 113      78.056  -3.355   4.719  1.00 59.03           O  
ANISOU 3789  OG1 THR B 113     8096   5921   8413   -241    468    411       O  
ATOM   3790  CG2 THR B 113      77.126  -2.452   6.748  1.00 57.57           C  
ANISOU 3790  CG2 THR B 113     7832   5683   8360   -231    392    298       C  
ATOM   3791  N   GLU B 114      75.643  -5.274   3.231  1.00 46.06           N  
ANISOU 3791  N   GLU B 114     6499   4495   6507     19    216    516       N  
ATOM   3792  CA  GLU B 114      75.248  -5.503   1.850  1.00 44.29           C  
ANISOU 3792  CA  GLU B 114     6380   4289   6158    108    195    607       C  
ATOM   3793  C   GLU B 114      73.727  -5.605   1.753  1.00 45.60           C  
ANISOU 3793  C   GLU B 114     6550   4496   6279    239     63    619       C  
ATOM   3794  O   GLU B 114      73.057  -6.079   2.676  1.00 51.13           O  
ANISOU 3794  O   GLU B 114     7139   5260   7028    246    -20    544       O  
ATOM   3795  CB  GLU B 114      75.939  -6.760   1.315  1.00 50.17           C  
ANISOU 3795  CB  GLU B 114     7084   5142   6837     67    196    589       C  
ATOM   3796  CG  GLU B 114      77.464  -6.602   1.237  1.00 48.44           C  
ANISOU 3796  CG  GLU B 114     6861   4880   6663    -54    335    580       C  
ATOM   3797  CD  GLU B 114      78.170  -7.869   0.787  1.00 53.40           C  
ANISOU 3797  CD  GLU B 114     7438   5617   7236    -90    337    552       C  
ATOM   3798  OE1 GLU B 114      79.161  -8.270   1.441  1.00 52.27           O  
ANISOU 3798  OE1 GLU B 114     7191   5505   7166   -187    377    477       O  
ATOM   3799  OE2 GLU B 114      77.722  -8.478  -0.212  1.00 53.21           O  
ANISOU 3799  OE2 GLU B 114     7474   5650   7094    -16    292    599       O  
ATOM   3800  N  ATHR B 115      73.188  -5.163   0.610  0.43 46.23           N  
ANISOU 3800  N  ATHR B 115     6762   4540   6265    348     46    712       N  
ATOM   3801  N  BTHR B 115      73.188  -5.153   0.614  0.57 46.09           N  
ANISOU 3801  N  BTHR B 115     6744   4520   6247    348     46    712       N  
ATOM   3802  CA ATHR B 115      71.741  -4.993   0.475  0.43 48.74           C  
ANISOU 3802  CA ATHR B 115     7090   4877   6553    487    -78    723       C  
ATOM   3803  CA BTHR B 115      71.741  -4.991   0.475  0.57 48.80           C  
ANISOU 3803  CA BTHR B 115     7097   4884   6560    487    -78    723       C  
ATOM   3804  C  ATHR B 115      70.981  -6.300   0.651  0.43 47.62           C  
ANISOU 3804  C  ATHR B 115     6821   4884   6388    514   -207    646       C  
ATOM   3805  C  BTHR B 115      70.989  -6.302   0.676  0.57 47.76           C  
ANISOU 3805  C  BTHR B 115     6836   4902   6408    511   -206    644       C  
ATOM   3806  O  ATHR B 115      69.819  -6.284   1.071  0.43 46.95           O  
ANISOU 3806  O  ATHR B 115     6673   4828   6338    588   -304    607       O  
ATOM   3807  O  BTHR B 115      69.853  -6.293   1.162  0.57 46.54           O  
ANISOU 3807  O  BTHR B 115     6614   4776   6294    579   -300    602       O  
ATOM   3808  CB ATHR B 115      71.401  -4.378  -0.885  0.43 51.21           C  
ANISOU 3808  CB ATHR B 115     7577   5134   6746    612    -82    837       C  
ATOM   3809  CB BTHR B 115      71.410  -4.388  -0.896  0.57 51.42           C  
ANISOU 3809  CB BTHR B 115     7604   5161   6771    611    -82    838       C  
ATOM   3810  OG1ATHR B 115      71.970  -5.179  -1.930  0.43 49.81           O  
ANISOU 3810  OG1ATHR B 115     7451   5024   6451    604    -68    869       O  
ATOM   3811  OG1BTHR B 115      72.132  -3.161  -1.066  0.57 54.96           O  
ANISOU 3811  OG1BTHR B 115     8184   5453   7245    580     59    915       O  
ATOM   3812  CG2ATHR B 115      71.934  -2.955  -0.982  0.43 54.36           C  
ANISOU 3812  CG2ATHR B 115     8114   5360   7180    599     50    918       C  
ATOM   3813  CG2BTHR B 115      69.920  -4.102  -1.025  0.57 45.98           C  
ANISOU 3813  CG2BTHR B 115     6920   4490   6061    768   -219    842       C  
ATOM   3814  N   ILE B 116      71.607  -7.437   0.335  1.00 46.03           N  
ANISOU 3814  N   ILE B 116     6578   4773   6138    453   -203    619       N  
ATOM   3815  CA  ILE B 116      70.921  -8.723   0.482  1.00 39.89           C  
ANISOU 3815  CA  ILE B 116     5686   4124   5345    470   -312    543       C  
ATOM   3816  C   ILE B 116      70.565  -9.007   1.937  1.00 42.74           C  
ANISOU 3816  C   ILE B 116     5907   4509   5821    415   -333    451       C  
ATOM   3817  O   ILE B 116      69.623  -9.762   2.216  1.00 43.76           O  
ANISOU 3817  O   ILE B 116     5946   4718   5965    448   -423    390       O  
ATOM   3818  CB  ILE B 116      71.770  -9.867  -0.112  1.00 49.11           C  
ANISOU 3818  CB  ILE B 116     6847   5370   6442    411   -289    532       C  
ATOM   3819  CG1 ILE B 116      70.913 -11.116  -0.286  1.00 55.34           C  
ANISOU 3819  CG1 ILE B 116     7551   6277   7196    451   -407    466       C  
ATOM   3820  CG2 ILE B 116      72.951 -10.198   0.797  1.00 43.73           C  
ANISOU 3820  CG2 ILE B 116     6092   4685   5838    278   -199    484       C  
ATOM   3821  CD1 ILE B 116      70.893 -11.646  -1.695  1.00 64.91           C  
ANISOU 3821  CD1 ILE B 116     8845   7545   8274    514   -447    499       C  
ATOM   3822  N   CYS B 117      71.289  -8.407   2.887  1.00 42.95           N  
ANISOU 3822  N   CYS B 117     5918   4467   5933    332   -248    436       N  
ATOM   3823  CA  CYS B 117      71.035  -8.679   4.300  1.00 44.44           C  
ANISOU 3823  CA  CYS B 117     5992   4679   6215    283   -261    350       C  
ATOM   3824  C   CYS B 117      69.929  -7.820   4.885  1.00 48.46           C  
ANISOU 3824  C   CYS B 117     6488   5137   6787    351   -297    337       C  
ATOM   3825  O   CYS B 117      69.452  -8.125   5.982  1.00 45.31           O  
ANISOU 3825  O   CYS B 117     5995   4767   6452    331   -317    265       O  
ATOM   3826  CB  CYS B 117      72.293  -8.448   5.130  1.00 43.99           C  
ANISOU 3826  CB  CYS B 117     5915   4581   6219    170   -168    320       C  
ATOM   3827  SG  CYS B 117      73.672  -9.499   4.657  1.00 47.52           S  
ANISOU 3827  SG  CYS B 117     6348   5092   6616     85   -121    314       S  
ATOM   3828  N   ALA B 118      69.552  -6.736   4.209  1.00 42.88           N  
ANISOU 3828  N   ALA B 118     5881   4350   6062    434   -296    408       N  
ATOM   3829  CA  ALA B 118      68.566  -5.818   4.769  1.00 45.79           C  
ANISOU 3829  CA  ALA B 118     6241   4658   6498    505   -323    396       C  
ATOM   3830  C   ALA B 118      67.263  -6.500   5.165  1.00 46.33           C  
ANISOU 3830  C   ALA B 118     6196   4815   6593    564   -422    326       C  
ATOM   3831  O   ALA B 118      66.768  -6.211   6.267  1.00 45.63           O  
ANISOU 3831  O   ALA B 118     6040   4707   6591    555   -414    268       O  
ATOM   3832  CB  ALA B 118      68.299  -4.663   3.785  1.00 47.36           C  
ANISOU 3832  CB  ALA B 118     6580   4760   6654    610   -320    494       C  
ATOM   3833  N   PRO B 119      66.673  -7.403   4.369  1.00 46.14           N  
ANISOU 3833  N   PRO B 119     6140   4886   6506    618   -509    318       N  
ATOM   3834  CA  PRO B 119      65.420  -8.044   4.796  1.00 56.51           C  
ANISOU 3834  CA  PRO B 119     7328   6277   7867    660   -591    237       C  
ATOM   3835  C   PRO B 119      65.584  -9.084   5.892  1.00 50.55           C  
ANISOU 3835  C   PRO B 119     6462   5580   7163    555   -559    153       C  
ATOM   3836  O   PRO B 119      64.572  -9.523   6.452  1.00 47.41           O  
ANISOU 3836  O   PRO B 119     5959   5228   6825    573   -596     81       O  
ATOM   3837  CB  PRO B 119      64.907  -8.712   3.511  1.00 54.44           C  
ANISOU 3837  CB  PRO B 119     7073   6095   7516    738   -691    247       C  
ATOM   3838  CG  PRO B 119      65.674  -8.078   2.404  1.00 62.36           C  
ANISOU 3838  CG  PRO B 119     8232   7043   8420    774   -666    352       C  
ATOM   3839  CD  PRO B 119      67.007  -7.781   2.986  1.00 53.50           C  
ANISOU 3839  CD  PRO B 119     7153   5852   7322    654   -539    379       C  
ATOM   3840  N   LEU B 120      66.806  -9.508   6.198  1.00 45.48           N  
ANISOU 3840  N   LEU B 120     5841   4939   6502    451   -489    159       N  
ATOM   3841  CA  LEU B 120      67.031 -10.584   7.151  1.00 41.99           C  
ANISOU 3841  CA  LEU B 120     5313   4553   6088    366   -464     90       C  
ATOM   3842  C   LEU B 120      67.301 -10.034   8.545  1.00 42.66           C  
ANISOU 3842  C   LEU B 120     5382   4585   6244    315   -398     54       C  
ATOM   3843  O   LEU B 120      67.988  -9.022   8.703  1.00 41.42           O  
ANISOU 3843  O   LEU B 120     5288   4350   6100    298   -349     86       O  
ATOM   3844  CB  LEU B 120      68.217 -11.440   6.716  1.00 37.34           C  
ANISOU 3844  CB  LEU B 120     4750   4002   5433    295   -436    107       C  
ATOM   3845  CG  LEU B 120      68.125 -12.061   5.325  1.00 39.50           C  
ANISOU 3845  CG  LEU B 120     5053   4331   5622    337   -492    137       C  
ATOM   3846  CD1 LEU B 120      69.412 -12.787   5.052  1.00 39.65           C  
ANISOU 3846  CD1 LEU B 120     5099   4376   5590    262   -444    151       C  
ATOM   3847  CD2 LEU B 120      66.933 -13.009   5.266  1.00 41.20           C  
ANISOU 3847  CD2 LEU B 120     5178   4623   5853    372   -568     72       C  
ATOM   3848  N   THR B 121      66.796 -10.729   9.560  1.00 35.45           N  
ANISOU 3848  N   THR B 121     4387   3712   5372    288   -391    -15       N  
ATOM   3849  CA  THR B 121      67.125 -10.369  10.943  1.00 37.54           C  
ANISOU 3849  CA  THR B 121     4643   3937   5682    240   -330    -56       C  
ATOM   3850  C   THR B 121      68.501 -10.940  11.285  1.00 37.66           C  
ANISOU 3850  C   THR B 121     4680   3971   5658    156   -291    -60       C  
ATOM   3851  O   THR B 121      68.667 -12.140  11.523  1.00 36.97           O  
ANISOU 3851  O   THR B 121     4557   3946   5543    121   -292    -87       O  
ATOM   3852  CB  THR B 121      66.026 -10.843  11.889  1.00 38.99           C  
ANISOU 3852  CB  THR B 121     4748   4150   5917    251   -325   -124       C  
ATOM   3853  OG1 THR B 121      64.835 -10.096  11.609  1.00 39.24           O  
ANISOU 3853  OG1 THR B 121     4753   4157   6000    335   -360   -128       O  
ATOM   3854  CG2 THR B 121      66.416 -10.614  13.348  1.00 32.41           C  
ANISOU 3854  CG2 THR B 121     3919   3287   5107    205   -261   -169       C  
ATOM   3855  N   VAL B 122      69.497 -10.064  11.296  1.00 36.80           N  
ANISOU 3855  N   VAL B 122     4626   3804   5553    125   -255    -36       N  
ATOM   3856  CA  VAL B 122      70.893 -10.436  11.479  1.00 33.37           C  
ANISOU 3856  CA  VAL B 122     4203   3384   5092     51   -223    -44       C  
ATOM   3857  C   VAL B 122      71.217 -10.385  12.965  1.00 36.80           C  
ANISOU 3857  C   VAL B 122     4615   3813   5554     14   -197   -113       C  
ATOM   3858  O   VAL B 122      70.885  -9.408  13.646  1.00 36.55           O  
ANISOU 3858  O   VAL B 122     4594   3722   5571     26   -178   -137       O  
ATOM   3859  CB  VAL B 122      71.808  -9.481  10.686  1.00 35.83           C  
ANISOU 3859  CB  VAL B 122     4579   3631   5405     31   -188      7       C  
ATOM   3860  CG1 VAL B 122      73.291  -9.777  10.936  1.00 34.78           C  
ANISOU 3860  CG1 VAL B 122     4437   3513   5265    -50   -152    -18       C  
ATOM   3861  CG2 VAL B 122      71.457  -9.542   9.193  1.00 37.15           C  
ANISOU 3861  CG2 VAL B 122     4790   3805   5522     82   -214     81       C  
ATOM   3862  N   PHE B 123      71.895 -11.414  13.464  1.00 33.78           N  
ANISOU 3862  N   PHE B 123     4209   3490   5137    -25   -197   -145       N  
ATOM   3863  CA  PHE B 123      72.373 -11.425  14.842  1.00 32.79           C  
ANISOU 3863  CA  PHE B 123     4076   3368   5016    -52   -182   -210       C  
ATOM   3864  C   PHE B 123      73.732 -10.733  14.948  1.00 36.69           C  
ANISOU 3864  C   PHE B 123     4581   3830   5528   -103   -164   -231       C  
ATOM   3865  O   PHE B 123      74.680 -11.099  14.240  1.00 35.51           O  
ANISOU 3865  O   PHE B 123     4427   3706   5361   -135   -163   -212       O  
ATOM   3866  CB  PHE B 123      72.478 -12.860  15.362  1.00 31.22           C  
ANISOU 3866  CB  PHE B 123     3857   3241   4764    -56   -192   -234       C  
ATOM   3867  CG  PHE B 123      73.141 -12.966  16.709  1.00 31.40           C  
ANISOU 3867  CG  PHE B 123     3887   3275   4767    -70   -186   -296       C  
ATOM   3868  CD1 PHE B 123      72.477 -12.560  17.856  1.00 39.32           C  
ANISOU 3868  CD1 PHE B 123     4904   4255   5781    -49   -168   -339       C  
ATOM   3869  CD2 PHE B 123      74.424 -13.462  16.826  1.00 38.23           C  
ANISOU 3869  CD2 PHE B 123     4747   4178   5600    -97   -202   -317       C  
ATOM   3870  CE1 PHE B 123      73.087 -12.659  19.103  1.00 39.20           C  
ANISOU 3870  CE1 PHE B 123     4909   4255   5730    -52   -170   -399       C  
ATOM   3871  CE2 PHE B 123      75.036 -13.566  18.067  1.00 38.98           C  
ANISOU 3871  CE2 PHE B 123     4851   4291   5667    -95   -214   -380       C  
ATOM   3872  CZ  PHE B 123      74.354 -13.175  19.207  1.00 37.89           C  
ANISOU 3872  CZ  PHE B 123     4740   4132   5527    -71   -200   -420       C  
ATOM   3873  N   PHE B 124      73.825  -9.756  15.860  1.00 31.54           N  
ANISOU 3873  N   PHE B 124     3940   3127   4918   -113   -148   -282       N  
ATOM   3874  CA  PHE B 124      75.021  -8.954  16.100  1.00 30.42           C  
ANISOU 3874  CA  PHE B 124     3797   2945   4815   -168   -130   -324       C  
ATOM   3875  C   PHE B 124      75.498  -9.144  17.538  1.00 39.65           C  
ANISOU 3875  C   PHE B 124     4950   4148   5969   -178   -150   -417       C  
ATOM   3876  O   PHE B 124      74.691  -9.207  18.470  1.00 33.88           O  
ANISOU 3876  O   PHE B 124     4233   3420   5219   -140   -154   -446       O  
ATOM   3877  CB  PHE B 124      74.754  -7.439  15.861  1.00 31.48           C  
ANISOU 3877  CB  PHE B 124     3969   2971   5022   -173    -91   -312       C  
ATOM   3878  CG  PHE B 124      74.389  -7.092  14.434  1.00 34.36           C  
ANISOU 3878  CG  PHE B 124     4371   3292   5392   -151    -71   -217       C  
ATOM   3879  CD1 PHE B 124      75.375  -6.938  13.468  1.00 35.74           C  
ANISOU 3879  CD1 PHE B 124     4560   3447   5572   -198    -37   -181       C  
ATOM   3880  CD2 PHE B 124      73.065  -6.935  14.058  1.00 34.68           C  
ANISOU 3880  CD2 PHE B 124     4433   3316   5429    -79    -87   -169       C  
ATOM   3881  CE1 PHE B 124      75.050  -6.611  12.157  1.00 37.17           C  
ANISOU 3881  CE1 PHE B 124     4797   3587   5741   -169    -16    -89       C  
ATOM   3882  CE2 PHE B 124      72.725  -6.609  12.745  1.00 34.00           C  
ANISOU 3882  CE2 PHE B 124     4391   3194   5332    -43    -82    -84       C  
ATOM   3883  CZ  PHE B 124      73.714  -6.444  11.793  1.00 36.77           C  
ANISOU 3883  CZ  PHE B 124     4776   3521   5673    -85    -46    -39       C  
ATOM   3884  N   ASP B 125      76.814  -9.173  17.723  1.00 41.53           N  
ANISOU 3884  N   ASP B 125     5158   4406   6214   -225   -161   -469       N  
ATOM   3885  CA  ASP B 125      77.443  -9.462  19.014  1.00 40.13           C  
ANISOU 3885  CA  ASP B 125     4964   4276   6007   -223   -200   -563       C  
ATOM   3886  C   ASP B 125      78.272  -8.243  19.416  1.00 37.32           C  
ANISOU 3886  C   ASP B 125     4590   3863   5726   -277   -190   -646       C  
ATOM   3887  O   ASP B 125      79.360  -8.019  18.874  1.00 42.08           O  
ANISOU 3887  O   ASP B 125     5151   4460   6377   -335   -179   -665       O  
ATOM   3888  CB  ASP B 125      78.284 -10.738  18.890  1.00 40.76           C  
ANISOU 3888  CB  ASP B 125     5012   4445   6030   -219   -237   -566       C  
ATOM   3889  CG  ASP B 125      78.871 -11.216  20.211  1.00 49.40           C  
ANISOU 3889  CG  ASP B 125     6102   5598   7070   -192   -291   -654       C  
ATOM   3890  OD1 ASP B 125      78.759 -10.514  21.237  1.00 42.57           O  
ANISOU 3890  OD1 ASP B 125     5255   4710   6211   -185   -302   -724       O  
ATOM   3891  OD2 ASP B 125      79.466 -12.324  20.215  1.00 44.59           O  
ANISOU 3891  OD2 ASP B 125     5476   5061   6407   -170   -326   -654       O  
ATOM   3892  N   GLY B 126      77.759  -7.448  20.363  1.00 37.67           N  
ANISOU 3892  N   GLY B 126     4663   3862   5786   -263   -187   -701       N  
ATOM   3893  CA  GLY B 126      78.448  -6.248  20.826  1.00 37.44           C  
ANISOU 3893  CA  GLY B 126     4620   3771   5836   -316   -177   -793       C  
ATOM   3894  C   GLY B 126      79.806  -6.494  21.456  1.00 44.30           C  
ANISOU 3894  C   GLY B 126     5429   4700   6702   -348   -231   -902       C  
ATOM   3895  O   GLY B 126      80.559  -5.535  21.666  1.00 45.36           O  
ANISOU 3895  O   GLY B 126     5531   4784   6919   -409   -222   -990       O  
ATOM   3896  N   ARG B 127      80.134  -7.745  21.778  1.00 37.12           N  
ANISOU 3896  N   ARG B 127     4504   3894   5705   -306   -288   -907       N  
ATOM   3897  CA  ARG B 127      81.481  -8.048  22.237  1.00 43.54           C  
ANISOU 3897  CA  ARG B 127     5250   4775   6518   -324   -351  -1008       C  
ATOM   3898  C   ARG B 127      82.504  -7.959  21.113  1.00 47.16           C  
ANISOU 3898  C   ARG B 127     5634   5225   7059   -398   -319   -998       C  
ATOM   3899  O   ARG B 127      83.700  -7.877  21.389  1.00 51.81           O  
ANISOU 3899  O   ARG B 127     6145   5850   7692   -433   -357  -1102       O  
ATOM   3900  CB  ARG B 127      81.513  -9.440  22.871  1.00 45.77           C  
ANISOU 3900  CB  ARG B 127     5551   5162   6677   -243   -418  -1005       C  
ATOM   3901  CG  ARG B 127      80.642  -9.553  24.124  1.00 43.30           C  
ANISOU 3901  CG  ARG B 127     5319   4860   6274   -171   -440  -1028       C  
ATOM   3902  CD  ARG B 127      80.496 -11.006  24.536  1.00 40.11           C  
ANISOU 3902  CD  ARG B 127     4958   4538   5745    -91   -476   -989       C  
ATOM   3903  NE  ARG B 127      79.860 -11.794  23.482  1.00 40.52           N  
ANISOU 3903  NE  ARG B 127     5018   4586   5791    -90   -427   -865       N  
ATOM   3904  CZ  ARG B 127      79.527 -13.080  23.611  1.00 40.85           C  
ANISOU 3904  CZ  ARG B 127     5104   4677   5743    -32   -432   -810       C  
ATOM   3905  NH1 ARG B 127      79.762 -13.724  24.750  1.00 37.20           N  
ANISOU 3905  NH1 ARG B 127     4690   4265   5178     38   -481   -856       N  
ATOM   3906  NH2 ARG B 127      78.947 -13.716  22.610  1.00 36.39           N  
ANISOU 3906  NH2 ARG B 127     4539   4104   5185    -40   -389   -713       N  
ATOM   3907  N   VAL B 128      82.071  -7.980  19.856  1.00 40.28           N  
ANISOU 3907  N   VAL B 128     4784   4311   6211   -417   -251   -882       N  
ATOM   3908  CA  VAL B 128      82.981  -7.903  18.717  1.00 43.65           C  
ANISOU 3908  CA  VAL B 128     5156   4723   6705   -485   -201   -860       C  
ATOM   3909  C   VAL B 128      83.048  -6.454  18.250  1.00 45.59           C  
ANISOU 3909  C   VAL B 128     5413   4845   7064   -562   -117   -865       C  
ATOM   3910  O   VAL B 128      82.009  -5.806  18.068  1.00 41.04           O  
ANISOU 3910  O   VAL B 128     4912   4189   6491   -543    -78   -800       O  
ATOM   3911  CB  VAL B 128      82.528  -8.816  17.566  1.00 42.03           C  
ANISOU 3911  CB  VAL B 128     4981   4544   6443   -455   -175   -732       C  
ATOM   3912  CG1 VAL B 128      83.496  -8.684  16.389  1.00 44.98           C  
ANISOU 3912  CG1 VAL B 128     5309   4901   6882   -525   -110   -712       C  
ATOM   3913  CG2 VAL B 128      82.387 -10.272  18.028  1.00 48.66           C  
ANISOU 3913  CG2 VAL B 128     5821   5490   7176   -380   -246   -724       C  
ATOM   3914  N   ASP B 129      84.267  -5.953  18.034  1.00 41.60           N  
ANISOU 3914  N   ASP B 129     4832   4318   6657   -647    -84   -943       N  
ATOM   3915  CA  ASP B 129      84.452  -4.574  17.589  1.00 48.75           C  
ANISOU 3915  CA  ASP B 129     5751   5091   7681   -732     14   -952       C  
ATOM   3916  C   ASP B 129      83.628  -4.268  16.342  1.00 43.94           C  
ANISOU 3916  C   ASP B 129     5238   4398   7060   -722    102   -797       C  
ATOM   3917  O   ASP B 129      83.639  -5.029  15.372  1.00 45.01           O  
ANISOU 3917  O   ASP B 129     5384   4574   7144   -703    121   -705       O  
ATOM   3918  CB  ASP B 129      85.932  -4.307  17.303  1.00 59.29           C  
ANISOU 3918  CB  ASP B 129     6979   6422   9126   -833     56  -1046       C  
ATOM   3919  CG  ASP B 129      86.739  -4.092  18.563  1.00 78.74           C  
ANISOU 3919  CG  ASP B 129     9348   8932  11640   -858    -24  -1228       C  
ATOM   3920  OD1 ASP B 129      87.830  -4.689  18.688  1.00 88.66           O  
ANISOU 3920  OD1 ASP B 129    10494  10278  12917   -876    -69  -1316       O  
ATOM   3921  OD2 ASP B 129      86.271  -3.330  19.436  1.00 89.33           O  
ANISOU 3921  OD2 ASP B 129    10725  10223  12995   -852    -48  -1289       O  
ATOM   3922  N   GLY B 130      82.903  -3.146  16.383  1.00 42.65           N  
ANISOU 3922  N   GLY B 130     5149   4115   6939   -724    150   -771       N  
ATOM   3923  CA  GLY B 130      82.164  -2.664  15.235  1.00 44.48           C  
ANISOU 3923  CA  GLY B 130     5480   4254   7167   -706    230   -633       C  
ATOM   3924  C   GLY B 130      80.747  -3.188  15.090  1.00 38.82           C  
ANISOU 3924  C   GLY B 130     4832   3570   6346   -596    181   -532       C  
ATOM   3925  O   GLY B 130      79.992  -2.654  14.270  1.00 43.51           O  
ANISOU 3925  O   GLY B 130     5512   4083   6936   -562    229   -428       O  
ATOM   3926  N   GLN B 131      80.354  -4.221  15.835  1.00 38.04           N  
ANISOU 3926  N   GLN B 131     4702   3586   6167   -536     89   -558       N  
ATOM   3927  CA  GLN B 131      79.056  -4.824  15.543  1.00 36.93           C  
ANISOU 3927  CA  GLN B 131     4611   3479   5941   -445     55   -465       C  
ATOM   3928  C   GLN B 131      77.880  -4.019  16.111  1.00 35.43           C  
ANISOU 3928  C   GLN B 131     4474   3220   5766   -394     53   -462       C  
ATOM   3929  O   GLN B 131      76.782  -4.069  15.544  1.00 40.05           O  
ANISOU 3929  O   GLN B 131     5109   3791   6319   -327     51   -375       O  
ATOM   3930  CB  GLN B 131      79.031  -6.274  16.032  1.00 37.08           C  
ANISOU 3930  CB  GLN B 131     4585   3631   5871   -404    -22   -484       C  
ATOM   3931  CG  GLN B 131      80.025  -7.171  15.233  1.00 38.40           C  
ANISOU 3931  CG  GLN B 131     4708   3866   6016   -436    -18   -464       C  
ATOM   3932  CD  GLN B 131      79.426  -8.490  14.783  1.00 54.44           C  
ANISOU 3932  CD  GLN B 131     6748   5982   7954   -375    -58   -396       C  
ATOM   3933  OE1 GLN B 131      78.533  -9.039  15.430  1.00 47.49           O  
ANISOU 3933  OE1 GLN B 131     5881   5142   7022   -317   -104   -396       O  
ATOM   3934  NE2 GLN B 131      79.923  -9.010  13.667  1.00 64.90           N  
ANISOU 3934  NE2 GLN B 131     8067   7331   9259   -391    -32   -342       N  
ATOM   3935  N   VAL B 132      78.061  -3.283  17.212  1.00 37.12           N  
ANISOU 3935  N   VAL B 132     4678   3394   6031   -418     50   -564       N  
ATOM   3936  CA  VAL B 132      76.993  -2.378  17.655  1.00 41.33           C  
ANISOU 3936  CA  VAL B 132     5267   3845   6593   -372     65   -562       C  
ATOM   3937  C   VAL B 132      76.672  -1.362  16.562  1.00 42.34           C  
ANISOU 3937  C   VAL B 132     5466   3846   6776   -370    138   -472       C  
ATOM   3938  O   VAL B 132      75.500  -1.094  16.265  1.00 38.52           O  
ANISOU 3938  O   VAL B 132     5033   3324   6278   -292    137   -404       O  
ATOM   3939  CB  VAL B 132      77.373  -1.680  18.975  1.00 45.37           C  
ANISOU 3939  CB  VAL B 132     5760   4325   7151   -406     56   -698       C  
ATOM   3940  CG1 VAL B 132      76.368  -0.574  19.302  1.00 43.56           C  
ANISOU 3940  CG1 VAL B 132     5594   3989   6969   -365     89   -697       C  
ATOM   3941  CG2 VAL B 132      77.434  -2.675  20.117  1.00 39.67           C  
ANISOU 3941  CG2 VAL B 132     4998   3726   6348   -376    -21   -773       C  
ATOM   3942  N   ASP B 133      77.702  -0.790  15.936  1.00 42.92           N  
ANISOU 3942  N   ASP B 133     5544   3849   6914   -451    205   -471       N  
ATOM   3943  CA  ASP B 133      77.465   0.176  14.863  1.00 44.25           C  
ANISOU 3943  CA  ASP B 133     5803   3885   7126   -446    287   -375       C  
ATOM   3944  C   ASP B 133      76.833  -0.477  13.637  1.00 42.32           C  
ANISOU 3944  C   ASP B 133     5603   3681   6795   -373    274   -240       C  
ATOM   3945  O   ASP B 133      76.022   0.156  12.949  1.00 40.67           O  
ANISOU 3945  O   ASP B 133     5481   3389   6582   -306    299   -150       O  
ATOM   3946  CB  ASP B 133      78.769   0.876  14.483  1.00 54.97           C  
ANISOU 3946  CB  ASP B 133     7157   5155   8575   -560    381   -408       C  
ATOM   3947  CG  ASP B 133      79.322   1.716  15.615  1.00 77.76           C  
ANISOU 3947  CG  ASP B 133    10005   7980  11561   -633    397   -550       C  
ATOM   3948  OD1 ASP B 133      80.443   1.425  16.084  1.00 87.19           O  
ANISOU 3948  OD1 ASP B 133    11107   9229  12792   -716    385   -657       O  
ATOM   3949  OD2 ASP B 133      78.616   2.649  16.054  1.00 85.44           O  
ANISOU 3949  OD2 ASP B 133    11035   8854  12575   -600    413   -563       O  
ATOM   3950  N   LEU B 134      77.189  -1.730  13.339  1.00 37.07           N  
ANISOU 3950  N   LEU B 134     4884   3142   6060   -377    231   -228       N  
ATOM   3951  CA  LEU B 134      76.505  -2.438  12.257  1.00 37.07           C  
ANISOU 3951  CA  LEU B 134     4920   3192   5973   -304    204   -117       C  
ATOM   3952  C   LEU B 134      75.024  -2.632  12.576  1.00 39.71           C  
ANISOU 3952  C   LEU B 134     5263   3556   6268   -199    135    -97       C  
ATOM   3953  O   LEU B 134      74.166  -2.530  11.688  1.00 40.42           O  
ANISOU 3953  O   LEU B 134     5410   3626   6321   -120    123     -8       O  
ATOM   3954  CB  LEU B 134      77.176  -3.790  12.000  1.00 37.97           C  
ANISOU 3954  CB  LEU B 134     4969   3434   6025   -331    170   -125       C  
ATOM   3955  CG  LEU B 134      78.585  -3.735  11.401  1.00 44.42           C  
ANISOU 3955  CG  LEU B 134     5771   4234   6874   -423    244   -132       C  
ATOM   3956  CD1 LEU B 134      79.258  -5.120  11.447  1.00 37.62           C  
ANISOU 3956  CD1 LEU B 134     4826   3506   5960   -442    198   -167       C  
ATOM   3957  CD2 LEU B 134      78.504  -3.225   9.980  1.00 44.29           C  
ANISOU 3957  CD2 LEU B 134     5855   4136   6837   -406    319    -15       C  
ATOM   3958  N   PHE B 135      74.706  -2.919  13.837  1.00 38.21           N  
ANISOU 3958  N   PHE B 135     5017   3417   6086   -194     90   -183       N  
ATOM   3959  CA  PHE B 135      73.305  -3.057  14.232  1.00 36.02           C  
ANISOU 3959  CA  PHE B 135     4736   3161   5788   -104     42   -177       C  
ATOM   3960  C   PHE B 135      72.551  -1.752  14.024  1.00 40.70           C  
ANISOU 3960  C   PHE B 135     5399   3630   6436    -49     74   -142       C  
ATOM   3961  O   PHE B 135      71.430  -1.749  13.503  1.00 39.76           O  
ANISOU 3961  O   PHE B 135     5301   3511   6296     43     43    -84       O  
ATOM   3962  CB  PHE B 135      73.226  -3.517  15.691  1.00 36.37           C  
ANISOU 3962  CB  PHE B 135     4724   3269   5828   -116     11   -279       C  
ATOM   3963  CG  PHE B 135      71.834  -3.496  16.277  1.00 37.04           C  
ANISOU 3963  CG  PHE B 135     4803   3360   5912    -36    -12   -290       C  
ATOM   3964  CD1 PHE B 135      70.941  -4.527  16.017  1.00 33.17           C  
ANISOU 3964  CD1 PHE B 135     4279   2955   5370     18    -53   -257       C  
ATOM   3965  CD2 PHE B 135      71.431  -2.453  17.098  1.00 39.45           C  
ANISOU 3965  CD2 PHE B 135     5130   3585   6275    -20     14   -343       C  
ATOM   3966  CE1 PHE B 135      69.667  -4.521  16.573  1.00 40.34           C  
ANISOU 3966  CE1 PHE B 135     5167   3870   6292     84    -62   -278       C  
ATOM   3967  CE2 PHE B 135      70.163  -2.442  17.652  1.00 42.77           C  
ANISOU 3967  CE2 PHE B 135     5537   4013   6700     53      4   -360       C  
ATOM   3968  CZ  PHE B 135      69.281  -3.483  17.384  1.00 36.29           C  
ANISOU 3968  CZ  PHE B 135     4674   3281   5835    103    -32   -328       C  
ATOM   3969  N   ARG B 136      73.164  -0.626  14.399  1.00 36.08           N  
ANISOU 3969  N   ARG B 136     4848   2935   5926   -102    135   -182       N  
ATOM   3970  CA  ARG B 136      72.506   0.659  14.199  1.00 39.10           C  
ANISOU 3970  CA  ARG B 136     5310   3182   6366    -48    174   -147       C  
ATOM   3971  C   ARG B 136      72.221   0.922  12.728  1.00 47.36           C  
ANISOU 3971  C   ARG B 136     6439   4175   7380     11    190    -19       C  
ATOM   3972  O   ARG B 136      71.233   1.585  12.400  1.00 41.89           O  
ANISOU 3972  O   ARG B 136     5804   3414   6697    110    182     33       O  
ATOM   3973  CB  ARG B 136      73.356   1.794  14.772  1.00 43.38           C  
ANISOU 3973  CB  ARG B 136     5879   3603   7001   -132    248   -217       C  
ATOM   3974  CG  ARG B 136      73.481   1.808  16.287  1.00 43.79           C  
ANISOU 3974  CG  ARG B 136     5870   3687   7083   -168    226   -352       C  
ATOM   3975  CD  ARG B 136      74.204   3.074  16.671  1.00 47.09           C  
ANISOU 3975  CD  ARG B 136     6324   3967   7603   -242    299   -419       C  
ATOM   3976  NE  ARG B 136      74.517   3.234  18.088  1.00 43.93           N  
ANISOU 3976  NE  ARG B 136     5874   3585   7233   -287    280   -564       N  
ATOM   3977  CZ  ARG B 136      73.701   3.795  18.975  1.00 48.19           C  
ANISOU 3977  CZ  ARG B 136     6431   4084   7795   -234    274   -620       C  
ATOM   3978  NH1 ARG B 136      72.494   4.205  18.604  1.00 46.48           N  
ANISOU 3978  NH1 ARG B 136     6267   3812   7581   -133    281   -545       N  
ATOM   3979  NH2 ARG B 136      74.094   3.945  20.232  1.00 45.28           N  
ANISOU 3979  NH2 ARG B 136     6028   3733   7442   -277    258   -756       N  
ATOM   3980  N   ASN B 137      73.065   0.416  11.828  1.00 41.43           N  
ANISOU 3980  N   ASN B 137     5700   3455   6585    -37    212     32       N  
ATOM   3981  CA  ASN B 137      72.819   0.617  10.408  1.00 46.29           C  
ANISOU 3981  CA  ASN B 137     6411   4028   7150     27    229    157       C  
ATOM   3982  C   ASN B 137      71.933  -0.464   9.789  1.00 47.88           C  
ANISOU 3982  C   ASN B 137     6583   4353   7255    118    134    204       C  
ATOM   3983  O   ASN B 137      71.414  -0.258   8.687  1.00 51.49           O  
ANISOU 3983  O   ASN B 137     7121   4782   7659    205    120    300       O  
ATOM   3984  CB  ASN B 137      74.149   0.708   9.649  1.00 48.35           C  
ANISOU 3984  CB  ASN B 137     6713   4246   7410    -68    319    192       C  
ATOM   3985  CG  ASN B 137      74.884   2.023   9.927  1.00 74.50           C  
ANISOU 3985  CG  ASN B 137    10082   7398  10829   -146    431    166       C  
ATOM   3986  OD1 ASN B 137      76.076   2.033  10.233  1.00 85.68           O  
ANISOU 3986  OD1 ASN B 137    11450   8804  12299   -268    491    100       O  
ATOM   3987  ND2 ASN B 137      74.161   3.138   9.833  1.00 73.16           N  
ANISOU 3987  ND2 ASN B 137    10007   7096  10694    -75    458    210       N  
ATOM   3988  N   ALA B 138      71.730  -1.588  10.467  1.00 41.05           N  
ANISOU 3988  N   ALA B 138     5612   3618   6367    103     69    138       N  
ATOM   3989  CA  ALA B 138      70.949  -2.674   9.883  1.00 42.29           C  
ANISOU 3989  CA  ALA B 138     5732   3889   6446    173    -13    169       C  
ATOM   3990  C   ALA B 138      69.461  -2.343   9.907  1.00 45.41           C  
ANISOU 3990  C   ALA B 138     6125   4275   6852    293    -73    179       C  
ATOM   3991  O   ALA B 138      68.969  -1.658  10.802  1.00 46.41           O  
ANISOU 3991  O   ALA B 138     6238   4348   7047    311    -62    130       O  
ATOM   3992  CB  ALA B 138      71.188  -3.975  10.645  1.00 34.02           C  
ANISOU 3992  CB  ALA B 138     4580   2969   5378    117    -50     94       C  
ATOM   3993  N  AARG B 139      68.740  -2.847   8.905  0.65 43.24           N  
ANISOU 3993  N  AARG B 139     5860   4058   6513    379   -140    234       N  
ATOM   3994  N  BARG B 139      68.742  -2.848   8.904  0.35 43.93           N  
ANISOU 3994  N  BARG B 139     5947   4145   6600    379   -140    234       N  
ATOM   3995  CA AARG B 139      67.295  -2.647   8.874  0.65 45.59           C  
ANISOU 3995  CA AARG B 139     6131   4364   6826    500   -211    231       C  
ATOM   3996  CA BARG B 139      67.297  -2.653   8.862  0.35 46.07           C  
ANISOU 3996  CA BARG B 139     6192   4426   6886    500   -211    231       C  
ATOM   3997  C  AARG B 139      66.589  -3.606   9.826  0.65 43.64           C  
ANISOU 3997  C  AARG B 139     5753   4221   6605    488   -254    139       C  
ATOM   3998  C  BARG B 139      66.588  -3.608   9.817  0.35 43.25           C  
ANISOU 3998  C  BARG B 139     5705   4172   6556    488   -254    140       C  
ATOM   3999  O  AARG B 139      65.614  -3.229  10.487  0.65 40.94           O  
ANISOU 3999  O  AARG B 139     5367   3865   6324    543   -269     94       O  
ATOM   4000  O  BARG B 139      65.612  -3.227  10.474  0.35 41.69           O  
ANISOU 4000  O  BARG B 139     5463   3960   6419    544   -269     95       O  
ATOM   4001  CB AARG B 139      66.783  -2.819   7.444  0.65 53.17           C  
ANISOU 4001  CB AARG B 139     7144   5352   7705    602   -278    310       C  
ATOM   4002  CB BARG B 139      66.794  -2.841   7.430  0.35 52.70           C  
ANISOU 4002  CB BARG B 139     7084   5294   7644    602   -279    311       C  
ATOM   4003  CG AARG B 139      65.290  -2.640   7.266  0.65 58.86           C  
ANISOU 4003  CG AARG B 139     7829   6094   8443    741   -369    301       C  
ATOM   4004  CG BARG B 139      65.411  -2.281   7.148  0.35 58.71           C  
ANISOU 4004  CG BARG B 139     7846   6036   8423    750   -354    322       C  
ATOM   4005  CD AARG B 139      64.925  -2.676   5.787  0.65 64.28           C  
ANISOU 4005  CD AARG B 139     8590   6800   9035    852   -442    381       C  
ATOM   4006  CD BARG B 139      65.064  -2.454   5.674  0.35 63.79           C  
ANISOU 4006  CD BARG B 139     8559   6712   8967    855   -429    400       C  
ATOM   4007  NE AARG B 139      63.490  -2.527   5.562  0.65 67.64           N  
ANISOU 4007  NE AARG B 139     8966   7256   9477    996   -547    361       N  
ATOM   4008  NE BARG B 139      63.717  -1.991   5.349  0.35 66.39           N  
ANISOU 4008  NE BARG B 139     8877   7039   9310   1013   -522    402       N  
ATOM   4009  CZ AARG B 139      62.853  -1.360   5.508  0.65 66.46           C  
ANISOU 4009  CZ AARG B 139     8876   7012   9365   1110   -559    392       C  
ATOM   4010  CZ BARG B 139      62.632  -2.758   5.394  0.35 67.13           C  
ANISOU 4010  CZ BARG B 139     8844   7244   9419   1071   -622    332       C  
ATOM   4011  NH1AARG B 139      61.546  -1.334   5.296  0.65 69.87           N  
ANISOU 4011  NH1AARG B 139     9241   7490   9817   1246   -665    360       N  
ATOM   4012  NH1BARG B 139      62.729  -4.032   5.758  0.35 62.09           N  
ANISOU 4012  NH1BARG B 139     8093   6718   8782    979   -633    263       N  
ATOM   4013  NH2AARG B 139      63.518  -0.222   5.670  0.65 63.83           N  
ANISOU 4013  NH2AARG B 139     8661   6535   9054   1090   -463    448       N  
ATOM   4014  NH2BARG B 139      61.448  -2.250   5.077  0.35 67.11           N  
ANISOU 4014  NH2BARG B 139     8825   7236   9436   1222   -710    328       N  
ATOM   4015  N   ASN B 140      67.080  -4.841   9.915  1.00 38.99           N  
ANISOU 4015  N   ASN B 140     5108   3731   5975    415   -262    111       N  
ATOM   4016  CA  ASN B 140      66.512  -5.867  10.779  1.00 39.41           C  
ANISOU 4016  CA  ASN B 140     5053   3875   6045    394   -285     33       C  
ATOM   4017  C   ASN B 140      67.642  -6.554  11.521  1.00 39.04           C  
ANISOU 4017  C   ASN B 140     4988   3863   5980    283   -240     -6       C  
ATOM   4018  O   ASN B 140      68.614  -6.982  10.899  1.00 39.31           O  
ANISOU 4018  O   ASN B 140     5052   3919   5965    235   -232     28       O  
ATOM   4019  CB  ASN B 140      65.733  -6.892   9.960  1.00 39.41           C  
ANISOU 4019  CB  ASN B 140     5000   3970   6003    444   -361     38       C  
ATOM   4020  CG  ASN B 140      64.536  -6.291   9.311  1.00 44.92           C  
ANISOU 4020  CG  ASN B 140     5696   4650   6720    567   -425     58       C  
ATOM   4021  OD1 ASN B 140      63.526  -6.065   9.972  1.00 41.82           O  
ANISOU 4021  OD1 ASN B 140     5237   4257   6397    612   -435      4       O  
ATOM   4022  ND2 ASN B 140      64.641  -5.986   8.011  1.00 41.80           N  
ANISOU 4022  ND2 ASN B 140     5381   4241   6262    631   -467    134       N  
ATOM   4023  N   GLY B 141      67.517  -6.671  12.838  1.00 36.25           N  
ANISOU 4023  N   GLY B 141     4590   3517   5664    251   -212    -78       N  
ATOM   4024  CA  GLY B 141      68.591  -7.322  13.567  1.00 35.96           C  
ANISOU 4024  CA  GLY B 141     4544   3518   5602    163   -183   -117       C  
ATOM   4025  C   GLY B 141      68.251  -7.535  15.024  1.00 36.69           C  
ANISOU 4025  C   GLY B 141     4598   3627   5717    148   -159   -195       C  
ATOM   4026  O   GLY B 141      67.285  -6.978  15.556  1.00 37.19           O  
ANISOU 4026  O   GLY B 141     4646   3656   5827    196   -148   -224       O  
ATOM   4027  N   VAL B 142      69.084  -8.360  15.657  1.00 34.17           N  
ANISOU 4027  N   VAL B 142     4268   3358   5356     89   -149   -229       N  
ATOM   4028  CA  VAL B 142      69.072  -8.602  17.095  1.00 33.11           C  
ANISOU 4028  CA  VAL B 142     4124   3240   5216     72   -122   -300       C  
ATOM   4029  C   VAL B 142      70.497  -8.406  17.592  1.00 38.04           C  
ANISOU 4029  C   VAL B 142     4775   3857   5820     13   -116   -333       C  
ATOM   4030  O   VAL B 142      71.445  -8.922  16.988  1.00 36.88           O  
ANISOU 4030  O   VAL B 142     4627   3744   5643    -24   -132   -309       O  
ATOM   4031  CB  VAL B 142      68.557 -10.019  17.427  1.00 35.99           C  
ANISOU 4031  CB  VAL B 142     4453   3683   5540     75   -123   -314       C  
ATOM   4032  CG1 VAL B 142      68.861 -10.397  18.873  1.00 33.59           C  
ANISOU 4032  CG1 VAL B 142     4166   3397   5200     56    -91   -375       C  
ATOM   4033  CG2 VAL B 142      67.061 -10.090  17.156  1.00 31.05           C  
ANISOU 4033  CG2 VAL B 142     3780   3059   4957    128   -122   -310       C  
ATOM   4034  N   LEU B 143      70.657  -7.634  18.669  1.00 32.61           N  
ANISOU 4034  N   LEU B 143     4108   3128   5156      5    -94   -396       N  
ATOM   4035  CA  LEU B 143      71.962  -7.310  19.230  1.00 30.09           C  
ANISOU 4035  CA  LEU B 143     3802   2800   4830    -49    -96   -451       C  
ATOM   4036  C   LEU B 143      72.046  -7.799  20.672  1.00 35.23           C  
ANISOU 4036  C   LEU B 143     4460   3496   5429    -42    -99   -527       C  
ATOM   4037  O   LEU B 143      71.091  -7.649  21.431  1.00 38.49           O  
ANISOU 4037  O   LEU B 143     4886   3896   5843     -4    -73   -553       O  
ATOM   4038  CB  LEU B 143      72.213  -5.778  19.168  1.00 31.23           C  
ANISOU 4038  CB  LEU B 143     3974   2841   5052    -67    -70   -470       C  
ATOM   4039  CG  LEU B 143      73.415  -5.216  19.925  1.00 33.28           C  
ANISOU 4039  CG  LEU B 143     4237   3079   5330   -125    -69   -556       C  
ATOM   4040  CD1 LEU B 143      74.716  -5.677  19.288  1.00 39.63           C  
ANISOU 4040  CD1 LEU B 143     5013   3921   6125   -184    -85   -546       C  
ATOM   4041  CD2 LEU B 143      73.360  -3.670  19.998  1.00 31.51           C  
ANISOU 4041  CD2 LEU B 143     4045   2734   5192   -138    -30   -584       C  
ATOM   4042  N   ILE B 144      73.181  -8.405  21.049  1.00 32.03           N  
ANISOU 4042  N   ILE B 144     4050   3146   4975    -72   -129   -563       N  
ATOM   4043  CA  ILE B 144      73.466  -8.666  22.459  1.00 35.53           C  
ANISOU 4043  CA  ILE B 144     4518   3624   5359    -58   -142   -643       C  
ATOM   4044  C   ILE B 144      74.698  -7.867  22.857  1.00 37.39           C  
ANISOU 4044  C   ILE B 144     4746   3840   5621   -101   -170   -724       C  
ATOM   4045  O   ILE B 144      75.599  -7.643  22.047  1.00 35.36           O  
ANISOU 4045  O   ILE B 144     4454   3574   5409   -150   -181   -714       O  
ATOM   4046  CB  ILE B 144      73.663 -10.164  22.790  1.00 35.72           C  
ANISOU 4046  CB  ILE B 144     4550   3734   5289    -35   -162   -630       C  
ATOM   4047  CG1 ILE B 144      74.864 -10.746  22.032  1.00 33.84           C  
ANISOU 4047  CG1 ILE B 144     4276   3540   5041    -68   -204   -612       C  
ATOM   4048  CG2 ILE B 144      72.372 -10.917  22.497  1.00 33.94           C  
ANISOU 4048  CG2 ILE B 144     4326   3517   5052     -3   -122   -568       C  
ATOM   4049  CD1 ILE B 144      75.363 -12.084  22.583  1.00 40.41           C  
ANISOU 4049  CD1 ILE B 144     5125   4450   5778    -38   -235   -621       C  
ATOM   4050  N   THR B 145      74.708  -7.385  24.102  1.00 34.05           N  
ANISOU 4050  N   THR B 145     4354   3408   5177    -85   -176   -813       N  
ATOM   4051  CA  THR B 145      75.880  -6.721  24.664  1.00 35.08           C  
ANISOU 4051  CA  THR B 145     4470   3532   5328   -122   -215   -917       C  
ATOM   4052  C   THR B 145      76.032  -7.128  26.116  1.00 37.24           C  
ANISOU 4052  C   THR B 145     4786   3864   5501    -75   -254  -1002       C  
ATOM   4053  O   THR B 145      75.098  -7.631  26.746  1.00 39.91           O  
ANISOU 4053  O   THR B 145     5177   4218   5767    -18   -225   -981       O  
ATOM   4054  CB  THR B 145      75.776  -5.197  24.630  1.00 41.14           C  
ANISOU 4054  CB  THR B 145     5242   4194   6197   -158   -180   -960       C  
ATOM   4055  OG1 THR B 145      74.691  -4.808  25.485  1.00 46.36           O  
ANISOU 4055  OG1 THR B 145     5954   4823   6838   -108   -148   -984       O  
ATOM   4056  CG2 THR B 145      75.537  -4.681  23.212  1.00 38.27           C  
ANISOU 4056  CG2 THR B 145     4861   3757   5921   -191   -134   -867       C  
ATOM   4057  N   GLU B 146      77.211  -6.844  26.661  1.00 32.75           N  
ANISOU 4057  N   GLU B 146     4193   3320   4929    -98   -315  -1107       N  
ATOM   4058  CA  GLU B 146      77.466  -7.026  28.079  1.00 36.93           C  
ANISOU 4058  CA  GLU B 146     4772   3902   5359    -45   -366  -1206       C  
ATOM   4059  C   GLU B 146      77.190  -5.778  28.898  1.00 46.15           C  
ANISOU 4059  C   GLU B 146     5970   5004   6560    -51   -351  -1304       C  
ATOM   4060  O   GLU B 146      77.128  -5.866  30.128  1.00 50.74           O  
ANISOU 4060  O   GLU B 146     6614   5621   7044      5   -380  -1382       O  
ATOM   4061  CB  GLU B 146      78.918  -7.468  28.298  1.00 35.49           C  
ANISOU 4061  CB  GLU B 146     4540   3798   5147    -51   -462  -1284       C  
ATOM   4062  CG  GLU B 146      79.197  -8.862  27.739  1.00 38.67           C  
ANISOU 4062  CG  GLU B 146     4929   4275   5491    -23   -482  -1199       C  
ATOM   4063  CD  GLU B 146      80.649  -9.270  27.895  1.00 52.92           C  
ANISOU 4063  CD  GLU B 146     6672   6156   7278    -21   -579  -1280       C  
ATOM   4064  OE1 GLU B 146      81.530  -8.393  27.775  1.00 55.56           O  
ANISOU 4064  OE1 GLU B 146     6929   6472   7708    -84   -608  -1375       O  
ATOM   4065  OE2 GLU B 146      80.905 -10.463  28.154  1.00 47.63           O  
ANISOU 4065  OE2 GLU B 146     6030   5564   6506     46   -623  -1254       O  
ATOM   4066  N   GLY B 147      77.031  -4.621  28.250  1.00 47.20           N  
ANISOU 4066  N   GLY B 147     6073   5039   6822   -112   -304  -1303       N  
ATOM   4067  CA  GLY B 147      76.822  -3.369  28.948  1.00 40.20           C  
