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***  T_2  ***

elNémo ID: 21062317175223878

Job options:

ID        	=	 21062317175223878
JOBID     	=	 T_2
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER T_2

HEADER    TRANSPORT PROTEIN                       23-SEP-20   7AGV              
TITLE     HIGH-RESOLUTION STRUCTURE OF THE K+/H+ ANTIPORTER SUBUNIT KHTT IN     
TITLE    2 COMPLEX WITH C-DI-AMP                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: K(+)/H(+) ANTIPORTER SUBUNIT KHTT;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: KHTT, YHAT, BSU09860;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    REGULATORY PROTEIN OF K+/H+ ANTIPORTER; C-DI-AMP BINDING PROTEIN,     
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.B.CEREIJA,J.P.GUERRA,J.H.MORAIS-CABRAL                              
REVDAT   3   14-APR-21 7AGV    1       JRNL                                     
REVDAT   2   07-APR-21 7AGV    1       JRNL                                     
REVDAT   1   31-MAR-21 7AGV    0                                                
JRNL        AUTH   T.B.CEREIJA,J.P.L.GUERRA,J.M.P.JORGE,J.H.MORAIS-CABRAL       
JRNL        TITL   C-DI-AMP, A LIKELY MASTER REGULATOR OF BACTERIAL K +         
JRNL        TITL 2 HOMEOSTASIS MACHINERY, ACTIVATES A K + EXPORTER.             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 118       2021              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   33790011                                                     
JRNL        DOI    10.1073/PNAS.2020653118                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 124712                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6261                            
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 81.4620 -  5.7477    0.94     3854   210  0.2113 0.2350        
REMARK   3     2  5.7477 -  4.5622    0.97     3936   185  0.1758 0.2215        
REMARK   3     3  4.5622 -  3.9856    0.97     3890   232  0.1606 0.1854        
REMARK   3     4  3.9856 -  3.6212    0.97     3943   199  0.1782 0.2101        
REMARK   3     5  3.6212 -  3.3616    0.98     3911   204  0.1925 0.2229        
REMARK   3     6  3.3616 -  3.1634    0.98     3914   217  0.2120 0.2676        
REMARK   3     7  3.1634 -  3.0050    0.98     3954   208  0.2108 0.2477        
REMARK   3     8  3.0050 -  2.8742    0.98     3943   199  0.2227 0.2785        
REMARK   3     9  2.8742 -  2.7635    0.98     3927   226  0.2191 0.2564        
REMARK   3    10  2.7635 -  2.6681    0.99     3933   238  0.2121 0.2466        
REMARK   3    11  2.6681 -  2.5847    0.99     3966   199  0.2132 0.2714        
REMARK   3    12  2.5847 -  2.5108    0.98     3945   199  0.2220 0.2683        
REMARK   3    13  2.5108 -  2.4447    0.98     3925   220  0.2216 0.2684        
REMARK   3    14  2.4447 -  2.3851    0.99     3989   205  0.2110 0.2563        
REMARK   3    15  2.3851 -  2.3308    0.98     3925   201  0.2273 0.2699        
REMARK   3    16  2.3308 -  2.2812    0.99     3960   193  0.2286 0.2866        
REMARK   3    17  2.2812 -  2.2356    0.99     3983   219  0.2224 0.2786        
REMARK   3    18  2.2356 -  2.1934    0.99     3978   185  0.2335 0.2813        
REMARK   3    19  2.1934 -  2.1542    0.99     3968   200  0.2400 0.2962        
REMARK   3    20  2.1542 -  2.1177    0.99     4033   190  0.2350 0.2790        
REMARK   3    21  2.1177 -  2.0836    0.99     3923   208  0.2453 0.3031        
REMARK   3    22  2.0836 -  2.0515    0.99     3950   221  0.2452 0.2841        
REMARK   3    23  2.0515 -  2.0213    0.99     3974   194  0.2517 0.2896        
REMARK   3    24  2.0213 -  1.9929    0.99     3995   207  0.2552 0.2827        
REMARK   3    25  1.9929 -  1.9659    0.99     3923   230  0.2494 0.2757        
REMARK   3    26  1.9659 -  1.9404    0.99     4000   226  0.2510 0.2914        
REMARK   3    27  1.9404 -  1.9161    0.99     3915   192  0.2665 0.3016        
REMARK   3    28  1.9161 -  1.8930    0.99     3988   213  0.2792 0.2996        
REMARK   3    29  1.8930 -  1.8710    0.99     3952   222  0.2955 0.3104        
REMARK   3    30  1.8710 -  1.8500    0.99     3954   219  0.3196 0.3680        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.57                          
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      :  0.009          10984                                  
REMARK   3   ANGLE     :  1.187          14833                                  
REMARK   3   CHIRALITY :  0.083           1645                                  
REMARK   3   PLANARITY :  0.004           1910                                  
REMARK   3   DIHEDRAL  : 14.532           4271                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 39                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 30 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6148  73.7795   0.5867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1307 T22:   0.1937                                     
REMARK   3      T33:   0.2941 T12:  -0.0139                                     
REMARK   3      T13:   0.0088 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9294 L22:   7.6040                                     
REMARK   3      L33:   8.3372 L12:   2.4972                                     
REMARK   3      L13:   0.4814 L23:   3.3178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0397 S12:  -0.1925 S13:  -0.0887                       
REMARK   3      S21:  -0.0151 S22:   0.1631 S23:  -0.7177                       
REMARK   3      S31:  -0.1683 S32:   0.1987 S33:  -0.1160                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  58.1980  77.9552  -3.9736              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1403 T22:   0.2283                                     
REMARK   3      T33:   0.2607 T12:  -0.0206                                     
REMARK   3      T13:  -0.0050 T23:  -0.0368                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3337 L22:   5.3299                                     
REMARK   3      L33:   7.0660 L12:  -0.2016                                     
REMARK   3      L13:  -0.4846 L23:  -2.5004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0888 S12:   0.0762 S13:  -0.1305                       
REMARK   3      S21:  -0.0643 S22:  -0.0255 S23:   0.1609                       
REMARK   3      S31:  -0.1337 S32:  -0.0476 S33:   0.0876                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  73.6509  87.0320 -15.9222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6331 T22:   0.8519                                     
REMARK   3      T33:   0.5157 T12:  -0.0298                                     
REMARK   3      T13:   0.1369 T23:   0.1008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7852 L22:   3.0285                                     
REMARK   3      L33:   6.8447 L12:  -0.3580                                     
REMARK   3      L13:  -0.3061 L23:  -3.4645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6149 S12:   1.0823 S13:   1.0494                       
REMARK   3      S21:  -0.1685 S22:  -1.2876 S23:  -0.8755                       
REMARK   3      S31:  -0.6407 S32:   0.5949 S33:   0.3313                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  69.8457  90.6850 -30.9084              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0123 T22:   0.8259                                     
REMARK   3      T33:   0.4866 T12:   0.2019                                     
REMARK   3      T13:   0.1685 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3510 L22:   9.4800                                     
REMARK   3      L33:   6.5392 L12:   1.9746                                     
REMARK   3      L13:  -1.5814 L23:   0.3883                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4483 S12:  -0.1620 S13:   0.5961                       
REMARK   3      S21:  -0.8394 S22:  -0.2921 S23:   0.0927                       
REMARK   3      S31:  -1.5648 S32:  -0.1819 S33:  -0.2965                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 30 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  49.0873  86.1499  -8.1721              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2908 T22:   0.3694                                     
REMARK   3      T33:   0.5299 T12:   0.0111                                     
REMARK   3      T13:  -0.1233 T23:   0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5831 L22:   7.5232                                     
REMARK   3      L33:   8.4520 L12:   1.1174                                     
REMARK   3      L13:  -0.3207 L23:   0.4978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1515 S12:   0.3733 S13:  -0.3934                       
REMARK   3      S21:  -0.7265 S22:   0.2183 S23:   1.5360                       
REMARK   3      S31:   0.3904 S32:  -0.9686 S33:  -0.0459                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6448  86.4265   0.7086              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3664 T22:   0.3292                                     
REMARK   3      T33:   0.4301 T12:   0.1440                                     
REMARK   3      T13:   0.0353 T23:   0.0739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1804 L22:   7.5642                                     
REMARK   3      L33:   8.9167 L12:  -0.1557                                     
REMARK   3      L13:  -3.5546 L23:  -0.7378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1430 S12:  -0.2480 S13:   0.3700                       
REMARK   3      S21:   0.9367 S22:   0.6214 S23:   1.2924                       
REMARK   3      S31:  -0.0363 S32:  -0.6478 S33:  -0.4203                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 56 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6137  74.7321 -10.5974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2854 T22:   0.2817                                     
REMARK   3      T33:   0.1654 T12:   0.0138                                     
REMARK   3      T13:   0.0527 T23:  -0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0944 L22:   7.1879                                     
REMARK   3      L33:   3.2229 L12:   0.2678                                     
REMARK   3      L13:   0.7728 L23:   1.0983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0849 S12:   0.5123 S13:  -0.2814                       
REMARK   3      S21:  -0.6179 S22:   0.1610 S23:  -0.2388                       
REMARK   3      S31:   0.2963 S32:   0.3068 S33:  -0.1455                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 103 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  65.7066  66.3114 -26.8411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9081 T22:   0.8317                                     
REMARK   3      T33:   0.5126 T12:   0.2220                                     
REMARK   3      T13:  -0.0988 T23:  -0.1759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3408 L22:   7.2333                                     
REMARK   3      L33:   8.6686 L12:  -2.4833                                     
REMARK   3      L13:  -8.0284 L23:   2.3599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2750 S12:   1.1880 S13:  -1.3073                       
REMARK   3      S21:  -1.0909 S22:  -1.1914 S23:   0.4407                       
REMARK   3      S31:   0.5353 S32:  -0.6231 S33:   0.9272                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 104 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2622  68.4304 -29.8262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8796 T22:   0.7925                                     
REMARK   3      T33:   0.3832 T12:   0.1405                                     
REMARK   3      T13:   0.1019 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2099 L22:   8.7230                                     
REMARK   3      L33:   7.1522 L12:   0.2232                                     
REMARK   3      L13:  -4.0254 L23:  -2.1370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5085 S12:   0.2138 S13:  -0.3584                       
REMARK   3      S21:  -0.6229 S22:  -0.0465 S23:  -0.6121                       
REMARK   3      S31:   1.1261 S32:  -0.2018 S33:   0.4697                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 30 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5336  44.4802  -1.4569              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.1914                                     
REMARK   3      T33:   0.3237 T12:   0.0005                                     
REMARK   3      T13:  -0.0250 T23:  -0.0531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8039 L22:   2.2538                                     
REMARK   3      L33:   6.7160 L12:  -0.1606                                     
REMARK   3      L13:  -0.1210 L23:   0.0907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1152 S12:   0.5157 S13:   0.2824                       
REMARK   3      S21:  -0.6100 S22:  -0.0285 S23:   0.3638                       
REMARK   3      S31:  -0.3721 S32:  -0.0796 S33:  -0.0137                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 31 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  51.8853  42.7575  -4.1441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2430 T22:   0.2640                                     
REMARK   3      T33:   0.4193 T12:   0.0040                                     
REMARK   3      T13:   0.0397 T23:  -0.0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4317 L22:   8.9745                                     
REMARK   3      L33:   5.9177 L12:   2.2822                                     
REMARK   3      L13:  -1.7540 L23:   0.7948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0531 S12:   0.8184 S13:  -0.1674                       
REMARK   3      S21:  -1.2368 S22:   0.4323 S23:  -0.5082                       
REMARK   3      S31:   0.1234 S32:   0.1041 S33:  -0.1770                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 56 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  52.7572  52.6514  13.7650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2793 T22:   0.2392                                     
REMARK   3      T33:   0.2574 T12:  -0.0815                                     
REMARK   3      T13:  -0.0671 T23:   0.0280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3195 L22:   6.1944                                     
REMARK   3      L33:   3.7729 L12:   1.0567                                     
REMARK   3      L13:   1.0766 L23:   1.3367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1639 S12:  -0.4732 S13:  -0.0761                       
REMARK   3      S21:   0.3874 S22:  -0.0143 S23:  -0.1403                       
REMARK   3      S31:  -0.0582 S32:   0.1799 S33:  -0.1562                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 78 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  39.4641  58.4203  17.7440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4278 T22:   0.3901                                     
REMARK   3      T33:   0.3641 T12:  -0.0559                                     
REMARK   3      T13:   0.1052 T23:  -0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7151 L22:   5.9785                                     
REMARK   3      L33:   9.0990 L12:  -0.9274                                     
REMARK   3      L13:   0.2933 L23:   2.5396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3835 S12:  -0.7882 S13:   0.2060                       
REMARK   3      S21:   0.3826 S22:  -0.7116 S23:   0.7473                       
REMARK   3      S31:  -0.6317 S32:  -1.1948 S33:   0.3792                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 93 THROUGH 115 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  38.0949  61.2894  35.4297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7783 T22:   0.8379                                     
REMARK   3      T33:  -0.0678 T12:  -0.5174                                     
REMARK   3      T13:   0.4318 T23:  -0.3488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0580 L22:   1.5551                                     
REMARK   3      L33:   5.1470 L12:   0.2794                                     
REMARK   3      L13:  -0.5805 L23:   0.0431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3051 S12:  -0.6878 S13:   0.5682                       
REMARK   3      S21:   1.7983 S22:  -0.1452 S23:   0.0069                       
REMARK   3      S31:  -0.9914 S32:  -0.6912 S33:   0.3844                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 116 THROUGH 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  49.2699  57.9662  31.1581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9851 T22:   0.8607                                     
REMARK   3      T33:   0.6125 T12:  -0.3605                                     
REMARK   3      T13:  -0.1335 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1682 L22:   5.8305                                     
REMARK   3      L33:   7.1486 L12:  -2.6018                                     
REMARK   3      L13:  -0.9422 L23:   2.3383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0903 S12:  -0.7173 S13:   0.2412                       
REMARK   3      S21:   1.0737 S22:  -0.1707 S23:  -1.5433                       
REMARK   3      S31:  -0.5746 S32:   1.0531 S33:  -0.1548                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 142 THROUGH 158 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4667  62.4473  25.3183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0999 T22:   0.8541                                     
REMARK   3      T33:   0.7589 T12:   0.1283                                     
REMARK   3      T13:   0.4719 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2721 L22:   9.3188                                     
REMARK   3      L33:   6.6566 L12:  -2.7266                                     
REMARK   3      L13:  -2.1958 L23:  -1.1597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5011 S12:   0.7364 S13:   1.3332                       
REMARK   3      S21:   1.7547 S22:   0.2625 S23:   1.9058                       
REMARK   3      S31:  -2.4695 S32:  -1.5175 S33:  -0.6834                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 30 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  62.3027  53.8413   7.8233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3562 T22:   0.3200                                     
REMARK   3      T33:   0.6851 T12:   0.0383                                     
REMARK   3      T13:  -0.1654 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6401 L22:   5.5245                                     
REMARK   3      L33:   5.5596 L12:  -0.3630                                     
REMARK   3      L13:  -0.4716 L23:  -1.8145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2398 S12:   0.0945 S13:  -0.5769                       
REMARK   3      S21:   0.0754 S22:  -0.1404 S23:  -1.9541                       
REMARK   3      S31:   0.7651 S32:   0.7914 S33:  -0.0624                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 31 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6060  54.8258  -1.1186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2553 T22:   0.3406                                     
REMARK   3      T33:   0.4783 T12:  -0.0382                                     
REMARK   3      T13:   0.0317 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0532 L22:   6.7337                                     
REMARK   3      L33:   7.9558 L12:   0.1448                                     
REMARK   3      L13:   0.1420 L23:  -0.0640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:   0.6539 S13:  -0.1660                       
REMARK   3      S21:  -0.7801 S22:   0.0772 S23:  -1.0875                       
REMARK   3      S31:   0.1129 S32:   0.7521 S33:  -0.0924                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 56 THROUGH 66 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7247  52.5840   7.0919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2191 T22:   0.2515                                     
REMARK   3      T33:   0.2532 T12:  -0.0146                                     
REMARK   3      T13:  -0.0323 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7525 L22:   8.4922                                     
REMARK   3      L33:   5.7842 L12:   0.7414                                     
REMARK   3      L13:  -1.5400 L23:  -0.8831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1663 S12:  -0.0122 S13:   0.1849                       
REMARK   3      S21:   0.1430 S22:   0.2365 S23:  -0.4569                       
REMARK   3      S31:   0.0689 S32:  -0.3661 S33:  -0.0184                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 67 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0106  36.6223  12.9714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4485 T22:   0.3557                                     
REMARK   3      T33:   0.4280 T12:  -0.0762                                     
REMARK   3      T13:  -0.0003 T23:   0.0483                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6064 L22:   5.0098                                     
REMARK   3      L33:   4.7080 L12:  -4.0605                                     
REMARK   3      L13:   3.4430 L23:  -4.8208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2203 S12:  -1.0269 S13:  -0.5968                       
REMARK   3      S21:   1.3411 S22:   0.0535 S23:   0.7242                       
REMARK   3      S31:   0.3648 S32:  -0.4106 S33:  -0.0589                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  49.2662  39.4308  22.4953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5721 T22:   0.4758                                     
REMARK   3      T33:   0.3862 T12:   0.0053                                     
REMARK   3      T13:  -0.1117 T23:   0.1254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2938 L22:   7.7972                                     
REMARK   3      L33:   7.9528 L12:   4.0881                                     
REMARK   3      L13:  -4.0465 L23:  -1.7406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2978 S12:  -1.6116 S13:  -0.8655                       
REMARK   3      S21:   1.0704 S22:  -0.7125 S23:  -0.9576                       
REMARK   3      S31:  -0.0293 S32:   0.4030 S33:   0.2668                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 93 THROUGH 129 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7656  38.2202  28.3794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9674 T22:   0.6388                                     
REMARK   3      T33:   0.4342 T12:  -0.2858                                     
REMARK   3      T13:   0.1188 T23:  -0.0440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1434 L22:   4.9696                                     
REMARK   3      L33:   3.3449 L12:  -1.3102                                     
REMARK   3      L13:  -2.7534 L23:  -2.3607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2717 S12:  -0.7165 S13:  -0.4816                       
REMARK   3      S21:   0.8999 S22:  -0.6533 S23:   0.8170                       
REMARK   3      S31:   0.7169 S32:  -0.6448 S33:   0.2389                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5623  39.2532  26.5202              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8234 T22:   0.7715                                     
REMARK   3      T33:   0.5985 T12:  -0.3309                                     
REMARK   3      T13:   0.1499 T23:  -0.1469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3936 L22:   2.5026                                     
REMARK   3      L33:   8.0973 L12:  -0.9559                                     
REMARK   3      L13:  -1.9265 L23:  -0.2172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2510 S12:  -0.1934 S13:  -0.0515                       
REMARK   3      S21:   0.6639 S22:  -0.3724 S23:   2.2547                       
REMARK   3      S31:  -0.0972 S32:  -1.0796 S33:   0.0462                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 142 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3116  35.1594  30.9876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3377 T22:   0.8858                                     
REMARK   3      T33:   0.5378 T12:  -0.1214                                     
REMARK   3      T13:  -0.0237 T23:   0.1615                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3954 L22:   7.2231                                     
REMARK   3      L33:   3.9248 L12:  -3.9474                                     
REMARK   3      L13:  -0.3614 L23:  -4.2878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0964 S12:  -1.1719 S13:  -1.1214                       
REMARK   3      S21:   1.9804 S22:  -0.2202 S23:  -0.4658                       
REMARK   3      S31:   1.8643 S32:   1.0905 S33:   0.4312                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID -1 THROUGH 18 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4276  74.2257   0.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2915 T22:   0.2125                                     
REMARK   3      T33:   0.3977 T12:  -0.0259                                     
REMARK   3      T13:  -0.0174 T23:  -0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7819 L22:   2.7554                                     
REMARK   3      L33:   9.3478 L12:   1.2396                                     
REMARK   3      L13:   1.1334 L23:   0.5726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0110 S12:   0.1615 S13:   0.0548                       
REMARK   3      S21:  -0.6725 S22:  -0.1871 S23:   0.1876                       
REMARK   3      S31:   0.6113 S32:  -0.3496 S33:   0.1854                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 19 THROUGH 30 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4776  80.4963  -1.9989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2953 T22:   0.2215                                     
REMARK   3      T33:   0.5701 T12:  -0.0327                                     
REMARK   3      T13:   0.0375 T23:   0.1701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1066 L22:   2.2691                                     
REMARK   3      L33:   3.1570 L12:   0.1720                                     
REMARK   3      L13:   0.8002 L23:  -0.7442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1823 S12:   0.4425 S13:   1.1123                       
REMARK   3      S21:  -0.5331 S22:   0.3944 S23:   0.0475                       
REMARK   3      S31:  -0.0745 S32:   0.2637 S33:   0.3130                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 31 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9813  75.4048  -2.6715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3601 T22:   0.4264                                     
REMARK   3      T33:   0.5004 T12:  -0.0180                                     
REMARK   3      T13:   0.0463 T23:   0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2265 L22:   4.7945                                     
REMARK   3      L33:   4.2519 L12:   3.3066                                     
REMARK   3      L13:  -3.9054 L23:  -0.5648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3272 S12:   0.5109 S13:  -0.3673                       
REMARK   3      S21:  -0.9466 S22:   0.3880 S23:  -0.0444                       
REMARK   3      S31:   0.6707 S32:   0.0911 S33:  -0.0260                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 56 THROUGH 103 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5523  90.5608  20.9762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6035 T22:   0.4759                                     
REMARK   3      T33:   0.3482 T12:  -0.2028                                     
REMARK   3      T13:   0.0253 T23:  -0.0658                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0856 L22:   3.1658                                     
REMARK   3      L33:   4.1859 L12:   0.5427                                     
REMARK   3      L13:  -0.8357 L23:  -0.4750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3566 S12:  -0.5450 S13:   0.4199                       
REMARK   3      S21:   1.1119 S22:  -0.3995 S23:   0.2917                       
REMARK   3      S31:  -0.7209 S32:   0.0219 S33:  -0.0633                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 104 THROUGH 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6578  89.5549  32.7970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2238 T22:   0.9778                                     
REMARK   3      T33:   0.4768 T12:  -0.4500                                     
REMARK   3      T13:   0.0688 T23:  -0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5394 L22:   6.8354                                     
REMARK   3      L33:   5.4462 L12:  -1.4344                                     
REMARK   3      L13:  -1.4164 L23:   0.1834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4316 S12:  -0.5264 S13:   0.2442                       
REMARK   3      S21:   1.6810 S22:  -0.3309 S23:  -0.4369                       
REMARK   3      S31:  -1.5169 S32:   0.9017 S33:  -0.1000                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 142 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9788  94.1873  26.2750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1731 T22:   0.8021                                     
REMARK   3      T33:   0.7396 T12:   0.0202                                     
REMARK   3      T13:   0.4410 T23:   0.0686                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9558 L22:   6.8604                                     
REMARK   3      L33:   7.7094 L12:  -0.7552                                     
REMARK   3      L13:   1.1671 L23:  -0.1348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3992 S12:   0.1426 S13:   1.2780                       
REMARK   3      S21:   1.6591 S22:  -0.0155 S23:   1.6832                       
REMARK   3      S31:  -1.9050 S32:  -1.3593 S33:  -0.3389                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 0 THROUGH 30 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0112  87.0862   9.1488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3281 T22:   0.4677                                     
REMARK   3      T33:   0.6476 T12:  -0.0029                                     
REMARK   3      T13:  -0.1688 T23:   0.1522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9066 L22:   1.7724                                     
REMARK   3      L33:   6.4149 L12:   2.7752                                     
REMARK   3      L13:   0.0882 L23:   0.1108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0208 S12:  -0.1503 S13:  -0.3276                       
REMARK   3      S21:   0.7189 S22:  -0.1813 S23:  -2.0054                       
REMARK   3      S31:   0.5398 S32:   1.2023 S33:   0.0853                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 31 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4816  88.3796   0.4590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2452 T22:   0.2829                                     
REMARK   3      T33:   0.5046 T12:  -0.0671                                     
REMARK   3      T13:   0.0450 T23:   0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0195 L22:   4.8678                                     
REMARK   3      L33:   9.1455 L12:   0.9593                                     
REMARK   3      L13:  -1.5218 L23:   1.5029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0177 S12:   0.0920 S13:  -0.0379                       
REMARK   3      S21:  -0.5865 S22:   0.0144 S23:  -1.0708                       
REMARK   3      S31:   0.0176 S32:   0.7079 S33:  -0.0944                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 56 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0045  76.7952  10.9231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2223 T22:   0.3050                                     
REMARK   3      T33:   0.2892 T12:  -0.0607                                     
REMARK   3      T13:   0.0202 T23:   0.0658                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2725 L22:   6.5229                                     
REMARK   3      L33:   3.4661 L12:   0.6738                                     
REMARK   3      L13:  -0.3755 L23:  -0.4329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0384 S12:  -0.5615 S13:  -0.4778                       
REMARK   3      S21:   0.4300 S22:   0.0718 S23:   0.1709                       
REMARK   3      S31:   0.2928 S32:   0.0824 S33:  -0.0622                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 78 THROUGH 148 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0721  70.6949  27.3942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6515 T22:   0.6643                                     
REMARK   3      T33:   0.4270 T12:  -0.1735                                     
REMARK   3      T13:  -0.0084 T23:   0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4372 L22:   6.0546                                     
REMARK   3      L33:   4.9954 L12:  -1.1602                                     
REMARK   3      L13:  -3.2464 L23:  -0.6938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2312 S12:  -0.7989 S13:  -0.4964                       
REMARK   3      S21:   1.0085 S22:  -0.4149 S23:   0.4782                       
REMARK   3      S31:   0.3185 S32:   0.0865 S33:   0.2148                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 149 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5818  64.9063  35.0150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2443 T22:   1.1698                                     
REMARK   3      T33:   0.5817 T12:   0.1548                                     
REMARK   3      T13:  -0.1514 T23:   0.4856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9921 L22:   3.3308                                     
REMARK   3      L33:   3.0893 L12:  -4.1779                                     
REMARK   3      L13:  -0.7242 L23:   2.6377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1565 S12:  -1.0323 S13:  -2.3970                       
REMARK   3      S21:   1.0746 S22:  -0.5355 S23:  -0.0629                       
REMARK   3      S31:   0.8206 S32:   0.4891 S33:  -0.1172                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID -1 THROUGH 77 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5508  46.0928  -1.9381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1763 T22:   0.2038                                     
REMARK   3      T33:   0.3190 T12:   0.0056                                     
REMARK   3      T13:  -0.0029 T23:  -0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2938 L22:   7.1541                                     
REMARK   3      L33:   5.7280 L12:  -0.9611                                     
REMARK   3      L13:   0.6900 L23:  -1.0621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0236 S12:  -0.1789 S13:  -0.4413                       
REMARK   3      S21:   0.1058 S22:   0.0488 S23:  -0.2054                       
REMARK   3      S31:  -0.2812 S32:  -0.2627 S33:   0.0055                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 78 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1417  58.0107 -27.8755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9149 T22:   0.8152                                     
REMARK   3      T33:   0.5456 T12:   0.0900                                     
REMARK   3      T13:   0.2263 T23:   0.0813                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1668 L22:   7.7878                                     
REMARK   3      L33:   8.2979 L12:   1.9318                                     
REMARK   3      L13:  -1.1613 L23:   3.1976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6286 S12:  -0.1418 S13:   0.6077                       
REMARK   3      S21:  -0.6005 S22:  -0.1709 S23:  -0.0604                       
REMARK   3      S31:  -1.2230 S32:  -0.0867 S33:  -0.3668                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 0 THROUGH 92 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5830  50.5038  -9.6115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2847 T22:   0.3744                                     
REMARK   3      T33:   0.4143 T12:  -0.0072                                     
REMARK   3      T13:  -0.0753 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6251 L22:   8.1807                                     
REMARK   3      L33:   4.8963 L12:  -2.9959                                     
REMARK   3      L13:  -0.4642 L23:   1.9328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1494 S12:   0.3525 S13:  -0.4490                       
REMARK   3      S21:  -0.4491 S22:  -0.0732 S23:   1.2365                       
REMARK   3      S31:  -0.2564 S32:  -0.6036 S33:   0.2490                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 93 THROUGH 161 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1285  35.6447 -31.4059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8844 T22:   0.7989                                     
REMARK   3      T33:   0.5552 T12:   0.0097                                     
REMARK   3      T13:   0.1150 T23:  -0.0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5007 L22:   9.3947                                     
REMARK   3      L33:   8.8829 L12:   0.3957                                     
REMARK   3      L13:  -5.4523 L23:  -0.7606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6960 S12:  -0.1522 S13:  -0.8939                       
REMARK   3      S21:  -0.5004 S22:   0.0797 S23:  -0.5566                       
REMARK   3      S31:   0.9671 S32:  -0.3320 S33:   0.5474                       
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 7AGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292111012.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979260                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124845                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 127.600                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.85500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: SAD STRUCTURE FROM DATA COLLECTED AT SOLEIL          
REMARK 200  -PROXIMA1.                                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 4.6 260 MM      
REMARK 280  CALCIUM CHLORIDE 15% (V/V) 2-PROPANOL, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.79900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     PHE A   159                                                      
REMARK 465     LEU A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     VAL A   165                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     LEU B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLU B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     VAL B   165                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     PHE C   159                                                      
REMARK 465     LEU C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     GLY C   162                                                      
REMARK 465     GLU C   163                                                      
REMARK 465     GLY C   164                                                      
REMARK 465     VAL C   165                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     LEU D   160                                                      
REMARK 465     SER D   161                                                      
REMARK 465     GLY D   162                                                      
REMARK 465     GLU D   163                                                      
REMARK 465     GLY D   164                                                      
REMARK 465     VAL D   165                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     LEU E   160                                                      
REMARK 465     SER E   161                                                      
REMARK 465     GLY E   162                                                      
REMARK 465     GLU E   163                                                      
REMARK 465     GLY E   164                                                      
REMARK 465     VAL E   165                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     GLU F   163                                                      
REMARK 465     GLY F   164                                                      
REMARK 465     VAL F   165                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     PHE G   159                                                      
REMARK 465     LEU G   160                                                      
REMARK 465     SER G   161                                                      
REMARK 465     GLY G   162                                                      
REMARK 465     GLU G   163                                                      
REMARK 465     GLY G   164                                                      
REMARK 465     VAL G   165                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     SER H    -1                                                      
REMARK 465     GLY H   162                                                      
REMARK 465     GLU H   163                                                      
REMARK 465     GLY H   164                                                      
REMARK 465     VAL H   165                                                      
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    VAL A  70      -64.90    -98.01                                   
REMARK 500    SER A  84     -168.80   -163.25                                   
REMARK 500    GLU A  94     -165.15    -73.20                                   
REMARK 500    VAL B  70      -61.43   -105.92                                   
REMARK 500    VAL B  70      -61.43   -104.07                                   
REMARK 500    GLU B  94     -164.32   -112.36                                   
REMARK 500    GLN B 125       -3.17     78.53                                   
REMARK 500    GLN C 125       80.65     59.54                                   
REMARK 500    ASN D  41     -161.23   -110.64                                   
REMARK 500    VAL D  70      -60.47   -103.09                                   
REMARK 500    GLN D 125       -9.59     91.38                                   
REMARK 500    PRO E   9      121.62    -37.58                                   
REMARK 500    ILE E  11      -54.98   -126.56                                   
REMARK 500    ARG E  43      -70.23    -74.44                                   
REMARK 500    VAL E  70      -61.68   -104.34                                   
REMARK 500    ASN E 124     -128.35     57.97                                   
REMARK 500    ASN E 130       71.03     42.25                                   
REMARK 500    GLU E 138      161.62     67.48                                   
REMARK 500    ASN E 140       10.78     58.14                                   
REMARK 500    SER F  21        2.89    -64.72                                   
REMARK 500    VAL F  70      -62.89   -103.10                                   
REMARK 500    SER F 161      102.37   -170.06                                   
REMARK 500    SER G  21        1.01    -65.27                                   
REMARK 500    VAL G  70      -67.05    -97.92                                   
REMARK 500    GLU G  77      -24.64   -144.08                                   
REMARK 500    PHE G  83      -53.15     67.16                                   
REMARK 500    GLN G 125       83.69   -163.43                                   
REMARK 500    GLU G 126     -149.83     38.47                                   
REMARK 500    THR H  19     -167.36    -75.15                                   
REMARK 500    ASP H  44       76.47   -163.47                                   
REMARK 500    VAL H  70      -64.68   -100.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 108   OD1                                                    
REMARK 620 2 ASP A 108   OD2  53.2                                              
REMARK 620 3 GLN A 111   OE1  60.9  80.7                                        
REMARK 620 4 HOH A 301   O   108.7  85.8  56.5                                  
REMARK 620 5 GLN E 111   OE1  38.9  78.6  91.3 146.3                            
REMARK 620 6 HOH E 324   O    78.7  81.0 138.9 156.2  49.0                      
REMARK 620 7 HOH E 333   O   153.8 152.4 115.5  85.7 120.7  97.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 111   OE1                                                    
REMARK 620 2 HOH C 301   O    44.7                                              
REMARK 620 3 HOH C 325   O    46.7   2.5                                        
REMARK 620 4 ASP G 108   OD1  44.6   1.3   2.1                                  
REMARK 620 5 ASP G 108   OD2  44.0   2.2   2.8   1.0                            
REMARK 620 6 GLN G 111   OE1  46.2   3.1   1.4   2.1   2.2                      
REMARK 620 7 HOH G 312   O    45.1   3.0   2.2   1.8   1.4   1.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7AGY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AGW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AHT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7AHM   RELATED DB: PDB                                   
DBREF  7AGV A    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV B    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV C    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV D    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV E    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV F    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV G    2   165  UNP    O07535   KHTT_BACSU       2    165             
DBREF  7AGV H    2   165  UNP    O07535   KHTT_BACSU       2    165             
SEQADV 7AGV GLY A   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER A   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY A    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU A    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY B   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER B   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY B    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU B    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY C   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER C   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY C    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU C    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY D   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER D   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY D    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU D    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY E   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER E   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY E    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU E    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY F   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER F   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY F    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU F    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY G   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER G   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY G    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU G    1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY H   -2  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV SER H   -1  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV GLY H    0  UNP  O07535              EXPRESSION TAG                 
SEQADV 7AGV LEU H    1  UNP  O07535              EXPRESSION TAG                 
SEQRES   1 A  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 A  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 A  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 A  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 A  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 A  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 A  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 A  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 A  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 A  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 A  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 A  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 A  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 B  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 B  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 B  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 B  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 B  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 B  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 B  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 B  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 B  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 B  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 B  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 B  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 B  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 C  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 C  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 C  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 C  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 C  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 C  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 C  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 C  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 C  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 C  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 C  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 C  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 C  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 D  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 D  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 D  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 D  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 D  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 D  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 D  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 D  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 D  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 D  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 D  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 D  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 D  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 E  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 E  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 E  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 E  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 E  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 E  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 E  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 E  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 E  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 E  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 E  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 E  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 E  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 F  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 F  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 F  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 F  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 F  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 F  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 F  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 F  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 F  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 F  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 F  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 F  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 F  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 G  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 G  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 G  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 G  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 G  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 G  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 G  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 G  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 G  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 G  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 G  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 G  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 G  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
SEQRES   1 H  168  GLY SER GLY LEU ASN ILE LYS GLU ASN ASP LEU PRO GLY          
SEQRES   2 H  168  ILE GLY LYS LYS PHE GLU ILE GLU THR ARG SER HIS GLU          
SEQRES   3 H  168  LYS MET THR ILE ILE ILE HIS ASP ASP GLY ARG ARG GLU          
SEQRES   4 H  168  ILE TYR ARG PHE ASN ASP ARG ASP PRO ASP GLU LEU LEU          
SEQRES   5 H  168  SER ASN ILE SER LEU ASP ASP SER GLU ALA ARG GLN ILE          
SEQRES   6 H  168  ALA ALA ILE LEU GLY GLY MET VAL TYR LYS PRO GLN ALA          
SEQRES   7 H  168  LEU GLU SER ILE GLU MET ALA PHE SER ASP LEU ILE ILE          
SEQRES   8 H  168  GLU TRP PHE LYS VAL GLU LYS GLY ALA LYS SER ILE GLY          
SEQRES   9 H  168  ARG THR LEU GLY GLU LEU ASP VAL ARG GLN ASN TYR ASP          
SEQRES  10 H  168  VAL THR VAL ILE ALA ILE ILE LYS HIS ASN GLN GLU LYS          
SEQRES  11 H  168  LEU LEU ASN PRO GLY ALA ASP SER ILE ILE GLU GLU ASN          
SEQRES  12 H  168  ASP THR LEU VAL LEU SER GLY GLU ARG LYS HIS LEU LYS          
SEQRES  13 H  168  LYS LEU ILE HIS ASP PHE LEU SER GLY GLU GLY VAL              
HET     CA  A 201       1                                                       
HET    ACT  A 202       4                                                       
HET    ACT  A 203       4                                                       
HET    2BA  B 201      44                                                       
HET    ACT  B 202       4                                                       
HET    2BA  C 201      44                                                       
HET    ACT  C 202       4                                                       
HET    ACT  C 203       4                                                       
HET    ACT  D 201       4                                                       
HET    2BA  E 201      44                                                       
HET    ACT  E 202       4                                                       
HET    ACT  E 203       4                                                       
HET    ACT  F 201       4                                                       
HET     CA  G 201       1                                                       
HET    ACT  G 202       4                                                       
HET    2BA  H 201      44                                                       
HET    ACT  H 202       4                                                       
HET    ACT  H 203       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     2BA (2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-               
HETNAM   2 2BA  AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D:3',            
HETNAM   3 2BA  2'-J][1,3,7,9,2,8 ]TETRAOXADIPHOSPHACYCLODODECINE-3,5,          
HETNAM   4 2BA  10,12-TETROL 5,12-DIOXIDE                                       
HETSYN     2BA BIS-(3',5')-CYCLIC-DIMERIC-ADENOSINE-MONOPHOSPHATE               
FORMUL   9   CA    2(CA 2+)                                                     
FORMUL  10  ACT    12(C2 H3 O2 1-)                                              
FORMUL  12  2BA    4(C20 H24 N10 O12 P2)                                        
FORMUL  27  HOH   *480(H2 O)                                                    
HELIX    1 AA1 ASP A   55  GLY A   67  1                                  13    
HELIX    2 AA2 THR A  103  ASP A  108  1                                   6    
HELIX    3 AA3 ASP A  108  ASP A  114  1                                   7    
HELIX    4 AA4 GLU A  148  ASP A  158  1                                  11    
HELIX    5 AA5 ASP B   55  GLY B   67  1                                  13    
HELIX    6 AA6 THR B  103  ASP B  108  1                                   6    
HELIX    7 AA7 ASP B  108  ASP B  114  1                                   7    
HELIX    8 AA8 GLU B  148  PHE B  159  1                                  12    
HELIX    9 AA9 ASP C   55  GLY C   67  1                                  13    
HELIX   10 AB1 THR C  103  ASP C  108  1                                   6    
HELIX   11 AB2 ASP C  108  ASP C  114  1                                   7    
HELIX   12 AB3 GLU C  148  ASP C  158  1                                  11    
HELIX   13 AB4 ASP D   55  GLY D   67  1                                  13    
HELIX   14 AB5 THR D  103  ASP D  108  1                                   6    
HELIX   15 AB6 ASP D  108  ASP D  114  1                                   7    
HELIX   16 AB7 GLU D  148  PHE D  159  1                                  12    
HELIX   17 AB8 ASP E   55  GLY E   67  1                                  13    
HELIX   18 AB9 THR E  103  ASP E  108  1                                   6    
HELIX   19 AC1 ASP E  108  ASP E  114  1                                   7    
HELIX   20 AC2 GLU E  148  PHE E  159  1                                  12    
HELIX   21 AC3 ASP F   55  GLY F   67  1                                  13    
HELIX   22 AC4 THR F  103  ASP F  108  1                                   6    
HELIX   23 AC5 ASP F  108  ASP F  114  1                                   7    
HELIX   24 AC6 GLU F  148  SER F  161  1                                  14    
HELIX   25 AC7 ASP G   55  GLY G   67  1                                  13    
HELIX   26 AC8 THR G  103  ASP G  108  1                                   6    
HELIX   27 AC9 ASP G  108  ASP G  114  1                                   7    
HELIX   28 AD1 GLU G  148  ASP G  158  1                                  11    
HELIX   29 AD2 ASP H   55  GLY H   67  1                                  13    
HELIX   30 AD3 THR H  103  ASP H  108  1                                   6    
HELIX   31 AD4 ASP H  108  ASP H  114  1                                   7    
HELIX   32 AD5 GLU H  148  LEU H  160  1                                  13    
SHEET    1 AA1 5 ASN A   2  LEU A   8  0                                        
SHEET    2 AA1 5 GLY A  12  GLU A  18 -1  O  GLU A  16   N  LYS A   4           
SHEET    3 AA1 5 LYS A  24  HIS A  30 -1  O  MET A  25   N  ILE A  17           
SHEET    4 AA1 5 ARG A  35  PHE A  40 -1  O  GLU A  36   N  ILE A  28           
SHEET    5 AA1 5 LEU A  48  LEU A  54 -1  O  LEU A  49   N  ARG A  39           
SHEET    1 AA2 5 SER A  78  GLU A  80  0                                        
SHEET    2 AA2 5 ILE A  87  LYS A  92 -1  O  ILE A  88   N  ILE A  79           
SHEET    3 AA2 5 THR A 142  GLY A 147 -1  O  LEU A 143   N  PHE A  91           
SHEET    4 AA2 5 THR A 116  ILE A 121 -1  N  ILE A 121   O  THR A 142           
SHEET    5 AA2 5 LYS A 127  LEU A 129 -1  O  LEU A 128   N  ILE A 120           
SHEET    1 AA3 5 ASN B   2  LEU B   8  0                                        
SHEET    2 AA3 5 GLY B  12  GLU B  18 -1  O  GLY B  12   N  LEU B   8           
SHEET    3 AA3 5 LYS B  24  HIS B  30 -1  O  MET B  25   N  ILE B  17           
SHEET    4 AA3 5 ARG B  35  ASN B  41 -1  O  GLU B  36   N  ILE B  28           
SHEET    5 AA3 5 ASP B  44  LEU B  54 -1  O  LEU B  49   N  ARG B  39           
SHEET    1 AA4 5 SER B  78  GLU B  80  0                                        
SHEET    2 AA4 5 ILE B  87  LYS B  92 -1  O  ILE B  88   N  ILE B  79           
SHEET    3 AA4 5 THR B 142  GLY B 147 -1  O  LEU B 145   N  GLU B  89           
SHEET    4 AA4 5 THR B 116  ILE B 121 -1  N  ILE B 121   O  THR B 142           
SHEET    5 AA4 5 LYS B 127  LEU B 129 -1  O  LEU B 128   N  ILE B 120           
SHEET    1 AA510 ASP C  44  LEU C  54  0                                        
SHEET    2 AA510 ARG C  35  ASN C  41 -1  N  ARG C  39   O  LEU C  49           
SHEET    3 AA510 LYS C  24  HIS C  30 -1  N  ILE C  28   O  GLU C  36           
SHEET    4 AA510 GLY C  12  GLU C  18 -1  N  ILE C  17   O  MET C  25           
SHEET    5 AA510 ASN C   2  LEU C   8 -1  N  ASN C   2   O  GLU C  18           
SHEET    6 AA510 ASN G   2  LEU G   8  1  O  ILE G   3   N  GLU C   5           
SHEET    7 AA510 GLY G  12  GLU G  18 -1  O  GLU G  16   N  LYS G   4           
SHEET    8 AA510 LYS G  24  HIS G  30 -1  O  MET G  25   N  ILE G  17           
SHEET    9 AA510 ARG G  35  PHE G  40 -1  O  GLU G  36   N  ILE G  28           
SHEET   10 AA510 LEU G  48  LEU G  54 -1  O  LEU G  49   N  ARG G  39           
SHEET    1 AA6 5 SER C  78  GLU C  80  0                                        
SHEET    2 AA6 5 ILE C  87  LYS C  92 -1  O  ILE C  88   N  ILE C  79           
SHEET    3 AA6 5 THR C 142  GLY C 147 -1  O  LEU C 145   N  GLU C  89           
SHEET    4 AA6 5 THR C 116  LYS C 122 -1  N  ILE C 121   O  THR C 142           
SHEET    5 AA6 5 GLU C 126  LEU C 129 -1  O  LEU C 128   N  ILE C 120           
SHEET    1 AA7 5 ASN D   2  LEU D   8  0                                        
SHEET    2 AA7 5 GLY D  12  GLU D  18 -1  O  GLU D  16   N  LYS D   4           
SHEET    3 AA7 5 LYS D  24  HIS D  30 -1  O  MET D  25   N  ILE D  17           
SHEET    4 AA7 5 ARG D  35  PHE D  40 -1  O  GLU D  36   N  ILE D  28           
SHEET    5 AA7 5 LEU D  48  LEU D  54 -1  O  LEU D  49   N  ARG D  39           
SHEET    1 AA8 5 SER D  78  GLU D  80  0                                        
SHEET    2 AA8 5 ILE D  87  LYS D  92 -1  O  ILE D  88   N  ILE D  79           
SHEET    3 AA8 5 THR D 142  GLY D 147 -1  O  LEU D 145   N  GLU D  89           
SHEET    4 AA8 5 THR D 116  ILE D 121 -1  N  ALA D 119   O  VAL D 144           
SHEET    5 AA8 5 LYS D 127  LEU D 129 -1  O  LEU D 128   N  ILE D 120           
SHEET    1 AA9 5 ASN E   2  LEU E   8  0                                        
SHEET    2 AA9 5 GLY E  12  GLU E  18 -1  O  GLU E  16   N  LYS E   4           
SHEET    3 AA9 5 LYS E  24  HIS E  30 -1  O  MET E  25   N  ILE E  17           
SHEET    4 AA9 5 ARG E  35  PHE E  40 -1  O  GLU E  36   N  ILE E  28           
SHEET    5 AA9 5 LEU E  48  LEU E  54 -1  O  LEU E  49   N  ARG E  39           
SHEET    1 AB1 5 SER E  78  GLU E  80  0                                        
SHEET    2 AB1 5 ILE E  87  LYS E  92 -1  O  ILE E  88   N  ILE E  79           
SHEET    3 AB1 5 THR E 142  GLY E 147 -1  O  LEU E 143   N  PHE E  91           
SHEET    4 AB1 5 THR E 116  LYS E 122 -1  N  ILE E 121   O  THR E 142           
SHEET    5 AB1 5 GLU E 126  LEU E 129 -1  O  LEU E 128   N  ILE E 120           
SHEET    1 AB2 5 ASN F   2  LEU F   8  0                                        
SHEET    2 AB2 5 GLY F  12  GLU F  18 -1  O  GLU F  16   N  LYS F   4           
SHEET    3 AB2 5 LYS F  24  HIS F  30 -1  O  MET F  25   N  ILE F  17           
SHEET    4 AB2 5 ARG F  35  PHE F  40 -1  O  GLU F  36   N  ILE F  28           
SHEET    5 AB2 5 LEU F  48  LEU F  54 -1  O  LEU F  49   N  ARG F  39           
SHEET    1 AB3 5 SER F  78  GLU F  80  0                                        
SHEET    2 AB3 5 ILE F  87  LYS F  92 -1  O  ILE F  88   N  ILE F  79           
SHEET    3 AB3 5 THR F 142  GLY F 147 -1  O  LEU F 143   N  PHE F  91           
SHEET    4 AB3 5 THR F 116  ILE F 121 -1  N  ALA F 119   O  VAL F 144           
SHEET    5 AB3 5 LYS F 127  LEU F 129 -1  O  LEU F 128   N  ILE F 120           
SHEET    1 AB4 5 SER G  78  GLU G  80  0                                        
SHEET    2 AB4 5 ILE G  87  VAL G  93 -1  O  ILE G  88   N  ILE G  79           
SHEET    3 AB4 5 ASP G 141  GLY G 147 -1  O  LEU G 143   N  PHE G  91           
SHEET    4 AB4 5 THR G 116  ILE G 121 -1  N  ILE G 121   O  THR G 142           
SHEET    5 AB4 5 LYS G 127  LEU G 129 -1  O  LEU G 128   N  ILE G 120           
SHEET    1 AB5 5 ASN H   2  LEU H   8  0                                        
SHEET    2 AB5 5 GLY H  12  GLU H  18 -1  O  GLY H  12   N  LEU H   8           
SHEET    3 AB5 5 LYS H  24  HIS H  30 -1  O  MET H  25   N  ILE H  17           
SHEET    4 AB5 5 ARG H  35  ASN H  41 -1  O  GLU H  36   N  ILE H  28           
SHEET    5 AB5 5 ASP H  44  LEU H  54 -1  O  LEU H  54   N  ARG H  35           
SHEET    1 AB6 5 SER H  78  GLU H  80  0                                        
SHEET    2 AB6 5 ILE H  87  LYS H  92 -1  O  ILE H  88   N  ILE H  79           
SHEET    3 AB6 5 THR H 142  GLY H 147 -1  O  LEU H 145   N  GLU H  89           
SHEET    4 AB6 5 THR H 116  ILE H 121 -1  N  ALA H 119   O  VAL H 144           
SHEET    5 AB6 5 LYS H 127  LEU H 129 -1  O  LEU H 128   N  ILE H 120           
LINK         OD1 ASP A 108                CA    CA A 201     1555   1555  2.59  
LINK         OD2 ASP A 108                CA    CA A 201     1555   1555  2.29  
LINK         OE1 GLN A 111                CA    CA A 201     1555   1555  2.53  
LINK        CA    CA A 201                 O   HOH A 301     1555   1555  2.35  
LINK        CA    CA A 201                 OE1 GLN E 111     1456   1555  2.40  
LINK        CA    CA A 201                 O   HOH E 324     1555   1654  2.38  
LINK        CA    CA A 201                 O   HOH E 333     1555   1654  2.51  
LINK         OE1 GLN C 111                CA    CA G 201     1555   1556  2.68  
LINK         O   HOH C 301                CA    CA G 201     1554   1555  2.42  
LINK         O   HOH C 325                CA    CA G 201     1554   1555  2.54  
LINK         OD1 ASP G 108                CA    CA G 201     1555   1555  2.64  
LINK         OD2 ASP G 108                CA    CA G 201     1555   1555  2.32  
LINK         OE1 GLN G 111                CA    CA G 201     1555   1555  2.51  
LINK        CA    CA G 201                 O   HOH G 312     1555   1555  2.45  
CRYST1   72.945  127.598   81.881  90.00  95.80  90.00 P 1 21 1     16          
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      0.013709  0.000000  0.001393        0.00000                         
SCALE2      0.000000  0.007837  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012276        0.00000                         
ATOM      1  N   SER A  -1      71.831  89.814   1.209  1.00 89.08           N  
ANISOU    1  N   SER A  -1    12616   7576  13653  -2121    689   -718       N  
ATOM      2  CA  SER A  -1      72.011  89.794  -0.236  1.00 92.98           C  
ANISOU    2  CA  SER A  -1    13304   7979  14046  -2261    789   -240       C  
ATOM      3  C   SER A  -1      72.280  88.376  -0.743  1.00 91.93           C  
ANISOU    3  C   SER A  -1    12857   8414  13659  -2258    913   -134       C  
ATOM      4  O   SER A  -1      71.960  88.037  -1.885  1.00 88.44           O  
ANISOU    4  O   SER A  -1    12572   7995  13035  -2212    966    237       O  
ATOM      5  CB  SER A  -1      73.172  90.701  -0.629  1.00 93.51           C  
ANISOU    5  CB  SER A  -1    13440   7858  14232  -2753    943   -208       C  
ATOM      6  OG  SER A  -1      74.391  90.176  -0.136  1.00 88.26           O  
ANISOU    6  OG  SER A  -1    12312   7686  13537  -3043   1088   -528       O  
ATOM      7  N   GLY A   0      72.873  87.553   0.115  1.00 88.36           N  
ANISOU    7  N   GLY A   0    11953   8422  13198  -2295    929   -472       N  
ATOM      8  CA  GLY A   0      73.327  86.238  -0.288  1.00 76.05           C  
ANISOU    8  CA  GLY A   0    10047   7367  11482  -2296   1022   -436       C  
ATOM      9  C   GLY A   0      72.645  85.115   0.463  1.00 63.84           C  
ANISOU    9  C   GLY A   0     8259   6100   9897  -1971    874   -561       C  
ATOM     10  O   GLY A   0      72.564  85.109   1.697  1.00 57.77           O  
ANISOU   10  O   GLY A   0     7315   5424   9209  -1893    720   -865       O  
ATOM     11  N   LEU A   1      72.153  84.151  -0.300  1.00 56.37           N  
ANISOU   11  N   LEU A   1     7307   5310   8800  -1808    918   -329       N  
ATOM     12  CA  LEU A   1      71.487  83.014   0.262  1.00 49.09           C  
ANISOU   12  CA  LEU A   1     6164   4656   7832  -1506    772   -379       C  
ATOM     13  C   LEU A   1      72.505  82.018   0.810  1.00 39.75           C  
ANISOU   13  C   LEU A   1     4488   3907   6708  -1573    718   -599       C  
ATOM     14  O   LEU A   1      73.606  81.903   0.283  1.00 39.17           O  
ANISOU   14  O   LEU A   1     4241   3995   6647  -1754    844   -641       O  
ATOM     15  CB  LEU A   1      70.675  82.299  -0.828  1.00 51.16           C  
ANISOU   15  CB  LEU A   1     6579   4991   7869  -1293    800    -54       C  
ATOM     16  CG  LEU A   1      69.338  82.904  -1.234  1.00 60.32           C  
ANISOU   16  CG  LEU A   1     8128   5858   8933  -1025    690    187       C  
ATOM     17  CD1 LEU A   1      68.567  81.960  -2.155  1.00 50.92           C  
ANISOU   17  CD1 LEU A   1     6967   4893   7488   -824    651    425       C  
ATOM     18  CD2 LEU A   1      68.536  83.222   0.010  1.00 53.10           C  
ANISOU   18  CD2 LEU A   1     7161   4909   8106   -743    490    -26       C  
ATOM     19  N  AASN A   2      72.121  81.320   1.876  0.42 35.73           N  
ANISOU   19  N  AASN A   2     3805   3657   6113  -1307    457   -686       N  
ATOM     20  N  BASN A   2      72.127  81.332   1.878  0.58 35.12           N  
ANISOU   20  N  BASN A   2     3729   3578   6037  -1310    458   -688       N  
ATOM     21  CA AASN A   2      72.803  80.100   2.302  0.42 36.28           C  
ANISOU   21  CA AASN A   2     3482   4099   6205  -1223    303   -758       C  
ATOM     22  CA BASN A   2      72.799  80.103   2.277  0.58 36.50           C  
ANISOU   22  CA BASN A   2     3513   4123   6233  -1224    309   -754       C  
ATOM     23  C  AASN A   2      71.951  78.935   1.862  0.42 32.76           C  
ANISOU   23  C  AASN A   2     3100   3746   5603   -932    267   -514       C  
ATOM     24  C  BASN A   2      71.934  78.976   1.795  0.58 31.86           C  
ANISOU   24  C  BASN A   2     2999   3617   5488   -939    282   -508       C  
ATOM     25  O  AASN A   2      70.783  78.852   2.237  0.42 31.13           O  
ANISOU   25  O  AASN A   2     3088   3527   5211   -736    172   -402       O  
ATOM     26  O  BASN A   2      70.739  78.961   2.064  0.58 30.38           O  
ANISOU   26  O  BASN A   2     3028   3394   5120   -748    206   -388       O  
ATOM     27  CB AASN A   2      72.944  80.046   3.828  0.42 36.90           C  
ANISOU   27  CB AASN A   2     3405   4398   6217  -1166     -4   -949       C  
ATOM     28  CB BASN A   2      72.918  80.022   3.797  0.58 36.13           C  
ANISOU   28  CB BASN A   2     3312   4298   6116  -1159      0   -939       C  
ATOM     29  CG AASN A   2      73.917  78.971   4.285  0.42 42.55           C  
ANISOU   29  CG AASN A   2     3709   5439   7018  -1096   -242  -1007       C  
ATOM     30  CG BASN A   2      73.739  81.155   4.367  0.58 43.43           C  
ANISOU   30  CG BASN A   2     4148   5168   7187  -1474     -5  -1265       C  
ATOM     31  OD1AASN A   2      73.519  77.893   4.729  0.42 52.73           O  
ANISOU   31  OD1AASN A   2     4986   6882   8167   -841   -457   -835       O  
ATOM     32  OD1BASN A   2      74.659  81.668   3.714  0.58 39.82           O  
ANISOU   32  OD1BASN A   2     3652   4628   6851  -1680    182  -1296       O  
ATOM     33  ND2AASN A   2      75.202  79.260   4.168  0.42 41.55           N  
ANISOU   33  ND2AASN A   2     3355   5394   7040  -1252   -204  -1171       N  
ATOM     34  ND2BASN A   2      73.413  81.559   5.585  0.58 51.89           N  
ANISOU   34  ND2BASN A   2     5278   6335   8102  -1457   -202  -1455       N  
ATOM     35  N   ILE A   3      72.507  78.015   1.080  1.00 25.40           N  
ANISOU   35  N   ILE A   3     1972   2917   4762   -919    361   -487       N  
ATOM     36  CA  ILE A   3      71.673  76.887   0.608  1.00 22.86           C  
ANISOU   36  CA  ILE A   3     1733   2638   4313   -685    339   -302       C  
ATOM     37  C   ILE A   3      72.400  75.583   0.915  1.00 25.01           C  
ANISOU   37  C   ILE A   3     1676   3063   4763   -538    186   -373       C  
ATOM     38  O   ILE A   3      73.555  75.446   0.563  1.00 31.52           O  
ANISOU   38  O   ILE A   3     2228   3956   5790   -610    270   -555       O  
ATOM     39  CB  ILE A   3      71.457  76.995  -0.923  1.00 31.76           C  
ANISOU   39  CB  ILE A   3     3035   3674   5357   -792    630   -209       C  
ATOM     40  CG1 ILE A   3      70.645  78.250  -1.255  1.00 35.36           C  
ANISOU   40  CG1 ILE A   3     3874   3908   5654   -861    690    -53       C  
ATOM     41  CG2 ILE A   3      70.734  75.772  -1.476  1.00 32.24           C  
ANISOU   41  CG2 ILE A   3     3130   3809   5312   -605    614   -114       C  
ATOM     42  CD1 ILE A   3      70.744  78.638  -2.716  1.00 44.90           C  
ANISOU   42  CD1 ILE A   3     5304   5026   6730  -1067    952     78       C  
ATOM     43  N   LYS A   4      71.712  74.656   1.583  1.00 28.17           N  
ANISOU   43  N   LYS A   4     2144   3496   5062   -324    -42   -222       N  
ATOM     44  CA  LYS A   4      72.317  73.367   1.897  1.00 30.93           C  
ANISOU   44  CA  LYS A   4     2264   3876   5612   -137   -248   -220       C  
ATOM     45  C   LYS A   4      71.573  72.366   1.052  1.00 29.60           C  
ANISOU   45  C   LYS A   4     2236   3588   5425    -38   -127   -122       C  
ATOM     46  O   LYS A   4      70.367  72.319   1.107  1.00 29.45           O  
ANISOU   46  O   LYS A   4     2483   3548   5159    -44   -114     41       O  
ATOM     47  CB  LYS A   4      72.015  72.974   3.338  1.00 31.52           C  
ANISOU   47  CB  LYS A   4     2421   4029   5527    -29   -613    -49       C  
ATOM     48  CG  LYS A   4      72.837  73.583   4.408  1.00 54.61           C  
ANISOU   48  CG  LYS A   4     5173   7131   8447    -87   -864   -162       C  
ATOM     49  CD  LYS A   4      72.819  72.621   5.596  1.00 65.79           C  
ANISOU   49  CD  LYS A   4     6640   8624   9732     74  -1286     68       C  
ATOM     50  CE  LYS A   4      72.601  71.186   5.106  1.00 56.32           C  
ANISOU   50  CE  LYS A   4     5496   7193   8711    286  -1326    269       C  
ATOM     51  NZ  LYS A   4      73.545  70.192   5.664  1.00 49.85           N  
ANISOU   51  NZ  LYS A   4     4579   6323   8041    515  -1657    349       N  
ATOM     52  N  AGLU A   5      72.285  71.573   0.260  0.52 29.87           N  
ANISOU   52  N  AGLU A   5     2052   3562   5735     40    -23   -285       N  
ATOM     53  N  BGLU A   5      72.325  71.551   0.312  0.48 29.50           N  
ANISOU   53  N  BGLU A   5     1993   3515   5699     48    -38   -286       N  
ATOM     54  CA AGLU A   5      71.612  70.568  -0.543  0.52 25.79           C  
ANISOU   54  CA AGLU A   5     1668   2918   5214    107     91   -268       C  
ATOM     55  CA BGLU A   5      71.766  70.548  -0.582  0.48 30.26           C  
ANISOU   55  CA BGLU A   5     2193   3486   5818    113     99   -298       C  
ATOM     56  C  AGLU A   5      71.996  69.191  -0.026  0.52 31.27           C  
ANISOU   56  C  AGLU A   5     2242   3421   6219    363   -168   -245       C  
ATOM     57  C  BGLU A   5      72.028  69.164   0.002  0.48 25.74           C  
ANISOU   57  C  BGLU A   5     1533   2716   5530    372   -179   -245       C  
ATOM     58  O  AGLU A   5      73.141  68.950   0.361  0.52 31.22           O  
ANISOU   58  O  AGLU A   5     2028   3414   6419    491   -324   -356       O  
ATOM     59  O  BGLU A   5      73.133  68.893   0.477  0.48 31.88           O  
ANISOU   59  O  BGLU A   5     2119   3487   6507    508   -362   -333       O  
ATOM     60  CB AGLU A   5      72.015  70.684  -2.017  0.52 37.45           C  
ANISOU   60  CB AGLU A   5     3050   4451   6729    -26    470   -529       C  
ATOM     61  CB BGLU A   5      72.452  70.661  -1.957  0.48 25.18           C  
ANISOU   61  CB BGLU A   5     1415   2906   5245     -7    456   -591       C  
ATOM     62  CG AGLU A   5      71.227  69.748  -2.926  0.52 25.45           C  
ANISOU   62  CG AGLU A   5     1693   2848   5128    -12    597   -574       C  
ATOM     63  CG BGLU A   5      72.232  72.022  -2.612  0.48 33.79           C  
ANISOU   63  CG BGLU A   5     2668   4123   6047   -290    714   -561       C  
ATOM     64  CD AGLU A   5      71.770  69.678  -4.341  0.52 37.85           C  
ANISOU   64  CD AGLU A   5     3167   4528   6687   -153    964   -892       C  
ATOM     65  CD BGLU A   5      72.820  72.121  -4.015  0.48 45.89           C  
ANISOU   65  CD BGLU A   5     4209   5757   7471   -473   1058   -773       C  
ATOM     66  OE1AGLU A   5      72.659  70.482  -4.682  0.52 39.60           O  
ANISOU   66  OE1AGLU A   5     3330   4886   6828   -302   1110   -990       O  
ATOM     67  OE1BGLU A   5      73.676  71.284  -4.380  0.48 47.72           O  
ANISOU   67  OE1BGLU A   5     4227   5998   7907   -386   1118  -1039       O  
ATOM     68  OE2AGLU A   5      71.291  68.821  -5.110  0.52 41.49           O  
ANISOU   68  OE2AGLU A   5     3698   4944   7121   -152   1081  -1037       O  
ATOM     69  OE2BGLU A   5      72.431  73.056  -4.749  0.48 55.18           O  
ANISOU   69  OE2BGLU A   5     5625   6991   8348   -708   1254   -665       O  
ATOM     70  N   ASN A   6      71.028  68.288  -0.026  1.00 33.96           N  
ANISOU   70  N   ASN A   6     2835   3586   6482    395   -218    -85       N  
ATOM     71  CA  ASN A   6      71.266  66.921   0.378  1.00 38.40           C  
ANISOU   71  CA  ASN A   6     3392   3839   7358    617   -460    -12       C  
ATOM     72  C   ASN A   6      70.542  66.004  -0.571  1.00 33.69           C  
ANISOU   72  C   ASN A   6     2950   3037   6815    567   -260   -124       C  
ATOM     73  O   ASN A   6      69.414  66.272  -0.954  1.00 33.17           O  
ANISOU   73  O   ASN A   6     3102   3089   6413    350    -99    -64       O  
ATOM     74  CB  ASN A   6      70.745  66.693   1.793  1.00 50.19           C  
ANISOU   74  CB  ASN A   6     5138   5285   8647    619   -805    397       C  
ATOM     75  CG  ASN A   6      71.633  67.317   2.838  1.00 56.20           C  
ANISOU   75  CG  ASN A   6     5736   6234   9384    702  -1096    467       C  
ATOM     76  OD1 ASN A   6      71.435  68.464   3.245  1.00 52.76           O  
ANISOU   76  OD1 ASN A   6     5316   6083   8647    535  -1049    471       O  
ATOM     77  ND2 ASN A   6      72.637  66.577   3.262  1.00 46.99           N  
ANISOU   77  ND2 ASN A   6     4490   4954   8412    901  -1334    451       N  
ATOM     78  N  AASP A   7      71.207  64.911  -0.929  0.52 34.90           N  
ANISOU   78  N  AASP A   7     2970   2890   7402    775   -295   -326       N  
ATOM     79  N  BASP A   7      71.189  64.909  -0.956  0.48 35.33           N  
ANISOU   79  N  BASP A   7     3026   2943   7455    772   -287   -331       N  
ATOM     80  CA AASP A   7      70.586  63.860  -1.717  0.52 38.97           C  
ANISOU   80  CA AASP A   7     3636   3121   8050    736   -145   -486       C  
ATOM     81  CA BASP A   7      70.518  63.921  -1.793  0.48 37.34           C  
ANISOU   81  CA BASP A   7     3435   2937   7817    715   -117   -498       C  
ATOM     82  C  AASP A   7      69.553  63.119  -0.866  0.52 43.68           C  
ANISOU   82  C  AASP A   7     4611   3437   8550    646   -369    -89       C  
ATOM     83  C  BASP A   7      69.616  63.027  -0.951  0.48 43.47           C  
ANISOU   83  C  BASP A   7     4569   3377   8569    664   -359   -125       C  
ATOM     84  O  AASP A   7      69.769  62.911   0.326  0.52 41.53           O  
ANISOU   84  O  AASP A   7     4452   3080   8246    733   -693    263       O  
ATOM     85  O  BASP A   7      69.989  62.617   0.146  0.48 44.41           O  
ANISOU   85  O  BASP A   7     4784   3375   8715    786   -686    179       O  
ATOM     86  CB AASP A   7      71.667  62.882  -2.200  0.52 39.67           C  
ANISOU   86  CB AASP A   7     3538   3048   8488    920   -141   -806       C  
ATOM     87  CB BASP A   7      71.539  63.074  -2.560  0.48 43.96           C  
ANISOU   87  CB BASP A   7     4061   3664   8976    856    -20   -897       C  
ATOM     88  CG AASP A   7      71.094  61.712  -2.956  0.52 48.52           C  
ANISOU   88  CG AASP A   7     4817   3866   9753    872     -8  -1008       C  
ATOM     89  CG BASP A   7      72.262  63.870  -3.622  0.48 58.61           C  
ANISOU   89  CG BASP A   7     5641   5885  10744    748    327  -1290       C  
ATOM     90  OD1AASP A   7      70.282  61.943  -3.877  0.52 51.39           O  
ANISOU   90  OD1AASP A   7     5258   4348   9917    642    287  -1214       O  
ATOM     91  OD1BASP A   7      71.772  63.899  -4.771  0.48 53.22           O  
ANISOU   91  OD1BASP A   7     5007   5319   9896    558    661  -1562       O  
ATOM     92  OD2AASP A   7      71.439  60.560  -2.614  0.52 55.36           O  
ANISOU   92  OD2AASP A   7     5752   4375  10907   1054   -211   -968       O  
ATOM     93  OD2BASP A   7      73.306  64.484  -3.303  0.48 69.55           O  
ANISOU   93  OD2BASP A   7     6801   7464  12162    801    267  -1318       O  
ATOM     94  N   LEU A   8      68.424  62.743  -1.470  1.00 42.58           N  
ANISOU   94  N   LEU A   8     4680   3270   8228    387   -177   -152       N  
ATOM     95  CA  LEU A   8      67.515  61.801  -0.841  1.00 43.13           C  
ANISOU   95  CA  LEU A   8     5079   3013   8294    229   -312    135       C  
ATOM     96  C   LEU A   8      67.506  60.593  -1.753  1.00 39.06           C  
ANISOU   96  C   LEU A   8     4607   2159   8078    232   -184   -205       C  
ATOM     97  O   LEU A   8      66.785  60.581  -2.750  1.00 37.38           O  
ANISOU   97  O   LEU A   8     4396   2040   7768      1     71   -509       O  
ATOM     98  CB  LEU A   8      66.117  62.384  -0.758  1.00 34.28           C  
ANISOU   98  CB  LEU A   8     4096   2265   6665   -133   -178    269       C  
ATOM     99  CG  LEU A   8      66.044  63.781  -0.155  1.00 38.06           C  
ANISOU   99  CG  LEU A   8     4487   3215   6757   -142   -205    441       C  
ATOM    100  CD1 LEU A   8      64.628  64.320  -0.229  1.00 36.40           C  
ANISOU  100  CD1 LEU A   8     4332   3358   6141   -427    -62    466       C  
ATOM    101  CD2 LEU A   8      66.545  63.737   1.287  1.00 46.38           C  
ANISOU  101  CD2 LEU A   8     5644   4171   7806    -38   -503    817       C  
ATOM    102  N   PRO A   9      68.321  59.577  -1.426  1.00 48.62           N  
ANISOU  102  N   PRO A   9     5849   3033   9591    485   -372   -179       N  
ATOM    103  CA  PRO A   9      68.569  58.442  -2.319  1.00 62.09           C  
ANISOU  103  CA  PRO A   9     7546   4435  11610    557   -252   -562       C  
ATOM    104  C   PRO A   9      67.287  57.778  -2.808  1.00 67.87           C  
ANISOU  104  C   PRO A   9     8554   5012  12222    195    -88   -652       C  
ATOM    105  O   PRO A   9      66.474  57.306  -2.001  1.00 49.27           O  
ANISOU  105  O   PRO A   9     6536   2451   9734    -22   -205   -283       O  
ATOM    106  CB  PRO A   9      69.395  57.487  -1.450  1.00 65.93           C  
ANISOU  106  CB  PRO A   9     8139   4516  12395    863   -575   -326       C  
ATOM    107  CG  PRO A   9      70.073  58.401  -0.456  1.00 55.38           C  
ANISOU  107  CG  PRO A   9     6659   3458  10926   1028   -821    -18       C  
ATOM    108  CD  PRO A   9      69.062  59.455  -0.157  1.00 52.96           C  
ANISOU  108  CD  PRO A   9     6453   3488  10183    716   -731    207       C  
ATOM    109  N   GLY A  10      67.123  57.775  -4.129  1.00 48.02           N  
ANISOU  109  N   GLY A  10     5886   2664   9694     82    199  -1163       N  
ATOM    110  CA  GLY A  10      65.993  57.157  -4.797  1.00 49.34           C  
ANISOU  110  CA  GLY A  10     6234   2782   9731   -277    352  -1373       C  
ATOM    111  C   GLY A  10      64.713  57.974  -4.729  1.00 44.79           C  
ANISOU  111  C   GLY A  10     5707   2594   8718   -661    417  -1229       C  
ATOM    112  O   GLY A  10      63.681  57.579  -5.255  1.00 49.60           O  
ANISOU  112  O   GLY A  10     6399   3289   9158   -998    513  -1404       O  
ATOM    113  N   ILE A  11      64.774  59.121  -4.074  1.00 41.98           N  
ANISOU  113  N   ILE A  11     5262   2506   8180   -612    349   -929       N  
ATOM    114  CA  ILE A  11      63.585  59.945  -3.875  1.00 45.54           C  
ANISOU  114  CA  ILE A  11     5712   3379   8214   -932    386   -761       C  
ATOM    115  C   ILE A  11      63.662  61.274  -4.626  1.00 41.69           C  
ANISOU  115  C   ILE A  11     5005   3511   7324   -859    490   -899       C  
ATOM    116  O   ILE A  11      62.723  61.661  -5.330  1.00 40.52           O  
ANISOU  116  O   ILE A  11     4805   3764   6826  -1076    562  -1047       O  
ATOM    117  CB  ILE A  11      63.345  60.207  -2.373  1.00 39.21           C  
ANISOU  117  CB  ILE A  11     5045   2558   7294   -958    201   -202       C  
ATOM    118  CG1 ILE A  11      62.938  58.903  -1.678  1.00 44.99           C  
ANISOU  118  CG1 ILE A  11     6105   2842   8148  -1143    111     19       C  
ATOM    119  CG2 ILE A  11      62.293  61.313  -2.164  1.00 40.56           C  
ANISOU  119  CG2 ILE A  11     5104   3352   6954  -1154    255    -84       C  
ATOM    120  CD1 ILE A  11      62.903  59.016  -0.169  1.00 48.80           C  
ANISOU  120  CD1 ILE A  11     6793   3299   8449  -1173    -53    559       C  
ATOM    121  N   GLY A  12      64.777  61.971  -4.468  1.00 36.06           N  
ANISOU  121  N   GLY A  12     4170   2862   6669   -568    470   -836       N  
ATOM    122  CA  GLY A  12      64.962  63.258  -5.124  1.00 32.79           C  
ANISOU  122  CA  GLY A  12     3619   2939   5900   -535    577   -904       C  
ATOM    123  C   GLY A  12      66.074  64.045  -4.458  1.00 28.91           C  
ANISOU  123  C   GLY A  12     3011   2467   5507   -288    510   -721       C  
ATOM    124  O   GLY A  12      67.145  63.506  -4.186  1.00 36.75           O  
ANISOU  124  O   GLY A  12     3902   3160   6901    -73    465   -800       O  
ATOM    125  N  ALYS A  13      65.816  65.322  -4.203  0.52 29.73           N  
ANISOU  125  N  ALYS A  13     3104   2912   5281   -310    483   -511       N  
ATOM    126  N  BLYS A  13      65.825  65.329  -4.201  0.48 29.80           N  
ANISOU  126  N  BLYS A  13     3112   2921   5290   -309    483   -511       N  
ATOM    127  CA ALYS A  13      66.793  66.162  -3.529  0.52 30.03           C  
ANISOU  127  CA ALYS A  13     3031   2990   5388   -147    417   -369       C  
ATOM    128  CA BLYS A  13      66.840  66.199  -3.597  0.48 29.22           C  
ANISOU  128  CA BLYS A  13     2921   2899   5283   -146    430   -386       C  
ATOM    129  C  ALYS A  13      66.085  67.078  -2.532  0.52 28.10           C  
ANISOU  129  C  ALYS A  13     2869   2928   4881   -184    277    -56       C  
ATOM    130  C  BLYS A  13      66.196  67.285  -2.711  0.48 31.38           C  
ANISOU  130  C  BLYS A  13     3266   3384   5274   -181    308    -85       C  
ATOM    131  O  ALYS A  13      64.893  67.328  -2.631  0.52 30.50           O  
ANISOU  131  O  ALYS A  13     3253   3408   4927   -310    282      4       O  
ATOM    132  O  BLYS A  13      65.144  67.831  -3.058  0.48 25.75           O  
ANISOU  132  O  BLYS A  13     2625   2892   4267   -290    339    -50       O  
ATOM    133  CB ALYS A  13      67.578  67.010  -4.528  0.52 32.51           C  
ANISOU  133  CB ALYS A  13     3226   3522   5604   -166    636   -579       C  
ATOM    134  CB BLYS A  13      67.720  66.842  -4.675  0.48 32.37           C  
ANISOU  134  CB BLYS A  13     3186   3479   5636   -159    666   -643       C  
ATOM    135  CG ALYS A  13      68.481  66.228  -5.445  0.52 32.70           C  
ANISOU  135  CG ALYS A  13     3093   3444   5888   -129    844   -980       C  
ATOM    136  CG BLYS A  13      68.973  67.510  -4.128  0.48 23.64           C  
ANISOU  136  CG BLYS A  13     1879   2385   4717    -37    646   -622       C  
ATOM    137  CD ALYS A  13      69.725  65.703  -4.755  0.52 30.31           C  
ANISOU  137  CD ALYS A  13     2542   2883   6092    130    742  -1065       C  
ATOM    138  CD BLYS A  13      69.931  67.953  -5.260  0.48 34.84           C  
ANISOU  138  CD BLYS A  13     3131   3981   6125   -135    966   -936       C  
ATOM    139  CE ALYS A  13      70.735  65.206  -5.785  0.52 36.54           C  
ANISOU  139  CE ALYS A  13     3068   3664   7149    180   1029  -1574       C  
ATOM    140  CE BLYS A  13      71.270  68.428  -4.708  0.48 39.83           C  
ANISOU  140  CE BLYS A  13     3460   4630   7044    -45    958  -1007       C  
ATOM    141  NZ ALYS A  13      71.900  64.620  -5.112  0.52 40.01           N  
ANISOU  141  NZ ALYS A  13     3282   3887   8035    441    814  -1614       N  
ATOM    142  NZ BLYS A  13      72.297  68.656  -5.777  0.48 41.12           N  
ANISOU  142  NZ BLYS A  13     3500   4961   7162   -192   1260  -1329       N  
ATOM    143  N   LYS A  14      66.854  67.598  -1.592  1.00 30.56           N  
ANISOU  143  N   LYS A  14     3113   3227   5273    -68    153     80       N  
ATOM    144  CA  LYS A  14      66.331  68.530  -0.600  1.00 27.97           C  
ANISOU  144  CA  LYS A  14     2846   3079   4702   -102     51    286       C  
ATOM    145  C   LYS A  14      67.226  69.766  -0.633  1.00 26.05           C  
ANISOU  145  C   LYS A  14     2495   2944   4459    -53     88    223       C  
ATOM    146  O   LYS A  14      68.437  69.627  -0.612  1.00 25.36           O  
ANISOU  146  O   LYS A  14     2243   2776   4615     29     65    124       O  
ATOM    147  CB  LYS A  14      66.411  67.900   0.783  1.00 28.95           C  
ANISOU  147  CB  LYS A  14     3044   3087   4869    -79   -171    513       C  
ATOM    148  CG  LYS A  14      65.949  68.838   1.930  1.00 36.22           C  
ANISOU  148  CG  LYS A  14     4019   4252   5493   -145   -245    651       C  
ATOM    149  CD  LYS A  14      65.560  68.047   3.180  1.00 42.61           C  
ANISOU  149  CD  LYS A  14     4998   5026   6167   -250   -404    913       C  
ATOM    150  CE  LYS A  14      66.764  67.444   3.866  1.00 55.54           C  
ANISOU  150  CE  LYS A  14     6648   6461   7993   -101   -691   1073       C  
ATOM    151  NZ  LYS A  14      67.755  68.518   4.135  1.00 58.69           N  
ANISOU  151  NZ  LYS A  14     6857   7033   8410     17   -780    944       N  
ATOM    152  N   PHE A  15      66.628  70.960  -0.684  1.00 25.63           N  
ANISOU  152  N   PHE A  15     2513   3047   4176   -104    140    255       N  
ATOM    153  CA  PHE A  15      67.386  72.219  -0.611  1.00 23.68           C  
ANISOU  153  CA  PHE A  15     2226   2828   3942   -118    179    210       C  
ATOM    154  C   PHE A  15      66.880  72.999   0.613  1.00 27.56           C  
ANISOU  154  C   PHE A  15     2774   3400   4299   -104     55    280       C  
ATOM    155  O   PHE A  15      65.696  73.299   0.696  1.00 27.31           O  
ANISOU  155  O   PHE A  15     2829   3450   4096    -89     62    315       O  
ATOM    156  CB  PHE A  15      67.099  73.070  -1.827  1.00 22.61           C  
ANISOU  156  CB  PHE A  15     2207   2718   3665   -189    346    191       C  
ATOM    157  CG  PHE A  15      67.648  72.485  -3.115  1.00 22.98           C  
ANISOU  157  CG  PHE A  15     2220   2771   3742   -272    533     63       C  
ATOM    158  CD1 PHE A  15      66.944  71.497  -3.797  1.00 29.93           C  
ANISOU  158  CD1 PHE A  15     3140   3691   4541   -275    554     10       C  
ATOM    159  CD2 PHE A  15      68.884  72.877  -3.594  1.00 27.36           C  
ANISOU  159  CD2 PHE A  15     2668   3320   4407   -387    716    -66       C  
ATOM    160  CE1 PHE A  15      67.471  70.948  -4.982  1.00 32.53           C  
ANISOU  160  CE1 PHE A  15     3435   4058   4867   -371    759   -194       C  
ATOM    161  CE2 PHE A  15      69.408  72.311  -4.765  1.00 35.15           C  
ANISOU  161  CE2 PHE A  15     3590   4374   5391   -492    953   -261       C  
ATOM    162  CZ  PHE A  15      68.684  71.348  -5.446  1.00 33.99           C  
ANISOU  162  CZ  PHE A  15     3514   4266   5133   -470    969   -333       C  
ATOM    163  N   GLU A  16      67.775  73.362   1.523  1.00 28.01           N  
ANISOU  163  N   GLU A  16     2742   3468   4432   -113    -54    240       N  
ATOM    164  CA  GLU A  16      67.355  74.119   2.699  1.00 29.09           C  
ANISOU  164  CA  GLU A  16     2937   3716   4401   -134   -146    224       C  
ATOM    165  C   GLU A  16      67.932  75.506   2.520  1.00 32.59           C  
ANISOU  165  C   GLU A  16     3378   4077   4928   -198    -68     76       C  
ATOM    166  O   GLU A  16      69.126  75.674   2.416  1.00 26.22           O  
ANISOU  166  O   GLU A  16     2434   3233   4295   -275    -71    -13       O  
ATOM    167  CB  GLU A  16      67.844  73.455   3.969  1.00 30.67           C  
ANISOU  167  CB  GLU A  16     3090   4021   4544   -140   -376    294       C  
ATOM    168  CG  GLU A  16      67.054  72.193   4.297  1.00 30.96           C  
ANISOU  168  CG  GLU A  16     3236   4077   4452   -144   -437    500       C  
ATOM    169  CD  GLU A  16      67.547  71.516   5.568  1.00 45.75           C  
ANISOU  169  CD  GLU A  16     5156   6020   6207   -164   -716    672       C  
ATOM    170  OE1 GLU A  16      66.882  70.566   6.035  1.00 45.69           O  
ANISOU  170  OE1 GLU A  16     5315   6007   6036   -240   -765    894       O  
ATOM    171  OE2 GLU A  16      68.594  71.936   6.100  1.00 55.49           O  
ANISOU  171  OE2 GLU A  16     6272   7318   7492   -131   -904    600       O  
ATOM    172  N   ILE A  17      67.060  76.498   2.410  1.00 27.35           N  
ANISOU  172  N   ILE A  17     2854   3356   4182   -167      8     35       N  
ATOM    173  CA  ILE A  17      67.479  77.845   2.039  1.00 26.54           C  
ANISOU  173  CA  ILE A  17     2845   3042   4197   -240     97    -58       C  
ATOM    174  C   ILE A  17      67.314  78.795   3.230  1.00 26.96           C  
ANISOU  174  C   ILE A  17     2925   3094   4224   -250     36   -268       C  
ATOM    175  O   ILE A  17      66.290  78.779   3.898  1.00 29.08           O  
ANISOU  175  O   ILE A  17     3207   3494   4346   -137      5   -333       O  
ATOM    176  CB  ILE A  17      66.596  78.336   0.874  1.00 33.26           C  
ANISOU  176  CB  ILE A  17     3890   3730   5019   -144    182     72       C  
ATOM    177  CG1 ILE A  17      66.748  77.389  -0.336  1.00 31.57           C  
ANISOU  177  CG1 ILE A  17     3664   3578   4754   -182    259    215       C  
ATOM    178  CG2 ILE A  17      66.984  79.739   0.461  1.00 31.94           C  
ANISOU  178  CG2 ILE A  17     3920   3241   4976   -234    257     60       C  
ATOM    179  CD1 ILE A  17      65.531  77.373  -1.256  1.00 37.94           C  
ANISOU  179  CD1 ILE A  17     4605   4398   5411    -48    231    349       C  
ATOM    180  N   GLU A  18      68.297  79.649   3.472  1.00 25.46           N  
ANISOU  180  N   GLU A  18     2723   2773   4179   -420     50   -430       N  
ATOM    181  CA  GLU A  18      68.148  80.639   4.535  1.00 29.69           C  
ANISOU  181  CA  GLU A  18     3306   3273   4701   -458     10   -711       C  
ATOM    182  C   GLU A  18      68.455  81.983   3.926  1.00 31.90           C  
ANISOU  182  C   GLU A  18     3772   3120   5227   -567    134   -788       C  
ATOM    183  O   GLU A  18      69.510  82.176   3.303  1.00 30.86           O  
ANISOU  183  O   GLU A  18     3619   2861   5247   -802    220   -744       O  
ATOM    184  CB  GLU A  18      69.121  80.363   5.680  1.00 37.78           C  
ANISOU  184  CB  GLU A  18     4138   4573   5643   -624   -153   -890       C  
ATOM    185  CG  GLU A  18      69.162  81.488   6.698  1.00 50.59           C  
ANISOU  185  CG  GLU A  18     5812   6167   7243   -742   -174  -1269       C  
ATOM    186  CD  GLU A  18      68.656  81.047   8.044  1.00 67.33           C  
ANISOU  186  CD  GLU A  18     7896   8695   8991   -718   -304  -1400       C  
ATOM    187  OE1 GLU A  18      69.014  79.923   8.458  1.00 69.32           O  
ANISOU  187  OE1 GLU A  18     8038   9262   9038   -731   -490  -1202       O  
ATOM    188  OE2 GLU A  18      67.908  81.820   8.683  1.00 68.39           O  
ANISOU  188  OE2 GLU A  18     8125   8824   9034   -691   -216  -1703       O  
ATOM    189  N   THR A  19      67.515  82.906   4.067  1.00 29.96           N  
ANISOU  189  N   THR A  19     3711   2627   5045   -403    156   -904       N  
ATOM    190  CA  THR A  19      67.634  84.207   3.426  1.00 35.84           C  
ANISOU  190  CA  THR A  19     4733   2828   6057   -462    240   -902       C  
ATOM    191  C   THR A  19      68.331  85.242   4.270  1.00 45.50           C  
ANISOU  191  C   THR A  19     5990   3840   7457   -701    264  -1284       C  
ATOM    192  O   THR A  19      68.503  85.084   5.489  1.00 40.47           O  
ANISOU  192  O   THR A  19     5162   3525   6690   -764    190  -1617       O  
ATOM    193  CB  THR A  19      66.245  84.796   3.081  1.00 36.51           C  
ANISOU  193  CB  THR A  19     5009   2634   6228    -85    196   -848       C  
ATOM    194  OG1 THR A  19      65.558  85.113   4.306  1.00 42.91           O  
ANISOU  194  OG1 THR A  19     5699   3566   7037     80    170  -1263       O  
ATOM    195  CG2 THR A  19      65.431  83.822   2.248  1.00 39.73           C  
ANISOU  195  CG2 THR A  19     5357   3286   6451    137    141   -523       C  
ATOM    196  N   ARG A  20      68.720  86.318   3.589  1.00 53.84           N  
ANISOU  196  N   ARG A  20     7329   4344   8785   -873    365  -1225       N  
ATOM    197  CA  ARG A  20      69.216  87.532   4.211  1.00 62.65           C  
ANISOU  197  CA  ARG A  20     8567   5141  10096  -1086    391  -1559       C  
ATOM    198  C   ARG A  20      68.244  88.037   5.278  1.00 64.89           C  
ANISOU  198  C   ARG A  20     8856   5396  10402   -795    321  -1961       C  
ATOM    199  O   ARG A  20      68.657  88.520   6.330  1.00 59.13           O  
ANISOU  199  O   ARG A  20     8042   4788   9636   -957    305  -2361       O  
ATOM    200  CB  ARG A  20      69.409  88.616   3.137  1.00 68.98           C  
ANISOU  200  CB  ARG A  20     9779   5393  11037  -1187    442  -1237       C  
ATOM    201  CG  ARG A  20      69.560  90.024   3.691  1.00 87.77           C  
ANISOU  201  CG  ARG A  20    12385   7358  13606  -1277    412  -1505       C  
ATOM    202  CD  ARG A  20      68.732  91.037   2.901  1.00101.92           C  
ANISOU  202  CD  ARG A  20    14664   8508  15553  -1020    320  -1232       C  
ATOM    203  NE  ARG A  20      69.323  91.361   1.605  1.00107.28           N  
ANISOU  203  NE  ARG A  20    15615   8911  16235  -1297    326   -750       N  
ATOM    204  CZ  ARG A  20      68.759  92.154   0.699  1.00110.11           C  
ANISOU  204  CZ  ARG A  20    16406   8727  16705  -1142    159   -385       C  
ATOM    205  NH1 ARG A  20      69.375  92.396  -0.450  1.00110.34           N  
ANISOU  205  NH1 ARG A  20    16546   8603  16774  -1462    194     62       N  
ATOM    206  NH2 ARG A  20      67.578  92.708   0.940  1.00114.82           N  
ANISOU  206  NH2 ARG A  20    17281   8976  17371   -652      2   -474       N  
ATOM    207  N   SER A  21      66.949  87.925   5.001  1.00 52.55           N  
ANISOU  207  N   SER A  21     7355   3739   8872   -358    281  -1870       N  
ATOM    208  CA  SER A  21      65.925  88.323   5.968  1.00 55.36           C  
ANISOU  208  CA  SER A  21     7629   4187   9218    -48    262  -2277       C  
ATOM    209  C   SER A  21      65.835  87.393   7.190  1.00 48.67           C  
ANISOU  209  C   SER A  21     6440   4028   8026   -120    272  -2633       C  
ATOM    210  O   SER A  21      64.970  87.586   8.035  1.00 52.39           O  
ANISOU  210  O   SER A  21     6801   4706   8396     77    317  -2988       O  
ATOM    211  CB  SER A  21      64.553  88.393   5.278  1.00 55.97           C  
ANISOU  211  CB  SER A  21     7767   4100   9400    457    193  -2065       C  
ATOM    212  OG  SER A  21      64.314  87.236   4.481  1.00 46.71           O  
ANISOU  212  OG  SER A  21     6478   3208   8062    535    143  -1669       O  
ATOM    213  N   HIS A  22      66.694  86.371   7.258  1.00 50.19           N  
ANISOU  213  N   HIS A  22     6470   4671   7929   -388    215  -2408       N  
ATOM    214  CA  HIS A  22      66.617  85.351   8.312  1.00 46.64           C  
ANISOU  214  CA  HIS A  22     5778   4915   7030   -452    153  -2512       C  
ATOM    215  C   HIS A  22      65.310  84.536   8.275  1.00 58.59           C  
ANISOU  215  C   HIS A  22     7188   6743   8331   -156    194  -2359       C  
ATOM    216  O   HIS A  22      64.689  84.301   9.303  1.00 64.11           O  
ANISOU  216  O   HIS A  22     7771   7854   8735   -149    249  -2642       O  
ATOM    217  CB  HIS A  22      66.799  85.981   9.694  1.00 54.47           C  
ANISOU  217  CB  HIS A  22     6732   6087   7875   -632    160  -3107       C  
ATOM    218  CG  HIS A  22      68.207  86.396   9.979  1.00 72.31           C  
ANISOU  218  CG  HIS A  22     8976   8292  10206  -1019     62  -3268       C  
ATOM    219  ND1 HIS A  22      68.904  87.272   9.173  1.00 78.59           N  
ANISOU  219  ND1 HIS A  22     9921   8543  11395  -1140    116  -3138       N  
ATOM    220  CD2 HIS A  22      69.062  86.034  10.966  1.00 71.73           C  
ANISOU  220  CD2 HIS A  22     8743   8713   9799  -1282   -107  -3391       C  
ATOM    221  CE1 HIS A  22      70.121  87.439   9.657  1.00 81.98           C  
ANISOU  221  CE1 HIS A  22    10233   9153  11764  -1472     21  -3249       C  
ATOM    222  NE2 HIS A  22      70.242  86.698  10.746  1.00 78.92           N  
ANISOU  222  NE2 HIS A  22     9646   9384  10957  -1531   -142  -3401       N  
ATOM    223  N   GLU A  23      64.899  84.130   7.084  1.00 34.86           N  
ANISOU  223  N   GLU A  23     4220   3573   5452     35    184  -1942       N  
ATOM    224  CA  GLU A  23      63.717  83.301   6.874  1.00 32.94           C  
ANISOU  224  CA  GLU A  23     3841   3622   5052    263    208  -1786       C  
ATOM    225  C   GLU A  23      64.157  81.992   6.256  1.00 41.75           C  
ANISOU  225  C   GLU A  23     4912   4950   6000    147    139  -1335       C  
ATOM    226  O   GLU A  23      65.140  81.961   5.526  1.00 30.63           O  
ANISOU  226  O   GLU A  23     3589   3332   4718     21     97  -1113       O  
ATOM    227  CB  GLU A  23      62.713  84.049   5.974  1.00 35.80           C  
ANISOU  227  CB  GLU A  23     4270   3592   5742    637    204  -1760       C  
ATOM    228  CG  GLU A  23      62.254  85.386   6.633  1.00 39.77           C  
ANISOU  228  CG  GLU A  23     4806   3791   6515    824    266  -2280       C  
ATOM    229  CD  GLU A  23      61.296  86.244   5.808  1.00 67.52           C  
ANISOU  229  CD  GLU A  23     8393   6822  10441   1282    180  -2264       C  
ATOM    230  OE1 GLU A  23      61.742  86.891   4.837  1.00 75.05           O  
ANISOU  230  OE1 GLU A  23     9661   7226  11628   1305     68  -1933       O  
ATOM    231  OE2 GLU A  23      60.097  86.321   6.165  1.00 64.61           O  
ANISOU  231  OE2 GLU A  23     7788   6706  10055   1540    215  -2466       O  
ATOM    232  N   LYS A  24      63.451  80.901   6.552  1.00 27.34           N  
ANISOU  232  N   LYS A  24     2947   3530   3909    159    156  -1234       N  
ATOM    233  CA  LYS A  24      63.891  79.575   6.106  1.00 35.37           C  
ANISOU  233  CA  LYS A  24     3939   4700   4800     44     84   -859       C  
ATOM    234  C   LYS A  24      62.841  78.947   5.204  1.00 35.14           C  
ANISOU  234  C   LYS A  24     3850   4714   4788    198    119   -670       C  
ATOM    235  O   LYS A  24      61.659  79.042   5.467  1.00 31.25           O  
ANISOU  235  O   LYS A  24     3233   4393   4245    318    195   -835       O  
ATOM    236  CB  LYS A  24      64.109  78.633   7.308  1.00 35.06           C  
ANISOU  236  CB  LYS A  24     3851   5065   4406   -161     30   -840       C  
ATOM    237  CG  LYS A  24      65.234  79.015   8.277  1.00 42.08           C  
ANISOU  237  CG  LYS A  24     4765   6035   5188   -344    -96  -1004       C  
ATOM    238  CD  LYS A  24      65.267  78.014   9.449  1.00 48.20           C  
ANISOU  238  CD  LYS A  24     5555   7238   5519   -526   -208   -894       C  
ATOM    239  CE  LYS A  24      66.609  77.988  10.180  1.00 49.78           C  
ANISOU  239  CE  LYS A  24     5752   7553   5611   -680   -476   -906       C  
ATOM    240  NZ  LYS A  24      66.972  79.306  10.751  1.00 51.58           N  
ANISOU  240  NZ  LYS A  24     5968   7772   5860   -772   -455  -1364       N  
ATOM    241  N   MET A  25      63.292  78.310   4.142  1.00 26.97           N  
ANISOU  241  N   MET A  25     2862   3559   3826    177     74   -383       N  
ATOM    242  CA  MET A  25      62.395  77.581   3.246  1.00 30.47           C  
ANISOU  242  CA  MET A  25     3247   4083   4246    265     79   -228       C  
ATOM    243  C   MET A  25      63.114  76.290   2.861  1.00 31.66           C  
ANISOU  243  C   MET A  25     3410   4267   4352    108     55     -6       C  
ATOM    244  O   MET A  25      64.324  76.292   2.591  1.00 30.78           O  
ANISOU  244  O   MET A  25     3351   4003   4342     34     33     59       O  
ATOM    245  CB  MET A  25      62.120  78.459   2.015  1.00 36.33           C  
ANISOU  245  CB  MET A  25     4094   4550   5158    459     33   -158       C  
ATOM    246  CG  MET A  25      61.376  77.824   0.844  1.00 49.59           C  
ANISOU  246  CG  MET A  25     5740   6318   6785    535    -23      6       C  
ATOM    247  SD  MET A  25      61.490  78.888  -0.633  1.00 42.81           S  
ANISOU  247  SD  MET A  25     5144   5110   6011    688   -134    212       S  
ATOM    248  CE  MET A  25      60.826  80.427  -0.014  1.00 55.04           C  
ANISOU  248  CE  MET A  25     6717   6400   7796    996   -219     19       C  
ATOM    249  N   THR A  26      62.377  75.182   2.829  1.00 29.06           N  
ANISOU  249  N   THR A  26     3007   4120   3913     49     71     70       N  
ATOM    250  CA  THR A  26      62.939  73.921   2.343  1.00 27.41           C  
ANISOU  250  CA  THR A  26     2828   3849   3737    -58     47    240       C  
ATOM    251  C   THR A  26      62.162  73.533   1.115  1.00 30.29           C  
ANISOU  251  C   THR A  26     3163   4229   4116    -24     76    258       C  
ATOM    252  O   THR A  26      60.942  73.594   1.117  1.00 28.05           O  
ANISOU  252  O   THR A  26     2772   4128   3758      6     90    179       O  
ATOM    253  CB  THR A  26      62.805  72.815   3.431  1.00 29.64           C  
ANISOU  253  CB  THR A  26     3122   4263   3877   -224     20    338       C  
ATOM    254  OG1 THR A  26      63.705  73.117   4.486  1.00 29.67           O  
ANISOU  254  OG1 THR A  26     3172   4284   3818   -256    -80    347       O  
ATOM    255  CG2 THR A  26      63.122  71.404   2.862  1.00 33.39           C  
ANISOU  255  CG2 THR A  26     3644   4579   4464   -297    -14    493       C  
ATOM    256  N   ILE A  27      62.867  73.162   0.049  1.00 25.96           N  
ANISOU  256  N   ILE A  27     2675   3537   3651    -40     89    313       N  
ATOM    257  CA  ILE A  27      62.205  72.714  -1.155  1.00 24.56           C  
ANISOU  257  CA  ILE A  27     2492   3421   3417    -52     99    299       C  
ATOM    258  C   ILE A  27      62.641  71.271  -1.365  1.00 32.85           C  
ANISOU  258  C   ILE A  27     3542   4388   4551   -188    142    291       C  
ATOM    259  O   ILE A  27      63.824  70.996  -1.411  1.00 26.58           O  
ANISOU  259  O   ILE A  27     2770   3431   3900   -187    173    292       O  
ATOM    260  CB  ILE A  27      62.652  73.536  -2.372  1.00 22.72           C  
ANISOU  260  CB  ILE A  27     2384   3102   3146      4    113    335       C  
ATOM    261  CG1 ILE A  27      62.150  74.986  -2.239  1.00 30.94           C  
ANISOU  261  CG1 ILE A  27     3486   4101   4169    177     26    374       C  
ATOM    262  CG2 ILE A  27      62.060  72.952  -3.667  1.00 27.78           C  
ANISOU  262  CG2 ILE A  27     3046   3873   3638    -49     96    306       C  
ATOM    263  CD1 ILE A  27      62.601  75.925  -3.376  1.00 29.51           C  
ANISOU  263  CD1 ILE A  27     3535   3760   3919    191     22    510       C  
ATOM    264  N   ILE A  28      61.678  70.359  -1.456  1.00 27.11           N  
ANISOU  264  N   ILE A  28     2763   3756   3780   -304    144    249       N  
ATOM    265  CA  ILE A  28      61.978  68.982  -1.826  1.00 28.78           C  
ANISOU  265  CA  ILE A  28     3014   3801   4119   -435    185    201       C  
ATOM    266  C   ILE A  28      61.532  68.780  -3.257  1.00 24.91           C  
ANISOU  266  C   ILE A  28     2511   3419   3535   -490    217     33       C  
ATOM    267  O   ILE A  28      60.370  69.040  -3.595  1.00 31.31           O  
ANISOU  267  O   ILE A  28     3232   4481   4184   -521    155    -21       O  
ATOM    268  CB  ILE A  28      61.172  67.987  -0.973  1.00 34.77           C  
ANISOU  268  CB  ILE A  28     3774   4550   4886   -634    185    258       C  
ATOM    269  CG1 ILE A  28      61.282  68.327   0.511  1.00 47.25           C  
ANISOU  269  CG1 ILE A  28     5392   6169   6394   -637    147    435       C  
ATOM    270  CG2 ILE A  28      61.632  66.536  -1.271  1.00 33.99           C  
ANISOU  270  CG2 ILE A  28     3782   4118   5014   -747    204    228       C  
ATOM    271  CD1 ILE A  28      62.575  67.947   1.128  1.00 41.76           C  
ANISOU  271  CD1 ILE A  28     4816   5205   5845   -558     46    588       C  
ATOM    272  N   ILE A  29      62.444  68.335  -4.103  1.00 28.65           N  
ANISOU  272  N   ILE A  29     3040   3752   4094   -499    305    -88       N  
ATOM    273  CA  ILE A  29      62.098  68.006  -5.472  1.00 30.57           C  
ANISOU  273  CA  ILE A  29     3302   4134   4178   -606    353   -295       C  
ATOM    274  C   ILE A  29      62.114  66.489  -5.594  1.00 35.47           C  
ANISOU  274  C   ILE A  29     3924   4538   5014   -757    422   -503       C  
ATOM    275  O   ILE A  29      63.164  65.876  -5.383  1.00 37.37           O  
ANISOU  275  O   ILE A  29     4182   4472   5543   -689    497   -562       O  
ATOM    276  CB  ILE A  29      63.163  68.547  -6.414  1.00 36.86           C  
ANISOU  276  CB  ILE A  29     4172   4949   4883   -573    484   -363       C  
ATOM    277  CG1 ILE A  29      63.357  70.044  -6.180  1.00 39.80           C  
ANISOU  277  CG1 ILE A  29     4606   5388   5127   -454    431   -125       C  
ATOM    278  CG2 ILE A  29      62.826  68.211  -7.883  1.00 38.05           C  
ANISOU  278  CG2 ILE A  29     4388   5319   4751   -731    544   -595       C  
ATOM    279  CD1 ILE A  29      64.305  70.676  -7.176  1.00 44.17           C  
ANISOU  279  CD1 ILE A  29     5275   5984   5523   -525    598   -149       C  
ATOM    280  N   HIS A  30      60.966  65.903  -5.922  1.00 32.89           N  
ANISOU  280  N   HIS A  30     3558   4347   4593   -950    378   -636       N  
ATOM    281  CA  HIS A  30      60.825  64.457  -6.165  1.00 31.60           C  
ANISOU  281  CA  HIS A  30     3430   3934   4642  -1160    450   -884       C  
ATOM    282  C   HIS A  30      61.099  64.088  -7.614  1.00 35.81           C  
ANISOU  282  C   HIS A  30     3990   4558   5059  -1247    555  -1267       C  
ATOM    283  O   HIS A  30      60.895  64.889  -8.526  1.00 37.67           O  
ANISOU  283  O   HIS A  30     4219   5179   4913  -1240    521  -1309       O  
ATOM    284  CB  HIS A  30      59.414  64.003  -5.798  1.00 34.88           C  
ANISOU  284  CB  HIS A  30     3759   4486   5010  -1422    384   -898       C  
ATOM    285  CG  HIS A  30      59.113  64.150  -4.342  1.00 39.12           C  
ANISOU  285  CG  HIS A  30     4288   4953   5623  -1432    357   -582       C  
ATOM    286  ND1 HIS A  30      59.211  63.101  -3.455  1.00 42.71           N  
ANISOU  286  ND1 HIS A  30     4890   5009   6326  -1605    401   -454       N  
ATOM    287  CD2 HIS A  30      58.721  65.224  -3.609  1.00 40.35           C  
ANISOU  287  CD2 HIS A  30     4336   5385   5612  -1308    298   -379       C  
ATOM    288  CE1 HIS A  30      58.892  63.518  -2.243  1.00 52.35           C  
ANISOU  288  CE1 HIS A  30     6105   6334   7452  -1630    384   -171       C  
ATOM    289  NE2 HIS A  30      58.591  64.807  -2.311  1.00 38.19           N  
ANISOU  289  NE2 HIS A  30     4130   4958   5424  -1443    340   -169       N  
ATOM    290  N   ASP A  31      61.571  62.867  -7.831  1.00 39.58           N  
ANISOU  290  N   ASP A  31     6814   2687   5539    785    378  -1100       N  
ATOM    291  CA  ASP A  31      61.913  62.462  -9.179  1.00 42.64           C  
ANISOU  291  CA  ASP A  31     7632   2874   5695    966    492  -1334       C  
ATOM    292  C   ASP A  31      60.716  62.386 -10.121  1.00 55.08           C  
ANISOU  292  C   ASP A  31     9521   4297   7109    573    242  -1588       C  
ATOM    293  O   ASP A  31      60.875  62.457 -11.340  1.00 51.87           O  
ANISOU  293  O   ASP A  31     9339   3913   6458    643    277  -1762       O  
ATOM    294  CB  ASP A  31      62.688  61.152  -9.145  1.00 46.78           C  
ANISOU  294  CB  ASP A  31     8505   3042   6229   1314    707  -1321       C  
ATOM    295  CG  ASP A  31      64.120  61.357  -8.714  1.00 56.24           C  
ANISOU  295  CG  ASP A  31     9387   4483   7497   1800    980  -1089       C  
ATOM    296  OD1 ASP A  31      64.650  62.452  -8.988  1.00 48.66           O  
ANISOU  296  OD1 ASP A  31     8098   3905   6485   1915   1065  -1036       O  
ATOM    297  OD2 ASP A  31      64.707  60.446  -8.099  1.00 49.07           O  
ANISOU  297  OD2 ASP A  31     8513   3430   6701   2033   1087   -930       O  
ATOM    298  N   ASP A  32      59.517  62.288  -9.560  1.00 50.79           N  
ANISOU  298  N   ASP A  32     8885   3707   6707    136    -22  -1553       N  
ATOM    299  CA  ASP A  32      58.321  62.206 -10.394  1.00 59.42           C  
ANISOU  299  CA  ASP A  32    10146   4749   7681   -284   -308  -1728       C  
ATOM    300  C   ASP A  32      57.840  63.601 -10.758  1.00 48.81           C  
ANISOU  300  C   ASP A  32     8440   3835   6271   -426   -459  -1708       C  
ATOM    301  O   ASP A  32      56.882  63.752 -11.502  1.00 51.29           O  
ANISOU  301  O   ASP A  32     8807   4209   6472   -736   -714  -1812       O  
ATOM    302  CB  ASP A  32      57.207  61.384  -9.720  1.00 58.38           C  
ANISOU  302  CB  ASP A  32     9997   4437   7747   -693   -502  -1649       C  
ATOM    303  CG  ASP A  32      56.598  62.083  -8.501  1.00 51.77           C  
ANISOU  303  CG  ASP A  32     8711   3811   7148   -905   -599  -1424       C  
ATOM    304  OD1 ASP A  32      57.084  63.152  -8.061  1.00 43.75           O  
ANISOU  304  OD1 ASP A  32     7273   3179   6169   -690   -483  -1283       O  
ATOM    305  OD2 ASP A  32      55.620  61.539  -7.954  1.00 63.96           O  
ANISOU  305  OD2 ASP A  32    10171   5279   8851  -1251   -732  -1323       O  
ATOM    306  N   GLY A  33      58.520  64.616 -10.228  1.00 38.15           N  
ANISOU  306  N   GLY A  33     6657   2837   5000   -191   -299  -1529       N  
ATOM    307  CA  GLY A  33      58.227  65.995 -10.581  1.00 37.71           C  
ANISOU  307  CA  GLY A  33     6264   3180   4882   -255   -384  -1480       C  
ATOM    308  C   GLY A  33      57.526  66.790  -9.494  1.00 36.07           C  
ANISOU  308  C   GLY A  33     5582   3230   4895   -435   -480  -1274       C  
ATOM    309  O   GLY A  33      57.458  68.015  -9.562  1.00 35.80           O  
ANISOU  309  O   GLY A  33     5261   3501   4839   -412   -490  -1196       O  
ATOM    310  N  AARG A  34      57.004  66.111  -8.483  0.50 36.27           N  
ANISOU  310  N  AARG A  34     5553   3113   5116   -598   -525  -1176       N  
ATOM    311  N  BARG A  34      57.023  66.087  -8.479  0.50 36.06           N  
ANISOU  311  N  BARG A  34     5532   3079   5090   -594   -522  -1177       N  
ATOM    312  CA AARG A  34      56.333  66.836  -7.417  0.50 30.46           C  
ANISOU  312  CA AARG A  34     4398   2619   4556   -730   -566   -979       C  
ATOM    313  CA BARG A  34      56.419  66.733  -7.313  0.50 37.14           C  
ANISOU  313  CA BARG A  34     5257   3440   5413   -714   -547   -971       C  
ATOM    314  C  AARG A  34      57.348  67.611  -6.585  0.50 33.57           C  
ANISOU  314  C  AARG A  34     4558   3211   4988   -461   -369   -843       C  
ATOM    315  C  BARG A  34      57.427  67.652  -6.634  0.50 33.18           C  
ANISOU  315  C  BARG A  34     4510   3168   4928   -443   -361   -848       C  
ATOM    316  O  AARG A  34      58.434  67.105  -6.293  0.50 32.57           O  
ANISOU  316  O  AARG A  34     4535   2976   4863   -229   -214   -818       O  
ATOM    317  O  BARG A  34      58.587  67.275  -6.476  0.50 36.01           O  
ANISOU  317  O  BARG A  34     4966   3447   5268   -192   -200   -833       O  
ATOM    318  CB AARG A  34      55.541  65.885  -6.523  0.50 44.13           C  
ANISOU  318  CB AARG A  34     6136   4162   6469   -976   -630   -879       C  
ATOM    319  CB BARG A  34      55.996  65.690  -6.267  0.50 31.89           C  
ANISOU  319  CB BARG A  34     4634   2553   4929   -869   -547   -861       C  
ATOM    320  CG AARG A  34      54.646  66.589  -5.513  0.50 45.90           C  
ANISOU  320  CG AARG A  34     5947   4648   6845  -1121   -651   -675       C  
ATOM    321  CG BARG A  34      54.757  64.854  -6.590  0.50 41.19           C  
ANISOU  321  CG BARG A  34     5952   3535   6162  -1267   -767   -909       C  
ATOM    322  CD AARG A  34      53.693  65.612  -4.848  0.50 46.35           C  
ANISOU  322  CD AARG A  34     6004   4537   7068  -1428   -722   -562       C  
ATOM    323  CD BARG A  34      54.547  63.785  -5.505  0.50 42.42           C  
ANISOU  323  CD BARG A  34     6188   3433   6498  -1394   -712   -766       C  
ATOM    324  NE AARG A  34      54.382  64.618  -4.031  0.50 40.42           N  
ANISOU  324  NE AARG A  34     5469   3508   6381  -1324   -577   -494       N  
ATOM    325  NE BARG A  34      55.415  62.619  -5.703  0.50 43.04           N  
ANISOU  325  NE BARG A  34     6740   3085   6527  -1226   -609   -869       N  
ATOM    326  CZ AARG A  34      54.688  64.790  -2.747  0.50 43.41           C  
ANISOU  326  CZ AARG A  34     5679   3985   6830  -1195   -421   -300       C  
ATOM    327  CZ BARG A  34      55.972  61.896  -4.729  0.50 48.58           C  
ANISOU  327  CZ BARG A  34     7542   3583   7333  -1072   -449   -723       C  
ATOM    328  NH1AARG A  34      55.298  63.823  -2.072  0.50 37.03           N  
ANISOU  328  NH1AARG A  34     5086   2919   6066  -1091   -315   -214       N  
ATOM    329  NH1BARG A  34      56.736  60.853  -5.037  0.50 49.01           N  
ANISOU  329  NH1BARG A  34     8053   3230   7337   -868   -345   -816       N  
ATOM    330  NH2AARG A  34      54.378  65.928  -2.138  0.50 46.72           N  
ANISOU  330  NH2AARG A  34     5754   4746   7253  -1154   -369   -189       N  
ATOM    331  NH2BARG A  34      55.784  62.206  -3.452  0.50 46.40           N  
ANISOU  331  NH2BARG A  34     6941   3500   7187  -1087   -378   -477       N  
ATOM    332  N   ARG A  35      56.976  68.835  -6.218  1.00 31.01           N  
ANISOU  332  N   ARG A  35     3927   3169   4689   -496   -388   -747       N  
ATOM    333  CA  ARG A  35      57.742  69.674  -5.289  1.00 29.63           C  
ANISOU  333  CA  ARG A  35     3543   3175   4541   -338   -256   -620       C  
ATOM    334  C   ARG A  35      56.936  69.818  -4.009  1.00 37.91           C  
ANISOU  334  C   ARG A  35     4404   4289   5710   -465   -262   -475       C  
ATOM    335  O   ARG A  35      55.708  69.966  -4.061  1.00 33.88           O  
ANISOU  335  O   ARG A  35     3788   3831   5255   -643   -354   -449       O  
ATOM    336  CB  ARG A  35      57.976  71.078  -5.846  1.00 30.97           C  
ANISOU  336  CB  ARG A  35     3589   3567   4609   -273   -244   -634       C  
ATOM    337  CG  ARG A  35      59.182  71.230  -6.759  1.00 30.68           C  
ANISOU  337  CG  ARG A  35     3657   3552   4446    -88   -145   -699       C  
ATOM    338  CD  ARG A  35      58.927  70.586  -8.116  1.00 33.13           C  
ANISOU  338  CD  ARG A  35     4235   3727   4626    -97   -202   -861       C  
ATOM    339  NE  ARG A  35      59.788  71.199  -9.135  1.00 33.49           N  
ANISOU  339  NE  ARG A  35     4337   3881   4504     63    -95   -900       N  
ATOM    340  CZ  ARG A  35      59.860  70.802 -10.397  1.00 36.56           C  
ANISOU  340  CZ  ARG A  35     4999   4187   4704    119    -90  -1042       C  
ATOM    341  NH1 ARG A  35      59.159  69.741 -10.808  1.00 34.93           N  
ANISOU  341  NH1 ARG A  35     5070   3754   4449      6   -217  -1187       N  
ATOM    342  NH2 ARG A  35      60.666  71.441 -11.240  1.00 39.26           N  
ANISOU  342  NH2 ARG A  35     5367   4662   4889    273     48  -1036       N  
ATOM    343  N   GLU A  36      57.622  69.780  -2.869  1.00 26.46           N  
ANISOU  343  N   GLU A  36     2903   2866   4287   -365   -164   -360       N  
ATOM    344  CA  GLU A  36      57.014  70.218  -1.610  1.00 33.80           C  
ANISOU  344  CA  GLU A  36     3679   3907   5257   -435   -127   -225       C  
ATOM    345  C   GLU A  36      57.854  71.375  -1.070  1.00 33.10           C  
ANISOU  345  C   GLU A  36     3509   3997   5071   -318    -72   -195       C  
ATOM    346  O   GLU A  36      59.077  71.311  -1.082  1.00 35.89           O  
ANISOU  346  O   GLU A  36     3888   4367   5381   -199    -55   -188       O  
ATOM    347  CB  GLU A  36      56.928  69.095  -0.558  1.00 38.03           C  
ANISOU  347  CB  GLU A  36     4280   4302   5868   -475    -84    -94       C  
ATOM    348  CG  GLU A  36      57.052  67.646  -1.064  1.00 59.31           C  
ANISOU  348  CG  GLU A  36     7200   6704   8631   -502   -115   -132       C  
ATOM    349  CD  GLU A  36      56.981  66.609   0.071  1.00 73.23           C  
ANISOU  349  CD  GLU A  36     9049   8307  10469   -534    -58     41       C  
ATOM    350  OE1 GLU A  36      55.847  66.200   0.422  1.00 88.08           O  
ANISOU  350  OE1 GLU A  36    10896  10129  12441   -764    -72    124       O  
ATOM    351  OE2 GLU A  36      58.044  66.198   0.617  1.00 46.00           O  
ANISOU  351  OE2 GLU A  36     5679   4808   6990   -332      0    127       O  
ATOM    352  N   ILE A  37      57.186  72.432  -0.611  1.00 27.10           N  
ANISOU  352  N   ILE A  37     2655   3365   4277   -355    -44   -168       N  
ATOM    353  CA  ILE A  37      57.880  73.571  -0.030  1.00 23.90           C  
ANISOU  353  CA  ILE A  37     2248   3074   3758   -299    -10   -159       C  
ATOM    354  C   ILE A  37      57.418  73.701   1.420  1.00 23.63           C  
ANISOU  354  C   ILE A  37     2227   3079   3673   -318     64    -61       C  
ATOM    355  O   ILE A  37      56.219  73.552   1.681  1.00 29.67           O  
ANISOU  355  O   ILE A  37     2932   3845   4494   -355    129     -8       O  
ATOM    356  CB  ILE A  37      57.532  74.853  -0.769  1.00 29.01           C  
ANISOU  356  CB  ILE A  37     2877   3783   4361   -287    -10   -229       C  
ATOM    357  CG1 ILE A  37      57.917  74.738  -2.254  1.00 35.95           C  
ANISOU  357  CG1 ILE A  37     3772   4642   5248   -266    -70   -314       C  
ATOM    358  CG2 ILE A  37      58.268  76.048  -0.124  1.00 28.35           C  
ANISOU  358  CG2 ILE A  37     2861   3756   4153   -279     15   -232       C  
ATOM    359  CD1 ILE A  37      57.359  75.878  -3.084  1.00 41.47           C  
ANISOU  359  CD1 ILE A  37     4462   5392   5904   -250    -83   -348       C  
ATOM    360  N   TYR A  38      58.359  73.901   2.344  1.00 26.02           N  
ANISOU  360  N   TYR A  38     2595   3431   3860   -301     50    -19       N  
ATOM    361  CA  TYR A  38      58.038  74.108   3.761  1.00 26.58           C  
ANISOU  361  CA  TYR A  38     2748   3545   3804   -311    119     60       C  
ATOM    362  C   TYR A  38      58.631  75.443   4.162  1.00 29.63           C  
ANISOU  362  C   TYR A  38     3251   3994   4012   -332     90    -11       C  
ATOM    363  O   TYR A  38      59.731  75.782   3.748  1.00 28.24           O  
ANISOU  363  O   TYR A  38     3057   3857   3816   -371    -23    -45       O  
ATOM    364  CB  TYR A  38      58.681  73.017   4.639  1.00 25.56           C  
ANISOU  364  CB  TYR A  38     2655   3410   3647   -302     79    194       C  
ATOM    365  CG  TYR A  38      58.226  71.608   4.279  1.00 22.44           C  
ANISOU  365  CG  TYR A  38     2220   2878   3427   -303    103    267       C  
ATOM    366  CD1 TYR A  38      58.874  70.896   3.258  1.00 37.58           C  
ANISOU  366  CD1 TYR A  38     4118   4697   5461   -251     35    224       C  
ATOM    367  CD2 TYR A  38      57.150  71.022   4.899  1.00 31.78           C  
ANISOU  367  CD2 TYR A  38     3410   4014   4651   -362    208    377       C  
ATOM    368  CE1 TYR A  38      58.465  69.628   2.894  1.00 31.48           C  
ANISOU  368  CE1 TYR A  38     3400   3734   4827   -271     50    259       C  
ATOM    369  CE2 TYR A  38      56.718  69.736   4.544  1.00 35.12           C  
ANISOU  369  CE2 TYR A  38     3834   4267   5241   -427    209    444       C  
ATOM    370  CZ  TYR A  38      57.393  69.055   3.537  1.00 37.38           C  
ANISOU  370  CZ  TYR A  38     4166   4410   5626   -386    117    367       C  
ATOM    371  OH  TYR A  38      57.004  67.793   3.169  1.00 39.83           O  
ANISOU  371  OH  TYR A  38     4567   4489   6077   -462    111    403       O  
ATOM    372  N   ARG A  39      57.909  76.180   4.993  1.00 26.63           N  
ANISOU  372  N   ARG A  39     3006   3616   3495   -311    204    -22       N  
ATOM    373  CA  ARG A  39      58.400  77.443   5.532  1.00 26.42           C  
ANISOU  373  CA  ARG A  39     3198   3584   3256   -354    179   -111       C  
ATOM    374  C   ARG A  39      58.430  77.308   7.049  1.00 27.12           C  
ANISOU  374  C   ARG A  39     3482   3712   3112   -367    210    -56       C  
ATOM    375  O   ARG A  39      57.455  76.884   7.649  1.00 36.10           O  
ANISOU  375  O   ARG A  39     4631   4854   4230   -279    383     22       O  
ATOM    376  CB  ARG A  39      57.431  78.560   5.152  1.00 30.54           C  
ANISOU  376  CB  ARG A  39     3806   4026   3771   -259    328   -194       C  
ATOM    377  CG  ARG A  39      57.593  79.007   3.707  1.00 36.11           C  
ANISOU  377  CG  ARG A  39     4399   4696   4624   -263    264   -251       C  
ATOM    378  CD  ARG A  39      58.776  80.004   3.553  1.00 33.47           C  
ANISOU  378  CD  ARG A  39     4223   4316   4179   -399    140   -332       C  
ATOM    379  NE  ARG A  39      58.451  81.295   4.200  1.00 41.64           N  
ANISOU  379  NE  ARG A  39     5584   5215   5024   -380    231   -418       N  
ATOM    380  CZ  ARG A  39      59.088  81.821   5.231  1.00 44.75           C  
ANISOU  380  CZ  ARG A  39     6254   5562   5187   -515    163   -478       C  
ATOM    381  NH1 ARG A  39      60.111  81.197   5.785  1.00 40.89           N  
ANISOU  381  NH1 ARG A  39     5699   5202   4635   -682    -22   -429       N  
ATOM    382  NH2 ARG A  39      58.694  82.986   5.718  1.00 64.62           N  
ANISOU  382  NH2 ARG A  39     9138   7894   7519   -474    272   -584       N  
ATOM    383  N   PHE A  40      59.549  77.666   7.668  1.00 33.68           N  
ANISOU  383  N   PHE A  40     4456   4589   3751   -495     35    -77       N  
ATOM    384  CA  PHE A  40      59.701  77.399   9.096  1.00 45.16           C  
ANISOU  384  CA  PHE A  40     6110   6107   4943   -522     12     -8       C  
ATOM    385  C   PHE A  40      59.936  78.648   9.873  1.00 45.82           C  
ANISOU  385  C   PHE A  40     6565   6140   4705   -622    -28   -146       C  
ATOM    386  O   PHE A  40      60.493  79.594   9.347  1.00 42.53           O  
ANISOU  386  O   PHE A  40     6215   5659   4284   -749   -141   -264       O  
ATOM    387  CB  PHE A  40      60.876  76.465   9.357  1.00 35.93           C  
ANISOU  387  CB  PHE A  40     4792   5075   3786   -594   -219    138       C  
ATOM    388  CG  PHE A  40      60.703  75.131   8.731  1.00 34.19           C  
ANISOU  388  CG  PHE A  40     4304   4843   3842   -479   -169    270       C  
ATOM    389  CD1 PHE A  40      59.866  74.180   9.312  1.00 40.63           C  
ANISOU  389  CD1 PHE A  40     5142   5624   4672   -392    -18    399       C  
ATOM    390  CD2 PHE A  40      61.325  74.839   7.544  1.00 34.10           C  
ANISOU  390  CD2 PHE A  40     4060   4833   4064   -465   -248    263       C  
ATOM    391  CE1 PHE A  40      59.688  72.955   8.723  1.00 41.00           C  
ANISOU  391  CE1 PHE A  40     5011   5599   4970   -326     16    506       C  
ATOM    392  CE2 PHE A  40      61.174  73.601   6.948  1.00 37.18           C  
ANISOU  392  CE2 PHE A  40     4293   5158   4676   -354   -197    353       C  
ATOM    393  CZ  PHE A  40      60.340  72.652   7.547  1.00 37.38           C  
ANISOU  393  CZ  PHE A  40     4374   5107   4721   -301    -78    467       C  
ATOM    394  N   ASN A  41      59.540  78.623  11.144  1.00 54.75           N  
ANISOU  394  N   ASN A  41     7976   7284   5542   -582     66   -126       N  
ATOM    395  CA  ASN A  41      59.905  79.675  12.069  1.00 53.06           C  
ANISOU  395  CA  ASN A  41     8211   7010   4939   -706    -14   -270       C  
ATOM    396  C   ASN A  41      61.433  79.866  12.117  1.00 64.92           C  
ANISOU  396  C   ASN A  41     9689   8617   6361  -1002   -416   -271       C  
ATOM    397  O   ASN A  41      62.182  78.939  12.450  1.00 47.36           O  
ANISOU  397  O   ASN A  41     7262   6588   4146  -1059   -618    -96       O  
ATOM    398  CB  ASN A  41      59.346  79.373  13.460  1.00 58.25           C  
ANISOU  398  CB  ASN A  41     9168   7709   5257   -606    141   -215       C  
ATOM    399  CG  ASN A  41      59.554  80.508  14.427  1.00 69.10           C  
ANISOU  399  CG  ASN A  41    11114   8974   6166   -709     99   -407       C  
ATOM    400  OD1 ASN A  41      60.578  80.586  15.113  1.00 78.20           O  
ANISOU  400  OD1 ASN A  41    12449  10214   7047   -951   -223   -418       O  
ATOM    401  ND2 ASN A  41      58.576  81.397  14.500  1.00 76.07           N  
ANISOU  401  ND2 ASN A  41    12302   9662   6941   -520    420   -555       N  
ATOM    402  N   ASP A  42      61.876  81.066  11.752  1.00 69.06           N  
ANISOU  402  N   ASP A  42    10400   9012   6826  -1187   -526   -439       N  
ATOM    403  CA  ASP A  42      63.279  81.471  11.851  1.00 71.67           C  
ANISOU  403  CA  ASP A  42    10724   9446   7061  -1536   -912   -438       C  
ATOM    404  C   ASP A  42      63.983  81.029  13.139  1.00 68.37           C  
ANISOU  404  C   ASP A  42    10433   9229   6315  -1691  -1184   -342       C  
ATOM    405  O   ASP A  42      64.991  80.316  13.104  1.00 69.41           O  
ANISOU  405  O   ASP A  42    10205   9619   6550  -1794  -1453   -145       O  
ATOM    406  CB  ASP A  42      63.377  82.996  11.719  1.00 91.48           C  
ANISOU  406  CB  ASP A  42    13641  11701   9417  -1744   -947   -665       C  
ATOM    407  CG  ASP A  42      62.497  83.735  12.722  1.00112.47           C  
ANISOU  407  CG  ASP A  42    16926  14121  11686  -1644   -744   -859       C  
ATOM    408  OD1 ASP A  42      61.612  83.090  13.328  1.00118.50           O  
ANISOU  408  OD1 ASP A  42    17735  14930  12360  -1363   -497   -804       O  
ATOM    409  OD2 ASP A  42      62.693  84.958  12.908  1.00119.09           O  
ANISOU  409  OD2 ASP A  42    18084  14720  12446  -1760   -765   -993       O  
ATOM    410  N   ARG A  43      63.439  81.472  14.268  1.00 52.09           N  
ANISOU  410  N   ARG A  43     8896   7055   3839  -1678  -1099   -469       N  
ATOM    411  CA  ARG A  43      63.983  81.206  15.591  1.00 59.56           C  
ANISOU  411  CA  ARG A  43    10033   8154   4442  -1791  -1322   -395       C  
ATOM    412  C   ARG A  43      63.765  79.760  16.061  1.00 67.10           C  
ANISOU  412  C   ARG A  43    10786   9340   5371  -1593  -1282   -139       C  
ATOM    413  O   ARG A  43      64.552  79.226  16.854  1.00 59.40           O  
ANISOU  413  O   ARG A  43     9755   8584   4232  -1689  -1561     26       O  
ATOM    414  CB  ARG A  43      63.343  82.160  16.600  1.00 67.30           C  
ANISOU  414  CB  ARG A  43    11591   8887   5092  -1728  -1133   -606       C  
ATOM    415  CG  ARG A  43      64.220  83.339  17.003  1.00 82.87           C  
ANISOU  415  CG  ARG A  43    13788  10731   6969  -2026  -1383   -739       C  
ATOM    416  CD  ARG A  43      63.646  84.667  16.517  1.00 82.69           C  
ANISOU  416  CD  ARG A  43    14091  10334   6993  -1995  -1158   -964       C  
ATOM    417  NE  ARG A  43      64.661  85.717  16.466  1.00 80.72           N  
ANISOU  417  NE  ARG A  43    13936   9972   6763  -2347  -1429  -1026       N  
ATOM    418  CZ  ARG A  43      64.934  86.549  17.466  1.00 92.50           C  
ANISOU  418  CZ  ARG A  43    15878  11311   7955  -2513  -1535  -1146       C  
ATOM    419  NH1 ARG A  43      65.880  87.469  17.325  1.00 96.46           N  
ANISOU  419  NH1 ARG A  43    16443  11717   8488  -2868  -1785  -1174       N  
ATOM    420  NH2 ARG A  43      64.264  86.465  18.608  1.00 99.22           N  
ANISOU  420  NH2 ARG A  43    17127  12109   8461  -2332  -1382  -1227       N  
ATOM    421  N   ASP A  44      62.690  79.137  15.592  1.00 63.77           N  
ANISOU  421  N   ASP A  44    10181   8834   5214  -1274   -898    -79       N  
ATOM    422  CA  ASP A  44      62.328  77.800  16.051  1.00 65.55           C  
ANISOU  422  CA  ASP A  44    10235   9189   5484  -1068   -781    170       C  
ATOM    423  C   ASP A  44      61.944  76.971  14.851  1.00 63.16           C  
ANISOU  423  C   ASP A  44     9450   8852   5698   -890   -609    280       C  
ATOM    424  O   ASP A  44      60.767  76.896  14.509  1.00 70.29           O  
ANISOU  424  O   ASP A  44    10334   9623   6749   -708   -266    246       O  
ATOM    425  CB  ASP A  44      61.149  77.869  17.026  1.00 68.69           C  
ANISOU  425  CB  ASP A  44    11036   9500   5563   -887   -432    137       C  
ATOM    426  CG  ASP A  44      60.743  76.495  17.572  1.00 74.21           C  
ANISOU  426  CG  ASP A  44    11591  10318   6289   -713   -294    427       C  
ATOM    427  OD1 ASP A  44      61.248  75.457  17.079  1.00 66.41           O  
ANISOU  427  OD1 ASP A  44    10201   9420   5612   -693   -434    635       O  
ATOM    428  OD2 ASP A  44      59.902  76.458  18.501  1.00 70.84           O  
ANISOU  428  OD2 ASP A  44    11480   9876   5561   -583    -18    457       O  
ATOM    429  N   PRO A  45      62.929  76.312  14.226  1.00 55.85           N  
ANISOU  429  N   PRO A  45     8133   8055   5033   -934   -846    426       N  
ATOM    430  CA  PRO A  45      62.687  75.652  12.935  1.00 54.25           C  
ANISOU  430  CA  PRO A  45     7542   7782   5291   -790   -707    474       C  
ATOM    431  C   PRO A  45      61.883  74.363  13.086  1.00 54.86           C  
ANISOU  431  C   PRO A  45     7529   7808   5506   -587   -488    655       C  
ATOM    432  O   PRO A  45      61.603  73.686  12.094  1.00 50.62           O  
ANISOU  432  O   PRO A  45     6734   7183   5318   -485   -382    691       O  
ATOM    433  CB  PRO A  45      64.101  75.355  12.430  1.00 61.53           C  
ANISOU  433  CB  PRO A  45     8136   8875   6368   -871  -1011    594       C  
ATOM    434  CG  PRO A  45      64.891  75.134  13.686  1.00 65.21           C  
ANISOU  434  CG  PRO A  45     8718   9549   6512   -967  -1286    755       C  
ATOM    435  CD  PRO A  45      64.291  76.063  14.735  1.00 60.10           C  
ANISOU  435  CD  PRO A  45     8572   8830   5432  -1090  -1242    582       C  
ATOM    436  N   ASP A  46      61.539  74.021  14.322  1.00 52.64           N  
ANISOU  436  N   ASP A  46     7494   7574   4935   -552   -428    772       N  
ATOM    437  CA  ASP A  46      60.642  72.912  14.572  1.00 49.84           C  
ANISOU  437  CA  ASP A  46     7103   7148   4685   -405   -182    957       C  
ATOM    438  C   ASP A  46      59.200  73.340  14.342  1.00 49.01           C  
ANISOU  438  C   ASP A  46     7054   6921   4648   -342    174    843       C  
ATOM    439  O   ASP A  46      58.303  72.506  14.304  1.00 51.31           O  
ANISOU  439  O   ASP A  46     7240   7149   5106   -268    398    986       O  
ATOM    440  CB  ASP A  46      60.802  72.404  15.999  1.00 51.26           C  
ANISOU  440  CB  ASP A  46     7530   7442   4503   -388   -228   1163       C  
ATOM    441  CG  ASP A  46      62.052  71.588  16.179  1.00 64.84           C  
ANISOU  441  CG  ASP A  46     9102   9292   6240   -375   -545   1386       C  
ATOM    442  OD1 ASP A  46      62.559  71.087  15.153  1.00 63.46           O  
ANISOU  442  OD1 ASP A  46     8609   9074   6428   -318   -622   1419       O  
ATOM    443  OD2 ASP A  46      62.521  71.446  17.334  1.00 73.76           O  
ANISOU  443  OD2 ASP A  46    10439  10576   7008   -398   -709   1538       O  
ATOM    444  N   GLU A  47      58.965  74.642  14.224  1.00 42.03           N  
ANISOU  444  N   GLU A  47     6334   6002   3632   -374    228    609       N  
ATOM    445  CA  GLU A  47      57.598  75.116  14.019  1.00 46.97           C  
ANISOU  445  CA  GLU A  47     6982   6541   4324   -255    579    534       C  
ATOM    446  C   GLU A  47      57.313  75.384  12.558  1.00 44.62           C  
ANISOU  446  C   GLU A  47     6393   6155   4405   -243    592    423       C  
ATOM    447  O   GLU A  47      57.856  76.320  11.971  1.00 36.86           O  
ANISOU  447  O   GLU A  47     5452   5127   3425   -305    455    244       O  
ATOM    448  CB  GLU A  47      57.323  76.388  14.809  1.00 51.40           C  
ANISOU  448  CB  GLU A  47     7966   7073   4492   -217    704    357       C  
ATOM    449  CG  GLU A  47      55.958  76.987  14.483  1.00 49.43           C  
ANISOU  449  CG  GLU A  47     7693   6745   4342    -26   1085    296       C  
ATOM    450  CD  GLU A  47      55.636  78.210  15.326  1.00 73.17           C  
ANISOU  450  CD  GLU A  47    11193   9676   6933     83   1275    123       C  
ATOM    451  OE1 GLU A  47      56.021  78.223  16.516  1.00 84.76           O  
ANISOU  451  OE1 GLU A  47    13038  11189   7976     40   1234    125       O  
ATOM    452  OE2 GLU A  47      55.005  79.156  14.799  1.00 69.97           O  
ANISOU  452  OE2 GLU A  47    10829   9153   6602    226   1464    -12       O  
ATOM    453  N   LEU A  48      56.446  74.575  11.966  1.00 31.96           N  
ANISOU  453  N   LEU A  48     4512   4526   3107   -190    747    540       N  
ATOM    454  CA  LEU A  48      56.123  74.752  10.562  1.00 32.50           C  
ANISOU  454  CA  LEU A  48     4319   4529   3501   -189    733    448       C  
ATOM    455  C   LEU A  48      55.096  75.875  10.394  1.00 31.36           C  
ANISOU  455  C   LEU A  48     4217   4368   3329    -66    963    347       C  
ATOM    456  O   LEU A  48      54.042  75.853  11.009  1.00 33.33           O  
ANISOU  456  O   LEU A  48     4476   4668   3519     45   1239    449       O  
ATOM    457  CB  LEU A  48      55.556  73.455   9.969  1.00 32.97           C  
ANISOU  457  CB  LEU A  48     4099   4553   3876   -223    769    602       C  
ATOM    458  CG  LEU A  48      55.169  73.462   8.487  1.00 30.71           C  
ANISOU  458  CG  LEU A  48     3561   4209   3898   -248    720    517       C  
ATOM    459  CD1 LEU A  48      56.403  73.565   7.584  1.00 29.67           C  
ANISOU  459  CD1 LEU A  48     3412   4032   3828   -286    475    389       C  
ATOM    460  CD2 LEU A  48      54.365  72.180   8.205  1.00 35.94           C  
ANISOU  460  CD2 LEU A  48     4029   4821   4804   -333    778    680       C  
ATOM    461  N   LEU A  49      55.398  76.822   9.528  1.00 30.61           N  
ANISOU  461  N   LEU A  49     4132   4209   3291    -65    869    176       N  
ATOM    462  CA  LEU A  49      54.506  77.972   9.317  1.00 39.24           C  
ANISOU  462  CA  LEU A  49     5298   5254   4356     99   1080     91       C  
ATOM    463  C   LEU A  49      53.474  77.697   8.216  1.00 33.53           C  
ANISOU  463  C   LEU A  49     4200   4573   3966    167   1160    173       C  
ATOM    464  O   LEU A  49      52.270  77.989   8.370  1.00 35.13           O  
ANISOU  464  O   LEU A  49     4304   4837   4206    341   1421    261       O  
ATOM    465  CB  LEU A  49      55.341  79.216   8.975  1.00 37.59           C  
ANISOU  465  CB  LEU A  49     5342   4920   4020     51    936   -113       C  
ATOM    466  CG  LEU A  49      56.370  79.636  10.019  1.00 38.65           C  
ANISOU  466  CG  LEU A  49     5859   5019   3806    -82    796   -208       C  
ATOM    467  CD1 LEU A  49      57.123  80.834   9.492  1.00 42.07           C  
ANISOU  467  CD1 LEU A  49     6493   5311   4181   -194    640   -387       C  
ATOM    468  CD2 LEU A  49      55.731  79.942  11.403  1.00 43.18           C  
ANISOU  468  CD2 LEU A  49     6788   5583   4036     56   1047   -209       C  
ATOM    469  N   SER A  50      53.943  77.136   7.104  1.00 30.47           N  
ANISOU  469  N   SER A  50     3601   4171   3805     39    937    155       N  
ATOM    470  CA  SER A  50      53.081  76.785   5.982  1.00 35.33           C  
ANISOU  470  CA  SER A  50     3894   4830   4702     43    932    217       C  
ATOM    471  C   SER A  50      53.821  75.757   5.116  1.00 36.66           C  
ANISOU  471  C   SER A  50     3944   4953   5031   -127    690    198       C  
ATOM    472  O   SER A  50      55.022  75.628   5.213  1.00 32.71           O  
ANISOU  472  O   SER A  50     3577   4406   4447   -188    549    132       O  
ATOM    473  CB  SER A  50      52.827  78.028   5.120  1.00 31.64           C  
ANISOU  473  CB  SER A  50     3438   4329   4256    169    943    119       C  
ATOM    474  OG  SER A  50      54.040  78.546   4.586  1.00 34.69           O  
ANISOU  474  OG  SER A  50     3992   4614   4574     87    754    -32       O  
ATOM    475  N   ASN A  51      53.094  75.025   4.284  1.00 32.32           N  
ANISOU  475  N   ASN A  51     3153   4425   4704   -199    645    263       N  
ATOM    476  CA  ASN A  51      53.728  74.123   3.335  1.00 28.01           C  
ANISOU  476  CA  ASN A  51     2571   3792   4281   -325    442    208       C  
ATOM    477  C   ASN A  51      52.811  74.022   2.151  1.00 35.78           C  
ANISOU  477  C   ASN A  51     3350   4810   5436   -381    369    209       C  
ATOM    478  O   ASN A  51      51.611  74.311   2.249  1.00 32.77           O  
ANISOU  478  O   ASN A  51     2777   4547   5127   -354    471    319       O  
ATOM    479  CB  ASN A  51      53.951  72.733   3.945  1.00 30.97           C  
ANISOU  479  CB  ASN A  51     2978   4089   4702   -430    429    316       C  
ATOM    480  CG  ASN A  51      52.643  71.963   4.142  1.00 41.76           C  
ANISOU  480  CG  ASN A  51     4164   5481   6220   -549    518    481       C  
ATOM    481  OD1 ASN A  51      52.238  71.157   3.310  1.00 49.37           O  
ANISOU  481  OD1 ASN A  51     5033   6371   7356   -704    402    487       O  
ATOM    482  ND2 ASN A  51      51.981  72.232   5.236  1.00 34.19           N  
ANISOU  482  ND2 ASN A  51     3174   4630   5186   -492    727    619       N  
ATOM    483  N   ILE A  52      53.351  73.601   1.025  1.00 32.92           N  
ANISOU  483  N   ILE A  52     3018   4366   5126   -451    195    103       N  
ATOM    484  CA  ILE A  52      52.530  73.494  -0.162  1.00 35.08           C  
ANISOU  484  CA  ILE A  52     3141   4677   5510   -532     73     90       C  
ATOM    485  C   ILE A  52      53.076  72.387  -1.041  1.00 37.41           C  
ANISOU  485  C   ILE A  52     3554   4816   5843   -661    -90     -9       C  
ATOM    486  O   ILE A  52      54.270  72.172  -1.115  1.00 34.08           O  
ANISOU  486  O   ILE A  52     3308   4292   5348   -593    -98    -95       O  
ATOM    487  CB  ILE A  52      52.446  74.857  -0.911  1.00 35.97           C  
ANISOU  487  CB  ILE A  52     3232   4879   5555   -388     60     31       C  
ATOM    488  CG1 ILE A  52      51.476  74.784  -2.097  1.00 42.72           C  
ANISOU  488  CG1 ILE A  52     3905   5825   6500   -464    -96     58       C  
ATOM    489  CG2 ILE A  52      53.824  75.333  -1.345  1.00 34.03           C  
ANISOU  489  CG2 ILE A  52     3194   4551   5184   -323     19   -108       C  
ATOM    490  CD1 ILE A  52      51.087  76.147  -2.630  1.00 40.59           C  
ANISOU  490  CD1 ILE A  52     3574   5666   6181   -281    -76     82       C  
ATOM    491  N  ASER A  53      52.176  71.654  -1.668  0.50 33.54           N  
ANISOU  491  N  ASER A  53     2971   4309   5465   -850   -216     17       N  
ATOM    492  N  BSER A  53      52.185  71.658  -1.700  0.50 33.93           N  
ANISOU  492  N  BSER A  53     3022   4357   5512   -850   -220     13       N  
ATOM    493  CA ASER A  53      52.582  70.684  -2.654  0.50 35.73           C  
ANISOU  493  CA ASER A  53     3438   4399   5737   -969   -376   -116       C  
ATOM    494  CA BSER A  53      52.614  70.636  -2.646  0.50 36.30           C  
ANISOU  494  CA BSER A  53     3521   4463   5810   -970   -375   -118       C  
ATOM    495  C  ASER A  53      52.325  71.288  -4.013  0.50 33.86           C  
ANISOU  495  C  ASER A  53     3183   4254   5430   -968   -530   -217       C  
ATOM    496  C  BSER A  53      52.211  70.992  -4.066  0.50 36.01           C  
ANISOU  496  C  BSER A  53     3468   4492   5720  -1024   -560   -219       C  
ATOM    497  O  ASER A  53      51.357  72.018  -4.203  0.50 31.21           O  
ANISOU  497  O  ASER A  53     2613   4116   5131   -979   -574   -126       O  
ATOM    498  O  BSER A  53      51.020  71.214  -4.347  0.50 28.40           O  
ANISOU  498  O  BSER A  53     2272   3686   4831  -1152   -666   -125       O  
ATOM    499  CB ASER A  53      51.781  69.398  -2.480  0.50 41.76           C  
ANISOU  499  CB ASER A  53     4192   5034   6641  -1245   -454    -37       C  
ATOM    500  CB BSER A  53      52.016  69.279  -2.294  0.50 43.10           C  
ANISOU  500  CB BSER A  53     4408   5165   6804  -1219   -422    -38       C  
ATOM    501  OG ASER A  53      52.045  68.846  -1.203  0.50 41.27           O  
ANISOU  501  OG ASER A  53     4173   4884   6625  -1228   -295     87       O  
ATOM    502  OG BSER A  53      52.302  68.352  -3.326  0.50 45.82           O  
ANISOU  502  OG BSER A  53     5012   5279   7121  -1341   -582   -195       O  
ATOM    503  N   LEU A  54      53.202  70.997  -4.961  1.00 31.92           N  
ANISOU  503  N   LEU A  54     3186   3876   5067   -922   -596   -384       N  
ATOM    504  CA  LEU A  54      53.005  71.468  -6.318  1.00 33.62           C  
ANISOU  504  CA  LEU A  54     3443   4167   5164   -928   -748   -480       C  
ATOM    505  C   LEU A  54      53.389  70.385  -7.314  1.00 37.52           C  
ANISOU  505  C   LEU A  54     4257   4442   5556  -1026   -867   -657       C  
ATOM    506  O   LEU A  54      54.410  69.724  -7.131  1.00 42.19           O  
ANISOU  506  O   LEU A  54     5071   4840   6119   -917   -747   -733       O  
ATOM    507  CB  LEU A  54      53.876  72.693  -6.565  1.00 30.89           C  
ANISOU  507  CB  LEU A  54     3122   3920   4695   -688   -633   -505       C  
ATOM    508  CG  LEU A  54      53.709  73.922  -5.647  1.00 32.65           C  
ANISOU  508  CG  LEU A  54     3155   4290   4962   -556   -494   -377       C  
ATOM    509  CD1 LEU A  54      54.865  74.888  -5.887  1.00 35.11           C  
ANISOU  509  CD1 LEU A  54     3580   4610   5149   -390   -393   -424       C  
ATOM    510  CD2 LEU A  54      52.375  74.570  -5.995  1.00 34.19           C  
ANISOU  510  CD2 LEU A  54     3130   4661   5201   -579   -590   -268       C  
ATOM    511  N   ASP A  55      52.602  70.196  -8.368  1.00 34.20           N  
ANISOU  511  N   ASP A  55     3883   4050   5063  -1212  -1104   -721       N  
ATOM    512  CA  ASP A  55      53.077  69.315  -9.439  1.00 41.25           C  
ANISOU  512  CA  ASP A  55     5183   4713   5776  -1266  -1200   -936       C  
ATOM    513  C   ASP A  55      54.145  70.008 -10.284  1.00 44.32           C  
ANISOU  513  C   ASP A  55     5744   5151   5944   -989  -1082  -1038       C  
ATOM    514  O   ASP A  55      54.455  71.172 -10.074  1.00 39.50           O  
ANISOU  514  O   ASP A  55     4933   4738   5337   -811   -965   -938       O  
ATOM    515  CB  ASP A  55      51.960  68.655 -10.277  1.00 44.44           C  
ANISOU  515  CB  ASP A  55     5677   5077   6129  -1622  -1532  -1003       C  
ATOM    516  CG  ASP A  55      51.136  69.636 -11.108  1.00 48.51           C  
ANISOU  516  CG  ASP A  55     5972   5917   6542  -1653  -1724   -932       C  
ATOM    517  OD1 ASP A  55      51.645  70.693 -11.526  1.00 49.77           O  
ANISOU  517  OD1 ASP A  55     6111   6223   6578  -1409  -1650   -924       O  
ATOM    518  OD2 ASP A  55      49.953  69.303 -11.385  1.00 49.45           O  
ANISOU  518  OD2 ASP A  55     5938   6158   6694  -1863  -1882   -863       O  
ATOM    519  N   ASP A  56      54.725  69.275 -11.220  1.00 41.09           N  
ANISOU  519  N   ASP A  56     5734   4541   5337   -953  -1088  -1232       N  
ATOM    520  CA  ASP A  56      55.826  69.819 -11.992  1.00 37.57           C  
ANISOU  520  CA  ASP A  56     5448   4147   4680   -675   -916  -1303       C  
ATOM    521  C   ASP A  56      55.398  71.063 -12.758  1.00 36.50           C  
ANISOU  521  C   ASP A  56     5174   4286   4410   -667  -1024  -1240       C  
ATOM    522  O   ASP A  56      56.115  72.059 -12.771  1.00 38.35           O  
ANISOU  522  O   ASP A  56     5298   4662   4609   -463   -848  -1156       O  
ATOM    523  CB  ASP A  56      56.343  68.768 -12.969  1.00 40.11           C  