ANISOU 4067  CA  GLY B 147     5215   4076   5984   -123   -284  -1401       C  
ATOM   4068  C   GLY B 147      75.861  -2.485  28.175  1.00 39.78           C  
ANISOU 4068  C   GLY B 147     5170   3909   6036   -142   -197  -1328       C  
ATOM   4069  O   GLY B 147      75.327  -2.879  27.135  1.00 38.93           O  
ANISOU 4069  O   GLY B 147     5047   3791   5952   -139   -160  -1204       O  
ATOM   4070  N   SER B 148      75.663  -1.274  28.695  1.00 39.33           N  
ANISOU 4070  N   SER B 148     5140   3765   6040   -154   -170  -1412       N  
ATOM   4071  CA  SER B 148      74.709  -0.364  28.076  1.00 44.20           C  
ANISOU 4071  CA  SER B 148     5775   4265   6752   -153    -90  -1349       C  
ATOM   4072  C   SER B 148      75.235   0.147  26.740  1.00 46.30           C  
ANISOU 4072  C   SER B 148     5999   4457   7134   -224    -65  -1286       C  
ATOM   4073  O   SER B 148      76.445   0.257  26.520  1.00 41.66           O  
ANISOU 4073  O   SER B 148     5366   3877   6587   -296    -94  -1339       O  
ATOM   4074  CB  SER B 148      74.392   0.813  29.009  1.00 43.74           C  
ANISOU 4074  CB  SER B 148     5764   4125   6732   -145    -63  -1461       C  
ATOM   4075  OG  SER B 148      75.542   1.589  29.306  1.00 46.30           O  
ANISOU 4075  OG  SER B 148     6063   4411   7117   -217    -97  -1588       O  
ATOM   4076  N   VAL B 149      74.300   0.430  25.835  1.00 41.52           N  
ANISOU 4076  N   VAL B 149     5412   3785   6578   -198     -7  -1173       N  
ATOM   4077  CA  VAL B 149      74.567   1.070  24.553  1.00 39.94           C  
ANISOU 4077  CA  VAL B 149     5205   3491   6478   -245     35  -1098       C  
ATOM   4078  C   VAL B 149      73.846   2.406  24.568  1.00 44.33           C  
ANISOU 4078  C   VAL B 149     5814   3906   7123   -225     97  -1106       C  
ATOM   4079  O   VAL B 149      72.647   2.455  24.867  1.00 38.94           O  
ANISOU 4079  O   VAL B 149     5160   3214   6420   -146    115  -1080       O  
ATOM   4080  CB  VAL B 149      74.078   0.222  23.367  1.00 39.21           C  
ANISOU 4080  CB  VAL B 149     5101   3443   6354   -212     37   -951       C  
ATOM   4081  CG1 VAL B 149      74.330   0.970  22.059  1.00 39.00           C  
ANISOU 4081  CG1 VAL B 149     5091   3312   6416   -250     87   -870       C  
ATOM   4082  CG2 VAL B 149      74.738  -1.154  23.369  1.00 39.60           C  
ANISOU 4082  CG2 VAL B 149     5103   3628   6315   -224    -20   -942       C  
ATOM   4083  N   LYS B 150      74.563   3.483  24.248  1.00 40.27           N  
ANISOU 4083  N   LYS B 150     5311   3275   6713   -297    137  -1144       N  
ATOM   4084  CA  LYS B 150      74.029   4.811  24.531  1.00 38.56           C  
ANISOU 4084  CA  LYS B 150     5153   2915   6583   -282    194  -1184       C  
ATOM   4085  C   LYS B 150      72.733   5.056  23.760  1.00 41.88           C  
ANISOU 4085  C   LYS B 150     5618   3274   7018   -192    234  -1055       C  
ATOM   4086  O   LYS B 150      72.653   4.799  22.556  1.00 42.69           O  
ANISOU 4086  O   LYS B 150     5726   3371   7124   -182    244   -931       O  
ATOM   4087  CB  LYS B 150      75.063   5.905  24.225  1.00 43.43           C  
ANISOU 4087  CB  LYS B 150     5778   3403   7322   -386    244  -1243       C  
ATOM   4088  CG  LYS B 150      75.633   5.977  22.804  1.00 37.44           C  
ANISOU 4088  CG  LYS B 150     5021   2589   6618   -440    293  -1132       C  
ATOM   4089  CD  LYS B 150      76.754   7.064  22.754  1.00 38.89           C  
ANISOU 4089  CD  LYS B 150     5203   2640   6932   -560    357  -1224       C  
ATOM   4090  CE  LYS B 150      77.323   7.240  21.350  1.00 49.02           C  
ANISOU 4090  CE  LYS B 150     6504   3848   8273   -618    432  -1113       C  
ATOM   4091  NZ  LYS B 150      77.988   5.999  20.869  1.00 55.71           N  
ANISOU 4091  NZ  LYS B 150     7277   4842   9049   -644    384  -1073       N  
ATOM   4092  N   GLY B 151      71.704   5.521  24.483  1.00 38.36           N  
ANISOU 4092  N   GLY B 151     5206   2793   6578   -118    251  -1092       N  
ATOM   4093  CA  GLY B 151      70.398   5.805  23.919  1.00 42.80           C  
ANISOU 4093  CA  GLY B 151     5798   3302   7162    -17    279   -995       C  
ATOM   4094  C   GLY B 151      69.474   4.610  23.700  1.00 39.47           C  
ANISOU 4094  C   GLY B 151     5332   3009   6656     58    241   -917       C  
ATOM   4095  O   GLY B 151      68.256   4.805  23.577  1.00 43.28           O  
ANISOU 4095  O   GLY B 151     5820   3467   7156    151    257   -877       O  
ATOM   4096  N   LEU B 152      69.994   3.394  23.646  1.00 35.75           N  
ANISOU 4096  N   LEU B 152     4814   2668   6103     23    194   -901       N  
ATOM   4097  CA  LEU B 152      69.167   2.203  23.391  1.00 36.08           C  
ANISOU 4097  CA  LEU B 152     4812   2823   6072     82    166   -831       C  
ATOM   4098  C   LEU B 152      68.615   1.627  24.691  1.00 43.20           C  
ANISOU 4098  C   LEU B 152     5701   3804   6909    114    167   -910       C  
ATOM   4099  O   LEU B 152      69.367   1.406  25.645  1.00 39.40           O  
ANISOU 4099  O   LEU B 152     5228   3366   6377     71    151   -999       O  
ATOM   4100  CB  LEU B 152      69.972   1.125  22.664  1.00 40.33           C  
ANISOU 4100  CB  LEU B 152     5316   3455   6554     32    124   -772       C  
ATOM   4101  CG  LEU B 152      70.560   1.483  21.298  1.00 46.51           C  
ANISOU 4101  CG  LEU B 152     6115   4176   7380     -2    131   -684       C  
ATOM   4102  CD1 LEU B 152      71.016   0.227  20.565  1.00 43.56           C  
ANISOU 4102  CD1 LEU B 152     5701   3912   6937    -25     91   -618       C  
ATOM   4103  CD2 LEU B 152      69.589   2.299  20.453  1.00 44.94           C  
ANISOU 4103  CD2 LEU B 152     5957   3878   7238     75    158   -602       C  
ATOM   4104  N   GLN B 153      67.311   1.366  24.723  1.00 43.90           N  
ANISOU 4104  N   GLN B 153     5769   3913   6998    193    187   -879       N  
ATOM   4105  CA  GLN B 153      66.689   0.811  25.923  1.00 38.23           C  
ANISOU 4105  CA  GLN B 153     5045   3261   6220    225    212   -945       C  
ATOM   4106  C   GLN B 153      66.858  -0.707  25.935  1.00 37.60           C  
ANISOU 4106  C   GLN B 153     4933   3310   6045    207    185   -911       C  
ATOM   4107  O   GLN B 153      66.426  -1.374  24.988  1.00 40.20           O  
ANISOU 4107  O   GLN B 153     5216   3677   6379    223    168   -824       O  
ATOM   4108  CB  GLN B 153      65.214   1.181  25.976  1.00 39.31           C  
ANISOU 4108  CB  GLN B 153     5161   3361   6412    312    259   -938       C  
ATOM   4109  CG  GLN B 153      64.939   2.689  25.744  1.00 38.31           C  
ANISOU 4109  CG  GLN B 153     5070   3096   6391    349    284   -951       C  
ATOM   4110  CD  GLN B 153      65.698   3.593  26.695  1.00 42.91           C  
ANISOU 4110  CD  GLN B 153     5715   3608   6982    305    305  -1059       C  
ATOM   4111  OE1 GLN B 153      65.299   3.769  27.842  1.00 39.66           O  
ANISOU 4111  OE1 GLN B 153     5323   3198   6548    330    344  -1150       O  
ATOM   4112  NE2 GLN B 153      66.786   4.205  26.207  1.00 37.62           N  
ANISOU 4112  NE2 GLN B 153     5077   2869   6349    239    285  -1056       N  
ATOM   4113  N   PRO B 154      67.468  -1.290  26.969  1.00 38.59           N  
ANISOU 4113  N   PRO B 154     5084   3499   6078    180    177   -977       N  
ATOM   4114  CA  PRO B 154      67.783  -2.722  26.942  1.00 40.91           C  
ANISOU 4114  CA  PRO B 154     5361   3901   6280    163    151   -939       C  
ATOM   4115  C   PRO B 154      66.671  -3.602  27.502  1.00 40.66           C  
ANISOU 4115  C   PRO B 154     5324   3923   6203    210    206   -930       C  
ATOM   4116  O   PRO B 154      65.819  -3.170  28.278  1.00 37.87           O  
ANISOU 4116  O   PRO B 154     4988   3540   5862    252    268   -980       O  
ATOM   4117  CB  PRO B 154      69.023  -2.811  27.842  1.00 40.52           C  
ANISOU 4117  CB  PRO B 154     5355   3886   6154    125    111  -1021       C  
ATOM   4118  CG  PRO B 154      68.764  -1.754  28.895  1.00 42.86           C  
ANISOU 4118  CG  PRO B 154     5700   4120   6466    147    146  -1123       C  
ATOM   4119  CD  PRO B 154      67.994  -0.630  28.182  1.00 43.28           C  
ANISOU 4119  CD  PRO B 154     5734   4066   6645    167    184  -1093       C  
ATOM   4120  N   SER B 155      66.726  -4.870  27.106  1.00 38.44           N  
ANISOU 4120  N   SER B 155     5017   3718   5869    198    191   -871       N  
ATOM   4121  CA  SER B 155      65.997  -5.958  27.751  1.00 42.05           C  
ANISOU 4121  CA  SER B 155     5482   4232   6262    222    249   -868       C  
ATOM   4122  C   SER B 155      67.022  -6.884  28.394  1.00 39.78           C  
ANISOU 4122  C   SER B 155     5253   4012   5852    202    219   -882       C  
ATOM   4123  O   SER B 155      67.943  -7.347  27.717  1.00 37.56           O  
ANISOU 4123  O   SER B 155     4955   3764   5553    168    152   -844       O  
ATOM   4124  CB  SER B 155      65.150  -6.736  26.743  1.00 43.70           C  
ANISOU 4124  CB  SER B 155     5616   4468   6520    227    260   -792       C  
ATOM   4125  OG  SER B 155      64.628  -7.927  27.332  1.00 39.87           O  
ANISOU 4125  OG  SER B 155     5141   4033   5974    232    322   -788       O  
ATOM   4126  N   VAL B 156      66.869  -7.151  29.690  1.00 36.05           N  
ANISOU 4126  N   VAL B 156     4853   3557   5288    230    268   -937       N  
ATOM   4127  CA  VAL B 156      67.799  -8.039  30.385  1.00 38.60           C  
ANISOU 4127  CA  VAL B 156     5245   3942   5478    233    235   -950       C  
ATOM   4128  C   VAL B 156      67.469  -9.482  30.015  1.00 41.51           C  
ANISOU 4128  C   VAL B 156     5605   4358   5809    231    266   -872       C  
ATOM   4129  O   VAL B 156      66.338  -9.943  30.208  1.00 40.06           O  
ANISOU 4129  O   VAL B 156     5416   4165   5638    246    361   -852       O  
ATOM   4130  CB  VAL B 156      67.747  -7.826  31.905  1.00 44.99           C  
ANISOU 4130  CB  VAL B 156     6157   4754   6185    277    276  -1033       C  
ATOM   4131  CG1 VAL B 156      68.587  -8.878  32.615  1.00 42.20           C  
ANISOU 4131  CG1 VAL B 156     5887   4468   5679    301    241  -1036       C  
ATOM   4132  CG2 VAL B 156      68.256  -6.421  32.268  1.00 48.70           C  
ANISOU 4132  CG2 VAL B 156     6636   5176   6690    272    232  -1126       C  
ATOM   4133  N   GLY B 157      68.455 -10.199  29.481  1.00 39.93           N  
ANISOU 4133  N   GLY B 157     5397   4204   5571    209    192   -835       N  
ATOM   4134  CA  GLY B 157      68.233 -11.551  29.014  1.00 36.47           C  
ANISOU 4134  CA  GLY B 157     4949   3802   5107    203    215   -763       C  
ATOM   4135  C   GLY B 157      68.279 -12.587  30.118  1.00 34.65           C  
ANISOU 4135  C   GLY B 157     4824   3601   4742    241    265   -765       C  
ATOM   4136  O   GLY B 157      68.340 -12.268  31.312  1.00 37.66           O  
ANISOU 4136  O   GLY B 157     5292   3979   5039    281    289   -822       O  
ATOM   4137  N   PRO B 158      68.252 -13.860  29.733  1.00 37.56           N  
ANISOU 4137  N   PRO B 158     5196   3995   5081    234    284   -702       N  
ATOM   4138  CA  PRO B 158      68.366 -14.933  30.727  1.00 39.24           C  
ANISOU 4138  CA  PRO B 158     5527   4224   5158    276    335   -690       C  
ATOM   4139  C   PRO B 158      69.740 -14.932  31.383  1.00 37.51           C  
ANISOU 4139  C   PRO B 158     5384   4049   4818    320    234   -728       C  
ATOM   4140  O   PRO B 158      70.721 -14.416  30.844  1.00 41.28           O  
ANISOU 4140  O   PRO B 158     5803   4551   5330    301    124   -753       O  
ATOM   4141  CB  PRO B 158      68.133 -16.211  29.909  1.00 36.43           C  
ANISOU 4141  CB  PRO B 158     5140   3876   4825    249    364   -615       C  
ATOM   4142  CG  PRO B 158      68.454 -15.849  28.494  1.00 39.69           C  
ANISOU 4142  CG  PRO B 158     5432   4301   5348    202    278   -594       C  
ATOM   4143  CD  PRO B 158      68.196 -14.360  28.347  1.00 34.04           C  
ANISOU 4143  CD  PRO B 158     4657   3558   4718    191    254   -640       C  
ATOM   4144  N   LYS B 159      69.798 -15.529  32.575  1.00 37.66           N  
ANISOU 4144  N   LYS B 159     5539   4078   4694    382    278   -737       N  
ATOM   4145  CA  LYS B 159      71.070 -15.635  33.284  1.00 43.50           C  
ANISOU 4145  CA  LYS B 159     6358   4868   5303    443    172   -780       C  
ATOM   4146  C   LYS B 159      72.055 -16.568  32.576  1.00 43.61           C  
ANISOU 4146  C   LYS B 159     6345   4924   5301    445     86   -735       C  
ATOM   4147  O   LYS B 159      73.276 -16.367  32.681  1.00 41.90           O  
ANISOU 4147  O   LYS B 159     6120   4757   5042    471    -38   -784       O  
ATOM   4148  CB  LYS B 159      70.831 -16.119  34.716  1.00 41.45           C  
ANISOU 4148  CB  LYS B 159     6269   4605   4874    525    242   -790       C  
ATOM   4149  CG  LYS B 159      70.125 -15.117  35.645  1.00 43.75           C  
ANISOU 4149  CG  LYS B 159     6608   4866   5148    541    310   -858       C  
ATOM   4150  CD  LYS B 159      70.053 -15.689  37.060  1.00 55.51           C  
ANISOU 4150  CD  LYS B 159     8289   6360   6442    634    373   -864       C  
ATOM   4151  CE  LYS B 159      69.395 -14.730  38.040  1.00 71.92           C  
ANISOU 4151  CE  LYS B 159    10428   8411   8487    657    445   -938       C  
ATOM   4152  NZ  LYS B 159      69.611 -15.182  39.448  1.00 83.63           N  
ANISOU 4152  NZ  LYS B 159    12114   9911   9749    763    474   -956       N  
ATOM   4153  N   GLN B 160      71.563 -17.593  31.869  1.00 38.33           N  
ANISOU 4153  N   GLN B 160     5658   4238   4668    417    151   -652       N  
ATOM   4154  CA  GLN B 160      72.406 -18.631  31.288  1.00 38.60           C  
ANISOU 4154  CA  GLN B 160     5687   4305   4675    429     89   -606       C  
ATOM   4155  C   GLN B 160      72.666 -18.392  29.799  1.00 41.20           C  
ANISOU 4155  C   GLN B 160     5867   4644   5144    354     33   -587       C  
ATOM   4156  O   GLN B 160      71.933 -17.670  29.115  1.00 39.15           O  
ANISOU 4156  O   GLN B 160     5518   4355   5004    294     65   -585       O  
ATOM   4157  CB  GLN B 160      71.780 -20.026  31.477  1.00 38.33           C  
ANISOU 4157  CB  GLN B 160     5745   4237   4581    450    200   -529       C  
ATOM   4158  CG  GLN B 160      70.563 -20.323  30.575  1.00 39.65           C  
ANISOU 4158  CG  GLN B 160     5829   4356   4879    370    306   -480       C  
ATOM   4159  CD  GLN B 160      69.229 -19.898  31.206  1.00 42.76           C  
ANISOU 4159  CD  GLN B 160     6246   4701   5301    354    441   -496       C  
ATOM   4160  OE1 GLN B 160      69.180 -18.966  32.001  1.00 41.56           O  
ANISOU 4160  OE1 GLN B 160     6128   4550   5113    382    438   -551       O  
ATOM   4161  NE2 GLN B 160      68.150 -20.591  30.850  1.00 42.76           N  
ANISOU 4161  NE2 GLN B 160     6222   4656   5370    309    562   -456       N  
ATOM   4162  N   ALA B 161      73.737 -19.017  29.306  1.00 33.34           N  
ANISOU 4162  N   ALA B 161     4851   3690   4125    368    -52   -572       N  
ATOM   4163  CA  ALA B 161      74.071 -18.988  27.889  1.00 33.38           C  
ANISOU 4163  CA  ALA B 161     4735   3706   4241    305    -95   -547       C  
ATOM   4164  C   ALA B 161      74.703 -20.324  27.531  1.00 34.87           C  
ANISOU 4164  C   ALA B 161     4950   3920   4379    334   -118   -501       C  
ATOM   4165  O   ALA B 161      74.957 -21.162  28.397  1.00 42.36           O  
ANISOU 4165  O   ALA B 161     6009   4875   5209    407   -111   -490       O  
ATOM   4166  CB  ALA B 161      75.008 -17.812  27.542  1.00 35.59           C  
ANISOU 4166  CB  ALA B 161     4928   4013   4582    276   -193   -611       C  
ATOM   4167  N   SER B 162      74.944 -20.525  26.239  1.00 34.63           N  
ANISOU 4167  N   SER B 162     4825   3899   4433    283   -142   -471       N  
ATOM   4168  CA  SER B 162      75.529 -21.767  25.750  1.00 35.32           C  
ANISOU 4168  CA  SER B 162     4926   4006   4488    305   -161   -430       C  
ATOM   4169  C   SER B 162      77.006 -21.559  25.435  1.00 37.69           C  
ANISOU 4169  C   SER B 162     5168   4365   4788    321   -274   -472       C  
ATOM   4170  O   SER B 162      77.361 -20.686  24.636  1.00 36.86           O  
ANISOU 4170  O   SER B 162     4961   4272   4773    263   -312   -496       O  
ATOM   4171  CB  SER B 162      74.806 -22.265  24.500  1.00 33.21           C  
ANISOU 4171  CB  SER B 162     4597   3712   4308    241   -108   -376       C  
ATOM   4172  OG  SER B 162      75.419 -23.475  24.041  1.00 37.90           O  
ANISOU 4172  OG  SER B 162     5209   4322   4870    265   -124   -344       O  
ATOM   4173  N   LEU B 163      77.857 -22.386  26.027  1.00 37.31           N  
ANISOU 4173  N   LEU B 163     5184   4349   4643    402   -323   -480       N  
ATOM   4174  CA  LEU B 163      79.288 -22.366  25.734  1.00 37.15           C  
ANISOU 4174  CA  LEU B 163     5096   4390   4627    426   -431   -527       C  
ATOM   4175  C   LEU B 163      79.683 -23.750  25.229  1.00 35.87           C  
ANISOU 4175  C   LEU B 163     4958   4236   4434    464   -429   -476       C  
ATOM   4176  O   LEU B 163      79.711 -24.704  26.007  1.00 36.00           O  
ANISOU 4176  O   LEU B 163     5090   4244   4344    550   -421   -451       O  
ATOM   4177  CB  LEU B 163      80.095 -21.987  26.974  1.00 34.14           C  
ANISOU 4177  CB  LEU B 163     4759   4055   4158    506   -518   -606       C  
ATOM   4178  CG  LEU B 163      81.614 -21.988  26.790  1.00 38.43           C  
ANISOU 4178  CG  LEU B 163     5219   4670   4712    539   -637   -675       C  
ATOM   4179  CD1 LEU B 163      81.996 -21.036  25.671  1.00 37.72           C  
ANISOU 4179  CD1 LEU B 163     4979   4586   4767    432   -646   -706       C  
ATOM   4180  CD2 LEU B 163      82.317 -21.598  28.088  1.00 39.21           C  
ANISOU 4180  CD2 LEU B 163     5360   4819   4720    626   -736   -768       C  
ATOM   4181  N   ASN B 164      79.989 -23.854  23.934  1.00 35.20           N  
ANISOU 4181  N   ASN B 164     4775   4161   4437    405   -432   -459       N  
ATOM   4182  CA  ASN B 164      80.397 -25.128  23.324  1.00 38.67           C  
ANISOU 4182  CA  ASN B 164     5227   4606   4861    435   -430   -418       C  
ATOM   4183  C   ASN B 164      79.382 -26.231  23.593  1.00 39.43           C  
ANISOU 4183  C   ASN B 164     5437   4640   4904    457   -337   -349       C  
ATOM   4184  O   ASN B 164      79.735 -27.397  23.821  1.00 35.87           O  
ANISOU 4184  O   ASN B 164     5063   4180   4385    528   -336   -321       O  
ATOM   4185  CB  ASN B 164      81.785 -25.538  23.807  1.00 38.33           C  
ANISOU 4185  CB  ASN B 164     5184   4622   4757    528   -529   -467       C  
ATOM   4186  CG  ASN B 164      82.794 -24.441  23.587  1.00 38.41           C  
ANISOU 4186  CG  ASN B 164     5069   4691   4836    496   -611   -551       C  
ATOM   4187  OD1 ASN B 164      82.788 -23.802  22.537  1.00 40.34           O  
ANISOU 4187  OD1 ASN B 164     5214   4931   5183    404   -588   -551       O  
ATOM   4188  ND2 ASN B 164      83.633 -24.182  24.583  1.00 36.96           N  
ANISOU 4188  ND2 ASN B 164     4892   4557   4595    572   -703   -627       N  
ATOM   4189  N   GLY B 165      78.106 -25.863  23.556  1.00 40.13           N  
ANISOU 4189  N   GLY B 165     5536   4680   5033    395   -254   -324       N  
ATOM   4190  CA  GLY B 165      77.037 -26.809  23.788  1.00 43.16           C  
ANISOU 4190  CA  GLY B 165     6010   4997   5390    395   -149   -269       C  
ATOM   4191  C   GLY B 165      76.692 -27.037  25.236  1.00 44.97           C  
ANISOU 4191  C   GLY B 165     6378   5195   5512    464   -104   -262       C  
ATOM   4192  O   GLY B 165      75.762 -27.801  25.518  1.00 41.59           O  
ANISOU 4192  O   GLY B 165     6034   4702   5067    459      5   -217       O  
ATOM   4193  N   VAL B 166      77.404 -26.405  26.160  1.00 35.81           N  
ANISOU 4193  N   VAL B 166     5247   4078   4280    529   -180   -308       N  
ATOM   4194  CA  VAL B 166      77.122 -26.514  27.587  1.00 36.91           C  
ANISOU 4194  CA  VAL B 166     5532   4196   4298    607   -145   -306       C  
ATOM   4195  C   VAL B 166      76.348 -25.277  28.004  1.00 39.05           C  
ANISOU 4195  C   VAL B 166     5774   4458   4604    557   -113   -342       C  
ATOM   4196  O   VAL B 166      76.866 -24.157  27.914  1.00 37.07           O  
ANISOU 4196  O   VAL B 166     5435   4254   4395    536   -197   -405       O  
ATOM   4197  CB  VAL B 166      78.417 -26.658  28.404  1.00 34.26           C  
ANISOU 4197  CB  VAL B 166     5255   3918   3844    728   -264   -345       C  
ATOM   4198  CG1 VAL B 166      78.107 -26.802  29.898  1.00 37.75           C  
ANISOU 4198  CG1 VAL B 166     5871   4337   4136    823   -228   -339       C  
ATOM   4199  CG2 VAL B 166      79.225 -27.834  27.895  1.00 39.82           C  
ANISOU 4199  CG2 VAL B 166     5971   4632   4528    783   -301   -314       C  
ATOM   4200  N   THR B 167      75.108 -25.464  28.462  1.00 36.65           N  
ANISOU 4200  N   THR B 167     5544   4090   4293    535     16   -308       N  
ATOM   4201  CA  THR B 167      74.331 -24.333  28.952  1.00 42.92           C  
ANISOU 4201  CA  THR B 167     6319   4872   5115    499     56   -345       C  
ATOM   4202  C   THR B 167      74.679 -24.088  30.413  1.00 43.72           C  
ANISOU 4202  C   THR B 167     6552   4989   5072    596     34   -379       C  
ATOM   4203  O   THR B 167      74.629 -25.006  31.235  1.00 40.38           O  
ANISOU 4203  O   THR B 167     6281   4536   4524    673     88   -339       O  
ATOM   4204  CB  THR B 167      72.835 -24.581  28.780  1.00 43.72           C  
ANISOU 4204  CB  THR B 167     6422   4904   5286    432    206   -308       C  
ATOM   4205  OG1 THR B 167      72.547 -24.681  27.382  1.00 43.27           O  
ANISOU 4205  OG1 THR B 167     6233   4845   5361    348    201   -292       O  
ATOM   4206  CG2 THR B 167      72.040 -23.418  29.368  1.00 41.42           C  
ANISOU 4206  CG2 THR B 167     6116   4600   5021    409    250   -350       C  
ATOM   4207  N   LEU B 168      75.060 -22.855  30.733  1.00 37.06           N  
ANISOU 4207  N   LEU B 168     5658   4187   4237    595    -47   -454       N  
ATOM   4208  CA  LEU B 168      75.598 -22.592  32.059  1.00 38.20           C  
ANISOU 4208  CA  LEU B 168     5917   4363   4236    696   -101   -505       C  
ATOM   4209  C   LEU B 168      75.380 -21.132  32.420  1.00 39.05           C  
ANISOU 4209  C   LEU B 168     5971   4481   4386    661   -124   -585       C  
ATOM   4210  O   LEU B 168      75.202 -20.276  31.551  1.00 39.73           O  
ANISOU 4210  O   LEU B 168     5918   4564   4614    571   -136   -607       O  
ATOM   4211  CB  LEU B 168      77.087 -22.950  32.129  1.00 41.41           C  
ANISOU 4211  CB  LEU B 168     6322   4839   4572    778   -252   -539       C  
ATOM   4212  CG  LEU B 168      78.038 -22.271  31.136  1.00 44.55           C  
ANISOU 4212  CG  LEU B 168     6542   5293   5092    720   -370   -597       C  
ATOM   4213  CD1 LEU B 168      78.593 -20.989  31.711  1.00 46.01           C  
ANISOU 4213  CD1 LEU B 168     6681   5523   5278    725   -466   -707       C  
ATOM   4214  CD2 LEU B 168      79.188 -23.224  30.756  1.00 40.86           C  
ANISOU 4214  CD2 LEU B 168     6060   4872   4593    781   -460   -586       C  
ATOM   4215  N   ILE B 169      75.376 -20.868  33.724  1.00 40.15           N  
ANISOU 4215  N   ILE B 169     6235   4627   4393    740   -124   -627       N  
ATOM   4216  CA  ILE B 169      75.424 -19.516  34.258  1.00 45.06           C  
ANISOU 4216  CA  ILE B 169     6827   5267   5027    730   -170   -724       C  
ATOM   4217  C   ILE B 169      76.879 -19.222  34.587  1.00 46.17           C  
ANISOU 4217  C   ILE B 169     6946   5488   5109    794   -345   -813       C  
ATOM   4218  O   ILE B 169      77.477 -19.881  35.446  1.00 44.06           O  
ANISOU 4218  O   ILE B 169     6801   5258   4682    910   -402   -822       O  
ATOM   4219  CB  ILE B 169      74.526 -19.361  35.491  1.00 46.36           C  
ANISOU 4219  CB  ILE B 169     7139   5394   5080    778    -63   -730       C  
ATOM   4220  CG1 ILE B 169      73.077 -19.702  35.122  1.00 44.27           C  
ANISOU 4220  CG1 ILE B 169     6873   5051   4895    709    118   -651       C  
ATOM   4221  CG2 ILE B 169      74.648 -17.943  36.058  1.00 42.52           C  
ANISOU 4221  CG2 ILE B 169     6623   4926   4605    773   -119   -842       C  
ATOM   4222  CD1 ILE B 169      72.116 -19.644  36.279  1.00 51.20           C  
ANISOU 4222  CD1 ILE B 169     7892   5884   5676    748    254   -650       C  
ATOM   4223  N   GLY B 170      77.455 -18.247  33.892  1.00 45.23           N  
ANISOU 4223  N   GLY B 170     6671   5394   5120    721   -429   -882       N  
ATOM   4224  CA  GLY B 170      78.900 -18.088  33.914  1.00 45.93           C  
ANISOU 4224  CA  GLY B 170     6695   5559   5197    759   -590   -968       C  
ATOM   4225  C   GLY B 170      79.391 -17.508  35.229  1.00 51.12           C  
ANISOU 4225  C   GLY B 170     7430   6261   5732    844   -679  -1082       C  
ATOM   4226  O   GLY B 170      78.782 -16.602  35.804  1.00 45.08           O  
ANISOU 4226  O   GLY B 170     6697   5467   4966    824   -636  -1131       O  
ATOM   4227  N   GLU B 171      80.514 -18.049  35.706  1.00 44.84           N  
ANISOU 4227  N   GLU B 171     6664   5541   4831    948   -811  -1132       N  
ATOM   4228  CA  GLU B 171      81.264 -17.501  36.830  1.00 48.77           C  
ANISOU 4228  CA  GLU B 171     7205   6104   5221   1036   -942  -1267       C  
ATOM   4229  C   GLU B 171      82.633 -16.993  36.419  1.00 52.54           C  
ANISOU 4229  C   GLU B 171     7512   6654   5795   1013  -1101  -1389       C  
ATOM   4230  O   GLU B 171      83.073 -15.953  36.907  1.00 50.74           O  
ANISOU 4230  O   GLU B 171     7233   6455   5590    999  -1183  -1527       O  
ATOM   4231  CB  GLU B 171      81.431 -18.553  37.935  1.00 49.57           C  
ANISOU 4231  CB  GLU B 171     7504   6240   5091   1206   -976  -1238       C  
ATOM   4232  CG  GLU B 171      80.155 -19.294  38.299  1.00 51.74           C  
ANISOU 4232  CG  GLU B 171     7955   6434   5268   1232   -799  -1104       C  
ATOM   4233  CD  GLU B 171      80.373 -20.328  39.393  1.00 66.62           C  
ANISOU 4233  CD  GLU B 171    10056   8342   6914   1406   -824  -1068       C  
ATOM   4234  OE1 GLU B 171      81.528 -20.477  39.847  1.00 67.94           O  
ANISOU 4234  OE1 GLU B 171    10231   8595   6989   1518   -996  -1150       O  
ATOM   4235  OE2 GLU B 171      79.395 -20.993  39.798  1.00 65.14           O  
ANISOU 4235  OE2 GLU B 171    10032   8084   6633   1435   -669   -962       O  
ATOM   4236  N   ALA B 172      83.319 -17.708  35.527  1.00 48.06           N  
ANISOU 4236  N   ALA B 172     6852   6115   5293   1003  -1139  -1348       N  
ATOM   4237  CA  ALA B 172      84.570 -17.233  34.955  1.00 50.08           C  
ANISOU 4237  CA  ALA B 172     6923   6431   5674    958  -1262  -1458       C  
ATOM   4238  C   ALA B 172      84.349 -16.409  33.696  1.00 48.67           C  
ANISOU 4238  C   ALA B 172     6587   6196   5711    788  -1182  -1442       C  
ATOM   4239  O   ALA B 172      85.281 -15.744  33.234  1.00 50.33           O  
ANISOU 4239  O   ALA B 172     6640   6436   6046    723  -1254  -1544       O  
ATOM   4240  CB  ALA B 172      85.499 -18.423  34.646  1.00 48.40           C  
ANISOU 4240  CB  ALA B 172     6688   6281   5422   1046  -1344  -1432       C  
ATOM   4241  N   VAL B 173      83.137 -16.444  33.137  1.00 44.82           N  
ANISOU 4241  N   VAL B 173     6139   5623   5266    718  -1032  -1320       N  
ATOM   4242  CA  VAL B 173      82.772 -15.721  31.927  1.00 46.88           C  
ANISOU 4242  CA  VAL B 173     6280   5823   5709    574   -949  -1285       C  
ATOM   4243  C   VAL B 173      81.383 -15.140  32.142  1.00 46.77           C  
ANISOU 4243  C   VAL B 173     6341   5729   5701    533   -829  -1236       C  
ATOM   4244  O   VAL B 173      80.609 -15.619  32.970  1.00 44.34           O  
ANISOU 4244  O   VAL B 173     6174   5407   5266    605   -778  -1192       O  
ATOM   4245  CB  VAL B 173      82.765 -16.625  30.672  1.00 47.03           C  
ANISOU 4245  CB  VAL B 173     6247   5832   5790    537   -898  -1170       C  
ATOM   4246  CG1 VAL B 173      84.145 -17.180  30.399  1.00 50.45           C  
ANISOU 4246  CG1 VAL B 173     6595   6343   6232    577  -1008  -1223       C  
ATOM   4247  CG2 VAL B 173      81.783 -17.772  30.855  1.00 39.56           C  
ANISOU 4247  CG2 VAL B 173     5439   4854   4736    596   -810  -1045       C  
ATOM   4248  N   LYS B 174      81.057 -14.118  31.361  1.00 41.68           N  
ANISOU 4248  N   LYS B 174     5603   5026   5207    420   -774  -1239       N  
ATOM   4249  CA  LYS B 174      79.750 -13.474  31.441  1.00 40.90           C  
ANISOU 4249  CA  LYS B 174     5553   4850   5138    381   -664  -1198       C  
ATOM   4250  C   LYS B 174      78.787 -14.147  30.472  1.00 37.15           C  
ANISOU 4250  C   LYS B 174     5079   4330   4705    346   -557  -1057       C  
ATOM   4251  O   LYS B 174      79.088 -14.265  29.280  1.00 40.65           O  
ANISOU 4251  O   LYS B 174     5429   4769   5246    285   -554  -1012       O  
ATOM   4252  CB  LYS B 174      79.877 -11.987  31.110  1.00 45.58           C  
ANISOU 4252  CB  LYS B 174     6054   5394   5871    289   -663  -1275       C  
ATOM   4253  CG  LYS B 174      78.723 -11.133  31.580  1.00 66.06           C  
ANISOU 4253  CG  LYS B 174     8706   7916   8476    276   -580  -1279       C  
ATOM   4254  CD  LYS B 174      79.195  -9.688  31.753  1.00 74.76           C  
ANISOU 4254  CD  LYS B 174     9747   8984   9674    218   -616  -1403       C  
ATOM   4255  CE  LYS B 174      78.176  -8.847  32.498  1.00 84.37           C  
ANISOU 4255  CE  LYS B 174    11038  10139  10878    228   -549  -1434       C  
ATOM   4256  NZ  LYS B 174      76.877  -8.791  31.780  1.00 86.45           N  
ANISOU 4256  NZ  LYS B 174    11307  10331  11209    198   -428  -1317       N  
ATOM   4257  N   THR B 175      77.634 -14.596  30.987  1.00 37.68           N  
ANISOU 4257  N   THR B 175     5251   4366   4699    384   -466   -995       N  
ATOM   4258  CA  THR B 175      76.584 -15.214  30.173  1.00 33.30           C  
ANISOU 4258  CA  THR B 175     4694   3768   4190    350   -362   -880       C  
ATOM   4259  C   THR B 175      75.285 -14.417  30.182  1.00 35.47           C  
ANISOU 4259  C   THR B 175     4972   3976   4530    312   -263   -866       C  
ATOM   4260  O   THR B 175      74.333 -14.790  29.492  1.00 38.33           O  
ANISOU 4260  O   THR B 175     5313   4302   4946    280   -182   -786       O  
ATOM   4261  CB  THR B 175      76.298 -16.650  30.644  1.00 34.52           C  
ANISOU 4261  CB  THR B 175     4958   3938   4219    423   -321   -812       C  
ATOM   4262  OG1 THR B 175      75.971 -16.647  32.035  1.00 38.75           O  
ANISOU 4262  OG1 THR B 175     5625   4473   4626    498   -297   -847       O  
ATOM   4263  CG2 THR B 175      77.514 -17.545  30.430  1.00 35.65           C  
ANISOU 4263  CG2 THR B 175     5091   4142   4312    467   -415   -810       C  
ATOM   4264  N   GLN B 176      75.232 -13.319  30.925  1.00 37.52           N  
ANISOU 4264  N   GLN B 176     5248   4216   4791    315   -273   -950       N  
ATOM   4265  CA  GLN B 176      74.040 -12.490  31.045  1.00 36.60           C  
ANISOU 4265  CA  GLN B 176     5136   4034   4736    291   -183   -950       C  
ATOM   4266  C   GLN B 176      74.181 -11.305  30.094  1.00 42.50           C  
ANISOU 4266  C   GLN B 176     5776   4738   5635    216   -202   -969       C  
ATOM   4267  O   GLN B 176      75.079 -10.475  30.272  1.00 40.59           O  
ANISOU 4267  O   GLN B 176     5503   4500   5420    196   -273  -1055       O  
ATOM   4268  CB  GLN B 176      73.905 -12.039  32.499  1.00 43.88           C  
ANISOU 4268  CB  GLN B 176     6159   4956   5555    350   -175  -1034       C  
ATOM   4269  CG  GLN B 176      72.995 -10.872  32.743  1.00 58.50           C  
ANISOU 4269  CG  GLN B 176     8006   6744   7478    328   -107  -1073       C  
ATOM   4270  CD  GLN B 176      71.562 -11.302  32.813  1.00 48.14           C  
ANISOU 4270  CD  GLN B 176     6729   5393   6168    339     25  -1003       C  
ATOM   4271  OE1 GLN B 176      71.110 -11.852  33.826  1.00 51.56           O  
ANISOU 4271  OE1 GLN B 176     7272   5835   6485    396     89  -1004       O  
ATOM   4272  NE2 GLN B 176      70.827 -11.059  31.734  1.00 50.84           N  
ANISOU 4272  NE2 GLN B 176     6978   5694   6645    286     70   -946       N  
ATOM   4273  N   PHE B 177      73.316 -11.229  29.078  1.00 35.76           N  
ANISOU 4273  N   PHE B 177     4867   3842   4880    175   -141   -893       N  
ATOM   4274  CA  PHE B 177      73.397 -10.176  28.069  1.00 33.86           C  
ANISOU 4274  CA  PHE B 177     4543   3551   4772    115   -151   -890       C  
ATOM   4275  C   PHE B 177      72.203  -9.228  28.133  1.00 41.81           C  
ANISOU 4275  C   PHE B 177     5550   4485   5850    115    -79   -892       C  
ATOM   4276  O   PHE B 177      71.113  -9.608  28.556  1.00 34.09           O  
ANISOU 4276  O   PHE B 177     4607   3501   4846    148     -7   -869       O  
ATOM   4277  CB  PHE B 177      73.464 -10.777  26.660  1.00 33.49           C  
ANISOU 4277  CB  PHE B 177     4430   3514   4780     79   -155   -799       C  
ATOM   4278  CG  PHE B 177      74.505 -11.851  26.512  1.00 40.04           C  
ANISOU 4278  CG  PHE B 177     5256   4413   5545     86   -213   -787       C  
ATOM   4279  CD1 PHE B 177      75.824 -11.593  26.833  1.00 42.54           C  
ANISOU 4279  CD1 PHE B 177     5555   4762   5844     79   -292   -861       C  
ATOM   4280  CD2 PHE B 177      74.165 -13.110  26.041  1.00 38.64           C  
ANISOU 4280  CD2 PHE B 177     5085   4264   5331    100   -190   -709       C  
ATOM   4281  CE1 PHE B 177      76.790 -12.590  26.701  1.00 40.04           C  
ANISOU 4281  CE1 PHE B 177     5229   4513   5473     97   -349   -855       C  
ATOM   4282  CE2 PHE B 177      75.123 -14.106  25.906  1.00 40.77           C  
ANISOU 4282  CE2 PHE B 177     5356   4592   5543    114   -241   -699       C  
ATOM   4283  CZ  PHE B 177      76.432 -13.842  26.234  1.00 40.81           C  
ANISOU 4283  CZ  PHE B 177     5342   4634   5529    117   -322   -769       C  
ATOM   4284  N   ASN B 178      72.429  -7.980  27.714  1.00 33.97           N  
ANISOU 4284  N   ASN B 178     4519   3434   4956     77    -92   -925       N  
ATOM   4285  CA  ASN B 178      71.343  -7.115  27.269  1.00 33.72           C  
ANISOU 4285  CA  ASN B 178     4466   3326   5019     77    -34   -899       C  
ATOM   4286  C   ASN B 178      70.953  -7.513  25.853  1.00 37.05           C  
ANISOU 4286  C   ASN B 178     4830   3745   5501     60    -28   -796       C  
ATOM   4287  O   ASN B 178      71.818  -7.845  25.036  1.00 35.42           O  
ANISOU 4287  O   ASN B 178     4593   3564   5302     24    -72   -763       O  
ATOM   4288  CB  ASN B 178      71.779  -5.643  27.274  1.00 34.30           C  
ANISOU 4288  CB  ASN B 178     4532   3323   5176     46    -46   -964       C  
ATOM   4289  CG  ASN B 178      71.839  -5.046  28.659  1.00 39.04           C  
ANISOU 4289  CG  ASN B 178     5190   3911   5732     70    -42  -1076       C  
ATOM   4290  OD1 ASN B 178      71.145  -5.482  29.579  1.00 41.05           O  
ANISOU 4290  OD1 ASN B 178     5498   4192   5909    120     -2  -1092       O  
ATOM   4291  ND2 ASN B 178      72.653  -4.009  28.807  1.00 44.80           N  
ANISOU 4291  ND2 ASN B 178     5913   4595   6514     30    -75  -1158       N  
ATOM   4292  N   TYR B 179      69.652  -7.454  25.554  1.00 36.47           N  
ANISOU 4292  N   TYR B 179     4740   3643   5473     88     26   -755       N  
ATOM   4293  CA  TYR B 179      69.118  -7.746  24.226  1.00 33.60           C  
ANISOU 4293  CA  TYR B 179     4322   3278   5165     86     23   -670       C  
ATOM   4294  C   TYR B 179      68.472  -6.510  23.619  1.00 38.64           C  
ANISOU 4294  C   TYR B 179     4942   3836   5905    102     37   -656       C  
ATOM   4295  O   TYR B 179      67.791  -5.755  24.316  1.00 38.65           O  
ANISOU 4295  O   TYR B 179     4958   3790   5937    133     77   -703       O  
ATOM   4296  CB  TYR B 179      68.064  -8.837  24.285  1.00 33.14           C  
ANISOU 4296  CB  TYR B 179     4246   3262   5083    112     66   -637       C  
ATOM   4297  CG  TYR B 179      68.639 -10.221  24.339  1.00 35.97           C  
ANISOU 4297  CG  TYR B 179     4619   3691   5358     97     50   -613       C  
ATOM   4298  CD1 TYR B 179      69.183 -10.731  25.518  1.00 35.16           C  
ANISOU 4298  CD1 TYR B 179     4581   3620   5158    108     57   -657       C  
ATOM   4299  CD2 TYR B 179      68.639 -11.022  23.206  1.00 41.36           C  
ANISOU 4299  CD2 TYR B 179     5259   4405   6052     81     26   -549       C  
ATOM   4300  CE1 TYR B 179      69.704 -12.035  25.557  1.00 37.39           C  
ANISOU 4300  CE1 TYR B 179     4887   3960   5361    106     43   -629       C  
ATOM   4301  CE2 TYR B 179      69.156 -12.303  23.232  1.00 42.30           C  
ANISOU 4301  CE2 TYR B 179     5394   4579   6099     70     15   -528       C  
ATOM   4302  CZ  TYR B 179      69.694 -12.799  24.401  1.00 39.44           C  
ANISOU 4302  CZ  TYR B 179     5097   4242   5645     85     25   -565       C  
ATOM   4303  OH  TYR B 179      70.182 -14.081  24.400  1.00 43.20           O  
ANISOU 4303  OH  TYR B 179     5597   4764   6051     86     15   -538       O  
ATOM   4304  N   TYR B 180      68.648  -6.348  22.306  1.00 35.25           N  
ANISOU 4304  N   TYR B 180     4485   3390   5519     90      7   -589       N  
ATOM   4305  CA  TYR B 180      68.015  -5.281  21.540  1.00 33.29           C  
ANISOU 4305  CA  TYR B 180     4230   3065   5355    121     13   -556       C  
ATOM   4306  C   TYR B 180      67.548  -5.848  20.203  1.00 37.51           C  
ANISOU 4306  C   TYR B 180     4726   3628   5898    142    -16   -472       C  
ATOM   4307  O   TYR B 180      68.151  -6.786  19.672  1.00 37.76           O  
ANISOU 4307  O   TYR B 180     4746   3720   5880    110    -44   -438       O  
ATOM   4308  CB  TYR B 180      68.978  -4.120  21.292  1.00 34.45           C  
ANISOU 4308  CB  TYR B 180     4414   3132   5545     84      8   -568       C  
ATOM   4309  CG  TYR B 180      69.759  -3.662  22.511  1.00 37.04           C  
ANISOU 4309  CG  TYR B 180     4772   3443   5859     48     18   -665       C  
ATOM   4310  CD1 TYR B 180      70.919  -4.322  22.908  1.00 37.81           C  
ANISOU 4310  CD1 TYR B 180     4867   3604   5895     -1    -15   -702       C  
ATOM   4311  CD2 TYR B 180      69.362  -2.538  23.238  1.00 38.52           C  
ANISOU 4311  CD2 TYR B 180     4990   3552   6096     69     52   -728       C  
ATOM   4312  CE1 TYR B 180      71.647  -3.898  24.012  1.00 36.99           C  
ANISOU 4312  CE1 TYR B 180     4786   3494   5774    -26    -23   -803       C  
ATOM   4313  CE2 TYR B 180      70.094  -2.094  24.344  1.00 35.22           C  
ANISOU 4313  CE2 TYR B 180     4600   3120   5661     37     52   -830       C  
ATOM   4314  CZ  TYR B 180      71.238  -2.801  24.730  1.00 35.78           C  
ANISOU 4314  CZ  TYR B 180     4664   3265   5665    -10      9   -870       C  
ATOM   4315  OH  TYR B 180      71.982  -2.397  25.821  1.00 38.91           O  
ANISOU 4315  OH  TYR B 180     5085   3660   6040    -33     -8   -983       O  
ATOM   4316  N   LYS B 181      66.481  -5.269  19.648  1.00 37.31           N  
ANISOU 4316  N   LYS B 181     4681   3561   5932    203    -15   -445       N  
ATOM   4317  CA  LYS B 181      65.944  -5.779  18.388  1.00 33.41           C  
ANISOU 4317  CA  LYS B 181     4151   3102   5441    236    -56   -377       C  
ATOM   4318  C   LYS B 181      65.403  -4.636  17.531  1.00 38.03           C  
ANISOU 4318  C   LYS B 181     4754   3609   6085    302    -73   -334       C  
ATOM   4319  O   LYS B 181      64.847  -3.659  18.049  1.00 41.29           O  
ANISOU 4319  O   LYS B 181     5179   3954   6556    344    -46   -366       O  
ATOM   4320  CB  LYS B 181      64.854  -6.822  18.657  1.00 37.56           C  
ANISOU 4320  CB  LYS B 181     4607   3698   5965    260    -48   -400       C  
ATOM   4321  CG  LYS B 181      64.161  -7.386  17.422  1.00 38.32           C  
ANISOU 4321  CG  LYS B 181     4650   3838   6072    298    -99   -353       C  
ATOM   4322  CD  LYS B 181      63.116  -8.425  17.858  1.00 36.59           C  
ANISOU 4322  CD  LYS B 181     4353   3681   5870    304    -74   -396       C  
ATOM   4323  CE  LYS B 181      62.081  -8.682  16.779  1.00 45.29           C  
ANISOU 4323  CE  LYS B 181     5380   4815   7014    360   -129   -382       C  
ATOM   4324  NZ  LYS B 181      62.518  -9.684  15.787  1.00 46.60           N  
ANISOU 4324  NZ  LYS B 181     5539   5041   7127    332   -180   -342       N  
ATOM   4325  N   LYS B 182      65.595  -4.756  16.216  1.00 36.71           N  
ANISOU 4325  N   LYS B 182     4601   3450   5899    317   -117   -260       N  
ATOM   4326  CA  LYS B 182      65.115  -3.782  15.241  1.00 38.78           C  
ANISOU 4326  CA  LYS B 182     4898   3642   6195    395   -142   -202       C  
ATOM   4327  C   LYS B 182      64.294  -4.492  14.176  1.00 39.59           C  
ANISOU 4327  C   LYS B 182     4953   3813   6275    458   -209   -162       C  
ATOM   4328  O   LYS B 182      64.673  -5.572  13.714  1.00 36.70           O  
ANISOU 4328  O   LYS B 182     4566   3526   5854    417   -234   -146       O  
ATOM   4329  CB  LYS B 182      66.272  -3.054  14.545  1.00 39.97           C  
ANISOU 4329  CB  LYS B 182     5139   3717   6330    358   -125   -143       C  
ATOM   4330  CG  LYS B 182      66.969  -2.010  15.368  1.00 53.46           C  
ANISOU 4330  CG  LYS B 182     6898   5330   8083    310    -65   -184       C  
ATOM   4331  CD  LYS B 182      68.224  -1.507  14.653  1.00 46.96           C  
ANISOU 4331  CD  LYS B 182     6149   4442   7252    250    -34   -134       C  
ATOM   4332  CE  LYS B 182      67.874  -0.630  13.462  1.00 42.30           C  
ANISOU 4332  CE  LYS B 182     5638   3762   6672    326    -34    -41       C  
ATOM   4333  NZ  LYS B 182      69.074   0.092  12.950  1.00 41.18           N  
ANISOU 4333  NZ  LYS B 182     5580   3524   6540    259     29      0       N  
ATOM   4334  N   VAL B 183      63.189  -3.876  13.762  1.00 39.64           N  
ANISOU 4334  N   VAL B 183     4944   3790   6327    562   -244   -153       N  
ATOM   4335  CA  VAL B 183      62.342  -4.418  12.707  1.00 39.98           C  
ANISOU 4335  CA  VAL B 183     4938   3899   6355    638   -324   -128       C  
ATOM   4336  C   VAL B 183      62.050  -3.301  11.719  1.00 44.70           C  
ANISOU 4336  C   VAL B 183     5609   4418   6955    746   -366    -58       C  
ATOM   4337  O   VAL B 183      61.505  -2.260  12.104  1.00 42.73           O  
ANISOU 4337  O   VAL B 183     5376   4090   6769    813   -350    -71       O  
ATOM   4338  CB  VAL B 183      61.035  -5.006  13.267  1.00 46.26           C  
ANISOU 4338  CB  VAL B 183     5607   4759   7210    674   -337   -208       C  
ATOM   4339  CG1 VAL B 183      60.108  -5.429  12.134  1.00 46.51           C  
ANISOU 4339  CG1 VAL B 183     5577   4855   7240    761   -434   -198       C  
ATOM   4340  CG2 VAL B 183      61.346  -6.183  14.182  1.00 42.70           C  
ANISOU 4340  CG2 VAL B 183     5106   4376   6743    570   -285   -263       C  
ATOM   4341  N   ASP B 184      62.405  -3.517  10.451  1.00 45.51           N  
ANISOU 4341  N   ASP B 184     5535   4129   7628   -423   -946    615       N  
ATOM   4342  CA  ASP B 184      62.162  -2.545   9.380  1.00 48.70           C  
ANISOU 4342  CA  ASP B 184     5797   4526   8179   -519  -1038    833       C  
ATOM   4343  C   ASP B 184      62.709  -1.168   9.739  1.00 51.10           C  
ANISOU 4343  C   ASP B 184     5756   4894   8767   -336   -737    743       C  
ATOM   4344  O   ASP B 184      62.065  -0.141   9.507  1.00 47.51           O  
ANISOU 4344  O   ASP B 184     4970   4416   8665   -390   -708    969       O  
ATOM   4345  CB  ASP B 184      60.675  -2.456   9.031  1.00 57.52           C  
ANISOU 4345  CB  ASP B 184     6698   5581   9578   -799  -1311   1262       C  
ATOM   4346  CG  ASP B 184      60.114  -3.775   8.526  1.00 74.77           C  