ANISOU  523  CB  ASP A  56     6270   4202   4768   -625   -894  -1531       C  
ATOM    524  CG  ASP A  56      57.369  69.341 -13.921  1.00 47.15           C  
ANISOU  524  CG  ASP A  56     7319   5190   5405   -341   -698  -1584       C  
ATOM    525  OD1 ASP A  56      58.500  69.589 -13.474  1.00 47.04           O  
ANISOU  525  OD1 ASP A  56     7190   5221   5462    -78   -415  -1499       O  
ATOM    526  OD2 ASP A  56      57.036  69.569 -15.090  1.00 42.35           O  
ANISOU  526  OD2 ASP A  56     6924   4642   4525   -396   -835  -1684       O  
ATOM    527  N   SER A  57      54.227  71.002 -13.396  1.00 37.18           N  
ANISOU  527  N   SER A  57     5263   4443   4421   -904  -1330  -1258       N  
ATOM    528  CA  SER A  57      53.736  72.161 -14.149  1.00 43.13           C  
ANISOU  528  CA  SER A  57     5885   5464   5040   -872  -1460  -1161       C  
ATOM    529  C   SER A  57      53.515  73.408 -13.274  1.00 46.43           C  
ANISOU  529  C   SER A  57     5890   6083   5666   -748  -1349   -930       C  
ATOM    530  O   SER A  57      53.940  74.523 -13.629  1.00 39.65           O  
ANISOU  530  O   SER A  57     5009   5345   4712   -561  -1242   -851       O  
ATOM    531  CB  SER A  57      52.458  71.807 -14.895  1.00 50.30           C  
ANISOU  531  CB  SER A  57     6812   6451   5849  -1168  -1856  -1182       C  
ATOM    532  OG  SER A  57      52.046  72.905 -15.682  1.00 56.45           O  
ANISOU  532  OG  SER A  57     7483   7493   6472  -1091  -1986  -1064       O  
ATOM    533  N   GLU A  58      52.858  73.223 -12.130  1.00 40.41           N  
ANISOU  533  N   GLU A  58     4845   5336   5174   -849  -1355   -820       N  
ATOM    534  CA  GLU A  58      52.640  74.328 -11.187  1.00 39.04           C  
ANISOU  534  CA  GLU A  58     4352   5308   5174   -708  -1212   -629       C  
ATOM    535  C   GLU A  58      53.943  74.929 -10.698  1.00 44.18           C  
ANISOU  535  C   GLU A  58     5081   5892   5813   -495   -928   -639       C  
ATOM    536  O   GLU A  58      54.092  76.161 -10.600  1.00 38.66           O  
ANISOU  536  O   GLU A  58     4300   5284   5103   -349   -830   -536       O  
ATOM    537  CB  GLU A  58      51.825  73.845  -9.977  1.00 40.86           C  
ANISOU  537  CB  GLU A  58     4317   5547   5662   -841  -1210   -521       C  
ATOM    538  CG  GLU A  58      50.379  73.499 -10.328  1.00 42.94           C  
ANISOU  538  CG  GLU A  58     4360   5962   5994  -1079  -1494   -424       C  
ATOM    539  CD  GLU A  58      49.661  72.709  -9.238  1.00 43.81           C  
ANISOU  539  CD  GLU A  58     4244   6052   6348  -1275  -1480   -320       C  
ATOM    540  OE1 GLU A  58      50.328  71.974  -8.468  1.00 45.31           O  
ANISOU  540  OE1 GLU A  58     4586   6029   6602  -1292  -1320   -391       O  
ATOM    541  OE2 GLU A  58      48.422  72.809  -9.171  1.00 59.66           O  
ANISOU  541  OE2 GLU A  58     5972   8262   8436  -1337  -1536   -168       O  
ATOM    542  N   ALA A  59      54.890  74.055 -10.371  1.00 34.57           N  
ANISOU  542  N   ALA A  59     4024   4508   4605   -484   -805   -746       N  
ATOM    543  CA  ALA A  59      56.172  74.520  -9.875  1.00 31.21           C  
ANISOU  543  CA  ALA A  59     3614   4061   4183   -318   -572   -727       C  
ATOM    544  C   ALA A  59      56.886  75.375 -10.908  1.00 27.80           C  
ANISOU  544  C   ALA A  59     3298   3704   3561   -197   -502   -731       C  
ATOM    545  O   ALA A  59      57.501  76.392 -10.566  1.00 31.13           O  
ANISOU  545  O   ALA A  59     3643   4184   4001   -118   -370   -640       O  
ATOM    546  CB  ALA A  59      57.052  73.343  -9.468  1.00 33.86           C  
ANISOU  546  CB  ALA A  59     4077   4232   4557   -288   -466   -806       C  
ATOM    547  N   ARG A  60      56.844  74.959 -12.168  1.00 32.58           N  
ANISOU  547  N   ARG A  60     4123   4295   3963   -202   -587   -834       N  
ATOM    548  CA  ARG A  60      57.551  75.716 -13.194  1.00 32.17           C  
ANISOU  548  CA  ARG A  60     4202   4322   3698    -80   -489   -816       C  
ATOM    549  C   ARG A  60      56.868  77.050 -13.504  1.00 38.62           C  
ANISOU  549  C   ARG A  60     4918   5275   4481    -71   -575   -672       C  
ATOM    550  O   ARG A  60      57.538  78.019 -13.852  1.00 35.83           O  
ANISOU  550  O   ARG A  60     4599   4972   4045     20   -438   -582       O  
ATOM    551  CB  ARG A  60      57.744  74.877 -14.488  1.00 37.89           C  
ANISOU  551  CB  ARG A  60     5262   4985   4148    -57   -526   -978       C  
ATOM    552  CG  ARG A  60      58.817  73.806 -14.335  1.00 40.26           C  
ANISOU  552  CG  ARG A  60     5718   5134   4446     59   -321  -1089       C  
ATOM    553  CD  ARG A  60      59.046  72.973 -15.606  1.00 40.11           C  
ANISOU  553  CD  ARG A  60     6116   5008   4115    129   -306  -1276       C  
ATOM    554  NE  ARG A  60      57.890  72.138 -15.920  1.00 37.87           N  
ANISOU  554  NE  ARG A  60     6031   4594   3764    -90   -609  -1425       N  
ATOM    555  CZ  ARG A  60      56.970  72.468 -16.823  1.00 46.28           C  
ANISOU  555  CZ  ARG A  60     7199   5761   4625   -234   -876  -1450       C  
ATOM    556  NH1 ARG A  60      57.087  73.605 -17.506  1.00 39.15           N  
ANISOU  556  NH1 ARG A  60     6253   5063   3558   -139   -847  -1332       N  
ATOM    557  NH2 ARG A  60      55.939  71.660 -17.053  1.00 47.81           N  
ANISOU  557  NH2 ARG A  60     7538   5852   4774   -492  -1190  -1571       N  
ATOM    558  N   GLN A  61      55.540  77.096 -13.404  1.00 36.49           N  
ANISOU  558  N   GLN A  61     4518   5067   4281   -160   -795   -624       N  
ATOM    559  CA  GLN A  61      54.816  78.349 -13.598  1.00 40.39           C  
ANISOU  559  CA  GLN A  61     4892   5683   4770    -88   -863   -452       C  
ATOM    560  C   GLN A  61      55.159  79.348 -12.491  1.00 40.78           C  
ANISOU  560  C   GLN A  61     4814   5687   4995      3   -664   -342       C  
ATOM    561  O   GLN A  61      55.491  80.515 -12.758  1.00 36.18           O  
ANISOU  561  O   GLN A  61     4299   5100   4347    103   -569   -236       O  
ATOM    562  CB  GLN A  61      53.302  78.108 -13.636  1.00 37.68           C  
ANISOU  562  CB  GLN A  61     4357   5460   4499   -182  -1133   -384       C  
ATOM    563  CG  GLN A  61      52.826  77.431 -14.888  1.00 49.36           C  
ANISOU  563  CG  GLN A  61     5994   7009   5751   -309  -1407   -467       C  
ATOM    564  CD  GLN A  61      51.357  77.059 -14.819  1.00 68.53           C  
ANISOU  564  CD  GLN A  61     8161   9587   8289   -476  -1711   -379       C  
ATOM    565  OE1 GLN A  61      51.009  75.924 -14.496  1.00 76.58           O  
ANISOU  565  OE1 GLN A  61     9155  10540   9401   -699  -1826   -479       O  
ATOM    566  NE2 GLN A  61      50.489  78.017 -15.120  1.00 68.61           N  
ANISOU  566  NE2 GLN A  61     7963   9802   8302   -370  -1839   -163       N  
ATOM    567  N   ILE A  62      55.089  78.894 -11.245  1.00 37.61           N  
ANISOU  567  N   ILE A  62     4273   5228   4790    -47   -603   -367       N  
ATOM    568  CA  ILE A  62      55.468  79.759 -10.143  1.00 34.79           C  
ANISOU  568  CA  ILE A  62     3865   4809   4547     14   -430   -300       C  
ATOM    569  C   ILE A  62      56.929  80.204 -10.259  1.00 39.12           C  
ANISOU  569  C   ILE A  62     4550   5296   5016     14   -272   -318       C  
ATOM    570  O   ILE A  62      57.264  81.359 -10.007  1.00 38.40           O  
ANISOU  570  O   ILE A  62     4515   5153   4922     43   -177   -238       O  
ATOM    571  CB  ILE A  62      55.204  79.082  -8.769  1.00 34.04           C  
ANISOU  571  CB  ILE A  62     3630   4677   4626    -45   -390   -323       C  
ATOM    572  CG1 ILE A  62      53.706  78.872  -8.588  1.00 37.27           C  
ANISOU  572  CG1 ILE A  62     3839   5182   5139    -51   -507   -241       C  
ATOM    573  CG2 ILE A  62      55.758  79.940  -7.661  1.00 34.54           C  
ANISOU  573  CG2 ILE A  62     3724   4665   4736     -4   -227   -288       C  
ATOM    574  CD1 ILE A  62      53.344  77.902  -7.497  1.00 40.91           C  
ANISOU  574  CD1 ILE A  62     4169   5625   5749   -151   -484   -250       C  
ATOM    575  N   ALA A  63      57.801  79.292 -10.666  1.00 31.09           N  
ANISOU  575  N   ALA A  63     3594   4282   3938    -20   -237   -409       N  
ATOM    576  CA  ALA A  63      59.220  79.628 -10.811  1.00 35.19           C  
ANISOU  576  CA  ALA A  63     4162   4806   4403    -17    -74   -382       C  
ATOM    577  C   ALA A  63      59.419  80.674 -11.910  1.00 34.57           C  
ANISOU  577  C   ALA A  63     4208   4763   4165     20    -30   -289       C  
ATOM    578  O   ALA A  63      60.231  81.590 -11.759  1.00 31.33           O  
ANISOU  578  O   ALA A  63     3808   4336   3760    -27     89   -193       O  
ATOM    579  CB  ALA A  63      60.052  78.378 -11.109  1.00 35.04           C  
ANISOU  579  CB  ALA A  63     4172   4797   4346     17     -7   -473       C  
ATOM    580  N   ALA A  64      58.654  80.569 -12.996  1.00 31.80           N  
ANISOU  580  N   ALA A  64     3962   4459   3662     76   -146   -300       N  
ATOM    581  CA  ALA A  64      58.760  81.565 -14.056  1.00 36.28           C  
ANISOU  581  CA  ALA A  64     4673   5062   4050    128   -113   -181       C  
ATOM    582  C   ALA A  64      58.315  82.966 -13.579  1.00 36.35           C  
ANISOU  582  C   ALA A  64     4677   4989   4147    149   -105    -32       C  
ATOM    583  O   ALA A  64      58.972  83.963 -13.876  1.00 35.13           O  
ANISOU  583  O   ALA A  64     4632   4782   3935    130     19     88       O  
ATOM    584  CB  ALA A  64      57.990  81.119 -15.338  1.00 36.66           C  
ANISOU  584  CB  ALA A  64     4862   5199   3868    181   -284   -218       C  
ATOM    585  N   ILE A  65      57.226  83.041 -12.820  1.00 31.32           N  
ANISOU  585  N   ILE A  65     3928   4321   3649    191   -210    -29       N  
ATOM    586  CA  ILE A  65      56.805  84.325 -12.226  1.00 33.44           C  
ANISOU  586  CA  ILE A  65     4238   4466   4002    268   -155     92       C  
ATOM    587  C   ILE A  65      57.844  84.892 -11.257  1.00 34.74           C  
ANISOU  587  C   ILE A  65     4468   4482   4249    146      5     77       C  
ATOM    588  O   ILE A  65      58.284  86.050 -11.381  1.00 30.69           O  
ANISOU  588  O   ILE A  65     4132   3830   3697    120     97    179       O  
ATOM    589  CB  ILE A  65      55.435  84.193 -11.515  1.00 32.54           C  
ANISOU  589  CB  ILE A  65     3957   4381   4025    378   -247    110       C  
ATOM    590  CG1 ILE A  65      54.369  83.764 -12.522  1.00 37.24           C  
ANISOU  590  CG1 ILE A  65     4452   5158   4541    450   -460    168       C  
ATOM    591  CG2 ILE A  65      55.036  85.505 -10.811  1.00 32.93           C  
ANISOU  591  CG2 ILE A  65     4101   4263   4145    522   -130    220       C  
ATOM    592  CD1 ILE A  65      53.051  83.319 -11.906  1.00 35.63           C  
ANISOU  592  CD1 ILE A  65     3979   5064   4495    502   -572    206       C  
ATOM    593  N   LEU A  66      58.251  84.066 -10.300  1.00 38.18           N  
ANISOU  593  N   LEU A  66     4778   4938   4789     48     17    -39       N  
ATOM    594  CA  LEU A  66      59.228  84.464  -9.289  1.00 37.54           C  
ANISOU  594  CA  LEU A  66     4731   4762   4770   -104    107    -57       C  
ATOM    595  C   LEU A  66      60.552  84.896  -9.898  1.00 35.26           C  
ANISOU  595  C   LEU A  66     4495   4489   4412   -248    193     18       C  
ATOM    596  O   LEU A  66      61.222  85.822  -9.415  1.00 33.25           O  
ANISOU  596  O   LEU A  66     4342   4115   4174   -407    244     72       O  
ATOM    597  CB  LEU A  66      59.494  83.297  -8.335  1.00 28.69           C  
ANISOU  597  CB  LEU A  66     3444   3715   3742   -164     80   -162       C  
ATOM    598  CG  LEU A  66      60.438  83.600  -7.177  1.00 32.08           C  
ANISOU  598  CG  LEU A  66     3884   4090   4214   -331    114   -173       C  
ATOM    599  CD1 LEU A  66      59.828  84.703  -6.242  1.00 31.37           C  
ANISOU  599  CD1 LEU A  66     3992   3806   4120   -325    137   -179       C  
ATOM    600  CD2 LEU A  66      60.713  82.288  -6.390  1.00 32.32           C  
ANISOU  600  CD2 LEU A  66     3741   4224   4317   -349     76   -240       C  
ATOM    601  N   GLY A  67      60.956  84.200 -10.953  1.00 33.37           N  
ANISOU  601  N   GLY A  67     4194   4400   4085   -209    217     25       N  
ATOM    602  CA  GLY A  67      62.240  84.468 -11.553  1.00 32.63           C  
ANISOU  602  CA  GLY A  67     4089   4379   3930   -320    346    125       C  
ATOM    603  C   GLY A  67      62.290  85.614 -12.543  1.00 29.96           C  
ANISOU  603  C   GLY A  67     3940   3977   3466   -332    417    281       C  
ATOM    604  O   GLY A  67      63.340  85.870 -13.135  1.00 36.98           O  
ANISOU  604  O   GLY A  67     4808   4946   4297   -436    553    401       O  
ATOM    605  N   GLY A  68      61.164  86.286 -12.752  1.00 33.67           N  
ANISOU  605  N   GLY A  68     4578   4320   3897   -209    340    312       N  
ATOM    606  CA  GLY A  68      61.128  87.461 -13.620  1.00 38.24           C  
ANISOU  606  CA  GLY A  68     5379   4793   4357   -194    401    492       C  
ATOM    607  C   GLY A  68      60.977  87.131 -15.103  1.00 38.35           C  
ANISOU  607  C   GLY A  68     5453   4969   4149    -59    408    559       C  
ATOM    608  O   GLY A  68      61.321  87.945 -15.972  1.00 37.33           O  
ANISOU  608  O   GLY A  68     5494   4807   3883    -77    505    739       O  
ATOM    609  N   MET A  69      60.441  85.944 -15.383  1.00 37.92           N  
ANISOU  609  N   MET A  69     5299   5072   4038     60    296    417       N  
ATOM    610  CA  MET A  69      60.300  85.441 -16.746  1.00 44.09           C  
ANISOU  610  CA  MET A  69     6187   6009   4558    170    272    425       C  
ATOM    611  C   MET A  69      58.965  85.816 -17.347  1.00 38.24           C  
ANISOU  611  C   MET A  69     5553   5274   3701    322     69    496       C  
ATOM    612  O   MET A  69      58.799  85.781 -18.555  1.00 44.71           O  
ANISOU  612  O   MET A  69     6530   6204   4253    401     22    560       O  
ATOM    613  CB  MET A  69      60.481  83.928 -16.770  1.00 41.83           C  
ANISOU  613  CB  MET A  69     5804   5846   4243    189    245    218       C  
ATOM    614  CG  MET A  69      61.868  83.460 -16.347  1.00 42.55           C  
ANISOU  614  CG  MET A  69     5761   5983   4424    107    460    191       C  
ATOM    615  SD  MET A  69      63.107  83.764 -17.636  1.00 77.84           S  
ANISOU  615  SD  MET A  69    10339  10590   8645    130    746    354       S  
ATOM    616  CE  MET A  69      63.699  85.409 -17.236  1.00 65.34           C  
ANISOU  616  CE  MET A  69     8728   8900   7198    -80    852    611       C  
ATOM    617  N   VAL A  70      58.019  86.209 -16.502  1.00 37.18           N  
ANISOU  617  N   VAL A  70     5331   5042   3754    381    -45    509       N  
ATOM    618  CA  VAL A  70      56.725  86.690 -16.971  1.00 43.14           C  
ANISOU  618  CA  VAL A  70     6117   5830   4445    563   -230    638       C  
ATOM    619  C   VAL A  70      56.702  88.219 -17.000  1.00 47.64           C  
ANISOU  619  C   VAL A  70     6876   6198   5027    658   -122    867       C  
ATOM    620  O   VAL A  70      56.574  88.844 -18.054  1.00 49.07           O  
ANISOU  620  O   VAL A  70     7240   6398   5005    758   -142   1056       O  
ATOM    621  CB  VAL A  70      55.591  86.192 -16.068  1.00 41.42           C  
ANISOU  621  CB  VAL A  70     5655   5651   4430    624   -387    559       C  
ATOM    622  CG1 VAL A  70      54.246  86.619 -16.649  1.00 45.47           C  
ANISOU  622  CG1 VAL A  70     6118   6276   4883    828   -594    738       C  
ATOM    623  CG2 VAL A  70      55.680  84.678 -15.887  1.00 38.29           C  
ANISOU  623  CG2 VAL A  70     5113   5379   4055    488   -476    335       C  
ATOM    624  N   TYR A  71      56.806  88.817 -15.827  1.00 39.46           N  
ANISOU  624  N   TYR A  71     5842   4944   4208    630     -9    850       N  
ATOM    625  CA  TYR A  71      57.081  90.239 -15.706  1.00 41.28           C  
ANISOU  625  CA  TYR A  71     6339   4888   4458    650    137   1021       C  
ATOM    626  C   TYR A  71      58.533  90.446 -15.266  1.00 44.65           C  
ANISOU  626  C   TYR A  71     6844   5187   4935    341    315    968       C  
ATOM    627  O   TYR A  71      58.951  89.966 -14.215  1.00 40.69           O  
ANISOU  627  O   TYR A  71     6206   4675   4581    191    335    798       O  
ATOM    628  CB  TYR A  71      56.134  90.890 -14.694  1.00 42.65           C  
ANISOU  628  CB  TYR A  71     6539   4862   4806    846    146   1040       C  
ATOM    629  CG  TYR A  71      56.372  92.370 -14.519  1.00 48.13           C  
ANISOU  629  CG  TYR A  71     7600   5176   5510    880    305   1192       C  
ATOM    630  CD1 TYR A  71      55.921  93.273 -15.473  1.00 52.10           C  
ANISOU  630  CD1 TYR A  71     8320   5587   5891   1097    304   1452       C  
ATOM    631  CD2 TYR A  71      57.036  92.870 -13.404  1.00 46.75           C  
ANISOU  631  CD2 TYR A  71     7599   4715   5451    686    437   1081       C  
ATOM    632  CE1 TYR A  71      56.119  94.626 -15.329  1.00 54.16           C  
ANISOU  632  CE1 TYR A  71     8977   5439   6163   1133    458   1601       C  
ATOM    633  CE2 TYR A  71      57.246  94.247 -13.256  1.00 44.67           C  
ANISOU  633  CE2 TYR A  71     7752   4037   5181    680    571   1203       C  
ATOM    634  CZ  TYR A  71      56.780  95.108 -14.226  1.00 52.54           C  
ANISOU  634  CZ  TYR A  71     8974   4912   6076    912    594   1464       C  
ATOM    635  OH  TYR A  71      56.968  96.461 -14.106  1.00 58.81           O  
ANISOU  635  OH  TYR A  71    10236   5244   6867    914    735   1597       O  
ATOM    636  N   LYS A  72      59.299  91.157 -16.081  1.00 44.55           N  
ANISOU  636  N   LYS A  72     7030   5103   4793    235    434   1144       N  
ATOM    637  CA  LYS A  72      60.677  91.504 -15.754  1.00 49.58           C  
ANISOU  637  CA  LYS A  72     7707   5643   5489    -95    594   1163       C  
ATOM    638  C   LYS A  72      60.714  92.835 -15.012  1.00 44.78           C  
ANISOU  638  C   LYS A  72     7393   4631   4991   -197    657   1240       C  
ATOM    639  O   LYS A  72      60.181  93.823 -15.517  1.00 46.30           O  
ANISOU  639  O   LYS A  72     7875   4606   5112    -40    686   1425       O  
ATOM    640  CB  LYS A  72      61.475  91.630 -17.052  1.00 53.73           C  
ANISOU  640  CB  LYS A  72     8298   6302   5814   -176    723   1352       C  
ATOM    641  CG  LYS A  72      62.915  92.044 -16.883  1.00 50.88           C  
ANISOU  641  CG  LYS A  72     7917   5898   5518   -537    902   1450       C  
ATOM    642  CD  LYS A  72      63.441  92.530 -18.244  1.00 55.27           C  
ANISOU  642  CD  LYS A  72     8623   6522   5855   -565   1070   1721       C  
ATOM    643  CE  LYS A  72      64.381  93.690 -18.093  1.00 61.70           C  
ANISOU  643  CE  LYS A  72     9591   7099   6752   -916   1219   1936       C  
ATOM    644  NZ  LYS A  72      63.732  94.805 -17.363  1.00 65.25           N  
ANISOU  644  NZ  LYS A  72    10370   7102   7319   -927   1134   1947       N  
ATOM    645  N   PRO A  73      61.324  92.863 -13.806  1.00 41.71           N  
ANISOU  645  N   PRO A  73     6970   4123   4755   -452    667   1099       N  
ATOM    646  CA  PRO A  73      61.487  94.130 -13.078  1.00 45.40           C  
ANISOU  646  CA  PRO A  73     7801   4161   5288   -615    719   1136       C  
ATOM    647  C   PRO A  73      62.076  95.177 -14.013  1.00 57.29           C  
ANISOU  647  C   PRO A  73     9581   5479   6705   -776    837   1402       C  
ATOM    648  O   PRO A  73      63.068  94.919 -14.694  1.00 50.13           O  
ANISOU  648  O   PRO A  73     8507   4791   5751  -1006    909   1519       O  
ATOM    649  CB  PRO A  73      62.465  93.768 -11.955  1.00 46.72           C  
ANISOU  649  CB  PRO A  73     7818   4365   5568   -982    680    974       C  
ATOM    650  CG  PRO A  73      62.166  92.310 -11.666  1.00 47.03           C  
ANISOU  650  CG  PRO A  73     7457   4768   5646   -819    594    797       C  
ATOM    651  CD  PRO A  73      61.879  91.719 -13.058  1.00 45.60           C  
ANISOU  651  CD  PRO A  73     7126   4857   5343   -596    616    902       C  
ATOM    652  N   GLN A  74      61.436  96.337 -14.081  1.00 60.90           N  
ANISOU  652  N   GLN A  74    10464   5538   7137   -621    882   1524       N  
ATOM    653  CA  GLN A  74      61.731  97.273 -15.154  1.00 64.78           C  
ANISOU  653  CA  GLN A  74    11241   5855   7518   -677    994   1823       C  
ATOM    654  C   GLN A  74      63.085  97.956 -15.026  1.00 69.01           C  
ANISOU  654  C   GLN A  74    11909   6208   8104  -1220   1081   1924       C  
ATOM    655  O   GLN A  74      63.633  98.431 -16.019  1.00 68.52           O  
ANISOU  655  O   GLN A  74    11857   6202   7977  -1329   1168   2154       O  
ATOM    656  CB  GLN A  74      60.599  98.292 -15.303  1.00 80.00           C  
ANISOU  656  CB  GLN A  74    13591   7399   9407   -291   1021   1957       C  
ATOM    657  CG  GLN A  74      59.307  97.652 -15.793  1.00 86.40           C  
ANISOU  657  CG  GLN A  74    14176   8501  10150    227    916   1967       C  
ATOM    658  CD  GLN A  74      58.199  98.651 -16.068  1.00 95.99           C  
ANISOU  658  CD  GLN A  74    15716   9421  11335    663    940   2161       C  
ATOM    659  OE1 GLN A  74      58.251  99.800 -15.625  1.00103.60           O  
ANISOU  659  OE1 GLN A  74    16973  10009  12383    614   1012   2137       O  
ATOM    660  NE2 GLN A  74      57.184  98.211 -16.807  1.00 88.58           N  
ANISOU  660  NE2 GLN A  74    14583   8774  10300   1071    827   2286       N  
ATOM    661  N   ALA A  75      63.638  97.983 -13.818  1.00 62.65           N  
ANISOU  661  N   ALA A  75    11054   5310   7439  -1530   1002   1713       N  
ATOM    662  CA  ALA A  75      64.893  98.694 -13.591  1.00 69.01           C  
ANISOU  662  CA  ALA A  75    11823   6054   8344  -2009    986   1751       C  
ATOM    663  C   ALA A  75      66.129  97.847 -13.907  1.00 65.34           C  
ANISOU  663  C   ALA A  75    10868   6041   7917  -2330   1017   1837       C  
ATOM    664  O   ALA A  75      67.206  98.378 -14.182  1.00 70.34           O  
ANISOU  664  O   ALA A  75    11381   6721   8623  -2659   1056   1987       O  
ATOM    665  CB  ALA A  75      64.953  99.233 -12.171  1.00 74.31           C  
ANISOU  665  CB  ALA A  75    12688   6445   9102  -2180    857   1496       C  
ATOM    666  N   LEU A  76      65.973  96.530 -13.878  1.00 64.39           N  
ANISOU  666  N   LEU A  76    10451   6261   7755  -2208   1018   1755       N  
ATOM    667  CA  LEU A  76      67.087  95.640 -14.178  1.00 60.18           C  
ANISOU  667  CA  LEU A  76     9419   6194   7251  -2417   1079   1830       C  
ATOM    668  C   LEU A  76      67.374  95.570 -15.683  1.00 66.79           C  
ANISOU  668  C   LEU A  76    10180   7259   7937  -2310   1290   2101       C  
ATOM    669  O   LEU A  76      66.530  95.135 -16.456  1.00 74.02           O  
ANISOU  669  O   LEU A  76    11141   8285   8696  -1885   1315   2080       O  
ATOM    670  CB  LEU A  76      66.796  94.253 -13.640  1.00 51.59           C  
ANISOU  670  CB  LEU A  76     7963   5439   6199  -2171    979   1579       C  
ATOM    671  CG  LEU A  76      66.449  94.227 -12.154  1.00 59.43           C  
ANISOU  671  CG  LEU A  76     9040   6244   7297  -2238    791   1321       C  
ATOM    672  CD1 LEU A  76      66.447  92.806 -11.691  1.00 56.37           C  
ANISOU  672  CD1 LEU A  76     8233   6228   6958  -2067    717   1140       C  
ATOM    673  CD2 LEU A  76      67.433  95.062 -11.354  1.00 60.07           C  
ANISOU  673  CD2 LEU A  76     9194   6151   7480  -2729    701   1345       C  
ATOM    674  N   GLU A  77      68.562  95.996 -16.100  1.00 63.25           N  
ANISOU  674  N   GLU A  77     9519   6941   7572  -2575   1395   2297       N  
ATOM    675  CA  GLU A  77      68.915  95.911 -17.519  1.00 75.56           C  
ANISOU  675  CA  GLU A  77    10998   8742   8971  -2457   1634   2563       C  
ATOM    676  C   GLU A  77      69.800  94.700 -17.819  1.00 80.31           C  
ANISOU  676  C   GLU A  77    11097   9858   9560  -2432   1788   2579       C  
ATOM    677  O   GLU A  77      69.820  94.194 -18.943  1.00 88.12           O  
ANISOU  677  O   GLU A  77    12045  11109  10329  -2198   1995   2701       O  
ATOM    678  CB  GLU A  77      69.586  97.196 -18.009  1.00 80.72           C  
ANISOU  678  CB  GLU A  77    11775   9193   9701  -2688   1732   2821       C  
ATOM    679  CG  GLU A  77      69.715  97.265 -19.529  1.00100.14           C  
ANISOU  679  CG  GLU A  77    14261  11839  11947  -2508   1982   3118       C  
ATOM    680  CD  GLU A  77      70.626  98.378 -20.006  1.00115.53           C  
ANISOU  680  CD  GLU A  77    16228  13659  14007  -2783   2133   3406       C  
ATOM    681  OE1 GLU A  77      71.048  99.204 -19.169  1.00122.79           O  
ANISOU  681  OE1 GLU A  77    17206  14291  15156  -3123   2011   3358       O  
ATOM    682  OE2 GLU A  77      70.923  98.422 -21.220  1.00120.77           O  
ANISOU  682  OE2 GLU A  77    16867  14511  14508  -2663   2376   3677       O  
ATOM    683  N   SER A  78      70.533  94.244 -16.809  1.00 64.17           N  
ANISOU  683  N   SER A  78     8952   8417   7011     43   1607   1602       N  
ATOM    684  CA  SER A  78      71.340  93.035 -16.930  1.00 69.00           C  
ANISOU  684  CA  SER A  78     9218   9391   7607    -57   1559   1617       C  
ATOM    685  C   SER A  78      71.429  92.331 -15.577  1.00 72.08           C  
ANISOU  685  C   SER A  78     9697   9606   8083   -462   1353   1245       C  
ATOM    686  O   SER A  78      71.335  92.973 -14.538  1.00 60.17           O  
ANISOU  686  O   SER A  78     8505   7626   6730   -800   1228   1138       O  
ATOM    687  CB  SER A  78      72.742  93.378 -17.424  1.00 65.05           C  
ANISOU  687  CB  SER A  78     8498   8923   7295   -239   1604   2206       C  
ATOM    688  OG  SER A  78      73.444  94.116 -16.441  1.00 90.08           O  
ANISOU  688  OG  SER A  78    11860  11617  10749   -805   1436   2381       O  
ATOM    689  N  AILE A  79      71.592  91.012 -15.601  0.59 57.01           N  
ANISOU  689  N  AILE A  79     7560   8058   6045   -411   1325   1047       N  
ATOM    690  N  BILE A  79      71.608  91.012 -15.593  0.41 69.03           N  
ANISOU  690  N  BILE A  79     9081   9577   7570   -417   1323   1050       N  
ATOM    691  CA AILE A  79      71.750  90.236 -14.377  0.59 64.36           C  
ANISOU  691  CA AILE A  79     8546   8865   7044   -775   1140    715       C  
ATOM    692  CA BILE A  79      71.810  90.258 -14.356  0.41 64.83           C  
ANISOU  692  CA BILE A  79     8603   8913   7116   -795   1136    733       C  
ATOM    693  C  AILE A  79      72.921  89.269 -14.489  0.59 62.64           C  
ANISOU  693  C  AILE A  79     8022   8925   6852   -880   1134    919       C  
ATOM    694  C  BILE A  79      72.924  89.222 -14.481  0.41 62.21           C  
ANISOU  694  C  BILE A  79     7963   8880   6792   -879   1132    910       C  
ATOM    695  O  AILE A  79      73.326  88.888 -15.593  0.59 61.57           O  
ANISOU  695  O  AILE A  79     7648   9165   6581   -551   1300   1187       O  
ATOM    696  O  BILE A  79      73.232  88.746 -15.578  0.41 60.92           O  
ANISOU  696  O  BILE A  79     7571   9108   6466   -527   1297   1127       O  
ATOM    697  CB AILE A  79      70.482  89.425 -14.042  0.59 57.91           C  
ANISOU  697  CB AILE A  79     7832   8187   5985   -596   1099    140       C  
ATOM    698  CB BILE A  79      70.518  89.546 -13.879  0.41 56.80           C  
ANISOU  698  CB BILE A  79     7725   7973   5883   -656   1081    143       C  
ATOM    699  CG1AILE A  79      70.129  88.496 -15.205  0.59 57.01           C  
ANISOU  699  CG1AILE A  79     7513   8597   5551   -161   1219     84       C  
ATOM    700  CG1BILE A  79      70.009  88.575 -14.948  0.41 57.78           C  
ANISOU  700  CG1BILE A  79     7659   8618   5676   -220   1190     21       C  
ATOM    701  CG2AILE A  79      69.321  90.350 -13.724  0.59 54.33           C  
ANISOU  701  CG2AILE A  79     7665   7467   5511   -490   1114    -45       C  
ATOM    702  CG2BILE A  79      69.449  90.556 -13.497  0.41 53.91           C  
ANISOU  702  CG2BILE A  79     7668   7292   5523   -585   1091    -17       C  
ATOM    703  CD1AILE A  79      68.935  87.605 -14.933  0.59 54.07           C  
ANISOU  703  CD1AILE A  79     7217   8412   4914    -52   1144   -437       C  
ATOM    704  CD1BILE A  79      70.187  87.111 -14.579  0.41 54.21           C  
ANISOU  704  CD1BILE A  79     7132   8382   5082   -308   1106   -277       C  
ATOM    705  N  AGLU A  80      73.458  88.873 -13.339  0.59 60.18           N  
ANISOU  705  N  AGLU A  80     7738   8434   6695  -1310    956    807       N  
ATOM    706  N  BGLU A  80      73.518  88.880 -13.342  0.41 60.67           N  
ANISOU  706  N  BGLU A  80     7789   8496   6765  -1320    955    828       N  
ATOM    707  CA AGLU A  80      74.546  87.908 -13.284  0.59 60.83           C  
ANISOU  707  CA AGLU A  80     7534   8780   6797  -1401    951    996       C  
ATOM    708  CA BGLU A  80      74.559  87.865 -13.266  0.41 62.52           C  
ANISOU  708  CA BGLU A  80     7744   9000   7008  -1404    949    990       C  
ATOM    709  C  AGLU A  80      74.117  86.693 -12.480  0.59 62.48           C  
ANISOU  709  C  AGLU A  80     7829   9041   6867  -1458    848    477       C  
ATOM    710  C  BGLU A  80      73.901  86.529 -12.941  0.41 63.86           C  
ANISOU  710  C  BGLU A  80     7980   9350   6932  -1258    922    456       C  
ATOM    711  O  AGLU A  80      73.653  86.826 -11.349  0.59 59.81           O  
ANISOU  711  O  AGLU A  80     7727   8379   6620  -1772    673    134       O  
ATOM    712  O  BGLU A  80      73.288  86.377 -11.884  0.41 60.09           O  
ANISOU  712  O  BGLU A  80     7722   8628   6480  -1499    762     30       O  
ATOM    713  CB AGLU A  80      75.791  88.529 -12.645  0.59 72.53           C  
ANISOU  713  CB AGLU A  80     8910  10047   8602  -1915    814   1449       C  
ATOM    714  CB BGLU A  80      75.576  88.248 -12.188  0.41 68.97           C  
ANISOU  714  CB BGLU A  80     8539   9533   8134  -1993    748   1231       C  
ATOM    715  CG AGLU A  80      76.317  89.773 -13.353  0.59 84.49           C  
ANISOU  715  CG AGLU A  80    10355  11475  10272  -1958    886   2011       C  
ATOM    716  CG BGLU A  80      76.119  89.670 -12.336  0.41 81.72           C  
ANISOU  716  CG BGLU A  80    10194  10871   9985  -2263    712   1720       C  
ATOM    717  CD AGLU A  80      75.868  91.065 -12.687  0.59 89.81           C  
ANISOU  717  CD AGLU A  80    11439  11584  11101  -2302    739   1940       C  
ATOM    718  CD BGLU A  80      76.213  90.414 -11.011  0.41 85.51           C  
ANISOU  718  CD BGLU A  80    11003  10807  10679  -2869    444   1632       C  
ATOM    719  OE1AGLU A  80      75.716  91.078 -11.445  0.59 89.66           O  
ANISOU  719  OE1AGLU A  80    11683  11213  11169  -2702    526   1643       O  
ATOM    720  OE1BGLU A  80      76.574  89.786  -9.994  0.41 77.62           O  
ANISOU  720  OE1BGLU A  80     9995   9751   9744  -3207    265   1467       O  
ATOM    721  OE2AGLU A  80      75.668  92.067 -13.409  0.59 93.74           O  
ANISOU  721  OE2AGLU A  80    12035  11970  11610  -2151    849   2187       O  
ATOM    722  OE2BGLU A  80      75.918  91.628 -10.987  0.41 90.05           O  
ANISOU  722  OE2BGLU A  80    11891  10990  11333  -2998    416   1726       O  
ATOM    723  N  AMET A  81      74.274  85.513 -13.069  0.59 63.98           N  
ANISOU  723  N  AMET A  81     7873   9620   6816  -1143    967    425       N  
ATOM    724  N  BMET A  81      74.031  85.566 -13.850  0.41 66.27           N  
ANISOU  724  N  BMET A  81     8137  10066   6978   -866   1082    490       N  
ATOM    725  CA AMET A  81      73.914  84.268 -12.409  0.59 64.17           C  
ANISOU  725  CA AMET A  81     8003   9708   6671  -1179    884    -44       C  
ATOM    726  CA BMET A  81      73.224  84.345 -13.813  0.41 70.18           C  
ANISOU  726  CA BMET A  81     8770  10739   7156   -676   1070    -17       C  
ATOM    727  C  AMET A  81      74.858  83.999 -11.237  0.59 58.74           C  
ANISOU  727  C  AMET A  81     7242   8864   6213  -1620    729     36       C  
ATOM    728  C  BMET A  81      73.341  83.534 -12.519  0.41 65.06           C  
ANISOU  728  C  BMET A  81     8209   9947   6564  -1018    897   -352       C  
ATOM    729  O  AMET A  81      76.053  84.247 -11.333  0.59 53.45           O  
ANISOU  729  O  AMET A  81     6317   8268   5721  -1743    756    549       O  
ATOM    730  O  BMET A  81      74.381  83.537 -11.857  0.41 63.56           O  
ANISOU  730  O  BMET A  81     7888   9662   6599  -1314    831   -108       O  
ATOM    731  CB AMET A  81      73.995  83.112 -13.408  0.59 68.52           C  
ANISOU  731  CB AMET A  81     8489  10673   6874   -729   1065    -50       C  
ATOM    732  CB BMET A  81      73.517  83.464 -15.033  0.41 77.08           C  
ANISOU  732  CB BMET A  81     9554  12025   7708   -213   1276    133       C  
ATOM    733  CG AMET A  81      73.511  83.455 -14.812  0.59 72.89           C  
ANISOU  733  CG AMET A  81     9034  11448   7211   -283   1243     91       C  
ATOM    734  CG BMET A  81      72.371  82.532 -15.404  0.41 85.75           C  
ANISOU  734  CG BMET A  81    10879  13301   8403     30   1264   -357       C  
ATOM    735  SD AMET A  81      71.725  83.303 -15.027  0.59 99.82           S  
ANISOU  735  SD AMET A  81    12708  14894  10323   -120   1170   -477       S  
ATOM    736  SD BMET A  81      72.463  81.894 -17.088  0.41 95.81           S  
ANISOU  736  SD BMET A  81    12178  14987   9240    609   1505   -162       S  
ATOM    737  CE AMET A  81      71.524  81.522 -15.046  0.59 77.75           C  
ANISOU  737  CE AMET A  81    10081  12335   7125      1   1155   -871       C  
ATOM    738  CE BMET A  81      70.874  81.070 -17.214  0.41 45.39           C  
ANISOU  738  CE BMET A  81     6129   8364   2754    584   1255   -711       C  
ATOM    739  N  AALA A  82      74.317  83.499 -10.131  0.59 58.10           N  
ANISOU  739  N  AALA A  82     7364   8592   6121  -1865    562   -440       N  
ATOM    740  N  BALA A  82      72.256  82.848 -12.168  0.41 63.98           N  
ANISOU  740  N  BALA A  82     8279   9817   6212   -991    816   -889       N  
ATOM    741  CA AALA A  82      75.141  83.069  -9.005  0.59 53.67           C  
ANISOU  741  CA AALA A  82     6749   7917   5727  -2258    407   -414       C  
ATOM    742  CA BALA A  82      72.181  82.093 -10.922  0.41 53.80           C  
ANISOU  742  CA BALA A  82     7110   8376   4953  -1305    652  -1261       C  
ATOM    743  C  AALA A  82      76.072  81.938  -9.439  0.59 49.72           C  
ANISOU  743  C  AALA A  82     6010   7793   5089  -2025    546   -178       C  
ATOM    744  C  BALA A  82      72.942  80.771 -11.024  0.41 49.29           C  
ANISOU  744  C  BALA A  82     6485   8034   4207  -1196    718  -1236       C  
ATOM    745  O  AALA A  82      75.656  81.040 -10.166  0.59 55.99           O  
ANISOU  745  O  AALA A  82     6871   8838   5564  -1614    700   -369       O  
ATOM    746  O  BALA A  82      72.728  79.986 -11.954  0.41 56.57           O  
ANISOU  746  O  BALA A  82     7469   9234   4792   -835    848  -1292       O  
ATOM    747  CB AALA A  82      74.254  82.603  -7.852  0.59 38.56           C  
ANISOU  747  CB AALA A  82     5121   5768   3764  -2477    238  -1014       C  
ATOM    748  CB BALA A  82      70.729  81.852 -10.531  0.41 55.28           C  
ANISOU  748  CB BALA A  82     7495   8471   5037  -1278    537  -1738       C  
ATOM    749  N  APHE A  83      77.320  81.983  -8.982  0.59 44.36           N  
ANISOU  749  N  APHE A  83     5079   7152   4623  -2286    490    254       N  
ATOM    750  N  BPHE A  83      73.827  80.547 -10.058  0.41 50.93           N  
ANISOU  750  N  BPHE A  83     6615   8114   4622  -1506    626  -1140       N  
ATOM    751  CA APHE A  83      78.302  80.929  -9.262  0.59 44.89           C  
ANISOU  751  CA APHE A  83     4902   7584   4570  -2045    642    545       C  
ATOM    752  CA BPHE A  83      74.702  79.379 -10.017  0.41 54.76           C  
ANISOU  752  CA BPHE A  83     7031   8795   4978  -1399    706  -1039       C  
ATOM    753  C  APHE A  83      78.536  80.732 -10.762  0.59 65.07           C  
ANISOU  753  C  APHE A  83     7318  10505   6902  -1468    952    875       C  
ATOM    754  C  BPHE A  83      75.495  79.257 -11.308  0.41 50.59           C  
ANISOU  754  C  BPHE A  83     6316   8593   4314   -963    964   -549       C  
ATOM    755  O  APHE A  83      78.644  79.603 -11.252  0.59 59.65           O  
ANISOU  755  O  APHE A  83     6681  10074   5910  -1052   1142    813       O  
ATOM    756  O  BPHE A  83      75.611  78.178 -11.881  0.41 50.26           O  
ANISOU  756  O  BPHE A  83     6384   8774   3939   -611   1120   -600       O  
ATOM    757  CB APHE A  83      77.899  79.604  -8.620  0.59 45.48           C  
ANISOU  757  CB APHE A  83     5196   7662   4422  -1987    610     37       C  
ATOM    758  CB BPHE A  83      73.923  78.094  -9.715  0.41 59.89           C  
ANISOU  758  CB BPHE A  83     7918   9331   5507  -1245    612  -1459       C  
ATOM    759  CG APHE A  83      77.797  79.660  -7.115  0.59 50.39           C  
ANISOU  759  CG APHE A  83     5941   7963   5244  -2524    326   -254       C  
ATOM    760  CG BPHE A  83      73.449  77.986  -8.289  0.41 60.50           C  
ANISOU  760  CG BPHE A  83     8021   8971   5997  -1464    386  -1577       C  
ATOM    761  CD1APHE A  83      78.932  79.796  -6.335  0.59 47.52           C  
ANISOU  761  CD1APHE A  83     5332   7597   5127  -2893    193    133       C  
ATOM    762  CD1BPHE A  83      73.265  79.119  -7.511  0.41 64.21           C  
ANISOU  762  CD1BPHE A  83     8483   9231   6681  -1773    298  -1585       C  
ATOM    763  CD2APHE A  83      76.567  79.560  -6.489  0.59 51.97           C  
ANISOU  763  CD2APHE A  83     6491   7891   5364  -2654    193   -885       C  
ATOM    764  CD2BPHE A  83      73.199  76.746  -7.723  0.41 67.39           C  
ANISOU  764  CD2BPHE A  83     8956   9625   7026  -1240    291  -1550       C  
ATOM    765  CE1APHE A  83      78.841  79.847  -4.947  0.59 44.29           C  
ANISOU  765  CE1APHE A  83     5130   6823   4876  -3185    -72   -128       C  
ATOM    766  CE1BPHE A  83      72.829  79.021  -6.202  0.41 64.67           C  
ANISOU  766  CE1BPHE A  83     8580   8934   7058  -1699    164  -1521       C  
ATOM    767  CE2APHE A  83      76.465  79.603  -5.106  0.59 50.39           C  
ANISOU  767  CE2APHE A  83     6455   7311   5379  -2730     20   -986       C  
ATOM    768  CE2BPHE A  83      72.763  76.643  -6.412  0.41 72.99           C  
ANISOU  768  CE2BPHE A  83     9636  10093   8005  -1355    214  -1539       C  
ATOM    769  CZ APHE A  83      77.598  79.744  -4.339  0.59 48.78           C  
ANISOU  769  CZ APHE A  83     6104   7042   5388  -2917   -114   -650       C  
ATOM    770  CZ BPHE A  83      72.582  77.785  -5.649  0.41 69.96           C  
ANISOU  770  CZ BPHE A  83     9242   9563   7778  -1537    171  -1515       C  
ATOM    771  N  ASER A  84      78.617  81.840 -11.482  0.59 66.45           N  
ANISOU  771  N  ASER A  84     7366  10675   7209  -1441   1007   1228       N  
ATOM    772  N  BSER A  84      76.027  80.394 -11.741  0.41 50.36           N  
ANISOU  772  N  BSER A  84     6046   8563   4527   -994   1013    -69       N  
ATOM    773  CA ASER A  84      78.720  81.802 -12.929  0.59 71.20           C  
ANISOU  773  CA ASER A  84     7868  11587   7596   -899   1295   1523       C  
ATOM    774  CA BSER A  84      76.791  80.518 -12.972  0.41 62.39           C  
ANISOU  774  CA BSER A  84     7348  10389   5967   -596   1267    471       C  
ATOM    775  C  ASER A  84      79.096  83.181 -13.435  0.59 72.37           C  
ANISOU  775  C  ASER A  84     7811  11692   7997  -1023   1308   2029       C  
ATOM    776  C  BSER A  84      77.561  81.832 -12.896  0.41 66.91           C  
ANISOU  776  C  BSER A  84     7625  10870   6928   -877   1221   1014       C  
ATOM    777  O  ASER A  84      78.828  84.186 -12.778  0.59 62.88           O  
ANISOU  777  O  ASER A  84     6700  10139   7051  -1471   1092   1966       O  
ATOM    778  O  BSER A  84      77.626  82.452 -11.836  0.41 69.68           O  
ANISOU  778  O  BSER A  84     7983  10921   7571  -1380    990    965       O  
ATOM    779  CB ASER A  84      77.386  81.364 -13.540  0.59 65.70           C  
ANISOU  779  CB ASER A  84     7528  10884   6550   -552   1358    969       C  
ATOM    780  CB BSER A  84      75.845  80.530 -14.173  0.41 63.53           C  
ANISOU  780  CB BSER A  84     7679  10665   5796   -178   1399    297       C  
ATOM    781  OG ASER A  84      77.412  81.469 -14.952  0.59 67.80           O  
ANISOU  781  OG ASER A  84     7746  11414   6603    -59   1609   1244       O  
ATOM    782  OG BSER A  84      76.544  80.731 -15.386  0.41 60.42           O  
ANISOU  782  OG BSER A  84     7098  10544   5314    222   1654    821       O  
ATOM    783  N  AASP A  85      79.723  83.227 -14.605  0.59 82.62           N  
ANISOU  783  N  AASP A  85     8869  13325   9198   -616   1573   2540       N  
ATOM    784  N  BASP A  85      78.147  82.257 -14.010  0.41 70.77           N  
ANISOU  784  N  BASP A  85     7889  11599   7399   -571   1435   1540       N  
ATOM    785  CA AASP A  85      80.081  84.496 -15.222  0.59 89.25           C  
ANISOU  785  CA AASP A  85     9514  14152  10246   -692   1615   3052       C  
ATOM    786  CA BASP A  85      78.803  83.559 -14.071  0.41 75.72           C  
ANISOU  786  CA BASP A  85     8264  12141   8366   -846   1391   2077       C  
ATOM    787  C  AASP A  85      79.014  84.907 -16.232  0.59 87.94           C  
ANISOU  787  C  AASP A  85     9587  13951   9873   -319   1734   2813       C  
ATOM    788  C  BASP A  85      78.450  84.277 -15.370  0.41 80.91           C  
ANISOU  788  C  BASP A  85     8918  12900   8923   -483   1577   2284       C  
ATOM    789  O  AASP A  85      78.985  86.051 -16.689  0.59 91.31           O  
ANISOU  789  O  AASP A  85     9968  14274  10452   -386   1746   3096       O  
ATOM    790  O  BASP A  85      78.951  85.365 -15.653  0.41 87.56           O  
ANISOU  790  O  BASP A  85     9577  13693   9999   -638   1583   2762       O  
ATOM    791  CB AASP A  85      81.454  84.400 -15.897  0.59100.06           C  
ANISOU  791  CB AASP A  85    10425  15942  11653   -480   1842   3838       C  
ATOM    792  CB BASP A  85      80.320  83.424 -13.912  0.41 83.45           C  
ANISOU  792  CB BASP A  85     8820  13366   9522   -965   1444   2734       C  
ATOM    793  CG AASP A  85      81.869  85.696 -16.566  0.59105.76           C  
ANISOU  793  CG AASP A  85    10968  16613  12603   -560   1840   4333       C  
ATOM    794  CG BASP A  85      80.885  82.234 -14.665  0.41 89.29           C  
ANISOU  794  CG BASP A  85     9432  14539   9954   -391   1748   2936       C  
ATOM    795  OD1AASP A  85      82.192  86.662 -15.844  0.59108.30           O  
ANISOU  795  OD1AASP A  85    11234  16662  13252  -1144   1586   4515       O  
ATOM    796  OD1BASP A  85      80.314  81.863 -15.711  0.41 93.49           O  
ANISOU  796  OD1BASP A  85    10155  15210  10157    128   1961   2774       O  
ATOM    797  OD2AASP A  85      81.870  85.749 -17.814  0.59108.61           O  
ANISOU  797  OD2AASP A  85    11304  17155  12809    -41   2052   4486       O  
ATOM    798  OD2BASP A  85      81.902  81.667 -14.206  0.41 91.82           O  
ANISOU  798  OD2BASP A  85     9488  15062  10339   -448   1777   3270       O  
ATOM    799  N  ALEU A  86      78.135  83.963 -16.566  0.59 81.02           N  
ANISOU  799  N  ALEU A  86     8981  13165   8638     49   1808   2304       N  
ATOM    800  N  BLEU A  86      77.576  83.651 -16.151  0.41 75.15           N  
ANISOU  800  N  BLEU A  86     8413  12310   7829    -24   1711   1928       N  
ATOM    801  CA ALEU A  86      77.077  84.194 -17.547  0.59 75.19           C  
ANISOU  801  CA ALEU A  86     8458  12462   7648    413   1903   2070       C  
ATOM    802  CA BLEU A  86      77.104  84.212 -17.415  0.41 74.33           C  
ANISOU  802  CA BLEU A  86     8346  12327   7570    360   1880   2061       C  
ATOM    803  C  ALEU A  86      76.241  85.409 -17.187  0.59 69.12           C  
ANISOU  803  C  ALEU A  86     7829  11346   7087    123   1729   1893       C  
ATOM    804  C  BLEU A  86      76.287  85.464 -17.125  0.41 68.10           C  
ANISOU  804  C  BLEU A  86     7690  11198   6984     89   1719   1910       C  
ATOM    805  O  ALEU A  86      75.611  85.459 -16.129  0.59 63.03           O  
ANISOU  805  O  ALEU A  86     7249  10283   6414   -217   1512   1462       O  
ATOM    806  O  BLEU A  86      75.693  85.585 -16.051  0.41 63.52           O  
ANISOU  806  O  BLEU A  86     7297  10313   6523   -269   1498   1504       O  
ATOM    807  CB ALEU A  86      76.164  82.971 -17.668  0.59 78.25           C  
ANISOU  807  CB ALEU A  86     9161  12945   7627    678   1906   1484       C  
ATOM    808  CB BLEU A  86      76.230  83.192 -18.154  0.41 78.36           C  
ANISOU  808  CB BLEU A  86     9133  13033   7609    818   1986   1639       C  
ATOM    809  CG ALEU A  86      76.568  81.834 -18.611  0.59 84.24           C  
ANISOU  809  CG ALEU A  86     9982  14029   7997   1196   2147   1587       C  
ATOM    810  CG BLEU A  86      76.815  81.987 -18.910  0.41 85.57           C  
ANISOU  810  CG BLEU A  86    10082  14230   8200   1276   2196   1754       C  
ATOM    811  CD1ALEU A  86      76.851  82.370 -20.008  0.59 87.07           C  
ANISOU  811  CD1ALEU A  86    10246  14474   8363   1574   2285   1973       C  
ATOM    812  CD1BLEU A  86      77.028  82.321 -20.380  0.41 88.77           C  
ANISOU  812  CD1BLEU A  86    10447  14715   8567   1699   2320   2065       C  
ATOM    813  CD2ALEU A  86      77.758  81.045 -18.070  0.59 89.63           C  
ANISOU  813  CD2ALEU A  86    10510  14759   8787   1152   2179   1812       C  
ATOM    814  CD2BLEU A  86      78.108  81.447 -18.290  0.41 91.34           C  
ANISOU  814  CD2BLEU A  86    10581  15024   9100   1172   2232   2077       C  
ATOM    815  N   ILE A  87      76.248  86.400 -18.065  1.00 61.60           N  
ANISOU  815  N   ILE A  87     6802  10416   6186    285   1846   2245       N  
ATOM    816  CA  ILE A  87      75.415  87.573 -17.860  1.00 66.79           C  
ANISOU  816  CA  ILE A  87     7645  10746   6986    113   1734   2107       C  
ATOM    817  C   ILE A  87      74.267  87.647 -18.869  1.00 68.03           C  
ANISOU  817  C   ILE A  87     7957  11051   6842    570   1846   1885       C  
ATOM    818  O   ILE A  87      74.481  87.536 -20.066  1.00 79.45           O  
ANISOU  818  O   ILE A  87     9297  12796   8093    981   2051   2162       O  
ATOM    819  CB  ILE A  87      76.255  88.875 -17.751  1.00 87.09           C  
ANISOU  819  CB  ILE A  87    10084  13094   9912   -216   1706   2662       C  
ATOM    820  CG1 ILE A  87      75.387  90.114 -17.983  1.00 84.75           C  
ANISOU  820  CG1 ILE A  87    10029  12509   9663   -191   1696   2607       C  
ATOM    821  CG2 ILE A  87      77.442  88.835 -18.689  1.00 97.34           C  
ANISOU  821  CG2 ILE A  87    11020  14741  11222     -9   1918   3321       C  
ATOM    822  CD1 ILE A  87      75.927  91.359 -17.301  1.00 83.78           C  
ANISOU  822  CD1 ILE A  87     9995  11953   9885   -709   1552   2920       C  
ATOM    823  N   ILE A  88      73.040  87.778 -18.368  1.00 55.95           N  
ANISOU  823  N   ILE A  88     6670   9341   5248    507   1710   1395       N  
ATOM    824  CA  ILE A  88      71.886  87.974 -19.239  1.00 63.18           C  
ANISOU  824  CA  ILE A  88     7697  10414   5896    891   1782   1225       C  
ATOM    825  C   ILE A  88      71.597  89.460 -19.337  1.00 66.17           C  
ANISOU  825  C   ILE A  88     8144  10525   6474    864   1808   1451       C  
ATOM    826  O   ILE A  88      71.590  90.148 -18.326  1.00 58.15           O  
ANISOU  826  O   ILE A  88     7267   9111   5717    502   1683   1395       O  
ATOM    827  CB  ILE A  88      70.639  87.258 -18.713  1.00 66.36           C  
ANISOU  827  CB  ILE A  88     8283  10850   6080    877   1635    620       C  
ATOM    828  CG1 ILE A  88      70.906  85.756 -18.596  1.00 67.06           C  
ANISOU  828  CG1 ILE A  88     8384  11156   5941    883   1602    378       C  
ATOM    829  CG2 ILE A  88      69.452  87.523 -19.635  1.00 53.81           C  
ANISOU  829  CG2 ILE A  88     6753   9480   4213   1248   1688    520       C  
ATOM    830  CD1 ILE A  88      69.721  84.968 -18.106  1.00 68.52           C  
ANISOU  830  CD1 ILE A  88     8746  11398   5891    822   1442   -191       C  
ATOM    831  N   GLU A  89      71.368  89.953 -20.551  1.00 62.54           N  
ANISOU  831  N   GLU A  89     7632  10259   5870   1254   1975   1709       N  
ATOM    832  CA  GLU A  89      71.161  91.383 -20.761  1.00 64.62           C  
ANISOU  832  CA  GLU A  89     7985  10268   6299   1279   2035   1977       C  
ATOM    833  C   GLU A  89      69.976  91.668 -21.686  1.00 68.38           C  
ANISOU  833  C   GLU A  89     8523  10960   6497   1738   2128   1881       C  
ATOM    834  O   GLU A  89      69.819  91.044 -22.739  1.00 71.82           O  
ANISOU  834  O   GLU A  89     8853  11802   6633   2098   2223   1910       O  
ATOM    835  CB  GLU A  89      72.440  92.040 -21.307  1.00 66.02           C  
ANISOU  835  CB  GLU A  89     7989  10414   6682   1220   2162   2604       C  
ATOM    836  CG  GLU A  89      72.477  93.557 -21.134  1.00 95.91           C  
ANISOU  836  CG  GLU A  89    11947  13779  10716   1043   2166   2890       C  
ATOM    837  CD  GLU A  89      73.806  94.176 -21.553  1.00 96.37           C  
ANISOU  837  CD  GLU A  89    11817  13803  10996    871   2249   3539       C  
ATOM    838  OE1 GLU A  89      73.875  95.421 -21.655  1.00 88.91           O  
ANISOU  838  OE1 GLU A  89    11034  12543  10206    765   2277   3834       O  
ATOM    839  OE2 GLU A  89      74.783  93.424 -21.773  1.00 96.18           O  
ANISOU  839  OE2 GLU A  89    11493  14071  10980    846   2295   3778       O  
ATOM    840  N   TRP A  90      69.145  92.620 -21.282  1.00 65.09           N  
ANISOU  840  N   TRP A  90     8304  10270   6158   1735   2103   1787       N  
ATOM    841  CA  TRP A  90      67.991  93.020 -22.068  1.00 73.02           C  
ANISOU  841  CA  TRP A  90     9342  11481   6920   2169   2191   1748       C  
ATOM    842  C   TRP A  90      68.323  94.316 -22.792  1.00 83.31           C  
ANISOU  842  C   TRP A  90    10690  12622   8342   2344   2364   2235       C  
ATOM    843  O   TRP A  90      68.463  95.364 -22.158  1.00 86.71           O  
ANISOU  843  O   TRP A  90    11343  12585   9017   2138   2364   2362       O  
ATOM    844  CB  TRP A  90      66.782  93.237 -21.156  1.00 75.29           C  
ANISOU  844  CB  TRP A  90     9816  11606   7185   2133   2093   1365       C  
ATOM    845  CG  TRP A  90      66.194  91.981 -20.570  1.00 72.94           C  
ANISOU  845  CG  TRP A  90     9467  11534   6714   2014   1927    882       C  
ATOM    846  CD1 TRP A  90      65.059  91.345 -20.977  1.00 72.01           C  
ANISOU  846  CD1 TRP A  90     9263  11833   6263   2256   1876    627       C  
ATOM    847  CD2 TRP A  90      66.704  91.220 -19.468  1.00 72.23           C  
ANISOU  847  CD2 TRP A  90     9414  11269   6762   1595   1776    617       C  
ATOM    848  NE1 TRP A  90      64.829  90.236 -20.199  1.00 61.87           N  
ANISOU  848  NE1 TRP A  90     7980  10627   4903   2000   1705    218       N  
ATOM    849  CE2 TRP A  90      65.828  90.133 -19.267  1.00 64.19           C  
ANISOU  849  CE2 TRP A  90     8352  10556   5483   1617   1653    195       C  
ATOM    850  CE3 TRP A  90      67.820  91.347 -18.631  1.00 75.27           C  
ANISOU  850  CE3 TRP A  90     9860  11283   7455   1182   1717    717       C  
ATOM    851  CZ2 TRP A  90      66.029  89.182 -18.269  1.00 62.30           C  
ANISOU  851  CZ2 TRP A  90     8147  10238   5284   1274   1499   -143       C  
ATOM    852  CZ3 TRP A  90      68.020  90.401 -17.639  1.00 72.17           C  
ANISOU  852  CZ3 TRP A  90     9481  10839   7103    854   1559    388       C  
ATOM    853  CH2 TRP A  90      67.129  89.332 -17.467  1.00 62.97           C  
ANISOU  853  CH2 TRP A  90     8292   9958   5677    918   1464    -45       C  
ATOM    854  N   PHE A  91      68.450  94.258 -24.115  1.00 70.36           N  
ANISOU  854  N   PHE A  91     8887  11338   6507   2716   2511   2510       N  
ATOM    855  CA  PHE A  91      68.772  95.467 -24.861  1.00 82.85           C  
ANISOU  855  CA  PHE A  91    10505  12785   8189   2895   2686   2992       C  
ATOM    856  C   PHE A  91      67.692  95.858 -25.862  1.00 87.92           C  
ANISOU  856  C   PHE A  91    11154  13705   8549   3413   2800   3026       C  
ATOM    857  O   PHE A  91      67.312  95.069 -26.727  1.00 74.91           O  
ANISOU  857  O   PHE A  91     9355  12530   6578   3712   2813   2941       O  
ATOM    858  CB  PHE A  91      70.128  95.353 -25.556  1.00 87.91           C  
ANISOU  858  CB  PHE A  91    10940  13545   8918   2860   2801   3452       C  
ATOM    859  CG  PHE A  91      70.687  96.677 -25.989  1.00100.01           C  
ANISOU  859  CG  PHE A  91    12532  14815  10653   2857   2941   3979       C  
ATOM    860  CD1 PHE A  91      71.173  97.575 -25.051  1.00102.45           C  
ANISOU  860  CD1 PHE A  91    13046  14589  11293   2402   2860   4119       C  
ATOM    861  CD2 PHE A  91      70.714  97.033 -27.328  1.00104.54           C  
ANISOU  861  CD2 PHE A  91    13002  15657  11063   3286   3143   4336       C  
ATOM    862  CE1 PHE A  91      71.685  98.800 -25.443  1.00107.12           C  
ANISOU  862  CE1 PHE A  91    13747  14906  12049   2350   2970   4612       C  
ATOM    863  CE2 PHE A  91      71.224  98.256 -27.724  1.00109.34           C  
ANISOU  863  CE2 PHE A  91    13679  16012  11852   3268   3272   4833       C  
ATOM    864  CZ  PHE A  91      71.709  99.140 -26.780  1.00109.73           C  
ANISOU  864  CZ  PHE A  91    13945  15516  12232   2786   3182   4973       C  
ATOM    865  N   LYS A  92      67.205  97.088 -25.725  1.00 77.70           N  
ANISOU  865  N   LYS A  92    10070  12098   7354   3515   2878   3163       N  
ATOM    866  CA  LYS A  92      66.180  97.614 -26.603  1.00 79.68           C  
ANISOU  866  CA  LYS A  92    10327  12588   7360   4021   3000   3253       C  
ATOM    867  C   LYS A  92      66.843  98.353 -27.751  1.00 88.85           C  
ANISOU  867  C   LYS A  92    11444  13776   8539   4250   3198   3777       C  
ATOM    868  O   LYS A  92      67.634  99.274 -27.545  1.00 93.01           O  
ANISOU  868  O   LYS A  92    12125  13875   9340   4041   3271   4106       O  
ATOM    869  CB  LYS A  92      65.241  98.548 -25.838  1.00 93.71           C  
ANISOU  869  CB  LYS A  92    12387  14020   9199   4092   3021   3141       C  
ATOM    870  CG  LYS A  92      64.019  98.977 -26.631  1.00 97.86           C  
ANISOU  870  CG  LYS A  92    12870  14872   9441   4649   3136   3210       C  
ATOM    871  CD  LYS A  92      63.003  99.687 -25.753  1.00100.68           C  
ANISOU  871  CD  LYS A  92    13486  14954   9815   4769   3171   3062       C  
ATOM    872  CE  LYS A  92      61.784 100.102 -26.560  1.00106.57           C  
ANISOU  872  CE  LYS A  92    14129  16095  10266   5359   3296   3191       C  
ATOM    873  NZ  LYS A  92      60.819 100.898 -25.752  1.00108.49           N  
ANISOU  873  NZ  LYS A  92    14638  16073  10511   5572   3395   3129       N  
ATOM    874  N   VAL A  93      66.523  97.932 -28.965  1.00 89.39           N  
ANISOU  874  N   VAL A  93    15438   9615   8911   3287   2490   -179       N  
ATOM    875  CA  VAL A  93      67.131  98.509 -30.146  1.00 88.70           C  
ANISOU  875  CA  VAL A  93    15882   9099   8721   3299   2491    116       C  
ATOM    876  C   VAL A  93      66.599  99.921 -30.363  1.00 94.74           C  
ANISOU  876  C   VAL A  93    17168   9159   9672   3698   2650    144       C  
ATOM    877  O   VAL A  93      65.398 100.117 -30.543  1.00 93.82           O  
ANISOU  877  O   VAL A  93    16936   8943   9770   4302   2481    207       O  
ATOM    878  CB  VAL A  93      66.841  97.638 -31.371  1.00 88.46           C  
ANISOU  878  CB  VAL A  93    15732   9321   8557   3552   2120    456       C  
ATOM    879  CG1 VAL A  93      67.726  98.048 -32.538  1.00 90.75           C  
ANISOU  879  CG1 VAL A  93    16596   9264   8622   3399   2196    749       C  
ATOM    880  CG2 VAL A  93      67.050  96.169 -31.019  1.00 77.46           C  
ANISOU  880  CG2 VAL A  93    13752   8589   7090   3280   1967    383       C  
ATOM    881  N   GLU A  94      67.503 100.897 -30.336  1.00102.05           N  
ANISOU  881  N   GLU A  94    18638   9575  10562   3354   2976     99       N  
ATOM    882  CA  GLU A  94      67.143 102.306 -30.486  1.00110.68           C  
ANISOU  882  CA  GLU A  94    20316   9878  11859   3671   3198    119       C  
ATOM    883  C   GLU A  94      66.759 102.658 -31.922  1.00118.36           C  
ANISOU  883  C   GLU A  94    21710  10474  12786   4166   2963    629       C  
ATOM    884  O   GLU A  94      66.511 101.775 -32.740  1.00123.46           O  
ANISOU  884  O   GLU A  94    22131  11531  13246   4340   2587    908       O  
ATOM    885  CB  GLU A  94      68.304 103.192 -30.029  1.00120.34           C  
ANISOU  885  CB  GLU A  94    22013  10660  13050   3049   3629    -98       C  
ATOM    886  CG  GLU A  94      68.663 103.025 -28.567  1.00127.69           C  
ANISOU  886  CG  GLU A  94    22636  11909  13970   2547   3822   -613       C  
ATOM    887  CD  GLU A  94      67.516 103.398 -27.650  1.00138.00           C  
ANISOU  887  CD  GLU A  94    23819  13111  15506   2956   3950   -950       C  
ATOM    888  OE1 GLU A  94      66.860 104.429 -27.910  1.00147.04           O  
ANISOU  888  OE1 GLU A  94    25369  13577  16921   3438   4114   -921       O  
ATOM    889  OE2 GLU A  94      67.263 102.656 -26.676  1.00137.49           O  
ANISOU  889  OE2 GLU A  94    23258  13621  15362   2809   3913  -1230       O  
ATOM    890  N   LYS A  95      66.714 103.953 -32.222  1.00119.31           N  
ANISOU  890  N   LYS A  95    22489   9789  13054   4372   3180    753       N  
ATOM    891  CA  LYS A  95      66.398 104.418 -33.567  1.00123.10           C  
ANISOU  891  CA  LYS A  95    23496   9835  13442   4828   2954   1297       C  
ATOM    892  C   LYS A  95      67.664 104.552 -34.403  1.00122.79           C  
ANISOU  892  C   LYS A  95    24014   9600  13039   4279   3151   1558       C  
ATOM    893  O   LYS A  95      68.553 105.333 -34.074  1.00129.21           O  
ANISOU  893  O   LYS A  95    25243   9948  13902   3791   3604   1410       O  
ATOM    894  CB  LYS A  95      65.684 105.771 -33.519  1.00134.86           C  
ANISOU  894  CB  LYS A  95    25462  10468  15309   5385   3096   1371       C  
ATOM    895  CG  LYS A  95      64.410 105.791 -32.692  1.00137.17           C  
ANISOU  895  CG  LYS A  95    25208  10858  16051   5972   3014   1085       C  
ATOM    896  CD  LYS A  95      63.678 107.122 -32.830  1.00144.63           C  
ANISOU  896  CD  LYS A  95    26585  10938  17430   6598   3119   1223       C  
ATOM    897  CE  LYS A  95      64.516 108.282 -32.309  1.00145.75           C  
ANISOU  897  CE  LYS A  95    27346  10368  17665   6106   3711    967       C  
ATOM    898  NZ  LYS A  95      63.778 109.572 -32.367  1.00151.48           N  
ANISOU  898  NZ  LYS A  95    28234  10471  18852   6540   3765   1042       N  
ATOM    899  N   GLY A  96      67.744 103.789 -35.486  1.00119.81           N  
ANISOU  899  N   GLY A  96    23647   9577  12299   4324   2842   1917       N  
ATOM    900  CA  GLY A  96      68.868 103.899 -36.395  1.00124.82           C  
ANISOU  900  CA  GLY A  96    24830  10026  12570   3847   3082   2185       C  
ATOM    901  C   GLY A  96      70.046 102.996 -36.076  1.00125.20           C  
ANISOU  901  C   GLY A  96    24464  10622  12486   3119   3310   1922       C  
ATOM    902  O   GLY A  96      71.180 103.300 -36.449  1.00131.83           O  
ANISOU  902  O   GLY A  96    25671  11231  13188   2580   3701   1991       O  
ATOM    903  N   ALA A  97      69.790 101.890 -35.386  1.00114.81           N  
ANISOU  903  N   ALA A  97    22364  10011  11247   3103   3082   1638       N  
ATOM    904  CA  ALA A  97      70.826 100.889 -35.167  1.00104.21           C  
ANISOU  904  CA  ALA A  97    20573   9214   9807   2522   3209   1459       C  
ATOM    905  C   ALA A  97      70.990 100.074 -36.441  1.00107.27           C  
ANISOU  905  C   ALA A  97    21067   9863   9829   2564   3062   1766       C  
ATOM    906  O   ALA A  97      70.026  99.878 -37.181  1.00112.07           O  
ANISOU  906  O   ALA A  97    21808  10515  10260   3079   2675   2012       O  
ATOM    907  CB  ALA A  97      70.466  99.994 -34.007  1.00 94.51           C  
ANISOU  907  CB  ALA A  97    18555   8587   8769   2510   3014   1107       C  
ATOM    908  N   LYS A  98      72.206  99.597 -36.695  1.00109.55           N  
ANISOU  908  N   LYS A  98    21280  10332  10011   2017   3369   1728       N  
ATOM    909  CA  LYS A  98      72.516  98.927 -37.958  1.00115.17           C  
ANISOU  909  CA  LYS A  98    22210  11207  10343   1983   3379   1975       C  
ATOM    910  C   LYS A  98      71.814  97.579 -38.095  1.00108.50           C  
ANISOU  910  C   LYS A  98    20851  10968   9406   2270   2940   1918       C  
ATOM    911  O   LYS A  98      71.749  97.011 -39.188  1.00108.26           O  
ANISOU  911  O   LYS A  98    21057  11069   9007   2352   2844   2099       O  
ATOM    912  CB  LYS A  98      74.027  98.740 -38.124  1.00120.14           C  
ANISOU  912  CB  LYS A  98    22792  11872  10983   1326   3905   1897       C  
ATOM    913  CG  LYS A  98      74.830 100.029 -38.143  1.00130.55           C  
ANISOU  913  CG  LYS A  98    24643  12580  12381    930   4394   1959       C  
ATOM    914  CD  LYS A  98      76.227  99.791 -38.704  1.00135.92           C  
ANISOU  914  CD  LYS A  98    25333  13298  13013    333   4932   1966       C  
ATOM    915  CE  LYS A  98      76.946  98.672 -37.961  1.00132.83           C  
ANISOU  915  CE  LYS A  98    24018  13519  12931     29   4936   1647       C  
ATOM    916  NZ  LYS A  98      78.256  98.340 -38.590  1.00134.40           N  
ANISOU  916  NZ  LYS A  98    24130  13783  13153   -472   5471   1652       N  
ATOM    917  N   SER A  99      71.293  97.072 -36.983  1.00 96.02           N  
ANISOU  917  N   SER A  99    18609   9742   8134   2382   2701   1651       N  
ATOM    918  CA  SER A  99      70.640  95.771 -36.978  1.00 91.18           C  
ANISOU  918  CA  SER A  99    17465   9678   7503   2589   2323   1569       C  
ATOM    919  C   SER A  99      69.205  95.871 -37.475  1.00 90.59           C  
ANISOU  919  C   SER A  99    17517   9588   7314   3183   1831   1736       C  
ATOM    920  O   SER A  99      68.654  94.900 -37.996  1.00 83.22           O  
ANISOU  920  O   SER A  99    16377   9016   6227   3346   1497   1756       O  
ATOM    921  CB  SER A  99      70.672  95.160 -35.573  1.00 77.60           C  
ANISOU  921  CB  SER A  99    15011   8340   6133   2430   2289   1255       C  
ATOM    922  OG  SER A  99      70.119  96.049 -34.620  1.00 78.86           O  
ANISOU  922  OG  SER A  99    15159   8290   6515   2577   2281   1128       O  
ATOM    923  N   ILE A 100      68.615  97.051 -37.315  1.00 88.42           N  
ANISOU  923  N   ILE A 100    17567   8875   7153   3500   1786   1845       N  
ATOM    924  CA  ILE A 100      67.206  97.268 -37.627  1.00 91.48           C  
ANISOU  924  CA  ILE A 100    17958   9230   7570   4126   1294   2003       C  
ATOM    925  C   ILE A 100      66.854  96.818 -39.035  1.00 94.10           C  
ANISOU  925  C   ILE A 100    18629   9680   7446   4318    920   2304       C  
ATOM    926  O   ILE A 100      67.340  97.377 -40.014  1.00 98.22           O  
ANISOU  926  O   ILE A 100    19877   9852   7589   4248   1047   2603       O  
ATOM    927  CB  ILE A 100      66.801  98.748 -37.448  1.00105.82           C  
ANISOU  927  CB  ILE A 100    20218  10406   9583   4461   1376   2142       C  
ATOM    928  CG1 ILE A 100      66.916  99.157 -35.975  1.00 95.10           C  
ANISOU  928  CG1 ILE A 100    18507   8969   8659   4308   1697   1762       C  
ATOM    929  CG2 ILE A 100      65.386  98.977 -37.959  1.00101.46           C  
ANISOU  929  CG2 ILE A 100    19661   9805   9085   5168    820   2383       C  
ATOM    930  CD1 ILE A 100      66.516 100.593 -35.697  1.00100.90           C  
ANISOU  930  CD1 ILE A 100    19668   9018   9652   4629   1853   1813       C  
ATOM    931  N   GLY A 101      66.017  95.790 -39.123  1.00 92.22           N  
ANISOU  931  N   GLY A 101    17885   9938   7215   4511    472   2212       N  
ATOM    932  CA  GLY A 101      65.607  95.243 -40.401  1.00 95.00           C  
ANISOU  932  CA  GLY A 101    18512  10481   7105   4647     46   2424       C  
ATOM    933  C   GLY A 101      66.436  94.048 -40.838  1.00 98.07           C  
ANISOU  933  C   GLY A 101    18852  11211   7200   4177    242   2263       C  
ATOM    934  O   GLY A 101      66.131  93.415 -41.849  1.00101.45           O  
ANISOU  934  O   GLY A 101    19413  11853   7280   4168    -71   2304       O  
ATOM    935  N   ARG A 102      67.489  93.740 -40.087  1.00 86.88           N  
ANISOU  935  N   ARG A 102    17167   9839   6006   3744    757   2028       N  
ATOM    936  CA  ARG A 102      68.342  92.604 -40.420  1.00 84.02           C  
ANISOU  936  CA  ARG A 102    16687   9750   5485   3338   1005   1865       C  
ATOM    937  C   ARG A 102      68.104  91.404 -39.510  1.00 78.70           C  
ANISOU  937  C   ARG A 102    15197   9520   5185   3257    898   1560       C  
ATOM    938  O   ARG A 102      67.564  91.543 -38.401  1.00 76.54           O  
ANISOU  938  O   ARG A 102    14438   9335   5307   3391    789   1446       O  
ATOM    939  CB  ARG A 102      69.819  93.015 -40.467  1.00 93.19           C  
ANISOU  939  CB  ARG A 102    18150  10645   6612   2895   1657   1875       C  
ATOM    940  CG  ARG A 102      70.231  93.547 -41.851  1.00 97.59           C  
ANISOU  940  CG  ARG A 102    19387  10903   6790   2762   1794   2069       C  
ATOM    941  CD  ARG A 102      71.553  94.298 -41.844  1.00101.48           C  
ANISOU  941  CD  ARG A 102    20139  11044   7375   2344   2424   2092       C  
ATOM    942  NE  ARG A 102      72.681  93.457 -41.460  1.00 94.17           N  
ANISOU  942  NE  ARG A 102    18756  10341   6684   1929   2856   1849       N  
ATOM    943  CZ  ARG A 102      73.398  92.722 -42.304  1.00 92.17           C  
ANISOU  943  CZ  ARG A 102    18482  10197   6342   1655   3102   1740       C  
ATOM    944  NH1 ARG A 102      73.108  92.704 -43.600  1.00 97.72           N  
ANISOU  944  NH1 ARG A 102    19646  10836   6649   1698   2968   1833       N  
ATOM    945  NH2 ARG A 102      74.407  91.995 -41.844  1.00 91.80           N  
ANISOU  945  NH2 ARG A 102    17949  10326   6604   1349   3486   1538       N  
ATOM    946  N   THR A 103      68.491  90.223 -39.986  1.00 77.25           N  
ANISOU  946  N   THR A 103    14905   9581   4863   3034    963   1428       N  
ATOM    947  CA  THR A 103      68.175  88.985 -39.276  1.00 73.16           C  
ANISOU  947  CA  THR A 103    13692   9437   4669   2973    824   1186       C  
ATOM    948  C   THR A 103      69.318  88.494 -38.394  1.00 69.23           C  
ANISOU  948  C   THR A 103    12795   8997   4514   2627   1264   1044       C  
ATOM    949  O   THR A 103      70.456  88.933 -38.527  1.00 69.86           O  
ANISOU  949  O   THR A 103    13104   8875   4565   2384   1694   1090       O  
ATOM    950  CB  THR A 103      67.796  87.863 -40.254  1.00 76.44           C  
ANISOU  950  CB  THR A 103    14183  10064   4796   2952    586   1090       C  
ATOM    951  OG1 THR A 103      68.981  87.336 -40.856  1.00 75.53           O  
ANISOU  951  OG1 THR A 103    14318   9872   4509   2631   1054   1016       O  
ATOM    952  CG2 THR A 103      66.877  88.390 -41.340  1.00 79.78           C  
ANISOU  952  CG2 THR A 103    15117  10437   4759   3236    122   1274       C  
ATOM    953  N   LEU A 104      69.002  87.574 -37.491  1.00 65.84           N  
ANISOU  953  N   LEU A 104    11748   8847   4422   2597   1139    891       N  
ATOM    954  CA  LEU A 104      70.009  86.966 -36.629  1.00 62.77           C  
ANISOU  954  CA  LEU A 104    10938   8550   4363   2308   1445    805       C  
ATOM    955  C   LEU A 104      71.089  86.242 -37.435  1.00 63.55           C  
ANISOU  955  C   LEU A 104    11163   8588   4394   2087   1790    764       C  
ATOM    956  O   LEU A 104      72.265  86.271 -37.078  1.00 63.04           O  
ANISOU  956  O   LEU A 104    10942   8466   4544   1851   2150    767       O  
ATOM    957  CB  LEU A 104      69.338  86.017 -35.646  1.00 59.98           C  
ANISOU  957  CB  LEU A 104     9991   8486   4312   2336   1213    703       C  
ATOM    958  CG  LEU A 104      68.566  86.746 -34.528  1.00 59.29           C  
ANISOU  958  CG  LEU A 104     9686   8466   4375   2469   1056    698       C  
ATOM    959  CD1 LEU A 104      68.213  85.782 -33.399  1.00 56.80           C  
ANISOU  959  CD1 LEU A 104     8804   8434   4344   2381    969    620       C  
ATOM    960  CD2 LEU A 104      69.353  87.941 -33.981  1.00 59.73           C  
ANISOU  960  CD2 LEU A 104     9927   8319   4447   2341   1319    740       C  
ATOM    961  N   GLY A 105      70.694  85.626 -38.543  1.00 65.55           N  
ANISOU  961  N   GLY A 105    11698   8853   4353   2155   1690    706       N  
ATOM    962  CA  GLY A 105      71.647  84.919 -39.379  1.00 67.16           C  
ANISOU  962  CA  GLY A 105    12074   8972   4470   1961   2086    611       C  
ATOM    963  C   GLY A 105      72.570  85.887 -40.103  1.00 70.26           C  
ANISOU  963  C   GLY A 105    12992   9108   4596   1821   2513    722       C  
ATOM    964  O   GLY A 105      73.770  85.646 -40.219  1.00 72.24           O  
ANISOU  964  O   GLY A 105    13154   9272   5022   1594   3014    669       O  
ATOM    965  N   GLU A 106      72.004  86.987 -40.593  1.00 77.30           N  
ANISOU  965  N   GLU A 106    14414   9858   5099   1962   2330    892       N  
ATOM    966  CA  GLU A 106      72.779  88.008 -41.289  1.00 84.88           C  
ANISOU  966  CA  GLU A 106    15897  10514   5838   1794   2700   1032       C  
ATOM    967  C   GLU A 106      73.790  88.689 -40.365  1.00 75.06           C  
ANISOU  967  C   GLU A 106    14414   9154   4951   1583   3096   1077       C  
ATOM    968  O   GLU A 106      74.920  88.978 -40.765  1.00 77.49           O  
ANISOU  968  O   GLU A 106    14805   9286   5352   1280   3564   1070       O  
ATOM    969  CB  GLU A 106      71.843  89.025 -41.952  1.00 79.97           C  
ANISOU  969  CB  GLU A 106    15821   9722   4841   2018   2311   1240       C  
ATOM    970  CG  GLU A 106      71.029  88.419 -43.085  1.00 85.73           C  
ANISOU  970  CG  GLU A 106    16835  10572   5167   2125   1934   1200       C  
ATOM    971  CD  GLU A 106      69.899  89.312 -43.565  1.00 90.97           C  
ANISOU  971  CD  GLU A 106    17889  11147   5531   2435   1400   1434       C  
ATOM    972  OE1 GLU A 106      69.588  90.317 -42.884  1.00 86.25           O  
ANISOU  972  OE1 GLU A 106    17298  10389   5084   2651   1301   1611       O  
ATOM    973  OE2 GLU A 106      69.315  88.996 -44.623  1.00 90.72           O  
ANISOU  973  OE2 GLU A 106    18153  11200   5117   2469   1073   1438       O  
ATOM    974  N   LEU A 107      73.387  88.930 -39.125  1.00 71.79           N  
ANISOU  974  N   LEU A 107    13549   8845   4883   1672   2820   1064       N  
ATOM    975  CA  LEU A 107      74.292  89.465 -38.126  1.00 83.67           C  
ANISOU  975  CA  LEU A 107    14722  10298   6770   1413   3072   1045       C  
ATOM    976  C   LEU A 107      75.250  88.388 -37.606  1.00 78.22           C  
ANISOU  976  C   LEU A 107    13387   9831   6500   1197   3275    915       C  
ATOM    977  O   LEU A 107      76.325  88.705 -37.095  1.00 71.86           O  
ANISOU  977  O   LEU A 107    12315   8995   5993    905   3560    902       O  
ATOM    978  CB  LEU A 107      73.483  90.064 -36.971  1.00 83.12           C  
ANISOU  978  CB  LEU A 107    14447  10274   6862   1569   2713   1039       C  
ATOM    979  CG  LEU A 107      72.495  91.144 -37.422  1.00 71.33           C  
ANISOU  979  CG  LEU A 107    13519   8517   5068   1867   2499   1182       C  
ATOM    980  CD1 LEU A 107      71.538  91.480 -36.309  1.00 88.91           C  
ANISOU  980  CD1 LEU A 107    15452  10827   7503   2088   2172   1113       C  
ATOM    981  CD2 LEU A 107      73.239  92.377 -37.865  1.00 80.53           C  
ANISOU  981  CD2 LEU A 107    15238   9259   6098   1669   2879   1316       C  
ATOM    982  N   ASP A 108      74.852  87.122 -37.745  1.00 76.06           N  
ANISOU  982  N   ASP A 108    12857   9761   6279   1339   3107    825       N  
ATOM    983  CA  ASP A 108      75.637  85.974 -37.261  1.00 69.59           C  
ANISOU  983  CA  ASP A 108    11428   9107   5905   1222   3251    738       C  
ATOM    984  C   ASP A 108      76.068  86.137 -35.803  1.00 64.45           C  
ANISOU  984  C   ASP A 108    10210   8615   5663   1084   3117    777       C  
ATOM    985  O   ASP A 108      77.229  85.924 -35.463  1.00 64.81           O  
ANISOU  985  O   ASP A 108     9856   8696   6072    872   3360    781       O  
ATOM    986  CB  ASP A 108      76.859  85.725 -38.162  1.00 69.83           C  
ANISOU  986  CB  ASP A 108    11542   8990   6001   1027   3835    683       C  
ATOM    987  CG  ASP A 108      76.707  84.481 -39.046  1.00 70.69           C  
ANISOU  987  CG  ASP A 108    11734   9100   6025   1140   3955    536       C  
ATOM    988  OD1 ASP A 108      76.414  83.381 -38.518  1.00 68.07           O  
ANISOU  988  OD1 ASP A 108    10966   8910   5989   1257   3731    473       O  
ATOM    989  OD2 ASP A 108      76.895  84.604 -40.285  1.00 73.86           O  
ANISOU  989  OD2 ASP A 108    12690   9335   6038   1085   4303    476       O  
ATOM    990  N   VAL A 109      75.112  86.498 -34.948  1.00 61.56           N  
ANISOU  990  N   VAL A 109     9800   8360   5230   1204   2724    797       N  
ATOM    991  CA  VAL A 109      75.396  86.915 -33.578  1.00 60.52           C  
ANISOU  991  CA  VAL A 109     9311   8365   5318   1037   2589    811       C  
ATOM    992  C   VAL A 109      76.185  85.891 -32.774  1.00 63.08           C  
ANISOU  992  C   VAL A 109     9002   8919   6048    904   2548    849       C  
ATOM    993  O   VAL A 109      77.203  86.221 -32.180  1.00 65.24           O  
ANISOU  993  O   VAL A 109     8994   9246   6550    639   2633    876       O  
ATOM    994  CB  VAL A 109      74.107  87.261 -32.816  1.00 58.72           C  
ANISOU  994  CB  VAL A 109     9135   8235   4942   1221   2231    785       C  
ATOM    995  CG1 VAL A 109      74.441  87.670 -31.398  1.00 58.40           C  
ANISOU  995  CG1 VAL A 109     8804   8343   5042    997   2133    760       C  
ATOM    996  CG2 VAL A 109      73.358  88.366 -33.539  1.00 60.34           C  
ANISOU  996  CG2 VAL A 109     9920   8178   4828   1407   2232    788       C  
ATOM    997  N   ARG A 110      75.715  84.651 -32.751  1.00 58.27           N  
ANISOU  997  N   ARG A 110     8164   8430   5546   1082   2391    866       N  
ATOM    998  CA  ARG A 110      76.453  83.597 -32.063  1.00 58.37           C  
ANISOU  998  CA  ARG A 110     7610   8596   5973   1015   2343    962       C  
ATOM    999  C   ARG A 110      77.799  83.296 -32.743  1.00 61.25           C  
ANISOU  999  C   ARG A 110     7777   8835   6661    917   2737    961       C  
ATOM   1000  O   ARG A 110      78.818  83.219 -32.061  1.00 63.26           O  
ANISOU 1000  O   ARG A 110     7557   9200   7278    753   2733   1057       O  
ATOM   1001  CB  ARG A 110      75.607  82.328 -31.920  1.00 56.71           C  
ANISOU 1001  CB  ARG A 110     7255   8461   5829   1216   2130    987       C  
ATOM   1002  CG  ARG A 110      76.305  81.164 -31.202  1.00 59.19           C  
ANISOU 1002  CG  ARG A 110     7030   8867   6594   1200   2058   1149       C  
ATOM   1003  CD  ARG A 110      76.650  81.490 -29.757  1.00 65.25           C  
ANISOU 1003  CD  ARG A 110     7480   9885   7427   1019   1774   1315       C  
ATOM   1004  NE  ARG A 110      77.387  80.407 -29.097  1.00 65.89           N  
ANISOU 1004  NE  ARG A 110     7055  10044   7935   1029   1645   1544       N  
ATOM   1005  CZ  ARG A 110      76.822  79.432 -28.385  1.00 66.04           C  
ANISOU 1005  CZ  ARG A 110     6931  10142   8019   1114   1399   1711       C  
ATOM   1006  NH1 ARG A 110      75.502  79.382 -28.239  1.00 57.36           N  
ANISOU 1006  NH1 ARG A 110     6101   9084   6608   1164   1287   1635       N  
ATOM   1007  NH2 ARG A 110      77.579  78.497 -27.822  1.00 64.50           N  
ANISOU 1007  NH2 ARG A 110     6304   9968   8235   1151   1270   1976       N  
ATOM   1008  N   GLN A 111      77.814  83.142 -34.072  1.00 62.59           N  
ANISOU 1008  N   GLN A 111     8296   8790   6696   1005   3080    847       N  
ATOM   1009  CA  GLN A 111      79.050  82.786 -34.768  1.00 66.01           C  
ANISOU 1009  CA  GLN A 111     8540   9090   7453    923   3561    804       C  
ATOM   1010  C   GLN A 111      80.155  83.820 -34.560  1.00 82.62           C  
ANISOU 1010  C   GLN A 111    10487  11190   9716    622   3793    837       C  
ATOM   1011  O   GLN A 111      81.300  83.470 -34.285  1.00 71.24           O  
ANISOU 1011  O   GLN A 111     8480   9802   8784    513   3964    881       O  
ATOM   1012  CB  GLN A 111      78.814  82.597 -36.278  1.00 67.76           C  
ANISOU 1012  CB  GLN A 111     9311   9082   7354   1012   3940    639       C  
ATOM   1013  CG  GLN A 111      80.091  82.280 -37.085  1.00 74.19           C  
ANISOU 1013  CG  GLN A 111     9982   9733   8474    913   4577    544       C  
ATOM   1014  CD  GLN A 111      79.885  82.370 -38.591  1.00 79.29           C  
ANISOU 1014  CD  GLN A 111    11332  10163   8633    915   5000    370       C  
ATOM   1015  OE1 GLN A 111      78.752  82.395 -39.076  1.00 77.63           O  
ANISOU 1015  OE1 GLN A 111    11659   9938   7898   1036   4735    324       O  
ATOM   1016  NE2 GLN A 111      80.988  82.427 -39.343  1.00 95.45           N  
ANISOU 1016  NE2 GLN A 111    13371  12058  10838    762   5662    274       N  
ATOM   1017  N   ASN A 112      79.808  85.093 -34.697  1.00 68.40           N  
ANISOU 1017  N   ASN A 112     9166   9303   7521    487   3795    817       N  
ATOM   1018  CA  ASN A 112      80.809  86.160 -34.705  1.00 86.21           C  
ANISOU 1018  CA  ASN A 112    11399  11473   9886    142   4098    812       C  
ATOM   1019  C   ASN A 112      80.952  86.945 -33.395  1.00 71.14           C  
ANISOU 1019  C   ASN A 112     9244   9724   8061    -99   3749    851       C  
ATOM   1020  O   ASN A 112      81.811  87.820 -33.286  1.00 74.23           O  
ANISOU 1020  O   ASN A 112     9566  10052   8588   -450   3959    820       O  
ATOM   1021  CB  ASN A 112      80.543  87.126 -35.864  1.00 73.38           C  
ANISOU 1021  CB  ASN A 112    10551   9544   7787     88   4450    773       C  
ATOM   1022  CG  ASN A 112      80.824  86.504 -37.223  1.00 78.82           C  
ANISOU 1022  CG  ASN A 112    11494  10076   8379    170   4941    701       C  
ATOM   1023  OD1 ASN A 112      81.048  85.297 -37.337  1.00 75.90           O  
ANISOU 1023  OD1 ASN A 112    10753   9790   8294    321   5010    641       O  
ATOM   1024  ND2 ASN A 112      80.813  87.331 -38.260  1.00 86.54           N  
ANISOU 1024  ND2 ASN A 112    13155  10795   8930     61   5307    707       N  
ATOM   1025  N   TYR A 113      80.119  86.646 -32.407  1.00 67.92           N  
ANISOU 1025  N   TYR A 113     8731   9519   7555     45   3250    894       N  
ATOM   1026  CA  TYR A 113      80.216  87.361 -31.139  1.00 68.10           C  
ANISOU 1026  CA  TYR A 113     8595   9708   7573   -209   2936    888       C  
ATOM   1027  C   TYR A 113      80.174  86.447 -29.919  1.00 69.72           C  
ANISOU 1027  C   TYR A 113     8270  10258   7961   -166   2481   1004       C  
ATOM   1028  O   TYR A 113      80.409  86.900 -28.796  1.00 71.63           O  
ANISOU 1028  O   TYR A 113     8335  10698   8183   -424   2197   1002       O  
ATOM   1029  CB  TYR A 113      79.108  88.408 -31.025  1.00 68.29           C  
ANISOU 1029  CB  TYR A 113     9231   9578   7139   -150   2833    799       C  
ATOM   1030  CG  TYR A 113      79.283  89.586 -31.945  1.00 71.93           C  
ANISOU 1030  CG  TYR A 113    10245   9668   7418   -276   3218    741       C  
ATOM   1031  CD1 TYR A 113      78.814  89.550 -33.250  1.00 78.93           C  
ANISOU 1031  CD1 TYR A 113    11616  10313   8059    -31   3458    779       C  
ATOM   1032  CD2 TYR A 113      79.921  90.738 -31.507  1.00 74.18           C  
ANISOU 1032  CD2 TYR A 113    10610   9828   7748   -673   3332    656       C  
ATOM   1033  CE1 TYR A 113      78.974  90.627 -34.090  1.00 76.69           C  
ANISOU 1033  CE1 TYR A 113    11908   9668   7564   -150   3804    790       C  
ATOM   1034  CE2 TYR A 113      80.083  91.819 -32.336  1.00 80.11           C  
ANISOU 1034  CE2 TYR A 113    11912  10179   8346   -809   3714    637       C  
ATOM   1035  CZ  TYR A 113      79.611  91.760 -33.627  1.00 79.59           C  
ANISOU 1035  CZ  TYR A 113    12348   9870   8021   -533   3952    732       C  
ATOM   1036  OH  TYR A 113      79.774  92.844 -34.454  1.00 78.39           O  
ANISOU 1036  OH  TYR A 113    12815   9296   7673   -673   4328    775       O  
ATOM   1037  N   ASP A 114      79.873  85.171 -30.142  1.00 65.34           N  
ANISOU 1037  N   ASP A 114     7519   9754   7551    134   2418   1104       N  
ATOM   1038  CA  ASP A 114      79.705  84.200 -29.053  1.00 64.50           C  
ANISOU 1038  CA  ASP A 114     7003   9917   7587    213   2002   1275       C  
ATOM   1039  C   ASP A 114      78.628  84.632 -28.054  1.00 62.33           C  
ANISOU 1039  C   ASP A 114     6986   9798   6898    183   1665   1247       C  
ATOM   1040  O   ASP A 114      78.719  84.359 -26.860  1.00 63.25           O  
ANISOU 1040  O   ASP A 114     6838  10182   7012     57   1318   1372       O  
ATOM   1041  CB  ASP A 114      81.037  83.910 -28.344  1.00 84.04           C  
ANISOU 1041  CB  ASP A 114     8821  12596  10515      5   1849   1431       C  
ATOM   1042  CG  ASP A 114      80.977  82.661 -27.474  1.00 81.62           C  
ANISOU 1042  CG  ASP A 114     8103  12492  10415    167   1459   1695       C  
ATOM   1043  OD1 ASP A 114      80.089  81.810 -27.716  1.00 73.46           O  
ANISOU 1043  OD1 ASP A 114     7241  11363   9307    452   1458   1735       O  
ATOM   1044  OD2 ASP A 114      81.815  82.534 -26.551  1.00 80.14           O  
ANISOU 1044  OD2 ASP A 114     7434  12553  10463    -10   1134   1877       O  
ATOM   1045  N   VAL A 115      77.604  85.301 -28.569  1.00 60.37           N  
ANISOU 1045  N   VAL A 115     7262   9378   6296    308   1782   1090       N  
ATOM   1046  CA  VAL A 115      76.438  85.680 -27.789  1.00 58.71           C  
ANISOU 1046  CA  VAL A 115     7292   9269   5748    355   1567   1021       C  
ATOM   1047  C   VAL A 115      75.216  84.946 -28.322  1.00 67.72           C  
ANISOU 1047  C   VAL A 115     8573  10360   6797    698   1540   1020       C  
ATOM   1048  O   VAL A 115      75.038  84.830 -29.532  1.00 62.65           O  
ANISOU 1048  O   VAL A 115     8142   9513   6151    879   1725    974       O  
ATOM   1049  CB  VAL A 115      76.184  87.201 -27.831  1.00 59.63           C  
ANISOU 1049  CB  VAL A 115     7859   9202   5597    237   1700    827       C  
ATOM   1050  CG1 VAL A 115      74.946  87.562 -26.985  1.00 58.65           C  
ANISOU 1050  CG1 VAL A 115     7935   9166   5183    327   1543    719       C  
ATOM   1051  CG2 VAL A 115      77.405  87.951 -27.325  1.00 62.76           C  
ANISOU 1051  CG2 VAL A 115     8122   9629   6096   -182   1732    783       C  
ATOM   1052  N   THR A 116      74.371  84.453 -27.418  1.00 55.12           N  
ANISOU 1052  N   THR A 116     6873   8965   5105    746   1314   1062       N  
ATOM   1053  CA  THR A 116      73.191  83.717 -27.827  1.00 53.38           C  
ANISOU 1053  CA  THR A 116     6706   8727   4851   1009   1269   1047       C  
ATOM   1054  C   THR A 116      71.934  84.548 -27.547  1.00 52.98           C  
ANISOU 1054  C   THR A 116     6911   8690   4530   1115   1237    886       C  
ATOM   1055  O   THR A 116      71.703  84.958 -26.403  1.00 53.66           O  
ANISOU 1055  O   THR A 116     6975   8938   4476    972   1174    849       O  
ATOM   1056  CB  THR A 116      73.101  82.353 -27.090  1.00 59.27           C  
ANISOU 1056  CB  THR A 116     7100   9649   5770    993   1097   1239       C  
ATOM   1057  OG1 THR A 116      74.253  81.550 -27.397  1.00 54.30           O  
ANISOU 1057  OG1 THR A 116     6198   8952   5482    972   1138   1397       O  
ATOM   1058  CG2 THR A 116      71.832  81.598 -27.485  1.00 58.51           C  
ANISOU 1058  CG2 THR A 116     7040   9525   5667   1193   1066   1188       C  
ATOM   1059  N   VAL A 117      71.129  84.813 -28.577  1.00 52.62           N  
ANISOU 1059  N   VAL A 117     7109   8476   4408   1368   1280    786       N  
ATOM   1060  CA  VAL A 117      69.851  85.490 -28.335  1.00 52.98           C  
ANISOU 1060  CA  VAL A 117     7292   8533   4307   1545   1228    653       C  
ATOM   1061  C   VAL A 117      68.832  84.454 -27.859  1.00 52.34           C  
ANISOU 1061  C   VAL A 117     6913   8667   4307   1610   1098    667       C  
ATOM   1062  O   VAL A 117      68.439  83.573 -28.618  1.00 54.25           O  
ANISOU 1062  O   VAL A 117     7069   8892   4651   1725   1016    689       O  
ATOM   1063  CB  VAL A 117      69.321  86.207 -29.600  1.00 60.17           C  
ANISOU 1063  CB  VAL A 117     8552   9195   5115   1822   1241    590       C  
ATOM   1064  CG1 VAL A 117      68.123  87.111 -29.242  1.00 55.31           C  
ANISOU 1064  CG1 VAL A 117     8031   8548   4437   2047   1198    466       C  
ATOM   1065  CG2 VAL A 117      70.421  87.021 -30.235  1.00 54.93           C  
ANISOU 1065  CG2 VAL A 117     8211   8280   4380   1710   1430    622       C  
ATOM   1066  N   ILE A 118      68.408  84.542 -26.602  1.00 52.92           N  
ANISOU 1066  N   ILE A 118     6855   8934   4318   1493   1108    636       N  
ATOM   1067  CA  ILE A 118      67.551  83.499 -26.059  1.00 52.89           C  
ANISOU 1067  CA  ILE A 118     6567   9132   4398   1476   1049    680       C  
ATOM   1068  C   ILE A 118      66.074  83.848 -26.214  1.00 54.95           C  
ANISOU 1068  C   ILE A 118     6773   9420   4687   1713   1061    504       C  
ATOM   1069  O   ILE A 118      65.206  82.980 -26.102  1.00 54.54           O  
ANISOU 1069  O   ILE A 118     6457   9500   4766   1722   1020    507       O  
ATOM   1070  CB  ILE A 118      67.902  83.177 -24.573  1.00 53.76           C  
ANISOU 1070  CB  ILE A 118     6560   9474   4391   1175   1069    793       C  
ATOM   1071  CG1 ILE A 118      67.789  84.422 -23.705  1.00 55.47           C  
ANISOU 1071  CG1 ILE A 118     6978   9743   4355   1082   1200    610       C  
ATOM   1072  CG2 ILE A 118      69.321  82.636 -24.474  1.00 73.95           C  
ANISOU 1072  CG2 ILE A 118     9049  12030   7018    988    966   1021       C  
ATOM   1073  CD1 ILE A 118      67.888  84.118 -22.174  1.00 57.36           C  
ANISOU 1073  CD1 ILE A 118     7174  10265   4353    758   1218    685       C  
ATOM   1074  N   ALA A 119      65.792  85.116 -26.492  1.00 55.18           N  
ANISOU 1074  N   ALA A 119     7026   9299   4641   1909   1120    357       N  
ATOM   1075  CA  ALA A 119      64.408  85.569 -26.643  1.00 57.23           C  
ANISOU 1075  CA  ALA A 119     7177   9563   5003   2205   1115    200       C  
ATOM   1076  C   ALA A 119      64.325  86.939 -27.313  1.00 58.84           C  
ANISOU 1076  C   ALA A 119     7708   9479   5168   2495   1123    121       C  
ATOM   1077  O   ALA A 119      65.283  87.714 -27.280  1.00 62.96           O  
ANISOU 1077  O   ALA A 119     8563   9809   5549   2385   1234    132       O  
ATOM   1078  CB  ALA A 119      63.704  85.608 -25.273  1.00 59.00           C  
ANISOU 1078  CB  ALA A 119     7197  10000   5221   2092   1329     77       C  
ATOM   1079  N   ILE A 120      63.175  87.230 -27.915  1.00 61.06           N  
ANISOU 1079  N   ILE A 120     7880   9720   5602   2858    991     59       N  
ATOM   1080  CA  ILE A 120      62.917  88.545 -28.491  1.00 63.70           C  
ANISOU 1080  CA  ILE A 120     8518   9744   5942   3206    975     31       C  
ATOM   1081  C   ILE A 120      61.549  89.054 -28.038  1.00 67.41           C  
ANISOU 1081  C   ILE A 120     8693  10249   6672   3538   1032   -134       C  
ATOM   1082  O   ILE A 120      60.538  88.378 -28.230  1.00 70.50           O  
ANISOU 1082  O   ILE A 120     8646  10867   7274   3671    855   -156       O  
ATOM   1083  CB  ILE A 120      62.965  88.515 -30.038  1.00 64.12           C  
ANISOU 1083  CB  ILE A 120     8803   9645   5916   3417    664    195       C  
ATOM   1084  CG1 ILE A 120      64.342  88.058 -30.525  1.00 61.24           C  
ANISOU 1084  CG1 ILE A 120     8720   9216   5332   3103    713    320       C  
ATOM   1085  CG2 ILE A 120      62.608  89.881 -30.617  1.00 67.81           C  
ANISOU 1085  CG2 ILE A 120     9614   9760   6388   3815    614    237       C  
ATOM   1086  CD1 ILE A 120      64.499  88.078 -32.038  1.00 62.29           C  
ANISOU 1086  CD1 ILE A 120     9195   9187   5286   3250    501    458       C  
ATOM   1087  N   ILE A 121      61.532  90.242 -27.435  1.00 78.66           N  
ANISOU 1087  N   ILE A 121    10337  11434   8117   3654   1306   -275       N  
ATOM   1088  CA  ILE A 121      60.301  90.856 -26.937  1.00 84.55           C  
ANISOU 1088  CA  ILE A 121    10811  12148   9165   4008   1466   -471       C  
ATOM   1089  C   ILE A 121      59.812  91.905 -27.921  1.00 95.31           C  
ANISOU 1089  C   ILE A 121    12372  13134  10707   4549   1272   -379       C  
ATOM   1090  O   ILE A 121      60.475  92.920 -28.132  1.00 93.94           O  
ANISOU 1090  O   ILE A 121    12730  12551  10411   4601   1381   -339       O  
ATOM   1091  CB  ILE A 121      60.521  91.568 -25.583  1.00 81.77           C  
ANISOU 1091  CB  ILE A 121    10624  11711   8733   3818   1954   -738       C  
ATOM   1092  CG1 ILE A 121      61.487  90.782 -24.690  1.00 79.09           C  
ANISOU 1092  CG1 ILE A 121    10341  11653   8056   3221   2075   -736       C  
ATOM   1093  CG2 ILE A 121      59.186  91.823 -24.879  1.00 91.54           C  
ANISOU 1093  CG2 ILE A 121    11444  13031  10307   4101   2230   -993       C  
ATOM   1094  CD1 ILE A 121      60.916  89.509 -24.121  1.00 71.29           C  
ANISOU 1094  CD1 ILE A 121     8868  11106   7113   3024   2084   -725       C  
ATOM   1095  N   LYS A 122      58.651  91.665 -28.521  1.00106.66           N  
ANISOU 1095  N   LYS A 122    13381  14699  12446   4940    964   -328       N  
ATOM   1096  CA  LYS A 122      58.098  92.599 -29.494  1.00123.43           C  
ANISOU 1096  CA  LYS A 122    15656  16491  14750   5509    676   -172       C  
ATOM   1097  C   LYS A 122      57.453  93.780 -28.777  1.00128.33           C  
ANISOU 1097  C   LYS A 122    16232  16796  15730   5901   1034   -372       C  
ATOM   1098  O   LYS A 122      57.283  93.751 -27.557  1.00128.84           O  
ANISOU 1098  O   LYS A 122    16081  16981  15892   5715   1500   -672       O  
ATOM   1099  CB  LYS A 122      57.075  91.895 -30.388  1.00134.34           C  
ANISOU 1099  CB  LYS A 122    16544  18167  16332   5773    135    -47       C  
ATOM   1100  CG  LYS A 122      57.563  90.570 -30.962  1.00135.56           C  
ANISOU 1100  CG  LYS A 122    16677  18648  16180   5350   -145     51       C  
ATOM   1101  CD  LYS A 122      58.667  90.764 -31.992  1.00135.35           C  
ANISOU 1101  CD  LYS A 122    17355  18373  15701   5240   -313    291       C  
ATOM   1102  CE  LYS A 122      59.320  89.437 -32.349  1.00131.12           C  
ANISOU 1102  CE  LYS A 122    16820  18110  14889   4775   -416    312       C  
ATOM   1103  NZ  LYS A 122      58.315  88.399 -32.709  1.00132.31           N  
ANISOU 1103  NZ  LYS A 122    16420  18632  15218   4789   -793    254       N  
ATOM   1104  N   HIS A 123      57.102  94.818 -29.534  1.00130.18           N  
ANISOU 1104  N   HIS A 123    16713  16603  16147   6443    836   -201       N  
ATOM   1105  CA  HIS A 123      56.446  95.992 -28.959  1.00135.25           C  
ANISOU 1105  CA  HIS A 123    17324  16846  17217   6909   1181   -383       C  
ATOM   1106  C   HIS A 123      55.091  95.618 -28.364  1.00136.02           C  
ANISOU 1106  C   HIS A 123    16555  17281  17844   7183   1276   -615       C  
ATOM   1107  O   HIS A 123      54.647  96.208 -27.378  1.00135.18           O  
ANISOU 1107  O   HIS A 123    16295  17019  18047   7329   1813   -938       O  
ATOM   1108  CB  HIS A 123      56.276  97.096 -30.005  1.00140.11           C  
ANISOU 1108  CB  HIS A 123    18359  16908  17969   7498    872    -67       C  
ATOM   1109  CG  HIS A 123      55.545  98.298 -29.495  1.00150.48           C  
ANISOU 1109  CG  HIS A 123    19623  17734  19819   8065   1215   -234       C  
ATOM   1110  ND1 HIS A 123      55.948  98.995 -28.377  1.00153.46           N  
ANISOU 1110  ND1 HIS A 123    20302  17788  20219   7871   1905   -604       N  
ATOM   1111  CD2 HIS A 123      54.429  98.923 -29.945  1.00158.81           C  
ANISOU 1111  CD2 HIS A 123    20347  18559  21435   8785    959    -97       C  
ATOM   1112  CE1 HIS A 123      55.116  99.999 -28.161  1.00160.98           C  
ANISOU 1112  CE1 HIS A 123    21146  18288  21733   8484   2128   -718       C  
ATOM   1113  NE2 HIS A 123      54.185  99.977 -29.099  1.00164.09           N  
ANISOU 1113  NE2 HIS A 123    21105  18747  22496   8924   1528   -393       N  
ATOM   1114  N   ASN A 124      54.448  94.623 -28.968  1.00137.18           N  
ANISOU 1114  N   ASN A 124    16139  17888  18094   7212    788   -479       N  
ATOM   1115  CA  ASN A 124      53.188  94.088 -28.468  1.00141.65           C  
ANISOU 1115  CA  ASN A 124    15794  18850  19177   7367    856   -691       C  
ATOM   1116  C   ASN A 124      53.412  93.201 -27.237  1.00138.79           C  
ANISOU 1116  C   ASN A 124    15218  18873  18644   6740   1382   -990       C  
ATOM   1117  O   ASN A 124      52.467  92.636 -26.685  1.00140.23           O  
ANISOU 1117  O   ASN A 124    14678  19411  19193   6723   1561  -1187       O  
ATOM   1118  CB  ASN A 124      52.474  93.314 -29.581  1.00144.19           C  
ANISOU 1118  CB  ASN A 124    15618  19527  19640   7531    105   -453       C  
ATOM   1119  CG  ASN A 124      51.026  93.002 -29.250  1.00152.31           C  
ANISOU 1119  CG  ASN A 124    15633  20883  21354   7777     98   -637       C  
ATOM   1120  OD1 ASN A 124      50.367  93.740 -28.516  1.00158.29           O  
ANISOU 1120  OD1 ASN A 124    16117  21413  22613   7992    553   -844       O  
ATOM   1121  ND2 ASN A 124      50.523  91.901 -29.797  1.00152.06           N  
ANISOU 1121  ND2 ASN A 124    15084  21317  21373   7563   -387   -570       N  
ATOM   1122  N   GLN A 125      54.678  93.080 -26.838  1.00133.98           N  
ANISOU 1122  N   GLN A 125    15238  18191  17477   6216   1608   -993       N  
ATOM   1123  CA  GLN A 125      55.087  92.451 -25.576  1.00128.83           C  
ANISOU 1123  CA  GLN A 125    14572  17815  16561   5627   2109  -1228       C  
ATOM   1124  C   GLN A 125      54.984  90.924 -25.519  1.00118.06           C  
ANISOU 1124  C   GLN A 125    12788  16974  15096   5184   1937  -1156       C  
ATOM   1125  O   GLN A 125      55.085  90.336 -24.440  1.00116.11           O  
ANISOU 1125  O   GLN A 125    12442  16981  14693   4747   2340  -1312       O  
ATOM   1126  CB  GLN A 125      54.372  93.092 -24.378  1.00141.79           C  
ANISOU 1126  CB  GLN A 125    15989  19387  18498   5768   2774  -1615       C  
ATOM   1127  CG  GLN A 125      54.740  94.550 -24.154  1.00148.35           C  
ANISOU 1127  CG  GLN A 125    17399  19636  19331   6037   3095  -1763       C  
ATOM   1128  CD  GLN A 125      56.226  94.741 -23.915  1.00145.93           C  
ANISOU 1128  CD  GLN A 125    17879  19160  18407   5521   3166  -1725       C  
ATOM   1129  OE1 GLN A 125      56.809  94.118 -23.025  1.00142.25           O  
ANISOU 1129  OE1 GLN A 125    17516  18992  17539   4936   3399  -1839       O  
ATOM   1130  NE2 GLN A 125      56.850  95.597 -24.718  1.00146.56           N  
ANISOU 1130  NE2 GLN A 125    18506  18764  18419   5724   2946  -1541       N  
ATOM   1131  N   GLU A 126      54.797  90.282 -26.668  1.00108.61           N  
ANISOU 1131  N   GLU A 126    11400  15912  13953   5272   1347   -920       N  
ATOM   1132  CA  GLU A 126      54.833  88.825 -26.710  1.00100.17           C  
ANISOU 1132  CA  GLU A 126    10042  15242  12774   4819   1180   -855       C  
ATOM   1133  C   GLU A 126      56.282  88.375 -26.826  1.00 92.88           C  
ANISOU 1133  C   GLU A 126     9723  14254  11312   4378   1125   -685       C  
ATOM   1134  O   GLU A 126      57.089  89.010 -27.507  1.00 96.00           O  
ANISOU 1134  O   GLU A 126    10656  14350  11468   4491    952   -541       O  
ATOM   1135  CB  GLU A 126      54.022  88.264 -27.881  1.00102.44           C  
ANISOU 1135  CB  GLU A 126     9884  15710  13329   5033    573   -734       C  
ATOM   1136  CG  GLU A 126      52.804  89.075 -28.266  1.00116.26           C  
ANISOU 1136  CG  GLU A 126    11157  17402  15613   5659    381   -783       C  
ATOM   1137  CD  GLU A 126      53.070  89.974 -29.455  1.00124.72           C  
ANISOU 1137  CD  GLU A 126    12693  18129  16564   6116   -110   -531       C  
ATOM   1138  OE1 GLU A 126      54.147  90.607 -29.497  1.00122.82           O  
ANISOU 1138  OE1 GLU A 126    13194  17540  15930   6060     40   -431       O  
ATOM   1139  OE2 GLU A 126      52.209  90.039 -30.356  1.00134.16           O  
ANISOU 1139  OE2 GLU A 126    13518  19411  18048   6506   -664   -417       O  
ATOM   1140  N   LYS A 127      56.607  87.275 -26.162  1.00 78.45           N  
ANISOU 1140  N   LYS A 127     7790  12690   9328   3882   1289   -686       N  
ATOM   1141  CA  LYS A 127      57.975  86.780 -26.143  1.00 74.06           C  
ANISOU 1141  CA  LYS A 127     7702  12088   8349   3484   1261   -522       C  
ATOM   1142  C   LYS A 127      58.165  85.624 -27.125  1.00 72.41           C  
ANISOU 1142  C   LYS A 127     7417  11983   8114   3336    855   -354       C  
ATOM   1143  O   LYS A 127      57.475  84.607 -27.047  1.00 74.40           O  
ANISOU 1143  O   LYS A 127     7228  12474   8565   3175    799   -385       O  
ATOM   1144  CB  LYS A 127      58.362  86.363 -24.720  1.00 72.17           C  
ANISOU 1144  CB  LYS A 127     7490  12022   7911   3044   1687   -584       C  
ATOM   1145  CG  LYS A 127      59.835  86.041 -24.529  1.00 80.99           C  
ANISOU 1145  CG  LYS A 127     9052  13084   8636   2678   1656   -409       C  
ATOM   1146  CD  LYS A 127      60.253  86.102 -23.052  1.00 84.97           C  
ANISOU 1146  CD  LYS A 127     9707  13717   8861   2316   2036   -478       C  
ATOM   1147  CE  LYS A 127      59.425  85.170 -22.173  1.00 83.69           C  
ANISOU 1147  CE  LYS A 127     9160  13863   8775   2082   2271   -506       C  
ATOM   1148  NZ  LYS A 127      59.930  85.111 -20.761  1.00 72.47           N  
ANISOU 1148  NZ  LYS A 127     7984  12597   6956   1672   2589   -512       N  
ATOM   1149  N   LEU A 128      59.087  85.800 -28.066  1.00 68.44           N  
ANISOU 1149  N   LEU A 128     7363  11271   7370   3371    616   -203       N  
ATOM   1150  CA  LEU A 128      59.495  84.716 -28.944  1.00 66.26           C  
ANISOU 1150  CA  LEU A 128     7136  11040   6999   3181    332    -86       C  
ATOM   1151  C   LEU A 128      60.708  84.017 -28.333  1.00 64.19           C  
ANISOU 1151  C   LEU A 128     7071  10777   6540   2772    547     17       C  
ATOM   1152  O   LEU A 128      61.771  84.620 -28.179  1.00 60.60           O  
ANISOU 1152  O   LEU A 128     6997  10157   5871   2713    678     85       O  
ATOM   1153  CB  LEU A 128      59.841  85.250 -30.336  1.00 66.67           C  
ANISOU 1153  CB  LEU A 128     7592  10872   6867   3428      8     17       C  
ATOM   1154  CG  LEU A 128      60.599  84.300 -31.268  1.00 64.77           C  
ANISOU 1154  CG  LEU A 128     7588  10600   6421   3204   -165    103       C  
ATOM   1155  CD1 LEU A 128      59.795  83.034 -31.541  1.00 66.33           C  
ANISOU 1155  CD1 LEU A 128     7375  11023   6804   3053   -386     13       C  
ATOM   1156  CD2 LEU A 128      60.946  85.005 -32.575  1.00 71.44           C  
ANISOU 1156  CD2 LEU A 128     8928  11223   6994   3433   -401    207       C  
ATOM   1157  N   LEU A 129      60.541  82.751 -27.965  1.00 63.36           N  
ANISOU 1157  N   LEU A 129     6684  10843   6544   2486    573     41       N  
ATOM   1158  CA  LEU A 129      61.630  81.991 -27.358  1.00 59.06           C  
ANISOU 1158  CA  LEU A 129     6276  10289   5875   2144    727    194       C  
ATOM   1159  C   LEU A 129      62.474  81.308 -28.417  1.00 57.23           C  
ANISOU 1159  C   LEU A 129     6257   9894   5592   2089    551    290       C  
ATOM   1160  O   LEU A 129      61.961  80.881 -29.449  1.00 58.34           O  
ANISOU 1160  O   LEU A 129     6350  10011   5806   2175    320    215       O  
ATOM   1161  CB  LEU A 129      61.084  80.951 -26.387  1.00 60.07           C  
ANISOU 1161  CB  LEU A 129     6063  10614   6148   1862    884    223       C  
ATOM   1162  CG  LEU A 129      60.253  81.582 -25.267  1.00 62.63           C  
ANISOU 1162  CG  LEU A 129     6189  11115   6492   1874   1167     96       C  
ATOM   1163  CD1 LEU A 129      59.642  80.517 -24.378  1.00 64.42           C  
ANISOU 1163  CD1 LEU A 129     6103  11533   6839   1557   1368    142       C  
ATOM   1164  CD2 LEU A 129      61.132  82.518 -24.469  1.00 61.72           C  
ANISOU 1164  CD2 LEU A 129     6426  10951   6075   1827   1360    116       C  
ATOM   1165  N   ASN A 130      63.764  81.204 -28.127  1.00 55.10           N  
ANISOU 1165  N   ASN A 130     6206   9526   5203   1932    670    436       N  
ATOM   1166  CA  ASN A 130      64.738  80.617 -29.032  1.00 67.79           C  
ANISOU 1166  CA  ASN A 130     8006  10952   6799   1886    617    512       C  
ATOM   1167  C   ASN A 130      64.578  81.038 -30.499  1.00 57.28           C  
ANISOU 1167  C   ASN A 130     6931   9482   5349   2102    449    406       C  
ATOM   1168  O   ASN A 130      64.240  80.224 -31.353  1.00 59.89           O  
ANISOU 1168  O   ASN A 130     7250   9780   5726   2087    305    329       O  
ATOM   1169  CB  ASN A 130      64.747  79.097 -28.857  1.00 66.39           C  
ANISOU 1169  CB  ASN A 130     7620  10773   6833   1679    624    590       C  
ATOM   1170  CG  ASN A 130      65.042  78.687 -27.417  1.00 68.58           C  
ANISOU 1170  CG  ASN A 130     7736  11167   7154   1460    766    781       C  
ATOM   1171  OD1 ASN A 130      65.926  79.256 -26.758  1.00 65.30           O  
ANISOU 1171  OD1 ASN A 130     7430  10780   6601   1404    839    899       O  
ATOM   1172  ND2 ASN A 130      64.298  77.712 -26.919  1.00 64.99           N  
ANISOU 1172  ND2 ASN A 130     7043  10785   6866   1301    792    820       N  
ATOM   1173  N   PRO A 131      64.821  82.326 -30.789  1.00 61.33           N  
ANISOU 1173  N   PRO A 131     7729   9895   5678   2278    466    403       N  
ATOM   1174  CA  PRO A 131      64.755  82.801 -32.177  1.00 59.90           C  
ANISOU 1174  CA  PRO A 131     7893   9564   5302   2473    307    370       C  
ATOM   1175  C   PRO A 131      65.784  82.075 -33.012  1.00 59.54           C  
ANISOU 1175  C   PRO A 131     8075   9372   5173   2327    408    394       C  
ATOM   1176  O   PRO A 131      66.750  81.567 -32.447  1.00 57.83           O  
ANISOU 1176  O   PRO A 131     7759   9126   5089   2136    625    469       O  
ATOM   1177  CB  PRO A 131      65.158  84.273 -32.065  1.00 57.87           C  
ANISOU 1177  CB  PRO A 131     7942   9150   4895   2609    424    424       C  
ATOM   1178  CG  PRO A 131      65.925  84.363 -30.779  1.00 56.68           C  
ANISOU 1178  CG  PRO A 131     7661   9048   4827   2382    677    462       C  
ATOM   1179  CD  PRO A 131      65.292  83.373 -29.867  1.00 54.37           C  
ANISOU 1179  CD  PRO A 131     6938   8996   4725   2258    651    439       C  
ATOM   1180  N   GLY A 132      65.583  82.044 -34.329  1.00 57.79           N  
ANISOU 1180  N   GLY A 132     8160   9065   4732   2422    253    331       N  
ATOM   1181  CA  GLY A 132      66.498  81.381 -35.230  1.00 58.14           C  
ANISOU 1181  CA  GLY A 132     8475   8951   4662   2287    421    294       C  
ATOM   1182  C   GLY A 132      67.090  82.366 -36.215  1.00 59.74           C  
ANISOU 1182  C   GLY A 132     9221   8971   4507   2372    521    351       C  
ATOM   1183  O   GLY A 132      66.963  83.579 -36.050  1.00 61.27           O  
ANISOU 1183  O   GLY A 132     9573   9113   4593   2520    489    456       O  
ATOM   1184  N   ALA A 133      67.730  81.840 -37.255  1.00 61.28           N  
ANISOU 1184  N   ALA A 133     9740   9033   4512   2267    688    274       N  
ATOM   1185  CA  ALA A 133      68.470  82.675 -38.192  1.00 63.31           C  
ANISOU 1185  CA  ALA A 133    10554   9095   4407   2274    904    343       C  
ATOM   1186  C   ALA A 133      67.589  83.683 -38.926  1.00 75.10           C  
ANISOU 1186  C   ALA A 133    12458  10579   5498   2499    556    434       C  
ATOM   1187  O   ALA A 133      68.037  84.782 -39.267  1.00 67.75           O  
ANISOU 1187  O   ALA A 133    11943   9464   4336   2553    703    589       O  
ATOM   1188  CB  ALA A 133      69.213  81.790 -39.201  1.00 65.30           C  
ANISOU 1188  CB  ALA A 133    11082   9219   4510   2106   1200    191       C  
ATOM   1189  N   ASP A 134      66.341  83.305 -39.180  1.00 67.99           N  
ANISOU 1189  N   ASP A 134    11432   9862   4541   2624     82    355       N  
ATOM   1190  CA  ASP A 134      65.447  84.148 -39.965  1.00 72.00           C  
ANISOU 1190  CA  ASP A 134    12286  10383   4688   2879   -350    470       C  
ATOM   1191  C   ASP A 134      64.651  85.175 -39.134  1.00 71.76           C  
ANISOU 1191  C   ASP A 134    11975  10382   4910   3181   -572    613       C  
ATOM   1192  O   ASP A 134      63.840  85.915 -39.687  1.00 75.63           O  
ANISOU 1192  O   ASP A 134    12669  10861   5205   3469   -967    747       O  
ATOM   1193  CB  ASP A 134      64.506  83.285 -40.811  1.00 80.21           C  
ANISOU 1193  CB  ASP A 134    13340  11621   5515   2855   -814    304       C  
ATOM   1194  CG  ASP A 134      65.239  82.508 -41.908  1.00 93.48           C  
ANISOU 1194  CG  ASP A 134    15519  13208   6793   2588   -586    139       C  
ATOM   1195  OD1 ASP A 134      66.452  82.737 -42.120  1.00 87.98           O  
ANISOU 1195  OD1 ASP A 134    15165  12289   5973   2465    -59    187       O  
ATOM   1196  OD2 ASP A 134      64.592  81.673 -42.575  1.00100.88           O  
ANISOU 1196  OD2 ASP A 134    16500  14289   7542   2480   -915    -67       O  
ATOM   1197  N   SER A 135      64.873  85.227 -37.818  1.00 68.06           N  
ANISOU 1197  N   SER A 135    11058   9940   4864   3128   -321    587       N  
ATOM   1198  CA  SER A 135      64.204  86.258 -37.011  1.00 68.39           C  
ANISOU 1198  CA  SER A 135    10897   9961   5127   3397   -415    668       C  
ATOM   1199  C   SER A 135      64.735  87.652 -37.344  1.00 71.98           C  
ANISOU 1199  C   SER A 135    11905  10078   5366   3537   -258    864       C  
ATOM   1200  O   SER A 135      65.934  87.919 -37.228  1.00 70.27           O  
ANISOU 1200  O   SER A 135    11937   9675   5086   3306    159    898       O  
ATOM   1201  CB  SER A 135      64.330  85.986 -35.510  1.00 64.68           C  
ANISOU 1201  CB  SER A 135     9905   9610   5061   3253   -159    569       C  
ATOM   1202  OG  SER A 135      63.657  84.792 -35.163  1.00 71.85           O  
ANISOU 1202  OG  SER A 135    10318  10790   6191   3147   -311    430       O  
ATOM   1203  N   ILE A 136      63.835  88.533 -37.764  1.00 77.32           N  
ANISOU 1203  N   ILE A 136    12750  10659   5969   3916   -597   1004       N  
ATOM   1204  CA  ILE A 136      64.209  89.889 -38.146  1.00 77.18           C  
ANISOU 1204  CA  ILE A 136    13320  10247   5759   4085   -477   1231       C  
ATOM   1205  C   ILE A 136      64.232  90.787 -36.915  1.00 81.66           C  
ANISOU 1205  C   ILE A 136    13693  10637   6697   4169   -202   1184       C  
ATOM   1206  O   ILE A 136      63.352  90.704 -36.064  1.00 83.23           O  
ANISOU 1206  O   ILE A 136    13363  11009   7251   4342   -315   1051       O  
ATOM   1207  CB  ILE A 136      63.228  90.472 -39.188  1.00 85.37           C  
ANISOU 1207  CB  ILE A 136    14677  11206   6552   4506  -1011   1462       C  
ATOM   1208  CG1 ILE A 136      63.022  89.485 -40.337  1.00 85.59           C  
ANISOU 1208  CG1 ILE A 136    14861  11488   6172   4387  -1367   1442       C  
ATOM   1209  CG2 ILE A 136      63.737  91.801 -39.720  1.00 89.44           C  
ANISOU 1209  CG2 ILE A 136    15933  11241   6808   4642   -850   1758       C  
ATOM   1210  CD1 ILE A 136      62.159  90.017 -41.448  1.00 98.99           C  
ANISOU 1210  CD1 ILE A 136    16939  13151   7522   4751  -1971   1704       C  
ATOM   1211  N   ILE A 137      65.250  91.632 -36.816  1.00 78.11           N  
ANISOU 1211  N   ILE A 137    13677   9841   6158   4004    198   1261       N  
ATOM   1212  CA  ILE A 137      65.340  92.581 -35.718  1.00 79.18           C  
ANISOU 1212  CA  ILE A 137    13749   9754   6584   4032    474   1179       C  
ATOM   1213  C   ILE A 137      64.659  93.888 -36.107  1.00 87.77           C  
ANISOU 1213  C   ILE A 137    15234  10427   7689   4490    330   1375       C  
ATOM   1214  O   ILE A 137      64.908  94.420 -37.185  1.00 88.13           O  
ANISOU 1214  O   ILE A 137    15890  10181   7416   4578    264   1645       O  
ATOM   1215  CB  ILE A 137      66.798  92.844 -35.336  1.00 81.28           C  
ANISOU 1215  CB  ILE A 137    14232   9848   6802   3568    962   1129       C  
ATOM   1216  CG1 ILE A 137      67.394  91.588 -34.695  1.00 77.92           C  
ANISOU 1216  CG1 ILE A 137    13300   9823   6485   3192   1072    951       C  
ATOM   1217  CG2 ILE A 137      66.898  94.046 -34.404  1.00 75.26           C  
ANISOU 1217  CG2 ILE A 137    13589   8758   6250   3576   1226   1040       C  
ATOM   1218  CD1 ILE A 137      68.770  91.782 -34.122  1.00 79.36           C  
ANISOU 1218  CD1 ILE A 137    13513   9921   6719   2746   1474    886       C  
ATOM   1219  N   GLU A 138      63.792  94.397 -35.236  1.00 90.92           N  
ANISOU 1219  N   GLU A 138    15305  10777   8463   4793    307   1250       N  
ATOM   1220  CA  GLU A 138      63.019  95.599 -35.549  1.00 98.64           C  
ANISOU 1220  CA  GLU A 138    16573  11330   9575   5326    153   1435       C  
ATOM   1221  C   GLU A 138      63.149  96.676 -34.474  1.00 95.42           C  
ANISOU 1221  C   GLU A 138    16249  10529   9478   5353    586   1255       C  
ATOM   1222  O   GLU A 138      63.677  96.424 -33.391  1.00 86.49           O  
ANISOU 1222  O   GLU A 138    14870   9553   8439   4962    936    958       O  
ATOM   1223  CB  GLU A 138      61.546  95.238 -35.765  1.00107.14           C  
ANISOU 1223  CB  GLU A 138    17137  12686  10884   5823   -371   1465       C  
ATOM   1224  CG  GLU A 138      61.318  94.246 -36.897  1.00112.34           C  
ANISOU 1224  CG  GLU A 138    17772  13707  11205   5788   -863   1615       C  
ATOM   1225  CD  GLU A 138      59.909  93.690 -36.916  1.00119.49           C  
ANISOU 1225  CD  GLU A 138    17997  14999  12406   6140  -1375   1555       C  
ATOM   1226  OE1 GLU A 138      58.974  94.419 -36.522  1.00124.16           O  
ANISOU 1226  OE1 GLU A 138    18305  15445  13426   6625  -1474   1564       O  
ATOM   1227  OE2 GLU A 138      59.739  92.519 -37.320  1.00121.11           O  
ANISOU 1227  OE2 GLU A 138    17928  15635  12454   5922  -1654   1476       O  
ATOM   1228  N   GLU A 139      62.664  97.877 -34.774  1.00 97.84           N  
ANISOU 1228  N   GLU A 139    16937  10306   9932   5814    548   1436       N  
ATOM   1229  CA  GLU A 139      62.747  98.979 -33.823  1.00100.92           C  
ANISOU 1229  CA  GLU A 139    17492  10224  10628   5861    992   1231       C  
ATOM   1230  C   GLU A 139      61.910  98.707 -32.573  1.00 97.68           C  
ANISOU 1230  C   GLU A 139    16386  10105  10622   5988   1115    843       C  
ATOM   1231  O   GLU A 139      60.802  98.178 -32.664  1.00 98.76           O  
ANISOU 1231  O   GLU A 139    15969  10576  10981   6367    775    851       O  
ATOM   1232  CB  GLU A 139      62.316 100.293 -34.476  1.00106.01           C  
ANISOU 1232  CB  GLU A 139    18704  10170  11403   6403    915   1542       C  
ATOM   1233  CG  GLU A 139      62.578 101.516 -33.618  1.00109.22           C  
ANISOU 1233  CG  GLU A 139    19451   9951  12097   6387   1446   1321       C  
ATOM   1234  CD  GLU A 139      62.022 102.784 -34.231  1.00126.21           C  
ANISOU 1234  CD  GLU A 139    22132  11348  14473   7013   1362   1651       C  
ATOM   1235  OE1 GLU A 139      61.540 102.729 -35.382  1.00120.81           O  
ANISOU 1235  OE1 GLU A 139    21607  10653  13643   7424    850   2109       O  
ATOM   1236  OE2 GLU A 139      62.062 103.836 -33.560  1.00131.70           O  
ANISOU 1236  OE2 GLU A 139    23113  11445  15481   7095   1796   1455       O  
ATOM   1237  N   ASN A 140      62.467  99.058 -31.415  1.00 97.25           N  
ANISOU 1237  N   ASN A 140    16374   9940  10634   5620   1610    494       N  
ATOM   1238  CA  ASN A 140      61.816  98.894 -30.109  1.00 96.22           C  
ANISOU 1238  CA  ASN A 140    15718  10049  10793   5639   1859     85       C  
ATOM   1239  C   ASN A 140      61.697  97.450 -29.636  1.00 90.77           C  
ANISOU 1239  C   ASN A 140    14383  10103  10003   5330   1732    -44       C  
ATOM   1240  O   ASN A 140      61.146  97.184 -28.571  1.00 90.79           O  
ANISOU 1240  O   ASN A 140    13951  10361  10183   5296   1949   -352       O  
ATOM   1241  CB  ASN A 140      60.451  99.592 -30.054  1.00102.73           C  
ANISOU 1241  CB  ASN A 140    16321  10599  12114   6374   1823     54       C  
ATOM   1242  CG  ASN A 140      60.556 101.088 -30.238  1.00108.95           C  
ANISOU 1242  CG  ASN A 140    17761  10555  13080   6681   2062    122       C  
ATOM   1243  OD1 ASN A 140      61.558 101.701 -29.871  1.00108.60           O  
ANISOU 1243  OD1 ASN A 140    18257  10150  12856   6245   2444    -15       O  
ATOM   1244  ND2 ASN A 140      59.521 101.688 -30.811  1.00119.39           N  
ANISOU 1244  ND2 ASN A 140    19027  11547  14790   7433   1819    343       N  
ATOM   1245  N   ASP A 141      62.208  96.516 -30.427  1.00 86.72           N  
ANISOU 1245  N   ASP A 141    13844   9903   9205   5096   1423    188       N  
ATOM   1246  CA  ASP A 141      62.287  95.136 -29.982  1.00 88.60           C  
ANISOU 1246  CA  ASP A 141    13564  10751   9347   4742   1345     86       C  
ATOM   1247  C   ASP A 141      63.329  95.071 -28.875  1.00 82.95           C  
ANISOU 1247  C   ASP A 141    12936  10118   8464   4161   1721   -140       C  
ATOM   1248  O   ASP A 141      64.375  95.712 -28.968  1.00 82.66           O  
ANISOU 1248  O   ASP A 141    13376   9770   8260   3888   1900   -114       O  
ATOM   1249  CB  ASP A 141      62.699  94.211 -31.136  1.00 90.19           C  
ANISOU 1249  CB  ASP A 141    13806  11174   9289   4620    985    356       C  
ATOM   1250  CG  ASP A 141      61.526  93.793 -32.009  1.00 93.38           C  
ANISOU 1250  CG  ASP A 141    13915  11752   9815   5068    507    508       C  
ATOM   1251  OD1 ASP A 141      60.503  94.506 -32.020  1.00101.33           O  
ANISOU 1251  OD1 ASP A 141    14799  12579  11123   5572    404    514       O  
ATOM   1252  OD2 ASP A 141      61.631  92.750 -32.689  1.00 93.69           O  
ANISOU 1252  OD2 ASP A 141    13829  12098   9669   4912    227    608       O  
ATOM   1253  N   THR A 142      63.044  94.317 -27.821  1.00 81.42           N  
ANISOU 1253  N   THR A 142    12287  10343   8304   3949   1830   -350       N  
ATOM   1254  CA  THR A 142      64.066  94.036 -26.819  1.00 74.25           C  
ANISOU 1254  CA  THR A 142    11429   9619   7165   3367   2054   -496       C  
ATOM   1255  C   THR A 142      64.707  92.677 -27.097  1.00 73.00           C  
ANISOU 1255  C   THR A 142    11019   9863   6853   3050   1822   -307       C  
ATOM   1256  O   THR A 142      64.007  91.679 -27.271  1.00 73.62           O  
ANISOU 1256  O   THR A 142    10686  10259   7028   3169   1626   -240       O  
ATOM   1257  CB  THR A 142      63.506  94.060 -25.387  1.00 75.93           C  
ANISOU 1257  CB  THR A 142    11412  10027   7412   3256   2354   -821       C  
ATOM   1258  OG1 THR A 142      62.943  95.349 -25.111  1.00 89.67           O  
ANISOU 1258  OG1 THR A 142    13404  11331   9336   3565   2644  -1049       O  
ATOM   1259  CG2 THR A 142      64.614  93.785 -24.392  1.00 74.03           C  
ANISOU 1259  CG2 THR A 142    11276   9998   6852   2634   2484   -925       C  
ATOM   1260  N   LEU A 143      66.034  92.645 -27.160  1.00 67.58           N  
ANISOU 1260  N   LEU A 143    10560   9137   5981   2650   1860   -230       N  
ATOM   1261  CA  LEU A 143      66.752  91.388 -27.343  1.00 63.81           C  
ANISOU 1261  CA  LEU A 143     9833   8988   5425   2368   1697    -65       C  
ATOM   1262  C   LEU A 143      67.197  90.868 -25.995  1.00 62.81           C  
ANISOU 1262  C   LEU A 143     9479   9187   5199   1958   1777   -166       C  
ATOM   1263  O   LEU A 143      67.717  91.626 -25.173  1.00 64.59           O  
ANISOU 1263  O   LEU A 143     9911   9328   5303   1691   1952   -333       O  
ATOM   1264  CB  LEU A 143      67.992  91.581 -28.200  1.00 63.11           C  
ANISOU 1264  CB  LEU A 143    10041   8692   5247   2175   1713     90       C  
ATOM   1265  CG  LEU A 143      67.824  92.119 -29.621  1.00 89.09           C  
ANISOU 1265  CG  LEU A 143    13702  11638   8512   2486   1654    250       C  
ATOM   1266  CD1 LEU A 143      69.102  91.843 -30.395  1.00 63.61           C  
ANISOU 1266  CD1 LEU A 143    10638   8348   5183   2205   1727    401       C  
ATOM   1267  CD2 LEU A 143      66.608  91.509 -30.308  1.00 64.76           C  
ANISOU 1267  CD2 LEU A 143    10420   8696   5490   2898   1367    331       C  
ATOM   1268  N   VAL A 144      66.998  89.577 -25.766  1.00 61.57           N  
ANISOU 1268  N   VAL A 144     8936   9387   5072   1886   1632    -59       N  
ATOM   1269  CA  VAL A 144      67.463  88.967 -24.521  1.00 60.17           C  
ANISOU 1269  CA  VAL A 144     8576   9527   4757   1498   1651    -63       C  
ATOM   1270  C   VAL A 144      68.712  88.171 -24.880  1.00 57.99           C  
ANISOU 1270  C   VAL A 144     8195   9335   4505   1260   1491    168       C  
ATOM   1271  O   VAL A 144      68.654  87.176 -25.628  1.00 56.05           O  
ANISOU 1271  O   VAL A 144     7753   9141   4403   1382   1360    335       O  
ATOM   1272  CB  VAL A 144      66.389  88.085 -23.867  1.00 60.25           C  
ANISOU 1272  CB  VAL A 144     8249   9840   4805   1553   1654    -76       C  
ATOM   1273  CG1 VAL A 144      66.859  87.600 -22.490  1.00 60.93           C  
ANISOU 1273  CG1 VAL A 144     8269  10231   4652   1135   1685    -49       C  
ATOM   1274  CG2 VAL A 144      65.086  88.866 -23.721  1.00 64.01           C  
ANISOU 1274  CG2 VAL A 144     8734  10211   5378   1872   1847   -316       C  
ATOM   1275  N   LEU A 145      69.845  88.648 -24.381  1.00 59.00           N  
ANISOU 1275  N   LEU A 145     8442   9452   4523    919   1516    150       N  
ATOM   1276  CA  LEU A 145      71.137  88.129 -24.787  1.00 58.02           C  
ANISOU 1276  CA  LEU A 145     8182   9358   4507    719   1409    345       C  
ATOM   1277  C   LEU A 145      71.831  87.390 -23.668  1.00 64.86           C  
ANISOU 1277  C   LEU A 145     8776  10561   5306    384   1231    477       C  
ATOM   1278  O   LEU A 145      71.853  87.857 -22.526  1.00 60.86           O  
ANISOU 1278  O   LEU A 145     8366  10207   4552    123   1220    353       O  
ATOM   1279  CB  LEU A 145      72.032  89.276 -25.260  1.00 59.65           C  
ANISOU 1279  CB  LEU A 145     8678   9271   4716    570   1550    256       C  
ATOM   1280  CG  LEU A 145      71.403  90.159 -26.341  1.00 66.33           C  
ANISOU 1280  CG  LEU A 145     9898   9726   5579    898   1712    182       C  
ATOM   1281  CD1 LEU A 145      72.108  91.517 -26.434  1.00 62.93           C  
ANISOU 1281  CD1 LEU A 145     9849   8955   5104    686   1912     53       C  
ATOM   1282  CD2 LEU A 145      71.403  89.429 -27.679  1.00 61.13           C  
ANISOU 1282  CD2 LEU A 145     9191   8999   5036   1139   1669    366       C  
ATOM   1283  N   SER A 146      72.414  86.243 -23.994  1.00 57.37           N  
ANISOU 1283  N   SER A 146     7517   9714   4568    392   1088    730       N  
ATOM   1284  CA  SER A 146      73.166  85.486 -23.006  1.00 58.71           C  
ANISOU 1284  CA  SER A 146     7407  10175   4726    123    856    941       C  
ATOM   1285  C   SER A 146      74.603  85.323 -23.456  1.00 62.34           C  
ANISOU 1285  C   SER A 146     7630  10594   5462     -5    781   1086       C  
ATOM   1286  O   SER A 146      74.855  84.939 -24.594  1.00 58.22           O  
ANISOU 1286  O   SER A 146     7029   9874   5218    198    908   1140       O  
ATOM   1287  CB  SER A 146      72.536  84.113 -22.792  1.00 57.61           C  
ANISOU 1287  CB  SER A 146     7044  10176   4669    266    753   1160       C  
ATOM   1288  OG  SER A 146      73.392  83.282 -22.037  1.00 65.46           O  
ANISOU 1288  OG  SER A 146     7770  11382   5720     72    496   1456       O  
ATOM   1289  N   GLY A 147      75.541  85.601 -22.558  1.00 62.53           N  
ANISOU 1289  N   GLY A 147     7528  10823   5409   -359    580   1133       N  
ATOM   1290  CA  GLY A 147      76.947  85.422 -22.871  1.00 67.79           C  
ANISOU 1290  CA  GLY A 147     7843  11499   6415   -499    487   1278       C  
ATOM   1291  C   GLY A 147      77.861  86.100 -21.875  1.00 68.51           C  
ANISOU 1291  C   GLY A 147     7849  11821   6360   -956    240   1232       C  
ATOM   1292  O   GLY A 147      77.408  86.568 -20.832  1.00 73.32           O  
ANISOU 1292  O   GLY A 147     8711  12608   6540  -1180    116   1105       O  
ATOM   1293  N   GLU A 148      79.152  86.135 -22.194  1.00 70.93           N  
ANISOU 1293  N   GLU A 148     7783  12136   7029  -1119    179   1314       N  
ATOM   1294  CA  GLU A 148      80.144  86.792 -21.354  1.00 81.91           C  
ANISOU 1294  CA  GLU A 148     9012  13761   8350  -1607   -102   1254       C  
ATOM   1295  C   GLU A 148      80.110  88.299 -21.560  1.00 80.21           C  
ANISOU 1295  C   GLU A 148     9227  13307   7941  -1885    182    855       C  
ATOM   1296  O   GLU A 148      79.755  88.778 -22.638  1.00 78.36           O  
ANISOU 1296  O   GLU A 148     9270  12693   7809  -1679    603    716       O  
ATOM   1297  CB  GLU A 148      81.539  86.249 -21.652  1.00 88.12           C  
ANISOU 1297  CB  GLU A 148     9134  14647   9701  -1668   -259   1488       C  
ATOM   1298  CG  GLU A 148      81.680  84.767 -21.383  1.00 92.41           C  
ANISOU 1298  CG  GLU A 148     9240  15367  10506  -1378   -560   1912       C  
ATOM   1299  CD  GLU A 148      82.891  84.171 -22.060  1.00104.46           C  
ANISOU 1299  CD  GLU A 148    10109  16842  12740  -1258   -524   2105       C  
ATOM   1300  OE1 GLU A 148      82.914  82.935 -22.243  1.00106.53           O  
ANISOU 1300  OE1 GLU A 148    10073  17063  13341   -893   -582   2408       O  
ATOM   1301  OE2 GLU A 148      83.817  84.936 -22.410  1.00112.02           O  
ANISOU 1301  OE2 GLU A 148    10841  17771  13950  -1536   -396   1940       O  
ATOM   1302  N   ARG A 149      80.484  89.030 -20.515  1.00 80.75           N  
ANISOU 1302  N   ARG A 149     9388  13581   7711  -2367    -67    681       N  
ATOM   1303  CA  ARG A 149      80.430  90.488 -20.500  1.00 82.66           C  
ANISOU 1303  CA  ARG A 149    10099  13564   7743  -2693    187    268       C  
ATOM   1304  C   ARG A 149      81.209  91.119 -21.644  1.00 83.40           C  
ANISOU 1304  C   ARG A 149    10118  13308   8262  -2777    536    187       C  
ATOM   1305  O   ARG A 149      80.712  92.025 -22.318  1.00 82.31           O  
ANISOU 1305  O   ARG A 149    10477  12734   8063  -2695    957    -30       O  
ATOM   1306  CB  ARG A 149      80.957  91.012 -19.162  1.00 88.27           C  
ANISOU 1306  CB  ARG A 149    10837  14604   8098  -3290   -204     94       C  
ATOM   1307  CG  ARG A 149      81.180  92.510 -19.126  1.00 91.68           C  
ANISOU 1307  CG  ARG A 149    11691  14737   8404  -3733     42   -358       C  
ATOM   1308  CD  ARG A 149      81.763  92.962 -17.794  1.00103.87           C  
ANISOU 1308  CD  ARG A 149    13258  16641   9565  -4392   -393   -568       C  
ATOM   1309  NE  ARG A 149      80.782  92.904 -16.714  1.00106.84           N  
ANISOU 1309  NE  ARG A 149    14085  17211   9299  -4395   -490   -699       N  
ATOM   1310  CZ  ARG A 149      80.637  91.873 -15.887  1.00108.96           C  
ANISOU 1310  CZ  ARG A 149    14159  17956   9287  -4338   -917   -396       C  
ATOM   1311  NH1 ARG A 149      81.415  90.807 -16.008  1.00105.59           N  
ANISOU 1311  NH1 ARG A 149    13075  17834   9211  -4230  -1332     72       N  
ATOM   1312  NH2 ARG A 149      79.714  91.910 -14.936  1.00113.11           N  
ANISOU 1312  NH2 ARG A 149    15159  18625   9194  -4384   -894   -552       N  
ATOM   1313  N   LYS A 150      82.429  90.635 -21.853  1.00 89.45           N  
ANISOU 1313  N   LYS A 150    10257  14256   9475  -2933    376    382       N  
ATOM   1314  CA  LYS A 150      83.294  91.134 -22.918  1.00 89.65           C  
ANISOU 1314  CA  LYS A 150    10129  13993   9942  -3067    759    323       C  
ATOM   1315  C   LYS A 150      82.586  91.037 -24.265  1.00 82.99           C  
ANISOU 1315  C   LYS A 150     9640  12729   9163  -2574   1272    366       C  
ATOM   1316  O   LYS A 150      82.501  92.012 -25.010  1.00 83.44           O  
ANISOU 1316  O   LYS A 150    10140  12372   9190  -2650   1694    191       O  
ATOM   1317  CB  LYS A 150      84.594  90.330 -22.957  1.00 93.28           C  
ANISOU 1317  CB  LYS A 150     9730  14754  10958  -3171    528    575       C  
ATOM   1318  CG  LYS A 150      85.240  90.136 -21.594  1.00101.44           C  
ANISOU 1318  CG  LYS A 150    10328  16299  11916  -3565   -147    648       C  
ATOM   1319  CD  LYS A 150      85.759  91.450 -21.025  1.00106.36           C  
ANISOU 1319  CD  LYS A 150    11128  16926  12357  -4260   -222    284       C  
ATOM   1320  CE  LYS A 150      87.041  91.889 -21.718  1.00108.98           C  
ANISOU 1320  CE  LYS A 150    10952  17156  13300  -4613     15    219       C  
ATOM   1321  NZ  LYS A 150      88.160  90.943 -21.454  1.00109.85           N  
ANISOU 1321  NZ  LYS A 150    10070  17710  13958  -4635   -431    533       N  
ATOM   1322  N   HIS A 151      82.060  89.853 -24.553  1.00 82.62           N  
ANISOU 1322  N   HIS A 151     9435  12780   9178  -2087   1208    608       N  
ATOM   1323  CA  HIS A 151      81.351  89.608 -25.803  1.00 81.94           C  
ANISOU 1323  CA  HIS A 151     9667  12363   9103  -1631   1601    650       C  
ATOM   1324  C   HIS A 151      80.079  90.441 -25.934  1.00 74.29           C  
ANISOU 1324  C   HIS A 151     9414  11109   7703  -1459   1759    465       C  
ATOM   1325  O   HIS A 151      79.773  90.927 -27.017  1.00 72.27           O  
ANISOU 1325  O   HIS A 151     9557  10483   7419  -1285   2121    424       O  
ATOM   1326  CB  HIS A 151      81.043  88.117 -25.953  1.00 83.44           C  
ANISOU 1326  CB  HIS A 151     9528  12724   9453  -1209   1454    907       C  
ATOM   1327  CG  HIS A 151      82.261  87.275 -26.170  1.00 85.72           C  
ANISOU 1327  CG  HIS A 151     9133  13153  10283  -1237   1431   1101       C  
ATOM   1328  ND1 HIS A 151      82.489  86.102 -25.485  1.00 87.24           N  
ANISOU 1328  ND1 HIS A 151     8821  13641  10687  -1102   1044   1363       N  
ATOM   1329  CD2 HIS A 151      83.324  87.443 -26.993  1.00 84.32           C  
ANISOU 1329  CD2 HIS A 151     8677  12839  10521  -1369   1780   1077       C  
ATOM   1330  CE1 HIS A 151      83.639  85.581 -25.876  1.00 89.64           C  
ANISOU 1330  CE1 HIS A 151     8527  13972  11559  -1104   1132   1491       C  
ATOM   1331  NE2 HIS A 151      84.165  86.375 -26.791  1.00 85.86           N  
ANISOU 1331  NE2 HIS A 151     8153  13252  11218  -1278   1602   1300       N  
ATOM   1332  N   LEU A 152      79.344  90.605 -24.834  1.00 72.61           N  
ANISOU 1332  N   LEU A 152     9366  11066   7156  -1498   1497    364       N  
ATOM   1333  CA  LEU A 152      78.134  91.426 -24.841  1.00 71.40           C  
ANISOU 1333  CA  LEU A 152     9813  10641   6673  -1311   1660    164       C  
ATOM   1334  C   LEU A 152      78.428  92.889 -25.174  1.00 85.40           C  
ANISOU 1334  C   LEU A 152    12040  11993   8417  -1573   1968    -67       C  
ATOM   1335  O   LEU A 152      77.740  93.489 -26.004  1.00 73.77           O  
ANISOU 1335  O   LEU A 152    11036  10115   6879  -1287   2246   -101       O  
ATOM   1336  CB  LEU A 152      77.406  91.345 -23.492  1.00 71.57           C  
ANISOU 1336  CB  LEU A 152     9896  10941   6358  -1371   1401     55       C  
ATOM   1337  CG  LEU A 152      76.709  90.040 -23.104  1.00 72.28           C  
ANISOU 1337  CG  LEU A 152     9720  11355   6389  -1075   1168    269       C  
ATOM   1338  CD1 LEU A 152      76.117  90.185 -21.706  1.00 70.30           C  
ANISOU 1338  CD1 LEU A 152     9615  11359   5737  -1255   1003    125       C  
ATOM   1339  CD2 LEU A 152      75.625  89.672 -24.098  1.00 64.99           C  
ANISOU 1339  CD2 LEU A 152     8950  10219   5523   -554   1355    331       C  
ATOM   1340  N   LYS A 153      79.435  93.459 -24.511  1.00 89.84           N  
ANISOU 1340  N   LYS A 153    12469  12638   9029  -2127   1890   -213       N  
ATOM   1341  CA  LYS A 153      79.867  94.832 -24.782  1.00 97.94           C  
ANISOU 1341  CA  LYS A 153    13902  13231  10081  -2481   2202   -443       C  
ATOM   1342  C   LYS A 153      80.207  95.000 -26.257  1.00 90.73           C  
ANISOU 1342  C   LYS A 153    13122  11942   9408  -2335   2605   -286       C  
ATOM   1343  O   LYS A 153      79.798  95.970 -26.898  1.00 89.82           O  
ANISOU 1343  O   LYS A 153    13602  11319   9208  -2249   2937   -356       O  
ATOM   1344  CB  LYS A 153      81.100  95.191 -23.948  1.00108.60           C  
ANISOU 1344  CB  LYS A 153    14926  14804  11531  -3171   2007   -600       C  
ATOM   1345  CG  LYS A 153      80.870  95.258 -22.453  1.00118.21           C  
ANISOU 1345  CG  LYS A 153    16157  16363  12393  -3449   1621   -807       C  
ATOM   1346  CD  LYS A 153      82.147  95.665 -21.733  1.00127.07           C  
ANISOU 1346  CD  LYS A 153    16960  17716  13606  -4181   1369   -968       C  
ATOM   1347  CE  LYS A 153      81.934  95.776 -20.233  1.00130.79           C  
ANISOU 1347  CE  LYS A 153    17545  18544  13605  -4521    964  -1198       C  
ATOM   1348  NZ  LYS A 153      80.878  96.765 -19.879  1.00132.26           N  
ANISOU 1348  NZ  LYS A 153    18509  18339  13404  -4473   1268  -1576       N  
ATOM   1349  N   LYS A 154      80.961  94.039 -26.779  1.00 87.55           N  
ANISOU 1349  N   LYS A 154    12187  11778   9300  -2301   2590    -64       N  
ATOM   1350  CA  LYS A 154      81.364  94.021 -28.182  1.00 89.46           C  
ANISOU 1350  CA  LYS A 154    12524  11734   9735  -2189   3016     81       C  
ATOM   1351  C   LYS A 154      80.159  94.066 -29.122  1.00 88.09           C  
ANISOU 1351  C   LYS A 154    12933  11245   9291  -1642   3182    178       C  
ATOM   1352  O   LYS A 154      80.103  94.895 -30.031  1.00 92.99           O  
ANISOU 1352  O   LYS A 154    14090  11412   9830  -1634   3545    198       O  
ATOM   1353  CB  LYS A 154      82.191  92.766 -28.464  1.00 89.09           C  
ANISOU 1353  CB  LYS A 154    11766  12032  10052  -2139   2963    273       C  
ATOM   1354  CG  LYS A 154      82.620  92.612 -29.909  1.00 91.12           C  
ANISOU 1354  CG  LYS A 154    12115  12031  10476  -2028   3466    387       C  
ATOM   1355  CD  LYS A 154      83.685  93.621 -30.270  1.00 92.77           C  
ANISOU 1355  CD  LYS A 154    12374  11980  10893  -2560   3878    288       C  
ATOM   1356  CE  LYS A 154      84.225  93.372 -31.668  1.00 89.25           C  
ANISOU 1356  CE  LYS A 154    11979  11327  10605  -2500   4447    402       C  
ATOM   1357  NZ  LYS A 154      85.531  94.036 -31.833  1.00 95.31           N  
ANISOU 1357  NZ  LYS A 154    12480  11989  11746  -3093   4838    317       N  
ATOM   1358  N   LEU A 155      79.205  93.165 -28.893  1.00 80.60           N  
ANISOU 1358  N   LEU A 155    11873  10542   8207  -1207   2893    258       N  
ATOM   1359  CA  LEU A 155      77.992  93.075 -29.704  1.00 77.17           C  
ANISOU 1359  CA  LEU A 155    11874   9905   7543   -684   2935    346       C  
ATOM   1360  C   LEU A 155      77.163  94.347 -29.617  1.00 73.64           C  
ANISOU 1360  C   LEU A 155    12049   9057   6875   -585   3016    223       C  
ATOM   1361  O   LEU A 155      76.659  94.840 -30.627  1.00 74.44           O  
ANISOU 1361  O   LEU A 155    12654   8787   6844   -314   3194    327       O  
ATOM   1362  CB  LEU A 155      77.142  91.868 -29.273  1.00 78.13           C  
ANISOU 1362  CB  LEU A 155    11671  10396   7618   -330   2589    414       C  
ATOM   1363  CG  LEU A 155      75.762  91.720 -29.925  1.00 65.81           C  
ANISOU 1363  CG  LEU A 155    10447   8711   5848    183   2527    468       C  
ATOM   1364  CD1 LEU A 155      75.873  91.389 -31.411  1.00 71.21           C  
ANISOU 1364  CD1 LEU A 155    11343   9217   6495    373   2727    615       C  
ATOM   1365  CD2 LEU A 155      74.911  90.683 -29.189  1.00 62.73           C  
ANISOU 1365  CD2 LEU A 155     9703   8687   5443    406   2203    478       C  
ATOM   1366  N   ILE A 156      77.018  94.874 -28.406  1.00 74.79           N  
ANISOU 1366  N   ILE A 156    12183   9264   6969   -795   2883      6       N  
ATOM   1367  CA  ILE A 156      76.254  96.097 -28.207  1.00 84.32           C  
ANISOU 1367  CA  ILE A 156    13960  10044   8033   -693   3009   -162       C  
ATOM   1368  C   ILE A 156      76.933  97.281 -28.889  1.00 88.20           C  
ANISOU 1368  C   ILE A 156    14935   9988   8587   -971   3384   -170       C  
ATOM   1369  O   ILE A 156      76.283  98.060 -29.589  1.00 87.17           O  
ANISOU 1369  O   ILE A 156    15379   9369   8374   -668   3559    -93       O  
ATOM   1370  CB  ILE A 156      76.032  96.382 -26.711  1.00 86.52           C  
ANISOU 1370  CB  ILE A 156    14154  10508   8211   -924   2853   -458       C  
ATOM   1371  CG1 ILE A 156      75.106  95.319 -26.122  1.00 81.51           C  
ANISOU 1371  CG1 ILE A 156    13177  10322   7470   -589   2561   -417       C  
ATOM   1372  CG2 ILE A 156      75.445  97.773 -26.502  1.00 91.50           C  
ANISOU 1372  CG2 ILE A 156    15399  10599   8768   -883   3089   -695       C  
ATOM   1373  CD1 ILE A 156      74.731  95.562 -24.686  1.00 76.03           C  
ANISOU 1373  CD1 ILE A 156    12484   9818   6586   -782   2464   -702       C  
ATOM   1374  N   HIS A 157      78.243  97.395 -28.697  1.00 93.20           N  
ANISOU 1374  N   HIS A 157    15316  10702   9393  -1548   3496   -236       N  
ATOM   1375  CA  HIS A 157      79.031  98.459 -29.318  1.00 97.07           C  
ANISOU 1375  CA  HIS A 157    16205  10690   9987  -1928   3905   -248       C  
ATOM   1376  C   HIS A 157      78.916  98.452 -30.844  1.00100.22           C  
ANISOU 1376  C   HIS A 157    16986  10770  10323  -1625   4195     61       C  
ATOM   1377  O   HIS A 157      78.915  99.505 -31.479  1.00105.00           O  
ANISOU 1377  O   HIS A 157    18227  10793  10874  -1681   4524    123       O  
ATOM   1378  CB  HIS A 157      80.498  98.347 -28.895  1.00100.87           C  
ANISOU 1378  CB  HIS A 157    16158  11432  10737  -2606   3939   -356       C  
ATOM   1379  CG  HIS A 157      81.451  99.037 -29.821  1.00112.54           C  
ANISOU 1379  CG  HIS A 157    17862  12505  12395  -2992   4425   -285       C  
ATOM   1380  ND1 HIS A 157      81.391 100.389 -30.083  1.00119.75           N  
ANISOU 1380  ND1 HIS A 157    19483  12758  13260  -3195   4773   -367       N  
ATOM   1381  CD2 HIS A 157      82.490  98.560 -30.548  1.00114.00           C  
ANISOU 1381  CD2 HIS A 157    17665  12821  12828  -3223   4676   -142       C  
ATOM   1382  CE1 HIS A 157      82.350 100.715 -30.931  1.00124.92           C  
ANISOU 1382  CE1 HIS A 157    20204  13168  14093  -3572   5215   -256       C  
ATOM   1383  NE2 HIS A 157      83.031  99.623 -31.228  1.00121.98           N  
ANISOU 1383  NE2 HIS A 157    19157  13286  13905  -3596   5183   -135       N  
ATOM   1384  N   ASP A 158      78.820  97.262 -31.427  1.00 97.68           N  
ANISOU 1384  N   ASP A 158    16327  10806   9979  -1322   4078    254       N  
ATOM   1385  CA  ASP A 158      78.649  97.136 -32.870  1.00 99.19           C  
ANISOU 1385  CA  ASP A 158    16915  10765  10008  -1041   4314    521       C  
ATOM   1386  C   ASP A 158      77.184  97.307 -33.260  1.00 97.21           C  
ANISOU 1386  C   ASP A 158    17145  10319   9471   -417   4094    646       C  
ATOM   1387  O   ASP A 158      76.852  98.121 -34.121  1.00101.83           O  
ANISOU 1387  O   ASP A 158    18404  10416   9870   -254   4278    823       O  
ATOM   1388  CB  ASP A 158      79.171  95.785 -33.362  1.00 83.10           C  
ANISOU 1388  CB  ASP A 158    14349   9156   8068   -999   4317    620       C  
ATOM   1389  CG  ASP A 158      80.681  95.658 -33.242  1.00 95.11           C  
ANISOU 1389  CG  ASP A 158    15376  10816   9947  -1560   4603    548       C  
ATOM   1390  OD1 ASP A 158      81.357  96.689 -33.044  1.00 95.16           O  
ANISOU 1390  OD1 ASP A 158    15546  10536  10074  -2029   4859    451       O  
ATOM   1391  OD2 ASP A 158      81.196  94.526 -33.363  1.00 84.28           O  
ANISOU 1391  OD2 ASP A 158    13430   9814   8779  -1534   4584    583       O  
TER    1392      ASP A 158                                                      
ATOM   1393  N   SER B  -1      48.972  73.095 -16.856  1.00108.72           N  
ANISOU 1393  N   SER B  -1    15896  10770  14644  -2807  -2301  -3585       N  
ATOM   1394  CA  SER B  -1      48.644  74.191 -15.950  1.00109.34           C  
ANISOU 1394  CA  SER B  -1    15570  11122  14851  -2681  -2414  -3060       C  
ATOM   1395  C   SER B  -1      48.179  73.682 -14.583  1.00113.07           C  
ANISOU 1395  C   SER B  -1    15838  11197  15926  -2803  -2243  -2720       C  
ATOM   1396  O   SER B  -1      48.938  73.033 -13.863  1.00111.87           O  
ANISOU 1396  O   SER B  -1    15950  10567  15989  -2582  -1895  -2649       O  
ATOM   1397  CB  SER B  -1      47.585  75.105 -16.570  1.00112.31           C  
ANISOU 1397  CB  SER B  -1    15548  12098  15027  -2896  -2867  -2961       C  
ATOM   1398  OG  SER B  -1      47.331  76.223 -15.738  1.00108.29           O  
ANISOU 1398  OG  SER B  -1    14628  11848  14670  -2706  -2941  -2490       O  
ATOM   1399  N   GLY B   0      46.929  73.971 -14.234  1.00115.69           N  
ANISOU 1399  N   GLY B   0    15675  11766  16517  -3134  -2461  -2485       N  
ATOM   1400  CA  GLY B   0      46.403  73.613 -12.928  1.00111.99           C  
ANISOU 1400  CA  GLY B   0    14941  11041  16569  -3285  -2249  -2114       C  
ATOM   1401  C   GLY B   0      46.462  74.784 -11.962  1.00101.67           C  
ANISOU 1401  C   GLY B   0    13229  10029  15374  -2987  -2194  -1662       C  
ATOM   1402  O   GLY B   0      46.200  74.632 -10.766  1.00 95.45           O  
ANISOU 1402  O   GLY B   0    12221   9090  14956  -3030  -1932  -1307       O  
ATOM   1403  N   LEU B   1      46.816  75.957 -12.486  1.00 92.45           N  
ANISOU 1403  N   LEU B   1    11983   9286  13858  -2695  -2406  -1674       N  
ATOM   1404  CA  LEU B   1      46.920  77.167 -11.676  1.00 79.86           C  
ANISOU 1404  CA  LEU B   1    10025   8044  12275  -2344  -2273  -1281       C  
ATOM   1405  C   LEU B   1      46.018  78.293 -12.165  1.00 76.78           C  
ANISOU 1405  C   LEU B   1     9162   8199  11813  -2372  -2654  -1190       C  
ATOM   1406  O   LEU B   1      46.046  78.659 -13.338  1.00 82.90           O  
ANISOU 1406  O   LEU B   1    10089   9205  12205  -2372  -3005  -1396       O  
ATOM   1407  CB  LEU B   1      48.362  77.695 -11.654  1.00 71.00           C  
ANISOU 1407  CB  LEU B   1     9253   6973  10752  -1817  -2012  -1268       C  
ATOM   1408  CG  LEU B   1      49.405  76.975 -10.804  1.00 65.67           C  
ANISOU 1408  CG  LEU B   1     8888   5900  10165  -1562  -1584  -1188       C  
ATOM   1409  CD1 LEU B   1      50.689  77.783 -10.767  1.00 65.55           C  
ANISOU 1409  CD1 LEU B   1     9013   6120   9773  -1067  -1385  -1145       C  
ATOM   1410  CD2 LEU B   1      48.888  76.729  -9.405  1.00 59.95           C  
ANISOU 1410  CD2 LEU B   1     7887   5057   9836  -1639  -1326   -794       C  
ATOM   1411  N   ASN B   2      45.239  78.859 -11.249  1.00 73.38           N  
ANISOU 1411  N   ASN B   2     8174   7993  11714  -2341  -2539   -858       N  
ATOM   1412  CA  ASN B   2      44.549  80.115 -11.513  1.00 72.42           C  
ANISOU 1412  CA  ASN B   2     7589   8361  11567  -2174  -2817   -705       C  
ATOM   1413  C   ASN B   2      45.467  81.273 -11.136  1.00 63.86           C  
ANISOU 1413  C   ASN B   2     6648   7420  10194  -1634  -2562   -511       C  
ATOM   1414  O   ASN B   2      45.807  81.440  -9.967  1.00 54.82           O  
ANISOU 1414  O   ASN B   2     5439   6215   9174  -1433  -2122   -309       O  
ATOM   1415  CB  ASN B   2      43.243  80.191 -10.716  1.00 81.42           C  
ANISOU 1415  CB  ASN B   2     8054   9708  13175  -2326  -2708   -488       C  
ATOM   1416  CG  ASN B   2      42.489  78.863 -10.693  1.00 97.91           C  
ANISOU 1416  CG  ASN B   2    10094  11604  15502  -2850  -2661   -623       C  
ATOM   1417  OD1 ASN B   2      42.462  78.129 -11.683  1.00105.63           O  
ANISOU 1417  OD1 ASN B   2    11378  12466  16289  -3122  -2917   -927       O  
ATOM   1418  ND2 ASN B   2      41.880  78.549  -9.554  1.00103.18           N  
ANISOU 1418  ND2 ASN B   2    10405  12250  16550  -3008  -2291   -408       N  
ATOM   1419  N   ILE B   3      45.882  82.059 -12.125  1.00 50.70           N  
ANISOU 1419  N   ILE B   3     5208   5943   8112  -1442  -2838   -573       N  
ATOM   1420  CA  ILE B   3      46.769  83.195 -11.877  1.00 48.45           C  
ANISOU 1420  CA  ILE B   3     5087   5764   7557  -1007  -2617   -406       C  
ATOM   1421  C   ILE B   3      46.078  84.489 -12.263  1.00 49.03           C  
ANISOU 1421  C   ILE B   3     4858   6141   7631   -813  -2936   -209       C  
ATOM   1422  O   ILE B   3      45.499  84.576 -13.331  1.00 51.59           O  
ANISOU 1422  O   ILE B   3     5153   6632   7818   -945  -3422   -263       O  
ATOM   1423  CB  ILE B   3      48.056  83.086 -12.706  1.00 51.10           C  
ANISOU 1423  CB  ILE B   3     6023   6022   7370   -928  -2580   -605       C  
ATOM   1424  CG1 ILE B   3      48.724  81.730 -12.471  1.00 58.64           C  
ANISOU 1424  CG1 ILE B   3     7288   6630   8363  -1059  -2316   -836       C  
ATOM   1425  CG2 ILE B   3      49.010  84.247 -12.381  1.00 43.93           C  
ANISOU 1425  CG2 ILE B   3     5248   5218   6224   -559  -2320   -429       C  
ATOM   1426  CD1 ILE B   3      49.899  81.459 -13.395  1.00 56.52           C  
ANISOU 1426  CD1 ILE B   3     7552   6302   7621   -989  -2265  -1118       C  
ATOM   1427  N   LYS B   4      46.133  85.490 -11.396  1.00 51.84           N  
ANISOU 1427  N   LYS B   4     5015   6554   8128   -483  -2670     15       N  
ATOM   1428  CA  LYS B   4      45.628  86.803 -11.759  1.00 51.16           C  
ANISOU 1428  CA  LYS B   4     4731   6651   8054   -210  -2938    213       C  
ATOM   1429  C   LYS B   4      46.752  87.814 -11.609  1.00 45.35           C  
ANISOU 1429  C   LYS B   4     4385   5834   7011     89  -2682    308       C  
ATOM   1430  O   LYS B   4      47.434  87.842 -10.589  1.00 47.35           O  
ANISOU 1430  O   LYS B   4     4710   5981   7301    190  -2223    297       O  
ATOM   1431  CB  LYS B   4      44.425  87.188 -10.896  1.00 60.84           C  
ANISOU 1431  CB  LYS B   4     5354   8000   9763    -82  -2788    345       C  
ATOM   1432  CG  LYS B   4      43.207  86.306 -11.111  1.00 68.60           C  
ANISOU 1432  CG  LYS B   4     5942   9124  10998   -405  -2967    260       C  
ATOM   1433  CD  LYS B   4      42.027  86.732 -10.247  1.00 81.94           C  
ANISOU 1433  CD  LYS B   4     7041  10995  13096   -260  -2739    365       C  
ATOM   1434  CE  LYS B   4      42.292  86.492  -8.767  1.00 88.76           C  
ANISOU 1434  CE  LYS B   4     7770  11753  14202   -247  -2180    395       C  
ATOM   1435  NZ  LYS B   4      41.042  86.636  -7.958  1.00 95.77           N  
ANISOU 1435  NZ  LYS B   4     8091  12867  15431   -214  -1925    434       N  
ATOM   1436  N   GLU B   5      46.966  88.628 -12.638  1.00 45.16           N  
ANISOU 1436  N   GLU B   5     4632   5869   6658    190  -2993    411       N  
ATOM   1437  CA  GLU B   5      48.023  89.634 -12.572  1.00 51.42           C  
ANISOU 1437  CA  GLU B   5     5801   6563   7173    395  -2752    514       C  
ATOM   1438  C   GLU B   5      47.403  91.024 -12.588  1.00 49.99           C  
ANISOU 1438  C   GLU B   5     5488   6362   7144    692  -2835    764       C  
ATOM   1439  O   GLU B   5      46.503  91.296 -13.370  1.00 49.18           O  
ANISOU 1439  O   GLU B   5     5271   6382   7033    717  -3137    865       O  
ATOM   1440  CB  GLU B   5      48.998  89.475 -13.747  1.00 56.34           C  
ANISOU 1440  CB  GLU B   5     6977   7226   7204    228  -2852    433       C  
ATOM   1441  CG  GLU B   5      50.186  90.436 -13.718  1.00 54.55           C  
ANISOU 1441  CG  GLU B   5     7123   6918   6685    340  -2560    530       C  
ATOM   1442  CD  GLU B   5      51.058  90.360 -14.974  1.00 54.96           C  
ANISOU 1442  CD  GLU B   5     7681   7075   6125    154  -2629    475       C  
ATOM   1443  OE1 GLU B   5      52.029  91.138 -15.070  1.00 58.30           O  
ANISOU 1443  OE1 GLU B   5     8396   7464   6293    172  -2389    567       O  
ATOM   1444  OE2 GLU B   5      50.783  89.527 -15.861  1.00 56.78           O  
ANISOU 1444  OE2 GLU B   5     8023   7436   6116    -42  -2899    317       O  
ATOM   1445  N  AASN B   6      47.891  91.897 -11.709  0.52 51.21           N  
ANISOU 1445  N  AASN B   6     5684   6352   7420    917  -2507    828       N  
ATOM   1446  N  BASN B   6      47.873  91.904 -11.715  0.48 51.23           N  
ANISOU 1446  N  BASN B   6     5683   6356   7425    919  -2510    830       N  
ATOM   1447  CA AASN B   6      47.436  93.285 -11.666  0.52 52.75           C  
ANISOU 1447  CA AASN B   6     5859   6438   7746   1205  -2477   1009       C  
ATOM   1448  CA BASN B   6      47.463  93.295 -11.819  0.48 53.21           C  
ANISOU 1448  CA BASN B   6     5955   6501   7760   1192  -2516   1023       C  
ATOM   1449  C  AASN B   6      48.608  94.259 -11.543  0.52 48.40           C  
ANISOU 1449  C  AASN B   6     5751   5650   6988   1277  -2277   1084       C  
ATOM   1450  C  BASN B   6      48.619  94.246 -11.598  0.48 48.83           C  
ANISOU 1450  C  BASN B   6     5818   5709   7027   1269  -2290   1088       C  
ATOM   1451  O  AASN B   6      49.650  93.919 -10.994  0.52 46.00           O  
ANISOU 1451  O  AASN B   6     5617   5310   6552   1160  -2006    945       O  
ATOM   1452  O  BASN B   6      49.645  93.888 -11.031  0.48 46.06           O  
ANISOU 1452  O  BASN B   6     5626   5323   6550   1153  -2017    945       O  
ATOM   1453  CB AASN B   6      46.438  93.499 -10.522  0.52 53.51           C  
ANISOU 1453  CB AASN B   6     5463   6553   8315   1418  -2235    955       C  
ATOM   1454  CB BASN B   6      46.294  93.622 -10.888  0.48 54.54           C  
ANISOU 1454  CB BASN B   6     5621   6698   8403   1428  -2354   1005       C  
ATOM   1455  CG AASN B   6      45.095  92.822 -10.776  0.52 56.30           C  
ANISOU 1455  CG AASN B   6     5346   7148   8899   1354  -2469    937       C  
ATOM   1456  CG BASN B   6      46.702  93.670  -9.438  0.48 52.04           C  
ANISOU 1456  CG BASN B   6     5208   6287   8276   1506  -1874    858       C  
ATOM   1457  OD1AASN B   6      44.861  91.691 -10.344  0.52 51.08           O  
ANISOU 1457  OD1AASN B   6     4428   6601   8379   1130  -2396    800       O  
ATOM   1458  OD1BASN B   6      46.658  92.660  -8.744  0.48 45.07           O  
ANISOU 1458  OD1BASN B   6     4100   5515   7510   1353  -1699    724       O  
ATOM   1459  ND2AASN B   6      44.207  93.517 -11.470  0.52 59.89           N  
ANISOU 1459  ND2AASN B   6     5676   7673   9407   1543  -2755   1090       N  
ATOM   1460  ND2BASN B   6      47.087  94.852  -8.966  0.48 59.22           N  
ANISOU 1460  ND2BASN B   6     6313   6980   9209   1728  -1656    882       N  
ATOM   1461  N   ASP B   7      48.441  95.468 -12.069  1.00 50.79           N  
ANISOU 1461  N   ASP B   7     6249   5799   7251   1440  -2376   1297       N  
ATOM   1462  CA  ASP B   7      49.502  96.452 -12.033  1.00 46.84           C  
ANISOU 1462  CA  ASP B   7     6196   5024   6578   1439  -2200   1390       C  
ATOM   1463  C   ASP B   7      49.532  97.163 -10.680  1.00 49.80           C  
ANISOU 1463  C   ASP B   7     6445   5158   7318   1655  -1836   1269       C  