ANISOU 4346  CG  ASP B 184     9285   7672  11452  -1077  -1713   1406       C  
ATOM   4347  OD1 ASP B 184      58.957  -4.093   8.868  1.00 78.33           O  
ANISOU 4347  OD1 ASP B 184     9528   8087  12148  -1272  -1906   1727       O  
ATOM   4348  OD2 ASP B 184      60.837  -4.500   7.804  1.00 75.79           O  
ANISOU 4348  OD2 ASP B 184     9965   7739  11092  -1094  -1816   1224       O  
ATOM   4349  N   GLY B 185      63.907  -1.155  10.316  1.00 46.16           N  
ANISOU 4349  N   GLY B 185     5212   4332   7996   -136   -526    454       N  
ATOM   4350  CA  GLY B 185      64.629   0.059  10.638  1.00 46.54           C  
ANISOU 4350  CA  GLY B 185     5032   4421   8232    -11   -304    359       C  
ATOM   4351  C   GLY B 185      64.272   0.699  11.962  1.00 48.02           C  
ANISOU 4351  C   GLY B 185     5016   4546   8684     22    -86    281       C  
ATOM   4352  O   GLY B 185      64.882   1.711  12.319  1.00 49.27           O  
ANISOU 4352  O   GLY B 185     5074   4689   8955     81     77    187       O  
ATOM   4353  N   VAL B 186      63.328   0.138  12.707  1.00 44.14           N  
ANISOU 4353  N   VAL B 186     4509   3992   8271    -20    -67    329       N  
ATOM   4354  CA  VAL B 186      62.826   0.741  13.935  1.00 50.06           C  
ANISOU 4354  CA  VAL B 186     5140   4626   9256     37    212    292       C  
ATOM   4355  C   VAL B 186      63.173  -0.166  15.104  1.00 46.45           C  
ANISOU 4355  C   VAL B 186     4892   4190   8567     69    260     64       C  
ATOM   4356  O   VAL B 186      62.900  -1.375  15.067  1.00 45.56           O  
ANISOU 4356  O   VAL B 186     4884   4130   8296     28     91     91       O  
ATOM   4357  CB  VAL B 186      61.308   0.975  13.862  1.00 52.78           C  
ANISOU 4357  CB  VAL B 186     5221   4860   9973     -3    273    651       C  
ATOM   4358  CG1 VAL B 186      60.788   1.541  15.175  1.00 54.22           C  
ANISOU 4358  CG1 VAL B 186     5358   4869  10373    123    676    629       C  
ATOM   4359  CG2 VAL B 186      60.983   1.889  12.696  1.00 56.34           C  
ANISOU 4359  CG2 VAL B 186     5432   5300  10674    -60    202    926       C  
ATOM   4360  N   VAL B 187      63.777   0.414  16.142  1.00 41.75           N  
ANISOU 4360  N   VAL B 187     4394   3537   7932    111    464   -148       N  
ATOM   4361  CA  VAL B 187      64.037  -0.352  17.351  1.00 39.08           C  
ANISOU 4361  CA  VAL B 187     4256   3208   7385    110    509   -334       C  
ATOM   4362  C   VAL B 187      62.709  -0.764  17.965  1.00 45.30           C  
ANISOU 4362  C   VAL B 187     4990   3889   8333    142    652   -198       C  
ATOM   4363  O   VAL B 187      61.753   0.020  18.026  1.00 49.26           O  
ANISOU 4363  O   VAL B 187     5339   4233   9146    198    886     -8       O  
ATOM   4364  CB  VAL B 187      64.913   0.448  18.328  1.00 44.91           C  
ANISOU 4364  CB  VAL B 187     5175   3870   8018     70    646   -546       C  
ATOM   4365  CG1 VAL B 187      65.053  -0.294  19.646  1.00 48.29           C  
ANISOU 4365  CG1 VAL B 187     5833   4290   8227     32    686   -705       C  
ATOM   4366  CG2 VAL B 187      66.289   0.689  17.716  1.00 39.99           C  
ANISOU 4366  CG2 VAL B 187     4533   3390   7271     26    454   -580       C  
ATOM   4367  N  AGLN B 188      62.626  -2.010  18.424  0.66 41.45           N  
ANISOU 4367  N  AGLN B 188     4603   3479   7668    126    539   -244       N  
ATOM   4368  N  BGLN B 188      62.642  -2.018  18.378  0.34 41.13           N  
ANISOU 4368  N  BGLN B 188     4559   3442   7625    125    530   -242       N  
ATOM   4369  CA AGLN B 188      61.362  -2.588  18.870  0.66 44.87           C  
ANISOU 4369  CA AGLN B 188     4939   3843   8268    147    615    -43       C  
ATOM   4370  CA BGLN B 188      61.444  -2.607  18.938  0.34 44.55           C  
ANISOU 4370  CA BGLN B 188     4918   3806   8202    148    618    -68       C  
ATOM   4371  C  AGLN B 188      61.449  -2.970  20.342  0.66 45.76           C  
ANISOU 4371  C  AGLN B 188     5251   3907   8228    192    812   -227       C  
ATOM   4372  C  BGLN B 188      61.587  -2.693  20.444  0.34 43.94           C  
ANISOU 4372  C  BGLN B 188     5050   3652   7993    198    866   -268       C  
ATOM   4373  O  AGLN B 188      62.359  -3.716  20.740  0.66 45.95           O  
ANISOU 4373  O  AGLN B 188     5461   4051   7948    146    666   -444       O  
ATOM   4374  O  BGLN B 188      62.684  -2.903  20.971  0.34 53.68           O  
ANISOU 4374  O  BGLN B 188     6503   4960   8934    149    796   -529       O  
ATOM   4375  CB AGLN B 188      61.005  -3.833  18.031  0.66 48.17           C  
ANISOU 4375  CB AGLN B 188     5326   4369   8608     48    258    121       C  
ATOM   4376  CB BGLN B 188      61.187  -3.991  18.344  0.34 46.36           C  
ANISOU 4376  CB BGLN B 188     5155   4150   8310     62    284     43       C  
ATOM   4377  CG AGLN B 188      59.503  -4.043  17.837  0.66 52.55           C  
ANISOU 4377  CG AGLN B 188     5628   4849   9490     -7    218    538       C  
ATOM   4378  CG BGLN B 188      60.681  -3.924  16.926  0.34 47.74           C  
ANISOU 4378  CG BGLN B 188     5193   4334   8614    -44     33    318       C  
ATOM   4379  CD AGLN B 188      59.170  -5.284  17.023  0.66 52.42           C  
ANISOU 4379  CD AGLN B 188     5686   4895   9336   -190   -211    704       C  
ATOM   4380  CD BGLN B 188      59.309  -3.297  16.855  0.34 54.55           C  
ANISOU 4380  CD BGLN B 188     5724   5084   9919    -57    148    724       C  
ATOM   4381  OE1AGLN B 188      59.385  -6.416  17.470  0.66 50.53           O  
ANISOU 4381  OE1AGLN B 188     5644   4699   8858   -210   -324    570       O  
ATOM   4382  OE1BGLN B 188      58.465  -3.538  17.718  0.34 58.37           O  
ANISOU 4382  OE1BGLN B 188     6092   5497  10588     -1    323    888       O  
ATOM   4383  NE2AGLN B 188      58.632  -5.076  15.824  0.66 53.35           N  
ANISOU 4383  NE2AGLN B 188     5690   4995   9586   -351   -468   1012       N  
ATOM   4384  NE2BGLN B 188      59.079  -2.475  15.837  0.34 60.91           N  
ANISOU 4384  NE2BGLN B 188     6349   5870  10923   -114     80    939       N  
ATOM   4385  N   GLN B 189      60.476  -2.502  21.132  1.00 45.18           N  
ANISOU 4385  N   GLN B 189     5141   3649   8377    293   1167    -92       N  
ATOM   4386  CA  GLN B 189      60.414  -2.798  22.557  1.00 46.63           C  
ANISOU 4386  CA  GLN B 189     5570   3743   8403    345   1412   -240       C  
ATOM   4387  C   GLN B 189      60.213  -4.295  22.760  1.00 57.26           C  
ANISOU 4387  C   GLN B 189     6879   5245   9633    304   1175   -198       C  
ATOM   4388  O   GLN B 189      59.193  -4.845  22.338  1.00 53.64           O  
ANISOU 4388  O   GLN B 189     6166   4801   9415    314   1091    126       O  
ATOM   4389  CB  GLN B 189      59.266  -2.026  23.191  1.00 54.93           C  
ANISOU 4389  CB  GLN B 189     6591   4525   9756    522   1919    -17       C  
ATOM   4390  CG  GLN B 189      59.101  -2.249  24.684  1.00 61.48           C  
ANISOU 4390  CG  GLN B 189     7754   5205  10400    603   2256   -151       C  
ATOM   4391  CD  GLN B 189      60.169  -1.531  25.484  1.00 72.97           C  
ANISOU 4391  CD  GLN B 189     9721   6529  11475    506   2363   -550       C  
ATOM   4392  OE1 GLN B 189      60.886  -0.684  24.951  1.00 77.28           O  
ANISOU 4392  OE1 GLN B 189    10324   7056  11981    415   2262   -673       O  
ATOM   4393  NE2 GLN B 189      60.287  -1.870  26.766  1.00 71.22           N  
ANISOU 4393  NE2 GLN B 189     9889   6212  10960    489   2532   -725       N  
ATOM   4394  N   LEU B 190      61.169  -4.953  23.410  1.00 42.79           N  
ANISOU 4394  N   LEU B 190     5288   3519   7450    234   1047   -475       N  
ATOM   4395  CA  LEU B 190      60.995  -6.363  23.718  1.00 36.47           C  
ANISOU 4395  CA  LEU B 190     4479   2840   6538    209    866   -444       C  
ATOM   4396  C   LEU B 190      60.030  -6.530  24.894  1.00 42.68           C  
ANISOU 4396  C   LEU B 190     5298   3499   7419    308   1181   -337       C  
ATOM   4397  O   LEU B 190      60.049  -5.728  25.832  1.00 47.53           O  
ANISOU 4397  O   LEU B 190     6144   3944   7973    368   1536   -453       O  
ATOM   4398  CB  LEU B 190      62.349  -7.015  24.034  1.00 42.70           C  
ANISOU 4398  CB  LEU B 190     5468   3786   6968    122    656   -707       C  
ATOM   4399  CG  LEU B 190      63.253  -7.151  22.810  1.00 50.73           C  
ANISOU 4399  CG  LEU B 190     6436   4931   7909     85    384   -728       C  
ATOM   4400  CD1 LEU B 190      64.650  -7.672  23.182  1.00 47.84           C  
ANISOU 4400  CD1 LEU B 190     6203   4706   7266     37    254   -882       C  
ATOM   4401  CD2 LEU B 190      62.600  -8.059  21.765  1.00 43.34           C  
ANISOU 4401  CD2 LEU B 190     5399   4022   7046     81    164   -539       C  
ATOM   4402  N   PRO B 191      59.174  -7.552  24.867  1.00 45.63           N  
ANISOU 4402  N   PRO B 191     5488   3922   7926    319   1072    -94       N  
ATOM   4403  CA  PRO B 191      58.163  -7.694  25.920  1.00 44.95           C  
ANISOU 4403  CA  PRO B 191     5370   3713   7994    450   1414     97       C  
ATOM   4404  C   PRO B 191      58.768  -8.131  27.243  1.00 43.29           C  
ANISOU 4404  C   PRO B 191     5498   3517   7433    445   1529   -194       C  
ATOM   4405  O   PRO B 191      59.817  -8.777  27.296  1.00 45.09           O  
ANISOU 4405  O   PRO B 191     5870   3908   7354    316   1235   -446       O  
ATOM   4406  CB  PRO B 191      57.231  -8.776  25.362  1.00 49.88           C  
ANISOU 4406  CB  PRO B 191     5680   4424   8849    394   1128    472       C  
ATOM   4407  CG  PRO B 191      58.155  -9.629  24.516  1.00 43.13           C  
ANISOU 4407  CG  PRO B 191     4933   3741   7714    217    637    266       C  
ATOM   4408  CD  PRO B 191      59.073  -8.621  23.859  1.00 42.95           C  
ANISOU 4408  CD  PRO B 191     5009   3720   7591    202    637     44       C  
ATOM   4409  N   GLU B 192      58.086  -7.771  28.326  1.00 45.85           N  
ANISOU 4409  N   GLU B 192     5957   3652   7813    596   1991   -114       N  
ATOM   4410  CA  GLU B 192      58.369  -8.385  29.618  1.00 46.88           C  
ANISOU 4410  CA  GLU B 192     6390   3790   7631    581   2091   -298       C  
ATOM   4411  C   GLU B 192      58.137  -9.885  29.517  1.00 48.54           C  
ANISOU 4411  C   GLU B 192     6360   4212   7873    528   1750   -162       C  
ATOM   4412  O   GLU B 192      57.160 -10.332  28.912  1.00 49.39           O  
ANISOU 4412  O   GLU B 192     6104   4340   8323    574   1660    207       O  
ATOM   4413  CB  GLU B 192      57.482  -7.776  30.707  1.00 52.84           C  
ANISOU 4413  CB  GLU B 192     7360   4257   8459    799   2719   -167       C  
ATOM   4414  CG  GLU B 192      57.617  -6.270  30.806  1.00 56.54           C  
ANISOU 4414  CG  GLU B 192     8153   4438   8893    868   3117   -287       C  
ATOM   4415  CD  GLU B 192      59.060  -5.833  31.006  1.00 79.29           C  
ANISOU 4415  CD  GLU B 192    11470   7346  11311    607   2866   -738       C  
ATOM   4416  OE1 GLU B 192      59.715  -6.359  31.933  1.00 83.02           O  
ANISOU 4416  OE1 GLU B 192    12279   7875  11389    450   2745   -962       O  
ATOM   4417  OE2 GLU B 192      59.543  -4.976  30.232  1.00 83.95           O  
ANISOU 4417  OE2 GLU B 192    12038   7910  11950    537   2761   -818       O  
ATOM   4418  N   THR B 193      59.045 -10.672  30.098  1.00 41.94           N  
ANISOU 4418  N   THR B 193     5728   3522   6687    401   1533   -418       N  
ATOM   4419  CA  THR B 193      59.057 -12.101  29.810  1.00 40.46           C  
ANISOU 4419  CA  THR B 193     5353   3525   6495    332   1162   -336       C  
ATOM   4420  C   THR B 193      59.580 -12.896  31.004  1.00 48.07           C  
ANISOU 4420  C   THR B 193     6533   4577   7156    278   1152   -501       C  
ATOM   4421  O   THR B 193      60.388 -12.402  31.797  1.00 41.58           O  
ANISOU 4421  O   THR B 193     6033   3730   6036    197   1252   -743       O  
ATOM   4422  CB  THR B 193      59.905 -12.391  28.549  1.00 42.64           C  
ANISOU 4422  CB  THR B 193     5558   3936   6707    214    750   -431       C  
ATOM   4423  OG1 THR B 193      59.798 -13.771  28.197  1.00 37.75           O  
ANISOU 4423  OG1 THR B 193     4843   3424   6076    161    439   -331       O  
ATOM   4424  CG2 THR B 193      61.382 -12.035  28.773  1.00 45.10           C  
ANISOU 4424  CG2 THR B 193     6104   4328   6702    116    675   -739       C  
ATOM   4425  N   TYR B 194      59.068 -14.119  31.153  1.00 45.62           N  
ANISOU 4425  N   TYR B 194     6055   4354   6922    290   1007   -332       N  
ATOM   4426  CA  TYR B 194      59.751 -15.117  31.960  1.00 45.92           C  
ANISOU 4426  CA  TYR B 194     6226   4533   6688    208    864   -474       C  
ATOM   4427  C   TYR B 194      60.838 -15.778  31.116  1.00 38.36           C  
ANISOU 4427  C   TYR B 194     5242   3729   5605    100    474   -592       C  
ATOM   4428  O   TYR B 194      60.843 -15.674  29.888  1.00 44.47           O  
ANISOU 4428  O   TYR B 194     5909   4488   6500     97    308   -541       O  
ATOM   4429  CB  TYR B 194      58.774 -16.182  32.472  1.00 44.09           C  
ANISOU 4429  CB  TYR B 194     5830   4320   6603    275    880   -227       C  
ATOM   4430  CG  TYR B 194      57.739 -15.683  33.458  1.00 42.73           C  
ANISOU 4430  CG  TYR B 194     5690   3991   6553    438   1347    -49       C  
ATOM   4431  CD1 TYR B 194      58.012 -15.641  34.817  1.00 43.10           C  
ANISOU 4431  CD1 TYR B 194     6061   4008   6308    447   1604   -203       C  
ATOM   4432  CD2 TYR B 194      56.489 -15.258  33.027  1.00 50.67           C  
ANISOU 4432  CD2 TYR B 194     6422   4863   7970    586   1553    323       C  
ATOM   4433  CE1 TYR B 194      57.068 -15.183  35.727  1.00 46.29           C  
ANISOU 4433  CE1 TYR B 194     6583   4218   6787    641   2121    -33       C  
ATOM   4434  CE2 TYR B 194      55.535 -14.801  33.923  1.00 53.65           C  
ANISOU 4434  CE2 TYR B 194     6818   5066   8499    802   2080    559       C  
ATOM   4435  CZ  TYR B 194      55.830 -14.769  35.273  1.00 54.95           C  
ANISOU 4435  CZ  TYR B 194     7376   5172   8331    850   2396    358       C  
ATOM   4436  OH  TYR B 194      54.880 -14.318  36.168  1.00 57.13           O  
ANISOU 4436  OH  TYR B 194     7755   5227   8725   1108   3004    601       O  
ATOM   4437  N   PHE B 195      61.755 -16.478  31.779  1.00 36.23           N  
ANISOU 4437  N   PHE B 195     5083   3592   5093     20    356   -710       N  
ATOM   4438  CA  PHE B 195      62.749 -17.289  31.086  1.00 36.38           C  
ANISOU 4438  CA  PHE B 195     5064   3733   5027    -19     78   -741       C  
ATOM   4439  C   PHE B 195      62.701 -18.726  31.589  1.00 40.59           C  
ANISOU 4439  C   PHE B 195     5560   4349   5513    -16    -39   -662       C  
ATOM   4440  O   PHE B 195      62.549 -18.953  32.789  1.00 42.00           O  
ANISOU 4440  O   PHE B 195     5785   4572   5599    -48     60   -663       O  
ATOM   4441  CB  PHE B 195      64.155 -16.708  31.291  1.00 40.84           C  
ANISOU 4441  CB  PHE B 195     5734   4387   5396   -120     36   -868       C  
ATOM   4442  CG  PHE B 195      64.377 -15.420  30.557  1.00 44.22           C  
ANISOU 4442  CG  PHE B 195     6185   4738   5878   -128     89   -933       C  
ATOM   4443  CD1 PHE B 195      64.241 -15.378  29.177  1.00 38.95           C  
ANISOU 4443  CD1 PHE B 195     5411   4029   5360    -41      8   -882       C  
ATOM   4444  CD2 PHE B 195      64.723 -14.261  31.234  1.00 42.53           C  
ANISOU 4444  CD2 PHE B 195     6153   4468   5537   -246    205  -1042       C  
ATOM   4445  CE1 PHE B 195      64.441 -14.187  28.479  1.00 44.37           C  
ANISOU 4445  CE1 PHE B 195     6095   4654   6110    -45     56   -927       C  
ATOM   4446  CE2 PHE B 195      64.926 -13.073  30.547  1.00 43.10           C  
ANISOU 4446  CE2 PHE B 195     6246   4457   5673   -256    249  -1093       C  
ATOM   4447  CZ  PHE B 195      64.788 -13.043  29.161  1.00 35.46           C  
ANISOU 4447  CZ  PHE B 195     5093   3485   4896   -141    179  -1030       C  
ATOM   4448  N   THR B 196      62.826 -19.689  30.674  1.00 39.12           N  
ANISOU 4448  N   THR B 196     5345   4156   5364     18   -233   -594       N  
ATOM   4449  CA  THR B 196      63.024 -21.076  31.076  1.00 42.63           C  
ANISOU 4449  CA  THR B 196     5796   4660   5742     25   -341   -532       C  
ATOM   4450  C   THR B 196      64.439 -21.254  31.628  1.00 41.85           C  
ANISOU 4450  C   THR B 196     5715   4711   5475      1   -338   -578       C  
ATOM   4451  O   THR B 196      65.326 -20.428  31.400  1.00 37.24           O  
ANISOU 4451  O   THR B 196     5141   4171   4837    -28   -314   -628       O  
ATOM   4452  CB  THR B 196      62.772 -22.042  29.909  1.00 41.81           C  
ANISOU 4452  CB  THR B 196     5779   4431   5677     56   -526   -448       C  
ATOM   4453  OG1 THR B 196      63.515 -21.632  28.749  1.00 39.92           O  
ANISOU 4453  OG1 THR B 196     5658   4131   5378    102   -540   -511       O  
ATOM   4454  CG2 THR B 196      61.273 -22.111  29.561  1.00 35.47           C  
ANISOU 4454  CG2 THR B 196     4913   3499   5065     -4   -632   -282       C  
ATOM   4455  N   GLN B 197      64.642 -22.342  32.374  1.00 39.47           N  
ANISOU 4455  N   GLN B 197     5385   4494   5119     -6   -383   -503       N  
ATOM   4456  CA  GLN B 197      65.861 -22.517  33.155  1.00 41.53           C  
ANISOU 4456  CA  GLN B 197     5601   4922   5259    -76   -401   -451       C  
ATOM   4457  C   GLN B 197      66.876 -23.455  32.502  1.00 41.70           C  
ANISOU 4457  C   GLN B 197     5582   4959   5304     44   -434   -312       C  
ATOM   4458  O   GLN B 197      68.010 -23.549  32.989  1.00 41.53           O  
ANISOU 4458  O   GLN B 197     5447   5082   5249     -4   -451   -166       O  
ATOM   4459  CB  GLN B 197      65.515 -23.022  34.560  1.00 41.88           C  
ANISOU 4459  CB  GLN B 197     5630   5061   5221   -171   -397   -415       C  
ATOM   4460  CG  GLN B 197      64.641 -22.056  35.357  1.00 41.45           C  
ANISOU 4460  CG  GLN B 197     5691   4954   5104   -251   -256   -522       C  
ATOM   4461  CD  GLN B 197      65.406 -20.816  35.808  1.00 54.16           C  
ANISOU 4461  CD  GLN B 197     7455   6590   6532   -424   -233   -612       C  
ATOM   4462  OE1 GLN B 197      66.526 -20.912  36.311  1.00 49.20           O  
ANISOU 4462  OE1 GLN B 197     6825   6099   5770   -587   -375   -531       O  
ATOM   4463  NE2 GLN B 197      64.806 -19.648  35.619  1.00 47.41           N  
ANISOU 4463  NE2 GLN B 197     6736   5590   5688   -409    -71   -733       N  
ATOM   4464  N   SER B 198      66.499 -24.139  31.424  1.00 40.25           N  
ANISOU 4464  N   SER B 198     5519   4603   5172    187   -434   -311       N  
ATOM   4465  CA  SER B 198      67.440 -24.869  30.569  1.00 42.70           C  
ANISOU 4465  CA  SER B 198     5914   4832   5477    363   -356   -192       C  
ATOM   4466  C   SER B 198      68.186 -25.964  31.327  1.00 42.64           C  
ANISOU 4466  C   SER B 198     5794   4924   5481    415   -315      6       C  
ATOM   4467  O   SER B 198      69.361 -26.228  31.061  1.00 45.31           O  
ANISOU 4467  O   SER B 198     6062   5289   5863    551   -184    210       O  
ATOM   4468  CB  SER B 198      68.437 -23.912  29.906  1.00 41.66           C  
ANISOU 4468  CB  SER B 198     5732   4734   5362    419   -267   -150       C  
ATOM   4469  OG  SER B 198      67.784 -22.955  29.097  1.00 42.00           O  
ANISOU 4469  OG  SER B 198     5881   4671   5405    388   -295   -313       O  
ATOM   4470  N   ARG B 199      67.509 -26.609  32.273  1.00 37.35           N  
ANISOU 4470  N   ARG B 199     5077   4310   4803    323   -403     -2       N  
ATOM   4471  CA  ARG B 199      68.110 -27.695  33.031  1.00 39.81           C  
ANISOU 4471  CA  ARG B 199     5268   4719   5140    359   -379    199       C  
ATOM   4472  C   ARG B 199      67.785 -29.036  32.373  1.00 41.99           C  
ANISOU 4472  C   ARG B 199     5776   4756   5424    528   -326    232       C  
ATOM   4473  O   ARG B 199      67.009 -29.119  31.421  1.00 43.62           O  
ANISOU 4473  O   ARG B 199     6265   4726   5582    554   -370     97       O  
ATOM   4474  CB  ARG B 199      67.628 -27.666  34.483  1.00 40.27           C  
ANISOU 4474  CB  ARG B 199     5180   4966   5157    158   -494    188       C  
ATOM   4475  CG  ARG B 199      68.078 -26.417  35.238  1.00 45.47           C  
ANISOU 4475  CG  ARG B 199     5744   5804   5728    -51   -545    167       C  
ATOM   4476  CD  ARG B 199      67.428 -26.277  36.601  1.00 41.21           C  
ANISOU 4476  CD  ARG B 199     5220   5370   5067   -244   -604    106       C  
ATOM   4477  NE  ARG B 199      66.012 -25.938  36.490  1.00 46.77           N  
ANISOU 4477  NE  ARG B 199     6049   5938   5785   -208   -540    -84       N  
ATOM   4478  CZ  ARG B 199      65.263 -25.500  37.499  1.00 51.02           C  
ANISOU 4478  CZ  ARG B 199     6665   6498   6223   -313   -480   -154       C  
ATOM   4479  NH1 ARG B 199      65.793 -25.352  38.706  1.00 51.09           N  
ANISOU 4479  NH1 ARG B 199     6724   6647   6039   -505   -515   -107       N  
ATOM   4480  NH2 ARG B 199      63.981 -25.218  37.305  1.00 43.65           N  
ANISOU 4480  NH2 ARG B 199     5776   5428   5380   -231   -373   -223       N  
ATOM   4481  N   ASN B 200      68.409 -30.096  32.869  1.00 46.24           N  
ANISOU 4481  N   ASN B 200     6226   5332   6011    618   -246    442       N  
ATOM   4482  CA  ASN B 200      68.139 -31.429  32.351  1.00 51.63           C  
ANISOU 4482  CA  ASN B 200     7195   5747   6676    770   -176    477       C  
ATOM   4483  C   ASN B 200      67.838 -32.378  33.503  1.00 48.08           C  
ANISOU 4483  C   ASN B 200     6577   5414   6277    694   -267    583       C  
ATOM   4484  O   ASN B 200      68.087 -32.077  34.674  1.00 53.28           O  
ANISOU 4484  O   ASN B 200     6904   6367   6975    554   -340    674       O  
ATOM   4485  CB  ASN B 200      69.297 -31.954  31.493  1.00 61.63           C  
ANISOU 4485  CB  ASN B 200     8628   6827   7964   1066    142    672       C  
ATOM   4486  CG  ASN B 200      70.602 -32.000  32.241  1.00 70.82           C  
ANISOU 4486  CG  ASN B 200     9370   8241   9296   1142    288   1026       C  
ATOM   4487  OD1 ASN B 200      70.863 -32.941  32.989  1.00 77.56           O  
ANISOU 4487  OD1 ASN B 200    10069   9161  10240   1174    324   1237       O  
ATOM   4488  ND2 ASN B 200      71.440 -30.988  32.036  1.00 73.25           N  
ANISOU 4488  ND2 ASN B 200     9469   8693   9671   1149    349   1147       N  
ATOM   4489  N   LEU B 201      67.289 -33.541  33.142  1.00 50.19           N  
ANISOU 4489  N   LEU B 201     7133   5422   6516    760   -280    577       N  
ATOM   4490  CA  LEU B 201      66.716 -34.452  34.132  1.00 61.15           C  
ANISOU 4490  CA  LEU B 201     8393   6885   7955    668   -410    652       C  
ATOM   4491  C   LEU B 201      67.762 -34.955  35.116  1.00 64.11           C  
ANISOU 4491  C   LEU B 201     8434   7488   8437    734   -283    922       C  
ATOM   4492  O   LEU B 201      67.578 -34.859  36.334  1.00 82.16           O  
ANISOU 4492  O   LEU B 201    10416  10051  10751    565   -415    978       O  
ATOM   4493  CB  LEU B 201      66.049 -35.632  33.428  1.00 64.46           C  
ANISOU 4493  CB  LEU B 201     9248   6931   8314    709   -464    626       C  
ATOM   4494  CG  LEU B 201      64.543 -35.527  33.241  1.00 66.79           C  
ANISOU 4494  CG  LEU B 201     9672   7122   8583    482   -784    503       C  
ATOM   4495  CD1 LEU B 201      63.956 -36.917  33.092  1.00 71.34           C  
ANISOU 4495  CD1 LEU B 201    10560   7415   9133    440   -919    580       C  
ATOM   4496  CD2 LEU B 201      63.925 -34.800  34.416  1.00 67.53           C  
ANISOU 4496  CD2 LEU B 201     9313   7562   8784    325   -904    508       C  
ATOM   4497  N   GLN B 202      68.866 -35.501  34.605  1.00 68.42           N  
ANISOU 4497  N   GLN B 202     9043   7906   9048    981     -6   1136       N  
ATOM   4498  CA  GLN B 202      69.831 -36.178  35.471  1.00 84.58           C  
ANISOU 4498  CA  GLN B 202    10744  10134  11256   1055    119   1500       C  
ATOM   4499  C   GLN B 202      70.490 -35.202  36.439  1.00 90.16           C  
ANISOU 4499  C   GLN B 202    10987  11254  12017    846    -13   1659       C  
ATOM   4500  O   GLN B 202      70.581 -35.468  37.644  1.00 97.50           O  
ANISOU 4500  O   GLN B 202    11621  12438  12985    673   -157   1825       O  
ATOM   4501  CB  GLN B 202      70.891 -36.874  34.624  1.00 90.22           C  
ANISOU 4501  CB  GLN B 202    11619  10588  12073   1418    529   1771       C  
ATOM   4502  CG  GLN B 202      70.347 -37.580  33.404  1.00105.91           C  
ANISOU 4502  CG  GLN B 202    14269  12074  13900   1604    685   1564       C  
ATOM   4503  CD  GLN B 202      71.205 -37.333  32.180  1.00122.63           C  
ANISOU 4503  CD  GLN B 202    16678  13925  15990   1914   1080   1652       C  
ATOM   4504  OE1 GLN B 202      71.373 -38.215  31.336  1.00132.73           O  
ANISOU 4504  OE1 GLN B 202    18489  14762  17179   2187   1409   1687       O  
ATOM   4505  NE2 GLN B 202      71.753 -36.125  32.077  1.00124.30           N  
ANISOU 4505  NE2 GLN B 202    16592  14375  16261   1876   1071   1699       N  
ATOM   4506  N   GLU B 203      70.961 -34.066  35.926  1.00 80.63           N  
ANISOU 4506  N   GLU B 203     9752  10097  10787    828     11   1623       N  
ATOM   4507  CA  GLU B 203      71.723 -33.100  36.706  1.00 78.20           C  
ANISOU 4507  CA  GLU B 203     9085  10122  10507    594   -138   1814       C  
ATOM   4508  C   GLU B 203      70.850 -31.983  37.267  1.00 68.38           C  
ANISOU 4508  C   GLU B 203     7913   9008   9060    285   -401   1471       C  
ATOM   4509  O   GLU B 203      71.344 -30.875  37.497  1.00 68.47           O  
ANISOU 4509  O   GLU B 203     7821   9175   9018     93   -512   1504       O  
ATOM   4510  CB  GLU B 203      72.839 -32.499  35.856  1.00 82.97           C  
ANISOU 4510  CB  GLU B 203     9595  10697  11232    751     48   2047       C  
ATOM   4511  CG  GLU B 203      73.530 -33.471  34.921  1.00 93.31           C  
ANISOU 4511  CG  GLU B 203    10997  11742  12713   1173    459   2323       C  
ATOM   4512  CD  GLU B 203      74.621 -32.799  34.108  1.00103.29           C  
ANISOU 4512  CD  GLU B 203    12138  12988  14120   1354    686   2607       C  
ATOM   4513  OE1 GLU B 203      75.703 -33.404  33.940  1.00109.78           O  
ANISOU 4513  OE1 GLU B 203    12738  13776  15198   1625   1006   3128       O  
ATOM   4514  OE2 GLU B 203      74.397 -31.659  33.645  1.00104.43           O  
ANISOU 4514  OE2 GLU B 203    12382  13150  14148   1239    568   2353       O  
ATOM   4515  N   PHE B 204      69.566 -32.244  37.484  1.00 61.99           N  
ANISOU 4515  N   PHE B 204     8182   7933   7440    424  -1392   -456       N  
ATOM   4516  CA  PHE B 204      68.662 -31.182  37.900  1.00 50.16           C  
ANISOU 4516  CA  PHE B 204     6901   6390   5768    252  -1216   -377       C  
ATOM   4517  C   PHE B 204      69.034 -30.676  39.287  1.00 56.69           C  
ANISOU 4517  C   PHE B 204     7970   7188   6380    188  -1350   -298       C  
ATOM   4518  O   PHE B 204      69.107 -31.450  40.244  1.00 65.21           O  
ANISOU 4518  O   PHE B 204     9238   8156   7382    265  -1489   -187       O  
ATOM   4519  CB  PHE B 204      67.217 -31.673  37.890  1.00 47.72           C  
ANISOU 4519  CB  PHE B 204     6756   5891   5484    253  -1013   -299       C  
ATOM   4520  CG  PHE B 204      66.218 -30.579  38.114  1.00 46.54           C  
ANISOU 4520  CG  PHE B 204     6756   5710   5219    110   -802   -262       C  
ATOM   4521  CD1 PHE B 204      65.928 -30.131  39.397  1.00 54.43           C  
ANISOU 4521  CD1 PHE B 204     8038   6625   6017     40   -780   -189       C  
ATOM   4522  CD2 PHE B 204      65.582 -29.979  37.040  1.00 46.52           C  
ANISOU 4522  CD2 PHE B 204     6601   5768   5305     53   -635   -310       C  
ATOM   4523  CE1 PHE B 204      65.018 -29.112  39.601  1.00 60.85           C  
ANISOU 4523  CE1 PHE B 204     8962   7395   6761    -64   -575   -203       C  
ATOM   4524  CE2 PHE B 204      64.668 -28.961  37.239  1.00 52.33           C  
ANISOU 4524  CE2 PHE B 204     7451   6444   5990    -42   -463   -280       C  
ATOM   4525  CZ  PHE B 204      64.389 -28.527  38.519  1.00 57.84           C  
ANISOU 4525  CZ  PHE B 204     8411   7037   6528    -91   -423   -246       C  
ATOM   4526  N   LYS B 205      69.251 -29.367  39.394  1.00 52.34           N  
ANISOU 4526  N   LYS B 205     7426   6734   5726     34  -1316   -352       N  
ATOM   4527  CA  LYS B 205      69.541 -28.712  40.655  1.00 62.42           C  
ANISOU 4527  CA  LYS B 205     8935   8003   6779    -62  -1424   -334       C  
ATOM   4528  C   LYS B 205      68.492 -27.645  40.934  1.00 58.10           C  
ANISOU 4528  C   LYS B 205     8588   7358   6128   -199  -1186   -353       C  
ATOM   4529  O   LYS B 205      68.187 -26.835  40.047  1.00 57.34           O  
ANISOU 4529  O   LYS B 205     8359   7272   6155   -271  -1040   -404       O  
ATOM   4530  CB  LYS B 205      70.939 -28.080  40.636  1.00 68.53           C  
ANISOU 4530  CB  LYS B 205     9515   8965   7558   -131  -1645   -433       C  
ATOM   4531  CG  LYS B 205      72.066 -29.099  40.661  1.00 72.18           C  
ANISOU 4531  CG  LYS B 205     9782   9528   8114     29  -1923   -432       C  
ATOM   4532  CD  LYS B 205      73.426 -28.432  40.504  1.00 79.89           C  
ANISOU 4532  CD  LYS B 205    10490  10729   9135    -57  -2114   -552       C  
ATOM   4533  CE  LYS B 205      74.548 -29.380  40.894  1.00 87.42           C  
ANISOU 4533  CE  LYS B 205    11282  11773  10160    120  -2442   -550       C  
ATOM   4534  NZ  LYS B 205      74.366 -30.726  40.285  1.00 91.80           N  
ANISOU 4534  NZ  LYS B 205    11717  12241  10923    361  -2427   -524       N  
ATOM   4535  N   PRO B 206      67.910 -27.618  42.130  1.00 56.88           N  
ANISOU 4535  N   PRO B 206     8746   7112   5753   -233  -1139   -311       N  
ATOM   4536  CA  PRO B 206      66.922 -26.581  42.448  1.00 58.68           C  
ANISOU 4536  CA  PRO B 206     9142   7247   5906   -339   -898   -381       C  
ATOM   4537  C   PRO B 206      67.575 -25.214  42.558  1.00 61.85           C  
ANISOU 4537  C   PRO B 206     9526   7688   6286   -478   -969   -526       C  
ATOM   4538  O   PRO B 206      68.751 -25.088  42.906  1.00 65.70           O  
ANISOU 4538  O   PRO B 206     9969   8292   6700   -527  -1219   -570       O  
ATOM   4539  CB  PRO B 206      66.358 -27.035  43.797  1.00 59.19           C  
ANISOU 4539  CB  PRO B 206     9533   7266   5690   -348   -849   -319       C  
ATOM   4540  CG  PRO B 206      67.484 -27.815  44.414  1.00 67.52           C  
ANISOU 4540  CG  PRO B 206    10627   8417   6610   -302  -1174   -231       C  
ATOM   4541  CD  PRO B 206      68.169 -28.513  43.270  1.00 64.64           C  
ANISOU 4541  CD  PRO B 206     9942   8086   6532   -178  -1310   -198       C  
ATOM   4542  N   ARG B 207      66.791 -24.174  42.265  1.00 58.00           N  
ANISOU 4542  N   ARG B 207     9063   7082   5891   -543   -759   -603       N  
ATOM   4543  CA  ARG B 207      67.309 -22.812  42.224  1.00 52.52           C  
ANISOU 4543  CA  ARG B 207     8350   6355   5251   -688   -809   -734       C  
ATOM   4544  C   ARG B 207      66.534 -21.868  43.135  1.00 56.96           C  
ANISOU 4544  C   ARG B 207     9171   6760   5710   -750   -649   -887       C  
ATOM   4545  O   ARG B 207      66.660 -20.645  43.005  1.00 59.96           O  
ANISOU 4545  O   ARG B 207     9551   7022   6208   -858   -639  -1007       O  
ATOM   4546  CB  ARG B 207      67.317 -22.293  40.784  1.00 51.23           C  
ANISOU 4546  CB  ARG B 207     7925   6173   5367   -716   -753   -678       C  
ATOM   4547  CG  ARG B 207      68.306 -23.050  39.911  1.00 54.61           C  
ANISOU 4547  CG  ARG B 207     8073   6806   5870   -688   -911   -598       C  
ATOM   4548  CD  ARG B 207      68.380 -22.557  38.479  1.00 55.13           C  
ANISOU 4548  CD  ARG B 207     7887   6920   6141   -750   -848   -533       C  
ATOM   4549  NE  ARG B 207      69.476 -23.231  37.781  1.00 58.44           N  
ANISOU 4549  NE  ARG B 207     8029   7582   6595   -739   -987   -518       N  
ATOM   4550  CZ  ARG B 207      69.694 -23.177  36.471  1.00 58.22           C  
ANISOU 4550  CZ  ARG B 207     7744   7696   6681   -781   -938   -462       C  
ATOM   4551  NH1 ARG B 207      68.884 -22.477  35.688  1.00 49.10           N  
ANISOU 4551  NH1 ARG B 207     6588   6454   5613   -838   -787   -372       N  
ATOM   4552  NH2 ARG B 207      70.727 -23.828  35.945  1.00 52.44           N  
ANISOU 4552  NH2 ARG B 207     6746   7208   5969   -760  -1044   -500       N  
ATOM   4553  N   SER B 208      65.743 -22.410  44.056  1.00 59.56           N  
ANISOU 4553  N   SER B 208     9720   7080   5830   -692   -515   -895       N  
ATOM   4554  CA  SER B 208      65.039 -21.606  45.044  1.00 63.00           C  
ANISOU 4554  CA  SER B 208    10402   7417   6119   -745   -340  -1089       C  
ATOM   4555  C   SER B 208      64.674 -22.510  46.207  1.00 60.23           C  
ANISOU 4555  C   SER B 208    10292   7179   5414   -727   -286  -1051       C  
ATOM   4556  O   SER B 208      64.705 -23.736  46.092  1.00 56.29           O  
ANISOU 4556  O   SER B 208     9760   6762   4867   -654   -344   -841       O  
ATOM   4557  CB  SER B 208      63.780 -20.954  44.463  1.00 64.47           C  
ANISOU 4557  CB  SER B 208    10522   7408   6565   -679    -52  -1138       C  
ATOM   4558  OG  SER B 208      62.744 -21.910  44.306  1.00 59.01           O  
ANISOU 4558  OG  SER B 208     9799   6738   5883   -569    144  -1008       O  
ATOM   4559  N   GLN B 209      64.320 -21.886  47.331  1.00 58.07           N  
ANISOU 4559  N   GLN B 209    10270   6905   4889   -803   -169  -1258       N  
ATOM   4560  CA  GLN B 209      63.894 -22.666  48.488  1.00 62.76           C  
ANISOU 4560  CA  GLN B 209    11121   7639   5088   -823    -80  -1210       C  
ATOM   4561  C   GLN B 209      62.636 -23.462  48.174  1.00 62.31           C  
ANISOU 4561  C   GLN B 209    11011   7536   5128   -732    214  -1056       C  
ATOM   4562  O   GLN B 209      62.464 -24.587  48.659  1.00 63.93           O  
ANISOU 4562  O   GLN B 209    11332   7840   5117   -734    217   -855       O  
ATOM   4563  CB  GLN B 209      63.656 -21.755  49.691  1.00 66.04           C  
ANISOU 4563  CB  GLN B 209    11804   8091   5199   -933     43  -1516       C  
ATOM   4564  CG  GLN B 209      63.306 -22.513  50.960  1.00 73.93           C  
ANISOU 4564  CG  GLN B 209    13095   9294   5701   -996    130  -1457       C  
ATOM   4565  CD  GLN B 209      64.404 -23.477  51.378  1.00 78.60           C  
ANISOU 4565  CD  GLN B 209    13776  10064   6025  -1029   -248  -1210       C  
ATOM   4566  OE1 GLN B 209      65.590 -23.164  51.281  1.00 80.96           O  
ANISOU 4566  OE1 GLN B 209    14008  10403   6350  -1064   -587  -1253       O  
ATOM   4567  NE2 GLN B 209      64.012 -24.656  51.839  1.00 82.07           N  
ANISOU 4567  NE2 GLN B 209    14350  10600   6232  -1021   -199   -941       N  
ATOM   4568  N   MET B 210      61.745 -22.893  47.362  1.00 57.58           N  
ANISOU 4568  N   MET B 210    10232   6778   4868   -659    444  -1133       N  
ATOM   4569  CA  MET B 210      60.537 -23.614  46.986  1.00 56.73           C  
ANISOU 4569  CA  MET B 210    10025   6637   4893   -583    707  -1004       C  
ATOM   4570  C   MET B 210      60.872 -24.865  46.182  1.00 57.10           C  
ANISOU 4570  C   MET B 210     9920   6707   5067   -527    540   -720       C  
ATOM   4571  O   MET B 210      60.277 -25.930  46.396  1.00 56.15           O  
ANISOU 4571  O   MET B 210     9843   6616   4874   -526    650   -556       O  
ATOM   4572  CB  MET B 210      59.604 -22.700  46.195  1.00 55.11           C  
ANISOU 4572  CB  MET B 210     9619   6262   5059   -499    921  -1137       C  
ATOM   4573  CG  MET B 210      58.330 -23.393  45.759  1.00 53.83           C  
ANISOU 4573  CG  MET B 210     9307   6083   5064   -428   1175  -1026       C  
ATOM   4574  SD  MET B 210      57.353 -22.443  44.583  1.00 61.60           S  
ANISOU 4574  SD  MET B 210     9989   6877   6537   -295   1321  -1111       S  
ATOM   4575  CE  MET B 210      56.939 -20.992  45.559  1.00 58.57           C  
ANISOU 4575  CE  MET B 210     9756   6383   6113   -288   1527  -1477       C  
ATOM   4576  N   GLU B 211      61.828 -24.762  45.257  1.00 53.67           N  
ANISOU 4576  N   GLU B 211     9303   6258   4831   -492    284   -673       N  
ATOM   4577  CA  GLU B 211      62.229 -25.946  44.507  1.00 53.92           C  
ANISOU 4577  CA  GLU B 211     9183   6319   4986   -424    124   -463       C  
ATOM   4578  C   GLU B 211      62.945 -26.947  45.402  1.00 56.82           C  
ANISOU 4578  C   GLU B 211     9737   6777   5075   -443    -78   -323       C  
ATOM   4579  O   GLU B 211      62.771 -28.160  45.244  1.00 63.57           O  
ANISOU 4579  O   GLU B 211    10575   7604   5974   -391   -103   -138       O  
ATOM   4580  CB  GLU B 211      63.108 -25.555  43.324  1.00 50.52           C  
ANISOU 4580  CB  GLU B 211     8496   5897   4802   -393    -71   -475       C  
ATOM   4581  CG  GLU B 211      62.393 -24.724  42.281  1.00 51.24           C  
ANISOU 4581  CG  GLU B 211     8396   5895   5179   -369     87   -531       C  
ATOM   4582  CD  GLU B 211      63.108 -24.754  40.950  1.00 57.48           C  
ANISOU 4582  CD  GLU B 211     8919   6743   6179   -348    -73   -467       C  
ATOM   4583  OE1 GLU B 211      64.342 -24.954  40.959  1.00 51.77           O  
ANISOU 4583  OE1 GLU B 211     8153   6125   5391   -374   -304   -459       O  
ATOM   4584  OE2 GLU B 211      62.436 -24.598  39.903  1.00 53.50           O  
ANISOU 4584  OE2 GLU B 211     8234   6203   5889   -308     29   -429       O  
ATOM   4585  N   ILE B 212      63.761 -26.460  46.341  1.00 53.43           N  
ANISOU 4585  N   ILE B 212     9488   6442   4371   -519   -247   -405       N  
ATOM   4586  CA  ILE B 212      64.370 -27.352  47.324  1.00 59.80           C  
ANISOU 4586  CA  ILE B 212    10505   7347   4869   -539   -461   -246       C  
ATOM   4587  C   ILE B 212      63.289 -28.079  48.117  1.00 65.46           C  
ANISOU 4587  C   ILE B 212    11450   8055   5366   -586   -221   -109       C  
ATOM   4588  O   ILE B 212      63.353 -29.301  48.305  1.00 62.98           O  
ANISOU 4588  O   ILE B 212    11207   7716   5005   -557   -324    144       O  
ATOM   4589  CB  ILE B 212      65.320 -26.568  48.249  1.00 63.13           C  
ANISOU 4589  CB  ILE B 212    11087   7903   4997   -637   -678   -391       C  
ATOM   4590  CG1 ILE B 212      66.528 -26.045  47.465  1.00 63.68           C  
ANISOU 4590  CG1 ILE B 212    10900   7996   5301   -616   -948   -480       C  
ATOM   4591  CG2 ILE B 212      65.771 -27.435  49.425  1.00 63.63           C  
ANISOU 4591  CG2 ILE B 212    11415   8092   4669   -670   -891   -204       C  
ATOM   4592  CD1 ILE B 212      67.465 -25.174  48.293  1.00 70.47           C  
ANISOU 4592  CD1 ILE B 212    11877   8978   5921   -742  -1172   -657       C  
ATOM   4593  N   ASP B 213      62.273 -27.341  48.581  1.00 62.43           N  
ANISOU 4593  N   ASP B 213    11171   7681   4867   -664    112   -275       N  
ATOM   4594  CA  ASP B 213      61.173 -27.958  49.319  1.00 62.21           C  
ANISOU 4594  CA  ASP B 213    11327   7683   4627   -741    400   -164       C  
ATOM   4595  C   ASP B 213      60.416 -28.966  48.457  1.00 59.31           C  
ANISOU 4595  C   ASP B 213    10776   7180   4578   -680    524     28       C  
ATOM   4596  O   ASP B 213      60.048 -30.047  48.934  1.00 60.01           O  
ANISOU 4596  O   ASP B 213    11006   7260   4535   -740    571    267       O  
ATOM   4597  CB  ASP B 213      60.212 -26.885  49.842  1.00 61.48           C  
ANISOU 4597  CB  ASP B 213    11305   7635   4419   -809    764   -445       C  
ATOM   4598  CG  ASP B 213      60.816 -26.040  50.952  1.00 69.64           C  
ANISOU 4598  CG  ASP B 213    12591   8818   5050   -909    679   -657       C  
ATOM   4599  OD1 ASP B 213      61.724 -26.526  51.657  1.00 70.63           O  
ANISOU 4599  OD1 ASP B 213    12914   9071   4850   -969    389   -515       O  
ATOM   4600  OD2 ASP B 213      60.371 -24.885  51.127  1.00 71.09           O  
ANISOU 4600  OD2 ASP B 213    12772   8985   5254   -923    889   -978       O  
ATOM   4601  N   PHE B 214      60.166 -28.630  47.189  1.00 55.11           N  
ANISOU 4601  N   PHE B 214     9939   6540   4460   -579    570    -67       N  
ATOM   4602  CA  PHE B 214      59.437 -29.549  46.318  1.00 57.72           C  
ANISOU 4602  CA  PHE B 214    10081   6758   5092   -533    671     71       C  
ATOM   4603  C   PHE B 214      60.175 -30.873  46.162  1.00 57.11           C  
ANISOU 4603  C   PHE B 214    10027   6617   5056   -490    393    312       C  
ATOM   4604  O   PHE B 214      59.556 -31.944  46.158  1.00 56.53           O  
ANISOU 4604  O   PHE B 214     9978   6448   5054   -524    481    490       O  
ATOM   4605  CB  PHE B 214      59.208 -28.916  44.946  1.00 53.81           C  
ANISOU 4605  CB  PHE B 214     9262   6200   4985   -435    702    -68       C  
ATOM   4606  CG  PHE B 214      58.582 -29.857  43.946  1.00 55.23           C  
ANISOU 4606  CG  PHE B 214     9228   6291   5467   -391    751     39       C  
ATOM   4607  CD1 PHE B 214      57.202 -29.992  43.870  1.00 54.72           C  
ANISOU 4607  CD1 PHE B 214     9081   6194   5517   -435   1055     30       C  
ATOM   4608  CD2 PHE B 214      59.373 -30.612  43.086  1.00 51.61           C  
ANISOU 4608  CD2 PHE B 214     8632   5792   5184   -309    495    118       C  
ATOM   4609  CE1 PHE B 214      56.621 -30.853  42.951  1.00 54.76           C  
ANISOU 4609  CE1 PHE B 214     8882   6124   5800   -417   1080    104       C  
ATOM   4610  CE2 PHE B 214      58.798 -31.479  42.171  1.00 46.69           C  
ANISOU 4610  CE2 PHE B 214     7822   5088   4829   -280    535    169       C  
ATOM   4611  CZ  PHE B 214      57.419 -31.598  42.101  1.00 48.04           C  
ANISOU 4611  CZ  PHE B 214     7925   5222   5106   -344    816    166       C  
ATOM   4612  N   LEU B 215      61.496 -30.821  46.006  1.00 57.77           N  
ANISOU 4612  N   LEU B 215    10082   6734   5134   -413     54    309       N  
ATOM   4613  CA  LEU B 215      62.245 -32.060  45.857  1.00 62.51           C  
ANISOU 4613  CA  LEU B 215    10678   7253   5821   -331   -228    508       C  
ATOM   4614  C   LEU B 215      62.310 -32.828  47.166  1.00 67.51           C  
ANISOU 4614  C   LEU B 215    11646   7885   6119   -412   -307    754       C  
ATOM   4615  O   LEU B 215      62.332 -34.063  47.156  1.00 77.14           O  
ANISOU 4615  O   LEU B 215    12913   8954   7442   -377   -419    984       O  
ATOM   4616  CB  LEU B 215      63.648 -31.760  45.336  1.00 63.67           C  
ANISOU 4616  CB  LEU B 215    10655   7467   6072   -219   -557    416       C  
ATOM   4617  CG  LEU B 215      63.680 -31.228  43.903  1.00 63.30           C  
ANISOU 4617  CG  LEU B 215    10268   7428   6355   -152   -505    237       C  
ATOM   4618  CD1 LEU B 215      65.094 -30.839  43.503  1.00 58.12           C  
ANISOU 4618  CD1 LEU B 215     9442   6883   5757    -87   -793    143       C  
ATOM   4619  CD2 LEU B 215      63.105 -32.260  42.944  1.00 54.09           C  
ANISOU 4619  CD2 LEU B 215     8932   6132   5488    -80   -434    295       C  
ATOM   4620  N   GLU B 216      62.302 -32.121  48.295  1.00 62.50           N  
ANISOU 4620  N   GLU B 216    11259   7409   5080   -530   -248    712       N  
ATOM   4621  CA  GLU B 216      62.522 -32.737  49.599  1.00 75.77           C  
ANISOU 4621  CA  GLU B 216    13285   9152   6352   -625   -370    957       C  
ATOM   4622  C   GLU B 216      61.232 -33.205  50.269  1.00 79.04           C  
ANISOU 4622  C   GLU B 216    13902   9557   6572   -795    -14   1112       C  
ATOM   4623  O   GLU B 216      61.200 -34.296  50.850  1.00 77.42           O  
ANISOU 4623  O   GLU B 216    13905   9277   6232   -857   -104   1441       O  
ATOM   4624  CB  GLU B 216      63.255 -31.752  50.517  1.00 83.30           C  
ANISOU 4624  CB  GLU B 216    14412  10330   6909   -690   -512    811       C  
ATOM   4625  CG  GLU B 216      63.709 -32.349  51.835  1.00 99.94           C  
ANISOU 4625  CG  GLU B 216    16873  12551   8548   -779   -733   1074       C  
ATOM   4626  CD  GLU B 216      64.559 -33.590  51.644  1.00111.89           C  
ANISOU 4626  CD  GLU B 216    18362  13913  10237   -640  -1135   1386       C  
ATOM   4627  OE1 GLU B 216      64.202 -34.650  52.202  1.00116.76           O  
ANISOU 4627  OE1 GLU B 216    19204  14436  10726   -699  -1149   1730       O  
ATOM   4628  OE2 GLU B 216      65.579 -33.507  50.925  1.00113.63           O  
ANISOU 4628  OE2 GLU B 216    18329  14099  10745   -472  -1431   1287       O  
ATOM   4629  N   LEU B 217      60.168 -32.410  50.210  1.00 73.19           N  
ANISOU 4629  N   LEU B 217    13094   8886   5829   -875    386    892       N  
ATOM   4630  CA  LEU B 217      58.966 -32.728  50.966  1.00 74.25           C  
ANISOU 4630  CA  LEU B 217    13400   9077   5734  -1060    760    999       C  
ATOM   4631  C   LEU B 217      58.075 -33.709  50.205  1.00 74.84           C  
ANISOU 4631  C   LEU B 217    13301   8947   6187  -1073    924   1156       C  
ATOM   4632  O   LEU B 217      58.236 -33.945  49.002  1.00 71.87           O  
ANISOU 4632  O   LEU B 217    12647   8405   6256   -928    802   1102       O  
ATOM   4633  CB  LEU B 217      58.175 -31.460  51.278  1.00 76.04           C  
ANISOU 4633  CB  LEU B 217    13598   9470   5823  -1124   1134    659       C  
ATOM   4634  CG  LEU B 217      58.917 -30.314  51.962  1.00 71.54           C  
ANISOU 4634  CG  LEU B 217    13177   9081   4925  -1128   1019    409       C  
ATOM   4635  CD1 LEU B 217      57.987 -29.125  52.123  1.00 72.80           C  
ANISOU 4635  CD1 LEU B 217    13265   9328   5067  -1159   1420     42       C  
ATOM   4636  CD2 LEU B 217      59.462 -30.768  53.305  1.00 77.26           C  
ANISOU 4636  CD2 LEU B 217    14290   9988   5078  -1270    855    618       C  
ATOM   4637  N   ALA B 218      57.109 -34.275  50.928  1.00 74.58           N  
ANISOU 4637  N   ALA B 218    13432   8950   5957  -1272   1217   1338       N  
ATOM   4638  CA  ALA B 218      56.071 -35.074  50.299  1.00 72.47           C  
ANISOU 4638  CA  ALA B 218    12986   8512   6037  -1338   1440   1442       C  
ATOM   4639  C   ALA B 218      55.033 -34.167  49.643  1.00 80.64           C  
ANISOU 4639  C   ALA B 218    13705   9615   7319  -1310   1793   1109       C  
ATOM   4640  O   ALA B 218      54.957 -32.964  49.915  1.00 85.85           O  
ANISOU 4640  O   ALA B 218    14346  10447   7825  -1274   1933    830       O  
ATOM   4641  CB  ALA B 218      55.399 -35.996  51.315  1.00 75.39           C  
ANISOU 4641  CB  ALA B 218    13628   8900   6117  -1600   1641   1777       C  
ATOM   4642  N   MET B 219      54.222 -34.770  48.767  1.00 80.57           N  
ANISOU 4642  N   MET B 219    13442   9452   7717  -1324   1916   1138       N  
ATOM   4643  CA  MET B 219      53.291 -33.998  47.947  1.00 74.05           C  
ANISOU 4643  CA  MET B 219    12266   8668   7203  -1259   2168    850       C  
ATOM   4644  C   MET B 219      52.326 -33.189  48.810  1.00 71.99           C  
ANISOU 4644  C   MET B 219    12030   8628   6695  -1375   2598    682       C  
ATOM   4645  O   MET B 219      52.166 -31.979  48.612  1.00 71.45           O  
ANISOU 4645  O   MET B 219    11816   8648   6683  -1252   2698    377       O  
ATOM   4646  CB  MET B 219      52.527 -34.936  47.008  1.00 70.00           C  
ANISOU 4646  CB  MET B 219    11500   7979   7116  -1301   2219    934       C  
ATOM   4647  CG  MET B 219      51.630 -34.228  45.998  1.00 71.54           C  
ANISOU 4647  CG  MET B 219    11298   8212   7671  -1212   2393    665       C  
ATOM   4648  SD  MET B 219      50.808 -35.329  44.819  1.00 70.78           S  
ANISOU 4648  SD  MET B 219    10890   7937   8066  -1271   2392    725       S  
ATOM   4649  CE  MET B 219      49.548 -36.070  45.859  1.00 73.25           C  
ANISOU 4649  CE  MET B 219    11285   8293   8255  -1593   2810    908       C  
ATOM   4650  N   ASP B 220      51.675 -33.843  49.777  1.00 68.69           N  
ANISOU 4650  N   ASP B 220    11794   8298   6008  -1615   2863    874       N  
ATOM   4651  CA  ASP B 220      50.686 -33.155  50.603  1.00 84.21           C  
ANISOU 4651  CA  ASP B 220    13751  10510   7734  -1738   3325    687       C  
ATOM   4652  C   ASP B 220      51.311 -32.055  51.449  1.00 80.80           C  
ANISOU 4652  C   ASP B 220    13544  10270   6884  -1680   3314    466       C  
ATOM   4653  O   ASP B 220      50.674 -31.023  51.685  1.00 82.85           O  
ANISOU 4653  O   ASP B 220    13682  10678   7119  -1641   3620    132       O  
ATOM   4654  CB  ASP B 220      49.965 -34.157  51.501  1.00 95.77           C  
ANISOU 4654  CB  ASP B 220    15389  12058   8940  -2050   3610    979       C  
ATOM   4655  CG  ASP B 220      49.139 -35.153  50.714  1.00112.07           C  
ANISOU 4655  CG  ASP B 220    17195  13935  11450  -2150   3690   1139       C  
ATOM   4656  OD1 ASP B 220      48.602 -34.773  49.651  1.00114.82           O  
ANISOU 4656  OD1 ASP B 220    17154  14215  12256  -2006   3726    911       O  
ATOM   4657  OD2 ASP B 220      49.028 -36.317  51.158  1.00120.88           O  
ANISOU 4657  OD2 ASP B 220    18504  14963  12461  -2382   3700   1502       O  
ATOM   4658  N   GLU B 221      52.544 -32.258  51.920  1.00 81.58           N  
ANISOU 4658  N   GLU B 221    13958  10364   6673  -1670   2955    628       N  
ATOM   4659  CA  GLU B 221      53.196 -31.249  52.748  1.00 87.97           C  
ANISOU 4659  CA  GLU B 221    14992  11364   7070  -1643   2906    407       C  
ATOM   4660  C   GLU B 221      53.609 -30.039  51.925  1.00 77.27           C  
ANISOU 4660  C   GLU B 221    13412   9919   6030  -1401   2762     56       C  
ATOM   4661  O   GLU B 221      53.413 -28.894  52.353  1.00 79.48           O  
ANISOU 4661  O   GLU B 221    13700  10320   6179  -1369   2948   -288       O  
ATOM   4662  CB  GLU B 221      54.410 -31.847  53.450  1.00 93.96           C  
ANISOU 4662  CB  GLU B 221    16120  12151   7430  -1703   2517    697       C  
ATOM   4663  CG  GLU B 221      54.072 -32.828  54.544  1.00109.18           C  
ANISOU 4663  CG  GLU B 221    18279  14208   8998  -1934   2610   1036       C  
ATOM   4664  CD  GLU B 221      55.073 -33.957  54.619  1.00117.60           C  
ANISOU 4664  CD  GLU B 221    19564  15116  10004  -1937   2158   1469       C  
ATOM   4665  OE1 GLU B 221      54.673 -35.078  55.001  1.00124.98           O  
ANISOU 4665  OE1 GLU B 221    20562  15995  10928  -2083   2188   1823       O  
ATOM   4666  OE2 GLU B 221      56.255 -33.725  54.277  1.00113.86           O  
ANISOU 4666  OE2 GLU B 221    19172  14558   9530  -1785   1762   1450       O  
ATOM   4667  N   PHE B 222      54.195 -30.267  50.748  1.00 63.98           N  
ANISOU 4667  N   PHE B 222    11532   8019   4758  -1240   2436    132       N  
ATOM   4668  CA  PHE B 222      54.580 -29.141  49.905  1.00 67.44           C  
ANISOU 4668  CA  PHE B 222    11758   8372   5494  -1043   2301   -148       C  
ATOM   4669  C   PHE B 222      53.366 -28.299  49.538  1.00 69.49           C  
ANISOU 4669  C   PHE B 222    11744   8629   6031   -980   2664   -426       C  
ATOM   4670  O   PHE B 222      53.392 -27.067  49.641  1.00 69.96           O  
ANISOU 4670  O   PHE B 222    11774   8700   6109   -891   2727   -733       O  
ATOM   4671  CB  PHE B 222      55.292 -29.627  48.644  1.00 58.46           C  
ANISOU 4671  CB  PHE B 222    10430   7047   4734   -908   1944     -6       C  
ATOM   4672  CG  PHE B 222      55.659 -28.512  47.708  1.00 57.93           C  
ANISOU 4672  CG  PHE B 222    10142   6904   4963   -742   1816   -239       C  
ATOM   4673  CD1 PHE B 222      56.848 -27.818  47.871  1.00 66.38           C  
ANISOU 4673  CD1 PHE B 222    11327   7996   5900   -700   1543   -336       C  
ATOM   4674  CD2 PHE B 222      54.804 -28.137  46.683  1.00 55.60           C  
ANISOU 4674  CD2 PHE B 222     9525   6523   5077   -648   1961   -346       C  
ATOM   4675  CE1 PHE B 222      57.189 -26.778  47.017  1.00 64.41           C  
ANISOU 4675  CE1 PHE B 222    10886   7661   5926   -585   1435   -517       C  
ATOM   4676  CE2 PHE B 222      55.134 -27.096  45.830  1.00 59.00           C  
ANISOU 4676  CE2 PHE B 222     9779   6876   5763   -513   1833   -508       C  
ATOM   4677  CZ  PHE B 222      56.329 -26.415  45.999  1.00 63.03           C  
ANISOU 4677  CZ  PHE B 222    10420   7388   6142   -492   1581   -586       C  
ATOM   4678  N   ILE B 223      52.285 -28.954  49.109  1.00 65.40           N  
ANISOU 4678  N   ILE B 223    11009   8080   5758  -1023   2893   -329       N  
ATOM   4679  CA  ILE B 223      51.083 -28.228  48.714  1.00 67.77           C  
ANISOU 4679  CA  ILE B 223    10997   8385   6369   -943   3214   -577       C  
ATOM   4680  C   ILE B 223      50.488 -27.486  49.901  1.00 76.36           C  
ANISOU 4680  C   ILE B 223    12202   9662   7148  -1012   3596   -842       C  
ATOM   4681  O   ILE B 223      49.957 -26.377  49.750  1.00 77.95           O  
ANISOU 4681  O   ILE B 223    12217   9841   7558   -871   3768  -1165       O  
ATOM   4682  CB  ILE B 223      50.077 -29.200  48.069  1.00 67.04           C  
ANISOU 4682  CB  ILE B 223    10640   8248   6585  -1009   3357   -409       C  
ATOM   4683  CG1 ILE B 223      50.571 -29.592  46.672  1.00 64.65           C  
ANISOU 4683  CG1 ILE B 223    10146   7760   6658   -886   2997   -283       C  
ATOM   4684  CG2 ILE B 223      48.688 -28.594  48.005  1.00 62.95           C  
ANISOU 4684  CG2 ILE B 223     9810   7803   6306   -972   3753   -650       C  
ATOM   4685  CD1 ILE B 223      49.746 -30.667  46.005  1.00 64.31           C  
ANISOU 4685  CD1 ILE B 223     9874   7657   6904   -971   3065   -123       C  
ATOM   4686  N   GLU B 224      50.588 -28.064  51.100  1.00 83.74           N  
ANISOU 4686  N   GLU B 224    13455  10785   7578  -1223   3725   -717       N  
ATOM   4687  CA  GLU B 224      50.122 -27.370  52.296  1.00 87.91           C  
ANISOU 4687  CA  GLU B 224    14130  11548   7726  -1308   4092   -999       C  
ATOM   4688  C   GLU B 224      50.983 -26.148  52.595  1.00 90.27           C  
ANISOU 4688  C   GLU B 224    14586  11829   7882  -1187   3917  -1309       C  
ATOM   4689  O   GLU B 224      50.462 -25.044  52.798  1.00 91.72           O  
ANISOU 4689  O   GLU B 224    14614  12025   8208  -1069   4100  -1683       O  
ATOM   4690  CB  GLU B 224      50.112 -28.328  53.488  1.00 91.09           C  
ANISOU 4690  CB  GLU B 224    14788  12170   7653  -1556   4134   -722       C  
ATOM   4691  CG  GLU B 224      49.844 -27.646  54.820  1.00 99.14           C  
ANISOU 4691  CG  GLU B 224    15896  13463   8308  -1606   4312   -970       C  
ATOM   4692  CD  GLU B 224      49.697 -28.632  55.965  1.00111.73           C  
ANISOU 4692  CD  GLU B 224    17700  15299   9456  -1850   4373   -664       C  
ATOM   4693  OE1 GLU B 224      49.727 -29.855  55.707  1.00113.49           O  
ANISOU 4693  OE1 GLU B 224    17982  15435   9705  -1981   4281   -252       O  
ATOM   4694  OE2 GLU B 224      49.549 -28.183  57.123  1.00119.15           O  
ANISOU 4694  OE2 GLU B 224    18745  16504  10024  -1911   4510   -832       O  
ATOM   4695  N   ARG B 225      52.308 -26.324  52.613  1.00 88.49           N  
ANISOU 4695  N   ARG B 225    14598  11551   7472  -1192   3482  -1146       N  
ATOM   4696  CA  ARG B 225      53.200 -25.232  52.995  1.00 88.71           C  
ANISOU 4696  CA  ARG B 225    14798  11580   7330  -1131   3295  -1429       C  
ATOM   4697  C   ARG B 225      53.052 -24.034  52.068  1.00 82.25           C  
ANISOU 4697  C   ARG B 225    13695  10527   7030   -907   3269  -1727       C  
ATOM   4698  O   ARG B 225      53.045 -22.885  52.525  1.00 83.03           O  
ANISOU 4698  O   ARG B 225    13850  10619   7078   -857   3376  -2112       O  
ATOM   4699  CB  ARG B 225      54.650 -25.713  53.006  1.00 87.79           C  
ANISOU 4699  CB  ARG B 225    14902  11440   7013  -1166   2798  -1172       C  
ATOM   4700  CG  ARG B 225      55.662 -24.588  53.147  1.00 84.93           C  
ANISOU 4700  CG  ARG B 225    14644  11038   6587  -1105   2540  -1450       C  
ATOM   4701  CD  ARG B 225      57.073 -25.124  53.257  1.00 84.24           C  
ANISOU 4701  CD  ARG B 225    14744  10979   6284  -1151   2058  -1200       C  
ATOM   4702  NE  ARG B 225      57.197 -26.085  54.350  1.00 89.25           N  
ANISOU 4702  NE  ARG B 225    15694  11847   6370  -1332   2049   -945       N  
ATOM   4703  CZ  ARG B 225      58.345 -26.628  54.739  1.00 89.52           C  
ANISOU 4703  CZ  ARG B 225    15918  11952   6142  -1379   1635   -709       C  
ATOM   4704  NH1 ARG B 225      59.477 -26.301  54.128  1.00 89.94           N  
ANISOU 4704  NH1 ARG B 225    15890  11887   6395  -1277   1237   -736       N  
ATOM   4705  NH2 ARG B 225      58.362 -27.495  55.742  1.00 96.47           N  
ANISOU 4705  NH2 ARG B 225    16972  13020   6662  -1502   1588   -429       N  
ATOM   4706  N   TYR B 226      52.938 -24.274  50.764  1.00 73.13           N  
ANISOU 4706  N   TYR B 226    12245   9169   6372   -778   3117  -1556       N  
ATOM   4707  CA  TYR B 226      52.865 -23.186  49.801  1.00 72.80           C  
ANISOU 4707  CA  TYR B 226    11950   8897   6815   -577   3038  -1756       C  
ATOM   4708  C   TYR B 226      51.439 -22.872  49.371  1.00 73.32           C  
ANISOU 4708  C   TYR B 226    11683   8907   7266   -459   3381  -1901       C  
ATOM   4709  O   TYR B 226      51.243 -22.132  48.402  1.00 69.64           O  
ANISOU 4709  O   TYR B 226    10968   8233   7260   -280   3290  -1979       O  
ATOM   4710  CB  TYR B 226      53.758 -23.496  48.597  1.00 65.67           C  
ANISOU 4710  CB  TYR B 226    10933   7837   6179   -510   2620  -1497       C  
ATOM   4711  CG  TYR B 226      55.221 -23.401  48.967  1.00 67.02           C  
ANISOU 4711  CG  TYR B 226    11363   8037   6066   -580   2269  -1459       C  
ATOM   4712  CD1 TYR B 226      55.946 -24.534  49.301  1.00 65.45           C  
ANISOU 4712  CD1 TYR B 226    11341   7956   5570   -689   2065  -1176       C  
ATOM   4713  CD2 TYR B 226      55.861 -22.169  49.036  1.00 64.24           C  
ANISOU 4713  CD2 TYR B 226    11071   7582   5758   -540   2136  -1714       C  
ATOM   4714  CE1 TYR B 226      57.274 -24.452  49.664  1.00 69.31           C  
ANISOU 4714  CE1 TYR B 226    12028   8492   5816   -740   1726  -1147       C  
ATOM   4715  CE2 TYR B 226      57.192 -22.076  49.397  1.00 68.81           C  
ANISOU 4715  CE2 TYR B 226    11852   8208   6085   -624   1810  -1695       C  
ATOM   4716  CZ  TYR B 226      57.894 -23.222  49.709  1.00 69.31           C  
ANISOU 4716  CZ  TYR B 226    12059   8424   5854   -716   1602  -1414       C  
ATOM   4717  OH  TYR B 226      59.221 -23.144  50.069  1.00 73.67           O  
ANISOU 4717  OH  TYR B 226    12774   9042   6178   -785   1254  -1396       O  
ATOM   4718  N   LYS B 227      50.444 -23.401  50.085  1.00 75.88           N  
ANISOU 4718  N   LYS B 227    11993   9426   7413   -562   3768  -1928       N  
ATOM   4719  CA  LYS B 227      49.049 -22.987  49.942  1.00 75.70           C  
ANISOU 4719  CA  LYS B 227    11644   9405   7715   -456   4150  -2148       C  
ATOM   4720  C   LYS B 227      48.570 -23.135  48.496  1.00 69.83           C  
ANISOU 4720  C   LYS B 227    10513   8480   7540   -304   4006  -1984       C  
ATOM   4721  O   LYS B 227      48.088 -22.190  47.869  1.00 70.80           O  
ANISOU 4721  O   LYS B 227    10376   8434   8089    -94   4017  -2172       O  
ATOM   4722  CB  LYS B 227      48.862 -21.551  50.449  1.00 76.08           C  
ANISOU 4722  CB  LYS B 227    11693   9385   7828   -314   4303  -2608       C  
ATOM   4723  CG  LYS B 227      49.148 -21.356  51.947  1.00 85.82           C  
ANISOU 4723  CG  LYS B 227    13210  10858   8540   -455   4366  -2762       C  
ATOM   4724  CD  LYS B 227      50.595 -20.939  52.203  1.00 92.22           C  
ANISOU 4724  CD  LYS B 227    14368  11599   9074   -503   4022  -2798       C  
ATOM   4725  CE  LYS B 227      50.859 -20.611  53.677  1.00 99.54           C  
ANISOU 4725  CE  LYS B 227    15539  12771   9511   -621   4060  -2992       C  
ATOM   4726  NZ  LYS B 227      51.012 -21.815  54.548  1.00 99.73           N  
ANISOU 4726  NZ  LYS B 227    15787  13108   8997   -859   4087  -2696       N  
ATOM   4727  N   LEU B 228      48.702 -24.358  47.976  1.00 62.65           N  
ANISOU 4727  N   LEU B 228     9574   7601   6629   -415   3854  -1628       N  
ATOM   4728  CA  LEU B 228      48.416 -24.647  46.576  1.00 64.68           C  
ANISOU 4728  CA  LEU B 228     9507   7723   7345   -309   3660  -1456       C  
ATOM   4729  C   LEU B 228      47.149 -25.476  46.386  1.00 67.10           C  
ANISOU 4729  C   LEU B 228     9526   8132   7835   -385   3927  -1374       C  
ATOM   4730  O   LEU B 228      46.950 -26.054  45.311  1.00 62.09           O  
ANISOU 4730  O   LEU B 228     8665   7431   7495   -363   3750  -1192       O  
ATOM   4731  CB  LEU B 228      49.609 -25.352  45.934  1.00 60.65           C  
ANISOU 4731  CB  LEU B 228     9140   7142   6764   -356   3240  -1166       C  
ATOM   4732  CG  LEU B 228      50.767 -24.429  45.558  1.00 63.68           C  
ANISOU 4732  CG  LEU B 228     9637   7390   7170   -245   2914  -1228       C  
ATOM   4733  CD1 LEU B 228      51.988 -25.241  45.154  1.00 55.02           C  
ANISOU 4733  CD1 LEU B 228     8685   6284   5936   -314   2553   -970       C  
ATOM   4734  CD2 LEU B 228      50.334 -23.515  44.428  1.00 62.99           C  
ANISOU 4734  CD2 LEU B 228     9239   7140   7553    -48   2834  -1310       C  
ATOM   4735  N   GLU B 229      46.295 -25.549  47.403  1.00 64.61           N  
ANISOU 4735  N   GLU B 229     9208   7998   7343   -493   4354  -1519       N  
ATOM   4736  CA  GLU B 229      45.024 -26.255  47.271  1.00 77.63           C  
ANISOU 4736  CA  GLU B 229    10542   9761   9193   -589   4645  -1469       C  
ATOM   4737  C   GLU B 229      44.157 -25.616  46.193  1.00 74.29           C  
ANISOU 4737  C   GLU B 229     9647   9235   9346   -357   4622  -1604       C  
ATOM   4738  O   GLU B 229      44.015 -24.393  46.128  1.00 75.42           O  
ANISOU 4738  O   GLU B 229     9684   9286   9687   -129   4645  -1870       O  
ATOM   4739  CB  GLU B 229      44.264 -26.254  48.602  1.00 80.81           C  
ANISOU 4739  CB  GLU B 229    10999  10412   9291   -742   5136  -1642       C  
ATOM   4740  CG  GLU B 229      44.909 -27.065  49.712  1.00 94.34           C  
ANISOU 4740  CG  GLU B 229    13152  12275  10417  -1012   5145  -1431       C  
ATOM   4741  CD  GLU B 229      45.976 -26.294  50.469  1.00106.07           C  
ANISOU 4741  CD  GLU B 229    15020  13770  11513   -963   5004  -1578       C  
ATOM   4742  OE1 GLU B 229      46.327 -25.172  50.042  1.00106.04           O  
ANISOU 4742  OE1 GLU B 229    14967  13610  11712   -734   4884  -1830       O  
ATOM   4743  OE2 GLU B 229      46.459 -26.812  51.499  1.00111.50           O  
ANISOU 4743  OE2 GLU B 229    16050  14615  11701  -1160   4988  -1431       O  
ATOM   4744  N   GLY B 230      43.558 -26.454  45.351  1.00 73.86           N  
ANISOU 4744  N   GLY B 230     9308   9184   9570   -418   4560  -1420       N  
ATOM   4745  CA  GLY B 230      42.717 -25.978  44.277  1.00 71.03           C  
ANISOU 4745  CA  GLY B 230     8489   8762   9738   -217   4490  -1504       C  
ATOM   4746  C   GLY B 230      43.441 -25.630  42.994  1.00 63.66           C  
ANISOU 4746  C   GLY B 230     7527   7640   9021    -45   4012  -1379       C  
ATOM   4747  O   GLY B 230      42.785 -25.230  42.023  1.00 63.92           O  
ANISOU 4747  O   GLY B 230     7193   7627   9469    121   3897  -1406       O  
ATOM   4748  N   TYR B 231      44.767 -25.765  42.949  1.00 57.98           N  
ANISOU 4748  N   TYR B 231     7167   6834   8029    -86   3726  -1237       N  
ATOM   4749  CA  TYR B 231      45.529 -25.484  41.739  1.00 56.63           C  
ANISOU 4749  CA  TYR B 231     6974   6527   8015     38   3300  -1110       C  
ATOM   4750  C   TYR B 231      46.017 -26.746  41.043  1.00 59.02           C  
ANISOU 4750  C   TYR B 231     7316   6851   8256   -107   3060   -861       C  
ATOM   4751  O   TYR B 231      46.818 -26.653  40.107  1.00 59.44           O  
ANISOU 4751  O   TYR B 231     7395   6837   8354    -41   2721   -757       O  
ATOM   4752  CB  TYR B 231      46.697 -24.550  42.059  1.00 56.55           C  
ANISOU 4752  CB  TYR B 231     7274   6399   7814    121   3137  -1175       C  
ATOM   4753  CG  TYR B 231      46.216 -23.177  42.456  1.00 61.93           C  
ANISOU 4753  CG  TYR B 231     7874   6986   8669    308   3303  -1448       C  
ATOM   4754  CD1 TYR B 231      45.799 -22.265  41.495  1.00 59.94           C  
ANISOU 4754  CD1 TYR B 231     7346   6590   8840    529   3152  -1479       C  
ATOM   4755  CD2 TYR B 231      46.140 -22.803  43.794  1.00 65.24           C  
ANISOU 4755  CD2 TYR B 231     8491   7460   8836    268   3612  -1684       C  
ATOM   4756  CE1 TYR B 231      45.332 -21.000  41.859  1.00 59.15           C  
ANISOU 4756  CE1 TYR B 231     7164   6347   8965    728   3293  -1741       C  
ATOM   4757  CE2 TYR B 231      45.676 -21.548  44.164  1.00 71.01           C  
ANISOU 4757  CE2 TYR B 231     9137   8082   9760    456   3778  -1992       C  
ATOM   4758  CZ  TYR B 231      45.276 -20.652  43.192  1.00 68.01           C  
ANISOU 4758  CZ  TYR B 231     8476   7506   9860    697   3614  -2021       C  
ATOM   4759  OH  TYR B 231      44.819 -19.406  43.556  1.00 78.02           O  
ANISOU 4759  OH  TYR B 231     9658   8609  11376    908   3761  -2333       O  
ATOM   4760  N   ALA B 232      45.560 -27.923  41.483  1.00 63.68           N  
ANISOU 4760  N   ALA B 232     7914   7528   8753   -313   3239   -773       N  
ATOM   4761  CA  ALA B 232      45.723 -29.178  40.741  1.00 59.50           C  
ANISOU 4761  CA  ALA B 232     7344   6984   8281   -443   3044   -583       C  
ATOM   4762  C   ALA B 232      47.190 -29.554  40.536  1.00 56.95           C  
ANISOU 4762  C   ALA B 232     7328   6576   7733   -451   2723   -446       C  
ATOM   4763  O   ALA B 232      47.561 -30.115  39.501  1.00 51.68           O  
ANISOU 4763  O   ALA B 232     6577   5874   7185   -444   2457   -363       O  
ATOM   4764  CB  ALA B 232      44.991 -29.117  39.397  1.00 57.41           C  
ANISOU 4764  CB  ALA B 232     6669   6737   8408   -351   2892   -602       C  
ATOM   4765  N   PHE B 233      48.042 -29.269  41.523  1.00 56.13           N  
ANISOU 4765  N   PHE B 233     7569   6459   7299   -468   2744   -444       N  
ATOM   4766  CA  PHE B 233      49.454 -29.612  41.388  1.00 53.72           C  
ANISOU 4766  CA  PHE B 233     7520   6090   6800   -465   2435   -325       C  
ATOM   4767  C   PHE B 233      49.674 -31.122  41.377  1.00 54.96           C  
ANISOU 4767  C   PHE B 233     7772   6197   6912   -617   2353   -138       C  
ATOM   4768  O   PHE B 233      50.597 -31.611  40.712  1.00 56.59           O  
ANISOU 4768  O   PHE B 233     8024   6340   7138   -577   2058    -64       O  
ATOM   4769  CB  PHE B 233      50.257 -28.956  42.511  1.00 60.04           C  
ANISOU 4769  CB  PHE B 233     8647   6906   7258   -461   2463   -378       C  
ATOM   4770  CG  PHE B 233      51.003 -27.726  42.082  1.00 54.89           C  
ANISOU 4770  CG  PHE B 233     7999   6210   6647   -303   2270   -491       C  
ATOM   4771  CD1 PHE B 233      50.367 -26.727  41.369  1.00 62.65           C  
ANISOU 4771  CD1 PHE B 233     8722   7157   7926   -162   2298   -614       C  
ATOM   4772  CD2 PHE B 233      52.346 -27.572  42.393  1.00 51.71           C  
ANISOU 4772  CD2 PHE B 233     7852   5791   6005   -305   2044   -457       C  
ATOM   4773  CE1 PHE B 233      51.058 -25.591  40.971  1.00 64.99           C  
ANISOU 4773  CE1 PHE B 233     9040   7375   8277    -45   2115   -681       C  
ATOM   4774  CE2 PHE B 233      53.041 -26.444  41.997  1.00 50.98           C  
ANISOU 4774  CE2 PHE B 233     7755   5649   5967   -201   1873   -551       C  
ATOM   4775  CZ  PHE B 233      52.393 -25.447  41.293  1.00 56.05           C  
ANISOU 4775  CZ  PHE B 233     8165   6228   6902    -80   1916   -654       C  
ATOM   4776  N   GLU B 234      48.842 -31.872  42.101  1.00 55.78           N  
ANISOU 4776  N   GLU B 234     7900   6319   6974   -795   2616    -65       N  
ATOM   4777  CA  GLU B 234      48.901 -33.330  42.040  1.00 58.31           C  
ANISOU 4777  CA  GLU B 234     8294   6533   7328   -954   2542    125       C  
ATOM   4778  C   GLU B 234      48.904 -33.812  40.594  1.00 63.50           C  
ANISOU 4778  C   GLU B 234     8693   7120   8313   -892   2300     94       C  
ATOM   4779  O   GLU B 234      49.661 -34.720  40.230  1.00 65.32           O  
ANISOU 4779  O   GLU B 234     9029   7226   8564   -904   2062    187       O  
ATOM   4780  CB  GLU B 234      47.718 -33.938  42.800  1.00 62.93           C  
ANISOU 4780  CB  GLU B 234     8842   7158   7910  -1182   2901    196       C  
ATOM   4781  CG  GLU B 234      47.499 -33.379  44.208  1.00 82.51           C  
ANISOU 4781  CG  GLU B 234    11530   9779  10039  -1262   3215    177       C  
ATOM   4782  CD  GLU B 234      46.691 -32.083  44.224  1.00 94.66           C  
ANISOU 4782  CD  GLU B 234    12821  11468  11679  -1136   3461    -95       C  
ATOM   4783  OE1 GLU B 234      46.416 -31.528  43.137  1.00 98.50           O  
ANISOU 4783  OE1 GLU B 234    12999  11931  12496   -965   3336   -228       O  
ATOM   4784  OE2 GLU B 234      46.327 -31.621  45.327  1.00101.02           O  
ANISOU 4784  OE2 GLU B 234    13740  12412  12230  -1204   3774   -178       O  
ATOM   4785  N   HIS B 235      48.081 -33.187  39.751  1.00 57.85           N  
ANISOU 4785  N   HIS B 235     7635   6491   7853   -812   2343    -51       N  
ATOM   4786  CA  HIS B 235      48.008 -33.543  38.340  1.00 58.32           C  
ANISOU 4786  CA  HIS B 235     7438   6542   8178   -763   2112   -102       C  
ATOM   4787  C   HIS B 235      49.125 -32.872  37.545  1.00 50.65           C  
ANISOU 4787  C   HIS B 235     6498   5599   7146   -578   1816   -147       C  
ATOM   4788  O   HIS B 235      49.949 -33.552  36.925  1.00 48.27           O  
ANISOU 4788  O   HIS B 235     6246   5249   6845   -566   1579   -127       O  
ATOM   4789  CB  HIS B 235      46.629 -33.159  37.795  1.00 56.81           C  
ANISOU 4789  CB  HIS B 235     6858   6459   8267   -764   2255   -212       C  
ATOM   4790  CG  HIS B 235      46.423 -33.485  36.348  1.00 57.02           C  
ANISOU 4790  CG  HIS B 235     6606   6524   8534   -734   2014   -275       C  
ATOM   4791  ND1 HIS B 235      45.978 -34.719  35.916  1.00 55.34           N  
ANISOU 4791  ND1 HIS B 235     6280   6254   8492   -901   1978   -274       N  
ATOM   4792  CD2 HIS B 235      46.567 -32.726  35.235  1.00 51.89           C  
ANISOU 4792  CD2 HIS B 235     5773   5977   7966   -574   1797   -342       C  
ATOM   4793  CE1 HIS B 235      45.875 -34.708  34.598  1.00 57.75           C  
ANISOU 4793  CE1 HIS B 235     6342   6647   8952   -840   1746   -371       C  
ATOM   4794  NE2 HIS B 235      46.227 -33.511  34.160  1.00 53.86           N  
ANISOU 4794  NE2 HIS B 235     5807   6267   8390   -644   1633   -394       N  
ATOM   4795  N   ILE B 236      49.198 -31.537  37.601  1.00 44.04           N  
ANISOU 4795  N   ILE B 236     5636   4833   6263   -442   1840   -214       N  
ATOM   4796  CA  ILE B 236      50.022 -30.775  36.657  1.00 43.81           C  
ANISOU 4796  CA  ILE B 236     5561   4850   6234   -299   1581   -242       C  
ATOM   4797  C   ILE B 236      51.505 -31.061  36.854  1.00 49.52           C  
ANISOU 4797  C   ILE B 236     6546   5532   6738   -287   1389   -188       C  
ATOM   4798  O   ILE B 236      52.253 -31.244  35.886  1.00 48.19           O  
ANISOU 4798  O   ILE B 236     6314   5409   6588   -241   1157   -197       O  
ATOM   4799  CB  ILE B 236      49.753 -29.267  36.793  1.00 41.12           C  
ANISOU 4799  CB  ILE B 236     5164   4530   5928   -171   1653   -306       C  
ATOM   4800  CG1 ILE B 236      48.298 -28.934  36.462  1.00 45.55           C  
ANISOU 4800  CG1 ILE B 236     5404   5138   6765   -136   1802   -369       C  
ATOM   4801  CG2 ILE B 236      50.731 -28.492  35.909  1.00 37.43           C  
ANISOU 4801  CG2 ILE B 236     4699   4090   5432    -68   1386   -285       C  
ATOM   4802  CD1 ILE B 236      47.888 -27.495  36.878  1.00 49.13           C  
ANISOU 4802  CD1 ILE B 236     5814   5552   7299      9   1929   -459       C  
ATOM   4803  N   VAL B 237      51.968 -31.033  38.095  1.00 49.48           N  
ANISOU 4803  N   VAL B 237     7280   5848   5669   -483   1489   -473       N  
ATOM   4804  CA  VAL B 237      53.393 -31.047  38.386  1.00 51.34           C  
ANISOU 4804  CA  VAL B 237     7649   6114   5746   -516   1284   -456       C  
ATOM   4805  C   VAL B 237      53.872 -32.431  38.798  1.00 45.63           C  
ANISOU 4805  C   VAL B 237     7024   5420   4894   -560   1169   -357       C  
ATOM   4806  O   VAL B 237      54.890 -32.908  38.301  1.00 49.94           O  
ANISOU 4806  O   VAL B 237     7522   5994   5460   -532    967   -292       O  
ATOM   4807  CB  VAL B 237      53.726 -29.999  39.467  1.00 50.24           C  
ANISOU 4807  CB  VAL B 237     7713   5936   5439   -584   1343   -558       C  
ATOM   4808  CG1 VAL B 237      55.215 -30.027  39.762  1.00 50.59           C  
ANISOU 4808  CG1 VAL B 237     7864   6018   5340   -634   1090   -529       C  
ATOM   4809  CG2 VAL B 237      53.270 -28.614  39.011  1.00 46.32           C  
ANISOU 4809  CG2 VAL B 237     7118   5377   5105   -525   1466   -654       C  
ATOM   4810  N   TYR B 238      53.161 -33.080  39.725  1.00 45.40           N  
ANISOU 4810  N   TYR B 238     7136   5371   4743   -630   1310   -339       N  
ATOM   4811  CA  TYR B 238      53.572 -34.404  40.184  1.00 50.53           C  
ANISOU 4811  CA  TYR B 238     7906   6025   5269   -674   1204   -225       C  
ATOM   4812  C   TYR B 238      53.247 -35.489  39.170  1.00 49.06           C  
ANISOU 4812  C   TYR B 238     7545   5836   5260   -622   1175   -150       C  
ATOM   4813  O   TYR B 238      53.947 -36.507  39.116  1.00 51.30           O  
ANISOU 4813  O   TYR B 238     7866   6108   5517   -614   1026    -53       O  
ATOM   4814  CB  TYR B 238      52.909 -34.738  41.521  1.00 52.52           C  
ANISOU 4814  CB  TYR B 238     8403   6245   5309   -787   1381   -224       C  
ATOM   4815  CG  TYR B 238      53.375 -33.867  42.666  1.00 57.79           C  
ANISOU 4815  CG  TYR B 238     9323   6907   5726   -875   1384   -294       C  
ATOM   4816  CD1 TYR B 238      54.488 -34.220  43.422  1.00 54.94           C  
ANISOU 4816  CD1 TYR B 238     9171   6564   5139   -942   1148   -214       C  
ATOM   4817  CD2 TYR B 238      52.706 -32.690  42.991  1.00 60.82           C  
ANISOU 4817  CD2 TYR B 238     9743   7259   6108   -897   1615   -441       C  
ATOM   4818  CE1 TYR B 238      54.922 -33.429  44.472  1.00 57.97           C  
ANISOU 4818  CE1 TYR B 238     9812   6948   5266  -1054   1122   -283       C  
ATOM   4819  CE2 TYR B 238      53.137 -31.885  44.039  1.00 59.68           C  
ANISOU 4819  CE2 TYR B 238     9867   7096   5714  -1000   1629   -529       C  
ATOM   4820  CZ  TYR B 238      54.245 -32.263  44.775  1.00 57.85           C  
ANISOU 4820  CZ  TYR B 238     9859   6896   5225  -1090   1372   -451       C  
ATOM   4821  OH  TYR B 238      54.689 -31.477  45.811  1.00 57.71           O  
ANISOU 4821  OH  TYR B 238    10129   6865   4933  -1221   1354   -540       O  
ATOM   4822  N   GLY B 239      52.201 -35.299  38.368  1.00 48.24           N  
ANISOU 4822  N   GLY B 239     7254   5731   5344   -590   1308   -191       N  
ATOM   4823  CA  GLY B 239      51.803 -36.308  37.404  1.00 47.64           C  
ANISOU 4823  CA  GLY B 239     7035   5650   5416   -573   1279   -136       C  
ATOM   4824  C   GLY B 239      50.933 -37.396  38.000  1.00 49.39           C  
ANISOU 4824  C   GLY B 239     7331   5831   5603   -656   1417    -86       C  
ATOM   4825  O   GLY B 239      51.076 -37.744  39.175  1.00 47.03           O  
ANISOU 4825  O   GLY B 239     7248   5507   5115   -722   1466    -49       O  
ATOM   4826  N   ASP B 240      50.026 -37.939  37.194  1.00 45.19           N  
ANISOU 4826  N   ASP B 240     6634   5293   5243   -670   1473    -78       N  
ATOM   4827  CA  ASP B 240      49.082 -38.965  37.623  1.00 45.83           C  
ANISOU 4827  CA  ASP B 240     6748   5330   5337   -766   1620    -36       C  
ATOM   4828  C   ASP B 240      49.358 -40.220  36.806  1.00 46.31           C  
ANISOU 4828  C   ASP B 240     6782   5352   5462   -776   1493     26       C  
ATOM   4829  O   ASP B 240      49.172 -40.218  35.584  1.00 43.80           O  
ANISOU 4829  O   ASP B 240     6291   5055   5295   -753   1413     -2       O  
ATOM   4830  CB  ASP B 240      47.643 -38.471  37.438  1.00 52.44           C  
ANISOU 4830  CB  ASP B 240     7388   6179   6356   -794   1814    -91       C  
ATOM   4831  CG  ASP B 240      46.594 -39.530  37.760  1.00 61.03           C  
ANISOU 4831  CG  ASP B 240     8463   7223   7503   -911   1977    -51       C  
ATOM   4832  OD1 ASP B 240      46.949 -40.634  38.228  1.00 58.77           O  
ANISOU 4832  OD1 ASP B 240     8358   6884   7088   -975   1959     22       O  
ATOM   4833  OD2 ASP B 240      45.396 -39.243  37.538  1.00 63.16           O  
ANISOU 4833  OD2 ASP B 240     8524   7502   7971   -939   2123    -85       O  
ATOM   4834  N   PHE B 241      49.807 -41.284  37.479  1.00 44.20           N  
ANISOU 4834  N   PHE B 241     6705   5017   5073   -817   1472    110       N  
ATOM   4835  CA  PHE B 241      50.223 -42.516  36.813  1.00 46.75           C  
ANISOU 4835  CA  PHE B 241     7039   5267   5456   -815   1365    166       C  
ATOM   4836  C   PHE B 241      49.235 -43.663  37.011  1.00 49.94           C  
ANISOU 4836  C   PHE B 241     7478   5592   5905   -937   1500    210       C  
ATOM   4837  O   PHE B 241      49.594 -44.827  36.797  1.00 49.21           O  
ANISOU 4837  O   PHE B 241     7467   5399   5829   -951   1442    270       O  
ATOM   4838  CB  PHE B 241      51.612 -42.931  37.299  1.00 44.54           C  
ANISOU 4838  CB  PHE B 241     6927   4939   5059   -749   1207    250       C  
ATOM   4839  CG  PHE B 241      52.675 -41.891  37.051  1.00 43.68           C  
ANISOU 4839  CG  PHE B 241     6764   4901   4933   -646   1063    210       C  
ATOM   4840  CD1 PHE B 241      52.814 -40.804  37.908  1.00 51.27           C  
ANISOU 4840  CD1 PHE B 241     7795   5925   5759   -651   1077    182       C  
ATOM   4841  CD2 PHE B 241      53.527 -41.993  35.962  1.00 45.50           C  
ANISOU 4841  CD2 PHE B 241     6884   5123   5279   -560    935    190       C  
ATOM   4842  CE1 PHE B 241      53.782 -39.842  37.683  1.00 48.00           C  
ANISOU 4842  CE1 PHE B 241     7330   5568   5340   -577    945    142       C  
ATOM   4843  CE2 PHE B 241      54.503 -41.028  35.728  1.00 51.61           C  
ANISOU 4843  CE2 PHE B 241     7598   5958   6054   -481    821    154       C  
ATOM   4844  CZ  PHE B 241      54.628 -39.947  36.589  1.00 47.91           C  
ANISOU 4844  CZ  PHE B 241     7187   5554   5463   -492    816    133       C  
ATOM   4845  N   SER B 242      47.991 -43.367  37.393  1.00 46.52           N  
ANISOU 4845  N   SER B 242     6972   5186   5517  -1025   1694    177       N  
ATOM   4846  CA  SER B 242      47.053 -44.431  37.729  1.00 50.77           C  
ANISOU 4846  CA  SER B 242     7548   5646   6097  -1163   1848    223       C  
ATOM   4847  C   SER B 242      46.244 -44.939  36.540  1.00 52.24           C  
ANISOU 4847  C   SER B 242     7523   5823   6503  -1230   1829    182       C  
ATOM   4848  O   SER B 242      45.691 -46.041  36.620  1.00 53.56           O  
ANISOU 4848  O   SER B 242     7734   5901   6717  -1351   1908    223       O  
ATOM   4849  CB  SER B 242      46.099 -43.971  38.843  1.00 56.37           C  
ANISOU 4849  CB  SER B 242     8291   6373   6754  -1248   2109    212       C  
ATOM   4850  OG  SER B 242      45.338 -42.850  38.444  1.00 56.87           O  
ANISOU 4850  OG  SER B 242     8108   6522   6976  -1217   2189    116       O  
ATOM   4851  N   HIS B 243      46.160 -44.186  35.447  1.00 47.98           N  
ANISOU 4851  N   HIS B 243     6776   5367   6087  -1171   1717    109       N  
ATOM   4852  CA  HIS B 243      45.394 -44.603  34.280  1.00 50.43           C  
ANISOU 4852  CA  HIS B 243     6901   5680   6578  -1254   1658     72       C  
ATOM   4853  C   HIS B 243      46.331 -44.942  33.127  1.00 49.81           C  
ANISOU 4853  C   HIS B 243     6864   5580   6480  -1202   1456     46       C  
ATOM   4854  O   HIS B 243      47.516 -44.598  33.143  1.00 45.16           O  
ANISOU 4854  O   HIS B 243     6377   4997   5786  -1078   1367     49       O  
ATOM   4855  CB  HIS B 243      44.412 -43.509  33.847  1.00 56.44           C  
ANISOU 4855  CB  HIS B 243     7391   6546   7509  -1249   1678     25       C  
ATOM   4856  CG  HIS B 243      43.600 -42.950  34.975  1.00 73.79           C  
ANISOU 4856  CG  HIS B 243     9534   8759   9745  -1268   1916     28       C  
ATOM   4857  ND1 HIS B 243      42.551 -43.637  35.550  1.00 73.71           N  
ANISOU 4857  ND1 HIS B 243     9479   8700   9826  -1410   2115     51       N  
ATOM   4858  CD2 HIS B 243      43.683 -41.769  35.635  1.00 74.64           C  
ANISOU 4858  CD2 HIS B 243     9635   8910   9812  -1172   2015     -2       C  
ATOM   4859  CE1 HIS B 243      42.026 -42.906  36.516  1.00 74.87           C  
ANISOU 4859  CE1 HIS B 243     9595   8865   9987  -1396   2344     34       C  
ATOM   4860  NE2 HIS B 243      42.694 -41.769  36.589  1.00 76.82           N  
ANISOU 4860  NE2 HIS B 243     9874   9163  10151  -1252   2287     -4       N  
ATOM   4861  N   SER B 244      45.787 -45.617  32.106  1.00 43.63           N  
ANISOU 4861  N   SER B 244     6004   4770   5803  -1310   1391     12       N  
ATOM   4862  CA  SER B 244      46.626 -45.978  30.964  1.00 42.78           C  
ANISOU 4862  CA  SER B 244     5964   4627   5663  -1281   1240    -34       C  
ATOM   4863  C   SER B 244      47.215 -44.745  30.293  1.00 44.46           C  
ANISOU 4863  C   SER B 244     6099   4948   5846  -1160   1121    -72       C  
ATOM   4864  O   SER B 244      48.360 -44.785  29.825  1.00 41.90           O  
ANISOU 4864  O   SER B 244     5876   4596   5448  -1075   1050    -94       O  
ATOM   4865  CB  SER B 244      45.847 -46.823  29.953  1.00 47.31           C  
ANISOU 4865  CB  SER B 244     6489   5157   6329  -1452   1187    -81       C  
ATOM   4866  OG  SER B 244      44.831 -46.091  29.305  1.00 58.54           O  
ANISOU 4866  OG  SER B 244     7685   6695   7862  -1519   1109   -104       O  
ATOM   4867  N   GLN B 245      46.470 -43.642  30.242  1.00 40.51           N  
ANISOU 4867  N   GLN B 245     5414   4557   5421  -1148   1113    -74       N  
ATOM   4868  CA  GLN B 245      47.033 -42.376  29.781  1.00 41.48           C  
ANISOU 4868  CA  GLN B 245     5481   4765   5515  -1028   1020    -93       C  
ATOM   4869  C   GLN B 245      47.595 -41.591  30.964  1.00 43.47           C  
ANISOU 4869  C   GLN B 245     5788   5035   5694   -910   1110    -71       C  
ATOM   4870  O   GLN B 245      46.901 -41.364  31.959  1.00 41.37           O  
ANISOU 4870  O   GLN B 245     5486   4774   5459   -927   1250    -52       O  
ATOM   4871  CB  GLN B 245      46.002 -41.533  29.024  1.00 51.06           C  
ANISOU 4871  CB  GLN B 245     6473   6065   6862  -1062    938    -94       C  
ATOM   4872  CG  GLN B 245      46.574 -40.942  27.712  1.00 71.97           C  
ANISOU 4872  CG  GLN B 245     9128   8759   9458  -1029    762   -117       C  
ATOM   4873  CD  GLN B 245      46.217 -39.477  27.470  1.00 83.50           C  
ANISOU 4873  CD  GLN B 245    10429  10299  11000   -948    701    -88       C  
ATOM   4874  OE1 GLN B 245      45.867 -38.741  28.394  1.00 94.42           O  
ANISOU 4874  OE1 GLN B 245    11723  11695  12460   -873    814    -70       O  
ATOM   4875  NE2 GLN B 245      46.313 -39.051  26.216  1.00 80.47           N  
ANISOU 4875  NE2 GLN B 245    10029   9954  10590   -967    531    -83       N  
ATOM   4876  N   LEU B 246      48.855 -41.187  30.841  1.00 39.09           N  
ANISOU 4876  N   LEU B 246     5326   4484   5042   -805   1039    -82       N  
ATOM   4877  CA  LEU B 246      49.548 -40.420  31.869  1.00 45.89           C  
ANISOU 4877  CA  LEU B 246     6258   5363   5815   -711   1080    -69       C  
ATOM   4878  C   LEU B 246      48.943 -39.025  31.998  1.00 44.74           C  
ANISOU 4878  C   LEU B 246     5982   5288   5731   -672   1120    -93       C  
ATOM   4879  O   LEU B 246      48.803 -38.302  31.015  1.00 46.43           O  
ANISOU 4879  O   LEU B 246     6079   5545   6018   -646   1032   -110       O  
ATOM   4880  CB  LEU B 246      51.035 -40.328  31.504  1.00 41.70           C  
ANISOU 4880  CB  LEU B 246     5811   4822   5213   -623    972    -76       C  
ATOM   4881  CG  LEU B 246      52.078 -40.223  32.616  1.00 51.74           C  
ANISOU 4881  CG  LEU B 246     7210   6074   6377   -557    963    -40       C  
ATOM   4882  CD1 LEU B 246      53.464 -40.595  32.084  1.00 47.20           C  
ANISOU 4882  CD1 LEU B 246     6672   5459   5801   -487    859    -36       C  
ATOM   4883  CD2 LEU B 246      52.093 -38.826  33.193  1.00 58.56           C  
ANISOU 4883  CD2 LEU B 246     8047   7003   7199   -517    984    -67       C  
ATOM   4884  N   GLY B 247      48.576 -38.643  33.229  1.00 43.84           N  
ANISOU 4884  N   GLY B 247     5907   5169   5582   -670   1263    -91       N  
ATOM   4885  CA  GLY B 247      47.943 -37.360  33.465  1.00 48.53           C  
ANISOU 4885  CA  GLY B 247     6386   5796   6259   -627   1349   -126       C  
ATOM   4886  C   GLY B 247      48.951 -36.307  33.877  1.00 43.11           C  
ANISOU 4886  C   GLY B 247     5797   5120   5464   -543   1318   -158       C  
ATOM   4887  O   GLY B 247      49.795 -36.549  34.743  1.00 43.24           O  
ANISOU 4887  O   GLY B 247     5996   5119   5316   -546   1316   -151       O  
ATOM   4888  N   GLY B 248      48.866 -35.136  33.244  1.00 43.65           N  
ANISOU 4888  N   GLY B 248     5747   5210   5629   -477   1276   -184       N  
ATOM   4889  CA  GLY B 248      49.693 -34.008  33.665  1.00 41.57           C  
ANISOU 4889  CA  GLY B 248     5567   4942   5286   -414   1269   -226       C  
ATOM   4890  C   GLY B 248      51.175 -34.210  33.395  1.00 42.74           C  
ANISOU 4890  C   GLY B 248     5825   5104   5311   -396   1111   -216       C  
ATOM   4891  O   GLY B 248      51.582 -34.695  32.330  1.00 43.16           O  
ANISOU 4891  O   GLY B 248     5832   5171   5394   -392    992   -191       O  
ATOM   4892  N   LEU B 249      51.995 -33.814  34.380  1.00 44.63           N  
ANISOU 4892  N   LEU B 249     6210   5334   5413   -394   1115   -242       N  
ATOM   4893  CA  LEU B 249      53.456 -33.905  34.338  1.00 41.25           C  
ANISOU 4893  CA  LEU B 249     5859   4917   4896   -377    965   -228       C  
ATOM   4894  C   LEU B 249      54.055 -32.947  33.309  1.00 42.93           C  
ANISOU 4894  C   LEU B 249     5980   5145   5188   -329    881   -252       C  
ATOM   4895  O   LEU B 249      54.692 -33.374  32.339  1.00 43.14           O  
ANISOU 4895  O   LEU B 249     5955   5182   5253   -313    788   -228       O  
ATOM   4896  CB  LEU B 249      53.906 -35.348  34.059  1.00 40.04           C  
ANISOU 4896  CB  LEU B 249     5730   4752   4729   -388    887   -164       C  
ATOM   4897  CG  LEU B 249      55.316 -35.746  34.504  1.00 44.77           C  
ANISOU 4897  CG  LEU B 249     6419   5342   5249   -371    756   -125       C  
ATOM   4898  CD1 LEU B 249      55.458 -35.669  36.030  1.00 40.77           C  
ANISOU 4898  CD1 LEU B 249     6086   4830   4576   -418    762   -107       C  
ATOM   4899  CD2 LEU B 249      55.657 -37.149  33.992  1.00 52.57           C  
ANISOU 4899  CD2 LEU B 249     7398   6287   6288   -356    706    -67       C  
ATOM   4900  N   HIS B 250      53.886 -31.642  33.527  1.00 37.88           N  
ANISOU 4900  N   HIS B 250     5334   4490   4569   -312    933   -304       N  
ATOM   4901  CA  HIS B 250      54.271 -30.638  32.541  1.00 38.25           C  
ANISOU 4901  CA  HIS B 250     5301   4532   4700   -275    875   -314       C  
ATOM   4902  C   HIS B 250      55.413 -29.733  32.977  1.00 38.20           C  
ANISOU 4902  C   HIS B 250     5370   4511   4631   -286    824   -358       C  
ATOM   4903  O   HIS B 250      55.793 -28.830  32.217  1.00 40.89           O  