ATOM   1464  O   ASP B   7      48.484  97.455 -10.105  1.00 54.39           O  
ANISOU 1464  O   ASP B   7     6669   5742   8253   1911  -1765   1229       O  
ATOM   1465  CB  ASP B   7      49.258  97.470 -13.151  1.00 52.01           C  
ANISOU 1465  CB  ASP B   7     7132   5562   7067   1511  -2441   1697       C  
ATOM   1466  CG  ASP B   7      50.348  98.501 -13.237  1.00 57.23           C  
ANISOU 1466  CG  ASP B   7     8295   5907   7542   1422  -2254   1828       C  
ATOM   1467  OD1 ASP B   7      51.534  98.117 -13.311  1.00 55.96           O  
ANISOU 1467  OD1 ASP B   7     8434   5791   7036   1128  -2105   1745       O  
ATOM   1468  OD2 ASP B   7      50.014  99.699 -13.214  1.00 64.42           O  
ANISOU 1468  OD2 ASP B   7     9302   6516   8659   1639  -2234   2008       O  
ATOM   1469  N   LEU B   8      50.733  97.431 -10.175  1.00 51.70           N  
ANISOU 1469  N   LEU B   8     6992   5231   7420   1526  -1577   1168       N  
ATOM   1470  CA  LEU B   8      50.893  98.260  -8.985  1.00 49.90           C  
ANISOU 1470  CA  LEU B   8     6753   4755   7451   1671  -1225   1004       C  
ATOM   1471  C   LEU B   8      51.723  99.493  -9.347  1.00 48.25           C  
ANISOU 1471  C   LEU B   8     7062   4173   7098   1571  -1166   1129       C  
ATOM   1472  O   LEU B   8      52.955  99.452  -9.279  1.00 49.26           O  
ANISOU 1472  O   LEU B   8     7436   4368   6911   1231   -937   1015       O  
ATOM   1473  CB  LEU B   8      51.580  97.490  -7.858  1.00 40.47           C  
ANISOU 1473  CB  LEU B   8     5416   3805   6157   1488   -838    684       C  
ATOM   1474  CG  LEU B   8      51.019  96.117  -7.451  1.00 45.61           C  
ANISOU 1474  CG  LEU B   8     5652   4796   6882   1472   -823    581       C  
ATOM   1475  CD1 LEU B   8      51.971  95.393  -6.496  1.00 38.73           C  
ANISOU 1475  CD1 LEU B   8     4780   4129   5806   1274   -489    358       C  
ATOM   1476  CD2 LEU B   8      49.623  96.269  -6.844  1.00 54.79           C  
ANISOU 1476  CD2 LEU B   8     6376   5938   8506   1786   -821    574       C  
ATOM   1477  N   PRO B   9      51.051 100.582  -9.731  1.00 53.26           N  
ANISOU 1477  N   PRO B   9     7792   4496   7946   1807  -1290   1345       N  
ATOM   1478  CA  PRO B   9      51.710 101.835 -10.124  1.00 56.34           C  
ANISOU 1478  CA  PRO B   9     8681   4461   8263   1694  -1230   1515       C  
ATOM   1479  C   PRO B   9      52.793 102.254  -9.129  1.00 60.98           C  
ANISOU 1479  C   PRO B   9     9540   4784   8844   1492   -882   1227       C  
ATOM   1480  O   PRO B   9      52.575 102.229  -7.910  1.00 53.63           O  
ANISOU 1480  O   PRO B   9     8360   3862   8155   1637   -627    889       O  
ATOM   1481  CB  PRO B   9      50.562 102.831 -10.113  1.00 62.49           C  
ANISOU 1481  CB  PRO B   9     9329   4985   9431   2102  -1263   1653       C  
ATOM   1482  CG  PRO B   9      49.382 102.012 -10.466  1.00 63.28           C  
ANISOU 1482  CG  PRO B   9     8971   5497   9577   2322  -1517   1715       C  
ATOM   1483  CD  PRO B   9      49.583 100.723  -9.742  1.00 54.42           C  
ANISOU 1483  CD  PRO B   9     7539   4734   8404   2172  -1403   1416       C  
ATOM   1484  N   GLY B  10      53.969 102.588  -9.647  1.00 59.68           N  
ANISOU 1484  N   GLY B  10     9789   4552   8333   1067   -784   1312       N  
ATOM   1485  CA  GLY B  10      55.075 103.007  -8.808  1.00 60.90           C  
ANISOU 1485  CA  GLY B  10    10083   4631   8426    732   -412   1003       C  
ATOM   1486  C   GLY B  10      55.766 101.888  -8.050  1.00 57.52           C  
ANISOU 1486  C   GLY B  10     9302   4769   7784    528   -197    654       C  
ATOM   1487  O   GLY B  10      56.768 102.126  -7.378  1.00 57.45           O  
ANISOU 1487  O   GLY B  10     9348   4811   7671    222     56    396       O  
ATOM   1488  N   ILE B  11      55.234 100.673  -8.148  1.00 44.75           N  
ANISOU 1488  N   ILE B  11     7326   3561   6114    688   -323    654       N  
ATOM   1489  CA  ILE B  11      55.791  99.516  -7.445  1.00 47.27           C  
ANISOU 1489  CA  ILE B  11     7333   4361   6266    563   -154    388       C  
ATOM   1490  C   ILE B  11      56.254  98.390  -8.386  1.00 46.29           C  
ANISOU 1490  C   ILE B  11     7158   4617   5814    396   -257    482       C  
ATOM   1491  O   ILE B  11      57.401  97.947  -8.319  1.00 53.97           O  
ANISOU 1491  O   ILE B  11     8108   5862   6535    137    -86    344       O  
ATOM   1492  CB  ILE B  11      54.762  98.908  -6.454  1.00 58.40           C  
ANISOU 1492  CB  ILE B  11     8354   5897   7938    885   -121    238       C  
ATOM   1493  CG1 ILE B  11      54.419  99.895  -5.338  1.00 66.96           C  
ANISOU 1493  CG1 ILE B  11     9465   6688   9289   1052     82     26       C  
ATOM   1494  CG2 ILE B  11      55.277  97.597  -5.873  1.00 48.48           C  
ANISOU 1494  CG2 ILE B  11     6836   5095   6488    770     -2     73       C  
ATOM   1495  CD1 ILE B  11      53.471  99.323  -4.304  1.00 66.44           C  
ANISOU 1495  CD1 ILE B  11     9014   6808   9422   1325    207   -135       C  
ATOM   1496  N   GLY B  12      55.361  97.927  -9.257  1.00 47.24           N  
ANISOU 1496  N   GLY B  12     7238   4765   5945    555   -542    685       N  
ATOM   1497  CA  GLY B  12      55.627  96.739 -10.062  1.00 40.96           C  
ANISOU 1497  CA  GLY B  12     6394   4310   4859    430   -638    687       C  
ATOM   1498  C   GLY B  12      54.333  96.002 -10.384  1.00 37.63           C  
ANISOU 1498  C   GLY B  12     5747   3952   4599    647   -941    765       C  
ATOM   1499  O   GLY B  12      53.349  96.630 -10.779  1.00 37.85           O  
ANISOU 1499  O   GLY B  12     5791   3780   4809    842  -1210    978       O  
ATOM   1500  N   LYS B  13      54.316  94.685 -10.162  1.00 36.93           N  
ANISOU 1500  N   LYS B  13     5425   4119   4487    620   -910    595       N  
ATOM   1501  CA  LYS B  13      53.136  93.872 -10.467  1.00 37.14           C  
ANISOU 1501  CA  LYS B  13     5216   4219   4677    724  -1191    631       C  
ATOM   1502  C   LYS B  13      52.800  92.946  -9.304  1.00 31.91           C  
ANISOU 1502  C   LYS B  13     4199   3651   4275    787  -1013    462       C  
ATOM   1503  O   LYS B  13      53.671  92.550  -8.536  1.00 34.81           O  
ANISOU 1503  O   LYS B  13     4563   4103   4561    726   -729    316       O  
ATOM   1504  CB  LYS B  13      53.390  93.001 -11.705  1.00 36.61           C  
ANISOU 1504  CB  LYS B  13     5331   4328   4252    533  -1380    604       C  
ATOM   1505  CG  LYS B  13      52.582  93.369 -12.975  1.00 56.87           C  
ANISOU 1505  CG  LYS B  13     8048   6883   6677    540  -1828    831       C  
ATOM   1506  CD  LYS B  13      52.784  94.796 -13.432  1.00 54.60           C  
ANISOU 1506  CD  LYS B  13     8076   6399   6269    583  -1890   1115       C  
ATOM   1507  CE  LYS B  13      52.589  94.944 -14.942  1.00 50.21           C  
ANISOU 1507  CE  LYS B  13     7860   5933   5284    473  -2271   1344       C  
ATOM   1508  NZ  LYS B  13      51.314  95.648 -15.369  1.00 54.80           N  
ANISOU 1508  NZ  LYS B  13     8274   6435   6113    694  -2593   1585       N  
ATOM   1509  N   LYS B  14      51.543  92.550  -9.222  1.00 36.46           N  
ANISOU 1509  N   LYS B  14     4466   4240   5145    887  -1198    509       N  
ATOM   1510  CA  LYS B  14      51.151  91.559  -8.234  1.00 36.82           C  
ANISOU 1510  CA  LYS B  14     4203   4376   5410    875  -1021    400       C  
ATOM   1511  C   LYS B  14      50.527  90.366  -8.946  1.00 31.48           C  
ANISOU 1511  C   LYS B  14     3415   3778   4770    715  -1279    377       C  
ATOM   1512  O   LYS B  14      49.682  90.549  -9.814  1.00 38.24           O  
ANISOU 1512  O   LYS B  14     4184   4654   5691    718  -1642    469       O  
ATOM   1513  CB  LYS B  14      50.123  92.179  -7.298  1.00 39.10           C  
ANISOU 1513  CB  LYS B  14     4148   4624   6085   1090   -914    439       C  
ATOM   1514  CG  LYS B  14      49.254  91.204  -6.539  1.00 44.48           C  
ANISOU 1514  CG  LYS B  14     4436   5426   7038   1044   -801    407       C  
ATOM   1515  CD  LYS B  14      48.566  91.950  -5.399  1.00 53.21           C  
ANISOU 1515  CD  LYS B  14     5252   6535   8430   1268   -525    385       C  
ATOM   1516  CE  LYS B  14      47.123  91.572  -5.258  1.00 63.71           C  
ANISOU 1516  CE  LYS B  14     6096   7994  10116   1282   -571    425       C  
ATOM   1517  NZ  LYS B  14      46.317  91.949  -6.453  1.00 61.14           N  
ANISOU 1517  NZ  LYS B  14     5685   7672   9875   1339   -995    522       N  
ATOM   1518  N   PHE B  15      50.940  89.161  -8.556  1.00 33.42           N  
ANISOU 1518  N   PHE B  15     3673   4046   4980    577  -1116    255       N  
ATOM   1519  CA  PHE B  15      50.364  87.923  -9.066  1.00 38.73           C  
ANISOU 1519  CA  PHE B  15     4269   4709   5738    379  -1310    183       C  
ATOM   1520  C   PHE B  15      49.669  87.193  -7.927  1.00 37.90           C  
ANISOU 1520  C   PHE B  15     3838   4582   5979    327  -1110    214       C  
ATOM   1521  O   PHE B  15      50.277  86.946  -6.890  1.00 39.72           O  
ANISOU 1521  O   PHE B  15     4116   4793   6184    381   -780    223       O  
ATOM   1522  CB  PHE B  15      51.466  87.017  -9.632  1.00 35.57           C  
ANISOU 1522  CB  PHE B  15     4224   4261   5030    261  -1257      9       C  
ATOM   1523  CG  PHE B  15      52.121  87.569 -10.873  1.00 37.48           C  
ANISOU 1523  CG  PHE B  15     4795   4575   4871    239  -1410    -37       C  
ATOM   1524  CD1 PHE B  15      53.097  88.544 -10.771  1.00 35.40           C  
ANISOU 1524  CD1 PHE B  15     4696   4361   4391    341  -1219     17       C  
ATOM   1525  CD2 PHE B  15      51.756  87.109 -12.130  1.00 44.65           C  
ANISOU 1525  CD2 PHE B  15     5859   5517   5588     68  -1736   -139       C  
ATOM   1526  CE1 PHE B  15      53.704  89.062 -11.911  1.00 38.00           C  
ANISOU 1526  CE1 PHE B  15     5341   4769   4327    267  -1306     15       C  
ATOM   1527  CE2 PHE B  15      52.361  87.617 -13.273  1.00 49.28           C  
ANISOU 1527  CE2 PHE B  15     6792   6213   5721     23  -1841   -158       C  
ATOM   1528  CZ  PHE B  15      53.341  88.597 -13.158  1.00 38.54           C  
ANISOU 1528  CZ  PHE B  15     5591   4896   4156    120  -1601    -58       C  
ATOM   1529  N   GLU B  16      48.403  86.867  -8.127  1.00 42.00           N  
ANISOU 1529  N   GLU B  16     4018   5138   6800    201  -1318    247       N  
ATOM   1530  CA  GLU B  16      47.644  86.059  -7.175  1.00 45.02           C  
ANISOU 1530  CA  GLU B  16     4075   5511   7518     53  -1115    293       C  
ATOM   1531  C   GLU B  16      47.403  84.679  -7.765  1.00 43.06           C  
ANISOU 1531  C   GLU B  16     3901   5121   7337   -291  -1296    185       C  
ATOM   1532  O   GLU B  16      46.710  84.540  -8.770  1.00 49.24           O  
ANISOU 1532  O   GLU B  16     4573   5955   8181   -460  -1692    107       O  
ATOM   1533  CB  GLU B  16      46.314  86.737  -6.847  1.00 42.12           C  
ANISOU 1533  CB  GLU B  16     3163   5315   7526    136  -1154    391       C  
ATOM   1534  CG  GLU B  16      46.506  88.067  -6.155  1.00 53.77           C  
ANISOU 1534  CG  GLU B  16     4600   6849   8981    491   -920    444       C  
ATOM   1535  CD  GLU B  16      45.212  88.805  -5.906  1.00 69.59           C  
ANISOU 1535  CD  GLU B  16     6077   8999  11366    665   -935    499       C  
ATOM   1536  OE1 GLU B  16      44.348  88.827  -6.808  1.00 80.38           O  
ANISOU 1536  OE1 GLU B  16     7261  10451  12830    613  -1300    514       O  
ATOM   1537  OE2 GLU B  16      45.064  89.367  -4.803  1.00 73.47           O  
ANISOU 1537  OE2 GLU B  16     6489   9548  11879    835   -530    475       O  
ATOM   1538  N   ILE B  17      47.986  83.665  -7.131  1.00 46.46           N  
ANISOU 1538  N   ILE B  17     4545   5356   7754   -390  -1029    180       N  
ATOM   1539  CA  ILE B  17      47.995  82.302  -7.650  1.00 43.18           C  
ANISOU 1539  CA  ILE B  17     4336   4674   7397   -689  -1148     42       C  
ATOM   1540  C   ILE B  17      47.159  81.370  -6.773  1.00 48.22           C  
ANISOU 1540  C   ILE B  17     4733   5174   8415   -980   -957    176       C  
ATOM   1541  O   ILE B  17      47.301  81.388  -5.550  1.00 48.12           O  
ANISOU 1541  O   ILE B  17     4662   5179   8441   -884   -587    382       O  
ATOM   1542  CB  ILE B  17      49.439  81.771  -7.668  1.00 42.07           C  
ANISOU 1542  CB  ILE B  17     4687   4324   6973   -532   -984    -51       C  
ATOM   1543  CG1 ILE B  17      50.329  82.737  -8.456  1.00 48.91           C  
ANISOU 1543  CG1 ILE B  17     5761   5369   7453   -293  -1085   -161       C  
ATOM   1544  CG2 ILE B  17      49.495  80.364  -8.234  1.00 43.13           C  
ANISOU 1544  CG2 ILE B  17     5099   4094   7194   -783  -1082   -244       C  
ATOM   1545  CD1 ILE B  17      51.792  82.690  -8.068  1.00 52.93           C  
ANISOU 1545  CD1 ILE B  17     6550   5842   7719    -41   -821   -181       C  
ATOM   1546  N   GLU B  18      46.279  80.583  -7.389  1.00 48.35           N  
ANISOU 1546  N   GLU B  18     4614   5076   8681  -1375  -1208     61       N  
ATOM   1547  CA  GLU B  18      45.554  79.541  -6.667  1.00 49.81           C  
ANISOU 1547  CA  GLU B  18     4633   5056   9237  -1757  -1014    183       C  
ATOM   1548  C   GLU B  18      45.775  78.176  -7.317  1.00 53.06           C  
ANISOU 1548  C   GLU B  18     5452   4996   9711  -2088  -1162    -26       C  
ATOM   1549  O   GLU B  18      45.594  78.018  -8.525  1.00 65.10           O  
ANISOU 1549  O   GLU B  18     7065   6503  11165  -2257  -1562   -324       O  
ATOM   1550  CB  GLU B  18      44.057  79.858  -6.568  1.00 53.92           C  
ANISOU 1550  CB  GLU B  18     4467   5881  10139  -2018  -1111    251       C  
ATOM   1551  CG  GLU B  18      43.226  78.702  -6.034  1.00 82.02           C  
ANISOU 1551  CG  GLU B  18     7830   9231  14104  -2553   -940    348       C  
ATOM   1552  CD  GLU B  18      42.029  79.162  -5.225  1.00 86.90           C  
ANISOU 1552  CD  GLU B  18     7791  10254  14973  -2624   -688    527       C  
ATOM   1553  OE1 GLU B  18      42.076  80.289  -4.675  1.00 75.46           O  
ANISOU 1553  OE1 GLU B  18     6094   9123  13455  -2224   -503    636       O  
ATOM   1554  OE2 GLU B  18      41.042  78.396  -5.138  1.00 96.18           O  
ANISOU 1554  OE2 GLU B  18     8761  11449  16333  -3046   -637    514       O  
ATOM   1555  N   THR B  19      46.157  77.189  -6.508  1.00 54.99           N  
ANISOU 1555  N   THR B  19     5981   4841  10071  -2175   -847    130       N  
ATOM   1556  CA  THR B  19      46.514  75.860  -7.016  1.00 57.71           C  
ANISOU 1556  CA  THR B  19     6809   4609  10509  -2409   -926    -70       C  
ATOM   1557  C   THR B  19      45.309  74.982  -7.343  1.00 71.28           C  
ANISOU 1557  C   THR B  19     8337   6104  12642  -3065  -1099   -178       C  
ATOM   1558  O   THR B  19      44.178  75.321  -7.007  1.00 71.51           O  
ANISOU 1558  O   THR B  19     7820   6508  12843  -3299  -1071    -39       O  
ATOM   1559  CB  THR B  19      47.415  75.100  -6.027  1.00 70.51           C  
ANISOU 1559  CB  THR B  19     8849   5810  12131  -2206   -558    188       C  
ATOM   1560  OG1 THR B  19      46.667  74.773  -4.847  1.00 60.22           O  
ANISOU 1560  OG1 THR B  19     7316   4470  11096  -2485   -257    582       O  
ATOM   1561  CG2 THR B  19      48.625  75.947  -5.654  1.00 70.83           C  
ANISOU 1561  CG2 THR B  19     9014   6123  11777  -1603   -418    280       C  
ATOM   1562  N   ARG B  20      45.575  73.849  -7.992  1.00 77.80           N  
ANISOU 1562  N   ARG B  20     9663   6473  13423  -3237  -1173   -460       N  
ATOM   1563  CA  ARG B  20      44.545  72.864  -8.311  1.00 89.84           C  
ANISOU 1563  CA  ARG B  20    11159   7854  15123  -3800  -1228   -613       C  
ATOM   1564  C   ARG B  20      43.871  72.410  -7.026  1.00 94.23           C  
ANISOU 1564  C   ARG B  20    11512   8333  15957  -4072   -849   -195       C  
ATOM   1565  O   ARG B  20      42.655  72.247  -6.970  1.00101.82           O  
ANISOU 1565  O   ARG B  20    12059   9526  17101  -4530   -863   -188       O  
ATOM   1566  CB  ARG B  20      45.168  71.667  -9.042  1.00 91.62           C  
ANISOU 1566  CB  ARG B  20    12061   7494  15258  -3870  -1246   -973       C  
ATOM   1567  CG  ARG B  20      44.257  70.455  -9.202  1.00102.39           C  
ANISOU 1567  CG  ARG B  20    13520   8539  16843  -4488  -1207  -1121       C  
ATOM   1568  CD  ARG B  20      43.106  70.738 -10.152  1.00101.68           C  
ANISOU 1568  CD  ARG B  20    12975   8921  16738  -4911  -1579  -1433       C  
ATOM   1569  NE  ARG B  20      42.371  69.524 -10.490  1.00117.05           N  
ANISOU 1569  NE  ARG B  20    15069  10527  18878  -5526  -1558  -1698       N  
ATOM   1570  CZ  ARG B  20      41.344  69.051  -9.790  1.00120.53           C  
ANISOU 1570  CZ  ARG B  20    15211  10956  19628  -6033  -1382  -1488       C  
ATOM   1571  NH1 ARG B  20      40.735  67.937 -10.173  1.00123.94           N  
ANISOU 1571  NH1 ARG B  20    15809  11039  20243  -6627  -1361  -1785       N  
ATOM   1572  NH2 ARG B  20      40.928  69.692  -8.706  1.00120.51           N  
ANISOU 1572  NH2 ARG B  20    14738  11300  19751  -5960  -1186  -1012       N  
ATOM   1573  N   SER B  21      44.679  72.236  -5.986  1.00 96.62           N  
ANISOU 1573  N   SER B  21    12105   8367  16240  -3775   -504    160       N  
ATOM   1574  CA  SER B  21      44.197  71.808  -4.678  1.00 97.62           C  
ANISOU 1574  CA  SER B  21    12153   8440  16497  -3985   -105    608       C  
ATOM   1575  C   SER B  21      43.787  73.005  -3.829  1.00 85.85           C  
ANISOU 1575  C   SER B  21    10064   7573  14980  -3822     89    902       C  
ATOM   1576  O   SER B  21      43.693  72.908  -2.606  1.00 77.93           O  
ANISOU 1576  O   SER B  21     9048   6625  13938  -3829    478   1299       O  
ATOM   1577  CB  SER B  21      45.286  71.008  -3.971  1.00 98.14           C  
ANISOU 1577  CB  SER B  21    12873   7954  16461  -3699    136    872       C  
ATOM   1578  OG  SER B  21      46.556  71.558  -4.274  1.00 73.49           O  
ANISOU 1578  OG  SER B  21     9968   4817  13139  -3101     32    773       O  
ATOM   1579  N   HIS B  22      43.581  74.136  -4.499  1.00 89.11           N  
ANISOU 1579  N   HIS B  22    10037   8455  15364  -3647   -181    690       N  
ATOM   1580  CA  HIS B  22      43.003  75.345  -3.907  1.00 93.26           C  
ANISOU 1580  CA  HIS B  22     9937   9603  15895  -3484    -34    858       C  
ATOM   1581  C   HIS B  22      43.886  76.125  -2.920  1.00 87.63           C  
ANISOU 1581  C   HIS B  22     9292   9020  14982  -3011    287   1154       C  
ATOM   1582  O   HIS B  22      43.376  76.942  -2.155  1.00 85.04           O  
ANISOU 1582  O   HIS B  22     8534   9160  14617  -2897    549   1308       O  
ATOM   1583  CB  HIS B  22      41.627  75.046  -3.290  1.00101.53           C  
ANISOU 1583  CB  HIS B  22    10532  10920  17124  -3919    205    984       C  
ATOM   1584  CG  HIS B  22      40.643  74.473  -4.262  1.00105.43           C  
ANISOU 1584  CG  HIS B  22    10827  11425  17807  -4402   -122    678       C  
ATOM   1585  ND1 HIS B  22      39.967  75.247  -5.181  1.00101.83           N  
ANISOU 1585  ND1 HIS B  22     9880  11423  17387  -4356   -512    417       N  
ATOM   1586  CD2 HIS B  22      40.220  73.200  -4.460  1.00113.39           C  
ANISOU 1586  CD2 HIS B  22    12083  12053  18950  -4947   -124    592       C  
ATOM   1587  CE1 HIS B  22      39.171  74.477  -5.903  1.00111.42           C  
ANISOU 1587  CE1 HIS B  22    11016  12585  18732  -4861   -748    174       C  
ATOM   1588  NE2 HIS B  22      39.306  73.230  -5.484  1.00113.26           N  
ANISOU 1588  NE2 HIS B  22    11690  12302  19042  -5251   -503    253       N  
ATOM   1589  N   GLU B  23      45.200  75.901  -2.959  1.00 70.56           N  
ANISOU 1589  N   GLU B  23     7718   6553  12539  -2647    268   1151       N  
ATOM   1590  CA  GLU B  23      46.131  76.647  -2.109  1.00 64.48           C  
ANISOU 1590  CA  GLU B  23     7095   6030  11372  -2125    503   1338       C  
ATOM   1591  C   GLU B  23      46.441  77.994  -2.758  1.00 55.55           C  
ANISOU 1591  C   GLU B  23     5778   5326  10002  -1733    279   1076       C  
ATOM   1592  O   GLU B  23      46.448  78.102  -3.982  1.00 56.35           O  
ANISOU 1592  O   GLU B  23     5901   5390  10117  -1750    -92    769       O  
ATOM   1593  CB  GLU B  23      47.434  75.865  -1.931  1.00 68.73           C  
ANISOU 1593  CB  GLU B  23     8270   6123  11722  -1861    529   1432       C  
ATOM   1594  CG  GLU B  23      47.255  74.427  -1.464  1.00 79.02           C  
ANISOU 1594  CG  GLU B  23     9904   6833  13288  -2211    687   1701       C  
ATOM   1595  CD  GLU B  23      47.170  74.310   0.039  1.00 95.27           C  
ANISOU 1595  CD  GLU B  23    11989   9001  15209  -2230   1098   2210       C  
ATOM   1596  OE1 GLU B  23      47.059  73.172   0.544  1.00111.90           O  
ANISOU 1596  OE1 GLU B  23    14452  10747  17319  -2438   1205   2424       O  
ATOM   1597  OE2 GLU B  23      47.217  75.357   0.717  1.00 94.05           O  
ANISOU 1597  OE2 GLU B  23    11572   9398  14765  -1988   1271   2299       O  
ATOM   1598  N   LYS B  24      46.709  79.015  -1.956  1.00 47.57           N  
ANISOU 1598  N   LYS B  24     4634   4698   8744  -1404    500   1194       N  
ATOM   1599  CA  LYS B  24      46.886  80.344  -2.539  1.00 46.77           C  
ANISOU 1599  CA  LYS B  24     4361   4934   8475  -1081    309    976       C  
ATOM   1600  C   LYS B  24      48.144  81.085  -2.094  1.00 42.88           C  
ANISOU 1600  C   LYS B  24     4146   4575   7570   -645    410    984       C  
ATOM   1601  O   LYS B  24      48.540  81.054  -0.929  1.00 49.67           O  
ANISOU 1601  O   LYS B  24     5114   5513   8246   -541    709   1193       O  
ATOM   1602  CB  LYS B  24      45.632  81.210  -2.359  1.00 62.83           C  
ANISOU 1602  CB  LYS B  24     5787   7344  10742  -1141    372    974       C  
ATOM   1603  CG  LYS B  24      45.089  81.278  -0.952  1.00 68.60           C  
ANISOU 1603  CG  LYS B  24     6270   8282  11511  -1208    862   1213       C  
ATOM   1604  CD  LYS B  24      43.719  81.955  -0.920  1.00 73.26           C  
ANISOU 1604  CD  LYS B  24     6168   9222  12444  -1284    932   1161       C  
ATOM   1605  CE  LYS B  24      42.648  81.067  -1.537  1.00 81.78           C  
ANISOU 1605  CE  LYS B  24     6909  10209  13956  -1776    740   1142       C  
ATOM   1606  NZ  LYS B  24      41.282  81.653  -1.432  1.00 76.80           N  
ANISOU 1606  NZ  LYS B  24     5719   9994  13467  -1764    781   1035       N  
ATOM   1607  N   MET B  25      48.778  81.734  -3.055  1.00 36.14           N  
ANISOU 1607  N   MET B  25     3415   3769   6548   -431    145    758       N  
ATOM   1608  CA  MET B  25      49.900  82.588  -2.762  1.00 35.26           C  
ANISOU 1608  CA  MET B  25     3485   3825   6089    -86    214    725       C  
ATOM   1609  C   MET B  25      49.810  83.858  -3.589  1.00 35.05           C  
ANISOU 1609  C   MET B  25     3334   3986   5999     55     12    548       C  
ATOM   1610  O   MET B  25      49.157  83.893  -4.633  1.00 42.62           O  
ANISOU 1610  O   MET B  25     4175   4914   7105    -68   -270    442       O  
ATOM   1611  CB  MET B  25      51.214  81.874  -3.065  1.00 40.77           C  
ANISOU 1611  CB  MET B  25     4589   4309   6593     46    150    674       C  
ATOM   1612  CG  MET B  25      51.168  81.066  -4.338  1.00 54.18           C  
ANISOU 1612  CG  MET B  25     6453   5721   8413   -106   -106    474       C  
ATOM   1613  SD  MET B  25      52.574  79.945  -4.436  1.00 84.75           S  
ANISOU 1613  SD  MET B  25    10763   9265  12173     93    -71    426       S  
ATOM   1614  CE  MET B  25      53.884  81.129  -4.486  1.00 30.74           C  
ANISOU 1614  CE  MET B  25     3935   2794   4952    445    -43    328       C  
ATOM   1615  N   THR B  26      50.487  84.885  -3.115  1.00 34.74           N  
ANISOU 1615  N   THR B  26     3351   4124   5724    294    134    530       N  
ATOM   1616  CA  THR B  26      50.527  86.166  -3.815  1.00 40.43           C  
ANISOU 1616  CA  THR B  26     4039   4947   6376    437    -26    409       C  
ATOM   1617  C   THR B  26      51.988  86.517  -3.971  1.00 35.91           C  
ANISOU 1617  C   THR B  26     3780   4399   5467    571    -17    324       C  
ATOM   1618  O   THR B  26      52.730  86.453  -3.003  1.00 36.50           O  
ANISOU 1618  O   THR B  26     3937   4556   5375    652    185    364       O  
ATOM   1619  CB  THR B  26      49.820  87.265  -3.007  1.00 43.09           C  
ANISOU 1619  CB  THR B  26     4106   5445   6823    571    163    433       C  
ATOM   1620  OG1 THR B  26      48.408  87.028  -3.003  1.00 43.47           O  
ANISOU 1620  OG1 THR B  26     3753   5530   7233    461    149    493       O  
ATOM   1621  CG2 THR B  26      50.097  88.638  -3.606  1.00 40.29           C  
ANISOU 1621  CG2 THR B  26     3832   5093   6384    755     25    339       C  
ATOM   1622  N   ILE B  27      52.433  86.840  -5.189  1.00 29.69           N  
ANISOU 1622  N   ILE B  27     3155   3576   4551    571   -237    215       N  
ATOM   1623  CA  ILE B  27      53.819  87.265  -5.373  1.00 32.72           C  
ANISOU 1623  CA  ILE B  27     3767   4031   4634    657   -183    127       C  
ATOM   1624  C   ILE B  27      53.809  88.737  -5.800  1.00 36.79           C  
ANISOU 1624  C   ILE B  27     4314   4592   5072    700   -247    111       C  
ATOM   1625  O   ILE B  27      53.116  89.101  -6.744  1.00 42.02           O  
ANISOU 1625  O   ILE B  27     4974   5194   5798    668   -474    140       O  
ATOM   1626  CB  ILE B  27      54.572  86.407  -6.436  1.00 31.59           C  
ANISOU 1626  CB  ILE B  27     3841   3816   4344    608   -291      2       C  
ATOM   1627  CG1 ILE B  27      54.711  84.953  -5.961  1.00 36.40           C  
ANISOU 1627  CG1 ILE B  27     4486   4275   5071    613   -213     20       C  
ATOM   1628  CG2 ILE B  27      55.963  86.991  -6.707  1.00 32.68           C  
ANISOU 1628  CG2 ILE B  27     4122   4102   4195    674   -198    -94       C  
ATOM   1629  CD1 ILE B  27      55.314  84.001  -6.985  1.00 38.87           C  
ANISOU 1629  CD1 ILE B  27     5021   4442   5305    602   -288   -166       C  
ATOM   1630  N   ILE B  28      54.544  89.587  -5.088  1.00 32.56           N  
ANISOU 1630  N   ILE B  28     3824   4143   4406    763    -75     77       N  
ATOM   1631  CA  ILE B  28      54.655  90.983  -5.490  1.00 39.99           C  
ANISOU 1631  CA  ILE B  28     4871   5031   5293    773   -114     64       C  
ATOM   1632  C   ILE B  28      56.006  91.142  -6.112  1.00 37.11           C  
ANISOU 1632  C   ILE B  28     4713   4746   4642    667    -92     -9       C  
ATOM   1633  O   ILE B  28      56.985  90.780  -5.494  1.00 34.13           O  
ANISOU 1633  O   ILE B  28     4310   4521   4138    659     52    -88       O  
ATOM   1634  CB  ILE B  28      54.595  91.946  -4.288  1.00 38.57           C  
ANISOU 1634  CB  ILE B  28     4635   4857   5164    854     88     10       C  
ATOM   1635  CG1 ILE B  28      53.325  91.717  -3.465  1.00 39.67           C  
ANISOU 1635  CG1 ILE B  28     4515   4995   5563    966    182     52       C  
ATOM   1636  CG2 ILE B  28      54.679  93.415  -4.777  1.00 37.18           C  
ANISOU 1636  CG2 ILE B  28     4635   4499   4993    859     41      0       C  
ATOM   1637  CD1 ILE B  28      52.072  92.001  -4.202  1.00 39.52           C  
ANISOU 1637  CD1 ILE B  28     4337   4845   5833   1052     -9    143       C  
ATOM   1638  N   ILE B  29      56.071  91.678  -7.329  1.00 30.28           N  
ANISOU 1638  N   ILE B  29     4033   3811   3661    584   -234     35       N  
ATOM   1639  CA  ILE B  29      57.357  91.856  -7.983  1.00 34.61           C  
ANISOU 1639  CA  ILE B  29     4756   4476   3918    438   -147    -32       C  
ATOM   1640  C   ILE B  29      57.634  93.334  -8.156  1.00 33.58           C  
ANISOU 1640  C   ILE B  29     4801   4231   3726    328   -111     35       C  
ATOM   1641  O   ILE B  29      56.903  94.019  -8.875  1.00 40.09           O  
ANISOU 1641  O   ILE B  29     5782   4863   4586    340   -286    196       O  
ATOM   1642  CB  ILE B  29      57.382  91.230  -9.379  1.00 34.73           C  
ANISOU 1642  CB  ILE B  29     4933   4528   3736    358   -282    -38       C  
ATOM   1643  CG1 ILE B  29      57.069  89.733  -9.312  1.00 39.85           C  
ANISOU 1643  CG1 ILE B  29     5472   5187   4480    436   -329   -139       C  
ATOM   1644  CG2 ILE B  29      58.750  91.459 -10.029  1.00 46.81           C  
ANISOU 1644  CG2 ILE B  29     6606   6234   4947    197   -101   -123       C  
ATOM   1645  CD1 ILE B  29      57.271  89.010 -10.653  1.00 45.23           C  
ANISOU 1645  CD1 ILE B  29     6355   5913   4919    345   -418   -257       C  
ATOM   1646  N   HIS B  30      58.676  93.828  -7.497  1.00 38.18           N  
ANISOU 1646  N   HIS B  30     5362   4914   4230    214     89    -75       N  
ATOM   1647  CA  HIS B  30      59.004  95.246  -7.582  1.00 36.67           C  
ANISOU 1647  CA  HIS B  30     5372   4547   4015     42    150    -37       C  
ATOM   1648  C   HIS B  30      59.848  95.535  -8.788  1.00 43.68           C  
ANISOU 1648  C   HIS B  30     6467   5501   4630   -215    199     35       C  
ATOM   1649  O   HIS B  30      60.662  94.704  -9.215  1.00 43.15           O  
ANISOU 1649  O   HIS B  30     6303   5728   4366   -284    296    -61       O  
ATOM   1650  CB  HIS B  30      59.723  95.747  -6.322  1.00 40.19           C  
ANISOU 1650  CB  HIS B  30     5711   5071   4488    -50    324   -227       C  
ATOM   1651  CG  HIS B  30      58.934  95.573  -5.066  1.00 37.22           C  
ANISOU 1651  CG  HIS B  30     5181   4667   4295    171    335   -308       C  
ATOM   1652  ND1 HIS B  30      58.579  96.634  -4.257  1.00 39.68           N  
ANISOU 1652  ND1 HIS B  30     5581   4759   4735    185    411   -412       N  
ATOM   1653  CD2 HIS B  30      58.425  94.468  -4.474  1.00 39.20           C  
ANISOU 1653  CD2 HIS B  30     5222   5068   4603    368    318   -306       C  
ATOM   1654  CE1 HIS B  30      57.901  96.187  -3.218  1.00 40.81           C  
ANISOU 1654  CE1 HIS B  30     5555   4987   4966    385    465   -485       C  
ATOM   1655  NE2 HIS B  30      57.788  94.876  -3.325  1.00 39.83           N  
ANISOU 1655  NE2 HIS B  30     5248   5083   4801    480    407   -390       N  
ATOM   1656  N   ASP B  31      59.661  96.724  -9.349  1.00 44.68           N  
ANISOU 1656  N   ASP B  31     6212   3817   6949    584    201   1223       N  
ATOM   1657  CA  ASP B  31      60.507  97.147 -10.443  1.00 47.64           C  
ANISOU 1657  CA  ASP B  31     6701   4146   7254    376    312   1369       C  
ATOM   1658  C   ASP B  31      61.978  97.241 -10.047  1.00 49.57           C  
ANISOU 1658  C   ASP B  31     6974   4343   7519    -33    442    869       C  
ATOM   1659  O   ASP B  31      62.851  97.157 -10.909  1.00 47.92           O  
ANISOU 1659  O   ASP B  31     6755   4269   7182   -255    484    897       O  
ATOM   1660  CB  ASP B  31      59.987  98.443 -11.061  1.00 53.14           C  
ANISOU 1660  CB  ASP B  31     7608   4397   8187    577    625   1870       C  
ATOM   1661  CG  ASP B  31      58.830  98.191 -11.999  1.00 59.92           C  
ANISOU 1661  CG  ASP B  31     8343   5539   8885    931    381   2469       C  
ATOM   1662  OD1 ASP B  31      58.781  97.080 -12.574  1.00 64.55           O  
ANISOU 1662  OD1 ASP B  31     8757   6660   9110    857      5   2468       O  
ATOM   1663  OD2 ASP B  31      57.974  99.076 -12.158  1.00 73.69           O  
ANISOU 1663  OD2 ASP B  31    10126   7117  10754   1203    505   2745       O  
ATOM   1664  N   ASP B  32      62.249  97.396  -8.751  1.00 48.23           N  
ANISOU 1664  N   ASP B  32     6812   4034   7480   -134    501    411       N  
ATOM   1665  CA  ASP B  32      63.631  97.466  -8.270  1.00 49.83           C  
ANISOU 1665  CA  ASP B  32     6948   4293   7690   -540    545    -95       C  
ATOM   1666  C   ASP B  32      64.246  96.077  -8.053  1.00 53.46           C  
ANISOU 1666  C   ASP B  32     7130   5333   7849   -572    184   -352       C  
ATOM   1667  O   ASP B  32      65.403  95.966  -7.666  1.00 49.31           O  
ANISOU 1667  O   ASP B  32     6443   4991   7302   -847    149   -736       O  
ATOM   1668  CB  ASP B  32      63.774  98.363  -7.014  1.00 50.64           C  
ANISOU 1668  CB  ASP B  32     7216   4011   8015   -700    759   -518       C  
ATOM   1669  CG  ASP B  32      63.071  97.796  -5.776  1.00 53.35           C  
ANISOU 1669  CG  ASP B  32     7550   4495   8224   -455    578   -730       C  
ATOM   1670  OD1 ASP B  32      62.833  96.575  -5.696  1.00 50.79           O  
ANISOU 1670  OD1 ASP B  32     7033   4621   7642   -270    254   -676       O  
ATOM   1671  OD2 ASP B  32      62.755  98.586  -4.861  1.00 59.75           O  
ANISOU 1671  OD2 ASP B  32     8591   4927   9184   -457    810   -962       O  
ATOM   1672  N   GLY B  33      63.471  95.022  -8.293  1.00 43.66           N  
ANISOU 1672  N   GLY B  33     5819   4373   6396   -290    -71   -135       N  
ATOM   1673  CA  GLY B  33      64.001  93.670  -8.180  1.00 37.06           C  
ANISOU 1673  CA  GLY B  33     4794   3988   5299   -272   -345   -325       C  
ATOM   1674  C   GLY B  33      63.520  92.883  -6.972  1.00 40.98           C  
ANISOU 1674  C   GLY B  33     5261   4619   5690    -78   -537   -502       C  
ATOM   1675  O   GLY B  33      63.616  91.654  -6.945  1.00 41.93           O  
ANISOU 1675  O   GLY B  33     5292   5033   5605     33   -740   -534       O  
ATOM   1676  N   ARG B  34      63.023  93.589  -5.963  1.00 34.32           N  
ANISOU 1676  N   ARG B  34     4536   3526   4977    -31   -422   -617       N  
ATOM   1677  CA  ARG B  34      62.552  92.938  -4.744  1.00 33.48           C  
ANISOU 1677  CA  ARG B  34     4451   3536   4734    154   -539   -768       C  
ATOM   1678  C   ARG B  34      61.334  92.063  -5.059  1.00 32.83           C  
ANISOU 1678  C   ARG B  34     4343   3531   4601    403   -634   -426       C  
ATOM   1679  O   ARG B  34      60.519  92.415  -5.918  1.00 36.67           O  
ANISOU 1679  O   ARG B  34     4820   3892   5220    470   -575    -82       O  
ATOM   1680  CB  ARG B  34      62.172  94.007  -3.710  1.00 39.18           C  
ANISOU 1680  CB  ARG B  34     5367   3928   5591    152   -311   -958       C  
ATOM   1681  CG  ARG B  34      63.367  94.649  -3.013  1.00 44.87           C  
ANISOU 1681  CG  ARG B  34     6115   4652   6283   -162   -290  -1442       C  
ATOM   1682  CD  ARG B  34      62.928  95.694  -1.985  1.00 47.16           C  
ANISOU 1682  CD  ARG B  34     6689   4564   6665   -189    -27  -1697       C  
ATOM   1683  NE  ARG B  34      62.274  96.843  -2.606  1.00 57.21           N  
ANISOU 1683  NE  ARG B  34     8150   5288   8300   -159    343  -1453       N  
ATOM   1684  CZ  ARG B  34      61.545  97.739  -1.946  1.00 62.22           C  
ANISOU 1684  CZ  ARG B  34     9072   5473   9096    -45    680  -1531       C  
ATOM   1685  NH1 ARG B  34      60.992  98.753  -2.594  1.00 73.41           N  
ANISOU 1685  NH1 ARG B  34    10652   6369  10871     53   1034  -1237       N  
ATOM   1686  NH2 ARG B  34      61.369  97.620  -0.639  1.00 67.30           N  
ANISOU 1686  NH2 ARG B  34     9867   6179   9523      9    694  -1884       N  
ATOM   1687  N   ARG B  35      61.198  90.946  -4.348  1.00 33.57           N  
ANISOU 1687  N   ARG B  35     4417   3837   4503    529   -779   -505       N  
ATOM   1688  CA  ARG B  35      59.962  90.149  -4.396  1.00 31.98           C  
ANISOU 1688  CA  ARG B  35     4187   3664   4298    696   -818   -238       C  
ATOM   1689  C   ARG B  35      59.461  89.957  -2.950  1.00 29.76           C  
ANISOU 1689  C   ARG B  35     4004   3352   3951    856   -718   -347       C  
ATOM   1690  O   ARG B  35      60.257  89.770  -2.037  1.00 31.77           O  
ANISOU 1690  O   ARG B  35     4346   3720   4004    862   -765   -624       O  
ATOM   1691  CB  ARG B  35      60.254  88.743  -4.929  1.00 28.96           C  
ANISOU 1691  CB  ARG B  35     3762   3515   3728    676  -1014   -212       C  
ATOM   1692  CG  ARG B  35      60.238  88.555  -6.435  1.00 30.19           C  
ANISOU 1692  CG  ARG B  35     3862   3740   3870    551  -1105    -36       C  
ATOM   1693  CD  ARG B  35      61.418  89.257  -7.143  1.00 32.13           C  
ANISOU 1693  CD  ARG B  35     4098   4003   4108    407  -1058   -137       C  
ATOM   1694  NE  ARG B  35      61.677  88.586  -8.432  1.00 35.27           N  
ANISOU 1694  NE  ARG B  35     4504   4552   4344    317  -1140    -55       N  
ATOM   1695  CZ  ARG B  35      62.601  88.971  -9.307  1.00 34.69           C  
ANISOU 1695  CZ  ARG B  35     4426   4533   4220    188  -1062    -82       C  
ATOM   1696  NH1 ARG B  35      62.759  88.278 -10.430  1.00 33.17           N  
ANISOU 1696  NH1 ARG B  35     4298   4486   3820    126  -1104    -31       N  
ATOM   1697  NH2 ARG B  35      63.335  90.068  -9.072  1.00 31.62           N  
ANISOU 1697  NH2 ARG B  35     3993   4036   3985     88   -905   -175       N  
ATOM   1698  N   GLU B  36      58.151  89.966  -2.750  1.00 33.07           N  
ANISOU 1698  N   GLU B  36     4385   3666   4512    996   -583   -114       N  
ATOM   1699  CA  GLU B  36      57.586  89.385  -1.523  1.00 35.65           C  
ANISOU 1699  CA  GLU B  36     4799   4019   4726   1147   -465   -147       C  
ATOM   1700  C   GLU B  36      56.599  88.292  -1.909  1.00 31.81           C  
ANISOU 1700  C   GLU B  36     4162   3622   4302   1156   -513    136       C  
ATOM   1701  O   GLU B  36      55.901  88.415  -2.906  1.00 32.95           O  
ANISOU 1701  O   GLU B  36     4100   3778   4642   1097   -575    378       O  
ATOM   1702  CB  GLU B  36      56.870  90.425  -0.652  1.00 37.43           C  
ANISOU 1702  CB  GLU B  36     5119   4016   5085   1298   -140   -178       C  
ATOM   1703  CG  GLU B  36      57.790  91.460  -0.031  1.00 37.34           C  
ANISOU 1703  CG  GLU B  36     5331   3874   4980   1223    -55   -556       C  
ATOM   1704  CD  GLU B  36      58.053  92.613  -0.972  1.00 47.46           C  
ANISOU 1704  CD  GLU B  36     6582   4914   6535   1107      6   -523       C  
ATOM   1705  OE1 GLU B  36      57.095  93.071  -1.638  1.00 50.76           O  
ANISOU 1705  OE1 GLU B  36     6882   5160   7247   1242    145   -181       O  
ATOM   1706  OE2 GLU B  36      59.214  93.062  -1.050  1.00 56.35           O  
ANISOU 1706  OE2 GLU B  36     7783   6039   7589    884    -78   -809       O  
ATOM   1707  N   ILE B  37      56.555  87.227  -1.121  1.00 28.55           N  
ANISOU 1707  N   ILE B  37     3861   3280   3707   1210   -486    108       N  
ATOM   1708  CA  ILE B  37      55.612  86.162  -1.369  1.00 33.18           C  
ANISOU 1708  CA  ILE B  37     4334   3890   4381   1145   -472    334       C  
ATOM   1709  C   ILE B  37      54.762  86.011  -0.102  1.00 35.46           C  
ANISOU 1709  C   ILE B  37     4688   4115   4672   1296   -157    416       C  
ATOM   1710  O   ILE B  37      55.297  86.022   1.007  1.00 37.15           O  
ANISOU 1710  O   ILE B  37     5165   4331   4620   1446    -51    258       O  
ATOM   1711  CB  ILE B  37      56.340  84.843  -1.605  1.00 35.82           C  
ANISOU 1711  CB  ILE B  37     4816   4279   4514   1070   -630    266       C  
ATOM   1712  CG1 ILE B  37      57.464  85.010  -2.655  1.00 35.00           C  
ANISOU 1712  CG1 ILE B  37     4703   4258   4337    976   -868    122       C  
ATOM   1713  CG2 ILE B  37      55.344  83.769  -2.054  1.00 37.93           C  
ANISOU 1713  CG2 ILE B  37     4988   4506   4916    890   -606    452       C  
ATOM   1714  CD1 ILE B  37      58.273  83.744  -2.829  1.00 39.97           C  
ANISOU 1714  CD1 ILE B  37     5494   4910   4783    987   -956     40       C  
ATOM   1715  N   TYR B  38      53.458  85.861  -0.281  1.00 31.20           N  
ANISOU 1715  N   TYR B  38     3887   3564   4403   1247    -13    666       N  
ATOM   1716  CA  TYR B  38      52.527  85.699   0.844  1.00 33.11           C  
ANISOU 1716  CA  TYR B  38     4135   3752   4694   1375    367    786       C  
ATOM   1717  C   TYR B  38      51.737  84.421   0.654  1.00 42.06           C  
ANISOU 1717  C   TYR B  38     5122   4907   5952   1161    410    984       C  
ATOM   1718  O   TYR B  38      51.238  84.172  -0.440  1.00 36.38           O  
ANISOU 1718  O   TYR B  38     4090   4278   5454    924    202   1094       O  
ATOM   1719  CB  TYR B  38      51.541  86.869   0.868  1.00 33.96           C  
ANISOU 1719  CB  TYR B  38     3961   3819   5122   1531    603    928       C  
ATOM   1720  CG  TYR B  38      52.192  88.210   1.060  1.00 35.14           C  
ANISOU 1720  CG  TYR B  38     4300   3836   5215   1707    651    722       C  
ATOM   1721  CD1 TYR B  38      52.716  88.898  -0.021  1.00 37.48           C  
ANISOU 1721  CD1 TYR B  38     4516   4113   5612   1637    390    703       C  
ATOM   1722  CD2 TYR B  38      52.297  88.789   2.319  1.00 38.21           C  
ANISOU 1722  CD2 TYR B  38     4991   4099   5429   1908    985    526       C  
ATOM   1723  CE1 TYR B  38      53.322  90.120   0.138  1.00 38.21           C  
ANISOU 1723  CE1 TYR B  38     4806   4014   5697   1733    482    507       C  
ATOM   1724  CE2 TYR B  38      52.897  90.029   2.490  1.00 38.91           C  
ANISOU 1724  CE2 TYR B  38     5289   4013   5482   1990   1050    270       C  
ATOM   1725  CZ  TYR B  38      53.417  90.682   1.384  1.00 43.09           C  
ANISOU 1725  CZ  TYR B  38     5717   4476   6178   1885    804    266       C  
ATOM   1726  OH  TYR B  38      54.031  91.911   1.491  1.00 46.62           O  
ANISOU 1726  OH  TYR B  38     6389   4684   6642   1901    906     13       O  
ATOM   1727  N   ARG B  39      51.587  83.625   1.713  1.00 36.63           N  
ANISOU 1727  N   ARG B  39     4672   4139   5108   1217    693   1031       N  
ATOM   1728  CA  ARG B  39      50.745  82.433   1.633  1.00 38.38           C  
ANISOU 1728  CA  ARG B  39     4775   4303   5504    962    837   1225       C  
ATOM   1729  C   ARG B  39      49.514  82.602   2.513  1.00 38.94           C  
ANISOU 1729  C   ARG B  39     4647   4371   5777   1032   1313   1435       C  
ATOM   1730  O   ARG B  39      49.626  83.013   3.666  1.00 40.09           O  
ANISOU 1730  O   ARG B  39     5060   4476   5697   1321   1628   1409       O  
ATOM   1731  CB  ARG B  39      51.538  81.186   2.061  1.00 44.73           C  
ANISOU 1731  CB  ARG B  39     6043   4947   6005    958    855   1187       C  
ATOM   1732  CG  ARG B  39      52.500  80.697   0.979  1.00 43.56           C  
ANISOU 1732  CG  ARG B  39     5996   4779   5776    824    458   1022       C  
ATOM   1733  CD  ARG B  39      51.827  79.674   0.069  1.00 47.45           C  
ANISOU 1733  CD  ARG B  39     6343   5166   6522    399    415   1077       C  
ATOM   1734  NE  ARG B  39      51.542  78.427   0.774  1.00 43.76           N  
ANISOU 1734  NE  ARG B  39     6162   4421   6044    317    755   1212       N  
ATOM   1735  CZ  ARG B  39      50.324  77.951   1.013  1.00 51.43           C  
ANISOU 1735  CZ  ARG B  39     6931   5309   7301     32   1056   1388       C  
ATOM   1736  NH1 ARG B  39      50.175  76.812   1.673  1.00 50.50           N  
ANISOU 1736  NH1 ARG B  39     7152   4872   7163    -42   1419   1528       N  
ATOM   1737  NH2 ARG B  39      49.253  78.606   0.584  1.00 45.19           N  
ANISOU 1737  NH2 ARG B  39     5577   4757   6836   -171   1014   1454       N  
ATOM   1738  N   PHE B  40      48.343  82.267   1.978  1.00 41.66           N  
ANISOU 1738  N   PHE B  40     4509   4794   6527    750   1375   1629       N  
ATOM   1739  CA  PHE B  40      47.096  82.487   2.706  1.00 46.38           C  
ANISOU 1739  CA  PHE B  40     4782   5440   7402    814   1859   1856       C  
ATOM   1740  C   PHE B  40      46.279  81.222   2.911  1.00 57.65           C  
ANISOU 1740  C   PHE B  40     6083   6794   9027    444   2133   2034       C  
ATOM   1741  O   PHE B  40      46.391  80.277   2.133  1.00 61.59           O  
ANISOU 1741  O   PHE B  40     6579   7236   9586     45   1869   1981       O  
ATOM   1742  CB  PHE B  40      46.241  83.467   1.940  1.00 50.16           C  
ANISOU 1742  CB  PHE B  40     4615   6152   8292    853   1740   1987       C  
ATOM   1743  CG  PHE B  40      46.820  84.825   1.872  1.00 45.27           C  
ANISOU 1743  CG  PHE B  40     4117   5514   7569   1234   1638   1871       C  
ATOM   1744  CD1 PHE B  40      46.627  85.724   2.910  1.00 47.14           C  
ANISOU 1744  CD1 PHE B  40     4493   5646   7774   1626   2094   1858       C  
ATOM   1745  CD2 PHE B  40      47.543  85.216   0.774  1.00 41.96           C  
ANISOU 1745  CD2 PHE B  40     3709   5151   7084   1178   1141   1760       C  
ATOM   1746  CE1 PHE B  40      47.159  86.990   2.852  1.00 53.15           C  
ANISOU 1746  CE1 PHE B  40     5417   6307   8472   1924   2047   1710       C  
ATOM   1747  CE2 PHE B  40      48.067  86.487   0.711  1.00 43.52           C  
ANISOU 1747  CE2 PHE B  40     4038   5269   7230   1484   1107   1665       C  
ATOM   1748  CZ  PHE B  40      47.871  87.373   1.758  1.00 43.20           C  
ANISOU 1748  CZ  PHE B  40     4148   5072   7193   1841   1561   1628       C  
ATOM   1749  N   ASN B  41      45.448  81.235   3.950  1.00 59.95           N  
ANISOU 1749  N   ASN B  41     6288   7063   9427    556   2710   2227       N  
ATOM   1750  CA  ASN B  41      44.493  80.166   4.203  1.00 67.33           C  
ANISOU 1750  CA  ASN B  41     7011   7929  10643    170   3084   2438       C  
ATOM   1751  C   ASN B  41      43.532  80.048   3.028  1.00 69.50           C  
ANISOU 1751  C   ASN B  41     6500   8465  11443   -282   2797   2506       C  
ATOM   1752  O   ASN B  41      42.927  81.036   2.599  1.00 63.23           O  
ANISOU 1752  O   ASN B  41     5119   7978  10930   -125   2678   2592       O  
ATOM   1753  CB  ASN B  41      43.719  80.430   5.499  1.00 71.92           C  
ANISOU 1753  CB  ASN B  41     7565   8499  11261    422   3810   2651       C  
ATOM   1754  CG  ASN B  41      42.878  79.243   5.927  1.00 87.00           C  
ANISOU 1754  CG  ASN B  41     9375  10271  13408     13   4300   2887       C  
ATOM   1755  OD1 ASN B  41      41.782  79.027   5.410  1.00 96.81           O  
ANISOU 1755  OD1 ASN B  41     9951  11694  15140   -364   4272   2962       O  
ATOM   1756  ND2 ASN B  41      43.388  78.467   6.879  1.00 91.85           N  
ANISOU 1756  ND2 ASN B  41    10702  10584  13612    102   4629   2944       N  
ATOM   1757  N   ASP B  42      43.400  78.835   2.508  1.00 81.00           N  
ANISOU 1757  N   ASP B  42     7962   9798  13015   -839   2682   2465       N  
ATOM   1758  CA  ASP B  42      42.610  78.597   1.307  1.00 91.92           C  
ANISOU 1758  CA  ASP B  42     8657  11470  14797  -1371   2298   2447       C  
ATOM   1759  C   ASP B  42      41.113  78.868   1.498  1.00 88.37           C  
ANISOU 1759  C   ASP B  42     7371  11359  14846  -1503   2581   2688       C  
ATOM   1760  O   ASP B  42      40.412  79.182   0.537  1.00 82.36           O  
ANISOU 1760  O   ASP B  42     6004  11013  14276  -1688   2126   2645       O  
ATOM   1761  CB  ASP B  42      42.854  77.175   0.789  1.00110.73           C  
ANISOU 1761  CB  ASP B  42    11357  13562  17153  -1984   2172   2265       C  
ATOM   1762  CG  ASP B  42      42.588  76.108   1.837  1.00131.72           C  
ANISOU 1762  CG  ASP B  42    14378  15799  19869  -2179   2835   2407       C  
ATOM   1763  OD1 ASP B  42      42.248  76.458   2.988  1.00138.46           O  
ANISOU 1763  OD1 ASP B  42    15254  16632  20722  -1831   3383   2648       O  
ATOM   1764  OD2 ASP B  42      42.731  74.911   1.507  1.00140.44           O  
ANISOU 1764  OD2 ASP B  42    15798  16559  21004  -2676   2846   2279       O  
ATOM   1765  N   ARG B  43      40.643  78.755   2.741  1.00 76.14           N  
ANISOU 1765  N   ARG B  43     5983   9657  13290  -1311   3212   2824       N  
ATOM   1766  CA  ARG B  43      39.231  78.969   3.075  1.00 83.17           C  
ANISOU 1766  CA  ARG B  43     6276  10834  14492  -1344   3458   2942       C  
ATOM   1767  C   ARG B  43      38.946  80.367   3.629  1.00 83.22           C  
ANISOU 1767  C   ARG B  43     6111  10996  14513   -657   3663   3071       C  
ATOM   1768  O   ARG B  43      37.804  80.687   3.970  1.00110.79           O  
ANISOU 1768  O   ARG B  43     9133  14701  18261   -580   3910   3191       O  
ATOM   1769  CB  ARG B  43      38.768  77.926   4.093  1.00 88.27           C  
ANISOU 1769  CB  ARG B  43     7202  11206  15133  -1605   4051   3013       C  
ATOM   1770  CG  ARG B  43      38.657  76.518   3.545  1.00106.54           C  
ANISOU 1770  CG  ARG B  43     9597  13356  17528  -2366   3917   2878       C  
ATOM   1771  CD  ARG B  43      37.519  76.407   2.545  1.00108.34           C  
ANISOU 1771  CD  ARG B  43     8982  14066  18117  -2907   3546   2776       C  
ATOM   1772  NE  ARG B  43      37.112  75.019   2.341  1.00109.60           N  
ANISOU 1772  NE  ARG B  43     9217  14063  18363  -3695   3618   2644       N  
ATOM   1773  CZ  ARG B  43      36.129  74.637   1.531  1.00116.63           C  
ANISOU 1773  CZ  ARG B  43     9466  15352  19496  -4333   3346   2482       C  
ATOM   1774  NH1 ARG B  43      35.441  75.540   0.844  1.00115.16           N  
ANISOU 1774  NH1 ARG B  43     8500  15763  19493  -4198   2968   2448       N  
ATOM   1775  NH2 ARG B  43      35.829  73.350   1.410  1.00125.17           N  
ANISOU 1775  NH2 ARG B  43    10714  16232  20615  -5087   3446   2361       N  
ATOM   1776  N   ASP B  44      39.988  81.183   3.731  1.00 77.11           N  
ANISOU 1776  N   ASP B  44     5751  10088  13459   -177   3589   3023       N  
ATOM   1777  CA  ASP B  44      39.877  82.548   4.227  1.00 87.15           C  
ANISOU 1777  CA  ASP B  44     7029  11394  14688    456   3776   3065       C  
ATOM   1778  C   ASP B  44      41.078  83.330   3.729  1.00 84.09           C  
ANISOU 1778  C   ASP B  44     6958  10938  14055    762   3424   2933       C  
ATOM   1779  O   ASP B  44      42.146  83.284   4.338  1.00 89.09           O  
ANISOU 1779  O   ASP B  44     8227  11322  14300    954   3611   2809       O  
ATOM   1780  CB  ASP B  44      39.843  82.566   5.756  1.00 93.38           C  
ANISOU 1780  CB  ASP B  44     8327  11924  15228    759   4466   3083       C  
ATOM   1781  CG  ASP B  44      39.546  83.952   6.329  1.00 94.18           C  
ANISOU 1781  CG  ASP B  44     8466  12014  15306   1334   4708   3077       C  
ATOM   1782  OD1 ASP B  44      39.745  84.968   5.627  1.00 78.90           O  
ANISOU 1782  OD1 ASP B  44     6380  10154  13443   1577   4362   3038       O  
ATOM   1783  OD2 ASP B  44      39.115  84.021   7.499  1.00 96.24           O  
ANISOU 1783  OD2 ASP B  44     8967  12150  15450   1527   5260   3107       O  
ATOM   1784  N   PRO B  45      40.900  84.069   2.624  1.00 82.82           N  
ANISOU 1784  N   PRO B  45     6385  11018  14065    820   2907   2956       N  
ATOM   1785  CA  PRO B  45      41.987  84.768   1.928  1.00 74.79           C  
ANISOU 1785  CA  PRO B  45     5618   9955  12845   1030   2489   2832       C  
ATOM   1786  C   PRO B  45      42.643  85.867   2.766  1.00 83.58           C  
ANISOU 1786  C   PRO B  45     7278  10787  13692   1576   2798   2695       C  
ATOM   1787  O   PRO B  45      43.716  86.343   2.385  1.00 81.20           O  
ANISOU 1787  O   PRO B  45     7313  10375  13164   1718   2518   2522       O  
ATOM   1788  CB  PRO B  45      41.284  85.407   0.719  1.00 79.56           C  
ANISOU 1788  CB  PRO B  45     5704  10876  13648   1008   1978   2947       C  
ATOM   1789  CG  PRO B  45      39.947  84.728   0.616  1.00 78.22           C  
ANISOU 1789  CG  PRO B  45     4942  10994  13784    662   2019   3083       C  
ATOM   1790  CD  PRO B  45      39.589  84.319   2.003  1.00 82.60           C  
ANISOU 1790  CD  PRO B  45     5657  11339  14388    718   2710   3113       C  
ATOM   1791  N   ASP B  46      42.012  86.268   3.868  1.00 82.63           N  
ANISOU 1791  N   ASP B  46     7279  10546  13573   1830   3336   2726       N  
ATOM   1792  CA  ASP B  46      42.543  87.344   4.704  1.00 83.82           C  
ANISOU 1792  CA  ASP B  46     8002  10421  13426   2249   3611   2525       C  
ATOM   1793  C   ASP B  46      43.391  86.821   5.869  1.00 82.88           C  
ANISOU 1793  C   ASP B  46     8569  10103  12819   2302   3948   2310       C  
ATOM   1794  O   ASP B  46      43.969  87.606   6.619  1.00 79.04           O  
ANISOU 1794  O   ASP B  46     8633   9422  11977   2558   4099   2059       O  
ATOM   1795  CB  ASP B  46      41.406  88.237   5.224  1.00 99.04           C  
ANISOU 1795  CB  ASP B  46     9731  12322  15577   2518   3985   2651       C  
ATOM   1796  CG  ASP B  46      41.865  89.660   5.532  1.00102.60           C  
ANISOU 1796  CG  ASP B  46    10628  12507  15847   2865   4080   2450       C  
ATOM   1797  OD1 ASP B  46      42.724  90.191   4.792  1.00 94.11           O  
ANISOU 1797  OD1 ASP B  46     9726  11365  14666   2863   3687   2314       O  
ATOM   1798  OD2 ASP B  46      41.364  90.253   6.513  1.00109.66           O  
ANISOU 1798  OD2 ASP B  46    11710  13247  16710   3105   4565   2414       O  
ATOM   1799  N   GLU B  47      43.461  85.500   6.021  1.00 84.06           N  
ANISOU 1799  N   GLU B  47     8728  10306  12903   2016   4045   2404       N  
ATOM   1800  CA  GLU B  47      44.307  84.889   7.048  1.00 61.96           C  
ANISOU 1800  CA  GLU B  47     6663   7349   9530   2060   4276   2253       C  
ATOM   1801  C   GLU B  47      45.682  84.536   6.476  1.00 63.69           C  
ANISOU 1801  C   GLU B  47     7311   7511   9377   1906   3621   2009       C  
ATOM   1802  O   GLU B  47      45.792  83.660   5.630  1.00 56.12           O  
ANISOU 1802  O   GLU B  47     6188   6588   8548   1547   3246   2071       O  
ATOM   1803  CB  GLU B  47      43.641  83.627   7.624  1.00 65.82           C  
ANISOU 1803  CB  GLU B  47     7130   7821  10059   1783   4663   2494       C  
ATOM   1804  CG  GLU B  47      42.308  83.879   8.320  1.00 88.73           C  
ANISOU 1804  CG  GLU B  47     9744  10741  13227   1850   5095   2639       C  
ATOM   1805  CD  GLU B  47      41.604  82.591   8.725  1.00 88.98           C  
ANISOU 1805  CD  GLU B  47     9692  10743  13374   1497   5397   2850       C  
ATOM   1806  OE1 GLU B  47      42.045  81.502   8.288  1.00 77.34           O  
ANISOU 1806  OE1 GLU B  47     8326   9198  11860   1139   5213   2897       O  
ATOM   1807  OE2 GLU B  47      40.608  82.667   9.476  1.00 94.41           O  
ANISOU 1807  OE2 GLU B  47    10233  11442  14198   1561   5830   2961       O  
ATOM   1808  N   LEU B  48      46.724  85.213   6.949  1.00 53.77           N  
ANISOU 1808  N   LEU B  48     6592   6175   7662   2161   3512   1709       N  
ATOM   1809  CA  LEU B  48      48.063  85.031   6.427  1.00 52.55           C  
ANISOU 1809  CA  LEU B  48     6760   6014   7194   2061   2925   1475       C  
ATOM   1810  C   LEU B  48      48.709  83.834   7.105  1.00 51.64           C  
ANISOU 1810  C   LEU B  48     7135   5868   6618   2003   2926   1493       C  
ATOM   1811  O   LEU B  48      48.700  83.740   8.327  1.00 51.87           O  
ANISOU 1811  O   LEU B  48     7562   5884   6260   2206   3316   1503       O  
ATOM   1812  CB  LEU B  48      48.906  86.291   6.655  1.00 47.47           C  
ANISOU 1812  CB  LEU B  48     6418   5324   6294   2303   2810   1133       C  
ATOM   1813  CG  LEU B  48      50.372  86.244   6.221  1.00 46.64           C  
ANISOU 1813  CG  LEU B  48     6600   5256   5863   2211   2246    863       C  
ATOM   1814  CD1 LEU B  48      50.560  86.377   4.677  1.00 41.34           C  
ANISOU 1814  CD1 LEU B  48     5542   4609   5555   2002   1777    902       C  
ATOM   1815  CD2 LEU B  48      51.208  87.269   6.972  1.00 50.95           C  
ANISOU 1815  CD2 LEU B  48     7566   5775   6017   2394   2266    481       C  
ATOM   1816  N   LEU B  49      49.268  82.924   6.310  1.00 45.95           N  
ANISOU 1816  N   LEU B  49     6419   5126   5914   1761   2515   1513       N  
ATOM   1817  CA  LEU B  49      49.947  81.751   6.866  1.00 52.50           C  
ANISOU 1817  CA  LEU B  49     7729   5875   6345   1774   2514   1579       C  
ATOM   1818  C   LEU B  49      51.434  82.032   7.028  1.00 45.83           C  
ANISOU 1818  C   LEU B  49     7267   5133   5014   1986   2106   1311       C  
ATOM   1819  O   LEU B  49      52.030  81.722   8.058  1.00 51.71           O  
ANISOU 1819  O   LEU B  49     8472   5935   5241   2224   2190   1314       O  
ATOM   1820  CB  LEU B  49      49.752  80.534   5.962  1.00 51.92           C  
ANISOU 1820  CB  LEU B  49     7501   5657   6568   1412   2369   1729       C  
ATOM   1821  CG  LEU B  49      48.298  80.132   5.728  1.00 60.44           C  
ANISOU 1821  CG  LEU B  49     8122   6683   8160   1085   2713   1970       C  
ATOM   1822  CD1 LEU B  49      48.192  78.953   4.772  1.00 51.19           C  
ANISOU 1822  CD1 LEU B  49     6852   5351   7247    639   2522   2012       C  
ATOM   1823  CD2 LEU B  49      47.632  79.812   7.056  1.00 54.51           C  
ANISOU 1823  CD2 LEU B  49     7584   5850   7276   1215   3370   2209       C  
ATOM   1824  N   SER B  50      52.031  82.626   5.997  1.00 48.85           N  
ANISOU 1824  N   SER B  50     7429   5578   5553   1894   1659   1097       N  
ATOM   1825  CA  SER B  50      53.430  82.985   6.044  1.00 37.74           C  
ANISOU 1825  CA  SER B  50     6260   4306   3773   2034   1273    823       C  
ATOM   1826  C   SER B  50      53.769  84.017   4.959  1.00 43.82           C  
ANISOU 1826  C   SER B  50     6725   5112   4810   1910    951    607       C  
ATOM   1827  O   SER B  50      52.989  84.251   4.025  1.00 39.72           O  
ANISOU 1827  O   SER B  50     5831   4530   4731   1735    948    719       O  
ATOM   1828  CB  SER B  50      54.296  81.708   5.844  1.00 37.04           C  
ANISOU 1828  CB  SER B  50     6387   4198   3489   2049   1040    911       C  
ATOM   1829  OG  SER B  50      54.153  81.206   4.519  1.00 39.77           O  
ANISOU 1829  OG  SER B  50     6466   4421   4224   1772    850    952       O  
ATOM   1830  N   ASN B  51      54.930  84.646   5.088  1.00 35.24           N  
ANISOU 1830  N   ASN B  51     5788   4154   3448   1990    680    317       N  
ATOM   1831  CA  ASN B  51      55.413  85.542   4.040  1.00 36.66           C  
ANISOU 1831  CA  ASN B  51     5735   4334   3859   1850    403    135       C  
ATOM   1832  C   ASN B  51      56.930  85.569   4.055  1.00 38.63           C  
ANISOU 1832  C   ASN B  51     6114   4768   3795   1866     45   -125       C  
ATOM   1833  O   ASN B  51      57.536  85.239   5.063  1.00 42.24           O  
ANISOU 1833  O   ASN B  51     6831   5394   3824   2031      6   -210       O  
ATOM   1834  CB  ASN B  51      54.872  86.953   4.235  1.00 40.14           C  
ANISOU 1834  CB  ASN B  51     6115   4659   4475   1892    634     15       C  
ATOM   1835  CG  ASN B  51      55.588  87.693   5.344  1.00 50.52           C  
ANISOU 1835  CG  ASN B  51     7771   6039   5386   1998    684   -336       C  
ATOM   1836  OD1 ASN B  51      56.320  88.647   5.098  1.00 57.90           O  
ANISOU 1836  OD1 ASN B  51     8721   6950   6329   1899    531   -625       O  
ATOM   1837  ND2 ASN B  51      55.385  87.248   6.573  1.00 46.49           N  
ANISOU 1837  ND2 ASN B  51     7556   5616   4493   2165    906   -321       N  
ATOM   1838  N   ILE B  52      57.538  85.948   2.931  1.00 42.19           N  
ANISOU 1838  N   ILE B  52     6358   5230   4444   1704   -216   -226       N  
ATOM   1839  CA  ILE B  52      58.989  86.009   2.841  1.00 39.16           C  
ANISOU 1839  CA  ILE B  52     5987   5053   3839   1690   -531   -466       C  
ATOM   1840  C   ILE B  52      59.418  87.160   1.920  1.00 37.45           C  
ANISOU 1840  C   ILE B  52     5580   4779   3872   1479   -633   -645       C  
ATOM   1841  O   ILE B  52      58.753  87.477   0.935  1.00 36.65           O  
ANISOU 1841  O   ILE B  52     5316   4507   4104   1370   -567   -485       O  
ATOM   1842  CB  ILE B  52      59.579  84.640   2.370  1.00 32.21           C  
ANISOU 1842  CB  ILE B  52     5097   4259   2884   1760   -712   -320       C  
ATOM   1843  CG1 ILE B  52      61.093  84.606   2.548  1.00 43.09           C  
ANISOU 1843  CG1 ILE B  52     6438   5932   4000   1847  -1005   -529       C  
ATOM   1844  CG2 ILE B  52      59.155  84.328   0.947  1.00 35.17           C  
ANISOU 1844  CG2 ILE B  52     5284   4476   3603   1566   -737   -182       C  
ATOM   1845  CD1 ILE B  52      61.638  83.186   2.500  1.00 39.14           C  
ANISOU 1845  CD1 ILE B  52     5943   5432   3498   1957   -979   -361       C  
ATOM   1846  N   SER B  53      60.508  87.825   2.278  1.00 35.55           N  
ANISOU 1846  N   SER B  53     5358   4694   3456   1409   -785   -966       N  
ATOM   1847  CA  SER B  53      61.026  88.907   1.447  1.00 33.68           C  
ANISOU 1847  CA  SER B  53     4973   4363   3462   1168   -829  -1135       C  
ATOM   1848  C   SER B  53      62.371  88.493   0.841  1.00 37.63           C  
ANISOU 1848  C   SER B  53     5275   5126   3897   1078  -1115  -1237       C  
ATOM   1849  O   SER B  53      63.238  87.963   1.564  1.00 37.93           O  
ANISOU 1849  O   SER B  53     5275   5450   3686   1154  -1262  -1317       O  
ATOM   1850  CB  SER B  53      61.190  90.155   2.300  1.00 43.06           C  
ANISOU 1850  CB  SER B  53     6325   5462   4576   1061   -704  -1482       C  
ATOM   1851  OG  SER B  53      59.957  90.443   2.952  1.00 47.96           O  
ANISOU 1851  OG  SER B  53     7142   5849   5232   1217   -374  -1386       O  
ATOM   1852  N   LEU B  54      62.535  88.777  -0.453  1.00 37.43           N  
ANISOU 1852  N   LEU B  54     5085   4994   4142    913  -1114  -1153       N  
ATOM   1853  CA  LEU B  54      63.666  88.337  -1.260  1.00 40.26           C  
ANISOU 1853  CA  LEU B  54     5237   5564   4495    843  -1287  -1194       C  
ATOM   1854  C   LEU B  54      64.188  89.481  -2.125  1.00 45.02           C  
ANISOU 1854  C   LEU B  54     5713   6060   5333    547  -1215  -1303       C  
ATOM   1855  O   LEU B  54      63.415  90.309  -2.564  1.00 40.78           O  
ANISOU 1855  O   LEU B  54     5267   5219   5011    460  -1031  -1182       O  
ATOM   1856  CB  LEU B  54      63.220  87.225  -2.206  1.00 31.52           C  
ANISOU 1856  CB  LEU B  54     4130   4410   3438    944  -1287   -912       C  
ATOM   1857  CG  LEU B  54      62.563  85.982  -1.594  1.00 35.12           C  
ANISOU 1857  CG  LEU B  54     4741   4830   3775   1155  -1228   -725       C  
ATOM   1858  CD1 LEU B  54      62.060  85.095  -2.728  1.00 32.51           C  
ANISOU 1858  CD1 LEU B  54     4425   4372   3554   1096  -1179   -527       C  
ATOM   1859  CD2 LEU B  54      63.535  85.238  -0.677  1.00 37.26           C  
ANISOU 1859  CD2 LEU B  54     5004   5285   3869   1306  -1231   -773       C  
ATOM   1860  N   ASP B  55      65.493  89.528  -2.374  1.00 41.24           N  
ANISOU 1860  N   ASP B  55     5009   5826   4835    412  -1323  -1488       N  
ATOM   1861  CA  ASP B  55      66.013  90.438  -3.402  1.00 37.11           C  
ANISOU 1861  CA  ASP B  55     4364   5187   4550    114  -1197  -1527       C  
ATOM   1862  C   ASP B  55      66.068  89.699  -4.733  1.00 38.66           C  
ANISOU 1862  C   ASP B  55     4496   5422   4773    177  -1168  -1274       C  
ATOM   1863  O   ASP B  55      65.695  88.528  -4.808  1.00 36.28           O  
ANISOU 1863  O   ASP B  55     4256   5196   4332    416  -1251  -1127       O  
ATOM   1864  CB  ASP B  55      67.362  91.067  -3.002  1.00 36.95           C  
ANISOU 1864  CB  ASP B  55     4097   5396   4547   -161  -1261  -1882       C  
ATOM   1865  CG  ASP B  55      68.473  90.050  -2.823  1.00 48.91           C  
ANISOU 1865  CG  ASP B  55     5361   7307   5916     -1  -1370  -1805       C  
ATOM   1866  OD1 ASP B  55      68.437  88.974  -3.458  1.00 47.25           O  
ANISOU 1866  OD1 ASP B  55     5133   7159   5661    241  -1368  -1592       O  
ATOM   1867  OD2 ASP B  55      69.408  90.344  -2.059  1.00 55.08           O  
ANISOU 1867  OD2 ASP B  55     5970   8315   6640   -121  -1453  -1984       O  
ATOM   1868  N   ASP B  56      66.489  90.385  -5.792  1.00 37.36           N  
ANISOU 1868  N   ASP B  56     4070   3931   6195   -411   -164   -143       N  
ATOM   1869  CA  ASP B  56      66.449  89.808  -7.128  1.00 40.36           C  
ANISOU 1869  CA  ASP B  56     4586   4397   6351   -478    -64    163       C  
ATOM   1870  C   ASP B  56      67.286  88.539  -7.256  1.00 37.28           C  
ANISOU 1870  C   ASP B  56     4195   4289   5682   -480     91    143       C  
ATOM   1871  O   ASP B  56      66.825  87.519  -7.774  1.00 32.52           O  
ANISOU 1871  O   ASP B  56     3716   3843   4796   -425    142    217       O  
ATOM   1872  CB  ASP B  56      66.915  90.820  -8.175  1.00 36.80           C  
ANISOU 1872  CB  ASP B  56     4171   3728   6084   -660    -35    447       C  
ATOM   1873  CG  ASP B  56      66.954  90.212  -9.578  1.00 41.31           C  
ANISOU 1873  CG  ASP B  56     4931   4436   6327   -740     94    750       C  
ATOM   1874  OD1 ASP B  56      65.882  90.054 -10.207  1.00 38.65           O  
ANISOU 1874  OD1 ASP B  56     4763   4088   5834   -678    -20    897       O  
ATOM   1875  OD2 ASP B  56      68.054  89.860 -10.038  1.00 39.54           O  
ANISOU 1875  OD2 ASP B  56     4677   4347   6001   -860    306    811       O  
ATOM   1876  N   SER B  57      68.520  88.598  -6.781  1.00 42.70           N  
ANISOU 1876  N   SER B  57     4718   5015   6491   -536    143     21       N  
ATOM   1877  CA  SER B  57      69.397  87.437  -6.866  1.00 37.98           C  
ANISOU 1877  CA  SER B  57     4068   4648   5713   -511    271    -20       C  
ATOM   1878  C   SER B  57      68.838  86.247  -6.094  1.00 35.02           C  
ANISOU 1878  C   SER B  57     3767   4443   5096   -329    206   -160       C  
ATOM   1879  O   SER B  57      68.843  85.116  -6.591  1.00 35.08           O  
ANISOU 1879  O   SER B  57     3854   4592   4884   -280    302   -106       O  
ATOM   1880  CB  SER B  57      70.815  87.792  -6.405  1.00 45.33           C  
ANISOU 1880  CB  SER B  57     4747   5568   6907   -592    286   -150       C  
ATOM   1881  OG  SER B  57      71.583  86.610  -6.296  1.00 54.54           O  
ANISOU 1881  OG  SER B  57     5829   6942   7951   -510    358   -233       O  
ATOM   1882  N   GLU B  58      68.300  86.494  -4.901  1.00 30.92           N  
ANISOU 1882  N   GLU B  58     3241   3899   4609   -236     61   -340       N  
ATOM   1883  CA  GLU B  58      67.664  85.418  -4.149  1.00 28.32           C  
ANISOU 1883  CA  GLU B  58     3010   3716   4033    -94     34   -423       C  
ATOM   1884  C   GLU B  58      66.457  84.820  -4.859  1.00 29.38           C  
ANISOU 1884  C   GLU B  58     3292   3862   4010    -70     94   -284       C  
ATOM   1885  O   GLU B  58      66.301  83.609  -4.899  1.00 32.89           O  
ANISOU 1885  O   GLU B  58     3814   4421   4263    -11    141   -257       O  
ATOM   1886  CB  GLU B  58      67.210  85.909  -2.769  1.00 33.16           C  
ANISOU 1886  CB  GLU B  58     3620   4319   4662    -19    -81   -642       C  
ATOM   1887  CG  GLU B  58      68.344  86.263  -1.830  1.00 35.51           C  
ANISOU 1887  CG  GLU B  58     3800   4647   5047    -16   -211   -839       C  
ATOM   1888  CD  GLU B  58      67.808  86.791  -0.510  1.00 51.94           C  
ANISOU 1888  CD  GLU B  58     5928   6735   7069     56   -314  -1091       C  
ATOM   1889  OE1 GLU B  58      66.836  87.579  -0.548  1.00 42.45           O  
ANISOU 1889  OE1 GLU B  58     4744   5401   5983     53   -279  -1143       O  
ATOM   1890  OE2 GLU B  58      68.338  86.403   0.557  1.00 54.64           O  
ANISOU 1890  OE2 GLU B  58     6299   7221   7242    127   -435  -1243       O  
ATOM   1891  N   ALA B  59      65.576  85.673  -5.397  1.00 27.80           N  
ANISOU 1891  N   ALA B  59     3118   3516   3929   -111     57   -202       N  
ATOM   1892  CA  ALA B  59      64.400  85.187  -6.075  1.00 26.71           C  
ANISOU 1892  CA  ALA B  59     3082   3379   3688    -90     51    -89       C  
ATOM   1893  C   ALA B  59      64.820  84.372  -7.289  1.00 27.94           C  
ANISOU 1893  C   ALA B  59     3342   3622   3652   -145    128     63       C  
ATOM   1894  O   ALA B  59      64.204  83.355  -7.605  1.00 27.17           O  
ANISOU 1894  O   ALA B  59     3331   3597   3394   -109    135     79       O  
ATOM   1895  CB  ALA B  59      63.512  86.345  -6.518  1.00 30.06           C  
ANISOU 1895  CB  ALA B  59     3492   3602   4326   -108    -60    -12       C  
ATOM   1896  N   ARG B  60      65.854  84.821  -7.988  1.00 28.36           N  
ANISOU 1896  N   ARG B  60     3382   3662   3732   -243    205    158       N  
ATOM   1897  CA  ARG B  60      66.295  84.057  -9.154  1.00 30.96           C  
ANISOU 1897  CA  ARG B  60     3820   4103   3841   -293    332    261       C  
ATOM   1898  C   ARG B  60      66.894  82.692  -8.785  1.00 32.18           C  
ANISOU 1898  C   ARG B  60     3944   4402   3880   -205    423    121       C  
ATOM   1899  O   ARG B  60      66.654  81.682  -9.462  1.00 35.52           O  
ANISOU 1899  O   ARG B  60     4485   4899   4111   -181    472    123       O  
ATOM   1900  CB  ARG B  60      67.239  84.881 -10.033  1.00 31.95           C  
ANISOU 1900  CB  ARG B  60     3937   4192   4010   -443    461    413       C  
ATOM   1901  CG  ARG B  60      66.483  85.876 -10.913  1.00 36.79           C  
ANISOU 1901  CG  ARG B  60     4698   4661   4621   -532    360    651       C  
ATOM   1902  CD  ARG B  60      67.392  86.561 -11.931  1.00 37.17           C  
ANISOU 1902  CD  ARG B  60     4801   4685   4637   -714    536    869       C  
ATOM   1903  NE  ARG B  60      68.353  87.457 -11.282  1.00 40.73           N  
ANISOU 1903  NE  ARG B  60     5031   5011   5432   -800    601    829       N  
ATOM   1904  CZ  ARG B  60      69.628  87.156 -11.048  1.00 45.84           C  
ANISOU 1904  CZ  ARG B  60     5487   5761   6169   -848    798    709       C  
ATOM   1905  NH1 ARG B  60      70.124  85.980 -11.428  1.00 50.60           N  
ANISOU 1905  NH1 ARG B  60     6097   6586   6544   -800    977    621       N  
ATOM   1906  NH2 ARG B  60      70.411  88.031 -10.438  1.00 48.66           N  
ANISOU 1906  NH2 ARG B  60     5623   5981   6886   -938    800    653       N  
ATOM   1907  N   GLN B  61      67.649  82.639  -7.703  1.00 30.24           N  
ANISOU 1907  N   GLN B  61     3548   4178   3764   -147    410    -11       N  
ATOM   1908  CA  GLN B  61      68.210  81.351  -7.280  1.00 32.17           C  
ANISOU 1908  CA  GLN B  61     3765   4518   3940    -37    442   -115       C  
ATOM   1909  C   GLN B  61      67.145  80.372  -6.815  1.00 33.65           C  
ANISOU 1909  C   GLN B  61     4080   4708   3998     51    371   -132       C  
ATOM   1910  O   GLN B  61      67.218  79.175  -7.103  1.00 31.62           O  
ANISOU 1910  O   GLN B  61     3887   4478   3651    109    415   -153       O  
ATOM   1911  CB  GLN B  61      69.249  81.539  -6.183  1.00 31.61           C  
ANISOU 1911  CB  GLN B  61     3512   4467   4031     17    372   -235       C  
ATOM   1912  CG  GLN B  61      70.455  82.324  -6.656  1.00 37.98           C  
ANISOU 1912  CG  GLN B  61     4129   5263   5039    -88    467   -239       C  
ATOM   1913  CD  GLN B  61      71.432  82.619  -5.529  1.00 53.42           C  
ANISOU 1913  CD  GLN B  61     5870   7223   7204    -45    325   -389       C  
ATOM   1914  OE1 GLN B  61      72.076  81.715  -5.004  1.00 49.26           O  
ANISOU 1914  OE1 GLN B  61     5263   6765   6688     83    257   -477       O  
ATOM   1915  NE2 GLN B  61      71.546  83.892  -5.157  1.00 51.25           N  
ANISOU 1915  NE2 GLN B  61     5502   6853   7119   -145    245   -427       N  
ATOM   1916  N   ILE B  62      66.176  80.869  -6.061  1.00 27.08           N  
ANISOU 1916  N   ILE B  62     3267   3831   3190     57    279   -139       N  
ATOM   1917  CA  ILE B  62      65.073  80.036  -5.592  1.00 29.75           C  
ANISOU 1917  CA  ILE B  62     3694   4166   3442    102    257   -140       C  
ATOM   1918  C   ILE B  62      64.225  79.549  -6.773  1.00 33.71           C  
ANISOU 1918  C   ILE B  62     4290   4634   3883     52    265    -72       C  
ATOM   1919  O   ILE B  62      63.796  78.371  -6.819  1.00 29.96           O  
ANISOU 1919  O   ILE B  62     3887   4150   3348     74    276    -81       O  
ATOM   1920  CB  ILE B  62      64.228  80.781  -4.487  1.00 26.30           C  
ANISOU 1920  CB  ILE B  62     3222   3710   3062    115    215   -200       C  
ATOM   1921  CG1 ILE B  62      65.111  81.040  -3.263  1.00 29.71           C  
ANISOU 1921  CG1 ILE B  62     3611   4202   3474    173    172   -305       C  
ATOM   1922  CG2 ILE B  62      62.972  80.004  -4.131  1.00 28.32           C  
ANISOU 1922  CG2 ILE B  62     3533   3961   3266    122    254   -184       C  
ATOM   1923  CD1 ILE B  62      64.427  81.900  -2.178  1.00 30.35           C  
ANISOU 1923  CD1 ILE B  62     3674   4285   3574    189    156   -429       C  
ATOM   1924  N   ALA B  63      63.957  80.444  -7.724  1.00 28.90           N  
ANISOU 1924  N   ALA B  63     3695   3988   3296    -21    229      1       N  
ATOM   1925  CA  ALA B  63      63.201  80.072  -8.914  1.00 30.03           C  
ANISOU 1925  CA  ALA B  63     3953   4119   3339    -69    175     60       C  
ATOM   1926  C   ALA B  63      63.926  78.966  -9.690  1.00 34.35           C  
ANISOU 1926  C   ALA B  63     4600   4736   3715    -63    271     14       C  
ATOM   1927  O   ALA B  63      63.284  78.084 -10.240  1.00 30.06           O  
ANISOU 1927  O   ALA B  63     4153   4180   3088    -70    222    -25       O  
ATOM   1928  CB  ALA B  63      62.963  81.302  -9.843  1.00 26.30           C  
ANISOU 1928  CB  ALA B  63     3521   3593   2877   -143     88    197       C  
ATOM   1929  N   ALA B  64      65.253  79.023  -9.753  1.00 31.08           N  
ANISOU 1929  N   ALA B  64     4139   4381   3288    -52    408    -11       N  
ATOM   1930  CA  ALA B  64      66.003  78.033 -10.540  1.00 33.73           C  
ANISOU 1930  CA  ALA B  64     4538   4782   3497    -28    540    -99       C  
ATOM   1931  C   ALA B  64      65.910  76.661  -9.849  1.00 30.11           C  
ANISOU 1931  C   ALA B  64     4073   4266   3100     80    514   -208       C  
ATOM   1932  O   ALA B  64      65.807  75.637 -10.506  1.00 32.98           O  
ANISOU 1932  O   ALA B  64     4537   4610   3385    102    541   -303       O  
ATOM   1933  CB  ALA B  64      67.445  78.441 -10.720  1.00 36.26           C  
ANISOU 1933  CB  ALA B  64     4739   5173   3864    -39    719   -117       C  