ANISOU 4903  O   HIS B 250     5661   4835   5040   -267    790   -366       O  
ATOM   4904  CB  HIS B 250      53.054 -29.778  32.188  1.00 40.77           C  
ANISOU 4904  CB  HIS B 250     5520   4817   5153   -238    966   -321       C  
ATOM   4905  CG  HIS B 250      51.920 -30.570  31.618  1.00 42.62           C  
ANISOU 4905  CG  HIS B 250     5640   5070   5482   -242    981   -271       C  
ATOM   4906  ND1 HIS B 250      51.949 -31.088  30.341  1.00 40.32           N  
ANISOU 4906  ND1 HIS B 250     5280   4812   5227   -254    866   -220       N  
ATOM   4907  CD2 HIS B 250      50.739 -30.952  32.156  1.00 43.11           C  
ANISOU 4907  CD2 HIS B 250     5648   5122   5608   -255   1101   -270       C  
ATOM   4908  CE1 HIS B 250      50.824 -31.747  30.113  1.00 42.53           C  
ANISOU 4908  CE1 HIS B 250     5469   5104   5588   -280    886   -187       C  
ATOM   4909  NE2 HIS B 250      50.074 -31.678  31.198  1.00 44.37           N  
ANISOU 4909  NE2 HIS B 250     5690   5312   5857   -278   1031   -213       N  
ATOM   4910  N   LEU B 251      55.949 -29.913  34.179  1.00 39.21           N  
ANISOU 4910  N   LEU B 251     5628   4642   4628   -331    808   -381       N  
ATOM   4911  CA  LEU B 251      57.069 -29.115  34.667  1.00 39.75           C  
ANISOU 4911  CA  LEU B 251     5768   4703   4631   -369    726   -424       C  
ATOM   4912  C   LEU B 251      58.281 -30.018  34.814  1.00 44.49           C  
ANISOU 4912  C   LEU B 251     6373   5344   5186   -387    566   -368       C  
ATOM   4913  O   LEU B 251      58.169 -31.122  35.350  1.00 42.86           O  
ANISOU 4913  O   LEU B 251     6223   5152   4911   -394    543   -315       O  
ATOM   4914  CB  LEU B 251      56.750 -28.462  36.014  1.00 38.55           C  
ANISOU 4914  CB  LEU B 251     5785   4514   4348   -429    813   -501       C  
ATOM   4915  CG  LEU B 251      56.033 -27.103  36.015  1.00 47.11           C  
ANISOU 4915  CG  LEU B 251     6877   5520   5504   -412    964   -587       C  
ATOM   4916  CD1 LEU B 251      56.985 -25.984  35.557  1.00 47.53           C  
ANISOU 4916  CD1 LEU B 251     6911   5540   5608   -427    880   -623       C  
ATOM   4917  CD2 LEU B 251      54.771 -27.125  35.157  1.00 50.21           C  
ANISOU 4917  CD2 LEU B 251     7116   5891   6072   -326   1080   -553       C  
ATOM   4918  N   LEU B 252      59.441 -29.542  34.358  1.00 39.09           N  
ANISOU 4918  N   LEU B 252     5623   4669   4562   -394    461   -372       N  
ATOM   4919  CA  LEU B 252      60.624 -30.402  34.356  1.00 45.48           C  
ANISOU 4919  CA  LEU B 252     6377   5506   5398   -389    317   -310       C  
ATOM   4920  C   LEU B 252      60.965 -30.885  35.762  1.00 41.37           C  
ANISOU 4920  C   LEU B 252     5989   4997   4732   -442    204   -276       C  
ATOM   4921  O   LEU B 252      61.364 -32.044  35.952  1.00 44.05           O  
ANISOU 4921  O   LEU B 252     6315   5341   5080   -413    115   -190       O  
ATOM   4922  CB  LEU B 252      61.817 -29.666  33.738  1.00 39.20           C  
ANISOU 4922  CB  LEU B 252     5469   4712   4711   -404    246   -328       C  
ATOM   4923  CG  LEU B 252      63.076 -30.535  33.616  1.00 42.81           C  
ANISOU 4923  CG  LEU B 252     5813   5187   5267   -381    117   -263       C  
ATOM   4924  CD1 LEU B 252      62.809 -31.731  32.682  1.00 43.92           C  
ANISOU 4924  CD1 LEU B 252     5883   5314   5493   -300    194   -218       C  
ATOM   4925  CD2 LEU B 252      64.280 -29.731  33.139  1.00 43.71           C  
ANISOU 4925  CD2 LEU B 252     5798   5303   5507   -416     64   -287       C  
ATOM   4926  N   ILE B 253      60.796 -30.021  36.767  1.00 41.31           N  
ANISOU 4926  N   ILE B 253     6133   4982   4581   -524    208   -340       N  
ATOM   4927  CA  ILE B 253      61.146 -30.405  38.131  1.00 41.87           C  
ANISOU 4927  CA  ILE B 253     6378   5067   4464   -604     82   -305       C  
ATOM   4928  C   ILE B 253      60.318 -31.598  38.596  1.00 44.33           C  
ANISOU 4928  C   ILE B 253     6790   5372   4683   -585    148   -235       C  
ATOM   4929  O   ILE B 253      60.794 -32.426  39.384  1.00 46.76           O  
ANISOU 4929  O   ILE B 253     7192   5687   4886   -615      2   -141       O  
ATOM   4930  CB  ILE B 253      60.996 -29.197  39.079  1.00 45.15           C  
ANISOU 4930  CB  ILE B 253     6982   5460   4711   -718    115   -416       C  
ATOM   4931  CG1 ILE B 253      61.586 -29.524  40.451  1.00 46.94           C  
ANISOU 4931  CG1 ILE B 253     7413   5711   4710   -834    -70   -375       C  
ATOM   4932  CG2 ILE B 253      59.530 -28.775  39.194  1.00 43.58           C  
ANISOU 4932  CG2 ILE B 253     6875   5213   4468   -705    385   -500       C  
ATOM   4933  CD1 ILE B 253      61.678 -28.320  41.400  1.00 46.36           C  
ANISOU 4933  CD1 ILE B 253     7556   5612   4444   -982    -70   -501       C  
ATOM   4934  N   GLY B 254      59.085 -31.727  38.104  1.00 43.77           N  
ANISOU 4934  N   GLY B 254     6689   5279   4661   -540    355   -265       N  
ATOM   4935  CA  GLY B 254      58.278 -32.881  38.471  1.00 41.70           C  
ANISOU 4935  CA  GLY B 254     6503   5004   4338   -536    434   -199       C  
ATOM   4936  C   GLY B 254      58.780 -34.157  37.822  1.00 44.21           C  
ANISOU 4936  C   GLY B 254     6707   5315   4774   -466    332    -93       C  
ATOM   4937  O   GLY B 254      58.737 -35.230  38.427  1.00 47.37           O  
ANISOU 4937  O   GLY B 254     7208   5691   5098   -479    292     -1       O  
ATOM   4938  N   LEU B 255      59.253 -34.062  36.577  1.00 44.67           N  
ANISOU 4938  N   LEU B 255     6575   5378   5019   -395    308   -105       N  
ATOM   4939  CA  LEU B 255      59.937 -35.197  35.966  1.00 52.74           C  
ANISOU 4939  CA  LEU B 255     7496   6374   6167   -327    226    -25       C  
ATOM   4940  C   LEU B 255      61.201 -35.542  36.734  1.00 50.33           C  
ANISOU 4940  C   LEU B 255     7212   6064   5845   -328     16     62       C  
ATOM   4941  O   LEU B 255      61.530 -36.719  36.902  1.00 44.00           O  
ANISOU 4941  O   LEU B 255     6417   5215   5087   -284    -57    165       O  
ATOM   4942  CB  LEU B 255      60.283 -34.899  34.509  1.00 46.72           C  
ANISOU 4942  CB  LEU B 255     6556   5615   5581   -272    267    -72       C  
ATOM   4943  CG  LEU B 255      59.202 -35.016  33.443  1.00 48.86           C  
ANISOU 4943  CG  LEU B 255     6780   5880   5907   -260    415   -114       C  
ATOM   4944  CD1 LEU B 255      58.271 -33.829  33.501  1.00 50.04           C  
ANISOU 4944  CD1 LEU B 255     6948   6056   6010   -294    505   -181       C  
ATOM   4945  CD2 LEU B 255      59.869 -35.121  32.068  1.00 47.25           C  
ANISOU 4945  CD2 LEU B 255     6447   5664   5841   -218    424   -133       C  
ATOM   4946  N   ALA B 256      61.922 -34.522  37.209  1.00 41.25           N  
ANISOU 4946  N   ALA B 256     6070   4955   4648   -380    -98     28       N  
ATOM   4947  CA  ALA B 256      63.146 -34.766  37.965  1.00 48.22           C  
ANISOU 4947  CA  ALA B 256     6952   5844   5526   -397   -344    121       C  
ATOM   4948  C   ALA B 256      62.855 -35.537  39.242  1.00 48.00           C  
ANISOU 4948  C   ALA B 256     7147   5798   5294   -449   -434    223       C  
ATOM   4949  O   ALA B 256      63.575 -36.484  39.578  1.00 55.37           O  
ANISOU 4949  O   ALA B 256     8060   6697   6282   -406   -611    362       O  
ATOM   4950  CB  ALA B 256      63.844 -33.445  38.287  1.00 45.69           C  
ANISOU 4950  CB  ALA B 256     6621   5571   5169   -483   -450     50       C  
ATOM   4951  N   LYS B 257      61.798 -35.153  39.962  1.00 48.34           N  
ANISOU 4951  N   LYS B 257     7406   5851   5111   -539   -301    164       N  
ATOM   4952  CA  LYS B 257      61.455 -35.849  41.196  1.00 49.09           C  
ANISOU 4952  CA  LYS B 257     7754   5925   4973   -613   -351    259       C  
ATOM   4953  C   LYS B 257      61.089 -37.303  40.919  1.00 48.38           C  
ANISOU 4953  C   LYS B 257     7645   5766   4969   -535   -302    374       C  
ATOM   4954  O   LYS B 257      61.543 -38.216  41.619  1.00 59.31           O  
ANISOU 4954  O   LYS B 257     9134   7110   6291   -538   -470    527       O  
ATOM   4955  CB  LYS B 257      60.309 -35.125  41.905  1.00 48.80           C  
ANISOU 4955  CB  LYS B 257     7939   5899   4704   -724   -141    147       C  
ATOM   4956  CG  LYS B 257      60.005 -35.668  43.298  1.00 49.39           C  
ANISOU 4956  CG  LYS B 257     8332   5956   4479   -841   -171    230       C  
ATOM   4957  CD  LYS B 257      59.000 -34.778  44.025  1.00 51.19           C  
ANISOU 4957  CD  LYS B 257     8781   6185   4482   -961     70     87       C  
ATOM   4958  CE  LYS B 257      58.677 -35.307  45.413  1.00 58.32           C  
ANISOU 4958  CE  LYS B 257    10041   7067   5050  -1101     76    162       C  
ATOM   4959  NZ  LYS B 257      59.792 -35.085  46.369  1.00 62.21           N  
ANISOU 4959  NZ  LYS B 257    10730   7592   5317  -1214   -242    230       N  
ATOM   4960  N   ARG B 258      60.277 -37.540  39.885  1.00 47.66           N  
ANISOU 4960  N   ARG B 258     7430   5654   5026   -472    -89    308       N  
ATOM   4961  CA  ARG B 258      59.880 -38.910  39.565  1.00 50.03           C  
ANISOU 4961  CA  ARG B 258     7722   5874   5412   -418    -28    396       C  
ATOM   4962  C   ARG B 258      61.078 -39.739  39.124  1.00 49.65           C  
ANISOU 4962  C   ARG B 258     7532   5766   5565   -308   -205    503       C  
ATOM   4963  O   ARG B 258      61.212 -40.906  39.510  1.00 55.12           O  
ANISOU 4963  O   ARG B 258     8303   6372   6270   -278   -273    639       O  
ATOM   4964  CB  ARG B 258      58.812 -38.905  38.475  1.00 45.70           C  
ANISOU 4964  CB  ARG B 258     7060   5322   4982   -395    205    293       C  
ATOM   4965  CG  ARG B 258      58.426 -40.300  37.974  1.00 53.41           C  
ANISOU 4965  CG  ARG B 258     8018   6206   6068   -356    272    357       C  
ATOM   4966  CD  ARG B 258      57.192 -40.821  38.678  1.00 60.43           C  
ANISOU 4966  CD  ARG B 258     9076   7065   6819   -449    424    383       C  
ATOM   4967  NE  ARG B 258      56.860 -42.193  38.288  1.00 65.26           N  
ANISOU 4967  NE  ARG B 258     9694   7572   7532   -433    477    450       N  
ATOM   4968  CZ  ARG B 258      55.897 -42.911  38.859  1.00 67.91           C  
ANISOU 4968  CZ  ARG B 258    10170   7853   7779   -519    604    498       C  
ATOM   4969  NH1 ARG B 258      55.180 -42.378  39.837  1.00 76.93           N  
ANISOU 4969  NH1 ARG B 258    11456   9043   8731   -621    709    482       N  
ATOM   4970  NH2 ARG B 258      55.653 -44.161  38.467  1.00 54.74           N  
ANISOU 4970  NH2 ARG B 258     8511   6072   6216   -514    647    554       N  
ATOM   4971  N   PHE B 259      61.970 -39.136  38.332  1.00 50.77           N  
ANISOU 4971  N   PHE B 259     7465   5942   5884   -245   -269    447       N  
ATOM   4972  CA  PHE B 259      63.094 -39.863  37.751  1.00 58.76           C  
ANISOU 4972  CA  PHE B 259     8295   6886   7145   -126   -379    523       C  
ATOM   4973  C   PHE B 259      64.018 -40.425  38.822  1.00 61.86           C  
ANISOU 4973  C   PHE B 259     8743   7241   7522   -111   -648    700       C  
ATOM   4974  O   PHE B 259      64.512 -41.554  38.693  1.00 58.61           O  
ANISOU 4974  O   PHE B 259     8268   6718   7283     -8   -711    819       O  
ATOM   4975  CB  PHE B 259      63.871 -38.945  36.806  1.00 62.87           C  
ANISOU 4975  CB  PHE B 259     8592   7459   7838    -91   -372    423       C  
ATOM   4976  CG  PHE B 259      64.973 -39.638  36.064  1.00 70.27           C  
ANISOU 4976  CG  PHE B 259     9315   8318   9065     33   -412    471       C  
ATOM   4977  CD1 PHE B 259      64.682 -40.489  35.007  1.00 74.37           C  
ANISOU 4977  CD1 PHE B 259     9779   8748   9729    108   -228    433       C  
ATOM   4978  CD2 PHE B 259      66.297 -39.444  36.422  1.00 75.02           C  
ANISOU 4978  CD2 PHE B 259     9767   8928   9809     68   -626    548       C  
ATOM   4979  CE1 PHE B 259      65.695 -41.136  34.321  1.00 82.68           C  
ANISOU 4979  CE1 PHE B 259    10647   9707  11062    225   -218    459       C  
ATOM   4980  CE2 PHE B 259      67.314 -40.084  35.740  1.00 79.69           C  
ANISOU 4980  CE2 PHE B 259    10130   9433  10714    195   -630    590       C  
ATOM   4981  CZ  PHE B 259      67.015 -40.932  34.690  1.00 77.90           C  
ANISOU 4981  CZ  PHE B 259     9865   9104  10628    279   -407    539       C  
ATOM   4982  N   LYS B 260      64.264 -39.656  39.888  1.00 59.78           N  
ANISOU 4982  N   LYS B 260     8605   7055   7053   -216   -819    724       N  
ATOM   4983  CA  LYS B 260      65.157 -40.128  40.942  1.00 67.41           C  
ANISOU 4983  CA  LYS B 260     9638   7996   7978   -224  -1129    910       C  
ATOM   4984  C   LYS B 260      64.621 -41.382  41.618  1.00 70.08           C  
ANISOU 4984  C   LYS B 260    10191   8234   8202   -220  -1138   1065       C  
ATOM   4985  O   LYS B 260      65.399 -42.179  42.152  1.00 76.38           O  
ANISOU 4985  O   LYS B 260    10990   8958   9072   -164  -1381   1260       O  
ATOM   4986  CB  LYS B 260      65.392 -39.021  41.973  1.00 71.98           C  
ANISOU 4986  CB  LYS B 260    10370   8681   8298   -380  -1302    884       C  
ATOM   4987  CG  LYS B 260      66.507 -38.056  41.588  1.00 85.42           C  
ANISOU 4987  CG  LYS B 260    11832  10450  10173   -379  -1449    823       C  
ATOM   4988  CD  LYS B 260      67.862 -38.765  41.527  1.00 95.20           C  
ANISOU 4988  CD  LYS B 260    12830  11637  11702   -266  -1721    993       C  
ATOM   4989  CE  LYS B 260      68.902 -37.948  40.763  1.00 96.07           C  
ANISOU 4989  CE  LYS B 260    12619  11795  12088   -237  -1768    912       C  
ATOM   4990  NZ  LYS B 260      68.623 -37.896  39.296  1.00 90.68           N  
ANISOU 4990  NZ  LYS B 260    11747  11082  11625   -134  -1446    771       N  
ATOM   4991  N   GLU B 261      63.305 -41.584  41.593  1.00 71.59           N  
ANISOU 4991  N   GLU B 261    10550   8411   8238   -279   -880    994       N  
ATOM   4992  CA  GLU B 261      62.679 -42.735  42.229  1.00 73.44           C  
ANISOU 4992  CA  GLU B 261    11007   8544   8352   -303   -845   1132       C  
ATOM   4993  C   GLU B 261      62.360 -43.861  41.256  1.00 66.33           C  
ANISOU 4993  C   GLU B 261     9992   7514   7698   -188   -678   1141       C  
ATOM   4994  O   GLU B 261      62.571 -45.032  41.583  1.00 61.55           O  
ANISOU 4994  O   GLU B 261     9462   6773   7151   -135   -762   1311       O  
ATOM   4995  CB  GLU B 261      61.396 -42.303  42.946  1.00 83.49           C  
ANISOU 4995  CB  GLU B 261    12552   9871   9301   -466   -649   1054       C  
ATOM   4996  CG  GLU B 261      61.633 -41.309  44.071  1.00 96.03           C  
ANISOU 4996  CG  GLU B 261    14340  11558  10590   -607   -790   1042       C  
ATOM   4997  CD  GLU B 261      62.856 -41.657  44.910  1.00103.13           C  
ANISOU 4997  CD  GLU B 261    15307  12438  11439   -609  -1178   1245       C  
ATOM   4998  OE1 GLU B 261      63.897 -40.982  44.754  1.00105.68           O  
ANISOU 4998  OE1 GLU B 261    15454  12824  11875   -582  -1393   1228       O  
ATOM   4999  OE2 GLU B 261      62.781 -42.609  45.717  1.00103.94           O  
ANISOU 4999  OE2 GLU B 261    15632  12460  11402   -642  -1279   1434       O  
ATOM   5000  N   SER B 262      61.873 -43.539  40.064  1.00 57.84           N  
ANISOU 5000  N   SER B 262     8751   6464   6762   -157   -454    965       N  
ATOM   5001  CA  SER B 262      61.442 -44.564  39.125  1.00 58.86           C  
ANISOU 5001  CA  SER B 262     8813   6472   7078    -88   -280    945       C  
ATOM   5002  C   SER B 262      61.717 -44.108  37.697  1.00 58.54           C  
ANISOU 5002  C   SER B 262     8526   6463   7255    -15   -169    786       C  
ATOM   5003  O   SER B 262      61.235 -43.047  37.288  1.00 54.49           O  
ANISOU 5003  O   SER B 262     7965   6069   6670    -75    -70    643       O  
ATOM   5004  CB  SER B 262      59.955 -44.860  39.333  1.00 57.39           C  
ANISOU 5004  CB  SER B 262     8805   6278   6724   -207    -63    903       C  
ATOM   5005  OG  SER B 262      59.532 -45.940  38.534  1.00 68.08           O  
ANISOU 5005  OG  SER B 262    10124   7501   8241   -170     78    892       O  
ATOM   5006  N   PRO B 263      62.469 -44.874  36.910  1.00 59.62           N  
ANISOU 5006  N   PRO B 263     8515   6482   7655    111   -167    807       N  
ATOM   5007  CA  PRO B 263      62.863 -44.405  35.577  1.00 59.83           C  
ANISOU 5007  CA  PRO B 263     8333   6536   7862    166    -54    658       C  
ATOM   5008  C   PRO B 263      61.709 -44.442  34.586  1.00 56.38           C  
ANISOU 5008  C   PRO B 263     7929   6108   7384     97    179    510       C  
ATOM   5009  O   PRO B 263      60.728 -45.173  34.745  1.00 54.28           O  
ANISOU 5009  O   PRO B 263     7802   5781   7040     36    271    526       O  
ATOM   5010  CB  PRO B 263      63.966 -45.387  35.173  1.00 68.91           C  
ANISOU 5010  CB  PRO B 263     9350   7526   9308    318    -91    733       C  
ATOM   5011  CG  PRO B 263      63.603 -46.645  35.891  1.00 68.94           C  
ANISOU 5011  CG  PRO B 263     9526   7379   9288    330   -126    882       C  
ATOM   5012  CD  PRO B 263      63.014 -46.209  37.211  1.00 70.55           C  
ANISOU 5012  CD  PRO B 263     9930   7685   9191    209   -252    970       C  
ATOM   5013  N   PHE B 264      61.843 -43.630  33.540  1.00 51.73           N  
ANISOU 5013  N   PHE B 264     7209   5595   6849     96    264    373       N  
ATOM   5014  CA  PHE B 264      60.864 -43.616  32.466  1.00 43.27           C  
ANISOU 5014  CA  PHE B 264     6156   4537   5748     28    443    243       C  
ATOM   5015  C   PHE B 264      61.556 -43.227  31.167  1.00 47.11           C  
ANISOU 5015  C   PHE B 264     6504   5029   6367     71    524    134       C  
ATOM   5016  O   PHE B 264      62.700 -42.768  31.161  1.00 50.14           O  
ANISOU 5016  O   PHE B 264     6758   5429   6864    142    458    149       O  
ATOM   5017  CB  PHE B 264      59.703 -42.677  32.783  1.00 39.91           C  
ANISOU 5017  CB  PHE B 264     5791   4244   5130    -83    470    196       C  
ATOM   5018  CG  PHE B 264      60.143 -41.313  33.224  1.00 47.03           C  
ANISOU 5018  CG  PHE B 264     6638   5268   5964    -87    380    182       C  
ATOM   5019  CD1 PHE B 264      60.513 -40.363  32.294  1.00 50.22           C  
ANISOU 5019  CD1 PHE B 264     6922   5736   6422    -78    410     89       C  
ATOM   5020  CD2 PHE B 264      60.207 -40.990  34.572  1.00 53.28           C  
ANISOU 5020  CD2 PHE B 264     7523   6098   6622   -116    268    260       C  
ATOM   5021  CE1 PHE B 264      60.932 -39.100  32.696  1.00 59.90           C  
ANISOU 5021  CE1 PHE B 264     8106   7054   7598    -93    332     72       C  
ATOM   5022  CE2 PHE B 264      60.619 -39.734  34.984  1.00 57.14           C  
ANISOU 5022  CE2 PHE B 264     7985   6685   7041   -140    187    229       C  
ATOM   5023  CZ  PHE B 264      60.981 -38.786  34.044  1.00 56.39           C  
ANISOU 5023  CZ  PHE B 264     7753   6644   7029   -126    220    134       C  
ATOM   5024  N   GLU B 265      60.842 -43.427  30.060  1.00 41.40           N  
ANISOU 5024  N   GLU B 265     5816   4290   5624      9    666     26       N  
ATOM   5025  CA  GLU B 265      61.366 -43.226  28.717  1.00 41.37           C  
ANISOU 5025  CA  GLU B 265     5742   4272   5703     20    780    -85       C  
ATOM   5026  C   GLU B 265      60.754 -41.964  28.126  1.00 44.59           C  
ANISOU 5026  C   GLU B 265     6139   4825   5978    -69    789   -159       C  
ATOM   5027  O   GLU B 265      59.538 -41.769  28.210  1.00 43.24           O  
ANISOU 5027  O   GLU B 265     6035   4713   5682   -156    780   -167       O  
ATOM   5028  CB  GLU B 265      61.046 -44.433  27.831  1.00 47.26           C  
ANISOU 5028  CB  GLU B 265     6581   4876   6500     -5    924   -154       C  
ATOM   5029  CG  GLU B 265      61.744 -44.433  26.486  1.00 73.58           C  
ANISOU 5029  CG  GLU B 265     9884   8158   9915      6   1075   -274       C  
ATOM   5030  CD  GLU B 265      63.140 -45.022  26.565  1.00 91.89           C  
ANISOU 5030  CD  GLU B 265    12093  10341  12481    154   1129   -246       C  
ATOM   5031  OE1 GLU B 265      63.325 -46.024  27.296  1.00 92.59           O  
ANISOU 5031  OE1 GLU B 265    12195  10298  12686    234   1090   -155       O  
ATOM   5032  OE2 GLU B 265      64.050 -44.477  25.905  1.00100.61           O  
ANISOU 5032  OE2 GLU B 265    13088  11461  13678    190   1214   -306       O  
ATOM   5033  N   LEU B 266      61.596 -41.111  27.535  1.00 41.44           N  
ANISOU 5033  N   LEU B 266     5645   4473   5628    -46    811   -204       N  
ATOM   5034  CA  LEU B 266      61.163 -39.885  26.861  1.00 41.37           C  
ANISOU 5034  CA  LEU B 266     5632   4576   5511   -121    822   -260       C  
ATOM   5035  C   LEU B 266      61.619 -39.938  25.410  1.00 44.76           C  
ANISOU 5035  C   LEU B 266     6074   4966   5967   -148    963   -354       C  
ATOM   5036  O   LEU B 266      62.823 -39.861  25.133  1.00 50.60           O  
ANISOU 5036  O   LEU B 266     6723   5666   6837    -89   1030   -373       O  
ATOM   5037  CB  LEU B 266      61.745 -38.640  27.531  1.00 43.04           C  
ANISOU 5037  CB  LEU B 266     5751   4876   5727    -97    727   -225       C  
ATOM   5038  CG  LEU B 266      61.347 -38.234  28.942  1.00 46.97           C  
ANISOU 5038  CG  LEU B 266     6269   5428   6149    -98    599   -155       C  
ATOM   5039  CD1 LEU B 266      62.013 -36.907  29.280  1.00 48.36           C  
ANISOU 5039  CD1 LEU B 266     6372   5677   6327   -102    529   -158       C  
ATOM   5040  CD2 LEU B 266      59.846 -38.120  29.034  1.00 46.87           C  
ANISOU 5040  CD2 LEU B 266     6345   5456   6009   -168    619   -164       C  
ATOM   5041  N  AGLU B 267      60.673 -40.071  24.482  0.57 39.12           N  
ANISOU 5041  N  AGLU B 267     5473   4260   5131   -250   1010   -411       N  
ATOM   5042  N  BGLU B 267      60.668 -40.056  24.489  0.43 39.14           N  
ANISOU 5042  N  BGLU B 267     5474   4264   5132   -250   1009   -410       N  
ATOM   5043  CA AGLU B 267      60.984 -40.014  23.055  0.57 38.10           C  
ANISOU 5043  CA AGLU B 267     5413   4104   4958   -313   1141   -503       C  
ATOM   5044  CA BGLU B 267      60.966 -40.006  23.063  0.43 38.99           C  
ANISOU 5044  CA BGLU B 267     5526   4219   5070   -314   1138   -502       C  
ATOM   5045  C  AGLU B 267      60.859 -38.560  22.617  0.57 42.44           C  
ANISOU 5045  C  AGLU B 267     5946   4767   5412   -366   1094   -492       C  
ATOM   5046  C  BGLU B 267      60.856 -38.552  22.619  0.43 41.88           C  
ANISOU 5046  C  BGLU B 267     5874   4696   5340   -366   1093   -491       C  
ATOM   5047  O  AGLU B 267      59.769 -37.979  22.661  0.57 38.31           O  
ANISOU 5047  O  AGLU B 267     5452   4322   4783   -424    986   -455       O  
ATOM   5048  O  BGLU B 267      59.768 -37.967  22.648  0.43 38.92           O  
ANISOU 5048  O  BGLU B 267     5529   4400   4858   -425    986   -455       O  
ATOM   5049  CB AGLU B 267      60.070 -40.934  22.247  0.57 42.30           C  
ANISOU 5049  CB AGLU B 267     6105   4581   5385   -422   1187   -568       C  
ATOM   5050  CB BGLU B 267      60.023 -40.903  22.268  0.43 42.29           C  
ANISOU 5050  CB BGLU B 267     6103   4585   5379   -424   1180   -565       C  
ATOM   5051  CG AGLU B 267      59.930 -40.584  20.754  0.57 46.93           C  
ANISOU 5051  CG AGLU B 267     6825   5185   5820   -548   1261   -650       C  
ATOM   5052  CG BGLU B 267      60.062 -42.376  22.647  0.43 44.52           C  
ANISOU 5052  CG BGLU B 267     6429   4727   5759   -386   1241   -580       C  
ATOM   5053  CD AGLU B 267      61.061 -41.101  19.883  0.57 57.50           C  
ANISOU 5053  CD AGLU B 267     8227   6411   7211   -540   1485   -756       C  
ATOM   5054  CD BGLU B 267      59.185 -43.210  21.739  0.43 57.44           C  
ANISOU 5054  CD BGLU B 267     8240   6303   7280   -526   1289   -665       C  
ATOM   5055  OE1AGLU B 267      61.217 -40.599  18.737  0.57 54.14           O  
ANISOU 5055  OE1AGLU B 267     7914   6005   6650   -639   1570   -816       O  
ATOM   5056  OE1BGLU B 267      59.162 -42.916  20.524  0.43 54.16           O  
ANISOU 5056  OE1BGLU B 267     7934   5905   6739   -631   1351   -748       O  
ATOM   5057  OE2AGLU B 267      61.792 -42.010  20.335  0.57 62.09           O  
ANISOU 5057  OE2AGLU B 267     8750   6871   7971   -434   1585   -774       O  
ATOM   5058  OE2BGLU B 267      58.508 -44.141  22.239  0.43 58.79           O  
ANISOU 5058  OE2BGLU B 267     8454   6409   7474   -550   1259   -647       O  
ATOM   5059  N   ASP B 268      61.989 -37.968  22.227  1.00 41.05           N  
ANISOU 5059  N   ASP B 268     5709   4587   5302   -340   1181   -515       N  
ATOM   5060  CA  ASP B 268      62.072 -36.560  21.837  1.00 38.39           C  
ANISOU 5060  CA  ASP B 268     5359   4331   4898   -386   1155   -496       C  
ATOM   5061  C   ASP B 268      61.814 -36.507  20.332  1.00 42.99           C  
ANISOU 5061  C   ASP B 268     6106   4903   5326   -506   1253   -554       C  
ATOM   5062  O   ASP B 268      62.734 -36.508  19.513  1.00 42.45           O  
ANISOU 5062  O   ASP B 268     6069   4786   5272   -532   1425   -616       O  
ATOM   5063  CB  ASP B 268      63.452 -36.027  22.228  1.00 50.30           C  
ANISOU 5063  CB  ASP B 268     6713   5830   6567   -318   1202   -489       C  
ATOM   5064  CG  ASP B 268      63.650 -34.536  21.966  1.00 50.08           C  
ANISOU 5064  CG  ASP B 268     6666   5867   6495   -369   1180   -466       C  
ATOM   5065  OD1 ASP B 268      62.738 -33.832  21.493  1.00 42.03           O  
ANISOU 5065  OD1 ASP B 268     5749   4892   5326   -440   1122   -442       O  
ATOM   5066  OD2 ASP B 268      64.771 -34.068  22.251  1.00 46.27           O  
ANISOU 5066  OD2 ASP B 268     6050   5377   6152   -337   1215   -465       O  
ATOM   5067  N   PHE B 269      60.527 -36.516  19.951  1.00 37.55           N  
ANISOU 5067  N   PHE B 269     5529   4254   4483   -592   1146   -534       N  
ATOM   5068  CA  PHE B 269      60.258 -36.827  18.545  1.00 38.10           C  
ANISOU 5068  CA  PHE B 269     5796   4300   4380   -728   1218   -595       C  
ATOM   5069  C   PHE B 269      60.437 -35.625  17.623  1.00 36.96           C  
ANISOU 5069  C   PHE B 269     5732   4200   4109   -808   1227   -565       C  
ATOM   5070  O   PHE B 269      60.412 -35.798  16.399  1.00 38.85           O  
ANISOU 5070  O   PHE B 269     6170   4417   4176   -937   1305   -615       O  
ATOM   5071  CB  PHE B 269      58.858 -37.458  18.370  1.00 37.72           C  
ANISOU 5071  CB  PHE B 269     5841   4270   4222   -816   1082   -586       C  
ATOM   5072  CG  PHE B 269      57.731 -36.655  18.969  1.00 35.75           C  
ANISOU 5072  CG  PHE B 269     5493   4113   3976   -803    874   -477       C  
ATOM   5073  CD1 PHE B 269      57.312 -36.883  20.269  1.00 35.85           C  
ANISOU 5073  CD1 PHE B 269     5367   4138   4118   -712    811   -436       C  
ATOM   5074  CD2 PHE B 269      57.086 -35.677  18.222  1.00 38.48           C  
ANISOU 5074  CD2 PHE B 269     5896   4522   4204   -883    753   -409       C  
ATOM   5075  CE1 PHE B 269      56.255 -36.147  20.820  1.00 47.10           C  
ANISOU 5075  CE1 PHE B 269     6698   5632   5566   -698    667   -352       C  
ATOM   5076  CE2 PHE B 269      56.044 -34.932  18.760  1.00 38.55           C  
ANISOU 5076  CE2 PHE B 269     5790   4594   4265   -852    582   -308       C  
ATOM   5077  CZ  PHE B 269      55.625 -35.164  20.060  1.00 40.35           C  
ANISOU 5077  CZ  PHE B 269     5867   4828   4635   -758    557   -290       C  
ATOM   5078  N   ILE B 270      60.655 -34.431  18.170  1.00 36.16           N  
ANISOU 5078  N   ILE B 270     5511   4148   4080   -749   1159   -488       N  
ATOM   5079  CA  ILE B 270      61.088 -33.266  17.400  1.00 38.59           C  
ANISOU 5079  CA  ILE B 270     5885   4470   4308   -813   1202   -454       C  
ATOM   5080  C   ILE B 270      62.360 -32.756  18.067  1.00 42.34           C  
ANISOU 5080  C   ILE B 270     6192   4926   4969   -727   1306   -466       C  
ATOM   5081  O   ILE B 270      62.285 -31.842  18.901  1.00 42.46           O  
ANISOU 5081  O   ILE B 270     6091   4976   5067   -670   1195   -402       O  
ATOM   5082  CB  ILE B 270      60.024 -32.154  17.378  1.00 46.12           C  
ANISOU 5082  CB  ILE B 270     6854   5482   5187   -837    999   -336       C  
ATOM   5083  CG1 ILE B 270      58.659 -32.697  16.966  1.00 49.15           C  
ANISOU 5083  CG1 ILE B 270     7331   5896   5448   -908    841   -306       C  
ATOM   5084  CG2 ILE B 270      60.455 -31.016  16.456  1.00 43.91           C  
ANISOU 5084  CG2 ILE B 270     6686   5193   4806   -919   1044   -286       C  
ATOM   5085  CD1 ILE B 270      57.521 -31.717  17.258  1.00 50.94           C  
ANISOU 5085  CD1 ILE B 270     7486   6169   5698   -883    628   -179       C  
ATOM   5086  N   PRO B 271      63.531 -33.331  17.773  1.00 37.37           N  
ANISOU 5086  N   PRO B 271     5534   4235   4431   -718   1516   -550       N  
ATOM   5087  CA  PRO B 271      64.754 -33.031  18.562  1.00 42.05           C  
ANISOU 5087  CA  PRO B 271     5910   4812   5257   -629   1580   -556       C  
ATOM   5088  C   PRO B 271      65.423 -31.712  18.181  1.00 39.86           C  
ANISOU 5088  C   PRO B 271     5614   4545   4987   -691   1643   -526       C  
ATOM   5089  O   PRO B 271      66.390 -31.642  17.431  1.00 43.71           O  
ANISOU 5089  O   PRO B 271     6109   4987   5513   -744   1859   -577       O  
ATOM   5090  CB  PRO B 271      65.655 -34.233  18.258  1.00 39.89           C  
ANISOU 5090  CB  PRO B 271     5599   4449   5108   -592   1794   -653       C  
ATOM   5091  CG  PRO B 271      65.244 -34.661  16.870  1.00 46.50           C  
ANISOU 5091  CG  PRO B 271     6696   5250   5722   -719   1935   -721       C  
ATOM   5092  CD  PRO B 271      63.737 -34.440  16.823  1.00 44.04           C  
ANISOU 5092  CD  PRO B 271     6525   5009   5198   -780   1700   -653       C  
ATOM   5093  N   MET B 272      64.888 -30.624  18.727  1.00 40.50           N  
ANISOU 5093  N   MET B 272     5673   4673   5043   -687   1469   -444       N  
ATOM   5094  CA  MET B 272      65.458 -29.296  18.540  1.00 41.39           C  
ANISOU 5094  CA  MET B 272     5765   4779   5182   -744   1504   -406       C  
ATOM   5095  C   MET B 272      65.348 -28.529  19.853  1.00 37.44           C  
ANISOU 5095  C   MET B 272     5125   4304   4794   -678   1330   -364       C  
ATOM   5096  O   MET B 272      64.718 -28.982  20.807  1.00 43.24           O  
ANISOU 5096  O   MET B 272     5811   5069   5550   -598   1191   -356       O  
ATOM   5097  CB  MET B 272      64.742 -28.544  17.418  1.00 42.48           C  
ANISOU 5097  CB  MET B 272     6127   4912   5099   -855   1493   -343       C  
ATOM   5098  CG  MET B 272      63.265 -28.315  17.732  1.00 43.82           C  
ANISOU 5098  CG  MET B 272     6357   5120   5172   -822   1261   -264       C  
ATOM   5099  SD  MET B 272      62.408 -27.586  16.336  1.00 54.49           S  
ANISOU 5099  SD  MET B 272     7964   6461   6279   -947   1200   -160       S  
ATOM   5100  CE  MET B 272      63.036 -25.904  16.386  1.00 54.20           C  
ANISOU 5100  CE  MET B 272     7908   6369   6315   -975   1231    -85       C  
ATOM   5101  N   ASP B 273      65.986 -27.360  19.898  1.00 34.87           N  
ANISOU 5101  N   ASP B 273     4757   3959   4535   -728   1356   -343       N  
ATOM   5102  CA  ASP B 273      65.908 -26.482  21.060  1.00 42.25           C  
ANISOU 5102  CA  ASP B 273     5602   4898   5551   -697   1209   -319       C  
ATOM   5103  C   ASP B 273      64.604 -25.692  20.991  1.00 34.67           C  
ANISOU 5103  C   ASP B 273     4780   3929   4464   -695   1094   -250       C  
ATOM   5104  O   ASP B 273      64.330 -25.047  19.973  1.00 41.88           O  
ANISOU 5104  O   ASP B 273     5828   4808   5277   -763   1135   -194       O  
ATOM   5105  CB  ASP B 273      67.104 -25.527  21.070  1.00 42.80           C  
ANISOU 5105  CB  ASP B 273     5577   4932   5752   -773   1289   -331       C  
ATOM   5106  CG  ASP B 273      67.402 -24.957  22.451  1.00 49.01           C  
ANISOU 5106  CG  ASP B 273     6240   5726   6656   -753   1143   -345       C  
ATOM   5107  OD1 ASP B 273      67.035 -25.607  23.456  1.00 44.60           O  
ANISOU 5107  OD1 ASP B 273     5634   5209   6104   -672   1014   -357       O  
ATOM   5108  OD2 ASP B 273      68.019 -23.860  22.527  1.00 41.54           O  
ANISOU 5108  OD2 ASP B 273     5262   4738   5784   -836   1162   -346       O  
ATOM   5109  N   SER B 274      63.798 -25.749  22.050  1.00 40.07           N  
ANISOU 5109  N   SER B 274     5432   4635   5159   -618    956   -246       N  
ATOM   5110  CA  SER B 274      62.577 -24.947  22.057  1.00 41.87           C  
ANISOU 5110  CA  SER B 274     5747   4836   5327   -598    866   -182       C  
ATOM   5111  C   SER B 274      62.119 -24.681  23.483  1.00 35.91           C  
ANISOU 5111  C   SER B 274     4933   4080   4633   -531    777   -210       C  
ATOM   5112  O   SER B 274      62.412 -25.446  24.407  1.00 38.95           O  
ANISOU 5112  O   SER B 274     5243   4507   5048   -496    749   -260       O  
ATOM   5113  CB  SER B 274      61.448 -25.606  21.245  1.00 47.27           C  
ANISOU 5113  CB  SER B 274     6521   5547   5891   -589    823   -132       C  
ATOM   5114  OG  SER B 274      61.144 -26.901  21.716  1.00 49.08           O  
ANISOU 5114  OG  SER B 274     6703   5830   6117   -541    800   -176       O  
ATOM   5115  N   THR B 275      61.393 -23.569  23.646  1.00 34.04           N  
ANISOU 5115  N   THR B 275     4744   3780   4410   -515    742   -171       N  
ATOM   5116  CA  THR B 275      60.920 -23.178  24.970  1.00 30.81           C  
ANISOU 5116  CA  THR B 275     4312   3346   4048   -464    702   -215       C  
ATOM   5117  C   THR B 275      60.034 -24.255  25.591  1.00 36.22           C  
ANISOU 5117  C   THR B 275     4968   4094   4700   -397    664   -227       C  
ATOM   5118  O   THR B 275      60.145 -24.547  26.788  1.00 37.58           O  
ANISOU 5118  O   THR B 275     5120   4286   4871   -382    650   -286       O  
ATOM   5119  CB  THR B 275      60.177 -21.842  24.870  1.00 33.90           C  
ANISOU 5119  CB  THR B 275     4762   3630   4488   -442    703   -169       C  
ATOM   5120  OG1 THR B 275      61.099 -20.827  24.465  1.00 37.76           O  
ANISOU 5120  OG1 THR B 275     5290   4045   5011   -521    746   -164       O  
ATOM   5121  CG2 THR B 275      59.551 -21.456  26.200  1.00 34.76           C  
ANISOU 5121  CG2 THR B 275     4869   3696   4642   -388    707   -233       C  
ATOM   5122  N   VAL B 276      59.149 -24.852  24.799  1.00 34.57           N  
ANISOU 5122  N   VAL B 276     4768   3915   4454   -374    642   -169       N  
ATOM   5123  CA  VAL B 276      58.329 -25.983  25.229  1.00 34.98           C  
ANISOU 5123  CA  VAL B 276     4787   4022   4482   -334    617   -176       C  
ATOM   5124  C   VAL B 276      58.840 -27.216  24.494  1.00 32.81           C  
ANISOU 5124  C   VAL B 276     4521   3801   4146   -370    627   -183       C  
ATOM   5125  O   VAL B 276      59.020 -27.183  23.271  1.00 36.77           O  
ANISOU 5125  O   VAL B 276     5075   4299   4597   -420    639   -149       O  
ATOM   5126  CB  VAL B 276      56.831 -25.759  24.942  1.00 39.80           C  
ANISOU 5126  CB  VAL B 276     5380   4615   5128   -292    575   -110       C  
ATOM   5127  CG1 VAL B 276      56.017 -27.008  25.331  1.00 39.74           C  
ANISOU 5127  CG1 VAL B 276     5327   4665   5106   -275    562   -120       C  
ATOM   5128  CG2 VAL B 276      56.303 -24.541  25.669  1.00 39.44           C  
ANISOU 5128  CG2 VAL B 276     5318   4486   5180   -238    604   -113       C  
ATOM   5129  N   LYS B 277      59.082 -28.293  25.234  1.00 35.36           N  
ANISOU 5129  N   LYS B 277     4811   4158   4465   -350    632   -225       N  
ATOM   5130  CA  LYS B 277      59.528 -29.555  24.655  1.00 40.38           C  
ANISOU 5130  CA  LYS B 277     5455   4815   5072   -368    662   -242       C  
ATOM   5131  C   LYS B 277      58.398 -30.573  24.753  1.00 40.44           C  
ANISOU 5131  C   LYS B 277     5475   4844   5048   -358    632   -230       C  
ATOM   5132  O   LYS B 277      57.639 -30.574  25.722  1.00 39.68           O  
ANISOU 5132  O   LYS B 277     5352   4754   4971   -325    608   -223       O  
ATOM   5133  CB  LYS B 277      60.780 -30.090  25.365  1.00 37.70           C  
ANISOU 5133  CB  LYS B 277     5057   4475   4792   -347    682   -282       C  
ATOM   5134  CG  LYS B 277      62.059 -29.334  25.046  1.00 42.35           C  
ANISOU 5134  CG  LYS B 277     5602   5046   5443   -379    724   -299       C  
ATOM   5135  CD  LYS B 277      62.419 -29.476  23.562  1.00 38.79           C  
ANISOU 5135  CD  LYS B 277     5195   4578   4964   -431    828   -304       C  
ATOM   5136  CE  LYS B 277      62.582 -30.951  23.160  1.00 40.02           C  
ANISOU 5136  CE  LYS B 277     5360   4726   5120   -415    893   -335       C  
ATOM   5137  NZ  LYS B 277      63.075 -31.085  21.748  1.00 41.15           N  
ANISOU 5137  NZ  LYS B 277     5574   4840   5220   -482   1034   -365       N  
ATOM   5138  N   ASN B 278      58.278 -31.429  23.743  1.00 39.59           N  
ANISOU 5138  N   ASN B 278     5419   4738   4887   -404    651   -235       N  
ATOM   5139  CA  ASN B 278      57.200 -32.404  23.689  1.00 41.89           C  
ANISOU 5139  CA  ASN B 278     5725   5041   5150   -424    616   -227       C  
ATOM   5140  C   ASN B 278      57.787 -33.799  23.618  1.00 35.80           C  
ANISOU 5140  C   ASN B 278     4988   4240   4374   -432    679   -277       C  
ATOM   5141  O   ASN B 278      58.623 -34.080  22.750  1.00 37.39           O  
ANISOU 5141  O   ASN B 278     5242   4414   4551   -461    754   -317       O  
ATOM   5142  CB  ASN B 278      56.288 -32.137  22.502  1.00 36.09           C  
ANISOU 5142  CB  ASN B 278     5041   4322   4349   -496    547   -183       C  
ATOM   5143  CG  ASN B 278      55.707 -30.745  22.556  1.00 59.89           C  
ANISOU 5143  CG  ASN B 278     8008   7338   7408   -467    481   -114       C  
ATOM   5144  OD1 ASN B 278      54.686 -30.519  23.189  1.00 49.75           O  
ANISOU 5144  OD1 ASN B 278     6642   6060   6202   -428    438    -81       O  
ATOM   5145  ND2 ASN B 278      56.396 -29.790  21.937  1.00 67.50           N  
ANISOU 5145  ND2 ASN B 278     9022   8281   8343   -482    496    -93       N  
ATOM   5146  N   TYR B 279      57.329 -34.667  24.516  1.00 35.10           N  
ANISOU 5146  N   TYR B 279     4879   4143   4316   -406    669   -275       N  
ATOM   5147  CA  TYR B 279      57.847 -36.022  24.629  1.00 33.22           C  
ANISOU 5147  CA  TYR B 279     4673   3849   4102   -395    726   -308       C  
ATOM   5148  C   TYR B 279      56.714 -37.027  24.551  1.00 36.93           C  
ANISOU 5148  C   TYR B 279     5186   4302   4543   -453    710   -308       C  
ATOM   5149  O   TYR B 279      55.615 -36.794  25.069  1.00 36.29           O  
ANISOU 5149  O   TYR B 279     5065   4258   4466   -470    659   -270       O  
ATOM   5150  CB  TYR B 279      58.589 -36.230  25.949  1.00 32.95           C  
ANISOU 5150  CB  TYR B 279     4586   3795   4137   -314    717   -286       C  
ATOM   5151  CG  TYR B 279      59.739 -35.277  26.145  1.00 33.40           C  
ANISOU 5151  CG  TYR B 279     4580   3869   4241   -274    710   -287       C  
ATOM   5152  CD1 TYR B 279      60.916 -35.413  25.406  1.00 38.21           C  
ANISOU 5152  CD1 TYR B 279     5160   4442   4916   -263    782   -321       C  
ATOM   5153  CD2 TYR B 279      59.655 -34.240  27.070  1.00 39.65           C  
ANISOU 5153  CD2 TYR B 279     5342   4702   5022   -260    648   -265       C  
ATOM   5154  CE1 TYR B 279      61.983 -34.534  25.585  1.00 37.26           C  
ANISOU 5154  CE1 TYR B 279     4955   4336   4865   -244    776   -321       C  
ATOM   5155  CE2 TYR B 279      60.715 -33.354  27.252  1.00 40.78           C  
ANISOU 5155  CE2 TYR B 279     5429   4854   5212   -249    629   -272       C  
ATOM   5156  CZ  TYR B 279      61.866 -33.510  26.510  1.00 40.02           C  
ANISOU 5156  CZ  TYR B 279     5280   4732   5196   -243    684   -295       C  
ATOM   5157  OH  TYR B 279      62.900 -32.637  26.695  1.00 44.40           O  
ANISOU 5157  OH  TYR B 279     5756   5295   5820   -248    666   -300       O  
ATOM   5158  N   PHE B 280      57.006 -38.147  23.903  1.00 35.65           N  
ANISOU 5158  N   PHE B 280     5103   4072   4372   -490    774   -357       N  
ATOM   5159  CA  PHE B 280      56.213 -39.367  24.007  1.00 36.05           C  
ANISOU 5159  CA  PHE B 280     5205   4072   4420   -545    779   -368       C  
ATOM   5160  C   PHE B 280      56.771 -40.117  25.214  1.00 37.64           C  
ANISOU 5160  C   PHE B 280     5387   4207   4706   -456    812   -337       C  
ATOM   5161  O   PHE B 280      57.868 -40.684  25.146  1.00 37.83           O  
ANISOU 5161  O   PHE B 280     5425   4150   4797   -394    879   -359       O  
ATOM   5162  CB  PHE B 280      56.330 -40.161  22.704  1.00 35.23           C  
ANISOU 5162  CB  PHE B 280     5228   3903   4254   -637    841   -450       C  
ATOM   5163  CG  PHE B 280      55.374 -41.330  22.572  1.00 35.41           C  
ANISOU 5163  CG  PHE B 280     5324   3871   4260   -739    832   -476       C  
ATOM   5164  CD1 PHE B 280      54.922 -42.035  23.679  1.00 37.50           C  
ANISOU 5164  CD1 PHE B 280     5553   4096   4601   -713    831   -431       C  
ATOM   5165  CD2 PHE B 280      54.950 -41.733  21.318  1.00 41.24           C  
ANISOU 5165  CD2 PHE B 280     6190   4588   4890   -883    826   -546       C  
ATOM   5166  CE1 PHE B 280      54.053 -43.128  23.540  1.00 40.17           C  
ANISOU 5166  CE1 PHE B 280     5958   4369   4935   -825    834   -456       C  
ATOM   5167  CE2 PHE B 280      54.086 -42.809  21.162  1.00 45.51           C  
ANISOU 5167  CE2 PHE B 280     6803   5071   5417  -1002    809   -580       C  
ATOM   5168  CZ  PHE B 280      53.635 -43.510  22.277  1.00 44.55           C  
ANISOU 5168  CZ  PHE B 280     6623   4905   5401   -972    818   -536       C  
ATOM   5169  N   ILE B 281      56.041 -40.098  26.327  1.00 36.29           N  
ANISOU 5169  N   ILE B 281     5184   4063   4541   -449    770   -278       N  
ATOM   5170  CA  ILE B 281      56.558 -40.583  27.602  1.00 36.28           C  
ANISOU 5170  CA  ILE B 281     5189   4015   4580   -375    770   -221       C  
ATOM   5171  C   ILE B 281      55.922 -41.923  27.951  1.00 41.36           C  
ANISOU 5171  C   ILE B 281     5908   4570   5238   -421    807   -200       C  
ATOM   5172  O   ILE B 281      54.710 -42.107  27.791  1.00 36.17           O  
ANISOU 5172  O   ILE B 281     5256   3933   4555   -518    814   -209       O  
ATOM   5173  CB  ILE B 281      56.330 -39.557  28.728  1.00 37.83           C  
ANISOU 5173  CB  ILE B 281     5343   4293   4739   -347    722   -174       C  
ATOM   5174  CG1 ILE B 281      56.778 -40.134  30.063  1.00 39.89           C  
ANISOU 5174  CG1 ILE B 281     5656   4507   4994   -302    699   -103       C  
ATOM   5175  CG2 ILE B 281      54.869 -39.141  28.795  1.00 42.89           C  
ANISOU 5175  CG2 ILE B 281     5956   4990   5352   -418    734   -173       C  
ATOM   5176  CD1 ILE B 281      56.789 -39.129  31.191  1.00 45.93           C  
ANISOU 5176  CD1 ILE B 281     6423   5340   5688   -289    657    -75       C  
ATOM   5177  N   THR B 282      56.750 -42.854  28.433  1.00 35.53           N  
ANISOU 5177  N   THR B 282     5216   3723   4561   -354    824   -163       N  
ATOM   5178  CA  THR B 282      56.308 -44.157  28.926  1.00 35.36           C  
ANISOU 5178  CA  THR B 282     5286   3586   4563   -386    860   -121       C  
ATOM   5179  C   THR B 282      56.915 -44.386  30.305  1.00 41.52           C  
ANISOU 5179  C   THR B 282     6096   4328   5352   -303    804     -6       C  
ATOM   5180  O   THR B 282      58.144 -44.443  30.444  1.00 40.38           O  
ANISOU 5180  O   THR B 282     5915   4138   5287   -194    758     28       O  
ATOM   5181  CB  THR B 282      56.721 -45.293  27.980  1.00 35.53           C  
ANISOU 5181  CB  THR B 282     5374   3459   4666   -390    942   -185       C  