ATOM   1934  N   ILE B  65      65.890  76.661  -8.527  1.00 25.57           N  
ANISOU 1934  N   ILE B  65     3410   3652   2655    141    451   -189       N  
ATOM   1935  CA  ILE B  65      65.713  75.392  -7.800  1.00 27.44           C  
ANISOU 1935  CA  ILE B  65     3681   3806   2941    226    415   -221       C  
ATOM   1936  C   ILE B  65      64.294  74.843  -8.013  1.00 32.03           C  
ANISOU 1936  C   ILE B  65     4362   4303   3504    160    351   -202       C  
ATOM   1937  O   ILE B  65      64.082  73.676  -8.432  1.00 31.57           O  
ANISOU 1937  O   ILE B  65     4385   4151   3459    172    347   -268       O  
ATOM   1938  CB  ILE B  65      65.984  75.582  -6.338  1.00 27.55           C  
ANISOU 1938  CB  ILE B  65     3627   3825   3017    290    356   -175       C  
ATOM   1939  CG1 ILE B  65      67.463  75.943  -6.109  1.00 32.54           C  
ANISOU 1939  CG1 ILE B  65     4119   4520   3726    364    364   -228       C  
ATOM   1940  CG2 ILE B  65      65.588  74.326  -5.529  1.00 30.49           C  
ANISOU 1940  CG2 ILE B  65     4089   4094   3403    350    315   -128       C  
ATOM   1941  CD1 ILE B  65      67.736  76.431  -4.662  1.00 36.65           C  
ANISOU 1941  CD1 ILE B  65     4584   5075   4264    413    244   -207       C  
ATOM   1942  N   LEU B  66      63.324  75.703  -7.754  1.00 30.65           N  
ANISOU 1942  N   LEU B  66     4154   4141   3350     90    295   -138       N  
ATOM   1943  CA  LEU B  66      61.924  75.351  -7.923  1.00 36.62           C  
ANISOU 1943  CA  LEU B  66     4929   4823   4161     16    226   -130       C  
ATOM   1944  C   LEU B  66      61.575  74.856  -9.319  1.00 40.61           C  
ANISOU 1944  C   LEU B  66     5533   5303   4595    -36    150   -201       C  
ATOM   1945  O   LEU B  66      60.804  73.905  -9.451  1.00 33.65           O  
ANISOU 1945  O   LEU B  66     4678   4318   3791    -78     93   -253       O  
ATOM   1946  CB  LEU B  66      61.027  76.544  -7.543  1.00 35.84           C  
ANISOU 1946  CB  LEU B  66     4726   4744   4147    -25    178    -82       C  
ATOM   1947  CG  LEU B  66      59.544  76.195  -7.426  1.00 33.30           C  
ANISOU 1947  CG  LEU B  66     4336   4345   3972    -92    129    -88       C  
ATOM   1948  CD1 LEU B  66      59.364  75.166  -6.296  1.00 29.97           C  
ANISOU 1948  CD1 LEU B  66     3918   3874   3596    -98    254    -65       C  
ATOM   1949  CD2 LEU B  66      58.751  77.487  -7.141  1.00 35.39           C  
ANISOU 1949  CD2 LEU B  66     4456   4619   4374    -97     85    -78       C  
ATOM   1950  N   GLY B  67      62.138  75.499 -10.349  1.00 28.46           N  
ANISOU 1950  N   GLY B  67     4059   3856   2900    -48    149   -206       N  
ATOM   1951  CA  GLY B  67      61.861  75.192 -11.723  1.00 31.63           C  
ANISOU 1951  CA  GLY B  67     4605   4280   3133   -100     69   -276       C  
ATOM   1952  C   GLY B  67      62.631  74.016 -12.297  1.00 38.05           C  
ANISOU 1952  C   GLY B  67     5524   5088   3846    -54    173   -447       C  
ATOM   1953  O   GLY B  67      62.483  73.720 -13.467  1.00 34.71           O  
ANISOU 1953  O   GLY B  67     5254   4707   3226    -94    124   -553       O  
ATOM   1954  N   GLY B  68      63.420  73.314 -11.495  1.00 34.07           N  
ANISOU 1954  N   GLY B  68     4949   4521   3474     41    294   -490       N  
ATOM   1955  CA  GLY B  68      64.101  72.128 -12.036  1.00 34.27           C  
ANISOU 1955  CA  GLY B  68     5049   4491   3481    113    381   -687       C  
ATOM   1956  C   GLY B  68      65.371  72.438 -12.820  1.00 39.16           C  
ANISOU 1956  C   GLY B  68     5679   5260   3939    157    579   -777       C  
ATOM   1957  O   GLY B  68      65.847  71.604 -13.620  1.00 33.80           O  
ANISOU 1957  O   GLY B  68     5083   4576   3185    208    681   -995       O  
ATOM   1958  N  AMET B  69      65.933  73.623 -12.600  0.36 35.01           N  
ANISOU 1958  N  AMET B  69     5057   4859   3386    131    658   -633       N  
ATOM   1959  N  BMET B  69      65.932  73.628 -12.621  0.64 34.55           N  
ANISOU 1959  N  BMET B  69     5001   4803   3324    130    659   -634       N  
ATOM   1960  CA AMET B  69      67.130  74.042 -13.337  0.36 39.69           C  
ANISOU 1960  CA AMET B  69     5622   5600   3858    131    894   -687       C  
ATOM   1961  CA BMET B  69      67.143  74.007 -13.369  0.64 38.06           C  
ANISOU 1961  CA BMET B  69     5419   5394   3648    132    898   -695       C  
ATOM   1962  C  AMET B  69      68.426  73.698 -12.607  0.36 40.68           C  
ANISOU 1962  C  AMET B  69     5524   5701   4232    264   1029   -764       C  
ATOM   1963  C  BMET B  69      68.431  73.663 -12.619  0.64 41.43           C  
ANISOU 1963  C  BMET B  69     5620   5794   4327    267   1031   -769       C  
ATOM   1964  O  AMET B  69      69.518  73.853 -13.155  0.36 43.06           O  
ANISOU 1964  O  AMET B  69     5733   6110   4519    278   1263   -854       O  
ATOM   1965  O  BMET B  69      69.528  73.798 -13.162  0.64 43.45           O  
ANISOU 1965  O  BMET B  69     5782   6156   4571    283   1265   -863       O  
ATOM   1966  CB AMET B  69      67.087  75.543 -13.627  0.36 45.76           C  
ANISOU 1966  CB AMET B  69     6399   6481   4506      1    909   -479       C  
ATOM   1967  CB BMET B  69      67.144  75.498 -13.706  0.64 43.30           C  
ANISOU 1967  CB BMET B  69     6094   6177   4181      2    925   -492       C  
ATOM   1968  CG AMET B  69      66.005  75.947 -14.601  0.36 52.61           C  
ANISOU 1968  CG AMET B  69     7497   7388   5104   -113    763   -394       C  
ATOM   1969  CG BMET B  69      65.990  75.963 -14.568  0.64 54.26           C  
ANISOU 1969  CG BMET B  69     7702   7594   5321   -112    758   -390       C  
ATOM   1970  SD AMET B  69      66.244  75.145 -16.195  0.36 51.49           S  
ANISOU 1970  SD AMET B  69     7614   7380   4570   -137    904   -604       S  
ATOM   1971  SD BMET B  69      66.030  77.747 -14.822  0.64 77.67           S  
ANISOU 1971  SD BMET B  69    10676  10615   8220   -246    754    -97       S  
ATOM   1972  CE AMET B  69      67.746  75.948 -16.756  0.36 60.64           C  
ANISOU 1972  CE AMET B  69     8676   8704   5661   -170   1253   -520       C  
ATOM   1973  CE BMET B  69      67.696  77.966 -15.452  0.64 65.34           C  
ANISOU 1973  CE BMET B  69     9061   9206   6558   -292   1156   -130       C  
ATOM   1974  N   VAL B  70      68.305  73.245 -11.365  1.00 33.67           N  
ANISOU 1974  N   VAL B  70     4543   4677   3573    359    879   -718       N  
ATOM   1975  CA  VAL B  70      69.477  72.866 -10.566  1.00 36.91           C  
ANISOU 1975  CA  VAL B  70     4747   5043   4234    510    910   -770       C  
ATOM   1976  C   VAL B  70      69.505  71.344 -10.503  1.00 41.03           C  
ANISOU 1976  C   VAL B  70     5316   5381   4894    655    869   -914       C  
ATOM   1977  O   VAL B  70      70.417  70.695 -11.016  1.00 38.44           O  
ANISOU 1977  O   VAL B  70     4900   5031   4676    772   1011  -1116       O  
ATOM   1978  CB  VAL B  70      69.425  73.513  -9.160  1.00 39.23           C  
ANISOU 1978  CB  VAL B  70     4940   5321   4643    520    740   -598       C  
ATOM   1979  CG1 VAL B  70      70.626  73.103  -8.308  1.00 36.10           C  
ANISOU 1979  CG1 VAL B  70     4343   4882   4492    688    687   -645       C  
ATOM   1980  CG2 VAL B  70      69.360  75.042  -9.285  1.00 41.58           C  
ANISOU 1980  CG2 VAL B  70     5192   5747   4860    376    772   -490       C  
ATOM   1981  N   TYR B  71      68.459  70.767  -9.928  1.00 33.86           N  
ANISOU 1981  N   TYR B  71     4540   4319   4006    637    693   -822       N  
ATOM   1982  CA  TYR B  71      68.264  69.335  -9.973  1.00 39.94           C  
ANISOU 1982  CA  TYR B  71     5395   4858   4923    729    640   -935       C  
ATOM   1983  C   TYR B  71      67.033  69.006 -10.823  1.00 34.30           C  
ANISOU 1983  C   TYR B  71     4873   4095   4064    590    602  -1011       C  
ATOM   1984  O   TYR B  71      65.961  69.501 -10.556  1.00 36.18           O  
ANISOU 1984  O   TYR B  71     5167   4358   4221    455    500   -860       O  
ATOM   1985  CB  TYR B  71      68.062  68.812  -8.564  1.00 38.36           C  
ANISOU 1985  CB  TYR B  71     5196   4481   4898    796    466   -737       C  
ATOM   1986  CG  TYR B  71      67.748  67.336  -8.535  1.00 37.68           C  
ANISOU 1986  CG  TYR B  71     5217   4091   5010    863    392   -794       C  
ATOM   1987  CD1 TYR B  71      68.755  66.397  -8.720  1.00 43.21           C  
ANISOU 1987  CD1 TYR B  71     5844   4621   5952   1065    407   -962       C  
ATOM   1988  CD2 TYR B  71      66.448  66.884  -8.314  1.00 32.99           C  
ANISOU 1988  CD2 TYR B  71     4767   3348   4419    724    311   -687       C  
ATOM   1989  CE1 TYR B  71      68.489  65.054  -8.684  1.00 46.42           C  
ANISOU 1989  CE1 TYR B  71     6352   4691   6595   1132    323  -1015       C  
ATOM   1990  CE2 TYR B  71      66.166  65.521  -8.297  1.00 35.71           C  
ANISOU 1990  CE2 TYR B  71     5205   3364   4998    759    243   -732       C  
ATOM   1991  CZ  TYR B  71      67.193  64.617  -8.459  1.00 36.59           C  
ANISOU 1991  CZ  TYR B  71     5274   3283   5345    967    238   -886       C  
ATOM   1992  OH  TYR B  71      66.967  63.246  -8.448  1.00 40.53           O  
ANISOU 1992  OH  TYR B  71     5867   3395   6137   1016    155   -939       O  
ATOM   1993  N   LYS B  72      67.201  68.196 -11.862  1.00 37.38           N  
ANISOU 1993  N   LYS B  72     5345   4420   4436    629    676  -1280       N  
ATOM   1994  CA  LYS B  72      66.068  67.812 -12.695  1.00 39.64           C  
ANISOU 1994  CA  LYS B  72     5816   4653   4594    501    583  -1398       C  
ATOM   1995  C   LYS B  72      65.389  66.570 -12.108  1.00 42.35           C  
ANISOU 1995  C   LYS B  72     6202   4661   5228    509    430  -1399       C  
ATOM   1996  O   LYS B  72      66.071  65.612 -11.784  1.00 40.71           O  
ANISOU 1996  O   LYS B  72     5957   4237   5272    663    451  -1484       O  
ATOM   1997  CB  LYS B  72      66.548  67.506 -14.106  1.00 39.85           C  
ANISOU 1997  CB  LYS B  72     5949   4775   4419    528    732  -1729       C  
ATOM   1998  CG  LYS B  72      65.506  66.817 -14.975  1.00 42.83           C  
ANISOU 1998  CG  LYS B  72     6529   5051   4693    428    583  -1939       C  
ATOM   1999  CD  LYS B  72      66.109  66.327 -16.290  1.00 41.69           C  
ANISOU 1999  CD  LYS B  72     6519   4990   4330    487    750  -2330       C  
ATOM   2000  CE  LYS B  72      65.167  65.394 -17.004  1.00 52.90           C  
ANISOU 2000  CE  LYS B  72     8132   6237   5731    418    543  -2553       C  
ATOM   2001  NZ  LYS B  72      64.957  64.120 -16.267  1.00 54.41           N  
ANISOU 2001  NZ  LYS B  72     8254   6018   6400    485    432  -2645       N  
ATOM   2002  N   PRO B  73      64.055  66.599 -11.936  1.00 39.38           N  
ANISOU 2002  N   PRO B  73     5881   4218   4864    342    277  -1287       N  
ATOM   2003  CA  PRO B  73      63.359  65.365 -11.524  1.00 34.42           C  
ANISOU 2003  CA  PRO B  73     5293   3246   4540    303    162  -1296       C  
ATOM   2004  C   PRO B  73      63.735  64.279 -12.491  1.00 38.85           C  
ANISOU 2004  C   PRO B  73     5950   3626   5185    382    166  -1660       C  
ATOM   2005  O   PRO B  73      63.566  64.470 -13.690  1.00 46.20           O  
ANISOU 2005  O   PRO B  73     6979   4705   5869    331    160  -1913       O  
ATOM   2006  CB  PRO B  73      61.884  65.720 -11.700  1.00 34.39           C  
ANISOU 2006  CB  PRO B  73     5296   3269   4500     87     24  -1234       C  
ATOM   2007  CG  PRO B  73      61.849  67.211 -11.469  1.00 36.77           C  
ANISOU 2007  CG  PRO B  73     5522   3882   4567     57     64  -1039       C  
ATOM   2008  CD  PRO B  73      63.135  67.743 -12.064  1.00 42.61           C  
ANISOU 2008  CD  PRO B  73     6284   4829   5079    186    203  -1141       C  
ATOM   2009  N   GLN B  74      64.274  63.173 -11.986  1.00 42.49           N  
ANISOU 2009  N   GLN B  74     6400   3770   5976    519    168  -1692       N  
ATOM   2010  CA  GLN B  74      64.886  62.187 -12.866  1.00 51.52           C  
ANISOU 2010  CA  GLN B  74     7603   4733   7239    654    209  -2090       C  
ATOM   2011  C   GLN B  74      63.903  61.490 -13.794  1.00 50.52           C  
ANISOU 2011  C   GLN B  74     7618   4441   7137    509     74  -2388       C  
ATOM   2012  O   GLN B  74      64.277  61.086 -14.888  1.00 46.65           O  
ANISOU 2012  O   GLN B  74     7219   4005   6500    559    137  -2710       O  
ATOM   2013  CB  GLN B  74      65.679  61.155 -12.067  1.00 58.98           C  
ANISOU 2013  CB  GLN B  74     8488   5317   8606    859    198  -2041       C  
ATOM   2014  CG  GLN B  74      67.015  61.674 -11.567  1.00 73.82           C  
ANISOU 2014  CG  GLN B  74    10206   7366  10474   1072    316  -1939       C  
ATOM   2015  CD  GLN B  74      67.896  60.564 -11.023  1.00 90.03           C  
ANISOU 2015  CD  GLN B  74    12192   9052  12964   1319    259  -1957       C  
ATOM   2016  OE1 GLN B  74      67.711  59.392 -11.353  1.00 90.26           O  
ANISOU 2016  OE1 GLN B  74    12306   8794  13194   1321    204  -2074       O  
ATOM   2017  NE2 GLN B  74      68.858  60.928 -10.180  1.00 96.86           N  
ANISOU 2017  NE2 GLN B  74    12900   9985  13916   1494    248  -1760       N  
ATOM   2018  N   ALA B  75      62.648  61.366 -13.380  1.00 45.14           N  
ANISOU 2018  N   ALA B  75     6940   3617   6593    301    -95  -2208       N  
ATOM   2019  CA  ALA B  75      61.720  60.533 -14.136  1.00 48.91           C  
ANISOU 2019  CA  ALA B  75     7509   3865   7208    155   -271  -2492       C  
ATOM   2020  C   ALA B  75      61.098  61.255 -15.320  1.00 47.19           C  
ANISOU 2020  C   ALA B  75     7376   3980   6572     24   -370  -2682       C  
ATOM   2021  O   ALA B  75      60.476  60.630 -16.165  1.00 52.86           O  
ANISOU 2021  O   ALA B  75     8179   4629   7275    -88   -504  -2891       O  
ATOM   2022  CB  ALA B  75      60.637  59.969 -13.226  1.00 51.46           C  
ANISOU 2022  CB  ALA B  75     7763   3848   7941    -33   -400  -2243       C  
ATOM   2023  N   LEU B  76      61.260  62.567 -15.386  1.00 44.19           N  
ANISOU 2023  N   LEU B  76     6976   3986   5828     27   -304  -2525       N  
ATOM   2024  CA  LEU B  76      60.654  63.323 -16.476  1.00 47.05           C  
ANISOU 2024  CA  LEU B  76     7449   4644   5785    -88   -446  -2654       C  
ATOM   2025  C   LEU B  76      61.488  63.224 -17.738  1.00 54.73           C  
ANISOU 2025  C   LEU B  76     8606   5824   6366     -8   -295  -2915       C  
ATOM   2026  O   LEU B  76      62.705  63.386 -17.707  1.00 66.72           O  
ANISOU 2026  O   LEU B  76    10118   7450   7781    156    -27  -2914       O  
ATOM   2027  CB  LEU B  76      60.430  64.780 -16.070  1.00 44.45           C  
ANISOU 2027  CB  LEU B  76     7025   4625   5240   -139   -426  -2280       C  
ATOM   2028  CG  LEU B  76      59.422  64.889 -14.930  1.00 52.80           C  
ANISOU 2028  CG  LEU B  76     7886   5530   6646   -264   -522  -1971       C  
ATOM   2029  CD1 LEU B  76      59.186  66.337 -14.562  1.00 59.93           C  
ANISOU 2029  CD1 LEU B  76     8689   6714   7366   -294   -504  -1667       C  
ATOM   2030  CD2 LEU B  76      58.122  64.210 -15.324  1.00 59.52           C  
ANISOU 2030  CD2 LEU B  76     8716   6170   7729   -445   -800  -2139       C  
ATOM   2031  N   GLU B  77      60.820  62.934 -18.845  1.00 50.50           N  
ANISOU 2031  N   GLU B  77     8218   5339   5630   -140   -458  -3112       N  
ATOM   2032  CA  GLU B  77      61.487  62.776 -20.125  1.00 60.39           C  
ANISOU 2032  CA  GLU B  77     9702   6769   6476   -106   -309  -3348       C  
ATOM   2033  C   GLU B  77      61.192  63.971 -21.022  1.00 62.13           C  
ANISOU 2033  C   GLU B  77    10039   7401   6167   -240   -361  -3268       C  
ATOM   2034  O   GLU B  77      61.994  64.321 -21.893  1.00 68.13           O  
ANISOU 2034  O   GLU B  77    10970   8391   6528   -200   -148  -3297       O  
ATOM   2035  CB  GLU B  77      61.049  61.471 -20.789  1.00 77.12           C  
ANISOU 2035  CB  GLU B  77    11932   8638   8732   -162   -442  -3669       C  
ATOM   2036  CG  GLU B  77      61.790  61.133 -22.078  1.00 95.08           C  
ANISOU 2036  CG  GLU B  77    14485  11036  10604   -100   -272  -3961       C  
ATOM   2037  CD  GLU B  77      61.074  61.620 -23.329  1.00100.00           C  
ANISOU 2037  CD  GLU B  77    15325  11944  10726   -309   -440  -4070       C  
ATOM   2038  OE1 GLU B  77      59.911  62.069 -23.226  1.00 98.23           O  
ANISOU 2038  OE1 GLU B  77    14970  11801  10550   -479   -748  -3954       O  
ATOM   2039  OE2 GLU B  77      61.680  61.547 -24.419  1.00100.38           O  
ANISOU 2039  OE2 GLU B  77    15645  12140  10354   -272   -283  -4253       O  
ATOM   2040  N   SER B  78      60.031  64.587 -20.818  1.00 62.90           N  
ANISOU 2040  N   SER B  78     8473   7379   8047    -15   -438  -2811       N  
ATOM   2041  CA  SER B  78      59.695  65.818 -21.528  1.00 60.14           C  
ANISOU 2041  CA  SER B  78     7972   7599   7278    214   -918  -2893       C  
ATOM   2042  C   SER B  78      58.708  66.663 -20.743  1.00 61.29           C  
ANISOU 2042  C   SER B  78     7941   7803   7543     30   -982  -2887       C  
ATOM   2043  O   SER B  78      57.997  66.153 -19.878  1.00 58.93           O  
ANISOU 2043  O   SER B  78     7544   7134   7713   -324   -702  -3066       O  
ATOM   2044  CB  SER B  78      59.148  65.519 -22.930  1.00 63.77           C  
ANISOU 2044  CB  SER B  78     8208   8414   7607    390  -1206  -3617       C  
ATOM   2045  OG  SER B  78      57.860  64.930 -22.876  1.00 67.55           O  
ANISOU 2045  OG  SER B  78     8306   8834   8527     65  -1171  -4378       O  
ATOM   2046  N   ILE B  79      58.668  67.957 -21.043  1.00 55.75           N  
ANISOU 2046  N   ILE B  79     7241   7507   6435    291  -1257  -2662       N  
ATOM   2047  CA  ILE B  79      57.705  68.854 -20.415  1.00 55.11           C  
ANISOU 2047  CA  ILE B  79     7005   7491   6444    184  -1281  -2649       C  
ATOM   2048  C   ILE B  79      57.117  69.886 -21.379  1.00 63.87           C  
ANISOU 2048  C   ILE B  79     7953   9145   7169    630  -1626  -2793       C  
ATOM   2049  O   ILE B  79      57.754  70.274 -22.357  1.00 56.87           O  
ANISOU 2049  O   ILE B  79     7236   8562   5809   1053  -1792  -2652       O  
ATOM   2050  CB  ILE B  79      58.338  69.618 -19.228  1.00 52.09           C  
ANISOU 2050  CB  ILE B  79     6919   6899   5974      5  -1038  -1980       C  
ATOM   2051  CG1 ILE B  79      59.529  70.447 -19.707  1.00 48.58           C  
ANISOU 2051  CG1 ILE B  79     6741   6692   5026    288  -1096  -1523       C  
ATOM   2052  CG2 ILE B  79      58.752  68.656 -18.132  1.00 50.39           C  
ANISOU 2052  CG2 ILE B  79     6850   6228   6068   -334   -708  -1792       C  
ATOM   2053  CD1 ILE B  79      60.204  71.247 -18.606  1.00 45.52           C  
ANISOU 2053  CD1 ILE B  79     6577   6198   4522     45   -864  -1001       C  
ATOM   2054  N   GLU B  80      55.893  70.327 -21.098  1.00 58.56           N  
ANISOU 2054  N   GLU B  80     6965   8593   6690    591  -1686  -3045       N  
ATOM   2055  CA  GLU B  80      55.336  71.478 -21.790  1.00 60.35           C  
ANISOU 2055  CA  GLU B  80     7084   9326   6520   1113  -1928  -3001       C  
ATOM   2056  C   GLU B  80      55.830  72.727 -21.074  1.00 66.71           C  
ANISOU 2056  C   GLU B  80     8286   9918   7141   1129  -1617  -2295       C  
ATOM   2057  O   GLU B  80      55.544  72.917 -19.888  1.00 54.38           O  
ANISOU 2057  O   GLU B  80     6757   7996   5911    716  -1334  -2135       O  
ATOM   2058  CB  GLU B  80      53.812  71.442 -21.755  1.00 64.81           C  
ANISOU 2058  CB  GLU B  80     7076  10150   7398   1099  -2095  -3562       C  
ATOM   2059  CG  GLU B  80      53.221  70.139 -22.243  1.00 80.79           C  
ANISOU 2059  CG  GLU B  80     8626  12318   9752    871  -2294  -4421       C  
ATOM   2060  CD  GLU B  80      51.740  70.248 -22.496  1.00 93.59           C  
ANISOU 2060  CD  GLU B  80     9551  14437  11572    971  -2562  -5071       C  
ATOM   2061  OE1 GLU B  80      51.239  71.389 -22.608  1.00 94.73           O  
ANISOU 2061  OE1 GLU B  80     9605  14957  11429   1446  -2696  -4788       O  
ATOM   2062  OE2 GLU B  80      51.078  69.193 -22.580  1.00101.31           O  
ANISOU 2062  OE2 GLU B  80    10054  15424  13014    579  -2582  -5873       O  
ATOM   2063  N   MET B  81      56.568  73.574 -21.784  1.00 60.19           N  
ANISOU 2063  N   MET B  81     7789   9285   5795   1577  -1599  -1910       N  
ATOM   2064  CA  MET B  81      57.156  74.766 -21.170  1.00 55.15           C  
ANISOU 2064  CA  MET B  81     7550   8403   5000   1520  -1192  -1321       C  
ATOM   2065  C   MET B  81      56.097  75.693 -20.562  1.00 55.91           C  
ANISOU 2065  C   MET B  81     7559   8447   5238   1540   -997  -1237       C  
ATOM   2066  O   MET B  81      54.997  75.825 -21.106  1.00 57.69           O  
ANISOU 2066  O   MET B  81     7450   9027   5442   1949  -1229  -1506       O  
ATOM   2067  CB  MET B  81      57.990  75.528 -22.201  1.00 63.72           C  
ANISOU 2067  CB  MET B  81     8995   9673   5543   2051  -1101  -1002       C  
ATOM   2068  CG  MET B  81      58.899  76.586 -21.592  1.00 70.03           C  
ANISOU 2068  CG  MET B  81    10217  10147   6244   1837   -572   -494       C  
ATOM   2069  SD  MET B  81      60.113  77.214 -22.771  1.00 91.66           S  
ANISOU 2069  SD  MET B  81    13394  12962   8470   2328   -326   -182       S  
ATOM   2070  CE  MET B  81      61.078  78.274 -21.692  1.00 79.10           C  
ANISOU 2070  CE  MET B  81    12129  10946   6980   1755    348    196       C  
ATOM   2071  N   ALA B  82      56.428  76.331 -19.435  1.00 50.80           N  
ANISOU 2071  N   ALA B  82     7182   7402   4717   1108   -567   -890       N  
ATOM   2072  CA  ALA B  82      55.495  77.238 -18.770  1.00 51.71           C  
ANISOU 2072  CA  ALA B  82     7286   7370   4991   1078   -268   -778       C  
ATOM   2073  C   ALA B  82      55.233  78.480 -19.611  1.00 54.73           C  
ANISOU 2073  C   ALA B  82     7851   7958   4985   1779    -80   -506       C  
ATOM   2074  O   ALA B  82      56.159  79.061 -20.164  1.00 57.78           O  
ANISOU 2074  O   ALA B  82     8626   8329   4998   2017    142   -204       O  
ATOM   2075  CB  ALA B  82      56.016  77.635 -17.370  1.00 50.60           C  
ANISOU 2075  CB  ALA B  82     7456   6769   5002    415    186   -511       C  
ATOM   2076  N   PHE B  83      53.968  78.876 -19.695  1.00 58.25           N  
ANISOU 2076  N   PHE B  83     8015   8584   5534   2143   -111   -599       N  
ATOM   2077  CA  PHE B  83      53.557  80.056 -20.459  1.00 62.40           C  
ANISOU 2077  CA  PHE B  83     8708   9328   5674   2961    116   -275       C  
ATOM   2078  C   PHE B  83      54.039  80.020 -21.908  1.00 65.13           C  
ANISOU 2078  C   PHE B  83     9168  10132   5448   3698   -162   -227       C  
ATOM   2079  O   PHE B  83      54.421  81.046 -22.474  1.00 67.15           O  
ANISOU 2079  O   PHE B  83     9893  10339   5284   4257    263    225       O  
ATOM   2080  CB  PHE B  83      54.017  81.334 -19.761  1.00 62.21           C  
ANISOU 2080  CB  PHE B  83     9263   8754   5620   2769    925    230       C  
ATOM   2081  CG  PHE B  83      53.624  81.395 -18.307  1.00 58.61           C  
ANISOU 2081  CG  PHE B  83     8775   7845   5649   2021   1231    179       C  
ATOM   2082  CD1 PHE B  83      52.290  81.507 -17.941  1.00 61.27           C  
ANISOU 2082  CD1 PHE B  83     8751   8228   6301   2158   1230     57       C  
ATOM   2083  CD2 PHE B  83      54.586  81.315 -17.307  1.00 54.37           C  
ANISOU 2083  CD2 PHE B  83     8538   6894   5225   1205   1508    231       C  
ATOM   2084  CE1 PHE B  83      51.921  81.548 -16.598  1.00 64.75           C  
ANISOU 2084  CE1 PHE B  83     9215   8208   7178   1476   1568     14       C  
ATOM   2085  CE2 PHE B  83      54.225  81.369 -15.966  1.00 52.82           C  
ANISOU 2085  CE2 PHE B  83     8365   6322   5381    559   1791    183       C  
ATOM   2086  CZ  PHE B  83      52.891  81.473 -15.608  1.00 59.06           C  
ANISOU 2086  CZ  PHE B  83     8874   7065   6500    682   1847     84       C  
ATOM   2087  N   SER B  84      54.003  78.829 -22.495  1.00 65.77           N  
ANISOU 2087  N   SER B  84     8859  10611   5520   3691   -795   -711       N  
ATOM   2088  CA  SER B  84      54.480  78.612 -23.856  1.00 71.09           C  
ANISOU 2088  CA  SER B  84     9637  11736   5639   4320  -1105   -754       C  
ATOM   2089  C   SER B  84      53.857  77.350 -24.430  1.00 73.20           C  
ANISOU 2089  C   SER B  84     9285  12555   5973   4338  -1827  -1469       C  
ATOM   2090  O   SER B  84      53.413  76.473 -23.687  1.00 71.53           O  
ANISOU 2090  O   SER B  84     8661  12193   6324   3681  -1985  -1910       O  
ATOM   2091  CB  SER B  84      56.005  78.449 -23.860  1.00 64.14           C  
ANISOU 2091  CB  SER B  84     9244  10460   4667   3954   -845   -519       C  
ATOM   2092  OG  SER B  84      56.463  78.043 -25.141  1.00 71.38           O  
ANISOU 2092  OG  SER B  84    10247  11767   5108   4481  -1149   -629       O  
ATOM   2093  N   ASP B  85      53.850  77.250 -25.753  1.00 78.63           N  
ANISOU 2093  N   ASP B  85     9943  13857   6075   5073  -2198  -1612       N  
ATOM   2094  CA  ASP B  85      53.426  76.026 -26.422  1.00 79.75           C  
ANISOU 2094  CA  ASP B  85     9546  14483   6273   4988  -2787  -2370       C  
ATOM   2095  C   ASP B  85      54.617  75.138 -26.754  1.00 82.23           C  
ANISOU 2095  C   ASP B  85    10144  14462   6636   4585  -2735  -2441       C  
ATOM   2096  O   ASP B  85      54.453  74.041 -27.288  1.00 79.28           O  
ANISOU 2096  O   ASP B  85     9434  14252   6438   4367  -3004  -3002       O  
ATOM   2097  CB  ASP B  85      52.637  76.353 -27.686  1.00 88.14           C  
ANISOU 2097  CB  ASP B  85    10373  16169   6949   5748  -2937  -2520       C  
ATOM   2098  CG  ASP B  85      51.400  77.163 -27.389  1.00107.55           C  
ANISOU 2098  CG  ASP B  85    12488  18999   9378   6177  -2969  -2461       C  
ATOM   2099  OD1 ASP B  85      50.995  77.188 -26.204  1.00100.65           O  
ANISOU 2099  OD1 ASP B  85    11358  17926   8960   5786  -2982  -2487       O  
ATOM   2100  OD2 ASP B  85      50.837  77.772 -28.326  1.00113.87           O  
ANISOU 2100  OD2 ASP B  85    13263  20290   9710   6924  -2960  -2380       O  
ATOM   2101  N   LEU B  86      55.815  75.609 -26.422  1.00 71.58           N  
ANISOU 2101  N   LEU B  86     9404  12636   5156   4472  -2329  -1872       N  
ATOM   2102  CA  LEU B  86      57.029  74.847 -26.699  1.00 72.02           C  
ANISOU 2102  CA  LEU B  86     9711  12381   5274   4145  -2236  -1861       C  
ATOM   2103  C   LEU B  86      57.166  73.656 -25.758  1.00 68.13           C  
ANISOU 2103  C   LEU B  86     8991  11583   5312   3348  -2341  -2229       C  
ATOM   2104  O   LEU B  86      56.630  73.665 -24.646  1.00 63.28           O  
ANISOU 2104  O   LEU B  86     8174  10689   5182   2871  -2211  -2243       O  
ATOM   2105  CB  LEU B  86      58.269  75.736 -26.592  1.00 74.96           C  
ANISOU 2105  CB  LEU B  86    10703  12332   5448   4199  -1694  -1189       C  
ATOM   2106  CG  LEU B  86      58.402  76.856 -27.627  1.00 77.66           C  
ANISOU 2106  CG  LEU B  86    11365  12733   5411   4932  -1361   -787       C  
ATOM   2107  CD1 LEU B  86      59.657  77.665 -27.348  1.00 80.38           C  
ANISOU 2107  CD1 LEU B  86    12244  12542   5756   4770   -724   -241       C  
ATOM   2108  CD2 LEU B  86      58.435  76.285 -29.026  1.00 81.87           C  
ANISOU 2108  CD2 LEU B  86    11786  13576   5745   5342  -1606  -1064       C  
ATOM   2109  N   ILE B  87      57.880  72.635 -26.219  1.00 65.16           N  
ANISOU 2109  N   ILE B  87     8666  11135   4957   3187  -2427  -2457       N  
ATOM   2110  CA  ILE B  87      58.143  71.440 -25.431  1.00 62.75           C  
ANISOU 2110  CA  ILE B  87     8221  10411   5211   2496  -2349  -2700       C  
ATOM   2111  C   ILE B  87      59.642  71.324 -25.176  1.00 58.65           C  
ANISOU 2111  C   ILE B  87     8115   9484   4684   2319  -2021  -2202       C  
ATOM   2112  O   ILE B  87      60.438  71.664 -26.037  1.00 65.15           O  
ANISOU 2112  O   ILE B  87     9244  10429   5080   2718  -1970  -1978       O  
ATOM   2113  CB  ILE B  87      57.615  70.175 -26.154  1.00 67.47           C  
ANISOU 2113  CB  ILE B  87     8464  11256   5916   2431  -2662  -3497       C  
ATOM   2114  CG1 ILE B  87      56.089  70.138 -26.103  1.00 81.72           C  
ANISOU 2114  CG1 ILE B  87     9682  13382   7984   2375  -2886  -4021       C  
ATOM   2115  CG2 ILE B  87      58.202  68.899 -25.564  1.00 65.66           C  
ANISOU 2115  CG2 ILE B  87     8277  10474   6197   1849  -2398  -3623       C  
ATOM   2116  CD1 ILE B  87      55.514  68.741 -26.017  1.00 95.02           C  
ANISOU 2116  CD1 ILE B  87    10953  14927  10224   1841  -2877  -4762       C  
ATOM   2117  N   ILE B  88      60.028  70.880 -23.980  1.00 55.24           N  
ANISOU 2117  N   ILE B  88     7682   8605   4700   1764  -1778  -2015       N  
ATOM   2118  CA  ILE B  88      61.421  70.546 -23.699  1.00 52.56           C  
ANISOU 2118  CA  ILE B  88     7593   7993   4385   1607  -1532  -1625       C  
ATOM   2119  C   ILE B  88      61.564  69.030 -23.554  1.00 65.95           C  
ANISOU 2119  C   ILE B  88     9177   9433   6446   1350  -1496  -1915       C  
ATOM   2120  O   ILE B  88      60.808  68.385 -22.829  1.00 54.40           O  
ANISOU 2120  O   ILE B  88     7515   7750   5405   1006  -1442  -2177       O  
ATOM   2121  CB  ILE B  88      61.963  71.285 -22.449  1.00 48.86           C  
ANISOU 2121  CB  ILE B  88     7244   7307   4013   1272  -1252  -1113       C  
ATOM   2122  CG1 ILE B  88      61.911  72.800 -22.669  1.00 49.57           C  
ANISOU 2122  CG1 ILE B  88     7521   7542   3770   1509  -1120   -845       C  
ATOM   2123  CG2 ILE B  88      63.384  70.833 -22.129  1.00 47.31           C  
ANISOU 2123  CG2 ILE B  88     7165   6971   3837   1134  -1070   -777       C  
ATOM   2124  CD1 ILE B  88      62.086  73.616 -21.391  1.00 51.64           C  
ANISOU 2124  CD1 ILE B  88     7855   7612   4155   1089   -828   -522       C  
ATOM   2125  N   GLU B  89      62.514  68.449 -24.273  1.00 57.96           N  
ANISOU 2125  N   GLU B  89     8326   8396   5300   1534  -1436  -1872       N  
ATOM   2126  CA  GLU B  89      62.677  67.006 -24.227  1.00 56.45           C  
ANISOU 2126  CA  GLU B  89     8094   7899   5457   1349  -1284  -2129       C  
ATOM   2127  C   GLU B  89      64.118  66.651 -23.891  1.00 65.93           C  
ANISOU 2127  C   GLU B  89     9488   8883   6679   1375  -1007  -1592       C  
ATOM   2128  O   GLU B  89      65.050  67.313 -24.349  1.00 57.52           O  
ANISOU 2128  O   GLU B  89     8571   7995   5291   1621   -997  -1255       O  
ATOM   2129  CB  GLU B  89      62.244  66.375 -25.560  1.00 61.01           C  
ANISOU 2129  CB  GLU B  89     8617   8675   5891   1560  -1461  -2777       C  
ATOM   2130  CG  GLU B  89      62.328  64.854 -25.595  1.00 64.07           C  
ANISOU 2130  CG  GLU B  89     8996   8665   6684   1323  -1179  -3150       C  
ATOM   2131  CD  GLU B  89      61.567  64.254 -26.764  1.00 87.07           C  
ANISOU 2131  CD  GLU B  89    11753  11824   9505   1367  -1367  -4017       C  
ATOM   2132  OE1 GLU B  89      61.191  65.006 -27.691  1.00 92.32           O  
ANISOU 2132  OE1 GLU B  89    12360  13059   9659   1724  -1776  -4230       O  
ATOM   2133  OE2 GLU B  89      61.342  63.026 -26.759  1.00 93.52           O  
ANISOU 2133  OE2 GLU B  89    12516  12280  10738   1059  -1068  -4506       O  
ATOM   2134  N   TRP B  90      64.294  65.626 -23.062  1.00 55.34           N  
ANISOU 2134  N   TRP B  90     8135   7168   5726   1153   -734  -1499       N  
ATOM   2135  CA  TRP B  90      65.621  65.111 -22.760  1.00 55.13           C  
ANISOU 2135  CA  TRP B  90     8227   6998   5721   1277   -476   -999       C  
ATOM   2136  C   TRP B  90      65.819  63.836 -23.559  1.00 72.97           C  
ANISOU 2136  C   TRP B  90    10595   8975   8156   1411   -236  -1297       C  
ATOM   2137  O   TRP B  90      65.103  62.857 -23.357  1.00 61.69           O  
ANISOU 2137  O   TRP B  90     9156   7181   7102   1212     -4  -1671       O  
ATOM   2138  CB  TRP B  90      65.781  64.836 -21.264  1.00 54.30           C  
ANISOU 2138  CB  TRP B  90     8095   6704   5835   1081   -274   -582       C  
ATOM   2139  CG  TRP B  90      65.931  66.089 -20.447  1.00 59.42           C  
ANISOU 2139  CG  TRP B  90     8667   7658   6251    936   -449   -242       C  
ATOM   2140  CD1 TRP B  90      67.097  66.630 -19.972  1.00 49.94           C  
ANISOU 2140  CD1 TRP B  90     7417   6739   4819    987   -452    240       C  
ATOM   2141  CD2 TRP B  90      64.877  66.964 -20.022  1.00 54.11           C  
ANISOU 2141  CD2 TRP B  90     7935   7051   5573    685   -597   -422       C  
ATOM   2142  NE1 TRP B  90      66.827  67.790 -19.273  1.00 52.61           N  
ANISOU 2142  NE1 TRP B  90     7703   7284   5002    725   -564    322       N  
ATOM   2143  CE2 TRP B  90      65.475  68.015 -19.288  1.00 47.13           C  
ANISOU 2143  CE2 TRP B  90     7036   6426   4445    565   -633    -33       C  
ATOM   2144  CE3 TRP B  90      63.485  66.958 -20.184  1.00 50.16           C  
ANISOU 2144  CE3 TRP B  90     7351   6437   5269    540   -678   -908       C  
ATOM   2145  CZ2 TRP B  90      64.729  69.046 -18.713  1.00 54.37           C  
ANISOU 2145  CZ2 TRP B  90     7942   7406   5310    315   -685    -76       C  
ATOM   2146  CZ3 TRP B  90      62.746  67.987 -19.622  1.00 56.38           C  
ANISOU 2146  CZ3 TRP B  90     8080   7331   6010    353   -772   -904       C  
ATOM   2147  CH2 TRP B  90      63.372  69.017 -18.889  1.00 51.11           C  
ANISOU 2147  CH2 TRP B  90     7484   6836   5098    246   -744   -468       C  
ATOM   2148  N   PHE B  91      66.780  63.865 -24.477  1.00 59.43           N  
ANISOU 2148  N   PHE B  91     9003   7382   6197   1720   -213  -1166       N  
ATOM   2149  CA  PHE B  91      66.997  62.749 -25.397  1.00 63.36           C  
ANISOU 2149  CA  PHE B  91     9652   7619   6804   1860     42  -1492       C  
ATOM   2150  C   PHE B  91      68.407  62.171 -25.306  1.00 64.17           C  
ANISOU 2150  C   PHE B  91     9867   7541   6975   2127    403   -942       C  
ATOM   2151  O   PHE B  91      69.400  62.864 -25.547  1.00 62.54           O  
ANISOU 2151  O   PHE B  91     9648   7608   6505   2351    328   -543       O  
ATOM   2152  CB  PHE B  91      66.695  63.175 -26.828  1.00 64.86           C  
ANISOU 2152  CB  PHE B  91     9923   8123   6600   2051   -230  -1973       C  
ATOM   2153  CG  PHE B  91      67.073  62.146 -27.854  1.00 77.74           C  
ANISOU 2153  CG  PHE B  91    11755   9533   8249   2199     42  -2309       C  
ATOM   2154  CD1 PHE B  91      66.289  61.021 -28.042  1.00 84.55           C  
ANISOU 2154  CD1 PHE B  91    12602  10090   9433   1938    252  -2980       C  
ATOM   2155  CD2 PHE B  91      68.214  62.303 -28.624  1.00 79.16           C  
ANISOU 2155  CD2 PHE B  91    12144   9772   8159   2557    166  -2000       C  
ATOM   2156  CE1 PHE B  91      66.635  60.068 -28.981  1.00 86.98           C  
ANISOU 2156  CE1 PHE B  91    13129  10157   9763   2022    577  -3349       C  
ATOM   2157  CE2 PHE B  91      68.567  61.354 -29.569  1.00 86.03           C  
ANISOU 2157  CE2 PHE B  91    13243  10404   9042   2690    470  -2313       C  
ATOM   2158  CZ  PHE B  91      67.774  60.237 -29.748  1.00 91.06           C  
ANISOU 2158  CZ  PHE B  91    13890  10740   9969   2417    673  -2994       C  
ATOM   2159  N   LYS B  92      68.483  60.890 -24.961  1.00 67.44           N  
ANISOU 2159  N   LYS B  92    10379   7471   7773   2120    865   -932       N  
ATOM   2160  CA  LYS B  92      69.760  60.226 -24.767  1.00 69.21           C  
ANISOU 2160  CA  LYS B  92    10683   7516   8096   2459   1263   -353       C  
ATOM   2161  C   LYS B  92      70.228  59.585 -26.073  1.00 72.56           C  
ANISOU 2161  C   LYS B  92    11328   7738   8502   2673   1535   -629       C  
ATOM   2162  O   LYS B  92      69.573  58.691 -26.601  1.00 76.28           O  
ANISOU 2162  O   LYS B  92    11975   7817   9191   2521   1821  -1215       O  
ATOM   2163  CB  LYS B  92      69.647  59.173 -23.659  1.00 71.91           C  
ANISOU 2163  CB  LYS B  92    11099   7390   8834   2462   1745    -75       C  
ATOM   2164  CG  LYS B  92      70.930  58.424 -23.367  1.00 74.86           C  
ANISOU 2164  CG  LYS B  92    11535   7618   9291   2941   2189    606       C  
ATOM   2165  CD  LYS B  92      70.744  57.478 -22.194  1.00 85.09           C  
ANISOU 2165  CD  LYS B  92    12968   8470  10892   3051   2700    969       C  
ATOM   2166  CE  LYS B  92      71.714  56.310 -22.265  1.00 92.58           C  
ANISOU 2166  CE  LYS B  92    14116   9026  12036   3584   3382   1447       C  
ATOM   2167  NZ  LYS B  92      71.383  55.257 -21.259  1.00 98.74           N  
ANISOU 2167  NZ  LYS B  92    15168   9211  13136   3749   4065   1753       N  
ATOM   2168  N   VAL B  93      71.352  60.069 -26.590  1.00 71.72           N  
ANISOU 2168  N   VAL B  93    11205   7897   8146   2984   1485   -263       N  
ATOM   2169  CA  VAL B  93      71.964  59.507 -27.788  1.00 75.00           C  
ANISOU 2169  CA  VAL B  93    11863   8112   8522   3238   1800   -423       C  
ATOM   2170  C   VAL B  93      72.565  58.162 -27.409  1.00 83.57           C  
ANISOU 2170  C   VAL B  93    13066   8671  10017   3457   2459   -101       C  
ATOM   2171  O   VAL B  93      73.427  58.099 -26.543  1.00 79.15           O  
ANISOU 2171  O   VAL B  93    12321   8202   9549   3723   2585    606       O  
ATOM   2172  CB  VAL B  93      73.077  60.433 -28.320  1.00 73.29           C  
ANISOU 2172  CB  VAL B  93    11579   8277   7989   3518   1667    -47       C  
ATOM   2173  CG1 VAL B  93      73.489  60.029 -29.726  1.00 76.59           C  
ANISOU 2173  CG1 VAL B  93    12319   8508   8273   3752   1946   -332       C  
ATOM   2174  CG2 VAL B  93      72.608  61.889 -28.301  1.00 69.15           C  
ANISOU 2174  CG2 VAL B  93    10934   8234   7107   3349   1140   -135       C  
ATOM   2175  N   GLU B  94      72.107  57.081 -28.029  1.00 83.72           N  
ANISOU 2175  N   GLU B  94    13382   8159  10268   3366   2916   -627       N  
ATOM   2176  CA  GLU B  94      72.615  55.762 -27.647  1.00 88.58           C  
ANISOU 2176  CA  GLU B  94    14191   8151  11315   3606   3702   -298       C  
ATOM   2177  C   GLU B  94      73.453  55.090 -28.732  1.00100.99           C  
ANISOU 2177  C   GLU B  94    16042   9409  12923   3905   4214   -337       C  
ATOM   2178  O   GLU B  94      73.902  55.743 -29.675  1.00 91.36           O  
ANISOU 2178  O   GLU B  94    14831   8526  11355   4010   3931   -440       O  
ATOM   2179  CB  GLU B  94      71.488  54.846 -27.148  1.00101.84           C  
ANISOU 2179  CB  GLU B  94    16032   9253  13411   3244   4123   -764       C  
ATOM   2180  CG  GLU B  94      70.810  55.363 -25.874  1.00100.86           C  
ANISOU 2180  CG  GLU B  94    15671   9330  13320   3035   3784   -553       C  
ATOM   2181  CD  GLU B  94      70.040  54.292 -25.116  1.00108.80           C  
ANISOU 2181  CD  GLU B  94    16883   9620  14835   2835   4466   -718       C  
ATOM   2182  OE1 GLU B  94      69.322  54.647 -24.154  1.00106.53           O  
ANISOU 2182  OE1 GLU B  94    16459   9416  14603   2606   4260   -670       O  
ATOM   2183  OE2 GLU B  94      70.155  53.099 -25.472  1.00117.48           O  
ANISOU 2183  OE2 GLU B  94    18317  10021  16298   2900   5292   -897       O  
ATOM   2184  N   LYS B  95      73.663  53.786 -28.576  1.00106.72           N  
ANISOU 2184  N   LYS B  95    17041   9432  14075   4069   5055   -224       N  
ATOM   2185  CA  LYS B  95      74.563  53.021 -29.433  1.00107.53           C  
ANISOU 2185  CA  LYS B  95    17435   9130  14292   4417   5705   -130       C  
ATOM   2186  C   LYS B  95      74.255  53.178 -30.918  1.00104.11           C  
ANISOU 2186  C   LYS B  95    17239   8745  13573   4164   5570   -981       C  
ATOM   2187  O   LYS B  95      73.107  53.054 -31.343  1.00105.37           O  
ANISOU 2187  O   LYS B  95    17502   8844  13690   3667   5434  -1889       O  
ATOM   2188  CB  LYS B  95      74.514  51.538 -29.053  1.00115.25           C  
ANISOU 2188  CB  LYS B  95    18662   9368  15758   4379   6583     -3       C  
ATOM   2189  CG  LYS B  95      74.677  51.262 -27.562  1.00117.86           C  
ANISOU 2189  CG  LYS B  95    18853   9642  16287   4668   6785    814       C  
ATOM   2190  CD  LYS B  95      74.661  49.764 -27.276  1.00123.88           C  
ANISOU 2190  CD  LYS B  95    19905   9731  17432   4599   7698   1002       C  
ATOM   2191  CE  LYS B  95      74.965  49.468 -25.816  1.00124.94           C  
ANISOU 2191  CE  LYS B  95    19948   9913  17611   5018   7936   1922       C  
ATOM   2192  NZ  LYS B  95      75.082  48.003 -25.563  1.00128.45           N  
ANISOU 2192  NZ  LYS B  95    20732   9725  18348   5065   8952   2223       N  
ATOM   2193  N   GLY B  96      75.290  53.468 -31.698  1.00107.85           N  
ANISOU 2193  N   GLY B  96    17770   9384  13824   4530   5603   -697       N  
ATOM   2194  CA  GLY B  96      75.188  53.484 -33.146  1.00107.55           C  
ANISOU 2194  CA  GLY B  96    18013   9384  13465   4373   5558  -1373       C  
ATOM   2195  C   GLY B  96      74.418  54.639 -33.758  1.00106.49           C  
ANISOU 2195  C   GLY B  96    17842   9871  12747   4174   4763  -1961       C  
ATOM   2196  O   GLY B  96      74.191  54.659 -34.968  1.00108.90           O  
ANISOU 2196  O   GLY B  96    18424  10271  12680   4108   4701  -2595       O  
ATOM   2197  N   ALA B  97      74.013  55.602 -32.934  1.00104.18           N  
ANISOU 2197  N   ALA B  97    17172  10074  12335   4061   4110  -1711       N  
ATOM   2198  CA  ALA B  97      73.294  56.773 -33.433  1.00 94.21           C  
ANISOU 2198  CA  ALA B  97    15830   9445  10520   3921   3348  -2121       C  
ATOM   2199  C   ALA B  97      74.148  57.545 -34.437  1.00 93.74           C  
ANISOU 2199  C   ALA B  97    15955   9666   9997   4301   3273  -1911       C  
ATOM   2200  O   ALA B  97      75.309  57.857 -34.171  1.00 94.21           O  
ANISOU 2200  O   ALA B  97    15897   9725  10173   4602   3469  -1183       O  
ATOM   2201  CB  ALA B  97      72.883  57.661 -32.293  1.00 88.68           C  
ANISOU 2201  CB  ALA B  97    14727   9127   9838   3775   2816  -1767       C  
ATOM   2202  N   LYS B  98      73.566  57.850 -35.592  1.00102.91           N  
ANISOU 2202  N   LYS B  98    17390  11097  10616   4304   3010  -2572       N  
ATOM   2203  CA  LYS B  98      74.313  58.432 -36.705  1.00107.06           C  
ANISOU 2203  CA  LYS B  98    18240  11779  10657   4707   3087  -2447       C  
ATOM   2204  C   LYS B  98      74.772  59.872 -36.460  1.00102.03           C  
ANISOU 2204  C   LYS B  98    17438  11555   9772   4928   2766  -1842       C  
ATOM   2205  O   LYS B  98      75.541  60.425 -37.245  1.00 93.05           O  
ANISOU 2205  O   LYS B  98    16516  10475   8363   5220   2930  -1584       O  
ATOM   2206  CB  LYS B  98      73.494  58.342 -37.995  1.00108.11           C  
ANISOU 2206  CB  LYS B  98    18577  12218  10282   4565   2790  -3246       C  
ATOM   2207  CG  LYS B  98      73.221  56.914 -38.450  1.00116.56           C  
ANISOU 2207  CG  LYS B  98    19772  12888  11629   4245   3205  -3907       C  
ATOM   2208  CD  LYS B  98      74.500  56.225 -38.915  1.00119.61           C  
ANISOU 2208  CD  LYS B  98    20398  12759  12287   4437   3897  -3485       C  
ATOM   2209  CE  LYS B  98      74.257  54.769 -39.288  1.00129.67           C  
ANISOU 2209  CE  LYS B  98    21791  13571  13905   4094   4390  -4099       C  
ATOM   2210  NZ  LYS B  98      73.873  53.948 -38.105  1.00129.23           N  
ANISOU 2210  NZ  LYS B  98    21547  13053  14502   3812   4705  -4090       N  
ATOM   2211  N   SER B  99      74.312  60.475 -35.368  1.00 87.58           N  
ANISOU 2211  N   SER B  99    15205   9973   8099   4703   2360  -1611       N  
ATOM   2212  CA  SER B  99      74.713  61.837 -35.038  1.00 89.94           C  
ANISOU 2212  CA  SER B  99    15339  10609   8226   4818   2146  -1103       C  
ATOM   2213  C   SER B  99      76.035  61.850 -34.271  1.00 89.29           C  
ANISOU 2213  C   SER B  99    14941  10381   8603   4874   2502   -380       C  
ATOM   2214  O   SER B  99      76.676  62.892 -34.146  1.00 79.96           O  
ANISOU 2214  O   SER B  99    13627   9411   7344   4950   2514      1       O  
ATOM   2215  CB  SER B  99      73.619  62.550 -34.231  1.00 79.80           C  
ANISOU 2215  CB  SER B  99    13776   9674   6871   4540   1581  -1216       C  
ATOM   2216  OG  SER B  99      73.540  62.039 -32.915  1.00 77.61           O  
ANISOU 2216  OG  SER B  99    13115   9250   7125   4228   1572   -992       O  
ATOM   2217  N   ILE B 100      76.443  60.686 -33.769  1.00 83.73           N  
ANISOU 2217  N   ILE B 100    14104   9333   8375   4855   2836   -217       N  
ATOM   2218  CA  ILE B 100      77.633  60.590 -32.923  1.00 83.33           C  
ANISOU 2218  CA  ILE B 100    13645   9280   8736   4978   3100    471       C  
ATOM   2219  C   ILE B 100      78.918  61.049 -33.619  1.00 85.00           C  
ANISOU 2219  C   ILE B 100    13876   9510   8908   5284   3475    789       C  
ATOM   2220  O   ILE B 100      79.284  60.539 -34.679  1.00 88.62           O  
ANISOU 2220  O   ILE B 100    14728   9650   9293   5530   3894    635       O  
ATOM   2221  CB  ILE B 100      77.827  59.168 -32.350  1.00 86.35           C  
ANISOU 2221  CB  ILE B 100    13964   9257   9589   5059   3494    648       C  
ATOM   2222  CG1 ILE B 100      76.690  58.825 -31.385  1.00 84.73           C  
ANISOU 2222  CG1 ILE B 100    13657   9018   9520   4732   3213    453       C  
ATOM   2223  CG2 ILE B 100      79.156  59.067 -31.629  1.00 87.42           C  
ANISOU 2223  CG2 ILE B 100    13651   9516  10048   5349   3754   1388       C  
ATOM   2224  CD1 ILE B 100      76.843  57.472 -30.706  1.00 89.63           C  
ANISOU 2224  CD1 ILE B 100    14277   9172  10608   4856   3717    700       C  
ATOM   2225  N   GLY B 101      79.589  62.019 -33.003  1.00 82.87           N  
ANISOU 2225  N   GLY B 101    13173   9606   8706   5226   3368   1179       N  
ATOM   2226  CA  GLY B 101      80.843  62.544 -33.503  1.00 84.83           C  
ANISOU 2226  CA  GLY B 101    13314   9897   9019   5432   3772   1457       C  
ATOM   2227  C   GLY B 101      80.657  63.704 -34.459  1.00 85.56           C  
ANISOU 2227  C   GLY B 101    13812  10023   8673   5447   3809   1226       C  
ATOM   2228  O   GLY B 101      81.628  64.254 -34.977  1.00 86.22           O  
ANISOU 2228  O   GLY B 101    13893  10066   8800   5591   4243   1400       O  
ATOM   2229  N   ARG B 102      79.406  64.071 -34.703  1.00 82.18           N  
ANISOU 2229  N   ARG B 102    13735   9667   7824   5341   3408    844       N  
ATOM   2230  CA  ARG B 102      79.102  65.168 -35.608  1.00 86.79           C  
ANISOU 2230  CA  ARG B 102    14774  10308   7894   5488   3449    680       C  
ATOM   2231  C   ARG B 102      78.738  66.397 -34.784  1.00 84.48           C  
ANISOU 2231  C   ARG B 102    14209  10327   7560   5200   3166    790       C  
ATOM   2232  O   ARG B 102      78.278  66.267 -33.655  1.00 78.12           O  
ANISOU 2232  O   ARG B 102    12991   9718   6975   4876   2767    820       O  
ATOM   2233  CB  ARG B 102      77.966  64.772 -36.553  1.00 84.08           C  
ANISOU 2233  CB  ARG B 102    14965   9934   7048   5630   3170    179       C  
ATOM   2234  CG  ARG B 102      78.265  63.501 -37.348  1.00 88.27           C  
ANISOU 2234  CG  ARG B 102    15727  10139   7674   5721   3418      3       C  
ATOM   2235  CD  ARG B 102      77.075  63.044 -38.177  1.00102.11           C  
ANISOU 2235  CD  ARG B 102    17810  11985   9002   5676   3031   -596       C  
ATOM   2236  NE  ARG B 102      76.752  63.971 -39.259  1.00105.43           N  
ANISOU 2236  NE  ARG B 102    18538  12621   8898   5830   2824   -638       N  
ATOM   2237  CZ  ARG B 102      75.836  63.737 -40.194  1.00115.17           C  
ANISOU 2237  CZ  ARG B 102    19999  14065   9697   5878   2484  -1118       C  
ATOM   2238  NH1 ARG B 102      75.609  64.636 -41.144  1.00121.28           N  
ANISOU 2238  NH1 ARG B 102    21027  15040  10016   6141   2333  -1034       N  
ATOM   2239  NH2 ARG B 102      75.150  62.601 -40.186  1.00116.84           N  
ANISOU 2239  NH2 ARG B 102    20158  14281   9956   5670   2340  -1698       N  
ATOM   2240  N   THR B 103      78.967  67.586 -35.332  1.00 79.58           N  
ANISOU 2240  N   THR B 103    13864   9702   6671   5325   3464    862       N  
ATOM   2241  CA  THR B 103      78.717  68.814 -34.582  1.00 76.99           C  
ANISOU 2241  CA  THR B 103    13326   9581   6345   5032   3366    962       C  
ATOM   2242  C   THR B 103      77.315  69.354 -34.854  1.00 75.79           C  
ANISOU 2242  C   THR B 103    13530   9543   5723   5111   2925    745       C  
ATOM   2243  O   THR B 103      76.682  68.981 -35.838  1.00 77.97           O  
ANISOU 2243  O   THR B 103    14152   9766   5706   5348   2670    547       O  
ATOM   2244  CB  THR B 103      79.762  69.905 -34.904  1.00 79.30           C  
ANISOU 2244  CB  THR B 103    13629   9714   6787   4974   3984   1178       C  
ATOM   2245  OG1 THR B 103      79.457  70.508 -36.165  1.00 82.06           O  
ANISOU 2245  OG1 THR B 103    14545   9783   6849   5176   4015   1185       O  
ATOM   2246  CG2 THR B 103      81.167  69.314 -34.945  1.00 82.00           C  
ANISOU 2246  CG2 THR B 103    13635   9964   7557   5018   4479   1342       C  
ATOM   2247  N   LEU B 104      76.835  70.230 -33.976  1.00 63.32           N  
ANISOU 2247  N   LEU B 104     9422   8422   6214   2425   2525    726       N  
ATOM   2248  CA  LEU B 104      75.530  70.863 -34.167  1.00 60.83           C  
ANISOU 2248  CA  LEU B 104     9276   8335   5503   2162   2193    559       C  
ATOM   2249  C   LEU B 104      75.485  71.665 -35.466  1.00 62.14           C  
ANISOU 2249  C   LEU B 104     9587   8548   5475   2116   2377    614       C  
ATOM   2250  O   LEU B 104      74.447  71.748 -36.112  1.00 62.17           O  
ANISOU 2250  O   LEU B 104     9891   8717   5013   1934   2259    501       O  
ATOM   2251  CB  LEU B 104      75.155  71.750 -32.972  1.00 58.00           C  
ANISOU 2251  CB  LEU B 104     8543   8176   5318   2097   1702    563       C  
ATOM   2252  CG  LEU B 104      74.896  71.017 -31.657  1.00 56.90           C  
ANISOU 2252  CG  LEU B 104     8351   8068   5199   2108   1464    506       C  
ATOM   2253  CD1 LEU B 104      74.398  71.982 -30.583  1.00 54.74           C  
ANISOU 2253  CD1 LEU B 104     7820   7998   4982   2014   1030    454       C  
ATOM   2254  CD2 LEU B 104      73.907  69.885 -31.870  1.00 71.74           C  
ANISOU 2254  CD2 LEU B 104    10664   9896   6697   1974   1550    338       C  
ATOM   2255  N   GLY B 105      76.619  72.243 -35.846  1.00 64.02           N  
ANISOU 2255  N   GLY B 105     9587   8664   6073   2281   2667    824       N  
ATOM   2256  CA  GLY B 105      76.718  72.965 -37.104  1.00 66.10           C  
ANISOU 2256  CA  GLY B 105    10022   8932   6163   2283   2943    944       C  
ATOM   2257  C   GLY B 105      76.480  72.036 -38.274  1.00 69.03           C  
ANISOU 2257  C   GLY B 105    10999   9239   5992   2251   3316    816       C  
ATOM   2258  O   GLY B 105      75.662  72.324 -39.149  1.00 70.76           O  
ANISOU 2258  O   GLY B 105    11559   9648   5676   2107   3241    771       O  
ATOM   2259  N   GLU B 106      77.180  70.904 -38.287  1.00 71.21           N  
ANISOU 2259  N   GLU B 106    11427   9248   6383   2385   3720    758       N  
ATOM   2260  CA  GLU B 106      77.101  69.985 -39.422  1.00 75.13           C  
ANISOU 2260  CA  GLU B 106    12577   9591   6380   2345   4193    580       C  
ATOM   2261  C   GLU B 106      75.735  69.311 -39.527  1.00 74.60           C  
ANISOU 2261  C   GLU B 106    12966   9681   5697   2010   3869    235       C  
ATOM   2262  O   GLU B 106      75.190  69.170 -40.623  1.00 77.56           O  
ANISOU 2262  O   GLU B 106    13768  10158   5545   1773   3871     68       O  
ATOM   2263  CB  GLU B 106      78.220  68.942 -39.359  1.00 78.34           C  
ANISOU 2263  CB  GLU B 106    13025   9591   7151   2621   4796    623       C  
ATOM   2264  CG  GLU B 106      78.424  68.159 -40.646  1.00 93.97           C  
ANISOU 2264  CG  GLU B 106    15594  11298   8810   2555   5285    455       C  
ATOM   2265  CD  GLU B 106      79.019  66.796 -40.380  1.00 94.27           C  
ANISOU 2265  CD  GLU B 106    15772  10891   9155   2716   5691    395       C  
ATOM   2266  OE1 GLU B 106      78.436  66.064 -39.556  1.00 87.92           O  
ANISOU 2266  OE1 GLU B 106    15043  10043   8319   2641   5489    239       O  
ATOM   2267  OE2 GLU B 106      80.071  66.464 -40.967  1.00 99.94           O  
ANISOU 2267  OE2 GLU B 106    16519  11282  10173   2937   6236    542       O  
ATOM   2268  N   LEU B 107      75.186  68.903 -38.382  1.00 71.48           N  
ANISOU 2268  N   LEU B 107    12368   9319   5470   1922   3484    136       N  
ATOM   2269  CA  LEU B 107      73.828  68.374 -38.321  1.00 82.98           C  
ANISOU 2269  CA  LEU B 107    14114  10951   6463   1565   3131   -158       C  
ATOM   2270  C   LEU B 107      72.816  69.478 -38.613  1.00 78.58           C  
ANISOU 2270  C   LEU B 107    13410  10848   5600   1383   2626    -99       C  
ATOM   2271  O   LEU B 107      71.737  69.213 -39.145  1.00 74.38           O  
ANISOU 2271  O   LEU B 107    13163  10556   4541   1065   2389   -301       O  
ATOM   2272  CB  LEU B 107      73.547  67.756 -36.946  1.00 81.58           C  
ANISOU 2272  CB  LEU B 107    13712  10683   6601   1559   2906   -203       C  
ATOM   2273  CG  LEU B 107      74.415  66.560 -36.549  1.00 70.40           C  
ANISOU 2273  CG  LEU B 107    12434   8817   5498   1779   3379   -195       C  
ATOM   2274  CD1 LEU B 107      74.206  66.224 -35.083  1.00 72.84           C  
ANISOU 2274  CD1 LEU B 107    12437   9116   6121   1841   3093   -111       C  
ATOM   2275  CD2 LEU B 107      74.128  65.357 -37.432  1.00 85.42           C  
ANISOU 2275  CD2 LEU B 107    15036  10426   6993   1567   3812   -528       C  
ATOM   2276  N   ASP B 108      73.168  70.710 -38.246  1.00 67.02           N  
ANISOU 2276  N   ASP B 108    11478   9489   4497   1579   2468    189       N  
ATOM   2277  CA  ASP B 108      72.392  71.890 -38.624  1.00 66.50           C  
ANISOU 2277  CA  ASP B 108    11271   9770   4227   1517   2124    344       C  
ATOM   2278  C   ASP B 108      70.984  71.834 -38.023  1.00 64.66           C  
ANISOU 2278  C   ASP B 108    10915   9827   3825   1287   1605    219       C  
ATOM   2279  O   ASP B 108      69.998  72.211 -38.666  1.00 66.28           O  
ANISOU 2279  O   ASP B 108    11185  10378   3619   1136   1329    255       O  
ATOM   2280  CB  ASP B 108      72.338  72.020 -40.157  1.00 70.90           C  
ANISOU 2280  CB  ASP B 108    12265  10461   4213   1465   2336    389       C  
ATOM   2281  CG  ASP B 108      72.359  73.460 -40.625  1.00 71.33           C  
ANISOU 2281  CG  ASP B 108    12110  10684   4308   1627   2273    756       C  
ATOM   2282  OD1 ASP B 108      72.515  74.365 -39.775  1.00 68.32           O  
ANISOU 2282  OD1 ASP B 108    11256  10243   4461   1765   2125    933       O  
ATOM   2283  OD2 ASP B 108      72.244  73.682 -41.847  1.00 75.31           O  
ANISOU 2283  OD2 ASP B 108    12965  11357   4294   1614   2404    867       O  
ATOM   2284  N   VAL B 109      70.920  71.355 -36.783  1.00 61.92           N  
ANISOU 2284  N   VAL B 109    10367   9358   3803   1280   1490    113       N  
ATOM   2285  CA  VAL B 109      69.669  71.062 -36.090  1.00 65.70           C  
ANISOU 2285  CA  VAL B 109    10745  10037   4182   1061   1120    -23       C  
ATOM   2286  C   VAL B 109      68.621  72.174 -36.162  1.00 62.17           C  
ANISOU 2286  C   VAL B 109    10014   9957   3649   1033    741    139       C  
ATOM   2287  O   VAL B 109      67.538  71.959 -36.707  1.00 63.03           O  
ANISOU 2287  O   VAL B 109    10201  10373   3374    791    503     74       O  
ATOM   2288  CB  VAL B 109      69.928  70.670 -34.627  1.00 65.96           C  
ANISOU 2288  CB  VAL B 109    10566   9879   4619   1153   1096    -58       C  
ATOM   2289  CG1 VAL B 109      68.615  70.334 -33.903  1.00 63.27           C  
ANISOU 2289  CG1 VAL B 109    10138   9718   4182    927    803   -179       C  
ATOM   2290  CG2 VAL B 109      70.887  69.494 -34.568  1.00 66.69           C  
ANISOU 2290  CG2 VAL B 109    10913   9611   4813   1234   1480   -141       C  
ATOM   2291  N   ARG B 110      68.934  73.359 -35.649  1.00 58.24           N  
ANISOU 2291  N   ARG B 110     9182   9425   3521   1269    697    354       N  
ATOM   2292  CA  ARG B 110      67.928  74.426 -35.638  1.00 68.95           C  
ANISOU 2292  CA  ARG B 110    10269  11055   4875   1309    421    543       C  
ATOM   2293  C   ARG B 110      67.505  74.834 -37.044  1.00 77.75           C  
ANISOU 2293  C   ARG B 110    11523  12453   5566   1292    359    739       C  
ATOM   2294  O   ARG B 110      66.328  75.089 -37.293  1.00 63.75           O  
ANISOU 2294  O   ARG B 110     9603  11041   3579   1215     52    849       O  
ATOM   2295  CB  ARG B 110      68.389  75.653 -34.845  1.00 56.48           C  
ANISOU 2295  CB  ARG B 110     8383   9291   3785   1547    464    697       C  
ATOM   2296  CG  ARG B 110      67.321  76.748 -34.732  1.00 63.11           C  
ANISOU 2296  CG  ARG B 110     8961  10321   4697   1647    275    904       C  
ATOM   2297  CD  ARG B 110      67.842  77.971 -33.977  1.00 64.77           C  
ANISOU 2297  CD  ARG B 110     8964  10247   5398   1842    400    987       C  
ATOM   2298  NE  ARG B 110      69.133  78.384 -34.511  1.00 60.65           N  
ANISOU 2298  NE  ARG B 110     8518   9474   5051   1923    664   1080       N  
ATOM   2299  CZ  ARG B 110      70.169  78.782 -33.780  1.00 62.00           C  
ANISOU 2299  CZ  ARG B 110     8572   9346   5639   1942    792    987       C  
ATOM   2300  NH1 ARG B 110      71.304  79.114 -34.386  1.00 57.34           N  
ANISOU 2300  NH1 ARG B 110     7993   8555   5238   1989   1056   1107       N  
ATOM   2301  NH2 ARG B 110      70.084  78.846 -32.454  1.00 54.32           N  
ANISOU 2301  NH2 ARG B 110     7464   8297   4876   1893    658    777       N  
ATOM   2302  N   GLN B 111      68.459  74.886 -37.965  1.00 63.73           N  
ANISOU 2302  N   GLN B 111    10012  10544   3656   1378    655    817       N  
ATOM   2303  CA  GLN B 111      68.122  75.266 -39.335  1.00 67.92           C  
ANISOU 2303  CA  GLN B 111    10752  11370   3687   1379    616   1033       C  
ATOM   2304  C   GLN B 111      67.223  74.226 -40.001  1.00 89.83           C  
ANISOU 2304  C   GLN B 111    13809  14495   5828   1026    364    800       C  
ATOM   2305  O   GLN B 111      66.231  74.571 -40.642  1.00 74.49           O  
ANISOU 2305  O   GLN B 111    11799  13006   3499    945     15    973       O  
ATOM   2306  CB  GLN B 111      69.382  75.519 -40.175  1.00 69.71           C  
ANISOU 2306  CB  GLN B 111    11246  11351   3890   1550   1077   1171       C  
ATOM   2307  CG  GLN B 111      69.079  75.913 -41.612  1.00 84.04           C  
ANISOU 2307  CG  GLN B 111    13353  13483   5094   1574   1074   1428       C  
ATOM   2308  CD  GLN B 111      68.173  77.134 -41.714  1.00 86.03           C  
ANISOU 2308  CD  GLN B 111    13285  14034   5368   1749    763   1849       C  
ATOM   2309  OE1 GLN B 111      68.258  78.059 -40.902  1.00 86.66           O  
ANISOU 2309  OE1 GLN B 111    12987  13894   6044   1957    797   2023       O  
ATOM   2310  NE2 GLN B 111      67.293  77.134 -42.708  1.00 80.77           N  
ANISOU 2310  NE2 GLN B 111    12726  13764   4197   1590    443   1963       N  
ATOM   2311  N   ASN B 112      67.553  72.952 -39.833  1.00 70.92           N  
ANISOU 2311  N   ASN B 112    11712  11886   3348    802    533    415       N  
ATOM   2312  CA  ASN B 112      66.841  71.904 -40.561  1.00 84.49           C  
ANISOU 2312  CA  ASN B 112    13794  13842   4465    382    372    111       C  
ATOM   2313  C   ASN B 112      65.603  71.329 -39.867  1.00 74.78           C  
ANISOU 2313  C   ASN B 112    12323  12837   3253     59    -25    -84       C  
ATOM   2314  O   ASN B 112      64.698  70.815 -40.542  1.00 81.45           O  
ANISOU 2314  O   ASN B 112    13290  13923   3733   -284   -325   -247       O  
ATOM   2315  CB  ASN B 112      67.800  70.784 -40.984  1.00 76.74           C  
ANISOU 2315  CB  ASN B 112    13266  12463   3428    258    843   -215       C  
ATOM   2316  CG  ASN B 112      68.771  71.232 -42.059  1.00 87.02           C  
ANISOU 2316  CG  ASN B 112    14777  13662   4624    438   1200    -45       C  
ATOM   2317  OD1 ASN B 112      68.564  72.262 -42.697  1.00 81.08           O  
ANISOU 2317  OD1 ASN B 112    13934  13182   3692    541   1049    282       O  
ATOM   2318  ND2 ASN B 112      69.829  70.454 -42.272  1.00 88.77           N  
ANISOU 2318  ND2 ASN B 112    15288  13453   4985    499   1707   -231       N  
ATOM   2319  N   TYR B 113      65.555  71.440 -38.538  1.00 70.27           N  
ANISOU 2319  N   TYR B 113    11380  12062   3256    194    -26    -58       N  
ATOM   2320  CA  TYR B 113      64.491  70.818 -37.749  1.00 77.05           C  
ANISOU 2320  CA  TYR B 113    12018  13039   4220    -93   -274   -233       C  
ATOM   2321  C   TYR B 113      63.701  71.790 -36.874  1.00 76.84           C  
ANISOU 2321  C   TYR B 113    11407  13217   4573    101   -529     45       C  
ATOM   2322  O   TYR B 113      62.755  71.384 -36.195  1.00 79.52           O  
ANISOU 2322  O   TYR B 113    11501  13678   5036   -106   -698    -45       O  
ATOM   2323  CB  TYR B 113      65.069  69.704 -36.863  1.00 67.83           C  
ANISOU 2323  CB  TYR B 113    11060  11387   3324   -156     55   -513       C  
ATOM   2324  CG  TYR B 113      65.582  68.538 -37.662  1.00 71.18           C  
ANISOU 2324  CG  TYR B 113    12079  11564   3401   -403    355   -838       C  
ATOM   2325  CD1 TYR B 113      66.888  68.522 -38.131  1.00 71.12           C  
ANISOU 2325  CD1 TYR B 113    12390  11232   3402   -139    779   -810       C  
ATOM   2326  CD2 TYR B 113      64.758  67.464 -37.968  1.00 75.17           C  
ANISOU 2326  CD2 TYR B 113    12831  12135   3595   -917    261  -1187       C  
ATOM   2327  CE1 TYR B 113      67.365  67.461 -38.889  1.00 75.85           C  
ANISOU 2327  CE1 TYR B 113    13488  11548   3782   -307   1130  -1100       C  
ATOM   2328  CE2 TYR B 113      65.224  66.395 -38.716  1.00 79.08           C  
ANISOU 2328  CE2 TYR B 113    13837  12295   3915  -1097    582  -1506       C  
ATOM   2329  CZ  TYR B 113      66.531  66.400 -39.177  1.00 78.93           C  
ANISOU 2329  CZ  TYR B 113    14087  11942   3963   -765   1026  -1451       C  
ATOM   2330  OH  TYR B 113      67.010  65.347 -39.923  1.00 83.45           O  
ANISOU 2330  OH  TYR B 113    15130  12151   4424   -912   1398  -1745       O  
ATOM   2331  N   ASP B 114      64.100  73.059 -36.879  1.00 73.22           N  
ANISOU 2331  N   ASP B 114    10748  12745   4328    493   -486    375       N  
ATOM   2332  CA  ASP B 114      63.470  74.072 -36.036  1.00 64.73           C  
ANISOU 2332  CA  ASP B 114     9191  11753   3652    731   -609    624       C  
ATOM   2333  C   ASP B 114      63.474  73.667 -34.566  1.00 66.43           C  
ANISOU 2333  C   ASP B 114     9292  11695   4253    727   -489    436       C  
ATOM   2334  O   ASP B 114      62.540  73.988 -33.839  1.00 62.25           O  
ANISOU 2334  O   ASP B 114     8418  11303   3931    755   -604    518       O  
ATOM   2335  CB  ASP B 114      62.029  74.345 -36.488  1.00 74.29           C  
ANISOU 2335  CB  ASP B 114    10053  13502   4673    614  -1001    827       C  
ATOM   2336  CG  ASP B 114      61.952  74.883 -37.905  1.00 78.64           C  
ANISOU 2336  CG  ASP B 114    10690  14407   4782    673  -1179   1107       C  
ATOM   2337  OD1 ASP B 114      62.700  75.832 -38.219  1.00 85.86           O  
ANISOU 2337  OD1 ASP B 114    11679  15144   5800   1022   -974   1370       O  
ATOM   2338  OD2 ASP B 114      61.151  74.351 -38.705  1.00 79.29           O  
ANISOU 2338  OD2 ASP B 114    10776  14955   4396    346  -1527   1067       O  
ATOM   2339  N   VAL B 115      64.513  72.944 -34.144  1.00 59.05           N  
ANISOU 2339  N   VAL B 115     8647  10390   3400    715   -237    220       N  
ATOM   2340  CA  VAL B 115      64.693  72.564 -32.751  1.00 56.33           C  
ANISOU 2340  CA  VAL B 115     8250   9798   3355    758   -123     94       C  
ATOM   2341  C   VAL B 115      65.973  73.218 -32.242  1.00 53.88           C  
ANISOU 2341  C   VAL B 115     7944   9190   3336   1053     53    157       C  
ATOM   2342  O   VAL B 115      66.989  73.241 -32.950  1.00 55.82           O  
ANISOU 2342  O   VAL B 115     8361   9295   3553   1133    208    187       O  
ATOM   2343  CB  VAL B 115      64.776  71.029 -32.562  1.00 58.63           C  
ANISOU 2343  CB  VAL B 115     8839   9919   3518    492      4   -166       C  
ATOM   2344  CG1 VAL B 115      65.077  70.675 -31.088  1.00 54.62           C  
ANISOU 2344  CG1 VAL B 115     8304   9165   3284    607    135   -208       C  
ATOM   2345  CG2 VAL B 115      63.487  70.362 -33.008  1.00 60.14           C  
ANISOU 2345  CG2 VAL B 115     8999  10390   3462     98   -183   -282       C  
ATOM   2346  N   THR B 116      65.898  73.799 -31.052  1.00 52.21           N  
ANISOU 2346  N   THR B 116     7535   8903   3399   1192     38    172       N  
ATOM   2347  CA  THR B 116      67.071  74.368 -30.397  1.00 50.70           C  
ANISOU 2347  CA  THR B 116     7319   8466   3478   1383    135    172       C  
ATOM   2348  C   THR B 116      67.629  73.441 -29.316  1.00 50.52           C  
ANISOU 2348  C   THR B 116     7403   8295   3495   1369    179     39       C  
ATOM   2349  O   THR B 116      66.922  73.039 -28.383  1.00 50.73           O  
ANISOU 2349  O   THR B 116     7426   8373   3475   1310    139    -30       O  
ATOM   2350  CB  THR B 116      66.778  75.761 -29.780  1.00 50.57           C  
ANISOU 2350  CB  THR B 116     7080   8427   3708   1535    104    242       C  
ATOM   2351  OG1 THR B 116      66.569  76.721 -30.825  1.00 52.00           O  
ANISOU 2351  OG1 THR B 116     7171   8669   3919   1634    123    455       O  
ATOM   2352  CG2 THR B 116      67.946  76.224 -28.940  1.00 49.86           C  
ANISOU 2352  CG2 THR B 116     6974   8105   3863   1617    147    153       C  
ATOM   2353  N   VAL B 117      68.899  73.078 -29.447  1.00 49.74           N  
ANISOU 2353  N   VAL B 117     7385   8023   3491   1451    288     52       N  
ATOM   2354  CA  VAL B 117      69.552  72.359 -28.358  1.00 49.60           C  
ANISOU 2354  CA  VAL B 117     7402   7898   3545   1517    294     21       C  
ATOM   2355  C   VAL B 117      69.942  73.380 -27.280  1.00 49.31           C  
ANISOU 2355  C   VAL B 117     7167   7882   3687   1602    134      0       C  
ATOM   2356  O   VAL B 117      70.849  74.189 -27.490  1.00 49.76           O  
ANISOU 2356  O   VAL B 117     7068   7870   3970   1660    121     36       O  
ATOM   2357  CB  VAL B 117      70.794  71.575 -28.841  1.00 50.68           C  
ANISOU 2357  CB  VAL B 117     7628   7854   3774   1621    486     95       C  
ATOM   2358  CG1 VAL B 117      71.378  70.776 -27.691  1.00 51.36           C  
ANISOU 2358  CG1 VAL B 117     7716   7872   3927   1742    467    153       C  
ATOM   2359  CG2 VAL B 117      70.421  70.655 -29.986  1.00 51.80           C  
ANISOU 2359  CG2 VAL B 117     8061   7926   3696   1498    699     40       C  
ATOM   2360  N   ILE B 118      69.261  73.357 -26.130  1.00 49.23           N  
ANISOU 2360  N   ILE B 118     7185   7950   3568   1578     41    -79       N  
ATOM   2361  CA  ILE B 118      69.496  74.398 -25.119  1.00 49.80           C  
ANISOU 2361  CA  ILE B 118     7158   8038   3725   1607    -94   -176       C  
ATOM   2362  C   ILE B 118      70.566  74.017 -24.093  1.00 51.19           C  
ANISOU 2362  C   ILE B 118     7324   8242   3883   1660   -251   -177       C  
ATOM   2363  O   ILE B 118      71.180  74.879 -23.464  1.00 52.58           O  
ANISOU 2363  O   ILE B 118     7394   8436   4149   1627   -414   -283       O  
ATOM   2364  CB  ILE B 118      68.188  74.837 -24.396  1.00 49.95           C  
ANISOU 2364  CB  ILE B 118     7228   8131   3621   1577    -64   -273       C  
ATOM   2365  CG1 ILE B 118      67.520  73.652 -23.711  1.00 52.32           C  
ANISOU 2365  CG1 ILE B 118     7689   8507   3682   1547     -7   -252       C  
ATOM   2366  CG2 ILE B 118      67.208  75.467 -25.388  1.00 52.28           C  
ANISOU 2366  CG2 ILE B 118     7413   8451   4002   1570     35   -205       C  
ATOM   2367  CD1 ILE B 118      66.371  74.065 -22.763  1.00 51.14           C  
ANISOU 2367  CD1 ILE B 118     7581   8423   3425   1542     84   -335       C  
ATOM   2368  N   ALA B 119      70.781  72.720 -23.930  1.00 57.41           N  
ANISOU 2368  N   ALA B 119     8224   9034   4556   1731   -204    -49       N  
ATOM   2369  CA  ALA B 119      71.873  72.229 -23.102  1.00 53.67           C  
ANISOU 2369  CA  ALA B 119     7690   8624   4078   1849   -363     66       C  
ATOM   2370  C   ALA B 119      72.316  70.857 -23.593  1.00 64.11           C  
ANISOU 2370  C   ALA B 119     9091   9820   5447   1992   -165    286       C  
ATOM   2371  O   ALA B 119      71.574  70.160 -24.299  1.00 53.23           O  
ANISOU 2371  O   ALA B 119     7916   8306   4004   1934     85    273       O  
ATOM   2372  CB  ALA B 119      71.461  72.168 -21.641  1.00 55.17           C  
ANISOU 2372  CB  ALA B 119     8030   8973   3959   1850   -517     13       C  
ATOM   2373  N   ILE B 120      73.547  70.496 -23.250  1.00 56.68           N  
ANISOU 2373  N   ILE B 120     7974   8917   4646   2169   -267    483       N  
ATOM   2374  CA  ILE B 120      74.030  69.138 -23.427  1.00 58.43           C  
ANISOU 2374  CA  ILE B 120     8285   8982   4933   2388    -36    746       C  
ATOM   2375  C   ILE B 120      74.524  68.618 -22.079  1.00 65.70           C  
ANISOU 2375  C   ILE B 120     9166  10083   5715   2582   -262    985       C  
ATOM   2376  O   ILE B 120      75.388  69.228 -21.454  1.00 63.85           O  
ANISOU 2376  O   ILE B 120     8626  10103   5533   2617   -621   1042       O  
ATOM   2377  CB  ILE B 120      75.167  69.069 -24.454  1.00 70.26           C  
ANISOU 2377  CB  ILE B 120     9555  10340   6801   2523    146    882       C  
ATOM   2378  CG1 ILE B 120      74.664  69.531 -25.820  1.00 67.06           C  
ANISOU 2378  CG1 ILE B 120     9265   9785   6431   2346    383    682       C  
ATOM   2379  CG2 ILE B 120      75.719  67.652 -24.540  1.00 62.31           C  
ANISOU 2379  CG2 ILE B 120     8655   9116   5905   2812    457   1177       C  
ATOM   2380  CD1 ILE B 120      75.692  69.463 -26.905  1.00 58.56           C  
ANISOU 2380  CD1 ILE B 120     8044   8543   5662   2475    662    806       C  
ATOM   2381  N   ILE B 121      73.954  67.506 -21.627  1.00 68.33           N  
ANISOU 2381  N   ILE B 121     9814  10299   5852   2683    -61   1130       N  
ATOM   2382  CA  ILE B 121      74.373  66.872 -20.382  1.00 66.36           C  
ANISOU 2382  CA  ILE B 121     9587  10210   5416   2926   -224   1449       C  
ATOM   2383  C   ILE B 121      75.120  65.577 -20.661  1.00 78.55           C  
ANISOU 2383  C   ILE B 121    11144  11500   7201   3274     86   1852       C  
ATOM   2384  O   ILE B 121      74.532  64.598 -21.121  1.00 78.15           O  
ANISOU 2384  O   ILE B 121    11438  11076   7181   3283    540   1874       O  
ATOM   2385  CB  ILE B 121      73.168  66.543 -19.490  1.00 66.24           C  
ANISOU 2385  CB  ILE B 121     9953  10215   4999   2833   -151   1399       C  
ATOM   2386  CG1 ILE B 121      72.232  67.750 -19.390  1.00 66.04           C  
ANISOU 2386  CG1 ILE B 121     9955  10336   4801   2518   -292    992       C  
ATOM   2387  CG2 ILE B 121      73.637  66.083 -18.117  1.00 70.80           C  
ANISOU 2387  CG2 ILE B 121    10579  11041   5281   3089   -379   1748       C  
ATOM   2388  CD1 ILE B 121      70.962  67.463 -18.644  1.00 67.45           C  
ANISOU 2388  CD1 ILE B 121    10465  10507   4654   2421   -120    938       C  
ATOM   2389  N   LYS B 122      76.418  65.572 -20.387  1.00 84.03           N  
ANISOU 2389  N   LYS B 122    11447  12380   8100   3550   -138   2171       N  
ATOM   2390  CA  LYS B 122      77.228  64.379 -20.604  1.00 88.47           C  
ANISOU 2390  CA  LYS B 122    11961  12693   8961   3972    195   2630       C  
ATOM   2391  C   LYS B 122      76.826  63.255 -19.660  1.00 90.48           C  
ANISOU 2391  C   LYS B 122    12566  12850   8962   4213    347   2977       C  
ATOM   2392  O   LYS B 122      76.091  63.477 -18.693  1.00 79.87           O  
ANISOU 2392  O   LYS B 122    11433  11737   7177   4072    109   2901       O  
ATOM   2393  CB  LYS B 122      78.717  64.712 -20.481  1.00 92.97           C  
ANISOU 2393  CB  LYS B 122    11907  13556   9860   4226   -119   2948       C  
ATOM   2394  CG  LYS B 122      79.199  65.668 -21.568  1.00 94.69           C  
ANISOU 2394  CG  LYS B 122    11792  13751  10434   4020   -102   2672       C  
ATOM   2395  CD  LYS B 122      80.698  65.915 -21.506  1.00109.94           C  
ANISOU 2395  CD  LYS B 122    13033  15943  12797   4254   -342   3018       C  
ATOM   2396  CE  LYS B 122      81.075  66.810 -20.336  1.00116.47           C  
ANISOU 2396  CE  LYS B 122    13487  17364  13400   4079  -1110   2999       C  
ATOM   2397  NZ  LYS B 122      82.539  67.097 -20.310  1.00123.43           N  
ANISOU 2397  NZ  LYS B 122    13595  18551  14752   4228  -1400   3321       N  
ATOM   2398  N   HIS B 123      77.308  62.047 -19.945  1.00 94.37           N  
ANISOU 2398  N   HIS B 123    13152  12958   9745   4595    814   3374       N  
ATOM   2399  CA  HIS B 123      76.946  60.863 -19.163  1.00 96.13           C  
ANISOU 2399  CA  HIS B 123    13757  12962   9806   4862   1094   3765       C  
ATOM   2400  C   HIS B 123      77.190  61.032 -17.662  1.00 98.48           C  
ANISOU 2400  C   HIS B 123    13922  13801   9694   5058    550   4134       C  
ATOM   2401  O   HIS B 123      76.514  60.412 -16.839  1.00 96.43           O  
ANISOU 2401  O   HIS B 123    14063  13474   9101   5124    686   4328       O  
ATOM   2402  CB  HIS B 123      77.690  59.623 -19.677  1.00103.17           C  
ANISOU 2402  CB  HIS B 123    14697  13340  11161   5333   1690   4209       C  
ATOM   2403  CG  HIS B 123      77.518  58.415 -18.808  1.00110.55           C  
ANISOU 2403  CG  HIS B 123    15976  14029  11999   5700   1993   4736       C  