ATOM   5182  OG1 THR B 282      56.248 -45.018  26.657  1.00 38.63           O  
ANISOU 5182  OG1 THR B 282     5776   3896   5008   -488    975   -294       O  
ATOM   5183  CG2 THR B 282      56.126 -46.613  28.465  1.00 37.32           C  
ANISOU 5183  CG2 THR B 282     5710   3551   4921   -443    984   -142       C  
ATOM   5184  N   ASP B 283      56.061 -44.529  31.316  1.00 39.09           N  
ANISOU 5184  N   ASP B 283     5852   4035   4965   -362    805     60       N  
ATOM   5185  CA  ASP B 283      56.513 -44.772  32.684  1.00 38.37           C  
ANISOU 5185  CA  ASP B 283     5842   3910   4828   -316    740    183       C  
ATOM   5186  C   ASP B 283      56.823 -46.251  32.881  1.00 46.10           C  
ANISOU 5186  C   ASP B 283     6920   4707   5888   -288    752    262       C  
ATOM   5187  O   ASP B 283      55.950 -47.110  32.694  1.00 44.33           O  
ANISOU 5187  O   ASP B 283     6769   4401   5673   -377    844    251       O  
ATOM   5188  CB  ASP B 283      55.459 -44.317  33.688  1.00 40.96           C  
ANISOU 5188  CB  ASP B 283     6230   4314   5017   -406    776    214       C  
ATOM   5189  CG  ASP B 283      55.930 -44.464  35.115  1.00 49.44           C  
ANISOU 5189  CG  ASP B 283     7435   5364   5984   -386    701    339       C  
ATOM   5190  OD1 ASP B 283      56.893 -43.764  35.493  1.00 51.12           O  
ANISOU 5190  OD1 ASP B 283     7624   5631   6169   -319    579    363       O  
ATOM   5191  OD2 ASP B 283      55.350 -45.276  35.858  1.00 47.82           O  
ANISOU 5191  OD2 ASP B 283     7368   5086   5718   -452    755    419       O  
ATOM   5192  N   ALA B 284      58.055 -46.551  33.294  1.00 44.77           N  
ANISOU 5192  N   ALA B 284     6747   4465   5798   -168    652    351       N  
ATOM   5193  CA  ALA B 284      58.488 -47.944  33.326  1.00 44.73           C  
ANISOU 5193  CA  ALA B 284     6815   4256   5925   -108    664    429       C  
ATOM   5194  C   ALA B 284      57.840 -48.724  34.468  1.00 49.41           C  
ANISOU 5194  C   ALA B 284     7587   4768   6420   -175    657    565       C  
ATOM   5195  O   ALA B 284      57.631 -49.934  34.346  1.00 48.46           O  
ANISOU 5195  O   ALA B 284     7561   4469   6384   -186    726    602       O  
ATOM   5196  CB  ALA B 284      60.013 -48.020  33.419  1.00 47.28           C  
ANISOU 5196  CB  ALA B 284     7040   4514   6410     56    549    502       C  
ATOM   5197  N   GLN B 285      57.501 -48.059  35.574  1.00 45.57           N  
ANISOU 5197  N   GLN B 285     7171   4397   5747   -232    594    635       N  
ATOM   5198  CA  GLN B 285      56.966 -48.783  36.725  1.00 47.93           C  
ANISOU 5198  CA  GLN B 285     7672   4616   5924   -307    600    777       C  
ATOM   5199  C   GLN B 285      55.501 -49.161  36.531  1.00 45.61           C  
ANISOU 5199  C   GLN B 285     7437   4309   5584   -463    791    710       C  
ATOM   5200  O   GLN B 285      55.094 -50.273  36.890  1.00 51.76           O  
ANISOU 5200  O   GLN B 285     8358   4936   6372   -521    853    798       O  
ATOM   5201  CB  GLN B 285      57.132 -47.951  38.001  1.00 49.57           C  
ANISOU 5201  CB  GLN B 285     7974   4942   5917   -337    486    863       C  
ATOM   5202  CG  GLN B 285      56.619 -48.646  39.261  1.00 58.23           C  
ANISOU 5202  CG  GLN B 285     9324   5960   6840   -434    500   1019       C  
ATOM   5203  CD  GLN B 285      57.338 -49.955  39.549  1.00 64.60           C  
ANISOU 5203  CD  GLN B 285    10234   6558   7754   -351    389   1202       C  
ATOM   5204  OE1 GLN B 285      58.565 -50.011  39.555  1.00 66.97           O  
ANISOU 5204  OE1 GLN B 285    10459   6818   8171   -210    195   1285       O  
ATOM   5205  NE2 GLN B 285      56.570 -51.018  39.782  1.00 67.51           N  
ANISOU 5205  NE2 GLN B 285    10762   6781   8110   -438    515   1271       N  
ATOM   5206  N   THR B 286      54.698 -48.266  35.956  1.00 42.94           N  
ANISOU 5206  N   THR B 286     6979   4118   5218   -535    879    567       N  
ATOM   5207  CA  THR B 286      53.257 -48.491  35.879  1.00 43.66           C  
ANISOU 5207  CA  THR B 286     7082   4219   5287   -691   1041    516       C  
ATOM   5208  C   THR B 286      52.767 -48.881  34.493  1.00 43.51           C  
ANISOU 5208  C   THR B 286     6955   4166   5412   -740   1103    389       C  
ATOM   5209  O   THR B 286      51.755 -49.587  34.382  1.00 46.00           O  
ANISOU 5209  O   THR B 286     7302   4417   5759   -875   1210    376       O  
ATOM   5210  CB  THR B 286      52.507 -47.232  36.321  1.00 47.27           C  
ANISOU 5210  CB  THR B 286     7477   4853   5631   -751   1101    459       C  
ATOM   5211  OG1 THR B 286      52.770 -46.181  35.383  1.00 44.54           O  
ANISOU 5211  OG1 THR B 286     6952   4626   5344   -687   1046    343       O  
ATOM   5212  CG2 THR B 286      52.963 -46.796  37.706  1.00 47.25           C  
ANISOU 5212  CG2 THR B 286     7626   4885   5442   -735   1048    562       C  
ATOM   5213  N   GLY B 287      53.454 -48.449  33.434  1.00 43.87           N  
ANISOU 5213  N   GLY B 287     6886   4250   5534   -655   1040    296       N  
ATOM   5214  CA  GLY B 287      52.921 -48.579  32.094  1.00 37.53           C  
ANISOU 5214  CA  GLY B 287     6002   3450   4809   -730   1084    164       C  
ATOM   5215  C   GLY B 287      52.019 -47.442  31.666  1.00 43.35           C  
ANISOU 5215  C   GLY B 287     6594   4365   5510   -801   1087     83       C  
ATOM   5216  O   GLY B 287      51.486 -47.478  30.547  1.00 48.27           O  
ANISOU 5216  O   GLY B 287     7154   5008   6179   -882   1088    -13       O  
ATOM   5217  N   SER B 288      51.816 -46.442  32.521  1.00 39.71           N  
ANISOU 5217  N   SER B 288     6091   4025   4972   -777   1083    120       N  
ATOM   5218  CA  SER B 288      51.156 -45.216  32.095  1.00 44.26           C  
ANISOU 5218  CA  SER B 288     6514   4753   5550   -799   1078     51       C  
ATOM   5219  C   SER B 288      52.003 -44.520  31.032  1.00 44.76           C  
ANISOU 5219  C   SER B 288     6506   4870   5631   -715    984    -17       C  
ATOM   5220  O   SER B 288      53.233 -44.461  31.146  1.00 44.83           O  
ANISOU 5220  O   SER B 288     6555   4849   5627   -606    932      3       O  
ATOM   5221  CB  SER B 288      50.944 -44.307  33.305  1.00 44.43           C  
ANISOU 5221  CB  SER B 288     6540   4857   5486   -776   1122     93       C  
ATOM   5222  OG  SER B 288      49.973 -43.315  33.038  1.00 45.79           O  
ANISOU 5222  OG  SER B 288     6558   5136   5705   -813   1164     38       O  
ATOM   5223  N   SER B 289      51.352 -44.015  29.977  1.00 39.84           N  
ANISOU 5223  N   SER B 289     5774   4319   5044   -774    958    -88       N  
ATOM   5224  CA  SER B 289      52.078 -43.384  28.873  1.00 41.52           C  
ANISOU 5224  CA  SER B 289     5950   4575   5252   -721    886   -148       C  
ATOM   5225  C   SER B 289      51.228 -42.280  28.253  1.00 38.40           C  
ANISOU 5225  C   SER B 289     5423   4299   4868   -763    835   -174       C  
ATOM   5226  O   SER B 289      50.025 -42.182  28.508  1.00 37.50           O  
ANISOU 5226  O   SER B 289     5221   4221   4805   -838    855   -155       O  
ATOM   5227  CB  SER B 289      52.480 -44.407  27.798  1.00 38.13           C  
ANISOU 5227  CB  SER B 289     5607   4041   4840   -765    893   -210       C  
ATOM   5228  OG  SER B 289      51.332 -44.945  27.145  1.00 40.48           O  
ANISOU 5228  OG  SER B 289     5900   4329   5153   -920    887   -250       O  
ATOM   5229  N   LYS B 290      51.868 -41.449  27.422  1.00 37.34           N  
ANISOU 5229  N   LYS B 290     5266   4215   4707   -714    774   -207       N  
ATOM   5230  CA  LYS B 290      51.179 -40.344  26.753  1.00 40.58           C  
ANISOU 5230  CA  LYS B 290     5566   4721   5131   -739    701   -208       C  
ATOM   5231  C   LYS B 290      51.983 -39.932  25.527  1.00 40.67           C  
ANISOU 5231  C   LYS B 290     5627   4746   5082   -730    645   -250       C  
ATOM   5232  O   LYS B 290      53.196 -39.729  25.632  1.00 37.64           O  
ANISOU 5232  O   LYS B 290     5290   4340   4673   -644    680   -264       O  
ATOM   5233  CB  LYS B 290      51.000 -39.154  27.705  1.00 37.44           C  
ANISOU 5233  CB  LYS B 290     5079   4383   4762   -656    726   -171       C  
ATOM   5234  CG  LYS B 290      50.376 -37.929  27.044  1.00 41.31           C  
ANISOU 5234  CG  LYS B 290     5450   4945   5302   -652    653   -157       C  
ATOM   5235  CD  LYS B 290      49.647 -37.029  28.058  1.00 41.85           C  
ANISOU 5235  CD  LYS B 290     5409   5039   5454   -600    723   -130       C  
ATOM   5236  CE  LYS B 290      50.609 -36.392  29.055  1.00 45.48           C  
ANISOU 5236  CE  LYS B 290     5945   5489   5846   -507    787   -144       C  
ATOM   5237  NZ  LYS B 290      49.856 -35.734  30.174  1.00 46.90           N  
ANISOU 5237  NZ  LYS B 290     6070   5669   6080   -481    903   -143       N  
ATOM   5238  N  ACYS B 291      51.306 -39.793  24.373  0.76 36.34           N  
ANISOU 5238  N  ACYS B 291     5067   4232   4507   -831    555   -262       N  
ATOM   5239  N  BCYS B 291      51.302 -39.791  24.384  0.24 37.66           N  
ANISOU 5239  N  BCYS B 291     5233   4399   4675   -830    555   -261       N  
ATOM   5240  CA ACYS B 291      52.017 -39.548  23.114  0.76 36.48           C  
ANISOU 5240  CA ACYS B 291     5184   4251   4426   -859    522   -304       C  
ATOM   5241  CA BCYS B 291      52.004 -39.560  23.124  0.24 38.37           C  
ANISOU 5241  CA BCYS B 291     5423   4490   4666   -860    522   -304       C  
ATOM   5242  C  ACYS B 291      52.583 -38.139  23.043  0.76 41.29           C  
ANISOU 5242  C  ACYS B 291     5748   4916   5024   -769    500   -271       C  
ATOM   5243  C  BCYS B 291      52.577 -38.151  23.045  0.24 39.80           C  
ANISOU 5243  C  BCYS B 291     5558   4727   4835   -769    500   -271       C  
ATOM   5244  O  ACYS B 291      53.679 -37.928  22.509  0.76 35.80           O  
ANISOU 5244  O  ACYS B 291     5133   4201   4269   -742    548   -307       O  
ATOM   5245  O  BCYS B 291      53.690 -37.956  22.544  0.24 38.67           O  
ANISOU 5245  O  BCYS B 291     5496   4563   4635   -740    551   -308       O  
ATOM   5246  CB ACYS B 291      51.097 -39.769  21.916  0.76 39.00           C  
ANISOU 5246  CB ACYS B 291     5540   4596   4684  -1019    400   -314       C  
ATOM   5247  CB BCYS B 291      51.067 -39.821  21.947  0.24 41.76           C  
ANISOU 5247  CB BCYS B 291     5887   4942   5036  -1021    402   -314       C  
ATOM   5248  SG ACYS B 291      50.405 -41.422  21.760  0.76 42.84           S  
ANISOU 5248  SG ACYS B 291     6106   5002   5171  -1175    412   -373       S  
ATOM   5249  SG BCYS B 291      49.500 -38.927  22.029  0.24 52.14           S  
ANISOU 5249  SG BCYS B 291     6997   6355   6460  -1055    240   -212       S  
ATOM   5250  N   VAL B 292      51.834 -37.153  23.506  1.00 36.49           N  
ANISOU 5250  N   VAL B 292     5011   4366   4489   -729    443   -206       N  
ATOM   5251  CA  VAL B 292      52.294 -35.765  23.482  1.00 38.43           C  
ANISOU 5251  CA  VAL B 292     5220   4642   4739   -648    427   -173       C  
ATOM   5252  C   VAL B 292      52.207 -35.247  24.910  1.00 40.93           C  
ANISOU 5252  C   VAL B 292     5448   4960   5145   -549    494   -156       C  
ATOM   5253  O   VAL B 292      51.116 -34.923  25.402  1.00 37.85           O  
ANISOU 5253  O   VAL B 292     4946   4587   4848   -542    487   -120       O  
ATOM   5254  CB  VAL B 292      51.494 -34.886  22.519  1.00 40.88           C  
ANISOU 5254  CB  VAL B 292     5487   4995   5051   -694    289   -107       C  
ATOM   5255  CG1 VAL B 292      52.100 -33.482  22.502  1.00 37.29           C  
ANISOU 5255  CG1 VAL B 292     5023   4542   4604   -610    294    -73       C  
ATOM   5256  CG2 VAL B 292      51.511 -35.485  21.110  1.00 40.66           C  
ANISOU 5256  CG2 VAL B 292     5596   4969   4885   -829    210   -127       C  
ATOM   5257  N   CYS B 293      53.349 -35.189  25.585  1.00 33.04           N  
ANISOU 5257  N   CYS B 293     4496   3937   4119   -482    564   -186       N  
ATOM   5258  CA  CYS B 293      53.448 -34.607  26.920  1.00 33.93           C  
ANISOU 5258  CA  CYS B 293     4576   4050   4266   -410    617   -181       C  
ATOM   5259  C   CYS B 293      54.328 -33.366  26.814  1.00 40.54           C  
ANISOU 5259  C   CYS B 293     5416   4891   5095   -360    606   -188       C  
ATOM   5260  O   CYS B 293      55.550 -33.475  26.662  1.00 36.54           O  
ANISOU 5260  O   CYS B 293     4955   4373   4557   -347    613   -212       O  
ATOM   5261  CB  CYS B 293      54.019 -35.604  27.917  1.00 36.23           C  
ANISOU 5261  CB  CYS B 293     4930   4308   4527   -395    668   -193       C  
ATOM   5262  SG  CYS B 293      53.927 -35.029  29.621  1.00 44.06           S  
ANISOU 5262  SG  CYS B 293     5936   5302   5502   -353    726   -187       S  
ATOM   5263  N   SER B 294      53.701 -32.196  26.889  1.00 41.15           N  
ANISOU 5263  N   SER B 294     5435   4972   5228   -333    598   -165       N  
ATOM   5264  CA  SER B 294      54.415 -30.927  26.789  1.00 38.24           C  
ANISOU 5264  CA  SER B 294     5078   4586   4863   -298    594   -169       C  
ATOM   5265  C   SER B 294      55.047 -30.568  28.127  1.00 35.93           C  
ANISOU 5265  C   SER B 294     4819   4278   4555   -265    648   -214       C  
ATOM   5266  O   SER B 294      54.379 -30.582  29.163  1.00 38.82           O  
ANISOU 5266  O   SER B 294     5184   4636   4932   -252    707   -228       O  
ATOM   5267  CB  SER B 294      53.459 -29.826  26.348  1.00 41.60           C  
ANISOU 5267  CB  SER B 294     5436   4993   5376   -275    562   -119       C  
ATOM   5268  OG  SER B 294      53.012 -30.048  25.017  1.00 45.34           O  
ANISOU 5268  OG  SER B 294     5903   5488   5836   -325    465    -62       O  
ATOM   5269  N   VAL B 295      56.336 -30.240  28.107  1.00 36.77           N  
ANISOU 5269  N   VAL B 295     4960   4380   4632   -267    631   -237       N  
ATOM   5270  CA  VAL B 295      57.114 -30.042  29.323  1.00 34.86           C  
ANISOU 5270  CA  VAL B 295     4759   4130   4355   -263    634   -274       C  
ATOM   5271  C   VAL B 295      57.850 -28.721  29.215  1.00 34.82           C  
ANISOU 5271  C   VAL B 295     4758   4099   4374   -272    624   -298       C  
ATOM   5272  O   VAL B 295      58.502 -28.446  28.200  1.00 35.20           O  
ANISOU 5272  O   VAL B 295     4782   4144   4450   -287    610   -285       O  
ATOM   5273  CB  VAL B 295      58.118 -31.190  29.561  1.00 37.70           C  
ANISOU 5273  CB  VAL B 295     5130   4505   4688   -267    593   -268       C  
ATOM   5274  CG1 VAL B 295      58.974 -30.892  30.792  1.00 40.15           C  
ANISOU 5274  CG1 VAL B 295     5482   4816   4959   -277    542   -286       C  
ATOM   5275  CG2 VAL B 295      57.386 -32.519  29.747  1.00 35.80           C  
ANISOU 5275  CG2 VAL B 295     4910   4268   4427   -267    612   -243       C  
ATOM   5276  N   ILE B 296      57.767 -27.913  30.261  1.00 34.71           N  
ANISOU 5276  N   ILE B 296     4792   4054   4340   -277    648   -341       N  
ATOM   5277  CA  ILE B 296      58.486 -26.643  30.290  1.00 36.86           C  
ANISOU 5277  CA  ILE B 296     5085   4283   4636   -304    640   -377       C  
ATOM   5278  C   ILE B 296      59.321 -26.586  31.565  1.00 36.59           C  
ANISOU 5278  C   ILE B 296     5120   4255   4526   -355    592   -430       C  
ATOM   5279  O   ILE B 296      58.897 -27.093  32.609  1.00 42.19           O  
ANISOU 5279  O   ILE B 296     5903   4979   5149   -362    604   -446       O  
ATOM   5280  CB  ILE B 296      57.506 -25.449  30.178  1.00 36.78           C  
ANISOU 5280  CB  ILE B 296     5087   4196   4693   -272    716   -386       C  
ATOM   5281  CG1 ILE B 296      58.274 -24.142  29.933  1.00 36.66           C  
ANISOU 5281  CG1 ILE B 296     5099   4112   4718   -307    713   -410       C  
ATOM   5282  CG2 ILE B 296      56.594 -25.370  31.409  1.00 37.91           C  
ANISOU 5282  CG2 ILE B 296     5287   4309   4809   -256    808   -438       C  
ATOM   5283  CD1 ILE B 296      57.371 -22.976  29.535  1.00 38.16           C  
ANISOU 5283  CD1 ILE B 296     5290   4198   5011   -258    779   -390       C  
ATOM   5284  N   ASP B 297      60.517 -25.992  31.479  1.00 37.12           N  
ANISOU 5284  N   ASP B 297     5170   4315   4620   -407    530   -451       N  
ATOM   5285  CA  ASP B 297      61.380 -25.845  32.654  1.00 40.14           C  
ANISOU 5285  CA  ASP B 297     5611   4707   4932   -480    437   -494       C  
ATOM   5286  C   ASP B 297      61.348 -24.395  33.137  1.00 40.36           C  
ANISOU 5286  C   ASP B 297     5733   4656   4944   -542    477   -577       C  
ATOM   5287  O   ASP B 297      62.262 -23.604  32.901  1.00 38.17           O  
ANISOU 5287  O   ASP B 297     5427   4351   4724   -607    433   -602       O  
ATOM   5288  CB  ASP B 297      62.818 -26.297  32.356  1.00 38.59           C  
ANISOU 5288  CB  ASP B 297     5301   4554   4808   -508    321   -460       C  
ATOM   5289  CG  ASP B 297      63.716 -26.225  33.601  1.00 50.20           C  
ANISOU 5289  CG  ASP B 297     6814   6045   6214   -593    167   -482       C  
ATOM   5290  OD1 ASP B 297      63.177 -26.245  34.730  1.00 49.74           O  
ANISOU 5290  OD1 ASP B 297     6910   5984   6004   -626    150   -512       O  
ATOM   5291  OD2 ASP B 297      64.956 -26.126  33.448  1.00 55.53           O  
ANISOU 5291  OD2 ASP B 297     7374   6738   6988   -638     64   -469       O  
ATOM   5292  N   LEU B 298      60.277 -24.052  33.837  1.00 42.59           N  
ANISOU 5292  N   LEU B 298     6131   4890   5161   -527    581   -628       N  
ATOM   5293  CA  LEU B 298      60.193 -22.787  34.548  1.00 43.86           C  
ANISOU 5293  CA  LEU B 298     6423   4955   5286   -591    644   -731       C  
ATOM   5294  C   LEU B 298      60.674 -22.977  35.976  1.00 42.81           C  
ANISOU 5294  C   LEU B 298     6448   4849   4970   -700    562   -795       C  
ATOM   5295  O   LEU B 298      60.528 -24.055  36.556  1.00 44.26           O  
ANISOU 5295  O   LEU B 298     6668   5104   5046   -696    516   -754       O  
ATOM   5296  CB  LEU B 298      58.749 -22.279  34.562  1.00 46.16           C  
ANISOU 5296  CB  LEU B 298     6753   5157   5630   -511    834   -761       C  
ATOM   5297  CG  LEU B 298      58.177 -21.768  33.247  1.00 48.65           C  
ANISOU 5297  CG  LEU B 298     6943   5416   6124   -416    890   -692       C  
ATOM   5298  CD1 LEU B 298      56.656 -21.599  33.373  1.00 40.67           C  
ANISOU 5298  CD1 LEU B 298     5919   4338   5197   -319   1051   -696       C  
ATOM   5299  CD2 LEU B 298      58.871 -20.441  32.871  1.00 40.27           C  
ANISOU 5299  CD2 LEU B 298     5912   4251   5137   -466    885   -725       C  
ATOM   5300  N   LEU B 299      61.235 -21.917  36.554  1.00 37.56           N  
ANISOU 5300  N   LEU B 299     5898   4116   4257   -812    538   -893       N  
ATOM   5301  CA  LEU B 299      61.420 -21.914  37.997  1.00 44.08           C  
ANISOU 5301  CA  LEU B 299     6939   4947   4864   -937    484   -974       C  
ATOM   5302  C   LEU B 299      60.067 -22.180  38.643  1.00 50.81           C  
ANISOU 5302  C   LEU B 299     7928   5764   5616   -888    687  -1016       C  
ATOM   5303  O   LEU B 299      59.056 -21.604  38.236  1.00 45.40           O  
ANISOU 5303  O   LEU B 299     7216   4985   5050   -797    895  -1051       O  
ATOM   5304  CB  LEU B 299      61.990 -20.570  38.466  1.00 39.86           C  
ANISOU 5304  CB  LEU B 299     6539   4312   4293  -1078    472  -1103       C  
ATOM   5305  CG  LEU B 299      62.462 -20.506  39.923  1.00 49.63           C  
ANISOU 5305  CG  LEU B 299     8023   5562   5270  -1258    355  -1192       C  
ATOM   5306  CD1 LEU B 299      63.747 -21.303  40.093  1.00 52.37           C  
ANISOU 5306  CD1 LEU B 299     8270   6043   5585  -1334     41  -1091       C  
ATOM   5307  CD2 LEU B 299      62.645 -19.065  40.380  1.00 54.52           C  
ANISOU 5307  CD2 LEU B 299     8825   6041   5848  -1395    422  -1358       C  
ATOM   5308  N   LEU B 300      60.030 -23.089  39.617  1.00 46.08           N  
ANISOU 5308  N   LEU B 300     7460   5234   4816   -943    629   -996       N  
ATOM   5309  CA  LEU B 300      58.737 -23.434  40.202  1.00 48.26           C  
ANISOU 5309  CA  LEU B 300     7852   5478   5005   -905    851  -1028       C  
ATOM   5310  C   LEU B 300      58.043 -22.206  40.785  1.00 51.76           C  
ANISOU 5310  C   LEU B 300     8473   5777   5415   -945   1093  -1194       C  
ATOM   5311  O   LEU B 300      56.814 -22.095  40.705  1.00 57.40           O  
ANISOU 5311  O   LEU B 300     9161   6423   6227   -851   1347  -1224       O  
ATOM   5312  CB  LEU B 300      58.898 -24.516  41.269  1.00 45.45           C  
ANISOU 5312  CB  LEU B 300     7665   5203   4401   -991    752   -980       C  
ATOM   5313  CG  LEU B 300      57.587 -25.144  41.745  1.00 53.94           C  
ANISOU 5313  CG  LEU B 300     8826   6262   5406   -952    989   -981       C  
ATOM   5314  CD1 LEU B 300      56.794 -25.673  40.551  1.00 51.17           C  
ANISOU 5314  CD1 LEU B 300     8201   5926   5313   -786   1081   -892       C  
ATOM   5315  CD2 LEU B 300      57.862 -26.258  42.739  1.00 55.55           C  
ANISOU 5315  CD2 LEU B 300     9213   6539   5353  -1047    866   -904       C  
ATOM   5316  N   ASP B 301      58.809 -21.265  41.348  1.00 54.57           N  
ANISOU 5316  N   ASP B 301     8998   6074   5662  -1085   1025  -1306       N  
ATOM   5317  CA  ASP B 301      58.211 -20.032  41.856  1.00 56.62           C  
ANISOU 5317  CA  ASP B 301     9441   6164   5907  -1124   1274  -1483       C  
ATOM   5318  C   ASP B 301      57.512 -19.261  40.744  1.00 55.29           C  
ANISOU 5318  C   ASP B 301     9067   5880   6059   -957   1447  -1474       C  
ATOM   5319  O   ASP B 301      56.443 -18.678  40.961  1.00 57.54           O  
ANISOU 5319  O   ASP B 301     9406   6027   6430   -890   1732  -1565       O  
ATOM   5320  CB  ASP B 301      59.276 -19.151  42.508  1.00 57.85           C  
ANISOU 5320  CB  ASP B 301     9804   6272   5906  -1322   1135  -1603       C  
ATOM   5321  CG  ASP B 301      60.077 -19.884  43.557  1.00 60.84           C  
ANISOU 5321  CG  ASP B 301    10375   6772   5971  -1500    892  -1582       C  
ATOM   5322  OD1 ASP B 301      60.731 -20.890  43.209  1.00 64.68           O  
ANISOU 5322  OD1 ASP B 301    10691   7404   6480  -1470    640  -1419       O  
ATOM   5323  OD2 ASP B 301      60.063 -19.447  44.724  1.00 70.16           O  
ANISOU 5323  OD2 ASP B 301    11886   7891   6881  -1672    949  -1727       O  
ATOM   5324  N   ASP B 302      58.103 -19.244  39.546  1.00 50.99           N  
ANISOU 5324  N   ASP B 302     8290   5380   5702   -890   1281  -1359       N  
ATOM   5325  CA  ASP B 302      57.486 -18.541  38.424  1.00 53.62           C  
ANISOU 5325  CA  ASP B 302     8447   5609   6318   -742   1400  -1317       C  
ATOM   5326  C   ASP B 302      56.190 -19.212  37.994  1.00 51.80           C  
ANISOU 5326  C   ASP B 302     8060   5402   6221   -580   1540  -1232       C  
ATOM   5327  O   ASP B 302      55.195 -18.532  37.723  1.00 50.39           O  
ANISOU 5327  O   ASP B 302     7823   5089   6235   -469   1737  -1253       O  
ATOM   5328  CB  ASP B 302      58.456 -18.469  37.241  1.00 47.69           C  
ANISOU 5328  CB  ASP B 302     7517   4913   5692   -734   1195  -1206       C  
ATOM   5329  CG  ASP B 302      59.599 -17.490  37.473  1.00 50.13           C  
ANISOU 5329  CG  ASP B 302     7933   5153   5961   -886   1099  -1293       C  
ATOM   5330  OD1 ASP B 302      59.454 -16.592  38.330  1.00 54.23           O  
ANISOU 5330  OD1 ASP B 302     8663   5536   6405   -971   1221  -1447       O  
ATOM   5331  OD2 ASP B 302      60.639 -17.610  36.789  1.00 52.77           O  
ANISOU 5331  OD2 ASP B 302     8142   5561   6348   -929    917  -1217       O  
ATOM   5332  N   PHE B 303      56.187 -20.545  37.897  1.00 48.34           N  
ANISOU 5332  N   PHE B 303     7537   5121   5708   -566   1431  -1129       N  
ATOM   5333  CA  PHE B 303      54.962 -21.241  37.520  1.00 47.76           C  
ANISOU 5333  CA  PHE B 303     7314   5073   5759   -441   1550  -1053       C  
ATOM   5334  C   PHE B 303      53.863 -21.012  38.553  1.00 48.52           C  
ANISOU 5334  C   PHE B 303     7532   5073   5829   -437   1834  -1166       C  
ATOM   5335  O   PHE B 303      52.704 -20.770  38.194  1.00 48.88           O  
ANISOU 5335  O   PHE B 303     7435   5042   6097   -315   2013  -1150       O  
ATOM   5336  CB  PHE B 303      55.231 -22.737  37.336  1.00 42.78           C  
ANISOU 5336  CB  PHE B 303     6610   4609   5037   -451   1392   -939       C  
ATOM   5337  CG  PHE B 303      54.017 -23.512  36.900  1.00 46.15           C  
ANISOU 5337  CG  PHE B 303     6878   5065   5591   -352   1491   -861       C  
ATOM   5338  CD1 PHE B 303      53.536 -23.401  35.600  1.00 51.04           C  
ANISOU 5338  CD1 PHE B 303     7280   5679   6434   -244   1454   -766       C  
ATOM   5339  CD2 PHE B 303      53.343 -24.332  37.793  1.00 50.85           C  
ANISOU 5339  CD2 PHE B 303     7552   5691   6079   -384   1615   -878       C  
ATOM   5340  CE1 PHE B 303      52.407 -24.109  35.197  1.00 49.10           C  
ANISOU 5340  CE1 PHE B 303     6879   5465   6314   -174   1515   -694       C  
ATOM   5341  CE2 PHE B 303      52.215 -25.034  37.399  1.00 48.41           C  
ANISOU 5341  CE2 PHE B 303     7080   5405   5910   -312   1708   -810       C  
ATOM   5342  CZ  PHE B 303      51.750 -24.925  36.098  1.00 46.13           C  
ANISOU 5342  CZ  PHE B 303     6554   5117   5856   -209   1646   -720       C  
ATOM   5343  N   VAL B 304      54.215 -21.070  39.841  1.00 47.95           N  
ANISOU 5343  N   VAL B 304     7726   5001   5492   -577   1882  -1278       N  
ATOM   5344  CA  VAL B 304      53.252 -20.777  40.900  1.00 54.13           C  
ANISOU 5344  CA  VAL B 304     8676   5676   6214   -600   2197  -1413       C  
ATOM   5345  C   VAL B 304      52.693 -19.367  40.742  1.00 55.06           C  
ANISOU 5345  C   VAL B 304     8779   5588   6553   -520   2423  -1522       C  
ATOM   5346  O   VAL B 304      51.478 -19.150  40.844  1.00 57.03           O  
ANISOU 5346  O   VAL B 304     8946   5733   6990   -415   2705  -1559       O  
ATOM   5347  CB  VAL B 304      53.902 -20.978  42.283  1.00 54.16           C  
ANISOU 5347  CB  VAL B 304     9028   5710   5840   -800   2173  -1517       C  
ATOM   5348  CG1 VAL B 304      53.074 -20.301  43.365  1.00 52.12           C  
ANISOU 5348  CG1 VAL B 304     9009   5296   5498   -852   2538  -1706       C  
ATOM   5349  CG2 VAL B 304      54.057 -22.468  42.579  1.00 53.83           C  
ANISOU 5349  CG2 VAL B 304     9002   5835   5617   -848   2029  -1394       C  
ATOM   5350  N   GLU B 305      53.569 -18.389  40.495  1.00 54.43           N  
ANISOU 5350  N   GLU B 305     8767   5432   6481   -566   2309  -1571       N  
ATOM   5351  CA  GLU B 305      53.104 -17.027  40.246  1.00 56.80           C  
ANISOU 5351  CA  GLU B 305     9052   5511   7018   -480   2506  -1656       C  
ATOM   5352  C   GLU B 305      52.146 -16.984  39.061  1.00 56.78           C  
ANISOU 5352  C   GLU B 305     8721   5472   7382   -265   2544  -1509       C  
ATOM   5353  O   GLU B 305      51.091 -16.339  39.128  1.00 57.55           O  
ANISOU 5353  O   GLU B 305     8750   5398   7717   -144   2810  -1558       O  
ATOM   5354  CB  GLU B 305      54.298 -16.099  40.009  1.00 56.81           C  
ANISOU 5354  CB  GLU B 305     9156   5450   6978   -578   2334  -1699       C  
ATOM   5355  CG  GLU B 305      53.934 -14.629  39.847  1.00 64.63           C  
ANISOU 5355  CG  GLU B 305    10184   6177   8194   -512   2538  -1797       C  
ATOM   5356  CD  GLU B 305      55.152 -13.752  39.597  1.00 70.18           C  
ANISOU 5356  CD  GLU B 305    10990   6817   8856   -634   2364  -1835       C  
ATOM   5357  OE1 GLU B 305      55.728 -13.824  38.493  1.00 66.84           O  
ANISOU 5357  OE1 GLU B 305    10382   6469   8544   -597   2142  -1681       O  
ATOM   5358  OE2 GLU B 305      55.544 -12.999  40.511  1.00 79.67           O  
ANISOU 5358  OE2 GLU B 305    12471   7892   9907   -785   2459  -2026       O  
ATOM   5359  N   ILE B 306      52.484 -17.691  37.978  1.00 50.13           N  
ANISOU 5359  N   ILE B 306     7671   4783   6591   -220   2281  -1328       N  
ATOM   5360  CA  ILE B 306      51.657 -17.673  36.772  1.00 51.58           C  
ANISOU 5360  CA  ILE B 306     7565   4949   7084    -46   2256  -1172       C  
ATOM   5361  C   ILE B 306      50.280 -18.271  37.050  1.00 56.68           C  
ANISOU 5361  C   ILE B 306     8069   5600   7868     47   2454  -1156       C  
ATOM   5362  O   ILE B 306      49.248 -17.688  36.697  1.00 57.17           O  
ANISOU 5362  O   ILE B 306     7956   5526   8238    194   2602  -1125       O  
ATOM   5363  CB  ILE B 306      52.360 -18.415  35.620  1.00 49.45           C  
ANISOU 5363  CB  ILE B 306     7158   4852   6780    -55   1947  -1004       C  
ATOM   5364  CG1 ILE B 306      53.587 -17.644  35.122  1.00 46.22           C  
ANISOU 5364  CG1 ILE B 306     6828   4406   6328   -124   1789  -1001       C  
ATOM   5365  CG2 ILE B 306      51.398 -18.641  34.468  1.00 49.45           C  
ANISOU 5365  CG2 ILE B 306     6890   4864   7036     91   1900   -841       C  
ATOM   5366  CD1 ILE B 306      54.561 -18.521  34.333  1.00 43.70           C  
ANISOU 5366  CD1 ILE B 306     6437   4270   5897   -183   1529   -888       C  
ATOM   5367  N   ILE B 307      50.237 -19.450  37.677  1.00 53.74           N  
ANISOU 5367  N   ILE B 307     7751   5374   7292    -36   2457  -1165       N  
ATOM   5368  CA  ILE B 307      48.958 -20.142  37.805  1.00 54.10           C  
ANISOU 5368  CA  ILE B 307     7629   5443   7486     36   2626  -1127       C  
ATOM   5369  C   ILE B 307      48.074 -19.455  38.841  1.00 58.25           C  
ANISOU 5369  C   ILE B 307     8239   5790   8102     62   3015  -1288       C  
ATOM   5370  O   ILE B 307      46.854 -19.375  38.669  1.00 60.07           O  
ANISOU 5370  O   ILE B 307     8243   5945   8636    188   3205  -1258       O  
ATOM   5371  CB  ILE B 307      49.168 -21.639  38.116  1.00 57.10           C  
ANISOU 5371  CB  ILE B 307     8050   6014   7632    -67   2521  -1076       C  
ATOM   5372  CG1 ILE B 307      47.854 -22.405  37.910  1.00 52.99           C  
ANISOU 5372  CG1 ILE B 307     7292   5527   7316      5   2642  -1000       C  
ATOM   5373  CG2 ILE B 307      49.725 -21.846  39.533  1.00 55.30           C  
ANISOU 5373  CG2 ILE B 307     8156   5797   7058   -226   2623  -1213       C  
ATOM   5374  CD1 ILE B 307      47.943 -23.907  38.161  1.00 48.12           C  
ANISOU 5374  CD1 ILE B 307     6710   5071   6503    -93   2558   -939       C  
ATOM   5375  N   LYS B 308      48.670 -18.914  39.909  1.00 58.13           N  
ANISOU 5375  N   LYS B 308     8547   5696   7843    -59   3144  -1464       N  
ATOM   5376  CA  LYS B 308      47.887 -18.246  40.945  1.00 63.83           C  
ANISOU 5376  CA  LYS B 308     9404   6232   8616    -54   3555  -1648       C  
ATOM   5377  C   LYS B 308      47.292 -16.923  40.485  1.00 62.18           C  
ANISOU 5377  C   LYS B 308     9051   5786   8788    115   3725  -1680       C  
ATOM   5378  O   LYS B 308      46.411 -16.393  41.165  1.00 65.26           O  
ANISOU 5378  O   LYS B 308     9446   6030   9321    152   4040  -1772       O  
ATOM   5379  CB  LYS B 308      48.732 -18.013  42.203  1.00 64.17           C  
ANISOU 5379  CB  LYS B 308     9878   6251   8251   -260   3626  -1837       C  
ATOM   5380  CG  LYS B 308      48.785 -19.220  43.139  1.00 68.81           C  
ANISOU 5380  CG  LYS B 308    10656   6994   8496   -415   3648  -1848       C  
ATOM   5381  CD  LYS B 308      49.443 -18.879  44.467  1.00 74.29           C  
ANISOU 5381  CD  LYS B 308    11756   7664   8807   -631   3671  -1986       C  
ATOM   5382  CE  LYS B 308      49.436 -20.073  45.408  1.00 75.52           C  
ANISOU 5382  CE  LYS B 308    12101   7962   8632   -783   3663  -1953       C  
ATOM   5383  NZ  LYS B 308      50.164 -19.792  46.676  1.00 84.33           N  
ANISOU 5383  NZ  LYS B 308    13614   9071   9357  -1007   3609  -2049       N  
ATOM   5384  N   SER B 309      47.736 -16.378  39.361  1.00 63.57           N  
ANISOU 5384  N   SER B 309     9086   5941   9129    199   3471  -1556       N  
ATOM   5385  CA  SER B 309      47.175 -15.128  38.873  1.00 70.95           C  
ANISOU 5385  CA  SER B 309     9885   6633  10441    370   3605  -1553       C  
ATOM   5386  C   SER B 309      46.017 -15.338  37.905  1.00 71.84           C  
ANISOU 5386  C   SER B 309     9585   6743  10967    572   3574  -1361       C  
ATOM   5387  O   SER B 309      45.456 -14.355  37.411  1.00 76.18           O  
ANISOU 5387  O   SER B 309     9977   7088  11879    740   3653  -1315       O  
ATOM   5388  CB  SER B 309      48.269 -14.288  38.208  1.00 68.19           C  
ANISOU 5388  CB  SER B 309     9633   6226  10048    339   3362  -1518       C  
ATOM   5389  OG  SER B 309      48.706 -14.887  37.004  1.00 71.38           O  
ANISOU 5389  OG  SER B 309     9857   6813  10451    355   2997  -1303       O  
ATOM   5390  N   GLN B 310      45.633 -16.585  37.642  1.00 66.58           N  
ANISOU 5390  N   GLN B 310     7634   6913  10750    368   3193  -1597       N  
ATOM   5391  CA  GLN B 310      44.607 -16.880  36.652  1.00 67.32           C  
ANISOU 5391  CA  GLN B 310     7352   6984  11245    454   3032  -1208       C  
ATOM   5392  C   GLN B 310      43.202 -16.768  37.232  1.00 71.66           C  
ANISOU 5392  C   GLN B 310     7599   7420  12211    501   3449  -1224       C  
ATOM   5393  O   GLN B 310      42.960 -17.054  38.410  1.00 68.87           O  
ANISOU 5393  O   GLN B 310     7403   7137  11628    406   3812  -1503       O  
ATOM   5394  CB  GLN B 310      44.793 -18.286  36.082  1.00 59.63           C  
ANISOU 5394  CB  GLN B 310     6505   6289   9862    333   2639   -980       C  
ATOM   5395  CG  GLN B 310      46.099 -18.488  35.345  1.00 61.16           C  
ANISOU 5395  CG  GLN B 310     6934   6583   9720    298   2248   -932       C  
ATOM   5396  CD  GLN B 310      46.289 -17.491  34.217  1.00 66.54           C  
ANISOU 5396  CD  GLN B 310     7400   7130  10752    403   2056   -739       C  
ATOM   5397  OE1 GLN B 310      45.372 -17.232  33.441  1.00 61.38           O  
ANISOU 5397  OE1 GLN B 310     6388   6424  10508    450   1976   -446       O  
ATOM   5398  NE2 GLN B 310      47.484 -16.928  34.123  1.00 56.84           N  
ANISOU 5398  NE2 GLN B 310     6364   5860   9371    420   1962   -860       N  
ATOM   5399  N   ASP B 311      42.268 -16.371  36.370  1.00 72.65           N  
ANISOU 5399  N   ASP B 311     7262   7392  12948    628   3384   -885       N  
ATOM   5400  CA  ASP B 311      40.850 -16.354  36.704  1.00 74.47           C  
ANISOU 5400  CA  ASP B 311     7116   7518  13660    681   3706   -787       C  
ATOM   5401  C   ASP B 311      40.275 -17.750  36.489  1.00 75.68           C  
ANISOU 5401  C   ASP B 311     7243   7961  13553    540   3490   -553       C  
ATOM   5402  O   ASP B 311      40.364 -18.302  35.387  1.00 71.86           O  
ANISOU 5402  O   ASP B 311     6700   7630  12971    473   3006   -226       O  
ATOM   5403  CB  ASP B 311      40.132 -15.312  35.848  1.00 70.58           C  
ANISOU 5403  CB  ASP B 311     6179   6752  13888    824   3591   -425       C  
ATOM   5404  CG  ASP B 311      38.652 -15.238  36.133  1.00 83.08           C  
ANISOU 5404  CG  ASP B 311     7431   8211  15925    846   3799   -257       C  
ATOM   5405  OD1 ASP B 311      37.884 -15.995  35.504  1.00 88.59           O  
ANISOU 5405  OD1 ASP B 311     7825   9069  16765    817   3587    112       O  
ATOM   5406  OD2 ASP B 311      38.255 -14.435  37.002  1.00 89.37           O  
ANISOU 5406  OD2 ASP B 311     8267   8755  16932    864   4175   -501       O  
ATOM   5407  N   LEU B 312      39.695 -18.327  37.542  1.00 80.27           N  
ANISOU 5407  N   LEU B 312     7885   8623  13992    457   3851   -732       N  
ATOM   5408  CA  LEU B 312      39.268 -19.721  37.531  1.00 82.76           C  
ANISOU 5408  CA  LEU B 312     8250   9196  14000    288   3672   -556       C  
ATOM   5409  C   LEU B 312      37.764 -19.884  37.332  1.00 84.67           C  
ANISOU 5409  C   LEU B 312     7984   9390  14796    311   3800   -267       C  
ATOM   5410  O   LEU B 312      37.204 -20.910  37.731  1.00 85.29           O  
ANISOU 5410  O   LEU B 312     8075   9634  14698    167   3853   -208       O  
ATOM   5411  CB  LEU B 312      39.697 -20.413  38.828  1.00 81.92           C  
ANISOU 5411  CB  LEU B 312     8559   9266  13300    132   3925   -864       C  
ATOM   5412  CG  LEU B 312      41.171 -20.299  39.229  1.00 71.60           C  
ANISOU 5412  CG  LEU B 312     7734   8040  11431     73   3818  -1132       C  
ATOM   5413  CD1 LEU B 312      41.451 -21.134  40.467  1.00 72.45           C  
ANISOU 5413  CD1 LEU B 312     8186   8383  10958   -130   3998  -1301       C  
ATOM   5414  CD2 LEU B 312      42.068 -20.715  38.078  1.00 65.02           C  
ANISOU 5414  CD2 LEU B 312     7024   7270  10410     71   3254   -929       C  
ATOM   5415  N   SER B 313      37.098 -18.913  36.711  1.00 84.59           N  
ANISOU 5415  N   SER B 313     7525   9155  15462    475   3806    -38       N  
ATOM   5416  CA  SER B 313      35.643 -18.936  36.610  1.00 87.84           C  
ANISOU 5416  CA  SER B 313     7528   9494  16352    492   3843    257       C  
ATOM   5417  C   SER B 313      35.131 -19.412  35.256  1.00 82.96           C  
ANISOU 5417  C   SER B 313     6518   9022  15979    411   3339    781       C  
ATOM   5418  O   SER B 313      33.914 -19.440  35.051  1.00 85.23           O  
ANISOU 5418  O   SER B 313     6452   9270  16660    410   3292   1081       O  
ATOM   5419  CB  SER B 313      35.069 -17.548  36.924  1.00 90.87           C  
ANISOU 5419  CB  SER B 313     7754   9503  17269    672   4108    211       C  
ATOM   5420  OG  SER B 313      35.746 -16.530  36.209  1.00 93.92           O  
ANISOU 5420  OG  SER B 313     8116   9705  17865    786   3912    289       O  
ATOM   5421  N   VAL B 314      36.018 -19.792  34.337  1.00 82.81           N  
ANISOU 5421  N   VAL B 314     6663   9189  15614    300   2885    882       N  
ATOM   5422  CA  VAL B 314      35.638 -20.290  33.020  1.00 83.70           C  
ANISOU 5422  CA  VAL B 314     6540   9507  15754    122   2321   1325       C  
ATOM   5423  C   VAL B 314      35.971 -21.771  32.947  1.00 78.92           C  
ANISOU 5423  C   VAL B 314     6320   9170  14497   -146   2076   1210       C  
ATOM   5424  O   VAL B 314      36.943 -22.238  33.551  1.00 73.91           O  
ANISOU 5424  O   VAL B 314     6186   8564  13332   -165   2171    855       O  
ATOM   5425  CB  VAL B 314      36.357 -19.530  31.885  1.00 87.68           C  
ANISOU 5425  CB  VAL B 314     7028  10021  16266    151   1920   1527       C  
ATOM   5426  CG1 VAL B 314      35.404 -19.287  30.724  1.00 95.50           C  
ANISOU 5426  CG1 VAL B 314     7447  11107  17730     58   1534   2123       C  
ATOM   5427  CG2 VAL B 314      36.949 -18.229  32.401  1.00 91.30           C  
ANISOU 5427  CG2 VAL B 314     7530  10165  16995    422   2257   1311       C  
ATOM   5428  N  AVAL B 315      35.158 -22.511  32.188  0.44 71.94           N  
ANISOU 5428  N  AVAL B 315     5176   8469  13691   -371   1749   1531       N  
ATOM   5429  N  BVAL B 315      35.157 -22.519  32.196  0.56 71.50           N  
ANISOU 5429  N  BVAL B 315     5122   8414  13633   -371   1752   1529       N  
ATOM   5430  CA AVAL B 315      35.388 -23.945  32.030  0.44 70.31           C  
ANISOU 5430  CA AVAL B 315     5293   8462  12960   -649   1527   1421       C  
ATOM   5431  CA BVAL B 315      35.407 -23.952  32.044  0.56 70.08           C  
ANISOU 5431  CA BVAL B 315     5273   8432  12922   -648   1531   1414       C  
ATOM   5432  C  AVAL B 315      36.718 -24.201  31.327  0.44 69.37           C  
ANISOU 5432  C  AVAL B 315     5623   8445  12288   -739   1207   1245       C  
ATOM   5433  C  BVAL B 315      36.742 -24.188  31.343  0.56 69.43           C  
ANISOU 5433  C  BVAL B 315     5638   8449  12292   -733   1212   1238       C  
ATOM   5434  O  AVAL B 315      37.504 -25.061  31.746  0.44 66.50           O  
ANISOU 5434  O  AVAL B 315     5701   8096  11472   -804   1252    955       O  
ATOM   5435  O  BVAL B 315      37.553 -25.018  31.774  0.56 65.98           O  
ANISOU 5435  O  BVAL B 315     5646   8022  11400   -792   1263    944       O  
ATOM   5436  CB AVAL B 315      34.208 -24.597  31.284  0.44 74.10           C  
ANISOU 5436  CB AVAL B 315     5374   9113  13669   -917   1230   1788       C  
ATOM   5437  CB BVAL B 315      34.242 -24.629  31.299  0.56 74.06           C  
ANISOU 5437  CB BVAL B 315     5388   9108  13642   -919   1231   1774       C  
ATOM   5438  CG1AVAL B 315      33.847 -23.799  30.031  0.44 77.15           C  
ANISOU 5438  CG1AVAL B 315     5347   9605  14361   -971    826   2217       C  
ATOM   5439  CG1BVAL B 315      34.678 -25.975  30.736  0.56 74.18           C  
ANISOU 5439  CG1BVAL B 315     5758   9308  13119  -1248    906   1644       C  
ATOM   5440  CG2AVAL B 315      34.526 -26.047  30.939  0.44 73.74           C  
ANISOU 5440  CG2AVAL B 315     5676   9232  13110  -1238    975   1640       C  
ATOM   5441  CG2BVAL B 315      33.049 -24.810  32.235  0.56 72.14           C  
ANISOU 5441  CG2BVAL B 315     4806   8773  13829   -870   1616   1861       C  
ATOM   5442  N   SER B 316      36.998 -23.456  30.261  1.00 67.93           N  
ANISOU 5442  N   SER B 316     5312   8330  12167   -744    893   1446       N  
ATOM   5443  CA  SER B 316      38.250 -23.623  29.535  1.00 70.09           C  
ANISOU 5443  CA  SER B 316     5980   8713  11940   -834    625   1285       C  
ATOM   5444  C   SER B 316      38.575 -22.353  28.769  1.00 64.66           C  
ANISOU 5444  C   SER B 316     5108   8020  11438   -724    451   1510       C  
ATOM   5445  O   SER B 316      37.699 -21.762  28.136  1.00 66.62           O  
ANISOU 5445  O   SER B 316     4885   8325  12103   -761    269   1935       O  
ATOM   5446  CB  SER B 316      38.188 -24.812  28.568  1.00 70.95           C  
ANISOU 5446  CB  SER B 316     6201   9068  11689  -1211    257   1306       C  
ATOM   5447  OG  SER B 316      37.289 -24.557  27.503  1.00 76.84           O  
ANISOU 5447  OG  SER B 316     6527  10022  12647  -1424    -96   1720       O  
ATOM   5448  N   LYS B 317      39.841 -21.950  28.816  1.00 65.38           N  
ANISOU 5448  N   LYS B 317     5547   8046  11249   -603    489   1272       N  
ATOM   5449  CA  LYS B 317      40.297 -20.851  27.982  1.00 70.59           C  
ANISOU 5449  CA  LYS B 317     6081   8720  12020   -543    288   1491       C  
ATOM   5450  C   LYS B 317      41.770 -21.057  27.662  1.00 62.40           C  
ANISOU 5450  C   LYS B 317     5512   7752  10445   -583    192   1209       C  
ATOM   5451  O   LYS B 317      42.458 -21.868  28.290  1.00 53.61           O  
ANISOU 5451  O   LYS B 317     4785   6603   8980   -581    342    845       O  
ATOM   5452  CB  LYS B 317      40.053 -19.482  28.642  1.00 79.37           C  
ANISOU 5452  CB  LYS B 317     6916   9517  13722   -220    595   1573       C  
ATOM   5453  CG  LYS B 317      40.794 -19.220  29.945  1.00 77.14           C  
ANISOU 5453  CG  LYS B 317     6965   8989  13355      5   1032   1113       C  
ATOM   5454  CD  LYS B 317      40.654 -17.750  30.348  1.00 77.91           C  
ANISOU 5454  CD  LYS B 317     6796   8761  14045    274   1314   1164       C  
ATOM   5455  CE  LYS B 317      41.407 -17.429  31.634  1.00 82.95           C  
ANISOU 5455  CE  LYS B 317     7782   9192  14542    428   1742    665       C  
ATOM   5456  NZ  LYS B 317      41.361 -15.973  31.966  1.00 83.73           N  
ANISOU 5456  NZ  LYS B 317     7655   8935  15225    656   2040    640       N  
ATOM   5457  N   VAL B 318      42.233 -20.342  26.643  1.00 56.86           N  
ANISOU 5457  N   VAL B 318     4739   7162   9705   -634    -71   1429       N  
ATOM   5458  CA  VAL B 318      43.650 -20.300  26.293  1.00 59.27           C  
ANISOU 5458  CA  VAL B 318     5419   7514   9586   -643   -131   1205       C  
ATOM   5459  C   VAL B 318      44.267 -19.085  26.967  1.00 61.63           C  
ANISOU 5459  C   VAL B 318     5727   7530  10162   -336    105   1131       C  
ATOM   5460  O   VAL B 318      43.728 -17.979  26.879  1.00 62.07           O  
ANISOU 5460  O   VAL B 318     5419   7441  10722   -204    124   1430       O  
ATOM   5461  CB  VAL B 318      43.856 -20.246  24.769  1.00 59.56           C  
ANISOU 5461  CB  VAL B 318     5398   7876   9354   -928   -533   1471       C  
ATOM   5462  CG1 VAL B 318      45.339 -20.082  24.437  1.00 57.34           C  
ANISOU 5462  CG1 VAL B 318     5466   7623   8698   -910   -536   1248       C  
ATOM   5463  CG2 VAL B 318      43.291 -21.497  24.110  1.00 65.53           C  
ANISOU 5463  CG2 VAL B 318     6193   8920   9784  -1296   -746   1455       C  
ATOM   5464  N   VAL B 319      45.394 -19.291  27.643  1.00 52.05           N  
ANISOU 5464  N   VAL B 319     4902   6217   8656   -238    283    747       N  
ATOM   5465  CA  VAL B 319      46.113 -18.231  28.336  1.00 52.11           C  
ANISOU 5465  CA  VAL B 319     4982   5975   8843     -6    502    601       C  
ATOM   5466  C   VAL B 319      47.474 -18.088  27.667  1.00 56.60           C  
ANISOU 5466  C   VAL B 319     5794   6640   9071    -56    332    536       C  
ATOM   5467  O   VAL B 319      48.212 -19.073  27.540  1.00 53.08           O  
ANISOU 5467  O   VAL B 319     5650   6333   8185   -170    273    327       O  
ATOM   5468  CB  VAL B 319      46.258 -18.536  29.838  1.00 52.39           C  
ANISOU 5468  CB  VAL B 319     5241   5846   8818    115    857    225       C  
ATOM   5469  CG1 VAL B 319      47.149 -17.511  30.503  1.00 59.25           C  
ANISOU 5469  CG1 VAL B 319     6242   6504   9766    276   1050     15       C  
ATOM   5470  CG2 VAL B 319      44.874 -18.554  30.509  1.00 55.45           C  
ANISOU 5470  CG2 VAL B 319     5354   6133   9582    168   1088    290       C  
ATOM   5471  N   LYS B 320      47.798 -16.871  27.226  1.00 48.02           N  
ANISOU 5471  N   LYS B 320     4550   5456   8239     27    274    732       N  
ATOM   5472  CA  LYS B 320      49.085 -16.581  26.600  1.00 50.79           C  
ANISOU 5472  CA  LYS B 320     5090   5887   8320    -15    139    704       C  
ATOM   5473  C   LYS B 320      50.031 -15.993  27.643  1.00 50.24           C  
ANISOU 5473  C   LYS B 320     5224   5564   8303    167    383    392       C  
ATOM   5474  O   LYS B 320      49.693 -15.007  28.305  1.00 55.04           O  
ANISOU 5474  O   LYS B 320     5676   5894   9342    325    585    378       O  
ATOM   5475  CB  LYS B 320      48.910 -15.609  25.434  1.00 63.14           C  
ANISOU 5475  CB  LYS B 320     6350   7525  10114    -78   -103   1164       C  
ATOM   5476  CG  LYS B 320      47.900 -16.044  24.389  1.00 66.86           C  
ANISOU 5476  CG  LYS B 320     6571   8295  10537   -313   -393   1543       C  
ATOM   5477  CD  LYS B 320      48.559 -16.826  23.270  1.00 72.21           C  
ANISOU 5477  CD  LYS B 320     7471   9360  10608   -612   -633   1519       C  
ATOM   5478  CE  LYS B 320      47.586 -17.053  22.125  1.00 80.43           C  
ANISOU 5478  CE  LYS B 320     8245  10751  11565   -921   -968   1936       C  
ATOM   5479  NZ  LYS B 320      47.045 -15.770  21.603  1.00 89.77           N  
ANISOU 5479  NZ  LYS B 320     8987  11904  13219   -886  -1153   2522       N  
ATOM   5480  N   VAL B 321      51.212 -16.589  27.782  1.00 44.54           N  
ANISOU 5480  N   VAL B 321     4828   4926   7167    125    372    138       N  
ATOM   5481  CA  VAL B 321      52.243 -16.111  28.699  1.00 46.82           C  
ANISOU 5481  CA  VAL B 321     5317   5042   7429    235    533   -132       C  
ATOM   5482  C   VAL B 321      53.524 -15.888  27.904  1.00 45.25           C  
ANISOU 5482  C   VAL B 321     5223   4939   7032    181    374    -88       C  
ATOM   5483  O   VAL B 321      53.919 -16.750  27.111  1.00 39.98           O  
ANISOU 5483  O   VAL B 321     4656   4494   6041     54    234    -65       O  
ATOM   5484  CB  VAL B 321      52.485 -17.113  29.843  1.00 46.66           C  
ANISOU 5484  CB  VAL B 321     5560   5039   7129    231    679   -441       C  
ATOM   5485  CG1 VAL B 321      53.518 -16.566  30.831  1.00 44.39           C  
ANISOU 5485  CG1 VAL B 321     5460   4625   6783    287    805   -686       C  
ATOM   5486  CG2 VAL B 321      51.158 -17.444  30.547  1.00 49.72           C  
ANISOU 5486  CG2 VAL B 321     5837   5379   7678    251    850   -461       C  
ATOM   5487  N   THR B 322      54.173 -14.738  28.114  1.00 41.38           N  
ANISOU 5487  N   THR B 322     4705   4266   6753    263    425    -99       N  
ATOM   5488  CA  THR B 322      55.429 -14.450  27.425  1.00 37.61           C  
ANISOU 5488  CA  THR B 322     4305   3866   6121    213    297    -47       C  
ATOM   5489  C   THR B 322      56.572 -15.155  28.148  1.00 35.57           C  
ANISOU 5489  C   THR B 322     4326   3642   5546    209    351   -345       C  
ATOM   5490  O   THR B 322      56.796 -14.925  29.342  1.00 38.29           O  
ANISOU 5490  O   THR B 322     4777   3840   5932    264    489   -570       O  
ATOM   5491  CB  THR B 322      55.687 -12.944  27.345  1.00 42.51           C  
ANISOU 5491  CB  THR B 322     4760   4254   7138    284    320     88       C  
ATOM   5492  OG1 THR B 322      54.579 -12.314  26.702  1.00 45.24           O  
ANISOU 5492  OG1 THR B 322     4787   4542   7862    300    259    442       O  
ATOM   5493  CG2 THR B 322      56.936 -12.678  26.509  1.00 42.23           C  
ANISOU 5493  CG2 THR B 322     4775   4335   6938    207    178    197       C  
ATOM   5494  N   ILE B 323      57.273 -16.034  27.430  1.00 35.08           N  
ANISOU 5494  N   ILE B 323     4371   3782   5178    122    252   -341       N  
ATOM   5495  CA  ILE B 323      58.351 -16.856  27.978  1.00 38.31           C  
ANISOU 5495  CA  ILE B 323     4982   4217   5357    126    287   -546       C  
ATOM   5496  C   ILE B 323      59.453 -16.940  26.929  1.00 33.98           C  
ANISOU 5496  C   ILE B 323     4443   3795   4674     61    214   -479       C  
ATOM   5497  O   ILE B 323      59.178 -17.223  25.760  1.00 36.37           O  
ANISOU 5497  O   ILE B 323     4693   4270   4857    -51    155   -363       O  
ATOM   5498  CB  ILE B 323      57.867 -18.274  28.355  1.00 35.31           C  
ANISOU 5498  CB  ILE B 323     4709   3901   4806    100    334   -658       C  
ATOM   5499  CG1 ILE B 323      56.647 -18.201  29.281  1.00 40.69           C  
ANISOU 5499  CG1 ILE B 323     5355   4495   5611    141    431   -696       C  
ATOM   5500  CG2 ILE B 323      58.967 -19.036  29.055  1.00 37.07           C  
ANISOU 5500  CG2 ILE B 323     5085   4104   4896    124    362   -793       C  
ATOM   5501  CD1 ILE B 323      56.159 -19.564  29.773  1.00 41.74           C  
ANISOU 5501  CD1 ILE B 323     5585   4674   5602    105    482   -778       C  
ATOM   5502  N   ASP B 324      60.695 -16.675  27.335  1.00 31.44           N  
ANISOU 5502  N   ASP B 324     4179   3412   4355     98    222   -551       N  
ATOM   5503  CA  ASP B 324      61.813 -16.672  26.386  1.00 37.86           C  
ANISOU 5503  CA  ASP B 324     4971   4329   5083     45    196   -489       C  
ATOM   5504  C   ASP B 324      61.504 -15.763  25.197  1.00 38.06           C  
ANISOU 5504  C   ASP B 324     4854   4452   5156    -40    122   -251       C  
ATOM   5505  O   ASP B 324      61.833 -16.079  24.051  1.00 36.43           O  
ANISOU 5505  O   ASP B 324     4634   4445   4762   -162    115   -179       O  
ATOM   5506  CB  ASP B 324      62.146 -18.093  25.891  1.00 36.99           C  
ANISOU 5506  CB  ASP B 324     4946   4336   4774     -5    268   -598       C  
ATOM   5507  CG  ASP B 324      62.651 -19.024  26.992  1.00 38.81           C  
ANISOU 5507  CG  ASP B 324     5268   4455   5021     80    320   -737       C  
ATOM   5508  OD1 ASP B 324      63.155 -18.530  28.029  1.00 37.92           O  
ANISOU 5508  OD1 ASP B 324     5166   4248   4994    139    275   -742       O  
ATOM   5509  OD2 ASP B 324      62.584 -20.281  26.791  1.00 38.52           O  
ANISOU 5509  OD2 ASP B 324     5287   4431   4919     60    404   -830       O  
ATOM   5510  N   TYR B 325      60.825 -14.640  25.469  1.00 36.87           N  
ANISOU 5510  N   TYR B 325     4583   4159   5268      6     82   -118       N  
ATOM   5511  CA  TYR B 325      60.420 -13.616  24.505  1.00 33.75           C  
ANISOU 5511  CA  TYR B 325     3992   3798   5033    -58    -16    204       C  
ATOM   5512  C   TYR B 325      59.314 -14.049  23.547  1.00 44.38           C  
ANISOU 5512  C   TYR B 325     5246   5370   6246   -184   -113    406       C  
ATOM   5513  O   TYR B 325      58.987 -13.287  22.638  1.00 44.38           O  
ANISOU 5513  O   TYR B 325     5059   5464   6338   -278   -239    754       O  
ATOM   5514  CB  TYR B 325      61.588 -13.100  23.650  1.00 37.07           C  
ANISOU 5514  CB  TYR B 325     4371   4319   5394   -142    -58    350       C  
ATOM   5515  CG  TYR B 325      62.647 -12.380  24.444  1.00 37.92           C  
ANISOU 5515  CG  TYR B 325     4502   4205   5702    -58    -12    238       C  
ATOM   5516  CD1 TYR B 325      62.368 -11.170  25.080  1.00 43.17           C  
ANISOU 5516  CD1 TYR B 325     5068   4578   6757     14     -3    279       C  
ATOM   5517  CD2 TYR B 325      63.925 -12.900  24.551  1.00 34.11           C  
ANISOU 5517  CD2 TYR B 325     4118   3788   5055    -69     32     88       C  
ATOM   5518  CE1 TYR B 325      63.342 -10.505  25.811  1.00 40.22           C  
ANISOU 5518  CE1 TYR B 325     4729   4012   6540     33     30    139       C  
ATOM   5519  CE2 TYR B 325      64.905 -12.248  25.279  1.00 34.31           C  
ANISOU 5519  CE2 TYR B 325     4142   3641   5252    -34     33     10       C  
ATOM   5520  CZ  TYR B 325      64.606 -11.057  25.909  1.00 37.49           C  
ANISOU 5520  CZ  TYR B 325     4482   3786   5977     -3     22     20       C  
ATOM   5521  OH  TYR B 325      65.582 -10.405  26.625  1.00 41.24           O  
ANISOU 5521  OH  TYR B 325     4969   4103   6596    -24     14    -91       O  
ATOM   5522  N   THR B 326      58.721 -15.227  23.709  1.00 35.69           N  
ANISOU 5522  N   THR B 326     4251   4368   4941   -218    -80    237       N  
ATOM   5523  CA  THR B 326      57.675 -15.667  22.791  1.00 36.21           C  
ANISOU 5523  CA  THR B 326     4228   4676   4855   -393   -197    415       C  
ATOM   5524  C   THR B 326      56.378 -15.912  23.564  1.00 36.05           C  
ANISOU 5524  C   THR B 326     4139   4529   5031   -309   -177    392       C  
ATOM   5525  O   THR B 326      56.385 -16.110  24.784  1.00 40.63           O  
ANISOU 5525  O   THR B 326     4815   4891   5732   -149    -34    154       O  
ATOM   5526  CB  THR B 326      58.116 -16.937  22.015  1.00 39.30           C  
ANISOU 5526  CB  THR B 326     4796   5333   4804   -586   -159    222       C  
ATOM   5527  OG1 THR B 326      57.306 -17.108  20.844  1.00 44.31           O  
ANISOU 5527  OG1 THR B 326     5340   6284   5213   -854   -314    434       O  
ATOM   5528  CG2 THR B 326      58.003 -18.185  22.886  1.00 38.40           C  
ANISOU 5528  CG2 THR B 326     4854   5098   4639   -507    -21   -115       C  
ATOM   5529  N   GLU B 327      55.255 -15.876  22.842  1.00 41.24           N  
ANISOU 5529  N   GLU B 327     4608   5351   5711   -446   -329    671       N  
ATOM   5530  CA  GLU B 327      53.945 -16.122  23.439  1.00 43.80           C  
ANISOU 5530  CA  GLU B 327     4812   5581   6250   -389   -311    696       C  
ATOM   5531  C   GLU B 327      53.707 -17.624  23.496  1.00 40.14           C  
ANISOU 5531  C   GLU B 327     4538   5256   5457   -509   -271    430       C  
ATOM   5532  O   GLU B 327      53.493 -18.264  22.461  1.00 42.67           O  
ANISOU 5532  O   GLU B 327     4874   5867   5471   -766   -401    486       O  
ATOM   5533  CB  GLU B 327      52.834 -15.448  22.637  1.00 50.66           C  
ANISOU 5533  CB  GLU B 327     5337   6564   7346   -495   -521   1172       C  
ATOM   5534  CG  GLU B 327      52.882 -13.929  22.609  1.00 71.20           C  
ANISOU 5534  CG  GLU B 327     7682   8948  10423   -358   -547   1500       C  
ATOM   5535  CD  GLU B 327      52.678 -13.315  23.977  1.00 87.09           C  
ANISOU 5535  CD  GLU B 327     9655  10522  12912    -71   -289   1301       C  
ATOM   5536  OE1 GLU B 327      53.680 -12.860  24.571  1.00 92.35           O  
ANISOU 5536  OE1 GLU B 327    10481  10990  13616     45   -145   1065       O  
ATOM   5537  OE2 GLU B 327      51.521 -13.295  24.457  1.00 91.37           O  
ANISOU 5537  OE2 GLU B 327    10004  10933  13778     10   -218   1367       O  
ATOM   5538  N   ILE B 328      53.713 -18.187  24.696  1.00 39.64           N  
ANISOU 5538  N   ILE B 328     4614   4994   5454   -356    -91    149       N  
ATOM   5539  CA  ILE B 328      53.398 -19.599  24.893  1.00 39.02           C  
ANISOU 5539  CA  ILE B 328     4684   4975   5167   -448    -36    -68       C  
ATOM   5540  C   ILE B 328      51.925 -19.717  25.264  1.00 46.45           C  
ANISOU 5540  C   ILE B 328     5442   5888   6317   -454    -49     57       C  
ATOM   5541  O   ILE B 328      51.446 -19.019  26.168  1.00 41.32           O  
ANISOU 5541  O   ILE B 328     4673   5040   5989   -273     62    100       O  
ATOM   5542  CB  ILE B 328      54.294 -20.226  25.971  1.00 41.50           C  
ANISOU 5542  CB  ILE B 328     5230   5112   5424   -306    144   -368       C  
ATOM   5543  CG1 ILE B 328      55.759 -20.152  25.528  1.00 36.90           C  
ANISOU 5543  CG1 ILE B 328     4774   4559   4686   -306    155   -458       C  
ATOM   5544  CG2 ILE B 328      53.875 -21.690  26.228  1.00 36.48           C  
ANISOU 5544  CG2 ILE B 328     4710   4483   4668   -391    208   -537       C  
ATOM   5545  CD1 ILE B 328      56.017 -20.815  24.184  1.00 38.66           C  
ANISOU 5545  CD1 ILE B 328     5047   5009   4632   -534    105   -493       C  
ATOM   5546  N   SER B 329      51.201 -20.586  24.561  1.00 45.18           N  
ANISOU 5546  N   SER B 329     5251   5927   5989   -683   -163     95       N  
ATOM   5547  CA  SER B 329      49.792 -20.827  24.850  1.00 52.08           C  
ANISOU 5547  CA  SER B 329     5927   6798   7063   -722   -190    230       C  
ATOM   5548  C   SER B 329      49.654 -21.933  25.887  1.00 50.98           C  
ANISOU 5548  C   SER B 329     5960   6515   6896   -665      1    -46       C  
ATOM   5549  O   SER B 329      50.205 -23.026  25.710  1.00 44.38           O  
ANISOU 5549  O   SER B 329     5347   5709   5806   -776     35   -276       O  
ATOM   5550  CB  SER B 329      49.026 -21.207  23.580  1.00 51.08           C  
ANISOU 5550  CB  SER B 329     5660   6988   6761  -1054   -446    436       C  
ATOM   5551  OG  SER B 329      48.971 -20.128  22.666  1.00 54.92           O  
ANISOU 5551  OG  SER B 329     5924   7639   7303  -1130   -659    807       O  
ATOM   5552  N   PHE B 330      48.919 -21.646  26.964  1.00 47.81           N  
ANISOU 5552  N   PHE B 330     5440   5944   6781   -500    150    -14       N  
ATOM   5553  CA  PHE B 330      48.552 -22.632  27.974  1.00 43.31           C  
ANISOU 5553  CA  PHE B 330     4978   5274   6202   -479    320   -185       C  
ATOM   5554  C   PHE B 330      47.062 -22.943  27.888  1.00 49.73           C  
ANISOU 5554  C   PHE B 330     5540   6150   7207   -591    280     -8       C  
ATOM   5555  O   PHE B 330      46.240 -22.046  27.679  1.00 48.91           O  
ANISOU 5555  O   PHE B 330     5128   6054   7403   -551    230    249       O  
ATOM   5556  CB  PHE B 330      48.874 -22.144  29.391  1.00 43.61           C  
ANISOU 5556  CB  PHE B 330     5101   5118   6352   -255    563   -316       C  
ATOM   5557  CG  PHE B 330      50.345 -22.117  29.718  1.00 46.19           C  
ANISOU 5557  CG  PHE B 330     5687   5392   6473   -177    595   -497       C  
ATOM   5558  CD1 PHE B 330      51.166 -21.114  29.216  1.00 45.07           C  
ANISOU 5558  CD1 PHE B 330     5538   5244   6344   -115    521   -463       C  
ATOM   5559  CD2 PHE B 330      50.900 -23.079  30.552  1.00 45.24           C  
ANISOU 5559  CD2 PHE B 330     5782   5222   6184   -173    689   -650       C  
ATOM   5560  CE1 PHE B 330      52.514 -21.083  29.520  1.00 42.96           C  
ANISOU 5560  CE1 PHE B 330     5472   4935   5918    -55    540   -606       C  
ATOM   5561  CE2 PHE B 330      52.248 -23.055  30.860  1.00 45.04           C  
ANISOU 5561  CE2 PHE B 330     5940   5158   6016   -109    689   -756       C  
ATOM   5562  CZ  PHE B 330      53.054 -22.054  30.341  1.00 43.91           C  
ANISOU 5562  CZ  PHE B 330     5784   5019   5881    -51    617   -747       C  
ATOM   5563  N   MET B 331      46.718 -24.214  28.063  1.00 47.85           N  
ANISOU 5563  N   MET B 331     5400   5927   6853   -731    307   -120       N  
ATOM   5564  CA  MET B 331      45.326 -24.634  28.178  1.00 51.85           C  
ANISOU 5564  CA  MET B 331     5674   6472   7554   -842    300     28       C  
ATOM   5565  C   MET B 331      44.940 -24.603  29.650  1.00 52.40           C  
ANISOU 5565  C   MET B 331     5733   6367   7808   -656    595    -30       C  
ATOM   5566  O   MET B 331      45.598 -25.243  30.474  1.00 47.88           O  
ANISOU 5566  O   MET B 331     5420   5703   7069   -606    742   -223       O  
ATOM   5567  CB  MET B 331      45.124 -26.039  27.607  1.00 66.39           C  
ANISOU 5567  CB  MET B 331     7627   8403   9196  -1128    193    -79       C  
ATOM   5568  CG  MET B 331      44.987 -26.093  26.102  1.00 84.77           C  
ANISOU 5568  CG  MET B 331     9885  10985  11340  -1426    -98      6       C  
ATOM   5569  SD  MET B 331      43.567 -25.140  25.533  1.00104.13           S  
ANISOU 5569  SD  MET B 331    11848  13630  14087  -1518   -333    473       S  
ATOM   5570  CE  MET B 331      42.263 -25.793  26.571  1.00 94.66           C  
ANISOU 5570  CE  MET B 331    10455  12298  13213  -1496   -163    529       C  
ATOM   5571  N   LEU B 332      43.889 -23.859  29.986  1.00 55.29           N  
ANISOU 5571  N   LEU B 332     5786   6695   8528   -569    694    153       N  
ATOM   5572  CA  LEU B 332      43.414 -23.767  31.362  1.00 50.83           C  
ANISOU 5572  CA  LEU B 332     5193   5994   8126   -429   1032     71       C  
ATOM   5573  C   LEU B 332      42.022 -24.379  31.445  1.00 57.54           C  
ANISOU 5573  C   LEU B 332     5774   6886   9201   -552   1066    239       C  
ATOM   5574  O   LEU B 332      41.089 -23.904  30.790  1.00 53.12           O  
ANISOU 5574  O   LEU B 332     4845   6377   8960   -592    944    506       O  
ATOM   5575  CB  LEU B 332      43.401 -22.316  31.856  1.00 55.89           C  
ANISOU 5575  CB  LEU B 332     5688   6488   9058   -204   1240     69       C  
ATOM   5576  CG  LEU B 332      42.799 -22.127  33.252  1.00 56.19           C  
ANISOU 5576  CG  LEU B 332     5680   6407   9261   -100   1655    -62       C  
ATOM   5577  CD1 LEU B 332      43.572 -22.923  34.288  1.00 52.23           C  
ANISOU 5577  CD1 LEU B 332     5569   5943   8334   -145   1790   -309       C  
ATOM   5578  CD2 LEU B 332      42.728 -20.653  33.641  1.00 56.68           C  
ANISOU 5578  CD2 LEU B 332     5578   6274   9685    100   1907   -119       C  
ATOM   5579  N   TRP B 333      41.891 -25.436  32.239  1.00 50.36           N  
ANISOU 5579  N   TRP B 333     5022   5961   8151   -627   1212    128       N  
ATOM   5580  CA  TRP B 333      40.613 -26.087  32.486  1.00 53.64           C  
ANISOU 5580  CA  TRP B 333     5199   6403   8778   -750   1287    272       C  
ATOM   5581  C   TRP B 333      40.259 -25.921  33.953  1.00 60.85           C  
ANISOU 5581  C   TRP B 333     6114   7232   9775   -624   1704    186       C  
ATOM   5582  O   TRP B 333      41.079 -26.215  34.830  1.00 58.37           O  
ANISOU 5582  O   TRP B 333     6123   6895   9162   -588   1851      1       O  
ATOM   5583  CB  TRP B 333      40.666 -27.572  32.127  1.00 51.18           C  
ANISOU 5583  CB  TRP B 333     5054   6139   8254   -999   1120    235       C  
ATOM   5584  CG  TRP B 333      40.703 -27.839  30.664  1.00 61.24           C  
ANISOU 5584  CG  TRP B 333     6285   7537   9444  -1215    756    291       C  
ATOM   5585  CD1 TRP B 333      41.814 -27.958  29.878  1.00 65.92           C  
ANISOU 5585  CD1 TRP B 333     7136   8164   9745  -1268    579    135       C  
ATOM   5586  CD2 TRP B 333      39.577 -28.033  29.801  1.00 66.34           C  
ANISOU 5586  CD2 TRP B 333     6609   8329  10268  -1455    530    515       C  
ATOM   5587  NE1 TRP B 333      41.448 -28.213  28.579  1.00 67.86           N  
ANISOU 5587  NE1 TRP B 333     7271   8585   9926  -1547    280    214       N  
ATOM   5588  CE2 TRP B 333      40.080 -28.263  28.505  1.00 70.16           C  
ANISOU 5588  CE2 TRP B 333     7207   8961  10488  -1681    214    461       C  
ATOM   5589  CE3 TRP B 333      38.191 -28.035  29.999  1.00 76.83           C  
ANISOU 5589  CE3 TRP B 333     7546   9694  11951  -1525    565    765       C  
ATOM   5590  CZ2 TRP B 333      39.249 -28.491  27.413  1.00 65.73           C  
ANISOU 5590  CZ2 TRP B 333     6408   8621   9947  -2012    -98    647       C  
ATOM   5591  CZ3 TRP B 333      37.366 -28.262  28.912  1.00 76.31           C  
ANISOU 5591  CZ3 TRP B 333     7206   9821  11968  -1824    234    987       C  
ATOM   5592  CH2 TRP B 333      37.897 -28.487  27.635  1.00 73.46           C  
ANISOU 5592  CH2 TRP B 333     6991   9641  11278  -2083   -110    926       C  
ATOM   5593  N   CYS B 334      39.043 -25.454  34.217  1.00 61.12           N  
ANISOU 5593  N   CYS B 334     5771   7238  10213   -581   1897    337       N  
ATOM   5594  CA  CYS B 334      38.572 -25.239  35.574  1.00 63.52           C  
ANISOU 5594  CA  CYS B 334     6043   7483  10610   -493   2359    230       C  
ATOM   5595  C   CYS B 334      37.204 -25.871  35.756  1.00 66.57           C  
ANISOU 5595  C   CYS B 334     6105   7905  11284   -615   2472    431       C  
ATOM   5596  O   CYS B 334      36.457 -26.082  34.797  1.00 66.12           O  
ANISOU 5596  O   CYS B 334     5738   7894  11490   -725   2204    686       O  
ATOM   5597  CB  CYS B 334      38.484 -23.751  35.918  1.00 63.38           C  
ANISOU 5597  CB  CYS B 334     5854   7323  10905   -266   2647    140       C  
ATOM   5598  SG  CYS B 334      40.064 -22.919  35.898  1.00 63.70           S  
ANISOU 5598  SG  CYS B 334     6263   7303  10636   -139   2572   -117       S  
ATOM   5599  N   LYS B 335      36.887 -26.161  37.017  1.00 68.35           N  
ANISOU 5599  N   LYS B 335     6399   8138  11434   -627   2870    327       N  
ATOM   5600  CA  LYS B 335      35.570 -26.655  37.399  1.00 73.62           C  
ANISOU 5600  CA  LYS B 335     6741   8832  12399   -726   3080    503       C  
ATOM   5601  C   LYS B 335      35.291 -26.203  38.824  1.00 77.80           C  
ANISOU 5601  C   LYS B 335     7291   9349  12919   -649   3663    313       C  
ATOM   5602  O   LYS B 335      36.051 -26.534  39.740  1.00 75.93           O  
ANISOU 5602  O   LYS B 335     7451   9196  12203   -708   3809    122       O  
ATOM   5603  CB  LYS B 335      35.486 -28.179  37.288  1.00 70.93           C  
ANISOU 5603  CB  LYS B 335     6535   8575  11839   -979   2863    620       C  
ATOM   5604  CG  LYS B 335      34.113 -28.739  37.632  1.00 81.49           C  
ANISOU 5604  CG  LYS B 335     7518   9944  13501  -1111   3053    831       C  
ATOM   5605  CD  LYS B 335      33.955 -30.189  37.184  1.00 87.33           C  
ANISOU 5605  CD  LYS B 335     8325  10716  14140  -1388   2752    973       C  
ATOM   5606  CE  LYS B 335      32.578 -30.728  37.565  1.00 91.00           C  
ANISOU 5606  CE  LYS B 335     8416  11212  14949  -1536   2947   1200       C  
ATOM   5607  NZ  LYS B 335      32.313 -32.071  36.981  1.00 93.43           N  
ANISOU 5607  NZ  LYS B 335     8734  11516  15250  -1836   2629   1336       N  
ATOM   5608  N   ASP B 336      34.218 -25.428  38.994  1.00 82.26           N  
ANISOU 5608  N   ASP B 336     7417   9819  14021   -535   3999    374       N  
ATOM   5609  CA  ASP B 336      33.755 -24.974  40.308  1.00 86.44           C  
ANISOU 5609  CA  ASP B 336     7937  10331  14574   -485   4599    154       C  
ATOM   5610  C   ASP B 336      34.812 -24.145  41.035  1.00 83.16           C  
ANISOU 5610  C   ASP B 336     7920   9890  13788   -398   4816   -242       C  
ATOM   5611  O   ASP B 336      34.996 -24.269  42.248  1.00 82.44           O  
ANISOU 5611  O   ASP B 336     8132   9923  13267   -497   5112   -473       O  
ATOM   5612  CB  ASP B 336      33.307 -26.156  41.167  1.00 89.30           C  
ANISOU 5612  CB  ASP B 336     8406  10872  14650   -707   4762    222       C  
ATOM   5613  CG  ASP B 336      32.159 -26.918  40.542  1.00 94.86           C  
ANISOU 5613  CG  ASP B 336     8715  11588  15741   -812   4558    586       C  
ATOM   5614  OD1 ASP B 336      31.175 -26.271  40.122  1.00 99.73           O  
ANISOU 5614  OD1 ASP B 336     8932  12091  16870   -676   4541    722       O  
ATOM   5615  OD2 ASP B 336      32.251 -28.159  40.455  1.00 96.27           O  
ANISOU 5615  OD2 ASP B 336     8992  11868  15719  -1042   4381    746       O  
ATOM   5616  N   GLY B 337      35.506 -23.288  40.290  1.00 78.91           N  
ANISOU 5616  N   GLY B 337     7377   9212  13393   -243   4635   -303       N  
ATOM   5617  CA  GLY B 337      36.470 -22.385  40.882  1.00 80.78           C  
ANISOU 5617  CA  GLY B 337     7962   9389  13340   -168   4790   -675       C  
ATOM   5618  C   GLY B 337      37.806 -22.999  41.227  1.00 77.24           C  
ANISOU 5618  C   GLY B 337     8025   9135  12187   -313   4604   -814       C  
ATOM   5619  O   GLY B 337      38.616 -22.343  41.895  1.00 76.23           O  
ANISOU 5619  O   GLY B 337     8187   9016  11762   -316   4789  -1137       O  
ATOM   5620  N   HIS B 338      38.065 -24.232  40.803  1.00 77.55           N  
ANISOU 5620  N   HIS B 338     8198   9312  11955   -444   4193   -572       N  
ATOM   5621  CA  HIS B 338      39.357 -24.869  40.999  1.00 75.60           C  
ANISOU 5621  CA  HIS B 338     8402   9200  11122   -552   3912   -620       C  
ATOM   5622  C   HIS B 338      39.950 -25.240  39.647  1.00 61.72           C  
ANISOU 5622  C   HIS B 338     6662   7380   9409   -508   3369   -445       C  
ATOM   5623  O   HIS B 338      39.226 -25.437  38.667  1.00 62.47           O  
ANISOU 5623  O   HIS B 338     6460   7415   9862   -496   3171   -233       O  
ATOM   5624  CB  HIS B 338      39.231 -26.109  41.890  1.00 80.83           C  
ANISOU 5624  CB  HIS B 338     9236  10057  11417   -774   3990   -503       C  
ATOM   5625  CG  HIS B 338      38.688 -25.814  43.254  1.00 92.65           C  
ANISOU 5625  CG  HIS B 338    10754  11687  12762   -879   4542   -678       C  
ATOM   5626  ND1 HIS B 338      37.343 -25.877  43.550  1.00101.18           N  
ANISOU 5626  ND1 HIS B 338    11501  12756  14186   -902   4908   -610       N  
ATOM   5627  CD2 HIS B 338      39.306 -25.431  44.396  1.00 96.86           C  
ANISOU 5627  CD2 HIS B 338    11596  12390  12815  -1000   4808   -936       C  
ATOM   5628  CE1 HIS B 338      37.158 -25.558  44.819  1.00103.70           C  
ANISOU 5628  CE1 HIS B 338    11964  13223  14215  -1004   5302   -825       C  
ATOM   5629  NE2 HIS B 338      38.334 -25.282  45.355  1.00102.99           N  
ANISOU 5629  NE2 HIS B 338    12268  13259  13605  -1085   5247  -1030       N  
ATOM   5630  N   VAL B 339      41.279 -25.302  39.594  1.00 57.35           N  
ANISOU 5630  N   VAL B 339     6446   6860   8482   -511   3137   -540       N  
ATOM   5631  CA  VAL B 339      41.959 -25.744  38.383  1.00 53.76           C  
ANISOU 5631  CA  VAL B 339     6053   6364   8012   -497   2681   -423       C  
ATOM   5632  C   VAL B 339      41.759 -27.243  38.220  1.00 60.96           C  
ANISOU 5632  C   VAL B 339     7006   7315   8840   -663   2505   -234       C  
ATOM   5633  O   VAL B 339      41.886 -28.009  39.183  1.00 60.42           O  
ANISOU 5633  O   VAL B 339     7104   7326   8527   -777   2626   -194       O  
ATOM   5634  CB  VAL B 339      43.454 -25.392  38.441  1.00 52.62           C  
ANISOU 5634  CB  VAL B 339     6225   6228   7540   -448   2530   -575       C  
ATOM   5635  CG1 VAL B 339      44.184 -25.917  37.203  1.00 50.88           C  
ANISOU 5635  CG1 VAL B 339     6070   5966   7298   -447   2122   -482       C  
ATOM   5636  CG2 VAL B 339      43.652 -23.892  38.563  1.00 55.98           C  
ANISOU 5636  CG2 VAL B 339     6606   6573   8092   -307   2705   -780       C  
ATOM   5637  N   GLU B 340      41.420 -27.668  37.004  1.00 59.47           N  
ANISOU 5637  N   GLU B 340     6659   7078   8859   -708   2223   -106       N  
ATOM   5638  CA  GLU B 340      41.517 -29.082  36.653  1.00 62.00           C  
ANISOU 5638  CA  GLU B 340     7076   7376   9106   -877   2022     -2       C  
ATOM   5639  C   GLU B 340      42.889 -29.374  36.052  1.00 56.59           C  
ANISOU 5639  C   GLU B 340     6659   6636   8206   -857   1767    -97       C  
ATOM   5640  O   GLU B 340      43.626 -30.225  36.560  1.00 51.40           O  
ANISOU 5640  O   GLU B 340     6222   5936   7372   -902   1753    -80       O  
ATOM   5641  CB  GLU B 340      40.390 -29.483  35.694  1.00 67.25           C  
ANISOU 5641  CB  GLU B 340     7440   8037  10074  -1012   1873    143       C  
ATOM   5642  CG  GLU B 340      38.998 -29.315  36.295  1.00 84.58           C  
ANISOU 5642  CG  GLU B 340     9314  10271  12550  -1036   2138    278       C  
ATOM   5643  CD  GLU B 340      37.915 -30.001  35.485  1.00 95.18           C  
ANISOU 5643  CD  GLU B 340    10369  11628  14168  -1235   1957    465       C  
ATOM   5644  OE1 GLU B 340      37.592 -31.170  35.793  1.00 99.94           O  
ANISOU 5644  OE1 GLU B 340    11012  12202  14758  -1414   1977    537       O  
ATOM   5645  OE2 GLU B 340      37.387 -29.372  34.541  1.00100.02           O  
ANISOU 5645  OE2 GLU B 340    10700  12284  15019  -1236   1779    567       O  
ATOM   5646  N   THR B 341      43.258 -28.648  34.995  1.00 47.84           N  
ANISOU 5646  N   THR B 341     5510   5528   7139   -788   1577   -165       N  
ATOM   5647  CA  THR B 341      44.632 -28.698  34.505  1.00 52.11           C  
ANISOU 5647  CA  THR B 341     6291   6028   7479   -741   1402   -279       C  
ATOM   5648  C   THR B 341      45.016 -27.358  33.886  1.00 51.96           C  
ANISOU 5648  C   THR B 341     6214   6046   7483   -607   1325   -341       C  
ATOM   5649  O   THR B 341      44.170 -26.501  33.609  1.00 50.86           O  
ANISOU 5649  O   THR B 341     5820   5938   7567   -565   1356   -263       O  
ATOM   5650  CB  THR B 341      44.842 -29.837  33.503  1.00 53.34           C  
ANISOU 5650  CB  THR B 341     6508   6117   7641   -904   1200   -300       C  
ATOM   5651  OG1 THR B 341      46.229 -29.897  33.152  1.00 52.83           O  
ANISOU 5651  OG1 THR B 341     6662   5993   7419   -838   1105   -423       O  
ATOM   5652  CG2 THR B 341      44.001 -29.622  32.250  1.00 54.24           C  
ANISOU 5652  CG2 THR B 341     6401   6321   7887  -1040   1022   -261       C  
ATOM   5653  N   PHE B 342      46.327 -27.194  33.683  1.00 46.64           N  
ANISOU 5653  N   PHE B 342     5752   5348   6623   -537   1227   -447       N  
ATOM   5654  CA  PHE B 342      46.909 -25.963  33.154  1.00 47.75           C  
ANISOU 5654  CA  PHE B 342     5871   5505   6765   -418   1153   -498       C  
ATOM   5655  C   PHE B 342      48.225 -26.398  32.520  1.00 48.71           C  
ANISOU 5655  C   PHE B 342     6198   5606   6703   -431    990   -584       C  
ATOM   5656  O   PHE B 342      49.170 -26.708  33.246  1.00 48.68           O  
ANISOU 5656  O   PHE B 342     6382   5556   6559   -380   1036   -637       O  
ATOM   5657  CB  PHE B 342      47.133 -24.940  34.259  1.00 44.10           C  
ANISOU 5657  CB  PHE B 342     5449   5022   6287   -280   1364   -581       C  
ATOM   5658  CG  PHE B 342      47.714 -23.628  33.790  1.00 46.04           C  
ANISOU 5658  CG  PHE B 342     5660   5234   6600   -161   1311   -632       C  
ATOM   5659  CD1 PHE B 342      47.002 -22.800  32.936  1.00 49.76           C  
ANISOU 5659  CD1 PHE B 342     5860   5687   7358   -124   1249   -507       C  
ATOM   5660  CD2 PHE B 342      48.946 -23.192  34.264  1.00 50.92           C  
ANISOU 5660  CD2 PHE B 342     6486   5834   7027   -100   1317   -764       C  
ATOM   5661  CE1 PHE B 342      47.520 -21.569  32.537  1.00 53.03           C  
ANISOU 5661  CE1 PHE B 342     6221   6039   7890    -16   1210   -509       C  
ATOM   5662  CE2 PHE B 342      49.478 -21.976  33.864  1.00 52.19           C  
ANISOU 5662  CE2 PHE B 342     6607   5939   7282     -4   1280   -808       C  
ATOM   5663  CZ  PHE B 342      48.766 -21.160  33.000  1.00 51.53           C  
ANISOU 5663  CZ  PHE B 342     6262   5810   7508     44   1236   -680       C  
ATOM   5664  N   TYR B 343      48.272 -26.452  31.188  1.00 43.78           N  
ANISOU 5664  N   TYR B 343     5521   5035   6080   -524    808   -581       N  
ATOM   5665  CA  TYR B 343      49.453 -27.020  30.553  1.00 44.80           C  
ANISOU 5665  CA  TYR B 343     5833   5131   6059   -561    723   -702       C  
ATOM   5666  C   TYR B 343      49.857 -26.253  29.302  1.00 44.64           C  
ANISOU 5666  C   TYR B 343     5769   5225   5969   -595    572   -708       C  
ATOM   5667  O   TYR B 343      48.999 -25.751  28.564  1.00 46.96           O  
ANISOU 5667  O   TYR B 343     5873   5648   6321   -692    456   -582       O  
ATOM   5668  CB  TYR B 343      49.243 -28.506  30.201  1.00 44.85           C  
ANISOU 5668  CB  TYR B 343     5902   5064   6076   -740    720   -771       C  
ATOM   5669  CG  TYR B 343      48.169 -28.809  29.182  1.00 45.84           C  
ANISOU 5669  CG  TYR B 343     5886   5302   6228   -976    604   -752       C  
ATOM   5670  CD1 TYR B 343      48.469 -28.867  27.829  1.00 47.99           C  
ANISOU 5670  CD1 TYR B 343     6189   5689   6357  -1154    470   -859       C  
ATOM   5671  CD2 TYR B 343      46.864 -29.077  29.575  1.00 46.39           C  
ANISOU 5671  CD2 TYR B 343     5788   5393   6446  -1060    626   -625       C  
ATOM   5672  CE1 TYR B 343      47.494 -29.163  26.891  1.00 55.07           C  
ANISOU 5672  CE1 TYR B 343     6962   6746   7215  -1440    325   -833       C  
ATOM   5673  CE2 TYR B 343      45.885 -29.382  28.644  1.00 51.51           C  
ANISOU 5673  CE2 TYR B 343     6282   6169   7120  -1316    479   -580       C  
ATOM   5674  CZ  TYR B 343      46.205 -29.419  27.304  1.00 55.09           C  
ANISOU 5674  CZ  TYR B 343     6780   6764   7390  -1520    310   -681       C  
ATOM   5675  OH  TYR B 343      45.231 -29.711  26.380  1.00 55.76           O  
ANISOU 5675  OH  TYR B 343     6714   7033   7440  -1839    126   -624       O  
ATOM   5676  N   PRO B 344      51.156 -26.174  29.026  1.00 49.01           N  
ANISOU 5676  N   PRO B 344     6468   5747   6405   -536    561   -812       N  
ATOM   5677  CA  PRO B 344      51.614 -25.506  27.809  1.00 46.68           C  
ANISOU 5677  CA  PRO B 344     6143   5586   6006   -598    436   -807       C  
ATOM   5678  C   PRO B 344      51.396 -26.397  26.602  1.00 49.40           C  
ANISOU 5678  C   PRO B 344     6518   6038   6214   -864    366   -910       C  
ATOM   5679  O   PRO B 344      51.380 -27.627  26.699  1.00 47.29           O  
ANISOU 5679  O   PRO B 344     6353   5658   5958   -958    454  -1062       O  
ATOM   5680  CB  PRO B 344      53.107 -25.282  28.077  1.00 48.88           C  
ANISOU 5680  CB  PRO B 344     6565   5777   6228   -453    491   -899       C  
ATOM   5681  CG  PRO B 344      53.489 -26.449  28.940  1.00 48.26           C  
ANISOU 5681  CG  PRO B 344     6611   5530   6195   -412    608   -983       C  
ATOM   5682  CD  PRO B 344      52.272 -26.779  29.780  1.00 48.21           C  
ANISOU 5682  CD  PRO B 344     6539   5500   6278   -433    655   -898       C  
ATOM   5683  N   LYS B 345      51.203 -25.761  25.454  1.00 44.36           N  
ANISOU 5683  N   LYS B 345     5785   5623   5448  -1018    210   -819       N  
ATOM   5684  CA  LYS B 345      50.887 -26.489  24.239  1.00 55.15           C  
ANISOU 5684  CA  LYS B 345     7183   7173   6601  -1355    125   -925       C  
ATOM   5685  C   LYS B 345      52.091 -26.537  23.311  1.00 64.02           C  
ANISOU 5685  C   LYS B 345     8462   8379   7486  -1448    176  -1114       C  
ATOM   5686  O   LYS B 345      52.956 -25.653  23.333  1.00 57.37           O  
ANISOU 5686  O   LYS B 345     7620   7539   6640  -1280    183  -1039       O  
ATOM   5687  CB  LYS B 345      49.683 -25.877  23.513  1.00 55.39           C  
ANISOU 5687  CB  LYS B 345     6972   7476   6599  -1560   -120   -644       C  
ATOM   5688  CG  LYS B 345      48.348 -26.275  24.144  1.00 62.33           C  
ANISOU 5688  CG  LYS B 345     7687   8298   7699  -1584   -142   -525       C  
ATOM   5689  CD  LYS B 345      47.248 -26.422  23.109  1.00 74.80           C  
ANISOU 5689  CD  LYS B 345     9084  10174   9165  -1954   -394   -361       C  
ATOM   5690  CE  LYS B 345      46.743 -25.069  22.637  1.00 78.64           C  
ANISOU 5690  CE  LYS B 345     9266  10862   9751  -1939   -624     67       C  
ATOM   5691  NZ  LYS B 345      45.563 -25.212  21.730  1.00 78.32           N  
ANISOU 5691  NZ  LYS B 345     8984  11138   9636  -2317   -920    323       N  
ATOM   5692  N   LEU B 346      52.137 -27.609  22.517  1.00 73.45           N  
ANISOU 5692  N   LEU B 346     9785   9622   8500  -1734    246  -1388       N  
ATOM   5693  CA  LEU B 346      53.143 -27.782  21.479  1.00 75.26           C  
ANISOU 5693  CA  LEU B 346    10160   9962   8472  -1900    351  -1628       C  
ATOM   5694  C   LEU B 346      53.252 -26.514  20.643  1.00 70.09           C  
ANISOU 5694  C   LEU B 346     9402   9644   7584  -1988    156  -1374       C  
ATOM   5695  O   LEU B 346      52.270 -26.074  20.039  1.00 72.65           O  
ANISOU 5695  O   LEU B 346     9578  10260   7763  -2222    -94  -1132       O  
ATOM   5696  CB  LEU B 346      52.760 -28.989  20.611  1.00 79.00           C  
ANISOU 5696  CB  LEU B 346    10758  10509   8749  -2304    430  -1962       C  
ATOM   5697  CG  LEU B 346      53.682 -29.564  19.528  1.00 85.08           C  
ANISOU 5697  CG  LEU B 346    11721  11349   9258  -2559    657  -2366       C  
ATOM   5698  CD1 LEU B 346      53.497 -31.076  19.443  1.00 85.36           C  
ANISOU 5698  CD1 LEU B 346    11898  11140   9395  -2764    890  -2790       C  
ATOM   5699  CD2 LEU B 346      53.407 -28.935  18.166  1.00 85.53           C  
ANISOU 5699  CD2 LEU B 346    11763  11920   8813  -2968    463  -2294       C  
ATOM   5700  N   GLN B 347      54.436 -25.904  20.647  1.00 69.68           N  
ANISOU 5700  N   GLN B 347     9393   9545   7538  -1801    252  -1374       N  
ATOM   5701  CA  GLN B 347      54.667 -24.671  19.892  1.00 73.80           C  
ANISOU 5701  CA  GLN B 347     9810  10350   7881  -1869     86  -1102       C  
ATOM   5702  C   GLN B 347      54.405 -24.880  18.407  1.00 77.30           C  
ANISOU 5702  C   GLN B 347    10295  11213   7863  -2348     -4  -1155       C  
ATOM   5703  O   GLN B 347      53.840 -24.014  17.743  1.00 84.37           O  
ANISOU 5703  O   GLN B 347    11027  12432   8597  -2529   -277   -791       O  
ATOM   5704  CB  GLN B 347      56.101 -24.158  20.091  1.00 75.74           C  
ANISOU 5704  CB  GLN B 347    10112  10462   8203  -1631    242  -1150       C  
ATOM   5705  CG  GLN B 347      56.366 -23.453  21.420  1.00 74.62           C  
ANISOU 5705  CG  GLN B 347     9890  10031   8430  -1229    235   -986       C  
ATOM   5706  CD  GLN B 347      57.854 -23.202  21.656  1.00 70.27           C  
ANISOU 5706  CD  GLN B 347     9402   9338   7958  -1037    391  -1078       C  
ATOM   5707  OE1 GLN B 347      58.480 -23.868  22.480  1.00 55.14           O  
ANISOU 5707  OE1 GLN B 347     7562   7163   6226   -854    548  -1247       O  
ATOM   5708  NE2 GLN B 347      58.425 -22.245  20.923  1.00 71.22           N  
ANISOU 5708  NE2 GLN B 347     9463   9638   7958  -1095    332   -923       N  
TER    5709      GLN B 347                                                      
HETATM 5710  N1  U5P A 401      92.364 -20.489 -25.572  1.00 38.09           N  
HETATM 5711  C2  U5P A 401      90.987 -20.500 -25.695  1.00 34.32           C  
HETATM 5712  N3  U5P A 401      90.304 -19.900 -24.664  1.00 35.93           N  
HETATM 5713  C4  U5P A 401      90.850 -19.317 -23.537  1.00 39.74           C  
HETATM 5714  C5  U5P A 401      92.283 -19.352 -23.479  1.00 46.07           C  
HETATM 5715  C6  U5P A 401      92.976 -19.931 -24.473  1.00 49.56           C  
HETATM 5716  O2  U5P A 401      90.419 -21.003 -26.655  1.00 38.61           O  
HETATM 5717  O4  U5P A 401      90.106 -18.825 -22.687  1.00 42.84           O  
HETATM 5718  C1' U5P A 401      93.133 -21.158 -26.660  1.00 37.39           C  
HETATM 5719  C2' U5P A 401      93.326 -20.273 -27.892  1.00 40.17           C  
HETATM 5720  O2' U5P A 401      93.381 -21.118 -29.027  1.00 42.07           O  
HETATM 5721  C3' U5P A 401      94.704 -19.693 -27.630  1.00 49.71           C  
HETATM 5722  C4' U5P A 401      95.434 -20.867 -26.996  1.00 51.87           C  
HETATM 5723  O3' U5P A 401      95.335 -19.196 -28.797  1.00 43.54           O  
HETATM 5724  O4' U5P A 401      94.417 -21.499 -26.174  1.00 40.97           O  
HETATM 5725  C5' U5P A 401      96.627 -20.505 -26.152  1.00 56.16           C  
HETATM 5726  O5' U5P A 401      96.239 -19.704 -25.047  1.00 60.76           O  
HETATM 5727  P   U5P A 401      97.322 -18.995 -24.117  1.00 73.98           P  
HETATM 5728  O1P U5P A 401      98.112 -18.107 -25.060  1.00 72.06           O  
HETATM 5729  O2P U5P A 401      96.532 -18.296 -23.025  1.00 74.74           O  
HETATM 5730  O3P U5P A 401      98.161 -20.135 -23.567  1.00 80.84           O  
HETATM 5731  C   TRS A 402      66.626 -37.992 -15.210  1.00 70.29           C  
HETATM 5732  C1  TRS A 402      67.005 -38.226 -16.670  1.00 75.13           C  
HETATM 5733  C2  TRS A 402      65.471 -38.918 -14.831  1.00 66.19           C  
HETATM 5734  C3  TRS A 402      66.186 -36.553 -14.977  1.00 61.06           C  
HETATM 5735  N   TRS A 402      67.814 -38.249 -14.371  1.00 65.85           N  
HETATM 5736  O1  TRS A 402      68.352 -37.859 -16.893  1.00 77.44           O  
HETATM 5737  O2  TRS A 402      65.920 -39.857 -13.888  1.00 50.42           O  
HETATM 5738  O3  TRS A 402      66.933 -36.024 -13.897  1.00 51.18           O  
HETATM 5739  C1  EDO A 403      58.719 -32.240   0.142  1.00 68.58           C  
HETATM 5740  O1  EDO A 403      57.667 -32.335   1.118  1.00 50.69           O  
HETATM 5741  C2  EDO A 403      58.348 -31.308  -1.011  1.00 75.29           C  
HETATM 5742  O2  EDO A 403      57.966 -30.013  -0.524  1.00 62.50           O  
HETATM 5743  C   ACT A 404     100.053 -15.416 -30.087  1.00 87.88           C  
HETATM 5744  O   ACT A 404     100.132 -15.181 -31.286  1.00 87.75           O  
HETATM 5745  OXT ACT A 404      99.009 -15.868 -29.487  1.00 89.58           O  
HETATM 5746  CH3 ACT A 404     101.248 -15.188 -29.132  1.00 78.66           C  
HETATM 5747  C1  EDO A 405      79.162 -29.655 -29.307  1.00 81.16           C  
HETATM 5748  O1  EDO A 405      77.976 -30.005 -30.031  1.00 74.74           O  
HETATM 5749  C2  EDO A 405      79.327 -30.568 -28.094  1.00 81.91           C  
HETATM 5750  O2  EDO A 405      79.329 -31.939 -28.514  1.00 81.44           O  
HETATM 5751  C1  EDO A 406      71.788 -15.190 -11.339  1.00 92.43           C  
HETATM 5752  O1  EDO A 406      71.930 -13.769 -11.460  1.00 91.88           O  
HETATM 5753  C2  EDO A 406      71.834 -15.837 -12.721  1.00 92.96           C  
HETATM 5754  O2  EDO A 406      73.154 -15.750 -13.278  1.00 89.31           O  
HETATM 5755  C1  EDO A 407     100.435  -4.967 -35.242  1.00 63.48           C  
HETATM 5756  O1  EDO A 407     101.720  -5.245 -35.810  1.00 76.73           O  
HETATM 5757  C2  EDO A 407      99.584  -4.335 -36.332  1.00 62.61           C  
HETATM 5758  O2  EDO A 407      99.033  -5.350 -37.166  1.00 52.63           O  
HETATM 5759  C1  EDO A 408      68.458 -24.763 -22.706  1.00 71.86           C  
HETATM 5760  O1  EDO A 408      69.792 -24.662 -23.246  1.00 59.17           O  
HETATM 5761  C2  EDO A 408      68.484 -25.014 -21.202  1.00 74.96           C  
HETATM 5762  O2  EDO A 408      67.694 -26.167 -20.845  1.00 78.97           O  
HETATM 5763  C1  EDO A 409      71.294  -7.440 -19.033  1.00 74.82           C  
HETATM 5764  O1  EDO A 409      71.778  -7.278 -20.372  1.00 76.49           O  
HETATM 5765  C2  EDO A 409      72.351  -8.153 -18.195  1.00 73.76           C  
HETATM 5766  O2  EDO A 409      71.781  -8.684 -16.988  1.00 75.00           O  
HETATM 5767  S   SO4 A 410      93.423  -7.856 -44.224  1.00157.95           S  
HETATM 5768  O1  SO4 A 410      92.975  -6.477 -44.400  1.00159.36           O  