ATOM   2404  ND1 HIS B 123      78.572  57.801 -18.167  1.00120.05           N  
ANISOU 2404  ND1 HIS B 123    16901  15337  13375   6325   1951   5472       N  
ATOM   2405  CD2 HIS B 123      76.410  57.718 -18.458  1.00110.33           C  
ANISOU 2405  CD2 HIS B 123    16523  13658  11738   5538   2357   4679       C  
ATOM   2406  CE1 HIS B 123      78.124  56.773 -17.468  1.00123.61           C  
ANISOU 2406  CE1 HIS B 123    17739  15517  13712   6437   2287   5732       C  
ATOM   2407  NE2 HIS B 123      76.814  56.701 -17.628  1.00119.36           N  
ANISOU 2407  NE2 HIS B 123    17786  14659  12908   6070   2571   5378       N  
ATOM   2408  N   ASN B 124      78.144  61.887 -17.313  1.00101.12           N  
ANISOU 2408  N   ASN B 124    13710  14682  10030   5111    -62   4215       N  
ATOM   2409  CA  ASN B 124      78.538  62.077 -15.922  1.00107.51           C  
ANISOU 2409  CA  ASN B 124    14363  16090  10398   5277   -668   4557       C  
ATOM   2410  C   ASN B 124      77.853  63.247 -15.211  1.00103.38           C  
ANISOU 2410  C   ASN B 124    13966  16002   9311   4811  -1169   4061       C  
ATOM   2411  O   ASN B 124      78.323  63.696 -14.164  1.00 99.48           O  
ANISOU 2411  O   ASN B 124    13278  16004   8515   4723  -1741   4104       O  
ATOM   2412  CB  ASN B 124      80.053  62.228 -15.837  1.00112.72           C  
ANISOU 2412  CB  ASN B 124    14305  17095  11429   5505  -1068   4898       C  
ATOM   2413  CG  ASN B 124      80.607  63.125 -16.922  1.00109.28           C  
ANISOU 2413  CG  ASN B 124    13411  16683  11429   5344  -1142   4606       C  
ATOM   2414  OD1 ASN B 124      80.002  63.275 -17.984  1.00 97.63           O  
ANISOU 2414  OD1 ASN B 124    12184  14756  10155   5088   -684   4170       O  
ATOM   2415  ND2 ASN B 124      81.759  63.729 -16.662  1.00104.06           N  
ANISOU 2415  ND2 ASN B 124    12072  16503  10965   5350  -1692   4748       N  
ATOM   2416  N   GLN B 125      76.751  63.725 -15.791  1.00 88.96           N  
ANISOU 2416  N   GLN B 125    12451  13897   7453   4394   -896   3491       N  
ATOM   2417  CA  GLN B 125      75.905  64.788 -15.222  1.00 90.12           C  
ANISOU 2417  CA  GLN B 125    12793  14313   7135   3982  -1181   3000       C  
ATOM   2418  C   GLN B 125      76.437  66.218 -15.391  1.00 85.08           C  
ANISOU 2418  C   GLN B 125    11755  14006   6567   3672  -1683   2593       C  
ATOM   2419  O   GLN B 125      75.769  67.176 -15.003  1.00102.20           O  
ANISOU 2419  O   GLN B 125    14098  16319   8415   3336  -1851   2151       O  
ATOM   2420  CB  GLN B 125      75.534  64.521 -13.746  1.00 95.43           C  
ANISOU 2420  CB  GLN B 125    13797  15278   7183   4055  -1362   3204       C  
ATOM   2421  CG  GLN B 125      74.940  63.144 -13.463  1.00105.43           C  
ANISOU 2421  CG  GLN B 125    15476  16159   8423   4293   -811   3590       C  
ATOM   2422  CD  GLN B 125      73.490  63.004 -13.901  1.00108.67           C  
ANISOU 2422  CD  GLN B 125    16339  16184   8765   4066   -274   3295       C  
ATOM   2423  OE1 GLN B 125      72.976  63.807 -14.685  1.00110.16           O  
ANISOU 2423  OE1 GLN B 125    16437  16276   9141   3704   -241   2773       O  
ATOM   2424  NE2 GLN B 125      72.823  61.975 -13.391  1.00110.91           N  
ANISOU 2424  NE2 GLN B 125    17002  16177   8961   4151    169   3551       N  
ATOM   2425  N   GLU B 126      77.626  66.366 -15.968  1.00 94.48           N  
ANISOU 2425  N   GLU B 126    12414  15270   8214   3784  -1858   2747       N  
ATOM   2426  CA  GLU B 126      78.144  67.694 -16.293  1.00 91.79           C  
ANISOU 2426  CA  GLU B 126    11677  15136   8063   3449  -2230   2360       C  
ATOM   2427  C   GLU B 126      77.322  68.338 -17.429  1.00 94.26           C  
ANISOU 2427  C   GLU B 126    12147  15051   8618   3143  -1843   1877       C  
ATOM   2428  O   GLU B 126      76.971  67.675 -18.405  1.00 76.00           O  
ANISOU 2428  O   GLU B 126     9976  12324   6575   3246  -1334   1934       O  
ATOM   2429  CB  GLU B 126      79.623  67.608 -16.664  1.00 96.62           C  
ANISOU 2429  CB  GLU B 126    11625  15908   9178   3657  -2440   2708       C  
ATOM   2430  CG  GLU B 126      80.234  68.922 -17.119  1.00100.87           C  
ANISOU 2430  CG  GLU B 126    11708  16585  10032   3289  -2738   2343       C  
ATOM   2431  CD  GLU B 126      81.693  68.768 -17.503  1.00109.59           C  
ANISOU 2431  CD  GLU B 126    12084  17845  11709   3501  -2882   2738       C  
ATOM   2432  OE1 GLU B 126      82.313  67.771 -17.074  1.00113.98           O  
ANISOU 2432  OE1 GLU B 126    12439  18564  12303   3943  -2943   3317       O  
ATOM   2433  OE2 GLU B 126      82.216  69.636 -18.238  1.00107.54           O  
ANISOU 2433  OE2 GLU B 126    11437  17530  11896   3252  -2891   2512       O  
ATOM   2434  N   LYS B 127      77.020  69.628 -17.298  1.00 77.35           N  
ANISOU 2434  N   LYS B 127     9999  13032   6360   2767  -2082   1411       N  
ATOM   2435  CA  LYS B 127      76.049  70.270 -18.176  1.00 73.85           C  
ANISOU 2435  CA  LYS B 127     9753  12265   6041   2520  -1743   1014       C  
ATOM   2436  C   LYS B 127      76.599  71.497 -18.901  1.00 70.92           C  
ANISOU 2436  C   LYS B 127     9032  11861   6053   2273  -1857    744       C  
ATOM   2437  O   LYS B 127      77.185  72.383 -18.279  1.00 78.35           O  
ANISOU 2437  O   LYS B 127     9762  13061   6948   2069  -2276    572       O  
ATOM   2438  CB  LYS B 127      74.800  70.656 -17.372  1.00 70.76           C  
ANISOU 2438  CB  LYS B 127     9804  11917   5165   2346  -1720    725       C  
ATOM   2439  CG  LYS B 127      73.626  71.149 -18.214  1.00 80.68           C  
ANISOU 2439  CG  LYS B 127    11241  12870   6544   2165  -1346    422       C  
ATOM   2440  CD  LYS B 127      72.375  71.347 -17.347  1.00 91.81           C  
ANISOU 2440  CD  LYS B 127    13042  14317   7524   2071  -1238    230       C  
ATOM   2441  CE  LYS B 127      71.164  71.743 -18.194  1.00 94.73           C  
ANISOU 2441  CE  LYS B 127    13496  14435   8063   1939   -879     22       C  
ATOM   2442  NZ  LYS B 127      69.899  71.848 -17.408  1.00102.21           N  
ANISOU 2442  NZ  LYS B 127    14753  15398   8684   1886   -682   -106       N  
ATOM   2443  N   LEU B 128      76.396  71.540 -20.215  1.00 67.24           N  
ANISOU 2443  N   LEU B 128     8539  11069   5939   2266  -1470    703       N  
ATOM   2444  CA  LEU B 128      76.805  72.678 -21.038  1.00 66.29           C  
ANISOU 2444  CA  LEU B 128     8147  10847   6194   2059  -1460    499       C  
ATOM   2445  C   LEU B 128      75.614  73.495 -21.520  1.00 62.44           C  
ANISOU 2445  C   LEU B 128     7939  10157   5629   1862  -1242    178       C  
ATOM   2446  O   LEU B 128      74.831  73.023 -22.349  1.00 59.34           O  
ANISOU 2446  O   LEU B 128     7758   9565   5223   1929   -899    213       O  
ATOM   2447  CB  LEU B 128      77.585  72.215 -22.264  1.00 66.11           C  
ANISOU 2447  CB  LEU B 128     7869  10627   6624   2233  -1152    748       C  
ATOM   2448  CG  LEU B 128      78.049  73.394 -23.124  1.00 71.69           C  
ANISOU 2448  CG  LEU B 128     8301  11213   7724   2030  -1086    594       C  
ATOM   2449  CD1 LEU B 128      79.036  74.251 -22.335  1.00 76.47           C  
ANISOU 2449  CD1 LEU B 128     8481  12073   8502   1825  -1542    516       C  
ATOM   2450  CD2 LEU B 128      78.664  72.926 -24.437  1.00 65.62           C  
ANISOU 2450  CD2 LEU B 128     7385  10217   7332   2214   -663    829       C  
ATOM   2451  N   LEU B 129      75.504  74.728 -21.036  1.00 63.41           N  
ANISOU 2451  N   LEU B 129     8048  10325   5720   1615  -1435   -129       N  
ATOM   2452  CA  LEU B 129      74.395  75.602 -21.396  1.00 63.61           C  
ANISOU 2452  CA  LEU B 129     8299  10150   5719   1487  -1211   -381       C  
ATOM   2453  C   LEU B 129      74.622  76.330 -22.719  1.00 65.42           C  
ANISOU 2453  C   LEU B 129     8347  10139   6372   1438   -977   -367       C  
ATOM   2454  O   LEU B 129      75.737  76.772 -23.011  1.00 65.49           O  
ANISOU 2454  O   LEU B 129     8032  10125   6727   1357  -1060   -329       O  
ATOM   2455  CB  LEU B 129      74.147  76.627 -20.295  1.00 65.67           C  
ANISOU 2455  CB  LEU B 129     8701  10475   5773   1271  -1413   -726       C  
ATOM   2456  CG  LEU B 129      73.590  76.101 -18.973  1.00 67.01           C  
ANISOU 2456  CG  LEU B 129     9189  10866   5407   1312  -1551   -784       C  
ATOM   2457  CD1 LEU B 129      73.244  77.271 -18.079  1.00 67.61           C  
ANISOU 2457  CD1 LEU B 129     9489  10921   5280   1080  -1626  -1198       C  
ATOM   2458  CD2 LEU B 129      72.367  75.224 -19.223  1.00 66.02           C  
ANISOU 2458  CD2 LEU B 129     9315  10662   5108   1496  -1218   -629       C  
ATOM   2459  N   ASN B 130      73.548  76.474 -23.492  1.00 62.53           N  
ANISOU 2459  N   ASN B 130     8168   9619   5971   1481   -691   -371       N  
ATOM   2460  CA  ASN B 130      73.610  77.085 -24.819  1.00 66.01           C  
ANISOU 2460  CA  ASN B 130     8509   9862   6709   1482   -445   -288       C  
ATOM   2461  C   ASN B 130      74.823  76.654 -25.652  1.00 58.96           C  
ANISOU 2461  C   ASN B 130     7374   8929   6099   1553   -356    -72       C  
ATOM   2462  O   ASN B 130      75.722  77.456 -25.889  1.00 61.82           O  
ANISOU 2462  O   ASN B 130     7476   9197   6817   1453   -353    -73       O  
ATOM   2463  CB  ASN B 130      73.559  78.613 -24.706  1.00 70.34           C  
ANISOU 2463  CB  ASN B 130     9012  10234   7480   1325   -420   -481       C  
ATOM   2464  CG  ASN B 130      72.221  79.117 -24.187  1.00 69.28           C  
ANISOU 2464  CG  ASN B 130     9128  10060   7136   1332   -343   -644       C  
ATOM   2465  OD1 ASN B 130      71.159  78.695 -24.652  1.00 62.65           O  
ANISOU 2465  OD1 ASN B 130     8406   9266   6133   1459   -197   -523       O  
ATOM   2466  ND2 ASN B 130      72.266  80.018 -23.213  1.00 61.02           N  
ANISOU 2466  ND2 ASN B 130     8155   8929   6101   1178   -426   -929       N  
ATOM   2467  N   PRO B 131      74.862  75.378 -26.072  1.00 56.82           N  
ANISOU 2467  N   PRO B 131     7193   8692   5702   1718   -229    108       N  
ATOM   2468  CA  PRO B 131      75.912  74.926 -26.995  1.00 59.83           C  
ANISOU 2468  CA  PRO B 131     7401   8981   6353   1837    -10    324       C  
ATOM   2469  C   PRO B 131      75.817  75.600 -28.358  1.00 58.99           C  
ANISOU 2469  C   PRO B 131     7334   8704   6377   1816    296    376       C  
ATOM   2470  O   PRO B 131      74.740  76.041 -28.768  1.00 56.50           O  
ANISOU 2470  O   PRO B 131     7236   8372   5860   1765    348    306       O  
ATOM   2471  CB  PRO B 131      75.607  73.432 -27.157  1.00 57.63           C  
ANISOU 2471  CB  PRO B 131     7371   8691   5833   2002    149    436       C  
ATOM   2472  CG  PRO B 131      74.138  73.322 -26.873  1.00 60.82           C  
ANISOU 2472  CG  PRO B 131     8093   9151   5867   1906     92    277       C  
ATOM   2473  CD  PRO B 131      73.949  74.276 -25.723  1.00 53.89           C  
ANISOU 2473  CD  PRO B 131     7111   8396   4970   1792   -211    116       C  
ATOM   2474  N   GLY B 132      76.939  75.662 -29.066  1.00 61.39           N  
ANISOU 2474  N   GLY B 132     7409   8900   7015   1880    517    546       N  
ATOM   2475  CA  GLY B 132      76.972  76.257 -30.392  1.00 66.86           C  
ANISOU 2475  CA  GLY B 132     8172   9433   7800   1888    863    652       C  
ATOM   2476  C   GLY B 132      77.284  75.262 -31.497  1.00 65.59           C  
ANISOU 2476  C   GLY B 132     8201   9187   7532   2060   1256    810       C  
ATOM   2477  O   GLY B 132      77.327  74.053 -31.258  1.00 59.37           O  
ANISOU 2477  O   GLY B 132     7536   8418   6604   2173   1288    816       O  
ATOM   2478  N   ALA B 133      77.510  75.778 -32.706  1.00 60.72           N  
ANISOU 2478  N   ALA B 133     7656   8444   6970   2085   1606    941       N  
ATOM   2479  CA  ALA B 133      77.731  74.950 -33.897  1.00 62.21           C  
ANISOU 2479  CA  ALA B 133     8140   8536   6961   2225   2049   1048       C  
ATOM   2480  C   ALA B 133      78.888  73.974 -33.765  1.00 64.69           C  
ANISOU 2480  C   ALA B 133     8271   8740   7568   2414   2302   1167       C  
ATOM   2481  O   ALA B 133      78.924  72.962 -34.457  1.00 68.67           O  
ANISOU 2481  O   ALA B 133     9112   9128   7852   2542   2662   1176       O  
ATOM   2482  CB  ALA B 133      77.947  75.832 -35.133  1.00 64.21           C  
ANISOU 2482  CB  ALA B 133     8471   8684   7243   2236   2405   1220       C  
ATOM   2483  N   ASP B 134      79.838  74.287 -32.892  1.00 66.18           N  
ANISOU 2483  N   ASP B 134     7924   8963   8258   2429   2123   1263       N  
ATOM   2484  CA  ASP B 134      81.051  73.478 -32.761  1.00 69.63           C  
ANISOU 2484  CA  ASP B 134     8042   9332   9083   2661   2357   1478       C  
ATOM   2485  C   ASP B 134      81.025  72.459 -31.613  1.00 69.41           C  
ANISOU 2485  C   ASP B 134     7946   9422   9003   2784   2055   1483       C  
ATOM   2486  O   ASP B 134      82.003  71.747 -31.394  1.00 72.82           O  
ANISOU 2486  O   ASP B 134     8071   9821   9777   3036   2214   1727       O  
ATOM   2487  CB  ASP B 134      82.275  74.385 -32.647  1.00 73.12           C  
ANISOU 2487  CB  ASP B 134     7834   9777  10169   2610   2379   1662       C  
ATOM   2488  CG  ASP B 134      82.492  75.220 -33.897  1.00 88.26           C  
ANISOU 2488  CG  ASP B 134     9830  11502  12202   2562   2851   1758       C  
ATOM   2489  OD1 ASP B 134      82.263  74.691 -35.009  1.00 80.44           O  
ANISOU 2489  OD1 ASP B 134     9305  10365  10895   2713   3337   1803       O  
ATOM   2490  OD2 ASP B 134      82.880  76.402 -33.767  1.00 89.43           O  
ANISOU 2490  OD2 ASP B 134     9618  11630  12730   2354   2756   1782       O  
ATOM   2491  N   SER B 135      79.917  72.384 -30.884  1.00 66.02           N  
ANISOU 2491  N   SER B 135     7788   9128   8168   2641   1659   1265       N  
ATOM   2492  CA  SER B 135      79.787  71.346 -29.864  1.00 66.54           C  
ANISOU 2492  CA  SER B 135     7894   9276   8113   2775   1450   1305       C  
ATOM   2493  C   SER B 135      79.568  69.989 -30.535  1.00 66.87           C  
ANISOU 2493  C   SER B 135     8390   9058   7959   2971   1927   1343       C  
ATOM   2494  O   SER B 135      78.718  69.851 -31.418  1.00 65.23           O  
ANISOU 2494  O   SER B 135     8666   8731   7388   2840   2147   1147       O  
ATOM   2495  CB  SER B 135      78.651  71.659 -28.886  1.00 62.92           C  
ANISOU 2495  CB  SER B 135     7613   9010   7282   2564    975   1072       C  
ATOM   2496  OG  SER B 135      78.893  72.870 -28.196  1.00 65.75           O  
ANISOU 2496  OG  SER B 135     7621   9551   7810   2371    582    986       O  
ATOM   2497  N   ILE B 136      80.353  68.996 -30.133  1.00 70.14           N  
ANISOU 2497  N   ILE B 136     8648   9381   8622   3281   2092   1603       N  
ATOM   2498  CA  ILE B 136      80.261  67.668 -30.717  1.00 71.95           C  
ANISOU 2498  CA  ILE B 136     9332   9264   8743   3486   2636   1636       C  
ATOM   2499  C   ILE B 136      79.327  66.769 -29.913  1.00 70.63           C  
ANISOU 2499  C   ILE B 136     9530   9064   8241   3452   2475   1547       C  
ATOM   2500  O   ILE B 136      79.414  66.710 -28.689  1.00 70.84           O  
ANISOU 2500  O   ILE B 136     9299   9304   8314   3533   2072   1703       O  
ATOM   2501  CB  ILE B 136      81.651  66.985 -30.786  1.00 77.36           C  
ANISOU 2501  CB  ILE B 136     9661   9772   9960   3927   3052   2037       C  
ATOM   2502  CG1 ILE B 136      82.650  67.854 -31.553  1.00 79.51           C  
ANISOU 2502  CG1 ILE B 136     9498  10065  10645   3960   3277   2168       C  
ATOM   2503  CG2 ILE B 136      81.538  65.605 -31.407  1.00 79.95           C  
ANISOU 2503  CG2 ILE B 136    10550   9636  10191   4147   3720   2034       C  
ATOM   2504  CD1 ILE B 136      84.053  67.272 -31.589  1.00 85.54           C  
ANISOU 2504  CD1 ILE B 136     9773  10701  12028   4411   3689   2614       C  
ATOM   2505  N   ILE B 137      78.436  66.073 -30.609  1.00 69.93           N  
ANISOU 2505  N   ILE B 137    10055   8719   7796   3303   2793   1294       N  
ATOM   2506  CA  ILE B 137      77.581  65.080 -29.975  1.00 75.82           C  
ANISOU 2506  CA  ILE B 137    11175   9339   8295   3248   2778   1218       C  
ATOM   2507  C   ILE B 137      78.358  63.789 -29.726  1.00 77.67           C  
ANISOU 2507  C   ILE B 137    11478   9210   8823   3659   3236   1528       C  
ATOM   2508  O   ILE B 137      78.954  63.217 -30.652  1.00 77.79           O  
ANISOU 2508  O   ILE B 137    11691   8859   9006   3843   3841   1561       O  
ATOM   2509  CB  ILE B 137      76.340  64.785 -30.830  1.00 78.22           C  
ANISOU 2509  CB  ILE B 137    12068   9505   8146   2867   2935    814       C  
ATOM   2510  CG1 ILE B 137      75.527  66.067 -31.022  1.00 76.72           C  
ANISOU 2510  CG1 ILE B 137    11754   9696   7701   2536   2476    603       C  
ATOM   2511  CG2 ILE B 137      75.500  63.683 -30.191  1.00 82.27           C  
ANISOU 2511  CG2 ILE B 137    12945   9823   8489   2770   2999    741       C  
ATOM   2512  CD1 ILE B 137      74.162  65.838 -31.608  1.00 80.56           C  
ANISOU 2512  CD1 ILE B 137    12676  10196   7737   2143   2450    265       C  
ATOM   2513  N   GLU B 138      78.359  63.343 -28.472  1.00 75.22           N  
ANISOU 2513  N   GLU B 138    11024   8991   8564   3835   2988   1782       N  
ATOM   2514  CA  GLU B 138      79.116  62.156 -28.077  1.00 87.27           C  
ANISOU 2514  CA  GLU B 138    12553  10200  10406   4307   3384   2195       C  
ATOM   2515  C   GLU B 138      78.248  61.030 -27.512  1.00 93.24           C  
ANISOU 2515  C   GLU B 138    13822  10657  10949   4274   3567   2182       C  
ATOM   2516  O   GLU B 138      77.105  61.250 -27.079  1.00 77.93           O  
ANISOU 2516  O   GLU B 138    12089   8884   8635   3903   3241   1922       O  
ATOM   2517  CB  GLU B 138      80.225  62.520 -27.086  1.00 82.83           C  
ANISOU 2517  CB  GLU B 138    11273  10016  10184   4674   2981   2686       C  
ATOM   2518  CG  GLU B 138      81.363  63.314 -27.699  1.00 84.25           C  
ANISOU 2518  CG  GLU B 138    10894  10347  10770   4792   3004   2808       C  
ATOM   2519  CD  GLU B 138      82.140  62.517 -28.738  1.00109.69           C  
ANISOU 2519  CD  GLU B 138    14240  13070  14368   5143   3830   2971       C  
ATOM   2520  OE1 GLU B 138      82.765  63.138 -29.628  1.00110.00           O  
ANISOU 2520  OE1 GLU B 138    14045  13111  14638   5130   4046   2928       O  
ATOM   2521  OE2 GLU B 138      82.132  61.268 -28.662  1.00113.93           O  
ANISOU 2521  OE2 GLU B 138    15135  13172  14981   5443   4324   3151       O  
ATOM   2522  N   GLU B 139      78.843  59.838 -27.495  1.00 86.69           N  
ANISOU 2522  N   GLU B 139    13159   9360  10417   4694   4137   2510       N  
ATOM   2523  CA  GLU B 139      78.152  58.564 -27.279  1.00101.99           C  
ANISOU 2523  CA  GLU B 139    15702  10786  12265   4682   4585   2492       C  
ATOM   2524  C   GLU B 139      76.997  58.507 -26.279  1.00104.18           C  
ANISOU 2524  C   GLU B 139    16158  11246  12181   4388   4198   2410       C  
ATOM   2525  O   GLU B 139      75.936  58.001 -26.614  1.00111.67           O  
ANISOU 2525  O   GLU B 139    17636  11890  12904   3986   4440   2037       O  
ATOM   2526  CB  GLU B 139      79.154  57.454 -26.954  1.00 96.11           C  
ANISOU 2526  CB  GLU B 139    14920   9614  11984   5338   5129   3072       C  
ATOM   2527  CG  GLU B 139      78.485  56.147 -26.554  1.00103.82           C  
ANISOU 2527  CG  GLU B 139    16509  10017  12921   5363   5608   3136       C  
ATOM   2528  CD  GLU B 139      79.015  54.957 -27.326  1.00112.41           C  
ANISOU 2528  CD  GLU B 139    18047  10280  14385   5688   6593   3219       C  
ATOM   2529  OE1 GLU B 139      80.203  54.981 -27.709  1.00122.24           O  
ANISOU 2529  OE1 GLU B 139    18906  11534  16006   6082   6822   3523       O  
ATOM   2530  OE2 GLU B 139      78.240  54.003 -27.553  1.00108.22           O  
ANISOU 2530  OE2 GLU B 139    18219   9138  13760   5436   7119   2946       O  
ATOM   2531  N   ASN B 140      77.192  58.991 -25.057  1.00 86.01           N  
ANISOU 2531  N   ASN B 140    13429   9437   9815   4565   3624   2746       N  
ATOM   2532  CA  ASN B 140      76.140  58.853 -24.042  1.00 84.65           C  
ANISOU 2532  CA  ASN B 140    13470   9400   9295   4351   3368   2723       C  
ATOM   2533  C   ASN B 140      75.499  60.167 -23.610  1.00 79.34           C  
ANISOU 2533  C   ASN B 140    12539   9336   8272   3979   2677   2437       C  
ATOM   2534  O   ASN B 140      74.802  60.220 -22.593  1.00 78.73           O  
ANISOU 2534  O   ASN B 140    12537   9468   7907   3882   2420   2487       O  
ATOM   2535  CB  ASN B 140      76.652  58.090 -22.822  1.00 91.12           C  
ANISOU 2535  CB  ASN B 140    14217  10205  10202   4864   3387   3367       C  
ATOM   2536  CG  ASN B 140      75.997  56.731 -22.671  1.00101.88           C  
ANISOU 2536  CG  ASN B 140    16189  10931  11589   4883   4017   3463       C  
ATOM   2537  OD1 ASN B 140      74.923  56.611 -22.082  1.00108.75           O  
ANISOU 2537  OD1 ASN B 140    17336  11825  12158   4575   3942   3331       O  
ATOM   2538  ND2 ASN B 140      76.643  55.698 -23.204  1.00 98.35           N  
ANISOU 2538  ND2 ASN B 140    15961   9867  11540   5243   4705   3698       N  
ATOM   2539  N   ASP B 141      75.743  61.214 -24.392  1.00 76.13           N  
ANISOU 2539  N   ASP B 141    11860   9166   7901   3794   2452   2155       N  
ATOM   2540  CA  ASP B 141      75.209  62.546 -24.130  1.00 71.62           C  
ANISOU 2540  CA  ASP B 141    11051   9088   7075   3468   1883   1874       C  
ATOM   2541  C   ASP B 141      73.697  62.531 -24.043  1.00 77.30           C  
ANISOU 2541  C   ASP B 141    12118   9787   7466   3046   1877   1537       C  
ATOM   2542  O   ASP B 141      73.037  61.750 -24.721  1.00 69.58           O  
ANISOU 2542  O   ASP B 141    11533   8436   6470   2838   2283   1344       O  
ATOM   2543  CB  ASP B 141      75.592  63.503 -25.266  1.00 69.28           C  
ANISOU 2543  CB  ASP B 141    10531   8881   6911   3322   1833   1625       C  
ATOM   2544  CG  ASP B 141      77.038  63.932 -25.211  1.00 77.15           C  
ANISOU 2544  CG  ASP B 141    11008  10048   8258   3651   1699   1929       C  
ATOM   2545  OD1 ASP B 141      77.768  63.439 -24.324  1.00 76.33           O  
ANISOU 2545  OD1 ASP B 141    10687  10026   8290   4011   1607   2350       O  
ATOM   2546  OD2 ASP B 141      77.442  64.755 -26.069  1.00 70.20           O  
ANISOU 2546  OD2 ASP B 141     9914   9233   7528   3548   1691   1779       O  
ATOM   2547  N   THR B 142      73.150  63.404 -23.208  1.00 76.79           N  
ANISOU 2547  N   THR B 142    11897  10123   7157   2899   1432   1452       N  
ATOM   2548  CA  THR B 142      71.729  63.692 -23.264  1.00 65.66           C  
ANISOU 2548  CA  THR B 142    10671   8770   5507   2496   1400   1123       C  
ATOM   2549  C   THR B 142      71.541  65.109 -23.797  1.00 60.42           C  
ANISOU 2549  C   THR B 142     9737   8408   4812   2288   1075    842       C  
ATOM   2550  O   THR B 142      72.043  66.062 -23.209  1.00 59.79           O  
ANISOU 2550  O   THR B 142     9370   8625   4721   2382    717    884       O  
ATOM   2551  CB  THR B 142      71.049  63.541 -21.896  1.00 69.43           C  
ANISOU 2551  CB  THR B 142    11253   9397   5730   2502   1290   1250       C  
ATOM   2552  OG1 THR B 142      71.013  62.157 -21.534  1.00 70.32           O  
ANISOU 2552  OG1 THR B 142    11687   9148   5883   2653   1691   1518       O  
ATOM   2553  CG2 THR B 142      69.632  64.068 -21.958  1.00 69.39           C  
ANISOU 2553  CG2 THR B 142    11299   9514   5553   2113   1243    929       C  
ATOM   2554  N   LEU B 143      70.852  65.233 -24.930  1.00 58.85           N  
ANISOU 2554  N   LEU B 143     9644   8123   4594   2001   1203    567       N  
ATOM   2555  CA  LEU B 143      70.554  66.540 -25.507  1.00 56.07           C  
ANISOU 2555  CA  LEU B 143     9068   8024   4212   1835    948    365       C  
ATOM   2556  C   LEU B 143      69.275  67.076 -24.870  1.00 60.29           C  
ANISOU 2556  C   LEU B 143     9567   8776   4565   1631    772    237       C  
ATOM   2557  O   LEU B 143      68.284  66.353 -24.775  1.00 56.43           O  
ANISOU 2557  O   LEU B 143     9264   8202   3976   1437    934    176       O  
ATOM   2558  CB  LEU B 143      70.338  66.434 -27.017  1.00 55.97           C  
ANISOU 2558  CB  LEU B 143     9194   7888   4186   1641   1138    181       C  
ATOM   2559  CG  LEU B 143      71.427  65.764 -27.872  1.00 76.00           C  
ANISOU 2559  CG  LEU B 143    11872  10130   6874   1811   1475    255       C  
ATOM   2560  CD1 LEU B 143      71.076  65.843 -29.357  1.00 66.51           C  
ANISOU 2560  CD1 LEU B 143    10869   8882   5518   1569   1622     22       C  
ATOM   2561  CD2 LEU B 143      72.787  66.383 -27.600  1.00 58.28           C  
ANISOU 2561  CD2 LEU B 143     9281   7966   4896   2137   1368    484       C  
ATOM   2562  N   VAL B 144      69.297  68.333 -24.433  1.00 53.20           N  
ANISOU 2562  N   VAL B 144     8428   8122   3662   1665    493    192       N  
ATOM   2563  CA  VAL B 144      68.078  68.976 -23.940  1.00 58.75           C  
ANISOU 2563  CA  VAL B 144     9081   8999   4242   1516    406     72       C  
ATOM   2564  C   VAL B 144      67.477  69.790 -25.086  1.00 66.38           C  
ANISOU 2564  C   VAL B 144     9901  10054   5267   1361    359    -52       C  
ATOM   2565  O   VAL B 144      68.013  70.832 -25.482  1.00 50.09           O  
ANISOU 2565  O   VAL B 144     7671   8044   3319   1438    237    -65       O  
ATOM   2566  CB  VAL B 144      68.335  69.875 -22.716  1.00 52.58           C  
ANISOU 2566  CB  VAL B 144     8205   8385   3387   1639    196     66       C  
ATOM   2567  CG1 VAL B 144      67.032  70.493 -22.254  1.00 52.36           C  
ANISOU 2567  CG1 VAL B 144     8159   8474   3263   1527    232    -52       C  
ATOM   2568  CG2 VAL B 144      69.001  69.070 -21.579  1.00 54.85           C  
ANISOU 2568  CG2 VAL B 144     8637   8671   3534   1819    172    251       C  
ATOM   2569  N   LEU B 145      66.371  69.297 -25.631  1.00 51.56           N  
ANISOU 2569  N   LEU B 145     8075   8202   3315   1132    454   -118       N  
ATOM   2570  CA  LEU B 145      65.833  69.836 -26.880  1.00 51.40           C  
ANISOU 2570  CA  LEU B 145     7931   8315   3283    985    376   -177       C  
ATOM   2571  C   LEU B 145      64.600  70.694 -26.640  1.00 55.73           C  
ANISOU 2571  C   LEU B 145     8222   9098   3854    930    273   -169       C  
ATOM   2572  O   LEU B 145      63.761  70.364 -25.793  1.00 53.00           O  
ANISOU 2572  O   LEU B 145     7849   8791   3497    858    352   -171       O  
ATOM   2573  CB  LEU B 145      65.483  68.689 -27.826  1.00 53.23           C  
ANISOU 2573  CB  LEU B 145     8374   8463   3388    716    501   -274       C  
ATOM   2574  CG  LEU B 145      66.603  67.690 -28.141  1.00 55.24           C  
ANISOU 2574  CG  LEU B 145     8936   8403   3650    790    730   -282       C  
ATOM   2575  CD1 LEU B 145      66.047  66.488 -28.895  1.00 56.90           C  
ANISOU 2575  CD1 LEU B 145     9439   8462   3718    452    917   -458       C  
ATOM   2576  CD2 LEU B 145      67.707  68.356 -28.963  1.00 53.35           C  
ANISOU 2576  CD2 LEU B 145     8657   8145   3468    980    720   -230       C  
ATOM   2577  N   SER B 146      64.500  71.800 -27.368  1.00 51.18           N  
ANISOU 2577  N   SER B 146     7453   8656   3337    998    152   -116       N  
ATOM   2578  CA  SER B 146      63.320  72.653 -27.291  1.00 52.11           C  
ANISOU 2578  CA  SER B 146     7284   8984   3532   1011     94    -40       C  
ATOM   2579  C   SER B 146      62.721  72.944 -28.657  1.00 53.69           C  
ANISOU 2579  C   SER B 146     7317   9421   3661    909    -55     62       C  
ATOM   2580  O   SER B 146      63.426  73.364 -29.573  1.00 55.53           O  
ANISOU 2580  O   SER B 146     7620   9634   3846    986   -103    118       O  
ATOM   2581  CB  SER B 146      63.633  73.976 -26.599  1.00 56.19           C  
ANISOU 2581  CB  SER B 146     7704   9421   4224   1271    121    -11       C  
ATOM   2582  OG  SER B 146      62.463  74.779 -26.543  1.00 55.40           O  
ANISOU 2582  OG  SER B 146     7331   9470   4248   1343    152     98       O  
ATOM   2583  N   GLY B 147      61.415  72.727 -28.787  1.00 59.37           N  
ANISOU 2583  N   GLY B 147     7795  10398   4365    733   -131    115       N  
ATOM   2584  CA  GLY B 147      60.716  73.025 -30.030  1.00 58.67           C  
ANISOU 2584  CA  GLY B 147     7484  10646   4162    628   -358    256       C  
ATOM   2585  C   GLY B 147      59.291  72.514 -30.014  1.00 62.04           C  
ANISOU 2585  C   GLY B 147     7587  11385   4602    349   -471    287       C  
ATOM   2586  O   GLY B 147      58.756  72.176 -28.955  1.00 62.16           O  
ANISOU 2586  O   GLY B 147     7503  11325   4789    309   -300    245       O  
ATOM   2587  N   GLU B 148      58.668  72.454 -31.188  1.00 65.49           N  
ANISOU 2587  N   GLU B 148     7842  12200   4842    137   -765    373       N  
ATOM   2588  CA  GLU B 148      57.304  71.953 -31.291  1.00 76.01           C  
ANISOU 2588  CA  GLU B 148     8774  13901   6203   -204   -946    405       C  
ATOM   2589  C   GLU B 148      57.284  70.432 -31.364  1.00 71.13           C  
ANISOU 2589  C   GLU B 148     8454  13165   5407   -727   -914     59       C  
ATOM   2590  O   GLU B 148      58.258  69.811 -31.781  1.00 70.46           O  
ANISOU 2590  O   GLU B 148     8881  12809   5081   -825   -828   -168       O  
ATOM   2591  CB  GLU B 148      56.593  72.571 -32.487  1.00 83.32           C  
ANISOU 2591  CB  GLU B 148     9324  15363   6970   -224  -1347    677       C  
ATOM   2592  CG  GLU B 148      56.568  74.087 -32.442  1.00 88.05           C  
ANISOU 2592  CG  GLU B 148     9641  16011   7802    333  -1306   1076       C  
ATOM   2593  CD  GLU B 148      55.789  74.693 -33.588  1.00 98.16           C  
ANISOU 2593  CD  GLU B 148    10503  17860   8933    377  -1707   1455       C  
ATOM   2594  OE1 GLU B 148      55.830  75.932 -33.745  1.00 98.46           O  
ANISOU 2594  OE1 GLU B 148    10364  17908   9139    857  -1652   1834       O  
ATOM   2595  OE2 GLU B 148      55.135  73.930 -34.328  1.00106.91           O  
ANISOU 2595  OE2 GLU B 148    11468  19405   9748    -79  -2080   1382       O  
ATOM   2596  N   ARG B 149      56.169  69.847 -30.937  1.00 74.40           N  
ANISOU 2596  N   ARG B 149     8537  13738   5992  -1053   -920     34       N  
ATOM   2597  CA  ARG B 149      55.996  68.398 -30.877  1.00 76.58           C  
ANISOU 2597  CA  ARG B 149     9068  13834   6195  -1594   -816   -289       C  
ATOM   2598  C   ARG B 149      56.332  67.698 -32.190  1.00 79.28           C  
ANISOU 2598  C   ARG B 149     9781  14240   6101  -2011  -1041   -569       C  
ATOM   2599  O   ARG B 149      57.059  66.702 -32.201  1.00 78.63           O  
ANISOU 2599  O   ARG B 149    10261  13723   5894  -2198   -785   -866       O  
ATOM   2600  CB  ARG B 149      54.551  68.064 -30.486  1.00 86.72           C  
ANISOU 2600  CB  ARG B 149     9785  15405   7758  -1945   -862   -220       C  
ATOM   2601  CG  ARG B 149      54.116  68.676 -29.175  1.00 90.51           C  
ANISOU 2601  CG  ARG B 149     9936  15807   8648  -1555   -546     36       C  
ATOM   2602  CD  ARG B 149      52.668  68.358 -28.836  1.00101.84           C  
ANISOU 2602  CD  ARG B 149    10743  17537  10413  -1890   -532    148       C  
ATOM   2603  NE  ARG B 149      51.746  69.285 -29.486  1.00112.30           N  
ANISOU 2603  NE  ARG B 149    11350  19462  11857  -1795   -910    471       N  
ATOM   2604  CZ  ARG B 149      50.439  69.338 -29.243  1.00118.49           C  
ANISOU 2604  CZ  ARG B 149    11395  20610  13015  -1952   -933    695       C  
ATOM   2605  NH1 ARG B 149      49.890  68.514 -28.360  1.00117.93           N  
ANISOU 2605  NH1 ARG B 149    11237  20340  13232  -2249   -564    602       N  
ATOM   2606  NH2 ARG B 149      49.680  70.218 -29.882  1.00122.70           N  
ANISOU 2606  NH2 ARG B 149    11248  21710  13661  -1787  -1297   1061       N  
ATOM   2607  N   LYS B 150      55.789  68.216 -33.290  1.00 92.74           N  
ANISOU 2607  N   LYS B 150    11191  16487   7557  -2138  -1496   -454       N  
ATOM   2608  CA  LYS B 150      56.015  67.626 -34.603  1.00 86.80           C  
ANISOU 2608  CA  LYS B 150    10822  15877   6281  -2565  -1743   -735       C  
ATOM   2609  C   LYS B 150      57.491  67.670 -34.986  1.00 90.82           C  
ANISOU 2609  C   LYS B 150    11996  15971   6539  -2255  -1482   -844       C  
ATOM   2610  O   LYS B 150      58.034  66.697 -35.505  1.00 84.45           O  
ANISOU 2610  O   LYS B 150    11763  14878   5446  -2574  -1322  -1212       O  
ATOM   2611  CB  LYS B 150      55.153  68.309 -35.670  1.00105.40           C  
ANISOU 2611  CB  LYS B 150    12705  18988   8356  -2687  -2335   -501       C  
ATOM   2612  CG  LYS B 150      55.358  69.810 -35.786  1.00103.36           C  
ANISOU 2612  CG  LYS B 150    12155  18944   8173  -2010  -2430      0       C  
ATOM   2613  CD  LYS B 150      54.420  70.422 -36.810  1.00108.66           C  
ANISOU 2613  CD  LYS B 150    12314  20395   8577  -2098  -3023    322       C  
ATOM   2614  CE  LYS B 150      54.589  71.928 -36.861  1.00105.63           C  
ANISOU 2614  CE  LYS B 150    11649  20133   8353  -1375  -3023    879       C  
ATOM   2615  NZ  LYS B 150      53.608  72.560 -37.776  1.00101.30           N  
ANISOU 2615  NZ  LYS B 150    10532  20344   7612  -1364  -3580   1311       N  
ATOM   2616  N   HIS B 151      58.149  68.790 -34.704  1.00 81.61           N  
ANISOU 2616  N   HIS B 151    10749  14731   5527  -1641  -1385   -529       N  
ATOM   2617  CA  HIS B 151      59.551  68.947 -35.075  1.00 80.37           C  
ANISOU 2617  CA  HIS B 151    11106  14223   5209  -1336  -1138   -574       C  
ATOM   2618  C   HIS B 151      60.467  68.068 -34.229  1.00 71.81           C  
ANISOU 2618  C   HIS B 151    10435  12517   4332  -1279   -675   -795       C  
ATOM   2619  O   HIS B 151      61.431  67.500 -34.731  1.00 71.82           O  
ANISOU 2619  O   HIS B 151    10946  12202   4141  -1293   -436   -986       O  
ATOM   2620  CB  HIS B 151      59.973  70.418 -35.003  1.00 73.93           C  
ANISOU 2620  CB  HIS B 151    10051  13483   4558   -758  -1157   -181       C  
ATOM   2621  CG  HIS B 151      59.377  71.268 -36.081  1.00 76.52           C  
ANISOU 2621  CG  HIS B 151    10112  14355   4605   -719  -1545    105       C  
ATOM   2622  ND1 HIS B 151      58.991  72.574 -35.875  1.00 77.72           N  
ANISOU 2622  ND1 HIS B 151     9800  14710   5019   -296  -1644    536       N  
ATOM   2623  CD2 HIS B 151      59.107  70.997 -37.380  1.00 80.96           C  
ANISOU 2623  CD2 HIS B 151    10838  15305   4617  -1033  -1849     43       C  
ATOM   2624  CE1 HIS B 151      58.506  73.072 -37.000  1.00 83.53           C  
ANISOU 2624  CE1 HIS B 151    10384  15946   5408   -308  -1999    794       C  
ATOM   2625  NE2 HIS B 151      58.563  72.133 -37.927  1.00 87.18           N  
ANISOU 2625  NE2 HIS B 151    11222  16569   5334   -768  -2164    495       N  
ATOM   2626  N   LEU B 152      60.156  67.946 -32.945  1.00 69.68           N  
ANISOU 2626  N   LEU B 152     9948  12081   4445  -1187   -523   -734       N  
ATOM   2627  CA  LEU B 152      60.948  67.097 -32.066  1.00 74.50           C  
ANISOU 2627  CA  LEU B 152    10916  12158   5233  -1100   -119   -860       C  
ATOM   2628  C   LEU B 152      60.908  65.647 -32.539  1.00 81.53           C  
ANISOU 2628  C   LEU B 152    12250  12782   5947  -1581     65  -1207       C  
ATOM   2629  O   LEU B 152      61.938  64.969 -32.578  1.00 70.66           O  
ANISOU 2629  O   LEU B 152    11341  10954   4551  -1474    407  -1324       O  
ATOM   2630  CB  LEU B 152      60.460  67.205 -30.617  1.00 65.65           C  
ANISOU 2630  CB  LEU B 152     9512  10971   4460   -954      0   -715       C  
ATOM   2631  CG  LEU B 152      60.806  68.510 -29.890  1.00 64.25           C  
ANISOU 2631  CG  LEU B 152     9078  10857   4478   -444    -28   -455       C  
ATOM   2632  CD1 LEU B 152      60.048  68.610 -28.589  1.00 61.72           C  
ANISOU 2632  CD1 LEU B 152     8501  10548   4402   -378     91   -353       C  
ATOM   2633  CD2 LEU B 152      62.298  68.621 -29.631  1.00 58.67           C  
ANISOU 2633  CD2 LEU B 152     8681   9816   3794    -96    148   -440       C  
ATOM   2634  N   LYS B 153      59.717  65.181 -32.903  1.00 83.76           N  
ANISOU 2634  N   LYS B 153    12362  13330   6132  -2117   -145  -1368       N  
ATOM   2635  CA  LYS B 153      59.546  63.798 -33.331  1.00 85.33           C  
ANISOU 2635  CA  LYS B 153    12994  13243   6186  -2681     41  -1763       C  
ATOM   2636  C   LYS B 153      60.379  63.485 -34.578  1.00 82.56           C  
ANISOU 2636  C   LYS B 153    13212  12751   5405  -2769    120  -2020       C  
ATOM   2637  O   LYS B 153      60.989  62.422 -34.665  1.00100.36           O  
ANISOU 2637  O   LYS B 153    16032  14462   7639  -2898    550  -2285       O  
ATOM   2638  CB  LYS B 153      58.066  63.480 -33.568  1.00 92.13           C  
ANISOU 2638  CB  LYS B 153    13476  14502   7026  -3318   -281  -1900       C  
ATOM   2639  CG  LYS B 153      57.764  61.992 -33.734  1.00 97.85           C  
ANISOU 2639  CG  LYS B 153    14618  14837   7723  -3984    -24  -2339       C  
ATOM   2640  CD  LYS B 153      56.323  61.752 -34.184  1.00102.34           C  
ANISOU 2640  CD  LYS B 153    14753  15900   8233  -4715   -445  -2513       C  
ATOM   2641  CE  LYS B 153      55.322  62.530 -33.334  1.00104.87           C  
ANISOU 2641  CE  LYS B 153    14233  16657   8954  -4546   -661  -2108       C  
ATOM   2642  NZ  LYS B 153      55.396  62.196 -31.877  1.00104.51           N  
ANISOU 2642  NZ  LYS B 153    14177  16138   9394  -4279   -149  -1933       N  
ATOM   2643  N   LYS B 154      60.428  64.420 -35.524  1.00 82.80           N  
ANISOU 2643  N   LYS B 154    13123  13237   5102  -2655   -230  -1910       N  
ATOM   2644  CA  LYS B 154      61.165  64.194 -36.774  1.00 85.50           C  
ANISOU 2644  CA  LYS B 154    14030  13497   4959  -2738   -132  -2138       C  
ATOM   2645  C   LYS B 154      62.677  64.151 -36.544  1.00 81.59           C  
ANISOU 2645  C   LYS B 154    13912  12454   4633  -2201    385  -2050       C  
ATOM   2646  O   LYS B 154      63.372  63.318 -37.121  1.00 95.01           O  
ANISOU 2646  O   LYS B 154    16209  13741   6148  -2302    778  -2328       O  
ATOM   2647  CB  LYS B 154      60.815  65.257 -37.823  1.00 87.33           C  
ANISOU 2647  CB  LYS B 154    14027  14383   4772  -2703   -626  -1953       C  
ATOM   2648  CG  LYS B 154      61.347  64.965 -39.219  1.00 91.86           C  
ANISOU 2648  CG  LYS B 154    15071  14825   5005  -2730   -547  -2131       C  
ATOM   2649  CD  LYS B 154      60.694  63.723 -39.813  1.00102.44           C  
ANISOU 2649  CD  LYS B 154    16721  16075   6128  -3414   -582  -2608       C  
ATOM   2650  CE  LYS B 154      61.135  63.482 -41.265  1.00104.85           C  
ANISOU 2650  CE  LYS B 154    17495  16332   6010  -3455   -529  -2795       C  
ATOM   2651  NZ  LYS B 154      60.759  64.609 -42.163  1.00106.87           N  
ANISOU 2651  NZ  LYS B 154    17456  17218   5933  -3260  -1033  -2481       N  
ATOM   2652  N   LEU B 155      63.181  65.047 -35.696  1.00 77.65           N  
ANISOU 2652  N   LEU B 155    13044  11948   4511  -1639    397  -1665       N  
ATOM   2653  CA  LEU B 155      64.610  65.087 -35.380  1.00 78.94           C  
ANISOU 2653  CA  LEU B 155    13416  11673   4903  -1137    811  -1529       C  
ATOM   2654  C   LEU B 155      65.083  63.801 -34.709  1.00 73.46           C  
ANISOU 2654  C   LEU B 155    13073  10382   4455  -1151   1287  -1674       C  
ATOM   2655  O   LEU B 155      66.116  63.236 -35.074  1.00 76.39           O  
ANISOU 2655  O   LEU B 155    13865  10333   4827   -980   1724  -1747       O  
ATOM   2656  CB  LEU B 155      64.940  66.285 -34.483  1.00 76.04           C  
ANISOU 2656  CB  LEU B 155    12554  11443   4896   -640    666  -1142       C  
ATOM   2657  CG  LEU B 155      66.364  66.321 -33.923  1.00 64.54           C  
ANISOU 2657  CG  LEU B 155    11172   9596   3753   -167   1006   -978       C  
ATOM   2658  CD1 LEU B 155      67.406  66.397 -35.043  1.00 66.09           C  
ANISOU 2658  CD1 LEU B 155    11681   9656   3775    -21   1267   -996       C  
ATOM   2659  CD2 LEU B 155      66.528  67.476 -32.938  1.00 60.33           C  
ANISOU 2659  CD2 LEU B 155    10164   9221   3539    190    803   -686       C  
ATOM   2660  N   ILE B 156      64.325  63.349 -33.717  1.00 84.10           N  
ANISOU 2660  N   ILE B 156    14239  11677   6038  -1316   1252  -1668       N  
ATOM   2661  CA  ILE B 156      64.667  62.134 -32.993  1.00 84.30           C  
ANISOU 2661  CA  ILE B 156    14586  11128   6315  -1306   1717  -1728       C  
ATOM   2662  C   ILE B 156      64.627  60.927 -33.930  1.00 90.91           C  
ANISOU 2662  C   ILE B 156    16041  11584   6917  -1759   2059  -2154       C  
ATOM   2663  O   ILE B 156      65.516  60.075 -33.902  1.00 94.87           O  
ANISOU 2663  O   ILE B 156    16986  11506   7554  -1570   2596  -2192       O  
ATOM   2664  CB  ILE B 156      63.740  61.929 -31.780  1.00 85.59           C  
ANISOU 2664  CB  ILE B 156    14448  11337   6736  -1429   1637  -1616       C  
ATOM   2665  CG1 ILE B 156      64.040  62.986 -30.712  1.00 83.79           C  
ANISOU 2665  CG1 ILE B 156    13771  11337   6729   -915   1447  -1230       C  
ATOM   2666  CG2 ILE B 156      63.901  60.534 -31.209  1.00 83.18           C  
ANISOU 2666  CG2 ILE B 156    14552  10415   6636  -1522   2152  -1689       C  
ATOM   2667  CD1 ILE B 156      63.266  62.811 -29.424  1.00 77.50           C  
ANISOU 2667  CD1 ILE B 156    12747  10554   6146   -947   1463  -1088       C  
ATOM   2668  N   HIS B 157      63.609  60.885 -34.783  1.00 92.26           N  
ANISOU 2668  N   HIS B 157    16236  12092   6728  -2352   1746  -2470       N  
ATOM   2669  CA  HIS B 157      63.467  59.827 -35.780  1.00 90.93           C  
ANISOU 2669  CA  HIS B 157    16694  11624   6229  -2904   2000  -2974       C  
ATOM   2670  C   HIS B 157      64.597  59.809 -36.818  1.00111.95           C  
ANISOU 2670  C   HIS B 157    19762  14059   8714  -2620   2285  -3024       C  
ATOM   2671  O   HIS B 157      65.058  58.736 -37.222  1.00116.70           O  
ANISOU 2671  O   HIS B 157    20878  14076   9386  -2725   2779  -3256       O  
ATOM   2672  CB  HIS B 157      62.109  59.940 -36.482  1.00 95.32           C  
ANISOU 2672  CB  HIS B 157    17064  12747   6407  -3618   1449  -3262       C  
ATOM   2673  CG  HIS B 157      61.994  59.103 -37.721  1.00114.93           C  
ANISOU 2673  CG  HIS B 157    20023  15052   8594  -4111   1531  -3696       C  
ATOM   2674  ND1 HIS B 157      62.255  59.599 -38.982  1.00120.39           N  
ANISOU 2674  ND1 HIS B 157    20754  16053   8936  -4017   1287  -3688       N  
ATOM   2675  CD2 HIS B 157      61.648  57.806 -37.892  1.00120.16           C  
ANISOU 2675  CD2 HIS B 157    21124  15231   9300  -4676   1852  -4116       C  
ATOM   2676  CE1 HIS B 157      62.075  58.643 -39.875  1.00125.65           C  
ANISOU 2676  CE1 HIS B 157    21874  16475   9392  -4500   1431  -4098       C  
ATOM   2677  NE2 HIS B 157      61.707  57.544 -39.241  1.00128.89           N  
ANISOU 2677  NE2 HIS B 157    22523  16393  10055  -4919   1773  -4367       N  
ATOM   2678  N   ASP B 158      65.037  60.990 -37.253  1.00103.51           N  
ANISOU 2678  N   ASP B 158    18388  13415   7526  -2231   1997  -2746       N  
ATOM   2679  CA  ASP B 158      66.077  61.084 -38.282  1.00104.03           C  
ANISOU 2679  CA  ASP B 158    18705  13323   7499  -1941   2246  -2721       C  
ATOM   2680  C   ASP B 158      67.486  60.901 -37.717  1.00101.76           C  
ANISOU 2680  C   ASP B 158    18530  12511   7624  -1339   2814  -2470       C  
ATOM   2681  O   ASP B 158      68.337  60.270 -38.344  1.00106.09           O  
ANISOU 2681  O   ASP B 158    19459  12617   8233  -1214   3291  -2550       O  
ATOM   2682  CB  ASP B 158      65.980  62.409 -39.048  1.00 96.90           C  
ANISOU 2682  CB  ASP B 158    17463  13054   6301  -1787   1777  -2511       C  
ATOM   2683  CG  ASP B 158      64.866  62.411 -40.085  1.00104.00           C  
ANISOU 2683  CG  ASP B 158    18374  14417   6725  -2313   1303  -2751       C  
ATOM   2684  OD1 ASP B 158      64.288  61.333 -40.357  1.00109.31           O  
ANISOU 2684  OD1 ASP B 158    19363  14888   7280  -2848   1369  -3142       O  
ATOM   2685  OD2 ASP B 158      64.578  63.493 -40.641  1.00104.54           O  
ANISOU 2685  OD2 ASP B 158    18138  15041   6543  -2188    876  -2528       O  
ATOM   2686  N   PHE B 159      67.728  61.461 -36.537  1.00 97.33           N  
ANISOU 2686  N   PHE B 159    17617  12021   7343   -961   2758  -2145       N  
ATOM   2687  CA  PHE B 159      69.014  61.309 -35.864  1.00 94.68           C  
ANISOU 2687  CA  PHE B 159    17291  11269   7414   -372   3221  -1853       C  
ATOM   2688  C   PHE B 159      68.817  60.648 -34.502  1.00 91.36           C  
ANISOU 2688  C   PHE B 159    16757  10577   7377   -281   3320  -1707       C  
ATOM   2689  O   PHE B 159      68.941  61.293 -33.464  1.00 84.72           O  
ANISOU 2689  O   PHE B 159    15415   9958   6817     36   3042  -1357       O  
ATOM   2690  CB  PHE B 159      69.712  62.665 -35.703  1.00 88.35           C  
ANISOU 2690  CB  PHE B 159    16000  10823   6746     90   2981  -1473       C  
ATOM   2691  CG  PHE B 159      70.178  63.270 -37.000  1.00 95.02           C  
ANISOU 2691  CG  PHE B 159    16923  11830   7351    123   3004  -1491       C  
ATOM   2692  CD1 PHE B 159      70.531  62.460 -38.071  1.00 97.51           C  
ANISOU 2692  CD1 PHE B 159    17677  11823   7551    -19   3373  -1720       C  
ATOM   2693  CD2 PHE B 159      70.265  64.645 -37.149  1.00 87.53           C  
ANISOU 2693  CD2 PHE B 159    15607  11322   6329    303   2677  -1252       C  
ATOM   2694  CE1 PHE B 159      70.960  63.009 -39.269  1.00104.58           C  
ANISOU 2694  CE1 PHE B 159    18638  12879   8219     25   3405  -1704       C  
ATOM   2695  CE2 PHE B 159      70.692  65.203 -38.341  1.00 94.35           C  
ANISOU 2695  CE2 PHE B 159    16531  12318   7000    346   2731  -1213       C  
ATOM   2696  CZ  PHE B 159      71.042  64.383 -39.405  1.00104.02           C  
ANISOU 2696  CZ  PHE B 159    18189  13265   8069    211   3090  -1436       C  
TER    2697      PHE B 159                                                      
ATOM   2698  N   SER C  -1      39.576  61.509   2.268  1.00 87.77           N  
ANISOU 2698  N   SER C  -1    12847   6245  14257   1157    241   -507       N  
ATOM   2699  CA  SER C  -1      39.018  60.452   1.433  1.00 93.14           C  
ANISOU 2699  CA  SER C  -1    13323   7288  14778   1319    153   -229       C  
ATOM   2700  C   SER C  -1      39.505  59.077   1.886  1.00 87.72           C  
ANISOU 2700  C   SER C  -1    12315   7114  13899   1065    190   -409       C  
ATOM   2701  O   SER C  -1      40.618  58.942   2.396  1.00 83.34           O  
ANISOU 2701  O   SER C  -1    11751   6620  13295    691    278   -587       O  
ATOM   2702  CB  SER C  -1      39.374  60.684  -0.042  1.00103.80           C  
ANISOU 2702  CB  SER C  -1    14901   8429  16108   1263     74    281       C  
ATOM   2703  OG  SER C  -1      40.773  60.585  -0.265  1.00104.07           O  
ANISOU 2703  OG  SER C  -1    15026   8431  16086    777    151    343       O  
ATOM   2704  N   GLY C   0      38.661  58.064   1.705  1.00 75.92           N  
ANISOU 2704  N   GLY C   0    10548   6001  12299   1274    110   -358       N  
ATOM   2705  CA  GLY C   0      39.012  56.706   2.058  1.00 77.96           C  
ANISOU 2705  CA  GLY C   0    10524   6705  12394   1072    120   -496       C  
ATOM   2706  C   GLY C   0      39.406  55.907   0.831  1.00 71.70           C  
ANISOU 2706  C   GLY C   0     9736   6012  11494    972     37   -175       C  
ATOM   2707  O   GLY C   0      39.507  56.431  -0.280  1.00 87.17           O  
ANISOU 2707  O   GLY C   0    11910   7735  13476   1019    -17    180       O  
ATOM   2708  N   LEU C   1      39.631  54.624   1.037  1.00 56.12           N  
ANISOU 2708  N   LEU C   1     7530   4400   9392    838     24   -288       N  
ATOM   2709  CA  LEU C   1      40.071  53.755  -0.037  1.00 41.19           C  
ANISOU 2709  CA  LEU C   1     5637   2691   7323    721    -52    -46       C  
ATOM   2710  C   LEU C   1      38.843  53.028  -0.608  1.00 42.62           C  
ANISOU 2710  C   LEU C   1     5629   3187   7378    985   -251     71       C  
ATOM   2711  O   LEU C   1      37.789  53.002   0.035  1.00 48.07           O  
ANISOU 2711  O   LEU C   1     6124   3952   8188   1216   -302    -80       O  
ATOM   2712  CB  LEU C   1      41.052  52.725   0.527  1.00 40.85           C  
ANISOU 2712  CB  LEU C   1     5463   2967   7090    412     43   -255       C  
ATOM   2713  CG  LEU C   1      42.314  53.284   1.187  1.00 41.45           C  
ANISOU 2713  CG  LEU C   1     5638   2874   7237    110    226   -419       C  
ATOM   2714  CD1 LEU C   1      43.028  52.198   1.935  1.00 42.51           C  
ANISOU 2714  CD1 LEU C   1     5567   3399   7186    -86    289   -633       C  
ATOM   2715  CD2 LEU C   1      43.233  53.894   0.129  1.00 40.98           C  
ANISOU 2715  CD2 LEU C   1     5820   2618   7132    -88    277   -127       C  
ATOM   2716  N   ASN C   2      38.970  52.459  -1.803  1.00 35.78           N  
ANISOU 2716  N   ASN C   2     4794   2545   6255    940   -361    312       N  
ATOM   2717  CA  ASN C   2      38.062  51.369  -2.203  1.00 37.31           C  
ANISOU 2717  CA  ASN C   2     4756   3149   6271   1044   -542    297       C  
ATOM   2718  C   ASN C   2      38.708  50.032  -1.888  1.00 37.04           C  
ANISOU 2718  C   ASN C   2     4609   3392   6072    778   -493     89       C  
ATOM   2719  O   ASN C   2      39.824  49.775  -2.322  1.00 30.28           O  
ANISOU 2719  O   ASN C   2     3879   2567   5059    573   -414    126       O  
ATOM   2720  CB  ASN C   2      37.698  51.432  -3.696  1.00 42.08           C  
ANISOU 2720  CB  ASN C   2     5429   3901   6657   1171   -720    625       C  
ATOM   2721  CG  ASN C   2      36.767  52.591  -4.036  1.00 54.17           C  
ANISOU 2721  CG  ASN C   2     7013   5221   8349   1529   -822    883       C  
ATOM   2722  OD1 ASN C   2      35.617  52.627  -3.603  1.00 57.85           O  
ANISOU 2722  OD1 ASN C   2     7265   5769   8947   1787   -920    794       O  
ATOM   2723  ND2 ASN C   2      37.255  53.529  -4.840  1.00 62.87           N  
ANISOU 2723  ND2 ASN C   2     8383   6069   9434   1558   -798   1233       N  
ATOM   2724  N   ILE C   3      38.019  49.166  -1.150  1.00 27.98           N  
ANISOU 2724  N   ILE C   3     3215   2452   4963    788   -535   -110       N  
ATOM   2725  CA  ILE C   3      38.649  47.917  -0.732  1.00 26.16           C  
ANISOU 2725  CA  ILE C   3     2903   2404   4634    559   -477   -275       C  
ATOM   2726  C   ILE C   3      37.714  46.761  -1.018  1.00 31.12           C  
ANISOU 2726  C   ILE C   3     3333   3296   5195    563   -642   -324       C  
ATOM   2727  O   ILE C   3      36.520  46.841  -0.743  1.00 31.74           O  
ANISOU 2727  O   ILE C   3     3215   3472   5371    700   -735   -336       O  
ATOM   2728  CB  ILE C   3      38.982  47.899   0.787  1.00 26.50           C  
ANISOU 2728  CB  ILE C   3     2843   2415   4812    473   -313   -475       C  
ATOM   2729  CG1 ILE C   3      39.824  49.130   1.177  1.00 34.91           C  
ANISOU 2729  CG1 ILE C   3     4082   3208   5974    435   -159   -500       C  
ATOM   2730  CG2 ILE C   3      39.724  46.609   1.149  1.00 29.88           C  
ANISOU 2730  CG2 ILE C   3     3206   3015   5134    274   -261   -568       C  
ATOM   2731  CD1 ILE C   3      39.918  49.344   2.688  1.00 40.10           C  
ANISOU 2731  CD1 ILE C   3     4613   3880   6745    397    -24   -742       C  
ATOM   2732  N   LYS C   4      38.258  45.695  -1.587  1.00 24.33           N  
ANISOU 2732  N   LYS C   4     2512   2553   4178    410   -675   -372       N  
ATOM   2733  CA  LYS C   4      37.434  44.517  -1.887  1.00 27.52           C  
ANISOU 2733  CA  LYS C   4     2754   3154   4549    353   -834   -463       C  
ATOM   2734  C   LYS C   4      38.086  43.335  -1.221  1.00 30.58           C  
ANISOU 2734  C   LYS C   4     3121   3519   4980    168   -739   -601       C  
ATOM   2735  O   LYS C   4      39.259  43.077  -1.440  1.00 32.12           O  
ANISOU 2735  O   LYS C   4     3467   3660   5078    104   -644   -629       O  
ATOM   2736  CB  LYS C   4      37.345  44.274  -3.402  1.00 34.07           C  
ANISOU 2736  CB  LYS C   4     3667   4136   5142    371  -1002   -423       C  
ATOM   2737  CG  LYS C   4      36.356  43.143  -3.788  1.00 48.24           C  
ANISOU 2737  CG  LYS C   4     5280   6137   6913    283  -1200   -569       C  
ATOM   2738  CD  LYS C   4      36.227  42.990  -5.296  1.00 55.69           C  
ANISOU 2738  CD  LYS C   4     6285   7306   7570    310  -1383   -574       C  
ATOM   2739  CE  LYS C   4      35.088  42.043  -5.671  1.00 66.19           C  
ANISOU 2739  CE  LYS C   4     7398   8865   8888    203  -1609   -749       C  
ATOM   2740  NZ  LYS C   4      35.460  40.609  -5.535  1.00 72.27           N  
ANISOU 2740  NZ  LYS C   4     8199   9532   9727    -37  -1591  -1020       N  
ATOM   2741  N   GLU C   5      37.332  42.580  -0.430  1.00 26.09           N  
ANISOU 2741  N   GLU C   5     2352   3010   4553     89   -763   -662       N  
ATOM   2742  CA  GLU C   5      37.945  41.439   0.246  1.00 22.76           C  
ANISOU 2742  CA  GLU C   5     1926   2527   4196    -66   -674   -726       C  
ATOM   2743  C   GLU C   5      37.357  40.164  -0.318  1.00 28.03           C  
ANISOU 2743  C   GLU C   5     2544   3208   4898   -203   -825   -819       C  
ATOM   2744  O   GLU C   5      36.171  40.088  -0.492  1.00 28.36           O  
ANISOU 2744  O   GLU C   5     2413   3375   4988   -238   -961   -827       O  
ATOM   2745  CB  GLU C   5      37.670  41.490   1.766  1.00 31.23           C  
ANISOU 2745  CB  GLU C   5     2815   3644   5405    -94   -549   -685       C  
ATOM   2746  CG  GLU C   5      38.286  40.294   2.531  1.00 30.76           C  
ANISOU 2746  CG  GLU C   5     2745   3536   5408   -231   -460   -668       C  
ATOM   2747  CD  GLU C   5      37.918  40.289   4.022  1.00 45.83           C  
ANISOU 2747  CD  GLU C   5     4539   5584   7289   -243   -319   -552       C  
ATOM   2748  OE1 GLU C   5      38.305  39.328   4.721  1.00 37.26           O  
ANISOU 2748  OE1 GLU C   5     3459   4490   6208   -326   -251   -459       O  
ATOM   2749  OE2 GLU C   5      37.269  41.256   4.487  1.00 35.71           O  
ANISOU 2749  OE2 GLU C   5     3159   4431   5979   -157   -285   -560       O  
ATOM   2750  N   ASN C   6      38.197  39.173  -0.632  1.00 26.23           N  
ANISOU 2750  N   ASN C   6     2460   2852   4653   -277   -802   -913       N  
ATOM   2751  CA  ASN C   6      37.706  37.889  -1.109  1.00 29.12           C  
ANISOU 2751  CA  ASN C   6     2825   3150   5088   -424   -924  -1043       C  
ATOM   2752  C   ASN C   6      38.332  36.775  -0.272  1.00 28.81           C  
ANISOU 2752  C   ASN C   6     2857   2915   5177   -483   -783   -988       C  
ATOM   2753  O   ASN C   6      39.406  36.935   0.281  1.00 27.11           O  
ANISOU 2753  O   ASN C   6     2693   2637   4969   -403   -653   -941       O  
ATOM   2754  CB  ASN C   6      38.099  37.633  -2.582  1.00 41.62           C  
ANISOU 2754  CB  ASN C   6     4569   4757   6486   -395  -1047  -1249       C  
ATOM   2755  CG  ASN C   6      37.275  38.437  -3.565  1.00 48.20           C  
ANISOU 2755  CG  ASN C   6     5337   5848   7127   -334  -1216  -1245       C  
ATOM   2756  OD1 ASN C   6      37.589  39.587  -3.876  1.00 54.46           O  
ANISOU 2756  OD1 ASN C   6     6189   6748   7756   -174  -1174  -1105       O  
ATOM   2757  ND2 ASN C   6      36.225  37.826  -4.077  1.00 47.91           N  
ANISOU 2757  ND2 ASN C   6     5188   5917   7099   -462  -1396  -1367       N  
ATOM   2758  N   ASP C   7      37.647  35.640  -0.210  1.00 32.43           N  
ANISOU 2758  N   ASP C   7     3303   3279   5740   -632   -827   -993       N  
ATOM   2759  CA  ASP C   7      38.131  34.512   0.561  1.00 34.82           C  
ANISOU 2759  CA  ASP C   7     3668   3353   6209   -687   -732   -911       C  
ATOM   2760  C   ASP C   7      39.091  33.716  -0.299  1.00 36.73           C  
ANISOU 2760  C   ASP C   7     4129   3395   6430   -610   -742  -1100       C  
ATOM   2761  O   ASP C   7      38.859  33.560  -1.490  1.00 34.18           O  
ANISOU 2761  O   ASP C   7     3889   3109   5990   -627   -850  -1311       O  
ATOM   2762  CB  ASP C   7      36.934  33.608   0.893  1.00 39.97           C  
ANISOU 2762  CB  ASP C   7     4232   3958   6996   -916   -783   -842       C  
ATOM   2763  CG  ASP C   7      37.273  32.530   1.893  1.00 45.56           C  
ANISOU 2763  CG  ASP C   7     4975   4422   7913   -994   -688   -671       C  
ATOM   2764  OD1 ASP C   7      37.791  32.877   2.973  1.00 49.76           O  
ANISOU 2764  OD1 ASP C   7     5423   5006   8477   -917   -569   -473       O  
ATOM   2765  OD2 ASP C   7      36.997  31.336   1.609  1.00 48.36           O  
ANISOU 2765  OD2 ASP C   7     5436   4535   8402  -1142   -734   -728       O  
ATOM   2766  N   LEU C   8      40.148  33.188   0.314  1.00 30.70           N  
ANISOU 2766  N   LEU C   8     3441   2452   5770   -513   -629  -1031       N  
ATOM   2767  CA  LEU C   8      41.000  32.178  -0.333  1.00 31.47           C  
ANISOU 2767  CA  LEU C   8     3739   2331   5887   -411   -617  -1198       C  
ATOM   2768  C   LEU C   8      40.821  30.913   0.494  1.00 31.84           C  
ANISOU 2768  C   LEU C   8     3821   2066   6209   -501   -588  -1048       C  
ATOM   2769  O   LEU C   8      41.448  30.766   1.540  1.00 33.73           O  
ANISOU 2769  O   LEU C   8     4020   2216   6579   -418   -488   -831       O  
ATOM   2770  CB  LEU C   8      42.468  32.635  -0.269  1.00 28.20           C  
ANISOU 2770  CB  LEU C   8     3369   1979   5367   -174   -499  -1216       C  
ATOM   2771  CG  LEU C   8      42.691  34.056  -0.785  1.00 28.81           C  
ANISOU 2771  CG  LEU C   8     3396   2353   5197   -120   -495  -1279       C  
ATOM   2772  CD1 LEU C   8      44.143  34.485  -0.554  1.00 32.74           C  
ANISOU 2772  CD1 LEU C   8     3903   2946   5590     73   -346  -1273       C  
ATOM   2773  CD2 LEU C   8      42.333  34.110  -2.278  1.00 38.13           C  
ANISOU 2773  CD2 LEU C   8     4669   3641   6177   -135   -612  -1517       C  
ATOM   2774  N   PRO C   9      39.926  30.014   0.058  1.00 40.58           N  
ANISOU 2774  N   PRO C   9     4995   3011   7413   -692   -677  -1143       N  
ATOM   2775  CA  PRO C   9      39.565  28.885   0.923  1.00 40.58           C  
ANISOU 2775  CA  PRO C   9     5023   2707   7688   -838   -648   -948       C  
ATOM   2776  C   PRO C   9      40.764  28.065   1.396  1.00 46.35           C  
ANISOU 2776  C   PRO C   9     5905   3132   8574   -630   -549   -849       C  
ATOM   2777  O   PRO C   9      41.530  27.535   0.584  1.00 41.99           O  
ANISOU 2777  O   PRO C   9     5545   2424   7986   -459   -545  -1082       O  
ATOM   2778  CB  PRO C   9      38.664  28.021   0.025  1.00 43.99           C  
ANISOU 2778  CB  PRO C   9     5565   2983   8168  -1064   -760  -1179       C  
ATOM   2779  CG  PRO C   9      38.121  28.971  -0.984  1.00 45.41           C  
ANISOU 2779  CG  PRO C   9     5652   3514   8088  -1091   -866  -1391       C  
ATOM   2780  CD  PRO C   9      39.196  29.990  -1.223  1.00 45.05           C  
ANISOU 2780  CD  PRO C   9     5605   3672   7840   -805   -808  -1422       C  
ATOM   2781  N   GLY C  10      40.902  27.962   2.712  1.00 39.68           N  
ANISOU 2781  N   GLY C  10     4957   2237   7884   -629   -467   -489       N  
ATOM   2782  CA  GLY C  10      41.909  27.124   3.326  1.00 41.49           C  
ANISOU 2782  CA  GLY C  10     5303   2185   8278   -424   -380   -300       C  
ATOM   2783  C   GLY C  10      43.258  27.823   3.387  1.00 38.28           C  
ANISOU 2783  C   GLY C  10     4858   1964   7723    -93   -300   -316       C  
ATOM   2784  O   GLY C  10      44.224  27.279   3.909  1.00 41.41           O  
ANISOU 2784  O   GLY C  10     5308   2224   8201    150   -223   -144       O  
ATOM   2785  N   ILE C  11      43.319  29.016   2.828  1.00 34.66           N  
ANISOU 2785  N   ILE C  11     4305   1833   7031    -77   -315   -513       N  
ATOM   2786  CA  ILE C  11      44.596  29.763   2.742  1.00 33.90           C  
ANISOU 2786  CA  ILE C  11     4168   1955   6758    205   -229   -578       C  
ATOM   2787  C   ILE C  11      44.598  31.051   3.542  1.00 35.45           C  
ANISOU 2787  C   ILE C  11     4137   2519   6814    166   -165   -408       C  
ATOM   2788  O   ILE C  11      45.543  31.337   4.290  1.00 35.84           O  
ANISOU 2788  O   ILE C  11     4080   2813   6724    341    -57   -229       O  
ATOM   2789  CB  ILE C  11      44.947  30.081   1.282  1.00 38.73           C  
ANISOU 2789  CB  ILE C  11     4893   2705   7117    286   -264   -959       C  
ATOM   2790  CG1 ILE C  11      45.309  28.791   0.562  1.00 42.07           C  
ANISOU 2790  CG1 ILE C  11     5538   2841   7605    406   -275  -1138       C  
ATOM   2791  CG2 ILE C  11      46.081  31.121   1.205  1.00 38.04           C  
ANISOU 2791  CG2 ILE C  11     4707   2948   6798    494   -163  -1011       C  
ATOM   2792  CD1 ILE C  11      45.597  28.941  -0.935  1.00 47.30           C  
ANISOU 2792  CD1 ILE C  11     6304   3650   8018    475   -301  -1511       C  
ATOM   2793  N   GLY C  12      43.557  31.860   3.367  1.00 35.15           N  
ANISOU 2793  N   GLY C  12     4012   2648   6696    -58   -228   -466       N  
ATOM   2794  CA  GLY C  12      43.487  33.128   4.062  1.00 31.02           C  
ANISOU 2794  CA  GLY C  12     3299   2535   5951    -92   -159   -344       C  
ATOM   2795  C   GLY C  12      42.480  34.069   3.429  1.00 26.74           C  
ANISOU 2795  C   GLY C  12     2714   2127   5318   -239   -245   -500       C  
ATOM   2796  O   GLY C  12      41.386  33.655   3.024  1.00 31.30           O  
ANISOU 2796  O   GLY C  12     3294   2558   6041   -411   -363   -564       O  
ATOM   2797  N   LYS C  13      42.859  35.335   3.330  1.00 28.32           N  
ANISOU 2797  N   LYS C  13     2869   2601   5290   -174   -193   -553       N  
ATOM   2798  CA  LYS C  13      42.003  36.340   2.700  1.00 28.57           C  
ANISOU 2798  CA  LYS C  13     2875   2746   5234   -246   -272   -660       C  
ATOM   2799  C   LYS C  13      42.857  37.211   1.762  1.00 30.04           C  
ANISOU 2799  C   LYS C  13     3174   3040   5199   -135   -244   -791       C  
ATOM   2800  O   LYS C  13      44.062  37.432   2.010  1.00 26.07           O  
ANISOU 2800  O   LYS C  13     2684   2636   4586    -42   -124   -771       O  
ATOM   2801  CB  LYS C  13      41.370  37.276   3.756  1.00 27.71           C  
ANISOU 2801  CB  LYS C  13     2573   2853   5102   -296   -215   -533       C  
ATOM   2802  CG  LYS C  13      40.389  36.662   4.749  1.00 32.61           C  
ANISOU 2802  CG  LYS C  13     3018   3495   5879   -430   -217   -367       C  
ATOM   2803  CD  LYS C  13      39.193  35.982   4.107  1.00 37.55           C  
ANISOU 2803  CD  LYS C  13     3673   4005   6588   -551   -349   -399       C  
ATOM   2804  CE  LYS C  13      38.122  35.687   5.175  1.00 45.52           C  
ANISOU 2804  CE  LYS C  13     4515   5167   7615   -675   -308   -203       C  
ATOM   2805  NZ  LYS C  13      37.232  34.563   4.762  1.00 48.78           N  
ANISOU 2805  NZ  LYS C  13     4948   5418   8169   -862   -408   -195       N  
ATOM   2806  N   LYS C  14      42.225  37.707   0.706  1.00 26.01           N  
ANISOU 2806  N   LYS C  14     2720   2553   4609   -158   -355   -897       N  
ATOM   2807  CA  LYS C  14      42.842  38.687  -0.214  1.00 24.28           C  
ANISOU 2807  CA  LYS C  14     2598   2461   4164    -86   -329   -946       C  
ATOM   2808  C   LYS C  14      42.137  40.028  -0.134  1.00 26.58           C  
ANISOU 2808  C   LYS C  14     2838   2834   4426    -97   -350   -854       C  
ATOM   2809  O   LYS C  14      40.925  40.062  -0.199  1.00 27.74           O  
ANISOU 2809  O   LYS C  14     2905   2981   4654   -126   -471   -845       O  
ATOM   2810  CB  LYS C  14      42.704  38.166  -1.643  1.00 28.63           C  
ANISOU 2810  CB  LYS C  14     3271   3007   4602    -67   -452  -1120       C  
ATOM   2811  CG  LYS C  14      43.274  39.129  -2.694  1.00 32.40           C  
ANISOU 2811  CG  LYS C  14     3840   3668   4801     -7   -425  -1115       C  
ATOM   2812  CD  LYS C  14      43.367  38.456  -4.068  1.00 37.30           C  
ANISOU 2812  CD  LYS C  14     4564   4372   5236     33   -520  -1325       C  
ATOM   2813  CE  LYS C  14      42.106  38.668  -4.883  1.00 50.46           C  
ANISOU 2813  CE  LYS C  14     6213   6130   6829    -14   -724  -1356       C  
ATOM   2814  NZ  LYS C  14      42.353  38.317  -6.314  1.00 63.76           N  
ANISOU 2814  NZ  LYS C  14     7991   8016   8217     31   -801  -1557       N  
ATOM   2815  N   PHE C  15      42.889  41.124   0.019  1.00 23.05           N  
ANISOU 2815  N   PHE C  15     2427   2448   3884    -74   -234   -792       N  
ATOM   2816  CA  PHE C  15      42.314  42.459   0.002  1.00 24.54           C  
ANISOU 2816  CA  PHE C  15     2617   2626   4081    -52   -246   -713       C  
ATOM   2817  C   PHE C  15      42.882  43.213  -1.189  1.00 30.48           C  
ANISOU 2817  C   PHE C  15     3529   3403   4650    -32   -240   -654       C  
ATOM   2818  O   PHE C  15      44.091  43.364  -1.304  1.00 29.72           O  
ANISOU 2818  O   PHE C  15     3489   3361   4441    -79   -115   -651       O  
ATOM   2819  CB  PHE C  15      42.697  43.227   1.271  1.00 20.92           C  
ANISOU 2819  CB  PHE C  15     2084   2165   3699    -82   -104   -699       C  
ATOM   2820  CG  PHE C  15      42.079  42.647   2.537  1.00 27.04           C  
ANISOU 2820  CG  PHE C  15     2675   2997   4603    -98    -92   -714       C  
ATOM   2821  CD1 PHE C  15      42.653  41.535   3.179  1.00 27.12           C  
ANISOU 2821  CD1 PHE C  15     2618   3069   4619   -137    -40   -702       C  
ATOM   2822  CD2 PHE C  15      40.941  43.210   3.070  1.00 23.46           C  
ANISOU 2822  CD2 PHE C  15     2103   2558   4253    -54   -123   -714       C  
ATOM   2823  CE1 PHE C  15      42.080  41.032   4.354  1.00 28.63           C  
ANISOU 2823  CE1 PHE C  15     2635   3345   4900   -168    -18   -646       C  
ATOM   2824  CE2 PHE C  15      40.342  42.695   4.231  1.00 29.06           C  
ANISOU 2824  CE2 PHE C  15     2609   3395   5038    -84    -92   -705       C  
ATOM   2825  CZ  PHE C  15      40.936  41.595   4.866  1.00 27.68           C  
ANISOU 2825  CZ  PHE C  15     2406   3287   4825   -155    -36   -641       C  
ATOM   2826  N   GLU C  16      42.010  43.699  -2.052  1.00 31.11           N  
ANISOU 2826  N   GLU C  16     3652   3488   4682     35   -373   -578       N  
ATOM   2827  CA  GLU C  16      42.447  44.546  -3.147  1.00 28.89           C  
ANISOU 2827  CA  GLU C  16     3519   3246   4212     56   -365   -439       C  
ATOM   2828  C   GLU C  16      42.058  45.950  -2.779  1.00 31.38           C  
ANISOU 2828  C   GLU C  16     3874   3383   4666    106   -335   -283       C  
ATOM   2829  O   GLU C  16      40.904  46.220  -2.404  1.00 28.19           O  
ANISOU 2829  O   GLU C  16     3381   2917   4414    219   -431   -273       O  
ATOM   2830  CB  GLU C  16      41.767  44.117  -4.444  1.00 33.88           C  
ANISOU 2830  CB  GLU C  16     4173   4046   4653    124   -550   -436       C  
ATOM   2831  CG  GLU C  16      42.150  42.715  -4.871  1.00 39.92           C  
ANISOU 2831  CG  GLU C  16     4928   4936   5303     82   -580   -662       C  
ATOM   2832  CD  GLU C  16      41.539  42.336  -6.211  1.00 63.58           C  
ANISOU 2832  CD  GLU C  16     7943   8151   8062    125   -768   -726       C  
ATOM   2833  OE1 GLU C  16      40.733  43.133  -6.740  1.00 71.09           O  
ANISOU 2833  OE1 GLU C  16     8885   9188   8937    200   -892   -550       O  
ATOM   2834  OE2 GLU C  16      41.873  41.248  -6.737  1.00 74.03           O  
ANISOU 2834  OE2 GLU C  16     9287   9571   9269    101   -797   -963       O  
ATOM   2835  N   ILE C  17      43.026  46.847  -2.861  1.00 28.80           N  
ANISOU 2835  N   ILE C  17     3671   2966   4305     20   -194   -175       N  
ATOM   2836  CA  ILE C  17      42.855  48.187  -2.353  1.00 26.65           C  
ANISOU 2836  CA  ILE C  17     3472   2425   4228     36   -133    -78       C  
ATOM   2837  C   ILE C  17      43.204  49.159  -3.456  1.00 28.23           C  
ANISOU 2837  C   ILE C  17     3868   2539   4320     18   -118    203       C  
ATOM   2838  O   ILE C  17      44.208  48.978  -4.156  1.00 34.96           O  
ANISOU 2838  O   ILE C  17     4778   3556   4950   -120    -38    277       O  
ATOM   2839  CB  ILE C  17      43.812  48.411  -1.160  1.00 29.48           C  
ANISOU 2839  CB  ILE C  17     3790   2713   4698   -133     48   -235       C  
ATOM   2840  CG1 ILE C  17      43.487  47.430  -0.028  1.00 35.16           C  
ANISOU 2840  CG1 ILE C  17     4307   3563   5488   -109     39   -448       C  
ATOM   2841  CG2 ILE C  17      43.808  49.862  -0.690  1.00 28.91           C  
ANISOU 2841  CG2 ILE C  17     3830   2315   4839   -163    128   -199       C  
ATOM   2842  CD1 ILE C  17      44.640  47.213   0.940  1.00 34.81           C  
ANISOU 2842  CD1 ILE C  17     4177   3625   5423   -269    190   -586       C  
ATOM   2843  N   GLU C  18      42.355  50.153  -3.639  1.00 29.17           N  
ANISOU 2843  N   GLU C  18     4073   2426   4583    178   -192    383       N  
ATOM   2844  CA  GLU C  18      42.595  51.199  -4.624  1.00 36.66           C  
ANISOU 2844  CA  GLU C  18     5231   3227   5471    179   -179    735       C  
ATOM   2845  C   GLU C  18      42.401  52.577  -4.004  1.00 39.35           C  
ANISOU 2845  C   GLU C  18     5713   3079   6158    223   -108    815       C  
ATOM   2846  O   GLU C  18      41.388  52.833  -3.349  1.00 40.02           O  
ANISOU 2846  O   GLU C  18     5729   3007   6471    447   -181    703       O  
ATOM   2847  CB  GLU C  18      41.655  51.043  -5.836  1.00 41.64           C  
ANISOU 2847  CB  GLU C  18     5858   4073   5890    403   -388    968       C  
ATOM   2848  CG  GLU C  18      42.010  52.009  -6.987  1.00 53.66           C  
ANISOU 2848  CG  GLU C  18     7594   5532   7264    394   -371   1414       C  
ATOM   2849  CD  GLU C  18      40.881  52.237  -7.990  1.00 65.99           C  
ANISOU 2849  CD  GLU C  18     9153   7244   8677    689   -598   1709       C  
ATOM   2850  OE1 GLU C  18      39.813  51.593  -7.890  1.00 56.84           O  
ANISOU 2850  OE1 GLU C  18     7801   6286   7508    880   -782   1538       O  
ATOM   2851  OE2 GLU C  18      41.070  53.080  -8.892  1.00 79.50           O  
ANISOU 2851  OE2 GLU C  18    11040   8897  10269    718   -594   2143       O  
ATOM   2852  N   THR C  19      43.367  53.467  -4.222  1.00 37.72           N  
ANISOU 2852  N   THR C  19     5698   2633   5999      5     40    994       N  
ATOM   2853  CA  THR C  19      43.302  54.836  -3.731  1.00 40.54           C  
ANISOU 2853  CA  THR C  19     6245   2436   6721      4    118   1063       C  
ATOM   2854  C   THR C  19      42.471  55.681  -4.702  1.00 55.02           C  
ANISOU 2854  C   THR C  19     8260   4032   8612    280     -5   1502       C  
ATOM   2855  O   THR C  19      42.300  55.310  -5.864  1.00 58.71           O  
ANISOU 2855  O   THR C  19     8722   4821   8764    361   -114   1798       O  
ATOM   2856  CB  THR C  19      44.713  55.470  -3.644  1.00 51.93           C  
ANISOU 2856  CB  THR C  19     7824   3695   8211   -409    326   1107       C  
ATOM   2857  OG1 THR C  19      45.243  55.632  -4.964  1.00 58.70           O  
ANISOU 2857  OG1 THR C  19     8802   4689   8812   -528    348   1539       O  
ATOM   2858  CG2 THR C  19      45.653  54.605  -2.846  1.00 49.94           C  
ANISOU 2858  CG2 THR C  19     7362   3779   7833   -663    434    739       C  
ATOM   2859  N   ARG C  20      41.964  56.818  -4.234  1.00 62.44           N  
ANISOU 2859  N   ARG C  20     9356   4424   9943    444      8   1538       N  
ATOM   2860  CA  ARG C  20      41.126  57.687  -5.067  1.00 75.42           C  
ANISOU 2860  CA  ARG C  20    11175   5867  11615    762   -122   1934       C  
ATOM   2861  C   ARG C  20      41.891  58.198  -6.299  1.00 79.66           C  
ANISOU 2861  C   ARG C  20    11940   6372  11955    560    -76   2448       C  
ATOM   2862  O   ARG C  20      41.290  58.661  -7.273  1.00 83.92           O  
ANISOU 2862  O   ARG C  20    12590   6928  12367    804   -208   2852       O  
ATOM   2863  CB  ARG C  20      40.563  58.845  -4.229  1.00 83.85           C  
ANISOU 2863  CB  ARG C  20    12392   6507  12962    940   -112   1703       C  
ATOM   2864  CG  ARG C  20      39.537  59.730  -4.925  1.00 94.82           C  
ANISOU 2864  CG  ARG C  20    13939   7700  14389   1345   -265   2030       C  
ATOM   2865  CD  ARG C  20      38.828  60.633  -3.920  1.00 99.15           C  
ANISOU 2865  CD  ARG C  20    14567   7894  15210   1597   -258   1710       C  
ATOM   2866  NE  ARG C  20      37.997  61.647  -4.567  1.00106.39           N  
ANISOU 2866  NE  ARG C  20    15689   8529  16206   1974   -398   2029       N  
ATOM   2867  CZ  ARG C  20      36.755  61.440  -4.995  1.00103.18           C  
ANISOU 2867  CZ  ARG C  20    15114   8376  15713   2430   -590   2162       C  
ATOM   2868  NH1 ARG C  20      36.190  60.248  -4.855  1.00101.81           N  
ANISOU 2868  NH1 ARG C  20    14568   8739  15375   2535   -654   2005       N  
ATOM   2869  NH2 ARG C  20      36.079  62.426  -5.570  1.00104.28           N  
ANISOU 2869  NH2 ARG C  20    15442   8242  15937   2767   -741   2453       N  
ATOM   2870  N   SER C  21      43.218  58.094  -6.246  1.00 80.54           N  
ANISOU 2870  N   SER C  21    12089   6510  12001    109    113   2422       N  
ATOM   2871  CA  SER C  21      44.090  58.439  -7.366  1.00 81.82           C  
ANISOU 2871  CA  SER C  21    12407   6771  11909   -156    199   2880       C  
ATOM   2872  C   SER C  21      44.437  57.196  -8.171  1.00 81.27           C  
ANISOU 2872  C   SER C  21    12123   7410  11345   -218    171   2951       C  
ATOM   2873  O   SER C  21      45.362  57.209  -8.981  1.00 80.92           O  
ANISOU 2873  O   SER C  21    12120   7618  11009   -492    285   3228       O  
ATOM   2874  CB  SER C  21      45.379  59.066  -6.848  1.00 84.91           C  