HETATM 5769  O2  SO4 A 410      93.913  -8.376 -45.499  1.00157.37           O  
HETATM 5770  O3  SO4 A 410      92.305  -8.672 -43.763  1.00158.32           O  
HETATM 5771  O4  SO4 A 410      94.496  -7.898 -43.234  1.00158.46           O  
HETATM 5772  N1  U5P B 401      48.928 -32.608  25.951  1.00 48.53           N  
HETATM 5773  C2  U5P B 401      50.129 -31.931  26.061  1.00 42.42           C  
HETATM 5774  N3  U5P B 401      50.414 -31.077  25.024  1.00 40.49           N  
HETATM 5775  C4  U5P B 401      49.639 -30.847  23.904  1.00 50.37           C  
HETATM 5776  C5  U5P B 401      48.411 -31.590  23.859  1.00 51.81           C  
HETATM 5777  C6  U5P B 401      48.107 -32.430  24.862  1.00 52.40           C  
HETATM 5778  O2  U5P B 401      50.878 -32.073  27.016  1.00 41.48           O  
HETATM 5779  O4  U5P B 401      50.031 -30.048  23.054  1.00 46.13           O  
HETATM 5780  C1' U5P B 401      48.597 -33.553  27.046  1.00 54.52           C  
HETATM 5781  C2' U5P B 401      47.950 -32.864  28.254  1.00 54.07           C  
HETATM 5782  O2' U5P B 401      48.313 -33.591  29.418  1.00 50.54           O  
HETATM 5783  C3' U5P B 401      46.476 -33.079  27.956  1.00 63.85           C  
HETATM 5784  C4' U5P B 401      46.467 -34.476  27.356  1.00 63.56           C  
HETATM 5785  O3' U5P B 401      45.634 -32.945  29.088  1.00 61.01           O  
HETATM 5786  O4' U5P B 401      47.678 -34.511  26.556  1.00 56.00           O  
HETATM 5787  C5' U5P B 401      45.274 -34.812  26.503  1.00 63.12           C  
HETATM 5788  O5' U5P B 401      45.231 -33.999  25.342  1.00 70.84           O  
HETATM 5789  P   U5P B 401      43.910 -33.913  24.454  1.00 78.72           P  
HETATM 5790  O1P U5P B 401      44.280 -33.007  23.296  1.00 80.62           O  
HETATM 5791  O2P U5P B 401      43.627 -35.332  23.994  1.00 90.41           O  
HETATM 5792  O3P U5P B 401      42.880 -33.285  25.373  1.00 77.07           O  
HETATM 5793  C   TRS B 402      80.817 -33.779  15.938  1.00 81.01           C  
HETATM 5794  C1  TRS B 402      81.958 -34.052  14.955  1.00 72.28           C  
HETATM 5795  C2  TRS B 402      79.788 -34.909  15.900  1.00 87.78           C  
HETATM 5796  C3  TRS B 402      80.141 -32.439  15.640  1.00 65.50           C  
HETATM 5797  N   TRS B 402      81.391 -33.724  17.288  1.00 81.60           N  
HETATM 5798  O1  TRS B 402      81.799 -35.325  14.361  1.00 50.26           O  
HETATM 5799  O2  TRS B 402      79.130 -34.963  14.650  1.00 83.18           O  
HETATM 5800  O3  TRS B 402      79.223 -32.569  14.569  1.00 54.03           O  
HETATM 5801  C1  EDO B 403      72.175   4.778  28.050  1.00 36.28           C  
HETATM 5802  O1  EDO B 403      71.955   5.430  26.815  1.00 39.42           O  
HETATM 5803  C2  EDO B 403      71.010   3.883  28.421  1.00 48.88           C  
HETATM 5804  O2  EDO B 403      71.336   3.403  29.734  1.00 64.70           O  
HETATM 5805  C1  EDO B 404      63.583  -9.353  32.061  1.00 63.75           C  
HETATM 5806  O1  EDO B 404      63.905  -9.221  30.673  1.00 56.54           O  
HETATM 5807  C2  EDO B 404      62.156  -9.876  32.221  1.00 62.17           C  
HETATM 5808  O2  EDO B 404      61.227  -9.135  31.417  1.00 50.11           O  
HETATM 5809  C   ACT B 405      33.893 -23.071  36.492  1.00 86.99           C  
HETATM 5810  O   ACT B 405      34.068 -23.106  35.282  1.00 89.28           O  
HETATM 5811  OXT ACT B 405      34.808 -22.839  37.366  1.00 76.03           O  
HETATM 5812  CH3 ACT B 405      32.501 -23.311  37.110  1.00 87.86           C  
HETATM 5813  C1  EDO B 406      52.627 -10.282  27.849  1.00 86.67           C  
HETATM 5814  O1  EDO B 406      53.847 -10.282  28.611  1.00 87.64           O  
HETATM 5815  C2  EDO B 406      51.794 -11.525  28.167  1.00 85.98           C  
HETATM 5816  O2  EDO B 406      51.337 -12.184  26.976  1.00 75.59           O  
HETATM 5817  C   ACT B 407      73.308  -7.373  31.910  1.00 95.07           C  
HETATM 5818  O   ACT B 407      74.400  -7.410  31.229  1.00 89.97           O  
HETATM 5819  OXT ACT B 407      72.178  -7.466  31.447  1.00 89.45           O  
HETATM 5820  CH3 ACT B 407      73.547  -7.199  33.424  1.00 95.03           C  
HETATM 5821  C   ACT B 408      78.458  -2.544  24.839  1.00 79.70           C  
HETATM 5822  O   ACT B 408      77.919  -1.452  24.735  1.00 81.11           O  
HETATM 5823  OXT ACT B 408      78.519  -3.245  25.917  1.00 74.30           O  
HETATM 5824  CH3 ACT B 408      79.140  -3.211  23.636  1.00 70.10           C  
HETATM 5825  C   FMT B 409      71.435 -35.241  15.443  1.00 94.21           C  
HETATM 5826  O1  FMT B 409      70.642 -35.051  16.365  1.00 94.77           O  
HETATM 5827  O2  FMT B 409      71.187 -35.928  14.452  1.00 93.12           O  
HETATM 5828  C   FMT B 410      77.038 -34.929  19.126  1.00 81.00           C  
HETATM 5829  O1  FMT B 410      78.036 -35.311  18.509  1.00 83.35           O  
HETATM 5830  O2  FMT B 410      75.874 -35.081  18.741  1.00 74.95           O  
HETATM 5831  C1  EDO B 411      80.077 -39.244  16.259  1.00 88.29           C  
HETATM 5832  O1  EDO B 411      81.177 -38.959  17.131  1.00 92.09           O  
HETATM 5833  C2  EDO B 411      78.906 -38.320  16.576  1.00 84.15           C  
HETATM 5834  O2  EDO B 411      78.195 -38.018  15.367  1.00 72.82           O  
HETATM 5835  O   HOH A 501      90.353 -36.512 -36.128  1.00 47.62           O  
HETATM 5836  O   HOH A 502      67.360 -33.768 -17.049  1.00 40.96           O  
HETATM 5837  O   HOH A 503      97.691 -22.927 -30.103  1.00 65.17           O  
HETATM 5838  O   HOH A 504      88.535 -16.728 -19.375  1.00 59.80           O  
HETATM 5839  O   HOH A 505      71.547  -0.278 -35.120  1.00 54.98           O  
HETATM 5840  O   HOH A 506      64.465 -17.098 -26.094  1.00 38.61           O  
HETATM 5841  O   HOH A 507      78.791 -29.097 -25.000  1.00 53.18           O  
HETATM 5842  O   HOH A 508      69.549 -10.232  -8.900  1.00 47.20           O  
HETATM 5843  O   HOH A 509      65.515 -42.523 -14.240  1.00 46.97           O  
HETATM 5844  O   HOH A 510      75.590 -24.380 -23.677  1.00 39.55           O  
HETATM 5845  O   HOH A 511      71.896 -12.159  -9.585  1.00 77.52           O  
HETATM 5846  O   HOH A 512      90.865 -10.230 -47.567  1.00 59.88           O  
HETATM 5847  O   HOH A 513      91.536  -4.804 -43.262  1.00 51.50           O  
HETATM 5848  O   HOH A 514      78.002 -24.504 -52.244  1.00 71.87           O  
HETATM 5849  O   HOH A 515      89.119  -5.550 -41.951  1.00 52.69           O  
HETATM 5850  O   HOH A 516      70.322 -26.465  -9.504  1.00 42.77           O  
HETATM 5851  O   HOH A 517      62.831 -26.017 -36.991  1.00 59.66           O  
HETATM 5852  O   HOH A 518      67.305  -8.269 -30.875  1.00 50.30           O  
HETATM 5853  O   HOH A 519      74.914 -16.113 -46.385  1.00 46.95           O  
HETATM 5854  O   HOH A 520      69.190 -39.611  -0.727  1.00 38.00           O  
HETATM 5855  O   HOH A 521      59.453 -20.756  -9.391  1.00 38.73           O  
HETATM 5856  O   HOH A 522      83.078 -27.074 -20.487  1.00 35.00           O  
HETATM 5857  O   HOH A 523      85.204 -31.318 -15.085  1.00 44.29           O  
HETATM 5858  O   HOH A 524      50.786 -15.327 -26.136  1.00 61.81           O  
HETATM 5859  O   HOH A 525      93.224  -1.708 -32.505  1.00 48.95           O  
HETATM 5860  O   HOH A 526      73.543 -24.354 -16.956  1.00 41.13           O  
HETATM 5861  O   HOH A 527      51.884 -21.638  -8.633  1.00 56.49           O  
HETATM 5862  O   HOH A 528      55.297 -33.157  -2.044  1.00 48.54           O  
HETATM 5863  O   HOH A 529      57.133 -14.716   1.594  1.00 73.25           O  
HETATM 5864  O   HOH A 530      85.089 -24.484 -46.545  1.00 44.97           O  
HETATM 5865  O   HOH A 531      56.633 -42.360   1.410  1.00 40.06           O  
HETATM 5866  O   HOH A 532      73.775 -31.447 -11.706  1.00 44.22           O  
HETATM 5867  O   HOH A 533      75.178 -15.959 -14.912  1.00 67.47           O  
HETATM 5868  O   HOH A 534      55.191 -29.245  -2.262  1.00 49.63           O  
HETATM 5869  O   HOH A 535      71.019 -28.150 -30.097  1.00 61.79           O  
HETATM 5870  O   HOH A 536      66.700 -12.705 -33.324  1.00 50.24           O  
HETATM 5871  O   HOH A 537      56.120 -27.662 -40.155  1.00 56.08           O  
HETATM 5872  O   HOH A 538      82.718  -6.623 -20.168  1.00 67.76           O  
HETATM 5873  O   HOH A 539      80.314 -23.426 -19.501  1.00 47.04           O  
HETATM 5874  O   HOH A 540      93.553 -19.130 -31.370  1.00 41.55           O  
HETATM 5875  O   HOH A 541      55.364 -57.943 -12.335  1.00 46.81           O  
HETATM 5876  O   HOH A 542      97.740 -21.805 -37.608  1.00 46.77           O  
HETATM 5877  O   HOH A 543      71.311 -49.124  -0.960  1.00 44.67           O  
HETATM 5878  O   HOH A 544      81.742 -10.225 -46.324  1.00 69.36           O  
HETATM 5879  O   HOH A 545      95.567  -4.263 -42.872  1.00 64.23           O  
HETATM 5880  O   HOH A 546      71.923 -28.224 -36.074  1.00 64.92           O  
HETATM 5881  O   HOH A 547      55.429 -30.265 -15.453  1.00 37.52           O  
HETATM 5882  O   HOH A 548      96.674 -32.943 -24.296  1.00 37.86           O  
HETATM 5883  O   HOH A 549      59.332 -21.427 -37.962  1.00 67.01           O  
HETATM 5884  O   HOH A 550      58.963  -7.705 -31.926  1.00 55.16           O  
HETATM 5885  O   HOH A 551      65.943  -3.443  -5.717  1.00 73.17           O  
HETATM 5886  O   HOH A 552      55.412 -25.619 -13.670  1.00 67.09           O  
HETATM 5887  O   HOH A 553      55.251 -20.296 -27.387  1.00 45.68           O  
HETATM 5888  O   HOH A 554      81.766 -33.373 -18.193  1.00 62.34           O  
HETATM 5889  O   HOH A 555      75.217 -19.398 -18.613  1.00 37.54           O  
HETATM 5890  O   HOH A 556      98.873 -33.015 -28.402  1.00 37.14           O  
HETATM 5891  O   HOH A 557      64.054 -25.756 -19.649  1.00 32.40           O  
HETATM 5892  O   HOH A 558      75.185 -10.556 -18.557  1.00 50.84           O  
HETATM 5893  O   HOH A 559      97.116 -17.153 -38.047  1.00 44.18           O  
HETATM 5894  O   HOH A 560      89.523  -1.143 -29.130  1.00 50.56           O  
HETATM 5895  O   HOH A 561      62.728 -34.474 -23.122  1.00 56.45           O  
HETATM 5896  O   HOH A 562      95.002  -6.745 -32.015  1.00 42.39           O  
HETATM 5897  O   HOH A 563      72.979 -10.505 -37.244  1.00 58.10           O  
HETATM 5898  O   HOH A 564      67.707  -8.486  -9.079  1.00 53.56           O  
HETATM 5899  O   HOH A 565      83.395  -9.551 -21.117  1.00 52.54           O  
HETATM 5900  O   HOH A 566      52.952 -47.749  -9.380  1.00 46.86           O  
HETATM 5901  O   HOH A 567      87.396  -3.211 -39.902  1.00 46.17           O  
HETATM 5902  O   HOH A 568      98.621 -27.195 -34.446  1.00 42.48           O  
HETATM 5903  O   HOH A 569      91.259 -16.324 -44.037  1.00 47.36           O  
HETATM 5904  O   HOH A 570      75.236 -11.374 -40.404  1.00 54.40           O  
HETATM 5905  O   HOH A 571      48.815  -9.867 -17.586  1.00 54.95           O  
HETATM 5906  O   HOH A 572      62.608  -4.523 -24.133  1.00 43.77           O  
HETATM 5907  O   HOH A 573      66.020 -24.129  -2.295  1.00 52.02           O  
HETATM 5908  O   HOH A 574      74.943 -15.789 -34.761  1.00 47.31           O  
HETATM 5909  O   HOH A 575      77.291 -28.584 -21.266  1.00 42.67           O  
HETATM 5910  O   HOH A 576      54.884 -24.303 -15.764  1.00 52.15           O  
HETATM 5911  O   HOH A 577      68.864 -25.118 -41.413  1.00 60.49           O  
HETATM 5912  O   HOH A 578      64.490 -22.004  -1.413  1.00 54.19           O  
HETATM 5913  O   HOH A 579      75.652 -30.703 -20.217  1.00 44.29           O  
HETATM 5914  O   HOH A 580      70.076 -10.067 -11.314  1.00 52.59           O  
HETATM 5915  O   HOH A 581      94.144  -4.401 -33.153  1.00 41.32           O  
HETATM 5916  O   HOH A 582      68.819 -18.311 -35.909  1.00 54.41           O  
HETATM 5917  O   HOH A 583      68.927 -19.098 -27.058  1.00 38.82           O  
HETATM 5918  O   HOH A 584      62.948  -3.919 -21.877  1.00 43.95           O  
HETATM 5919  O   HOH A 585      53.339 -28.989 -14.204  1.00 54.30           O  
HETATM 5920  O   HOH A 586      60.981  -8.477  -8.381  1.00 68.89           O  
HETATM 5921  O   HOH A 587      60.349 -26.941 -21.936  1.00 33.80           O  
HETATM 5922  O   HOH A 588      99.147 -24.321 -32.093  1.00 49.05           O  
HETATM 5923  O   HOH A 589      75.906 -22.633 -25.876  1.00 38.50           O  
HETATM 5924  O   HOH A 590      60.486 -29.760 -19.915  1.00 39.86           O  
HETATM 5925  O   HOH A 591      75.673 -24.875 -29.361  1.00 42.43           O  
HETATM 5926  O   HOH A 592      72.888 -12.920 -34.041  1.00 44.67           O  
HETATM 5927  O   HOH A 593      49.470 -32.935 -19.233  1.00 57.31           O  
HETATM 5928  O   HOH A 594      70.904 -21.153 -13.987  1.00 55.27           O  
HETATM 5929  O   HOH A 595      61.645 -51.138  -2.704  1.00 41.90           O  
HETATM 5930  O   HOH A 596      72.590 -23.872 -25.768  1.00 41.55           O  
HETATM 5931  O   HOH A 597      49.488 -35.756 -19.778  1.00 45.72           O  
HETATM 5932  O   HOH A 598      69.252 -24.337 -32.287  1.00 45.02           O  
HETATM 5933  O   HOH A 599      53.647 -24.184  -3.567  1.00 52.87           O  
HETATM 5934  O   HOH A 600      88.785  -6.105 -39.526  1.00 40.63           O  
HETATM 5935  O   HOH A 601      63.257 -27.129 -21.885  1.00 32.57           O  
HETATM 5936  O   HOH A 602      94.492 -25.098 -41.208  1.00 66.09           O  
HETATM 5937  O   HOH A 603      68.188  -5.864 -28.087  1.00 43.92           O  
HETATM 5938  O   HOH A 604      51.298 -15.989 -12.289  1.00 69.09           O  
HETATM 5939  O   HOH A 605      66.427  -6.991 -13.196  1.00 49.47           O  
HETATM 5940  O   HOH A 606      66.392 -45.918   1.535  1.00 33.73           O  
HETATM 5941  O   HOH A 607      99.477 -33.371 -37.926  1.00 47.45           O  
HETATM 5942  O   HOH A 608      55.537 -20.124 -17.695  1.00 54.95           O  
HETATM 5943  O   HOH A 609      66.260 -18.792  -6.890  1.00 45.16           O  
HETATM 5944  O   HOH A 610      47.168 -18.663 -18.412  1.00 60.45           O  
HETATM 5945  O   HOH A 611      68.754 -17.556 -14.719  1.00 36.22           O  
HETATM 5946  O   HOH A 612      79.935  -5.956 -35.696  1.00 37.93           O  
HETATM 5947  O   HOH A 613      90.117 -34.551 -25.022  1.00 36.99           O  
HETATM 5948  O   HOH A 614      56.126  -4.482 -27.452  1.00 63.91           O  
HETATM 5949  O   HOH A 615      63.256 -43.622 -15.022  1.00 58.13           O  
HETATM 5950  O   HOH A 616      94.513 -15.170 -43.328  1.00 62.42           O  
HETATM 5951  O   HOH A 617      55.582 -55.345 -13.433  1.00 48.58           O  
HETATM 5952  O   HOH A 618      68.790 -29.558 -28.601  1.00 50.18           O  
HETATM 5953  O   HOH A 619      57.930 -36.124 -15.134  1.00 46.84           O  
HETATM 5954  O   HOH A 620      76.138 -17.671 -20.535  1.00 35.98           O  
HETATM 5955  O   HOH A 621      48.352 -10.172 -12.519  1.00 53.55           O  
HETATM 5956  O   HOH A 622      96.093 -28.603 -40.000  1.00 50.70           O  
HETATM 5957  O   HOH A 623      80.271  -3.703 -39.870  1.00 42.67           O  
HETATM 5958  O   HOH A 624      83.959 -13.411 -22.224  1.00 42.59           O  
HETATM 5959  O   HOH A 625      77.827 -21.035 -28.442  1.00 34.55           O  
HETATM 5960  O   HOH A 626      75.155  -6.615 -22.031  1.00 63.57           O  
HETATM 5961  O   HOH A 627      63.095 -16.450 -28.270  1.00 41.62           O  
HETATM 5962  O   HOH A 628      88.535  -2.951 -33.058  1.00 42.21           O  
HETATM 5963  O   HOH A 629      51.444 -51.214  -7.216  1.00 59.88           O  
HETATM 5964  O   HOH A 630      57.569 -12.857 -31.162  1.00 66.66           O  
HETATM 5965  O   HOH A 631     100.623 -10.976 -32.712  1.00 67.69           O  
HETATM 5966  O   HOH A 632      49.993 -12.197 -19.342  1.00 58.74           O  
HETATM 5967  O   HOH A 633      82.997 -19.794 -20.604  1.00 55.76           O  
HETATM 5968  O   HOH A 634      87.524 -27.615 -39.887  1.00 46.33           O  
HETATM 5969  O   HOH A 635      53.504 -28.028 -24.202  1.00 60.22           O  
HETATM 5970  O   HOH A 636      52.737 -13.633 -24.985  1.00 50.89           O  
HETATM 5971  O   HOH A 637      47.453 -32.930  -6.922  1.00 54.55           O  
HETATM 5972  O   HOH A 638      68.914 -18.866  -8.690  1.00 48.95           O  
HETATM 5973  O   HOH A 639      76.778 -12.687 -45.296  1.00 65.53           O  
HETATM 5974  O   HOH A 640      54.689 -21.935  -0.508  1.00 59.18           O  
HETATM 5975  O   HOH A 641      62.977 -22.035 -12.203  1.00 35.62           O  
HETATM 5976  O   HOH A 642      58.758 -48.818  -5.058  1.00 35.99           O  
HETATM 5977  O   HOH A 643      91.737 -26.069 -49.411  1.00 70.61           O  
HETATM 5978  O   HOH A 644      73.605 -29.590  -1.094  1.00 49.12           O  
HETATM 5979  O   HOH A 645      79.420 -21.858 -35.658  1.00 39.37           O  
HETATM 5980  O   HOH A 646      97.044 -17.138 -27.812  1.00 63.19           O  
HETATM 5981  O   HOH A 647      65.543 -23.741 -20.761  1.00 36.08           O  
HETATM 5982  O   HOH A 648      50.586 -52.369 -10.021  1.00 57.97           O  
HETATM 5983  O   HOH A 649      68.391 -34.781 -11.441  1.00 31.86           O  
HETATM 5984  O   HOH A 650      61.312 -18.742 -34.354  1.00 45.10           O  
HETATM 5985  O   HOH A 651      57.801 -11.772   1.525  1.00 59.09           O  
HETATM 5986  O   HOH A 652      79.187 -26.022 -28.179  1.00 52.31           O  
HETATM 5987  O   HOH A 653      96.682 -26.757 -24.152  1.00 51.52           O  
HETATM 5988  O   HOH A 654      99.209  -4.882 -28.015  1.00 53.60           O  
HETATM 5989  O   HOH A 655      95.577 -21.462 -30.836  1.00 39.76           O  
HETATM 5990  O   HOH A 656      61.618 -26.422 -18.164  1.00 33.67           O  
HETATM 5991  O   HOH A 657      73.553 -22.192 -15.030  1.00 37.50           O  
HETATM 5992  O   HOH A 658      76.249 -31.098 -15.766  1.00 49.53           O  
HETATM 5993  O   HOH A 659      71.096 -32.531  -0.571  1.00 42.53           O  
HETATM 5994  O   HOH A 660      92.747  -4.705 -24.391  1.00 56.07           O  
HETATM 5995  O   HOH A 661      70.110 -40.281 -14.827  1.00 58.19           O  
HETATM 5996  O   HOH A 662      70.898 -17.586 -28.350  1.00 37.24           O  
HETATM 5997  O   HOH A 663      54.621 -44.972  -0.794  1.00 39.65           O  
HETATM 5998  O   HOH A 664      59.710 -11.408 -31.483  1.00 59.71           O  
HETATM 5999  O   HOH A 665      82.630 -34.424 -21.682  1.00 45.99           O  
HETATM 6000  O   HOH A 666      63.645 -49.839 -13.101  1.00 38.93           O  
HETATM 6001  O   HOH A 667      82.253 -24.543 -20.854  1.00 39.70           O  
HETATM 6002  O   HOH A 668      93.348  -2.121 -39.344  1.00 43.58           O  
HETATM 6003  O   HOH A 669      83.698 -36.188 -27.271  1.00 49.69           O  
HETATM 6004  O   HOH A 670      62.162 -20.650  -9.873  1.00 35.73           O  
HETATM 6005  O   HOH A 671      66.053 -29.253 -33.021  1.00 65.78           O  
HETATM 6006  O   HOH A 672     101.248 -29.682 -26.717  1.00 61.04           O  
HETATM 6007  O   HOH A 673      58.167 -35.060  -3.454  1.00 57.43           O  
HETATM 6008  O   HOH A 674      64.224 -52.131  -9.796  1.00 38.49           O  
HETATM 6009  O   HOH A 675      42.084 -35.431 -10.818  1.00 51.14           O  
HETATM 6010  O   HOH A 676      75.836 -15.312 -17.383  1.00 50.57           O  
HETATM 6011  O   HOH A 677      62.898  -8.454   0.477  1.00 54.05           O  
HETATM 6012  O   HOH A 678      59.604  -0.954  -7.571  1.00 78.32           O  
HETATM 6013  O   HOH A 679     101.984 -32.559 -38.425  1.00 56.60           O  
HETATM 6014  O   HOH A 680      71.811 -35.101  -3.900  1.00 46.11           O  
HETATM 6015  O   HOH A 681      75.260 -21.998 -29.081  1.00 37.30           O  
HETATM 6016  O   HOH A 682      64.515 -23.910 -11.255  1.00 38.83           O  
HETATM 6017  O   HOH A 683      81.332 -33.822 -25.380  1.00 68.93           O  
HETATM 6018  O   HOH A 684      94.430 -23.908 -24.006  1.00 45.61           O  
HETATM 6019  O   HOH A 685      45.253 -43.548  -6.778  1.00 51.68           O  
HETATM 6020  O   HOH A 686      46.984 -45.581  -8.463  1.00 55.54           O  
HETATM 6021  O   HOH A 687      52.930 -21.286 -29.915  1.00 55.73           O  
HETATM 6022  O   HOH A 688      95.332  -9.755 -47.707  1.00 76.54           O  
HETATM 6023  O   HOH A 689      54.439 -26.189 -18.314  1.00 42.04           O  
HETATM 6024  O   HOH A 690      45.546 -37.164  -4.488  1.00 45.40           O  
HETATM 6025  O   HOH A 691      68.052 -24.978 -38.568  1.00 71.75           O  
HETATM 6026  O   HOH A 692      99.981 -11.383 -40.711  1.00 73.29           O  
HETATM 6027  O   HOH A 693      91.764 -27.909 -40.773  1.00 51.98           O  
HETATM 6028  O   HOH A 694      66.437 -19.122 -26.234  1.00 34.44           O  
HETATM 6029  O   HOH A 695      94.087 -34.406 -40.476  1.00 61.46           O  
HETATM 6030  O   HOH A 696      76.441 -27.983 -47.473  1.00 67.31           O  
HETATM 6031  O   HOH A 697      71.808 -28.982  -8.178  1.00 33.86           O  
HETATM 6032  O   HOH A 698      61.784 -55.020  -7.509  1.00 39.71           O  
HETATM 6033  O   HOH A 699      79.462 -23.356 -28.314  1.00 48.89           O  
HETATM 6034  O   HOH A 700      64.808  -2.996 -25.218  1.00 47.98           O  
HETATM 6035  O   HOH A 701     101.095  -3.119 -30.698  1.00 54.78           O  
HETATM 6036  O   HOH A 702      59.002 -19.902 -33.931  1.00 48.54           O  
HETATM 6037  O   HOH A 703      53.442 -55.425 -15.286  1.00 64.96           O  
HETATM 6038  O   HOH A 704      71.115 -10.506 -33.890  1.00 51.37           O  
HETATM 6039  O   HOH A 705      48.619 -45.601 -11.403  1.00 45.47           O  
HETATM 6040  O   HOH A 706      68.757 -17.045 -33.549  1.00 56.74           O  
HETATM 6041  O   HOH A 707      68.566   1.103 -20.043  1.00 57.66           O  
HETATM 6042  O   HOH A 708     102.487 -26.807 -30.439  1.00 49.05           O  
HETATM 6043  O   HOH A 709      69.690  -7.144 -31.058  1.00 52.86           O  
HETATM 6044  O   HOH A 710      51.978 -23.175 -36.811  1.00 76.42           O  
HETATM 6045  O   HOH A 711      57.682  -1.042 -10.495  1.00 66.11           O  
HETATM 6046  O   HOH A 712      71.924 -16.533 -46.921  1.00 58.81           O  
HETATM 6047  O   HOH A 713      48.491 -46.655 -14.742  1.00 73.96           O  
HETATM 6048  O   HOH A 714      98.721 -23.321 -34.525  1.00 57.42           O  
HETATM 6049  O   HOH A 715      70.091  -3.974 -17.229  1.00 69.35           O  
HETATM 6050  O   HOH A 716      89.354 -28.151 -46.778  1.00 71.37           O  
HETATM 6051  O   HOH A 717      51.654  -8.431 -31.849  1.00 74.91           O  
HETATM 6052  O   HOH A 718      65.252 -26.426 -35.454  1.00 62.35           O  
HETATM 6053  O   HOH A 719      78.963  -5.189 -41.910  1.00 67.88           O  
HETATM 6054  O   HOH A 720      76.963 -32.335 -39.175  1.00 67.78           O  
HETATM 6055  O   HOH A 721      98.836 -29.085 -26.054  1.00 63.95           O  
HETATM 6056  O   HOH A 722      77.089  -7.987 -19.628  1.00 62.00           O  
HETATM 6057  O   HOH A 723      87.387 -40.266 -30.787  1.00 74.13           O  
HETATM 6058  O   HOH A 724      69.425 -10.361  -6.679  1.00 72.01           O  
HETATM 6059  O   HOH A 725      55.995 -19.583   0.518  1.00 53.93           O  
HETATM 6060  O   HOH A 726      95.675 -18.565 -40.405  1.00 55.36           O  
HETATM 6061  O   HOH A 727      71.560 -26.980 -27.174  1.00 62.16           O  
HETATM 6062  O   HOH A 728      70.962 -35.432  -1.429  1.00 44.32           O  
HETATM 6063  O   HOH A 729      52.950 -27.044  -2.824  1.00 65.76           O  
HETATM 6064  O   HOH A 730      95.911  -1.700 -39.379  1.00 62.56           O  
HETATM 6065  O   HOH A 731      96.704 -21.614 -40.288  1.00 72.47           O  
HETATM 6066  O   HOH A 732      97.728  -7.681 -48.048  1.00 84.72           O  
HETATM 6067  O   HOH A 733      87.812 -29.154 -42.118  1.00 61.62           O  
HETATM 6068  O   HOH A 734      93.309  -3.388 -41.789  1.00 62.67           O  
HETATM 6069  O   HOH A 735      94.254 -29.076 -41.319  1.00 53.88           O  
HETATM 6070  O   HOH A 736      73.815 -25.748 -27.122  1.00 49.58           O  
HETATM 6071  O   HOH A 737      69.128 -14.974 -34.503  1.00 75.68           O  
HETATM 6072  O   HOH A 738      54.335 -26.713 -26.406  1.00 44.86           O  
HETATM 6073  O   HOH A 739     101.911 -24.496 -31.385  1.00 60.60           O  
HETATM 6074  O   HOH A 740      50.907 -47.674 -11.369  1.00 59.26           O  
HETATM 6075  O   HOH A 741      91.102 -27.017 -43.515  1.00 59.22           O  
HETATM 6076  O   HOH A 742      88.935 -28.260 -44.079  1.00 52.08           O  
HETATM 6077  O   HOH B 501      58.741 -45.506  36.435  1.00 51.17           O  
HETATM 6078  O   HOH B 502      80.993 -42.258   0.022  1.00 68.09           O  
HETATM 6079  O   HOH B 503      45.266 -29.850  24.035  1.00 59.41           O  
HETATM 6080  O   HOH B 504      75.898  -9.416  -1.371  1.00 69.27           O  
HETATM 6081  O   HOH B 505      69.091 -11.705  35.100  1.00 54.74           O  
HETATM 6082  O   HOH B 506      71.040 -15.283  26.348  1.00 42.37           O  
HETATM 6083  O   HOH B 507      60.398 -33.404  20.898  1.00 36.72           O  
HETATM 6084  O   HOH B 508      70.778 -25.893  20.342  1.00 49.57           O  
HETATM 6085  O   HOH B 509      77.335 -31.020  17.633  1.00 48.47           O  
HETATM 6086  O   HOH B 510      83.904 -12.510   8.548  1.00 56.39           O  
HETATM 6087  O   HOH B 511      62.940 -12.432   9.148  1.00 44.36           O  
HETATM 6088  O   HOH B 512      83.905 -19.825  40.272  1.00 49.95           O  
HETATM 6089  O   HOH B 513      74.444 -35.680  16.526  1.00 61.82           O  
HETATM 6090  O   HOH B 514      80.367  -0.859  17.149  1.00 43.34           O  
HETATM 6091  O   HOH B 515      65.094  -3.428  21.580  1.00 36.86           O  
HETATM 6092  O   HOH B 516      63.093 -23.018  19.071  1.00 38.85           O  
HETATM 6093  O   HOH B 517      65.343 -27.299  24.316  1.00 41.31           O  
HETATM 6094  O   HOH B 518      61.548 -19.426  35.247  1.00 54.17           O  
HETATM 6095  O   HOH B 519      70.874 -26.381   9.824  1.00 43.26           O  
HETATM 6096  O   HOH B 520      90.974 -32.671  -1.065  1.00 37.15           O  
HETATM 6097  O   HOH B 521      65.521 -27.681  29.905  1.00 44.91           O  
HETATM 6098  O   HOH B 522      77.739 -15.818  38.021  1.00 63.89           O  
HETATM 6099  O   HOH B 523      60.690 -38.187  15.483  1.00 44.46           O  
HETATM 6100  O   HOH B 524      83.252 -17.946  13.116  1.00 57.18           O  
HETATM 6101  O   HOH B 525      51.012 -19.045  21.501  1.00 62.93           O  
HETATM 6102  O   HOH B 526      49.840 -46.704  28.703  1.00 37.83           O  
HETATM 6103  O   HOH B 527      70.455 -24.657  24.185  1.00 49.58           O  
HETATM 6104  O   HOH B 528      56.753  -2.712  19.491  1.00 77.28           O  
HETATM 6105  O   HOH B 529      73.453 -19.763   1.636  1.00 40.14           O  
HETATM 6106  O   HOH B 530      44.907 -36.482  37.510  1.00 50.54           O  
HETATM 6107  O   HOH B 531      69.388  -6.515   8.452  1.00 39.25           O  
HETATM 6108  O   HOH B 532      60.442 -19.860  18.173  1.00 49.94           O  
HETATM 6109  O   HOH B 533      58.424 -15.637  18.986  1.00 43.08           O  
HETATM 6110  O   HOH B 534      62.552 -12.547  11.607  1.00 51.24           O  
HETATM 6111  O   HOH B 535      58.903  -4.261  27.789  1.00 56.69           O  
HETATM 6112  O   HOH B 536      75.294   3.870  28.032  1.00 42.35           O  
HETATM 6113  O   HOH B 537      75.593 -32.189  19.724  1.00 50.18           O  
HETATM 6114  O   HOH B 538      81.249 -24.044  20.237  1.00 41.28           O  
HETATM 6115  O   HOH B 539      47.221 -31.953  31.836  1.00 47.27           O  
HETATM 6116  O   HOH B 540      67.112 -26.212  17.480  1.00 42.74           O  
HETATM 6117  O   HOH B 541      76.022 -22.458  20.014  1.00 33.99           O  
HETATM 6118  O   HOH B 542      47.377 -28.427  44.238  1.00 62.15           O  
HETATM 6119  O   HOH B 543      83.539 -37.301  14.849  1.00 52.41           O  
HETATM 6120  O   HOH B 544      80.030 -13.279  17.810  1.00 49.16           O  
HETATM 6121  O   HOH B 545      67.832 -25.175  26.198  1.00 46.55           O  
HETATM 6122  O   HOH B 546      70.477 -32.453  12.262  1.00 43.65           O  
HETATM 6123  O   HOH B 547      71.497  -0.007  26.868  1.00 37.76           O  
HETATM 6124  O   HOH B 548      83.791 -15.910   3.674  1.00 43.74           O  
HETATM 6125  O   HOH B 549      78.805 -37.036   1.074  1.00 40.54           O  
HETATM 6126  O   HOH B 550      62.761   3.142  28.345  1.00 54.95           O  
HETATM 6127  O   HOH B 551      72.378  -5.660   8.169  1.00 63.16           O  
HETATM 6128  O   HOH B 552      65.172 -32.893  25.328  1.00 56.55           O  
HETATM 6129  O   HOH B 553      68.099 -19.303   9.091  1.00 46.95           O  
HETATM 6130  O   HOH B 554      59.001  -1.587  12.738  1.00 56.53           O  
HETATM 6131  O   HOH B 555      62.301 -14.942   9.066  1.00 63.49           O  
HETATM 6132  O   HOH B 556      96.840 -35.309   9.708  1.00 49.02           O  
HETATM 6133  O   HOH B 557      71.878 -13.813  28.497  1.00 37.74           O  
HETATM 6134  O   HOH B 558      99.763 -19.504  11.007  1.00 50.36           O  
HETATM 6135  O   HOH B 559      61.538 -20.015  46.903  1.00 66.77           O  
HETATM 6136  O   HOH B 560      77.276 -16.039   9.441  1.00 34.85           O  
HETATM 6137  O   HOH B 561      85.717 -21.733  15.730  1.00 37.54           O  
HETATM 6138  O   HOH B 562      85.253 -20.797   2.506  1.00 38.94           O  
HETATM 6139  O   HOH B 563      80.617 -13.074  27.398  1.00 38.39           O  
HETATM 6140  O   HOH B 564      68.049 -18.690  36.564  1.00 63.15           O  
HETATM 6141  O   HOH B 565      95.370 -24.383   1.516  1.00 60.07           O  
HETATM 6142  O   HOH B 566      65.992 -31.728  21.633  1.00 47.54           O  
HETATM 6143  O   HOH B 567      58.053 -43.468  25.353  1.00 36.77           O  
HETATM 6144  O   HOH B 568      62.103  -7.702  28.309  1.00 41.31           O  
HETATM 6145  O   HOH B 569      46.928 -41.504  34.747  1.00 46.79           O  
HETATM 6146  O   HOH B 570      43.103 -40.241  38.801  1.00 66.50           O  
HETATM 6147  O   HOH B 571      79.144  -5.974  24.953  1.00 39.40           O  
HETATM 6148  O   HOH B 572      74.594 -14.875  34.540  1.00 39.80           O  
HETATM 6149  O   HOH B 573      78.469   1.085  28.146  1.00 40.47           O  
HETATM 6150  O   HOH B 574      80.970  -1.123  12.238  1.00 47.03           O  
HETATM 6151  O   HOH B 575      92.240 -17.816   0.949  1.00 75.64           O  
HETATM 6152  O   HOH B 576      63.495 -10.098   9.232  1.00 54.81           O  
HETATM 6153  O   HOH B 577      79.465 -10.373  -1.118  1.00 60.69           O  
HETATM 6154  O   HOH B 578      45.927 -45.248  26.950  1.00 59.16           O  
HETATM 6155  O   HOH B 579      45.092 -39.339  32.287  1.00 53.42           O  
HETATM 6156  O   HOH B 580      42.983 -32.169  38.376  1.00 56.76           O  
HETATM 6157  O   HOH B 581      92.687 -39.373   5.531  1.00 45.68           O  
HETATM 6158  O   HOH B 582      82.045  -7.990  12.265  1.00 63.23           O  
HETATM 6159  O   HOH B 583      56.982 -32.432  46.974  1.00 56.50           O  
HETATM 6160  O   HOH B 584      70.502 -17.979   7.167  1.00 47.01           O  
HETATM 6161  O   HOH B 585      81.559 -41.964  10.406  1.00 67.48           O  
HETATM 6162  O   HOH B 586      77.453 -23.106  22.232  1.00 34.96           O  
HETATM 6163  O   HOH B 587      70.560  -3.679  31.570  1.00 43.69           O  
HETATM 6164  O   HOH B 588      65.788  -3.849  23.975  1.00 35.95           O  
HETATM 6165  O   HOH B 589      73.699 -25.496  25.022  1.00 50.83           O  
HETATM 6166  O   HOH B 590      64.307 -41.475  27.823  1.00 56.56           O  
HETATM 6167  O   HOH B 591      84.022 -47.049   4.226  1.00 48.28           O  
HETATM 6168  O   HOH B 592      43.006 -32.156  28.894  1.00 75.47           O  
HETATM 6169  O   HOH B 593      86.474  -7.581  18.295  1.00 61.90           O  
HETATM 6170  O   HOH B 594      66.961 -12.667  33.669  1.00 49.16           O  
HETATM 6171  O   HOH B 595      51.671 -45.524  24.463  1.00 42.29           O  
HETATM 6172  O   HOH B 596      64.673  -0.863  29.285  1.00 60.16           O  
HETATM 6173  O   HOH B 597      68.276 -19.242  27.486  1.00 37.68           O  
HETATM 6174  O   HOH B 598      46.606 -47.901  38.457  1.00 63.69           O  
HETATM 6175  O   HOH B 599      73.700  -7.321  -1.612  1.00 53.81           O  
HETATM 6176  O   HOH B 600      64.278 -25.918  26.405  1.00 43.78           O  
HETATM 6177  O   HOH B 601      56.547 -36.323  40.066  1.00 56.95           O  
HETATM 6178  O   HOH B 602      46.196 -14.714  27.934  1.00 63.92           O  
HETATM 6179  O   HOH B 603      85.820 -13.516  31.663  1.00 54.97           O  
HETATM 6180  O   HOH B 604      60.849 -27.046  36.019  1.00 42.91           O  
HETATM 6181  O   HOH B 605      70.661 -24.380  32.926  1.00 62.24           O  
HETATM 6182  O   HOH B 606      98.754 -26.996  19.519  1.00 80.17           O  
HETATM 6183  O   HOH B 607      87.169 -24.220   2.165  1.00 51.24           O  
HETATM 6184  O   HOH B 608      74.826 -18.830  12.511  1.00 33.55           O  
HETATM 6185  O   HOH B 609      70.093 -30.867   1.422  1.00 49.73           O  
HETATM 6186  O   HOH B 610      83.955  -9.933   5.697  1.00 68.63           O  
HETATM 6187  O   HOH B 611      68.942   2.089  14.889  1.00 55.18           O  
HETATM 6188  O   HOH B 612      68.592 -32.751  20.696  1.00 52.59           O  
HETATM 6189  O   HOH B 613      53.363 -38.555  40.915  1.00 64.24           O  
HETATM 6190  O   HOH B 614      56.926 -26.993  21.266  1.00 51.64           O  
HETATM 6191  O   HOH B 615      74.955   2.417  31.911  1.00 57.48           O  
HETATM 6192  O   HOH B 616      86.821 -19.550  14.173  1.00 56.45           O  
HETATM 6193  O   HOH B 617      73.462 -22.272   2.536  1.00 45.65           O  
HETATM 6194  O   HOH B 618      59.693 -16.093  41.081  1.00 75.34           O  
HETATM 6195  O   HOH B 619      81.823 -46.184   1.340  1.00 54.29           O  
HETATM 6196  O   HOH B 620      81.740  -6.358  25.846  1.00 44.34           O  
HETATM 6197  O   HOH B 621      64.911 -38.079  18.677  1.00 58.70           O  
HETATM 6198  O   HOH B 622      83.171 -16.406  15.687  1.00 55.23           O  
HETATM 6199  O   HOH B 623      48.510 -40.155  24.454  1.00 50.80           O  
HETATM 6200  O   HOH B 624      64.726  -5.864  30.990  1.00 45.11           O  
HETATM 6201  O   HOH B 625      67.528 -18.177  15.068  1.00 37.88           O  
HETATM 6202  O   HOH B 626      81.242  -6.365   1.285  1.00 57.68           O  
HETATM 6203  O   HOH B 627      61.351 -21.951  21.098  1.00 36.09           O  
HETATM 6204  O   HOH B 628      84.495 -40.983  -1.157  1.00 32.88           O  
HETATM 6205  O   HOH B 629      79.696 -21.485  22.180  1.00 32.69           O  
HETATM 6206  O   HOH B 630      78.402 -21.773  18.503  1.00 36.21           O  
HETATM 6207  O   HOH B 631      93.682 -23.160  19.908  1.00 55.09           O  
HETATM 6208  O   HOH B 632      70.365 -28.289  36.890  1.00 68.54           O  
HETATM 6209  O   HOH B 633      91.352 -42.786   3.003  1.00 45.91           O  
HETATM 6210  O   HOH B 634      60.662 -28.894  19.759  1.00 55.51           O  
HETATM 6211  O   HOH B 635      85.997 -36.893  15.422  1.00 50.11           O  
HETATM 6212  O   HOH B 636      76.935   3.371  20.638  1.00 45.10           O  
HETATM 6213  O   HOH B 637      56.855 -20.056  20.023  1.00 60.66           O  
HETATM 6214  O   HOH B 638      63.201  -3.632  24.893  1.00 41.77           O  
HETATM 6215  O   HOH B 639      65.690   1.916  22.454  1.00 39.52           O  
HETATM 6216  O   HOH B 640      67.741 -22.344  14.482  1.00 49.55           O  
HETATM 6217  O   HOH B 641      66.131   1.908  29.824  1.00 45.98           O  
HETATM 6218  O   HOH B 642      61.777 -25.592  28.873  1.00 38.94           O  
HETATM 6219  O   HOH B 643      68.312 -33.350  16.206  1.00 50.37           O  
HETATM 6220  O   HOH B 644      64.401 -24.924  29.512  1.00 39.13           O  
HETATM 6221  O   HOH B 645      76.993 -32.478  11.940  1.00 34.96           O  
HETATM 6222  O   HOH B 646      49.195 -47.384  38.027  1.00 58.59           O  
HETATM 6223  O   HOH B 647      62.907   0.263  23.148  1.00 46.91           O  
HETATM 6224  O   HOH B 648      66.204 -24.489  15.490  1.00 43.95           O  
HETATM 6225  O   HOH B 649      80.550  -3.495  18.955  1.00 39.15           O  
HETATM 6226  O   HOH B 650      85.847 -27.388   3.902  1.00 53.30           O  
HETATM 6227  O   HOH B 651      61.900 -16.019  34.614  1.00 55.77           O  
HETATM 6228  O   HOH B 652      73.557 -32.022   0.993  1.00 42.73           O  
HETATM 6229  O   HOH B 653      82.329 -11.978  14.496  1.00 51.06           O  
HETATM 6230  O   HOH B 654      67.582  -7.247  -0.465  1.00 61.31           O  
HETATM 6231  O   HOH B 655      74.042 -28.134  28.633  1.00 57.17           O  
HETATM 6232  O   HOH B 656      80.586 -16.954  -2.190  1.00 73.92           O  
HETATM 6233  O   HOH B 657      88.910 -42.618  13.709  1.00 40.72           O  
HETATM 6234  O   HOH B 658      81.606 -14.394   0.574  1.00 63.76           O  
HETATM 6235  O   HOH B 659      64.405 -39.536  21.923  1.00 48.94           O  
HETATM 6236  O   HOH B 660      46.741 -35.236  31.279  1.00 53.25           O  
HETATM 6237  O   HOH B 661      83.322  -1.346  18.613  1.00 60.05           O  
HETATM 6238  O   HOH B 662      72.236  -1.913  30.765  1.00 50.79           O  
HETATM 6239  O   HOH B 663      56.307 -12.230  22.308  1.00 53.47           O  
HETATM 6240  O   HOH B 664      89.428 -44.884  10.327  1.00 43.38           O  
HETATM 6241  O   HOH B 665      65.890 -19.122  28.802  1.00 40.69           O  
HETATM 6242  O   HOH B 666      49.923 -41.469  40.376  1.00 55.10           O  
HETATM 6243  O   HOH B 667      74.820 -17.366  10.104  1.00 35.23           O  
HETATM 6244  O   HOH B 668      73.713 -21.538  21.175  1.00 37.68           O  
HETATM 6245  O   HOH B 669      52.440 -22.495  22.745  1.00 51.48           O  
HETATM 6246  O   HOH B 670      83.476 -23.115   0.935  1.00 57.88           O  
HETATM 6247  O   HOH B 671      75.019  -4.410  -1.529  1.00 70.87           O  
HETATM 6248  O   HOH B 672      74.318  -3.648   9.001  1.00 46.43           O  
HETATM 6249  O   HOH B 673      59.672 -30.836  21.249  1.00 39.39           O  
HETATM 6250  O   HOH B 674      62.353 -12.738  33.935  1.00 59.28           O  
HETATM 6251  O   HOH B 675      64.178 -18.966  47.584  1.00 68.58           O  
HETATM 6252  O   HOH B 676      74.584 -21.218  11.627  1.00 41.11           O  
HETATM 6253  O   HOH B 677      70.539 -18.005  26.554  1.00 37.67           O  
HETATM 6254  O   HOH B 678      70.234  -3.261   6.402  1.00 57.88           O  
HETATM 6255  O   HOH B 679      68.825 -35.368  31.421  1.00 73.96           O  
HETATM 6256  O   HOH B 680      71.860 -23.372  22.057  1.00 42.90           O  
HETATM 6257  O   HOH B 681      53.533 -12.726  30.240  1.00 51.75           O  
HETATM 6258  O   HOH B 682      52.919 -18.788  47.064  1.00 70.01           O  
HETATM 6259  O   HOH B 683      84.400 -17.869  18.453  1.00 38.53           O  
HETATM 6260  O   HOH B 684      73.355 -25.133  20.922  1.00 51.66           O  
HETATM 6261  O   HOH B 685      71.065 -29.277   8.624  1.00 36.17           O  
HETATM 6262  O   HOH B 686      76.046 -26.087  33.630  1.00 61.70           O  
HETATM 6263  O   HOH B 687     101.296 -27.631   7.220  1.00 52.69           O  
HETATM 6264  O   HOH B 688      69.159 -23.878  45.606  1.00 62.89           O  
HETATM 6265  O   HOH B 689      93.072 -46.281   7.938  1.00 46.48           O  
HETATM 6266  O   HOH B 690      93.598 -19.607   6.540  1.00 61.23           O  
HETATM 6267  O   HOH B 691      50.583 -14.757  41.639  1.00 62.93           O  
HETATM 6268  O   HOH B 692      71.250   0.415  29.354  1.00 43.32           O  
HETATM 6269  O   HOH B 693      43.474 -43.374  30.480  1.00 53.16           O  
HETATM 6270  O   HOH B 694      82.342   0.789  13.824  1.00 60.00           O  
HETATM 6271  O   HOH B 695      68.106   1.464  10.439  1.00 65.91           O  
HETATM 6272  O   HOH B 696      53.946 -45.271  40.719  1.00 59.50           O  
HETATM 6273  O   HOH B 697      99.523 -31.077  11.560  1.00 58.49           O  
HETATM 6274  O   HOH B 698      55.418  -6.425  27.696  1.00 53.59           O  
HETATM 6275  O   HOH B 699      97.761 -22.445   4.686  1.00 46.75           O  
HETATM 6276  O   HOH B 700      76.122  -1.354  31.740  1.00 65.21           O  
HETATM 6277  O   HOH B 701      77.337 -14.476  34.061  1.00 49.28           O  
HETATM 6278  O   HOH B 702      65.584  -3.137  31.372  1.00 60.91           O  
HETATM 6279  O   HOH B 703      48.812 -36.833  24.141  1.00 54.51           O  
HETATM 6280  O   HOH B 704      67.388 -17.087  33.806  1.00 61.72           O  
HETATM 6281  O   HOH B 705     100.416 -42.202  15.494  1.00 57.57           O  
HETATM 6282  O   HOH B 706     100.953 -30.268   8.997  1.00 64.91           O  
HETATM 6283  O   HOH B 707      78.529 -30.271  24.172  1.00 61.11           O  
HETATM 6284  O   HOH B 708      72.425 -33.820  19.464  1.00 67.47           O  
HETATM 6285  O   HOH B 709      49.615 -43.710  24.812  1.00 67.20           O  
HETATM 6286  O   HOH B 710      80.715  -2.445  21.052  1.00 57.43           O  
HETATM 6287  O   HOH B 711      51.892 -37.029  50.008  1.00 73.13           O  
HETATM 6288  O   HOH B 712      64.060 -18.146  13.053  1.00 70.21           O  
HETATM 6289  O   HOH B 713      60.094 -16.078  15.274  1.00 64.47           O  
HETATM 6290  O   HOH B 714      78.086  -0.049  30.456  1.00 65.73           O  
HETATM 6291  O   HOH B 715      44.711 -37.994  34.590  1.00 64.55           O  
HETATM 6292  O   HOH B 716      76.539 -23.086  35.842  1.00 66.47           O  
HETATM 6293  O   HOH B 717      47.879 -43.469  26.381  1.00 59.54           O  
HETATM 6294  O   HOH B 718      83.310 -25.381   1.670  1.00 71.10           O  
HETATM 6295  O   HOH B 719      62.870 -12.365   6.915  1.00 69.80           O  
HETATM 6296  O   HOH B 720      68.741   1.600  30.891  1.00 48.41           O  
HETATM 6297  O   HOH B 721      65.266 -35.156  45.861  1.00 74.33           O  
HETATM 6298  O   HOH B 722      61.846 -28.329  28.818  1.00 61.77           O  
HETATM 6299  O   HOH B 723      53.353 -19.650  51.397  1.00 74.72           O  
HETATM 6300  O   HOH B 724      70.247 -27.221  27.691  1.00 72.08           O  
HETATM 6301  O   HOH B 725      79.495 -13.154  -0.528  1.00 53.05           O  
HETATM 6302  O   HOH B 726      44.486 -32.549  40.466  1.00 63.12           O  
HETATM 6303  O   HOH B 727      80.500 -11.873  15.836  1.00 63.72           O  
HETATM 6304  O   HOH B 728      63.611 -46.805  30.654  1.00 79.34           O  
HETATM 6305  O   HOH B 729      75.074 -34.231   1.755  1.00 41.10           O  
HETATM 6306  O   HOH B 730      75.247 -24.542   0.193  1.00 80.33           O  
HETATM 6307  O   HOH B 731      75.171  -4.253  32.742  1.00 87.92           O  
HETATM 6308  O   HOH B 732      79.408   0.514  10.693  1.00 61.74           O  
HETATM 6309  O   HOH B 733      95.965 -23.372  21.756  1.00 60.46           O  
HETATM 6310  O   HOH B 734      73.027 -27.991   0.730  1.00 59.28           O  
HETATM 6311  O   HOH B 735      84.533 -13.089   3.865  1.00 67.62           O  
HETATM 6312  O   HOH B 736      57.037   0.329  26.026  1.00 50.30           O  
HETATM 6313  O   HOH B 737      67.647 -27.496  27.658  1.00 55.96           O  
HETATM 6314  O   HOH B 738      84.806 -17.932  26.669  1.00 49.24           O  
HETATM 6315  O   HOH B 739      80.979   0.098  27.112  1.00 55.43           O  
HETATM 6316  O   HOH B 740      85.180 -17.280  10.350  1.00 61.29           O  
HETATM 6317  O   HOH B 741      98.452 -34.139  11.487  1.00 56.56           O  
HETATM 6318  O   HOH B 742      71.755 -24.320   1.534  1.00 69.47           O  
HETATM 6319  O   HOH B 743      68.076  -2.904  32.434  1.00 54.98           O  
HETATM 6320  O   HOH B 744      60.594 -12.123   8.754  1.00 66.41           O  
CONECT 5710 5711 5715 5718                                                      
CONECT 5711 5710 5712 5716                                                      
CONECT 5712 5711 5713                                                           
CONECT 5713 5712 5714 5717                                                      
CONECT 5714 5713 5715                                                           
CONECT 5715 5710 5714