ANISOU 2874  CB  SER C  21    12914   6927  12421   -647    405   2724       C  
ATOM   2875  OG  SER C  21      46.042  58.166  -5.978  1.00 79.19           O  
ANISOU 2875  OG  SER C  21    11944   6444  11701   -869    515   2300       O  
ATOM   2876  N   HIS C  22      43.712  56.113  -7.907  1.00 77.61           N  
ANISOU 2876  N   HIS C  22    11422   7323  10742     18     19   2604       N  
ATOM   2877  CA  HIS C  22      43.825  54.870  -8.670  1.00 76.45           C  
ANISOU 2877  CA  HIS C  22    11083   7858  10105     23    -60   2527       C  
ATOM   2878  C   HIS C  22      45.141  54.090  -8.526  1.00 74.45           C  
ANISOU 2878  C   HIS C  22    10711   7941   9634   -321    118   2269       C  
ATOM   2879  O   HIS C  22      45.458  53.283  -9.393  1.00 81.06           O  
ANISOU 2879  O   HIS C  22    11450   9303  10046   -340     97   2283       O  
ATOM   2880  CB  HIS C  22      43.498  55.104 -10.153  1.00 80.13           C  
ANISOU 2880  CB  HIS C  22    11630   8609  10207    168   -177   3040       C  
ATOM   2881  CG  HIS C  22      42.251  55.903 -10.374  1.00 88.45           C  
ANISOU 2881  CG  HIS C  22    12781   9374  11452    549   -364   3361       C  
ATOM   2882  ND1 HIS C  22      40.994  55.413 -10.093  1.00 90.00           N  
ANISOU 2882  ND1 HIS C  22    12794   9696  11704    893   -582   3138       N  
ATOM   2883  CD2 HIS C  22      42.071  57.160 -10.840  1.00 95.08           C  
ANISOU 2883  CD2 HIS C  22    13867   9806  12453    655   -362   3906       C  
ATOM   2884  CE1 HIS C  22      40.092  56.336 -10.377  1.00 94.72           C  
ANISOU 2884  CE1 HIS C  22    13496  10020  12473   1229   -712   3513       C  
ATOM   2885  NE2 HIS C  22      40.718  57.405 -10.835  1.00 98.87           N  
ANISOU 2885  NE2 HIS C  22    14303  10208  13056   1098   -585   3935       N  
ATOM   2886  N   GLU C  23      45.891  54.304  -7.442  1.00 64.00           N  
ANISOU 2886  N   GLU C  23     9374   6363   8581   -567    285   2006       N  
ATOM   2887  CA  GLU C  23      47.031  53.432  -7.129  1.00 49.18           C  
ANISOU 2887  CA  GLU C  23     7317   4854   6516   -816    425   1708       C  
ATOM   2888  C   GLU C  23      46.509  52.154  -6.494  1.00 47.87           C  
ANISOU 2888  C   GLU C  23     6942   4920   6326   -623    311   1280       C  
ATOM   2889  O   GLU C  23      45.566  52.196  -5.715  1.00 40.87           O  
ANISOU 2889  O   GLU C  23     6031   3794   5702   -439    208   1119       O  
ATOM   2890  CB  GLU C  23      48.022  54.109  -6.179  1.00 57.18           C  
ANISOU 2890  CB  GLU C  23     8348   5582   7795  -1159    623   1578       C  
ATOM   2891  CG  GLU C  23      48.897  55.186  -6.834  1.00 69.04           C  
ANISOU 2891  CG  GLU C  23    10017   6929   9286  -1492    788   1982       C  
ATOM   2892  CD  GLU C  23      49.853  54.618  -7.881  1.00 77.23           C  
ANISOU 2892  CD  GLU C  23    10934   8564   9845  -1655    892   2153       C  
ATOM   2893  OE1 GLU C  23      50.754  53.822  -7.524  1.00 73.58           O  
ANISOU 2893  OE1 GLU C  23    10243   8493   9222  -1792    993   1850       O  
ATOM   2894  OE2 GLU C  23      49.700  54.972  -9.068  1.00 87.08           O  
ANISOU 2894  OE2 GLU C  23    12303   9925  10856  -1619    875   2599       O  
ATOM   2895  N   LYS C  24      47.116  51.019  -6.807  1.00 38.51           N  
ANISOU 2895  N   LYS C  24     5602   4191   4839   -660    339   1101       N  
ATOM   2896  CA  LYS C  24      46.539  49.744  -6.391  1.00 45.51           C  
ANISOU 2896  CA  LYS C  24     6328   5255   5708   -473    213    760       C  
ATOM   2897  C   LYS C  24      47.516  48.850  -5.660  1.00 46.63           C  
ANISOU 2897  C   LYS C  24     6302   5589   5825   -588    334    451       C  
ATOM   2898  O   LYS C  24      48.695  48.770  -5.987  1.00 37.85           O  
ANISOU 2898  O   LYS C  24     5141   4720   4519   -753    485    471       O  
ATOM   2899  CB  LYS C  24      45.940  49.001  -7.583  1.00 56.51           C  
ANISOU 2899  CB  LYS C  24     7705   6985   6780   -292     52    803       C  
ATOM   2900  CG  LYS C  24      44.818  49.767  -8.267  1.00 75.39           C  
ANISOU 2900  CG  LYS C  24    10210   9264   9170   -114   -115   1115       C  
ATOM   2901  CD  LYS C  24      44.240  48.991  -9.433  1.00 83.69           C  
ANISOU 2901  CD  LYS C  24    11206  10740   9852     40   -295   1109       C  
ATOM   2902  CE  LYS C  24      43.181  49.805 -10.150  1.00 92.76           C  
ANISOU 2902  CE  LYS C  24    12435  11856  10954    237   -472   1472       C  
ATOM   2903  NZ  LYS C  24      43.750  50.999 -10.833  1.00 96.90           N  
ANISOU 2903  NZ  LYS C  24    13143  12300  11373    152   -360   1961       N  
ATOM   2904  N   MET C  25      46.999  48.155  -4.665  1.00 29.78           N  
ANISOU 2904  N   MET C  25     4058   3380   3877   -483    265    188       N  
ATOM   2905  CA  MET C  25      47.832  47.339  -3.812  1.00 30.42           C  
ANISOU 2905  CA  MET C  25     3978   3611   3971   -548    362    -59       C  
ATOM   2906  C   MET C  25      46.958  46.138  -3.485  1.00 39.47           C  
ANISOU 2906  C   MET C  25     5040   4780   5178   -357    217   -251       C  
ATOM   2907  O   MET C  25      45.748  46.281  -3.340  1.00 36.97           O  
ANISOU 2907  O   MET C  25     4745   4299   5004   -248     83   -230       O  
ATOM   2908  CB  MET C  25      48.162  48.146  -2.574  1.00 36.98           C  
ANISOU 2908  CB  MET C  25     4775   4233   5042   -703    464   -119       C  
ATOM   2909  CG  MET C  25      48.843  47.451  -1.434  1.00 59.99           C  
ANISOU 2909  CG  MET C  25     7495   7309   7990   -747    536   -349       C  
ATOM   2910  SD  MET C  25      48.821  48.636  -0.068  1.00 51.28           S  
ANISOU 2910  SD  MET C  25     6380   5949   7155   -913    605   -452       S  
ATOM   2911  CE  MET C  25      49.656  47.751   1.221  1.00 52.56           C  
ANISOU 2911  CE  MET C  25     6273   6438   7262   -950    669   -681       C  
ATOM   2912  N   THR C  26      47.559  44.957  -3.421  1.00 27.66           N  
ANISOU 2912  N   THR C  26     3442   3485   3583   -314    246   -423       N  
ATOM   2913  CA  THR C  26      46.838  43.748  -2.983  1.00 27.96           C  
ANISOU 2913  CA  THR C  26     3409   3478   3735   -183    130   -593       C  
ATOM   2914  C   THR C  26      47.568  43.230  -1.757  1.00 35.12           C  
ANISOU 2914  C   THR C  26     4177   4417   4749   -203    232   -693       C  
ATOM   2915  O   THR C  26      48.795  43.164  -1.757  1.00 31.80           O  
ANISOU 2915  O   THR C  26     3692   4186   4204   -244    363   -715       O  
ATOM   2916  CB  THR C  26      46.808  42.667  -4.073  1.00 34.98           C  
ANISOU 2916  CB  THR C  26     4333   4521   4438    -75     49   -718       C  
ATOM   2917  OG1 THR C  26      45.894  43.056  -5.101  1.00 39.32           O  
ANISOU 2917  OG1 THR C  26     4974   5094   4871    -42    -92   -633       O  
ATOM   2918  CG2 THR C  26      46.338  41.316  -3.501  1.00 37.86           C  
ANISOU 2918  CG2 THR C  26     4636   4774   4975      9    -35   -903       C  
ATOM   2919  N   ILE C  27      46.827  42.898  -0.701  1.00 27.11           N  
ANISOU 2919  N   ILE C  27     3086   3275   3939   -174    177   -730       N  
ATOM   2920  CA  ILE C  27      47.443  42.320   0.507  1.00 23.80           C  
ANISOU 2920  CA  ILE C  27     2520   2936   3587   -170    256   -779       C  
ATOM   2921  C   ILE C  27      46.840  40.945   0.714  1.00 31.55           C  
ANISOU 2921  C   ILE C  27     3474   3831   4681    -59    162   -822       C  
ATOM   2922  O   ILE C  27      45.616  40.808   0.755  1.00 28.72           O  
ANISOU 2922  O   ILE C  27     3130   3336   4448    -62     49   -811       O  
ATOM   2923  CB  ILE C  27      47.165  43.148   1.758  1.00 29.10           C  
ANISOU 2923  CB  ILE C  27     3102   3579   4378   -257    299   -766       C  
ATOM   2924  CG1 ILE C  27      47.788  44.542   1.630  1.00 30.77           C  
ANISOU 2924  CG1 ILE C  27     3363   3789   4539   -410    397   -751       C  
ATOM   2925  CG2 ILE C  27      47.728  42.438   3.004  1.00 31.63           C  
ANISOU 2925  CG2 ILE C  27     3244   4067   4708   -236    359   -786       C  
ATOM   2926  CD1 ILE C  27      47.507  45.448   2.852  1.00 29.08           C  
ANISOU 2926  CD1 ILE C  27     3080   3517   4451   -497    440   -825       C  
ATOM   2927  N   ILE C  28      47.697  39.929   0.801  1.00 25.93           N  
ANISOU 2927  N   ILE C  28     2720   3193   3939     40    209   -865       N  
ATOM   2928  CA  ILE C  28      47.232  38.565   1.052  1.00 25.63           C  
ANISOU 2928  CA  ILE C  28     2687   2990   4062    136    133   -884       C  
ATOM   2929  C   ILE C  28      47.566  38.264   2.504  1.00 30.06           C  
ANISOU 2929  C   ILE C  28     3092   3624   4704    155    199   -757       C  
ATOM   2930  O   ILE C  28      48.720  38.413   2.915  1.00 30.72           O  
ANISOU 2930  O   ILE C  28     3071   3929   4671    204    303   -735       O  
ATOM   2931  CB  ILE C  28      47.959  37.541   0.187  1.00 26.60           C  
ANISOU 2931  CB  ILE C  28     2886   3094   4128    294    139  -1019       C  
ATOM   2932  CG1 ILE C  28      47.849  37.880  -1.308  1.00 34.58           C  
ANISOU 2932  CG1 ILE C  28     4023   4164   4953    283     94  -1159       C  
ATOM   2933  CG2 ILE C  28      47.411  36.105   0.462  1.00 31.98           C  
ANISOU 2933  CG2 ILE C  28     3616   3484   5053    370     54  -1043       C  
ATOM   2934  CD1 ILE C  28      46.430  37.851  -1.852  1.00 36.90           C  
ANISOU 2934  CD1 ILE C  28     4403   4298   5320    197    -75  -1204       C  
ATOM   2935  N   ILE C  29      46.575  37.880   3.292  1.00 27.11           N  
ANISOU 2935  N   ILE C  29     2670   3133   4496    106    142   -660       N  
ATOM   2936  CA  ILE C  29      46.847  37.501   4.669  1.00 28.99           C  
ANISOU 2936  CA  ILE C  29     2752   3494   4768    132    202   -496       C  
ATOM   2937  C   ILE C  29      46.632  35.981   4.826  1.00 28.52           C  
ANISOU 2937  C   ILE C  29     2737   3197   4904    222    152   -383       C  
ATOM   2938  O   ILE C  29      45.520  35.488   4.639  1.00 32.33           O  
ANISOU 2938  O   ILE C  29     3279   3444   5560    126     63   -370       O  
ATOM   2939  CB  ILE C  29      45.885  38.198   5.626  1.00 32.19           C  
ANISOU 2939  CB  ILE C  29     3036   3996   5197      1    203   -429       C  
ATOM   2940  CG1 ILE C  29      45.956  39.719   5.454  1.00 36.16           C  
ANISOU 2940  CG1 ILE C  29     3541   4614   5584    -81    243   -562       C  
ATOM   2941  CG2 ILE C  29      46.206  37.822   7.065  1.00 31.32           C  
ANISOU 2941  CG2 ILE C  29     2741   4112   5046     26    270   -249       C  
ATOM   2942  CD1 ILE C  29      44.980  40.445   6.407  1.00 39.76           C  
ANISOU 2942  CD1 ILE C  29     3951   5147   6008   -147    239   -530       C  
ATOM   2943  N   HIS C  30      47.699  35.269   5.168  1.00 29.19           N  
ANISOU 2943  N   HIS C  30     2783   3337   4972    403    209   -295       N  
ATOM   2944  CA  HIS C  30      47.661  33.817   5.376  1.00 31.63           C  
ANISOU 2944  CA  HIS C  30     3159   3353   5503    531    176   -152       C  
ATOM   2945  C   HIS C  30      47.286  33.452   6.790  1.00 35.10           C  
ANISOU 2945  C   HIS C  30     3458   3872   6008    487    197    177       C  
ATOM   2946  O   HIS C  30      47.554  34.198   7.724  1.00 34.35           O  
ANISOU 2946  O   HIS C  30     3169   4167   5714    451    260    273       O  
ATOM   2947  CB  HIS C  30      49.026  33.217   5.042  1.00 28.88           C  
ANISOU 2947  CB  HIS C  30     2827   3035   5110    820    230   -197       C  
ATOM   2948  CG  HIS C  30      49.374  33.341   3.594  1.00 38.89           C  
ANISOU 2948  CG  HIS C  30     4232   4240   6303    881    222   -517       C  
ATOM   2949  ND1 HIS C  30      49.196  32.308   2.700  1.00 36.84           N  
ANISOU 2949  ND1 HIS C  30     4170   3604   6223    993    161   -693       N  
ATOM   2950  CD2 HIS C  30      49.851  34.385   2.880  1.00 37.48           C  
ANISOU 2950  CD2 HIS C  30     4023   4341   5876    827    270   -690       C  
ATOM   2951  CE1 HIS C  30      49.574  32.705   1.497  1.00 42.44           C  
ANISOU 2951  CE1 HIS C  30     4943   4435   6749   1029    175   -975       C  
ATOM   2952  NE2 HIS C  30      49.977  33.957   1.577  1.00 34.75           N  
ANISOU 2952  NE2 HIS C  30     3833   3855   5516    925    244   -942       N  
ATOM   2953  N   ASP C  31      46.665  32.292   6.962  1.00 35.94           N  
ANISOU 2953  N   ASP C  31     4682   2339   6636   -293   -792    482       N  
ATOM   2954  CA  ASP C  31      46.264  31.896   8.290  1.00 32.71           C  
ANISOU 2954  CA  ASP C  31     4527   1804   6097   -440   -763    755       C  
ATOM   2955  C   ASP C  31      47.440  31.614   9.225  1.00 40.31           C  
ANISOU 2955  C   ASP C  31     5669   2669   6976   -197   -974    999       C  
ATOM   2956  O   ASP C  31      47.272  31.629  10.442  1.00 42.65           O  
ANISOU 2956  O   ASP C  31     6203   2944   7059   -316  -1011   1269       O  
ATOM   2957  CB  ASP C  31      45.299  30.703   8.206  1.00 35.68           C  
ANISOU 2957  CB  ASP C  31     5107   1948   6503   -684   -589    749       C  
ATOM   2958  CG  ASP C  31      43.934  31.130   7.718  1.00 44.22           C  
ANISOU 2958  CG  ASP C  31     5971   3228   7601   -988   -419    576       C  
ATOM   2959  OD1 ASP C  31      43.544  32.271   8.054  1.00 44.52           O  
ANISOU 2959  OD1 ASP C  31     5800   3534   7580  -1049   -366    586       O  
ATOM   2960  OD2 ASP C  31      43.270  30.355   6.996  1.00 42.52           O  
ANISOU 2960  OD2 ASP C  31     5776   2916   7463  -1158   -344    419       O  
ATOM   2961  N   ASP C  32      48.618  31.358   8.663  1.00 36.94           N  
ANISOU 2961  N   ASP C  32     5123   2227   6686    120  -1102    901       N  
ATOM   2962  CA  ASP C  32      49.806  31.110   9.485  1.00 48.07           C  
ANISOU 2962  CA  ASP C  32     6590   3622   8051    377  -1339   1107       C  
ATOM   2963  C   ASP C  32      50.519  32.420   9.887  1.00 40.01           C  
ANISOU 2963  C   ASP C  32     5340   2935   6927    458  -1523   1098       C  
ATOM   2964  O   ASP C  32      51.557  32.387  10.535  1.00 50.34           O  
ANISOU 2964  O   ASP C  32     6615   4327   8185    641  -1761   1224       O  
ATOM   2965  CB  ASP C  32      50.774  30.122   8.797  1.00 45.25           C  
ANISOU 2965  CB  ASP C  32     6175   3084   7934    663  -1337   1007       C  
ATOM   2966  CG  ASP C  32      51.462  30.725   7.563  1.00 45.66           C  
ANISOU 2966  CG  ASP C  32     5880   3331   8140    790  -1254    671       C  
ATOM   2967  OD1 ASP C  32      51.156  31.870   7.189  1.00 42.25           O  
ANISOU 2967  OD1 ASP C  32     5263   3159   7632    671  -1207    526       O  
ATOM   2968  OD2 ASP C  32      52.290  30.040   6.942  1.00 58.30           O  
ANISOU 2968  OD2 ASP C  32     7416   4798   9936    999  -1198    558       O  
ATOM   2969  N   GLY C  33      49.950  33.555   9.487  1.00 35.97           N  
ANISOU 2969  N   GLY C  33     4658   2607   6403    313  -1407    939       N  
ATOM   2970  CA  GLY C  33      50.457  34.886   9.851  1.00 40.69           C  
ANISOU 2970  CA  GLY C  33     5053   3572   6834    314  -1462    854       C  
ATOM   2971  C   GLY C  33      51.235  35.631   8.767  1.00 38.47           C  
ANISOU 2971  C   GLY C  33     4411   3441   6766    478  -1422    583       C  
ATOM   2972  O   GLY C  33      51.489  36.847   8.853  1.00 34.18           O  
ANISOU 2972  O   GLY C  33     3693   3170   6124    421  -1379    461       O  
ATOM   2973  N   ARG C  34      51.612  34.899   7.730  1.00 36.54           N  
ANISOU 2973  N   ARG C  34     4107   3095   6681    588  -1309    430       N  
ATOM   2974  CA  ARG C  34      52.367  35.458   6.614  1.00 37.12           C  
ANISOU 2974  CA  ARG C  34     3942   3334   6829    653  -1156    169       C  
ATOM   2975  C   ARG C  34      51.533  36.478   5.836  1.00 36.74           C  
ANISOU 2975  C   ARG C  34     3818   3420   6719    500   -976     31       C  
ATOM   2976  O   ARG C  34      50.337  36.281   5.645  1.00 31.11           O  
ANISOU 2976  O   ARG C  34     3198   2603   6020    385   -934     64       O  
ATOM   2977  CB  ARG C  34      52.763  34.292   5.697  1.00 43.84           C  
ANISOU 2977  CB  ARG C  34     4826   3982   7848    777  -1061     64       C  
ATOM   2978  CG  ARG C  34      53.589  34.659   4.490  1.00 60.47           C  
ANISOU 2978  CG  ARG C  34     6748   6193  10036    836   -877   -183       C  
ATOM   2979  CD  ARG C  34      54.283  33.423   3.901  1.00 53.22           C  
ANISOU 2979  CD  ARG C  34     5849   5043   9329   1016   -798   -269       C  
ATOM   2980  NE  ARG C  34      53.486  32.667   2.929  1.00 61.21           N  
ANISOU 2980  NE  ARG C  34     7041   5842  10374    946   -643   -413       N  
ATOM   2981  CZ  ARG C  34      52.756  31.589   3.225  1.00 64.41           C  
ANISOU 2981  CZ  ARG C  34     7690   5971  10814    912   -681   -322       C  
ATOM   2982  NH1 ARG C  34      52.683  31.158   4.476  1.00 55.59           N  
ANISOU 2982  NH1 ARG C  34     6680   4754   9689    959   -863    -47       N  
ATOM   2983  NH2 ARG C  34      52.084  30.944   2.274  1.00 63.28           N  
ANISOU 2983  NH2 ARG C  34     7722   5638  10684    794   -529   -510       N  
ATOM   2984  N   ARG C  35      52.166  37.559   5.385  1.00 29.42           N  
ANISOU 2984  N   ARG C  35     2740   2701   5736    488   -864   -104       N  
ATOM   2985  CA  ARG C  35      51.503  38.537   4.520  1.00 25.34           C  
ANISOU 2985  CA  ARG C  35     2189   2295   5144    376   -689   -196       C  
ATOM   2986  C   ARG C  35      52.316  38.645   3.222  1.00 35.96           C  
ANISOU 2986  C   ARG C  35     3468   3670   6525    429   -542   -367       C  
ATOM   2987  O   ARG C  35      53.529  38.593   3.272  1.00 32.02           O  
ANISOU 2987  O   ARG C  35     2880   3198   6090    511   -526   -425       O  
ATOM   2988  CB  ARG C  35      51.521  39.922   5.172  1.00 31.86           C  
ANISOU 2988  CB  ARG C  35     2965   3287   5851    296   -636   -176       C  
ATOM   2989  CG  ARG C  35      50.363  40.258   6.087  1.00 29.40           C  
ANISOU 2989  CG  ARG C  35     2666   2983   5520    199   -662    -65       C  
ATOM   2990  CD  ARG C  35      50.345  39.411   7.382  1.00 32.03           C  
ANISOU 2990  CD  ARG C  35     3111   3239   5820    191   -859     89       C  
ATOM   2991  NE  ARG C  35      49.619  40.129   8.419  1.00 30.16           N  
ANISOU 2991  NE  ARG C  35     2970   3100   5389      6   -756    130       N  
ATOM   2992  CZ  ARG C  35      49.502  39.722   9.677  1.00 34.94           C  
ANISOU 2992  CZ  ARG C  35     3788   3701   5786    -99   -841    261       C  
ATOM   2993  NH1 ARG C  35      50.014  38.552  10.060  1.00 30.65           N  
ANISOU 2993  NH1 ARG C  35     3389   3032   5226    -10  -1081    427       N  
ATOM   2994  NH2 ARG C  35      48.847  40.487  10.543  1.00 27.76           N  
ANISOU 2994  NH2 ARG C  35     2977   2888   4683   -294   -658    232       N  
ATOM   2995  N   GLU C  36      51.649  38.842   2.085  1.00 31.99           N  
ANISOU 2995  N   GLU C  36     2978   3163   6013    387   -445   -444       N  
ATOM   2996  CA  GLU C  36      52.302  39.284   0.852  1.00 33.70           C  
ANISOU 2996  CA  GLU C  36     3134   3428   6244    417   -262   -603       C  
ATOM   2997  C   GLU C  36      51.609  40.565   0.404  1.00 34.31           C  
ANISOU 2997  C   GLU C  36     3192   3630   6215    335   -196   -536       C  
ATOM   2998  O   GLU C  36      50.391  40.649   0.429  1.00 33.92           O  
ANISOU 2998  O   GLU C  36     3188   3599   6099    266   -300   -424       O  
ATOM   2999  CB  GLU C  36      52.216  38.239  -0.274  1.00 42.08           C  
ANISOU 2999  CB  GLU C  36     4276   4315   7399    477   -183   -807       C  
ATOM   3000  CG  GLU C  36      52.258  36.751   0.136  1.00 50.60           C  
ANISOU 3000  CG  GLU C  36     5454   5175   8595    537   -276   -820       C  
ATOM   3001  CD  GLU C  36      52.076  35.797  -1.070  1.00 70.15           C  
ANISOU 3001  CD  GLU C  36     8123   7445  11087    505   -140  -1088       C  
ATOM   3002  OE1 GLU C  36      53.109  35.390  -1.647  1.00 82.87           O  
ANISOU 3002  OE1 GLU C  36     9712   9018  12758    595     69  -1255       O  
ATOM   3003  OE2 GLU C  36      50.920  35.448  -1.449  1.00 47.78           O  
ANISOU 3003  OE2 GLU C  36     5481   4609   8066    302   -230  -1088       O  
ATOM   3004  N   ILE C  37      52.386  41.578   0.022  1.00 29.35           N  
ANISOU 3004  N   ILE C  37     2507   3086   5560    316    -20   -573       N  
ATOM   3005  CA  ILE C  37      51.798  42.789  -0.519  1.00 30.23           C  
ANISOU 3005  CA  ILE C  37     2633   3266   5587    252     68   -469       C  
ATOM   3006  C   ILE C  37      52.305  42.906  -1.962  1.00 32.77           C  
ANISOU 3006  C   ILE C  37     3090   3617   5742    198    280   -563       C  
ATOM   3007  O   ILE C  37      53.477  42.626  -2.245  1.00 32.93           O  
ANISOU 3007  O   ILE C  37     3028   3616   5867    225    480   -755       O  
ATOM   3008  CB  ILE C  37      52.250  44.043   0.268  1.00 32.02           C  
ANISOU 3008  CB  ILE C  37     2833   3519   5812    195    149   -406       C  
ATOM   3009  CG1 ILE C  37      51.955  43.895   1.770  1.00 38.52           C  
ANISOU 3009  CG1 ILE C  37     3718   4341   6578    172     -9   -348       C  
ATOM   3010  CG2 ILE C  37      51.558  45.282  -0.270  1.00 29.96           C  
ANISOU 3010  CG2 ILE C  37     2568   3245   5568    171    261   -263       C  
ATOM   3011  CD1 ILE C  37      52.559  45.060   2.619  1.00 37.25           C  
ANISOU 3011  CD1 ILE C  37     3526   4192   6436    107     68   -380       C  
ATOM   3012  N   TYR C  38      51.410  43.272  -2.866  1.00 30.06           N  
ANISOU 3012  N   TYR C  38     2948   3333   5139    117    232   -425       N  
ATOM   3013  CA  TYR C  38      51.747  43.425  -4.268  1.00 33.28           C  
ANISOU 3013  CA  TYR C  38     3588   3795   5264     17    417   -474       C  
ATOM   3014  C   TYR C  38      51.349  44.828  -4.633  1.00 33.58           C  
ANISOU 3014  C   TYR C  38     3728   3860   5171    -26    448   -203       C  
ATOM   3015  O   TYR C  38      50.262  45.270  -4.255  1.00 36.35           O  
ANISOU 3015  O   TYR C  38     4036   4213   5562     25    216     20       O  
ATOM   3016  CB  TYR C  38      50.952  42.429  -5.128  1.00 32.57           C  
ANISOU 3016  CB  TYR C  38     3723   3759   4895    -69    242   -534       C  
ATOM   3017  CG  TYR C  38      51.256  40.982  -4.823  1.00 33.17           C  
ANISOU 3017  CG  TYR C  38     3752   3720   5131    -27    237   -799       C  
ATOM   3018  CD1 TYR C  38      52.308  40.343  -5.445  1.00 33.53           C  
ANISOU 3018  CD1 TYR C  38     3867   3693   5178    -29    532  -1090       C  
ATOM   3019  CD2 TYR C  38      50.495  40.257  -3.900  1.00 29.29           C  
ANISOU 3019  CD2 TYR C  38     3153   3155   4822     16    -20   -754       C  
ATOM   3020  CE1 TYR C  38      52.610  39.036  -5.181  1.00 40.58           C  
ANISOU 3020  CE1 TYR C  38     4723   4409   6286     54    548  -1319       C  
ATOM   3021  CE2 TYR C  38      50.802  38.943  -3.609  1.00 36.13           C  
ANISOU 3021  CE2 TYR C  38     4021   3845   5861     65    -12   -952       C  
ATOM   3022  CZ  TYR C  38      51.865  38.339  -4.262  1.00 42.57           C  
ANISOU 3022  CZ  TYR C  38     4905   4557   6713    106    259  -1230       C  
ATOM   3023  OH  TYR C  38      52.193  37.032  -4.010  1.00 44.50           O  
ANISOU 3023  OH  TYR C  38     5156   4557   7193    198    290  -1420       O  
ATOM   3024  N   ARG C  39      52.225  45.532  -5.358  1.00 31.95           N  
ANISOU 3024  N   ARG C  39     3648   3643   4850   -116    767   -217       N  
ATOM   3025  CA  ARG C  39      51.917  46.867  -5.854  1.00 34.45           C  
ANISOU 3025  CA  ARG C  39     4145   3922   5023   -164    833     82       C  
ATOM   3026  C   ARG C  39      51.846  46.823  -7.369  1.00 35.75           C  
ANISOU 3026  C   ARG C  39     4710   4181   4691   -307    899    163       C  
ATOM   3027  O   ARG C  39      52.750  46.295  -8.025  1.00 37.55           O  
ANISOU 3027  O   ARG C  39     5056   4451   4761   -429   1200    -90       O  
ATOM   3028  CB  ARG C  39      52.987  47.883  -5.395  1.00 38.38           C  
ANISOU 3028  CB  ARG C  39     4515   4293   5777   -217   1185     35       C  
ATOM   3029  CG  ARG C  39      52.841  48.235  -3.911  1.00 41.24           C  
ANISOU 3029  CG  ARG C  39     4573   4571   6525   -120   1070     13       C  
ATOM   3030  CD  ARG C  39      51.755  49.312  -3.678  1.00 36.16           C  
ANISOU 3030  CD  ARG C  39     4005   3799   5934    -45    951    325       C  
ATOM   3031  NE  ARG C  39      52.186  50.626  -4.168  1.00 46.59           N  
ANISOU 3031  NE  ARG C  39     5503   4944   7254   -140   1247    484       N  
ATOM   3032  CZ  ARG C  39      51.689  51.236  -5.240  1.00 47.89           C  
ANISOU 3032  CZ  ARG C  39     5984   5044   7167   -139   1244    812       C  
ATOM   3033  NH1 ARG C  39      52.133  52.434  -5.599  1.00 48.00           N  
ANISOU 3033  NH1 ARG C  39     6190   4838   7209   -237   1548    978       N  
ATOM   3034  NH2 ARG C  39      50.733  50.661  -5.946  1.00 42.30           N  
ANISOU 3034  NH2 ARG C  39     5413   4484   6175    -58    914    991       N  
ATOM   3035  N   PHE C  40      50.770  47.366  -7.930  1.00 34.22           N  
ANISOU 3035  N   PHE C  40     4725   4029   4247   -292    619    514       N  
ATOM   3036  CA  PHE C  40      50.585  47.295  -9.386  1.00 40.75           C  
ANISOU 3036  CA  PHE C  40     5998   4995   4492   -455    583    633       C  
ATOM   3037  C   PHE C  40      50.592  48.628 -10.083  1.00 53.88           C  
ANISOU 3037  C   PHE C  40     7975   6572   5927   -501    692   1034       C  
ATOM   3038  O   PHE C  40      50.236  49.649  -9.498  1.00 55.54           O  
ANISOU 3038  O   PHE C  40     8051   6603   6449   -350    636   1313       O  
ATOM   3039  CB  PHE C  40      49.278  46.592  -9.742  1.00 40.60           C  
ANISOU 3039  CB  PHE C  40     6028   5158   4240   -447     55    725       C  
ATOM   3040  CG  PHE C  40      49.198  45.189  -9.224  1.00 46.75           C  
ANISOU 3040  CG  PHE C  40     6596   5981   5184   -455    -37    347       C  
ATOM   3041  CD1 PHE C  40      49.806  44.153  -9.915  1.00 54.86           C  
ANISOU 3041  CD1 PHE C  40     7842   7068   5936   -626    159    -16       C  
ATOM   3042  CD2 PHE C  40      48.529  44.906  -8.052  1.00 48.94           C  
ANISOU 3042  CD2 PHE C  40     6493   6203   5897   -302   -268    348       C  
ATOM   3043  CE1 PHE C  40      49.746  42.860  -9.441  1.00 55.87           C  
ANISOU 3043  CE1 PHE C  40     7809   7155   6263   -617     97   -345       C  
ATOM   3044  CE2 PHE C  40      48.460  43.605  -7.575  1.00 47.42           C  
ANISOU 3044  CE2 PHE C  40     6164   6004   5851   -325   -335     45       C  
ATOM   3045  CZ  PHE C  40      49.077  42.585  -8.273  1.00 44.72           C  
ANISOU 3045  CZ  PHE C  40     6042   5676   5273   -470   -164   -290       C  
ATOM   3046  N   ASN C  41      50.990  48.579 -11.350  1.00 60.85           N  
ANISOU 3046  N   ASN C  41     9316   7559   6244   -723    874   1053       N  
ATOM   3047  CA  ASN C  41      50.796  49.664 -12.288  1.00 71.10           C  
ANISOU 3047  CA  ASN C  41    11064   8812   7138   -802    880   1517       C  
ATOM   3048  C   ASN C  41      49.316  50.022 -12.360  1.00 73.76           C  
ANISOU 3048  C   ASN C  41    11393   9204   7430   -606    229   1974       C  
ATOM   3049  O   ASN C  41      48.490  49.202 -12.765  1.00 71.73           O  
ANISOU 3049  O   ASN C  41    11166   9198   6889   -635   -222   1943       O  
ATOM   3050  CB  ASN C  41      51.290  49.241 -13.667  1.00 71.29           C  
ANISOU 3050  CB  ASN C  41    11635   9019   6432  -1114   1113   1414       C  
ATOM   3051  CG  ASN C  41      51.425  50.408 -14.622  1.00 83.35           C  
ANISOU 3051  CG  ASN C  41    13706  10460   7503  -1256   1277   1887       C  
ATOM   3052  OD1 ASN C  41      50.476  50.770 -15.320  1.00 90.69           O  
ANISOU 3052  OD1 ASN C  41    14971  11488   7999  -1231    803   2350       O  
ATOM   3053  ND2 ASN C  41      52.613  51.001 -14.665  1.00 89.43           N  
ANISOU 3053  ND2 ASN C  41    14561  11041   8376  -1418   1940   1793       N  
ATOM   3054  N   ASP C  42      48.990  51.244 -11.957  1.00 71.31           N  
ANISOU 3054  N   ASP C  42    11009   8639   7449   -411    194   2374       N  
ATOM   3055  CA  ASP C  42      47.613  51.724 -11.954  1.00 80.73           C  
ANISOU 3055  CA  ASP C  42    12100   9825   8747   -155   -384   2835       C  
ATOM   3056  C   ASP C  42      46.937  51.607 -13.320  1.00 94.01           C  
ANISOU 3056  C   ASP C  42    14228  11769   9722   -257   -847   3191       C  
ATOM   3057  O   ASP C  42      45.718  51.455 -13.409  1.00101.19           O  
ANISOU 3057  O   ASP C  42    14953  12838  10656    -97  -1465   3428       O  
ATOM   3058  CB  ASP C  42      47.586  53.177 -11.490  1.00 93.25           C  
ANISOU 3058  CB  ASP C  42    13652  11007  10773     54   -210   3209       C  
ATOM   3059  CG  ASP C  42      48.696  54.001 -12.102  1.00101.44           C  
ANISOU 3059  CG  ASP C  42    15159  11827  11558   -161    327   3334       C  
ATOM   3060  OD1 ASP C  42      49.843  53.899 -11.614  1.00100.48           O  
ANISOU 3060  OD1 ASP C  42    14928  11618  11629   -335    865   2923       O  
ATOM   3061  OD2 ASP C  42      48.422  54.746 -13.067  1.00109.69           O  
ANISOU 3061  OD2 ASP C  42    16670  12788  12218   -167    202   3859       O  
ATOM   3062  N   ARG C  43      47.741  51.673 -14.376  1.00 94.23           N  
ANISOU 3062  N   ARG C  43    14833  11859   9110   -550   -541   3212       N  
ATOM   3063  CA  ARG C  43      47.235  51.632 -15.741  1.00104.21           C  
ANISOU 3063  CA  ARG C  43    16651  13386   9559   -714   -942   3560       C  
ATOM   3064  C   ARG C  43      47.138  50.206 -16.280  1.00100.02           C  
ANISOU 3064  C   ARG C  43    16226  13255   8524   -989  -1120   3100       C  
ATOM   3065  O   ARG C  43      46.427  49.954 -17.252  1.00105.92           O  
ANISOU 3065  O   ARG C  43    17196  14293   8754  -1069  -1582   3230       O  
ATOM   3066  CB  ARG C  43      48.144  52.455 -16.655  1.00116.65           C  
ANISOU 3066  CB  ARG C  43    18773  14836  10715   -900   -431   3749       C  
ATOM   3067  CG  ARG C  43      48.494  53.834 -16.120  1.00123.93           C  
ANISOU 3067  CG  ARG C  43    19600  15305  12181   -704    -85   4080       C  
ATOM   3068  CD  ARG C  43      47.416  54.857 -16.438  1.00132.10           C  
ANISOU 3068  CD  ARG C  43    20578  16247  13366   -327   -547   4683       C  
ATOM   3069  NE  ARG C  43      47.661  56.129 -15.765  1.00133.83           N  
ANISOU 3069  NE  ARG C  43    20637  15988  14224   -126   -214   4951       N  
ATOM   3070  CZ  ARG C  43      47.277  57.312 -16.237  1.00143.93           C  
ANISOU 3070  CZ  ARG C  43    22039  17061  15586    107   -265   5488       C  
ATOM   3071  NH1 ARG C  43      46.635  57.393 -17.396  1.00151.50           N  
ANISOU 3071  NH1 ARG C  43    23329  18255  15978    203   -649   5822       N  
ATOM   3072  NH2 ARG C  43      47.543  58.418 -15.554  1.00144.01           N  
ANISOU 3072  NH2 ARG C  43    21801  16636  16279     74    -80   5620       N  
ATOM   3073  N   ASP C  44      47.847  49.274 -15.647  1.00 82.91           N  
ANISOU 3073  N   ASP C  44    13774  11075   6652  -1072   -712   2472       N  
ATOM   3074  CA  ASP C  44      47.946  47.916 -16.170  1.00 87.47           C  
ANISOU 3074  CA  ASP C  44    14509  11927   6796  -1350   -727   1972       C  
ATOM   3075  C   ASP C  44      48.103  46.899 -15.051  1.00 80.15           C  
ANISOU 3075  C   ASP C  44    13021  10928   6505  -1244   -604   1442       C  
ATOM   3076  O   ASP C  44      49.159  46.815 -14.428  1.00 80.32           O  
ANISOU 3076  O   ASP C  44    12851  10750   6917  -1209    -44   1132       O  
ATOM   3077  CB  ASP C  44      49.115  47.811 -17.158  1.00 98.89           C  
ANISOU 3077  CB  ASP C  44    16548  13407   7620  -1700    -99   1742       C  
ATOM   3078  CG  ASP C  44      49.399  46.379 -17.586  1.00107.47           C  
ANISOU 3078  CG  ASP C  44    17775  14684   8377  -1971     55   1109       C  
ATOM   3079  OD1 ASP C  44      48.461  45.552 -17.610  1.00109.17           O  
ANISOU 3079  OD1 ASP C  44    17879  15095   8505  -2000   -492    984       O  
ATOM   3080  OD2 ASP C  44      50.571  46.083 -17.908  1.00112.91           O  
ANISOU 3080  OD2 ASP C  44    18670  15301   8931  -2164    759    714       O  
ATOM   3081  N   PRO C  45      47.050  46.104 -14.813  1.00 82.67           N  
ANISOU 3081  N   PRO C  45    13076  11412   6921  -1213  -1148   1352       N  
ATOM   3082  CA  PRO C  45      46.956  45.197 -13.661  1.00 76.36           C  
ANISOU 3082  CA  PRO C  45    11752  10516   6746  -1092  -1125    968       C  
ATOM   3083  C   PRO C  45      47.851  43.967 -13.791  1.00 76.67           C  
ANISOU 3083  C   PRO C  45    11913  10525   6692  -1288   -698    361       C  
ATOM   3084  O   PRO C  45      48.051  43.248 -12.813  1.00 74.42           O  
ANISOU 3084  O   PRO C  45    11250  10089   6936  -1171   -576     62       O  
ATOM   3085  CB  PRO C  45      45.480  44.786 -13.667  1.00 77.66           C  
ANISOU 3085  CB  PRO C  45    11697  10892   6917  -1087  -1837   1104       C  
ATOM   3086  CG  PRO C  45      45.082  44.867 -15.098  1.00 80.68           C  
ANISOU 3086  CG  PRO C  45    12607  11569   6481  -1344  -2189   1293       C  
ATOM   3087  CD  PRO C  45      45.878  45.999 -15.700  1.00 82.23           C  
ANISOU 3087  CD  PRO C  45    13238  11668   6338  -1336  -1839   1622       C  
ATOM   3088  N   ASP C  46      48.386  43.741 -14.984  1.00 74.91           N  
ANISOU 3088  N   ASP C  46    12235  10424   5803  -1577   -455    193       N  
ATOM   3089  CA  ASP C  46      49.279  42.618 -15.231  1.00 78.88           C  
ANISOU 3089  CA  ASP C  46    12884  10860   6228  -1752     32   -410       C  
ATOM   3090  C   ASP C  46      50.735  42.978 -14.935  1.00 74.92           C  
ANISOU 3090  C   ASP C  46    12293  10137   6035  -1665    762   -577       C  
ATOM   3091  O   ASP C  46      51.620  42.131 -15.031  1.00 76.95           O  
ANISOU 3091  O   ASP C  46    12565  10288   6383  -1733   1240  -1072       O  
ATOM   3092  CB  ASP C  46      49.147  42.152 -16.684  1.00 84.64           C  
ANISOU 3092  CB  ASP C  46    14267  11833   6060  -2150      4   -589       C  
ATOM   3093  CG  ASP C  46      47.742  41.696 -17.024  1.00101.18           C  
ANISOU 3093  CG  ASP C  46    16415  14188   7840  -2297   -762   -490       C  
ATOM   3094  OD1 ASP C  46      46.996  41.335 -16.089  1.00101.56           O  
ANISOU 3094  OD1 ASP C  46    15955  14177   8457  -2118  -1131   -469       O  
ATOM   3095  OD2 ASP C  46      47.385  41.692 -18.223  1.00113.17           O  
ANISOU 3095  OD2 ASP C  46    18424  15964   8610  -2583   -983   -436       O  
ATOM   3096  N   GLU C  47      50.980  44.233 -14.575  1.00 64.01           N  
ANISOU 3096  N   GLU C  47    10791   8667   4863  -1517    854   -180       N  
ATOM   3097  CA  GLU C  47      52.342  44.713 -14.387  1.00 56.90           C  
ANISOU 3097  CA  GLU C  47     9802   7592   4228  -1503   1527   -317       C  
ATOM   3098  C   GLU C  47      52.683  44.954 -12.923  1.00 55.55           C  
ANISOU 3098  C   GLU C  47     9005   7215   4886  -1208   1560   -325       C  
ATOM   3099  O   GLU C  47      52.237  45.933 -12.327  1.00 55.98           O  
ANISOU 3099  O   GLU C  47     8889   7199   5181  -1057   1334     60       O  
ATOM   3100  CB  GLU C  47      52.566  46.000 -15.171  1.00 65.19           C  
ANISOU 3100  CB  GLU C  47    11269   8656   4844  -1650   1725     93       C  
ATOM   3101  CG  GLU C  47      53.942  46.623 -14.947  1.00 71.05           C  
ANISOU 3101  CG  GLU C  47    11873   9209   5913  -1686   2435    -31       C  
ATOM   3102  CD  GLU C  47      54.257  47.714 -15.955  1.00 84.48           C  
ANISOU 3102  CD  GLU C  47    14127  10907   7067  -1936   2757    316       C  
ATOM   3103  OE1 GLU C  47      54.289  48.900 -15.558  1.00 82.09           O  
ANISOU 3103  OE1 GLU C  47    13745  10422   7024  -1850   2778    706       O  
ATOM   3104  OE2 GLU C  47      54.474  47.381 -17.141  1.00 95.78           O  
ANISOU 3104  OE2 GLU C  47    16093  12489   7812  -2230   3003    189       O  
ATOM   3105  N   LEU C  48      53.481  44.067 -12.342  1.00 48.87           N  
ANISOU 3105  N   LEU C  48     7833   6262   4473  -1123   1840   -763       N  
ATOM   3106  CA  LEU C  48      53.820  44.185 -10.922  1.00 43.86           C  
ANISOU 3106  CA  LEU C  48     6634   5474   4556   -868   1806   -781       C  
ATOM   3107  C   LEU C  48      54.956  45.198 -10.783  1.00 47.46           C  
ANISOU 3107  C   LEU C  48     6956   5838   5240   -905   2282   -755       C  
ATOM   3108  O   LEU C  48      55.973  45.108 -11.492  1.00 48.16           O  
ANISOU 3108  O   LEU C  48     7160   5925   5212  -1066   2819  -1007       O  
ATOM   3109  CB  LEU C  48      54.241  42.820 -10.387  1.00 46.71           C  
ANISOU 3109  CB  LEU C  48     6718   5743   5285   -746   1862  -1203       C  
ATOM   3110  CG  LEU C  48      54.512  42.624  -8.902  1.00 43.34           C  
ANISOU 3110  CG  LEU C  48     5764   5186   5518   -489   1724  -1231       C  
ATOM   3111  CD1 LEU C  48      53.260  42.899  -8.090  1.00 39.56           C  
ANISOU 3111  CD1 LEU C  48     5189   4731   5111   -389   1197   -909       C  
ATOM   3112  CD2 LEU C  48      55.012  41.189  -8.687  1.00 54.89           C  
ANISOU 3112  CD2 LEU C  48     7073   6520   7263   -376   1825  -1623       C  
ATOM   3113  N   LEU C  49      54.772  46.171  -9.902  1.00 47.61           N  
ANISOU 3113  N   LEU C  49     6738   5769   5583   -791   2129   -480       N  
ATOM   3114  CA  LEU C  49      55.804  47.175  -9.646  1.00 52.77           C  
ANISOU 3114  CA  LEU C  49     7229   6311   6509   -867   2549   -475       C  
ATOM   3115  C   LEU C  49      56.755  46.700  -8.554  1.00 50.44           C  
ANISOU 3115  C   LEU C  49     6373   5968   6825   -741   2659   -811       C  
ATOM   3116  O   LEU C  49      57.962  46.894  -8.643  1.00 44.72           O  
ANISOU 3116  O   LEU C  49     5448   5218   6327   -846   3113  -1038       O  
ATOM   3117  CB  LEU C  49      55.176  48.504  -9.222  1.00 47.44           C  
ANISOU 3117  CB  LEU C  49     6602   5518   5907   -828   2361    -52       C  
ATOM   3118  CG  LEU C  49      54.303  49.235 -10.241  1.00 48.38           C  
ANISOU 3118  CG  LEU C  49     7242   5640   5502   -907   2219    391       C  
ATOM   3119  CD1 LEU C  49      53.755  50.540  -9.625  1.00 48.71           C  
ANISOU 3119  CD1 LEU C  49     7234   5469   5803   -793   2072    778       C  
ATOM   3120  CD2 LEU C  49      55.085  49.508 -11.530  1.00 56.43           C  
ANISOU 3120  CD2 LEU C  49     8700   6685   6056  -1199   2722    380       C  
ATOM   3121  N   SER C  50      56.204  46.076  -7.519  1.00 45.09           N  
ANISOU 3121  N   SER C  50     5431   5287   6414   -526   2232   -827       N  
ATOM   3122  CA  SER C  50      57.003  45.663  -6.374  1.00 43.22           C  
ANISOU 3122  CA  SER C  50     4694   5017   6712   -387   2213  -1058       C  
ATOM   3123  C   SER C  50      56.200  44.700  -5.532  1.00 41.37           C  
ANISOU 3123  C   SER C  50     4354   4777   6586   -184   1748  -1040       C  
ATOM   3124  O   SER C  50      54.977  44.676  -5.627  1.00 34.84           O  
ANISOU 3124  O   SER C  50     3756   3971   5509   -172   1445   -825       O  
ATOM   3125  CB  SER C  50      57.398  46.879  -5.521  1.00 36.51           C  
ANISOU 3125  CB  SER C  50     3607   4112   6152   -443   2257   -956       C  
ATOM   3126  OG  SER C  50      56.274  47.583  -5.032  1.00 41.34           O  
ANISOU 3126  OG  SER C  50     4363   4669   6673   -402   1950   -648       O  
ATOM   3127  N   ASN C  51      56.870  43.906  -4.704  1.00 40.81           N  
ANISOU 3127  N   ASN C  51     3927   4674   6904    -30   1681  -1243       N  
ATOM   3128  CA  ASN C  51      56.119  43.015  -3.808  1.00 33.62           C  
ANISOU 3128  CA  ASN C  51     2962   3722   6089    138   1260  -1181       C  
ATOM   3129  C   ASN C  51      57.008  42.652  -2.639  1.00 44.23           C  
ANISOU 3129  C   ASN C  51     4091   5054   7662    216   1015  -1166       C  
ATOM   3130  O   ASN C  51      58.237  42.739  -2.731  1.00 42.52           O  
ANISOU 3130  O   ASN C  51     3730   4848   7575    189   1155  -1276       O  
ATOM   3131  CB  ASN C  51      55.671  41.744  -4.548  1.00 32.14           C  
ANISOU 3131  CB  ASN C  51     3007   3476   5727    168   1233  -1313       C  
ATOM   3132  CG  ASN C  51      56.796  40.761  -4.753  1.00 48.97           C  
ANISOU 3132  CG  ASN C  51     4989   5515   8104    267   1438  -1589       C  
ATOM   3133  OD1 ASN C  51      56.885  39.749  -4.061  1.00 62.55           O  
ANISOU 3133  OD1 ASN C  51     6622   7137  10006    406   1187  -1567       O  
ATOM   3134  ND2 ASN C  51      57.661  41.042  -5.718  1.00 46.41           N  
ANISOU 3134  ND2 ASN C  51     4709   5227   7696    149   1837  -1745       N  
ATOM   3135  N   ILE C  52      56.399  42.274  -1.526  1.00 35.23           N  
ANISOU 3135  N   ILE C  52     2956   3897   6530    290    660  -1021       N  
ATOM   3136  CA  ILE C  52      57.191  42.010  -0.332  1.00 39.57           C  
ANISOU 3136  CA  ILE C  52     3378   4460   7195    343    442   -983       C  
ATOM   3137  C   ILE C  52      56.467  40.946   0.491  1.00 38.24           C  
ANISOU 3137  C   ILE C  52     3296   4227   7008    443    160   -872       C  
ATOM   3138  O   ILE C  52      55.255  40.877   0.463  1.00 35.27           O  
ANISOU 3138  O   ILE C  52     3061   3824   6515    417     87   -786       O  
ATOM   3139  CB  ILE C  52      57.414  43.330   0.465  1.00 38.20           C  
ANISOU 3139  CB  ILE C  52     3165   4365   6985    231    403   -915       C  
ATOM   3140  CG1 ILE C  52      58.390  43.130   1.631  1.00 46.65           C  
ANISOU 3140  CG1 ILE C  52     4061   5488   8177    282    205   -931       C  
ATOM   3141  CG2 ILE C  52      56.092  43.950   0.897  1.00 40.79           C  
ANISOU 3141  CG2 ILE C  52     3659   4690   7150    178    309   -759       C  
ATOM   3142  CD1 ILE C  52      58.674  44.428   2.411  1.00 46.87           C  
ANISOU 3142  CD1 ILE C  52     4031   5594   8183    150    190   -938       C  
ATOM   3143  N   SER C  53      57.227  40.091   1.162  1.00 35.20           N  
ANISOU 3143  N   SER C  53     2805   3801   6768    562     18   -871       N  
ATOM   3144  CA  SER C  53      56.674  39.057   2.027  1.00 34.23           C  
ANISOU 3144  CA  SER C  53     2772   3586   6648    654   -226   -741       C  
ATOM   3145  C   SER C  53      57.096  39.372   3.438  1.00 38.78           C  
ANISOU 3145  C   SER C  53     3271   4251   7213    666   -452   -622       C  
ATOM   3146  O   SER C  53      58.248  39.736   3.682  1.00 37.69           O  
ANISOU 3146  O   SER C  53     2927   4200   7192    696   -465   -680       O  
ATOM   3147  CB  SER C  53      57.222  37.682   1.639  1.00 49.84           C  
ANISOU 3147  CB  SER C  53     4702   5399   8835    826   -201   -817       C  
ATOM   3148  OG  SER C  53      56.912  37.372   0.294  1.00 60.92           O  
ANISOU 3148  OG  SER C  53     6188   6718  10241    807     46   -992       O  
ATOM   3149  N   LEU C  54      56.166  39.223   4.368  1.00 34.56           N  
ANISOU 3149  N   LEU C  54     2880   3699   6552    635   -629   -471       N  
ATOM   3150  CA  LEU C  54      56.386  39.604   5.755  1.00 39.21           C  
ANISOU 3150  CA  LEU C  54     3422   4392   7083    620   -851   -367       C  
ATOM   3151  C   LEU C  54      55.878  38.485   6.653  1.00 38.95           C  
ANISOU 3151  C   LEU C  54     3516   4239   7044    708  -1097   -179       C  
ATOM   3152  O   LEU C  54      54.862  37.857   6.343  1.00 43.04           O  
ANISOU 3152  O   LEU C  54     4202   4608   7543    690  -1052   -127       O  
ATOM   3153  CB  LEU C  54      55.598  40.884   6.061  1.00 35.72           C  
ANISOU 3153  CB  LEU C  54     3050   4050   6471    443   -771   -375       C  
ATOM   3154  CG  LEU C  54      55.965  42.126   5.242  1.00 39.25           C  
ANISOU 3154  CG  LEU C  54     3433   4566   6915    343   -525   -513       C  
ATOM   3155  CD1 LEU C  54      54.940  43.203   5.466  1.00 37.85           C  
ANISOU 3155  CD1 LEU C  54     3362   4406   6613    211   -424   -491       C  
ATOM   3156  CD2 LEU C  54      57.361  42.601   5.621  1.00 36.91           C  
ANISOU 3156  CD2 LEU C  54     2908   4389   6729    335   -576   -608       C  
ATOM   3157  N   ASP C  55      56.573  38.207   7.747  1.00 34.30           N  
ANISOU 3157  N   ASP C  55     2855   3706   6471    793  -1378    -58       N  
ATOM   3158  CA  ASP C  55      55.987  37.279   8.718  1.00 36.94           C  
ANISOU 3158  CA  ASP C  55     3391   3911   6734    846  -1637    188       C  
ATOM   3159  C   ASP C  55      55.058  38.079   9.627  1.00 42.05           C  
ANISOU 3159  C   ASP C  55     4168   4662   7146    650  -1743    271       C  
ATOM   3160  O   ASP C  55      54.974  39.287   9.473  1.00 34.18           O  
ANISOU 3160  O   ASP C  55     3064   3828   6095    509  -1601    109       O  
ATOM   3161  CB  ASP C  55      57.043  36.473   9.490  1.00 39.46           C  
ANISOU 3161  CB  ASP C  55     3637   4221   7135   1040  -1941    353       C  
ATOM   3162  CG  ASP C  55      57.974  37.328  10.359  1.00 50.17           C  
ANISOU 3162  CG  ASP C  55     4792   5871   8399    992  -2182    345       C  
ATOM   3163  OD1 ASP C  55      57.589  38.398  10.869  1.00 46.13           O  
ANISOU 3163  OD1 ASP C  55     4310   5543   7672    776  -2214    287       O  
ATOM   3164  OD2 ASP C  55      59.116  36.881  10.576  1.00 54.70           O  
ANISOU 3164  OD2 ASP C  55     5160   6494   9128   1170  -2363    396       O  
ATOM   3165  N   ASP C  56      54.380  37.425  10.569  1.00 34.20           N  
ANISOU 3165  N   ASP C  56     4505   2193   6296    128  -2124    697       N  
ATOM   3166  CA  ASP C  56      53.381  38.118  11.389  1.00 42.02           C  
ANISOU 3166  CA  ASP C  56     5611   3345   7009   -102  -2023    929       C  
ATOM   3167  C   ASP C  56      53.965  39.289  12.191  1.00 43.65           C  
ANISOU 3167  C   ASP C  56     5772   3806   7006   -120  -1993    992       C  
ATOM   3168  O   ASP C  56      53.386  40.374  12.233  1.00 39.08           O  
ANISOU 3168  O   ASP C  56     5192   3452   6204   -250  -1795    981       O  
ATOM   3169  CB  ASP C  56      52.676  37.125  12.338  1.00 42.50           C  
ANISOU 3169  CB  ASP C  56     5819   3321   7008   -241  -2086   1156       C  
ATOM   3170  CG  ASP C  56      51.747  37.825  13.302  1.00 41.59           C  
ANISOU 3170  CG  ASP C  56     5801   3390   6610   -464  -1946   1363       C  
ATOM   3171  OD1 ASP C  56      50.715  38.341  12.840  1.00 37.76           O  
ANISOU 3171  OD1 ASP C  56     5288   2990   6070   -583  -1765   1320       O  
ATOM   3172  OD2 ASP C  56      52.052  37.881  14.508  1.00 43.33           O  
ANISOU 3172  OD2 ASP C  56     6123   3676   6663   -516  -2017   1546       O  
ATOM   3173  N  ASER C  57      55.126  39.079  12.803  0.32 41.80           N  
ANISOU 3173  N  ASER C  57     5483   3542   6856     17  -2201   1025       N  
ATOM   3174  N  BSER C  57      55.106  39.055  12.832  0.68 40.56           N  
ANISOU 3174  N  BSER C  57     5333   3379   6697     14  -2205   1034       N  
ATOM   3175  CA ASER C  57      55.733  40.122  13.635  0.32 41.68           C  
ANISOU 3175  CA ASER C  57     5425   3775   6639    -16  -2209   1062       C  
ATOM   3176  CA BSER C  57      55.760  40.115  13.607  0.68 42.28           C  
ANISOU 3176  CA BSER C  57     5494   3848   6722    -10  -2210   1055       C  
ATOM   3177  C  ASER C  57      56.308  41.298  12.834  0.32 38.58           C  
ANISOU 3177  C  ASER C  57     4824   3616   6220     16  -2000    788       C  
ATOM   3178  C  BSER C  57      56.048  41.316  12.715  0.68 38.92           C  
ANISOU 3178  C  BSER C  57     4891   3656   6242    -10  -1958    791       C  
ATOM   3179  O  ASER C  57      56.407  42.411  13.349  0.32 35.50           O  
ANISOU 3179  O  ASER C  57     4426   3441   5621    -81  -1922    796       O  
ATOM   3180  O  BSER C  57      55.675  42.453  13.027  0.68 30.90           O  
ANISOU 3180  O  BSER C  57     3907   2849   4986   -146  -1806    806       O  
ATOM   3181  CB ASER C  57      56.792  39.523  14.568  0.32 44.50           C  
ANISOU 3181  CB ASER C  57     5777   4050   7082    100  -2510   1157       C  
ATOM   3182  CB BSER C  57      57.058  39.589  14.238  0.68 44.30           C  
ANISOU 3182  CB BSER C  57     5670   4023   7139    159  -2508   1075       C  
ATOM   3183  OG ASER C  57      57.761  38.801  13.836  0.32 44.33           O  
ANISOU 3183  OG ASER C  57     5559   3876   7408    328  -2614    948       O  
ATOM   3184  OG BSER C  57      57.665  40.552  15.091  0.68 43.50           O  
ANISOU 3184  OG BSER C  57     5533   4143   6853    119  -2578   1111       O  
ATOM   3185  N   GLU C  58      56.692  41.054  11.583  1.00 31.91           N  
ANISOU 3185  N   GLU C  58     3834   2717   5573    134  -1902    543       N  
ATOM   3186  CA  GLU C  58      57.132  42.133  10.692  1.00 36.83           C  
ANISOU 3186  CA  GLU C  58     4307   3548   6138    116  -1660    307       C  
ATOM   3187  C   GLU C  58      55.933  42.927  10.213  1.00 35.82           C  
ANISOU 3187  C   GLU C  58     4315   3518   5779    -50  -1443    328       C  
ATOM   3188  O   GLU C  58      55.958  44.153  10.189  1.00 35.01           O  
ANISOU 3188  O   GLU C  58     4195   3598   5510   -145  -1299    291       O  
ATOM   3189  CB  GLU C  58      57.897  41.567   9.490  1.00 39.32           C  
ANISOU 3189  CB  GLU C  58     4454   3790   6696    275  -1589     29       C  
ATOM   3190  CG  GLU C  58      59.234  40.891   9.850  1.00 39.37           C  
ANISOU 3190  CG  GLU C  58     4236   3709   7013    484  -1794    -62       C  
ATOM   3191  CD  GLU C  58      59.837  40.121   8.675  1.00 57.03           C  
ANISOU 3191  CD  GLU C  58     6311   5836   9524    663  -1702   -370       C  
ATOM   3192  OE1 GLU C  58      59.073  39.504   7.887  1.00 48.47           O  
ANISOU 3192  OE1 GLU C  58     5376   4610   8430    662  -1630   -432       O  
ATOM   3193  OE2 GLU C  58      61.081  40.137   8.533  1.00 58.50           O  
ANISOU 3193  OE2 GLU C  58     6204   6082   9943    802  -1696   -578       O  
ATOM   3194  N   ALA C  59      54.868  42.220   9.828  1.00 31.58           N  
ANISOU 3194  N   ALA C  59     3905   2832   5261    -83  -1446    382       N  
ATOM   3195  CA  ALA C  59      53.665  42.886   9.377  1.00 25.65           C  
ANISOU 3195  CA  ALA C  59     3250   2152   4344   -217  -1295    398       C  
ATOM   3196  C   ALA C  59      53.107  43.827  10.440  1.00 27.22           C  
ANISOU 3196  C   ALA C  59     3502   2493   4347   -347  -1248    556       C  
ATOM   3197  O   ALA C  59      52.632  44.931  10.142  1.00 29.09           O  
ANISOU 3197  O   ALA C  59     3749   2853   4450   -419  -1107    509       O  
ATOM   3198  CB  ALA C  59      52.592  41.827   9.025  1.00 28.84           C  
ANISOU 3198  CB  ALA C  59     3750   2355   4851   -248  -1363    448       C  
ATOM   3199  N   ARG C  60      53.082  43.352  11.679  1.00 31.34           N  
ANISOU 3199  N   ARG C  60     4087   2978   4844   -380  -1372    745       N  
ATOM   3200  CA  ARG C  60      52.487  44.146  12.749  1.00 33.91           C  
ANISOU 3200  CA  ARG C  60     4488   3445   4951   -514  -1299    870       C  
ATOM   3201  C   ARG C  60      53.378  45.324  13.124  1.00 37.87           C  
ANISOU 3201  C   ARG C  60     4933   4126   5332   -507  -1270    782       C  
ATOM   3202  O   ARG C  60      52.890  46.377  13.550  1.00 31.63           O  
ANISOU 3202  O   ARG C  60     4179   3466   4372   -599  -1146    772       O  
ATOM   3203  CB  ARG C  60      52.171  43.280  13.978  1.00 31.66           C  
ANISOU 3203  CB  ARG C  60     4343   3081   4606   -592  -1419   1113       C  
ATOM   3204  CG  ARG C  60      50.873  42.453  13.841  1.00 31.84           C  
ANISOU 3204  CG  ARG C  60     4433   2963   4700   -702  -1366   1226       C  
ATOM   3205  CD  ARG C  60      50.548  41.681  15.141  1.00 32.18           C  
ANISOU 3205  CD  ARG C  60     4654   2938   4634   -838  -1443   1505       C  
ATOM   3206  NE  ARG C  60      51.496  40.575  15.420  1.00 38.32           N  
ANISOU 3206  NE  ARG C  60     5506   3523   5532   -729  -1716   1611       N  
ATOM   3207  CZ  ARG C  60      52.530  40.654  16.260  1.00 40.71           C  
ANISOU 3207  CZ  ARG C  60     5862   3876   5729   -662  -1895   1677       C  
ATOM   3208  NH1 ARG C  60      52.775  41.776  16.923  1.00 40.41           N  
ANISOU 3208  NH1 ARG C  60     5846   4065   5442   -714  -1845   1671       N  
ATOM   3209  NH2 ARG C  60      53.342  39.619  16.427  1.00 39.86           N  
ANISOU 3209  NH2 ARG C  60     5766   3604   5776   -536  -2122   1702       N  
ATOM   3210  N   GLN C  61      54.687  45.159  12.990  1.00 31.23           N  
ANISOU 3210  N   GLN C  61     3980   3280   4605   -398  -1389    699       N  
ATOM   3211  CA AGLN C  61      55.601  46.283  13.245  0.50 32.56           C  
ANISOU 3211  CA AGLN C  61     4056   3609   4704   -416  -1367    591       C  
ATOM   3212  CA BGLN C  61      55.611  46.278  13.234  0.50 32.55           C  
ANISOU 3212  CA BGLN C  61     4054   3608   4706   -415  -1368    590       C  
ATOM   3213  C   GLN C  61      55.385  47.389  12.209  1.00 33.66           C  
ANISOU 3213  C   GLN C  61     4156   3822   4810   -467  -1142    438       C  
ATOM   3214  O   GLN C  61      55.272  48.581  12.551  1.00 35.51           O  
ANISOU 3214  O   GLN C  61     4424   4161   4909   -558  -1057    407       O  
ATOM   3215  CB AGLN C  61      57.056  45.817  13.233  0.50 34.99           C  
ANISOU 3215  CB AGLN C  61     4186   3897   5210   -288  -1541    509       C  
ATOM   3216  CB BGLN C  61      57.054  45.807  13.140  0.50 35.28           C  
ANISOU 3216  CB BGLN C  61     4217   3930   5257   -285  -1530    499       C  
ATOM   3217  CG AGLN C  61      57.509  45.129  14.516  0.50 34.60           C  
ANISOU 3217  CG AGLN C  61     4192   3801   5151   -246  -1839    676       C  
ATOM   3218  CG BGLN C  61      57.566  45.017  14.328  0.50 36.01           C  
ANISOU 3218  CG BGLN C  61     4346   3961   5374   -224  -1834    655       C  
ATOM   3219  CD AGLN C  61      58.880  44.481  14.384  0.50 39.71           C  
ANISOU 3219  CD AGLN C  61     4617   4380   6090    -68  -2058    581       C  
ATOM   3220  CD BGLN C  61      58.977  44.523  14.090  0.50 39.41           C  
ANISOU 3220  CD BGLN C  61     4532   4346   6097    -53  -2014    527       C  
ATOM   3221  OE1AGLN C  61      59.896  45.165  14.253  0.50 34.35           O  
ANISOU 3221  OE1AGLN C  61     3723   3825   5504    -52  -2055    413       O  
ATOM   3222  OE1BGLN C  61      59.371  44.302  12.944  0.50 41.02           O  
ANISOU 3222  OE1BGLN C  61     4563   4512   6511     38  -1884    336       O  
ATOM   3223  NE2AGLN C  61      58.912  43.153  14.416  0.50 37.50           N  
ANISOU 3223  NE2AGLN C  61     4369   3887   5993     67  -2252    676       N  
ATOM   3224  NE2BGLN C  61      59.753  44.361  15.164  0.50 36.80           N  
ANISOU 3224  NE2BGLN C  61     4175   4027   5779     -7  -2316    613       N  
ATOM   3225  N   ILE C  62      55.330  47.000  10.943  1.00 29.49           N  
ANISOU 3225  N   ILE C  62     3589   3221   4395   -412  -1061    341       N  
ATOM   3226  CA  ILE C  62      55.096  47.949   9.879  1.00 29.78           C  
ANISOU 3226  CA  ILE C  62     3647   3303   4364   -470   -878    234       C  
ATOM   3227  C   ILE C  62      53.733  48.614  10.022  1.00 36.29           C  
ANISOU 3227  C   ILE C  62     4605   4126   5059   -547   -818    313       C  
ATOM   3228  O   ILE C  62      53.601  49.830   9.833  1.00 30.38           O  
ANISOU 3228  O   ILE C  62     3894   3426   4222   -612   -724    274       O  
ATOM   3229  CB  ILE C  62      55.281  47.287   8.514  1.00 29.24           C  
ANISOU 3229  CB  ILE C  62     3556   3167   4388   -404   -816    110       C  
ATOM   3230  CG1 ILE C  62      56.763  46.933   8.346  1.00 32.73           C  
ANISOU 3230  CG1 ILE C  62     3804   3644   4986   -326   -813    -32       C  
ATOM   3231  CG2 ILE C  62      54.803  48.210   7.415  1.00 32.03           C  
ANISOU 3231  CG2 ILE C  62     4016   3549   4604   -485   -663     55       C  
ATOM   3232  CD1 ILE C  62      57.074  46.148   7.031  1.00 38.55           C  
ANISOU 3232  CD1 ILE C  62     4505   4322   5818   -243   -718   -212       C  
ATOM   3233  N   ALA C  63      52.721  47.829  10.373  1.00 27.46           N  
ANISOU 3233  N   ALA C  63     3541   2933   3959   -543   -875    420       N  
ATOM   3234  CA  ALA C  63      51.384  48.381  10.628  1.00 28.70           C  
ANISOU 3234  CA  ALA C  63     3758   3100   4048   -607   -809    473       C  
ATOM   3235  C   ALA C  63      51.367  49.404  11.764  1.00 29.09           C  
ANISOU 3235  C   ALA C  63     3828   3258   3966   -669   -754    485       C  
ATOM   3236  O   ALA C  63      50.625  50.389  11.684  1.00 28.53           O  
ANISOU 3236  O   ALA C  63     3777   3203   3861   -694   -666    439       O  
ATOM   3237  CB  ALA C  63      50.388  47.261  10.944  1.00 29.47           C  
ANISOU 3237  CB  ALA C  63     3870   3111   4216   -629   -857    584       C  
ATOM   3238  N   ALA C  64      52.124  49.138  12.833  1.00 28.00           N  
ANISOU 3238  N   ALA C  64     3696   3180   3762   -685   -830    537       N  
ATOM   3239  CA  ALA C  64      52.178  50.068  13.980  1.00 30.31           C  
ANISOU 3239  CA  ALA C  64     4042   3587   3889   -755   -794    520       C  
ATOM   3240  C   ALA C  64      52.766  51.397  13.527  1.00 27.41           C  
ANISOU 3240  C   ALA C  64     3645   3247   3522   -768   -739    376       C  
ATOM   3241  O   ALA C  64      52.265  52.474  13.899  1.00 30.89           O  
ANISOU 3241  O   ALA C  64     4135   3714   3887   -810   -650    308       O  
ATOM   3242  CB  ALA C  64      53.008  49.503  15.147  1.00 31.75           C  
ANISOU 3242  CB  ALA C  64     4266   3825   3972   -772   -951    608       C  
ATOM   3243  N   ILE C  65      53.827  51.323  12.726  1.00 26.57           N  
ANISOU 3243  N   ILE C  65     3455   3122   3516   -739   -777    320       N  
ATOM   3244  CA  ILE C  65      54.477  52.560  12.245  1.00 27.59           C  
ANISOU 3244  CA  ILE C  65     3563   3266   3653   -798   -706    204       C  
ATOM   3245  C   ILE C  65      53.533  53.301  11.306  1.00 28.15           C  
ANISOU 3245  C   ILE C  65     3722   3250   3725   -805   -596    190       C  
ATOM   3246  O   ILE C  65      53.249  54.478  11.500  1.00 29.23           O  
ANISOU 3246  O   ILE C  65     3923   3357   3824   -852   -549    140       O  
ATOM   3247  CB  ILE C  65      55.783  52.265  11.507  1.00 32.12           C  
ANISOU 3247  CB  ILE C  65     4001   3857   4346   -791   -715    136       C  
ATOM   3248  CG1 ILE C  65      56.811  51.666  12.460  1.00 28.05           C  
ANISOU 3248  CG1 ILE C  65     3363   3411   3882   -762   -883    134       C  
ATOM   3249  CG2 ILE C  65      56.324  53.533  10.781  1.00 30.80           C  
ANISOU 3249  CG2 ILE C  65     3833   3684   4184   -903   -589     42       C  
ATOM   3250  CD1 ILE C  65      58.072  51.093  11.756  1.00 33.88           C  
ANISOU 3250  CD1 ILE C  65     3892   4165   4818   -709   -897     39       C  
ATOM   3251  N   LEU C  66      53.025  52.595  10.301  1.00 26.95           N  
ANISOU 3251  N   LEU C  66     3581   3034   3624   -750   -590    227       N  
ATOM   3252  CA  LEU C  66      52.119  53.206   9.328  1.00 27.22           C  
ANISOU 3252  CA  LEU C  66     3711   2976   3655   -744   -553    229       C  
ATOM   3253  C   LEU C  66      50.871  53.793   9.997  1.00 25.89           C  
ANISOU 3253  C   LEU C  66     3568   2776   3494   -721   -550    238       C  
ATOM   3254  O   LEU C  66      50.358  54.853   9.570  1.00 29.10           O  
ANISOU 3254  O   LEU C  66     4046   3093   3918   -715   -543    212       O  
ATOM   3255  CB  LEU C  66      51.672  52.142   8.303  1.00 31.30           C  
ANISOU 3255  CB  LEU C  66     4241   3442   4211   -687   -594    255       C  
ATOM   3256  CG  LEU C  66      50.869  52.626   7.096  1.00 32.38           C  
ANISOU 3256  CG  LEU C  66     4499   3486   4320   -680   -619    262       C  
ATOM   3257  CD1 LEU C  66      51.706  53.560   6.259  1.00 30.05           C  
ANISOU 3257  CD1 LEU C  66     4313   3177   3926   -760   -544    238       C  
ATOM   3258  CD2 LEU C  66      50.345  51.440   6.248  1.00 29.84           C  
ANISOU 3258  CD2 LEU C  66     4190   3120   4028   -631   -696    262       C  
ATOM   3259  N   GLY C  67      50.369  53.088  11.016  1.00 26.24           N  
ANISOU 3259  N   GLY C  67     3556   2881   3534   -709   -551    274       N  
ATOM   3260  CA  GLY C  67      49.123  53.454  11.670  1.00 30.79           C  
ANISOU 3260  CA  GLY C  67     4109   3457   4131   -693   -493    255       C  
ATOM   3261  C   GLY C  67      49.220  54.534  12.741  1.00 33.04           C  
ANISOU 3261  C   GLY C  67     4427   3793   4335   -725   -417    159       C  
ATOM   3262  O   GLY C  67      48.224  54.884  13.367  1.00 33.10           O  
ANISOU 3262  O   GLY C  67     4400   3816   4360   -706   -327     98       O  
ATOM   3263  N   GLY C  68      50.416  55.082  12.935  1.00 29.85           N  
ANISOU 3263  N   GLY C  68     4072   3412   3858   -777   -445    116       N  
ATOM   3264  CA  GLY C  68      50.600  56.174  13.885  1.00 36.88           C  
ANISOU 3264  CA  GLY C  68     5015   4327   4671   -820   -401     -8       C  
ATOM   3265  C   GLY C  68      50.784  55.760  15.337  1.00 35.91           C  
ANISOU 3265  C   GLY C  68     4919   4358   4368   -876   -389    -19       C  
ATOM   3266  O   GLY C  68      50.690  56.591  16.234  1.00 34.60           O  
ANISOU 3266  O   GLY C  68     4817   4229   4102   -909   -333   -152       O  
ATOM   3267  N   MET C  69      51.056  54.479  15.563  1.00 32.70           N  
ANISOU 3267  N   MET C  69     4493   4025   3908   -887   -456    118       N  
ATOM   3268  CA  MET C  69      51.239  53.931  16.903  1.00 37.99           C  
ANISOU 3268  CA  MET C  69     5239   4826   4368   -953   -486    168       C  
ATOM   3269  C   MET C  69      52.678  54.040  17.404  1.00 36.38           C  
ANISOU 3269  C   MET C  69     5062   4682   4078   -997   -664    148       C  
ATOM   3270  O   MET C  69      52.939  53.792  18.576  1.00 38.78           O  
ANISOU 3270  O   MET C  69     5472   5095   4168  -1058   -741    177       O  
ATOM   3271  CB  MET C  69      50.808  52.455  16.947  1.00 36.38           C  
ANISOU 3271  CB  MET C  69     5029   4626   4167   -952   -512    359       C  
ATOM   3272  CG  MET C  69      49.354  52.203  16.610  1.00 42.12           C  
ANISOU 3272  CG  MET C  69     5697   5314   4994   -942   -351    379       C  
ATOM   3273  SD  MET C  69      48.263  53.163  17.672  1.00 73.01           S  
ANISOU 3273  SD  MET C  69     9637   9334   8771   -995   -108    223       S  
ATOM   3274  CE  MET C  69      47.685  54.386  16.491  1.00 57.12           C  
ANISOU 3274  CE  MET C  69     7500   7175   7029   -866    -70     52       C  
ATOM   3275  N   VAL C  70      53.623  54.395  16.533  1.00 32.71           N  
ANISOU 3275  N   VAL C  70     4500   4154   3772   -981   -736     99       N  
ATOM   3276  CA  VAL C  70      54.988  54.636  17.015  1.00 41.16           C  
ANISOU 3276  CA  VAL C  70     5534   5287   4818  -1035   -904     39       C  
ATOM   3277  C   VAL C  70      55.234  56.142  17.116  1.00 41.47           C  
ANISOU 3277  C   VAL C  70     5605   5296   4855  -1117   -853   -146       C  
ATOM   3278  O   VAL C  70      55.479  56.678  18.195  1.00 37.58           O  
ANISOU 3278  O   VAL C  70     5203   4876   4201  -1189   -922   -248       O  
ATOM   3279  CB  VAL C  70      56.055  53.949  16.134  1.00 41.24           C  
ANISOU 3279  CB  VAL C  70     5370   5268   5031   -988  -1007     81       C  
ATOM   3280  CG1 VAL C  70      57.453  54.249  16.680  1.00 41.06           C  
ANISOU 3280  CG1 VAL C  70     5246   5318   5038  -1046  -1194     -6       C  
ATOM   3281  CG2 VAL C  70      55.783  52.402  16.055  1.00 32.70           C  
ANISOU 3281  CG2 VAL C  70     4277   4164   3983   -891  -1081    250       C  
ATOM   3282  N   TYR C  71      55.103  56.828  15.990  1.00 33.46           N  
ANISOU 3282  N   TYR C  71     4553   4157   4004  -1116   -742   -186       N  
ATOM   3283  CA  TYR C  71      55.040  58.289  15.999  1.00 36.46           C  
ANISOU 3283  CA  TYR C  71     5006   4436   4410  -1187   -679   -338       C  
ATOM   3284  C   TYR C  71      53.646  58.735  15.572  1.00 36.35           C  
ANISOU 3284  C   TYR C  71     5072   4302   4438  -1101   -537   -344       C  
ATOM   3285  O   TYR C  71      53.155  58.375  14.494  1.00 34.37           O  
ANISOU 3285  O   TYR C  71     4791   3975   4292  -1035   -493   -239       O  
ATOM   3286  CB  TYR C  71      56.064  58.871  15.041  1.00 31.98           C  
ANISOU 3286  CB  TYR C  71     4358   3785   4009  -1282   -683   -363       C  
ATOM   3287  CG  TYR C  71      56.030  60.384  14.940  1.00 35.38           C  
ANISOU 3287  CG  TYR C  71     4892   4051   4499  -1378   -635   -488       C  
ATOM   3288  CD1 TYR C  71      56.568  61.170  15.946  1.00 41.17           C  
ANISOU 3288  CD1 TYR C  71     5663   4796   5185  -1483   -719   -655       C  
ATOM   3289  CD2 TYR C  71      55.472  61.020  13.825  1.00 35.04           C  
ANISOU 3289  CD2 TYR C  71     4934   3818   4562  -1366   -537   -436       C  
ATOM   3290  CE1 TYR C  71      56.562  62.544  15.853  1.00 50.70           C  
ANISOU 3290  CE1 TYR C  71     6976   5808   6478  -1576   -689   -781       C  
ATOM   3291  CE2 TYR C  71      55.470  62.402  13.721  1.00 33.08           C  
ANISOU 3291  CE2 TYR C  71     4807   3366   4394  -1453   -523   -528       C  
ATOM   3292  CZ  TYR C  71      56.005  63.157  14.744  1.00 36.00           C  
ANISOU 3292  CZ  TYR C  71     5202   3731   4747  -1557   -590   -707       C  
ATOM   3293  OH  TYR C  71      56.026  64.539  14.694  1.00 44.00           O  
ANISOU 3293  OH  TYR C  71     6349   4503   5868  -1651   -592   -818       O  
ATOM   3294  N   LYS C  72      53.004  59.509  16.437  1.00 37.58           N  
ANISOU 3294  N   LYS C  72     5322   4442   4516  -1096   -479   -490       N  
ATOM   3295  CA  LYS C  72      51.716  60.108  16.123  1.00 37.85           C  
ANISOU 3295  CA  LYS C  72     5388   4342   4651   -993   -362   -549       C  
ATOM   3296  C   LYS C  72      51.936  61.472  15.460  1.00 33.93           C  
ANISOU 3296  C   LYS C  72     4963   3610   4318  -1019   -385   -634       C  
ATOM   3297  O   LYS C  72      52.659  62.307  15.982  1.00 35.90           O  
ANISOU 3297  O   LYS C  72     5278   3817   4545  -1122   -427   -771       O  
ATOM   3298  CB  LYS C  72      50.924  60.273  17.422  1.00 44.08           C  
ANISOU 3298  CB  LYS C  72     6227   5231   5292   -968   -251   -705       C  
ATOM   3299  CG  LYS C  72      49.651  61.104  17.305  1.00 52.47           C  
ANISOU 3299  CG  LYS C  72     7278   6150   6510   -844   -123   -852       C  
ATOM   3300  CD  LYS C  72      49.279  61.674  18.668  1.00 52.39           C  
ANISOU 3300  CD  LYS C  72     7342   6224   6340   -857      7  -1107       C  
ATOM   3301  CE  LYS C  72      48.163  62.682  18.566  1.00 51.70           C  
ANISOU 3301  CE  LYS C  72     7215   5957   6472   -709    124  -1318       C  
ATOM   3302  NZ  LYS C  72      48.668  63.945  17.985  1.00 48.52           N  
ANISOU 3302  NZ  LYS C  72     6904   5269   6262   -700     -7  -1402       N  
ATOM   3303  N   PRO C  73      51.303  61.701  14.311  1.00 29.32           N  
ANISOU 3303  N   PRO C  73     4389   2856   3897   -938   -382   -545       N  
ATOM   3304  CA  PRO C  73      51.299  62.997  13.617  1.00 30.41           C  
ANISOU 3304  CA  PRO C  73     4644   2717   4192   -951   -424   -579       C  
ATOM   3305  C   PRO C  73      50.890  64.074  14.604  1.00 35.84           C  
ANISOU 3305  C   PRO C  73     5398   3297   4924   -913   -395   -823       C  
ATOM   3306  O   PRO C  73      49.824  63.962  15.213  1.00 35.28           O  
ANISOU 3306  O   PRO C  73     5268   3274   4863   -774   -311   -938       O  
ATOM   3307  CB  PRO C  73      50.186  62.813  12.589  1.00 29.22           C  
ANISOU 3307  CB  PRO C  73     4487   2447   4167   -802   -453   -460       C  
ATOM   3308  CG  PRO C  73      50.210  61.375  12.290  1.00 30.03           C  
ANISOU 3308  CG  PRO C  73     4480   2756   4174   -796   -438   -318       C  
ATOM   3309  CD  PRO C  73      50.443  60.722  13.633  1.00 30.04           C  
ANISOU 3309  CD  PRO C  73     4400   2988   4028   -828   -369   -402       C  
ATOM   3310  N   GLN C  74      51.727  65.090  14.794  1.00 32.62           N  
ANISOU 3310  N   GLN C  74     5096   2748   4549  -1046   -445   -927       N  
ATOM   3311  CA  GLN C  74      51.509  65.994  15.910  1.00 38.67           C  
ANISOU 3311  CA  GLN C  74     5933   3443   5317  -1028   -418  -1210       C  
ATOM   3312  C   GLN C  74      50.243  66.833  15.800  1.00 47.05           C  
ANISOU 3312  C   GLN C  74     7033   4253   6592   -828   -390  -1344       C  
ATOM   3313  O   GLN C  74      49.682  67.229  16.812  1.00 45.23           O  
ANISOU 3313  O   GLN C  74     6802   4040   6345   -743   -300  -1611       O  
ATOM   3314  CB  GLN C  74      52.716  66.922  16.113  1.00 49.44           C  
ANISOU 3314  CB  GLN C  74     7401   4679   6705  -1237   -506  -1309       C  
ATOM   3315  CG  GLN C  74      53.695  66.441  17.164  1.00 66.47           C  
ANISOU 3315  CG  GLN C  74     9507   7106   8642  -1382   -544  -1403       C  
ATOM   3316  CD  GLN C  74      54.741  67.494  17.484  1.00 71.65           C  
ANISOU 3316  CD  GLN C  74    10245   7614   9365  -1589   -648  -1565       C  
ATOM   3317  OE1 GLN C  74      55.140  68.272  16.615  1.00 71.43           O  
ANISOU 3317  OE1 GLN C  74    10234   7357   9550  -1656   -672  -1473       O  
ATOM   3318  NE2 GLN C  74      55.173  67.539  18.741  1.00 80.93           N  
ANISOU 3318  NE2 GLN C  74    11443   8947  10359  -1660   -710  -1780       N  
ATOM   3319  N   ALA C  75      49.799  67.124  14.585  1.00 44.12           N  
ANISOU 3319  N   ALA C  75     6699   3645   6420   -746   -477  -1174       N  
ATOM   3320  CA  ALA C  75      48.684  68.053  14.442  1.00 47.25           C  
ANISOU 3320  CA  ALA C  75     7127   3742   7084   -536   -517  -1306       C  
ATOM   3321  C   ALA C  75      47.302  67.403  14.540  1.00 44.39           C  
ANISOU 3321  C   ALA C  75     6562   3501   6804   -304   -439  -1348       C  
ATOM   3322  O   ALA C  75      46.293  68.104  14.524  1.00 53.29           O  
ANISOU 3322  O   ALA C  75     7644   4406   8196    -93   -467  -1501       O  
ATOM   3323  CB  ALA C  75      48.817  68.873  13.165  1.00 47.03           C  
ANISOU 3323  CB  ALA C  75     7281   3342   7246   -555   -702  -1111       C  
ATOM   3324  N   LEU C  76      47.244  66.079  14.655  1.00 43.49           N  
ANISOU 3324  N   LEU C  76     6307   3716   6502   -341   -347  -1226       N  
ATOM   3325  CA  LEU C  76      45.945  65.398  14.771  1.00 39.70           C  
ANISOU 3325  CA  LEU C  76     5609   3362   6114   -168   -254  -1263       C  
ATOM   3326  C   LEU C  76      45.504  65.258  16.232  1.00 44.99           C  
ANISOU 3326  C   LEU C  76     6177   4253   6664   -153     -7  -1538       C  
ATOM   3327  O   LEU C  76      46.199  64.658  17.036  1.00 53.69           O  
ANISOU 3327  O   LEU C  76     7330   5608   7462   -315     87  -1532       O  
ATOM   3328  CB  LEU C  76      45.978  64.021  14.112  1.00 34.77           C  
ANISOU 3328  CB  LEU C  76     4898   2940   5376   -225   -280   -993       C  
ATOM   3329  CG  LEU C  76      46.231  64.086  12.603  1.00 41.39           C  
ANISOU 3329  CG  LEU C  76     5844   3587   6295   -231   -494   -744       C  
ATOM   3330  CD1 LEU C  76      46.003  62.742  11.993  1.00 41.81           C  
ANISOU 3330  CD1 LEU C  76     5791   3820   6273   -245   -514   -553       C  
ATOM   3331  CD2 LEU C  76      45.381  65.144  11.916  1.00 43.33           C  
ANISOU 3331  CD2 LEU C  76     6131   3492   6843    -47   -662   -778       C  
ATOM   3332  N   GLU C  77      44.347  65.810  16.570  1.00 43.16           N  
ANISOU 3332  N   GLU C  77     5806   3927   6667     42     94  -1783       N  
ATOM   3333  CA  GLU C  77      43.857  65.713  17.949  1.00 47.36           C  
ANISOU 3333  CA  GLU C  77     6249   4688   7058     42    389  -2076       C  
ATOM   3334  C   GLU C  77      42.698  64.729  18.122  1.00 45.20           C  
ANISOU 3334  C   GLU C  77     5696   4643   6834    102    587  -2066       C  
ATOM   3335  O   GLU C  77      42.380  64.317  19.235  1.00 46.94           O  
ANISOU 3335  O   GLU C  77     5861   5130   6842     27    872  -2223       O  
ATOM   3336  CB  GLU C  77      43.523  67.090  18.520  1.00 60.42           C  
ANISOU 3336  CB  GLU C  77     7943   6113   8899    183    450  -2460       C  
ATOM   3337  CG  GLU C  77      44.693  68.074  18.456  1.00 80.41           C  
ANISOU 3337  CG  GLU C  77    10760   8406  11388     79    263  -2487       C  
ATOM   3338  CD  GLU C  77      46.001  67.522  19.029  1.00 91.72           C  
ANISOU 3338  CD  GLU C  77    12364  10090  12396   -200    259  -2378       C  
ATOM   3339  OE1 GLU C  77      45.972  66.615  19.894  1.00 87.77           O  
ANISOU 3339  OE1 GLU C  77    11825   9941  11583   -296    437  -2390       O  
ATOM   3340  OE2 GLU C  77      47.072  68.011  18.608  1.00101.25           O  
ANISOU 3340  OE2 GLU C  77    13742  11129  13599   -330     65  -2275       O  
ATOM   3341  N   SER C  78      42.075  64.332  17.021  1.00 40.30           N  
ANISOU 3341  N   SER C  78     7009   3300   5005     80    975   -784       N  
ATOM   3342  CA  SER C  78      41.158  63.208  17.102  1.00 38.95           C  
ANISOU 3342  CA  SER C  78     6439   3611   4750    141    972   -808       C  
ATOM   3343  C   SER C  78      41.023  62.578  15.740  1.00 38.84           C  
ANISOU 3343  C   SER C  78     6341   3612   4806    320    842   -550       C  
ATOM   3344  O   SER C  78      41.273  63.220  14.726  1.00 47.18           O  
ANISOU 3344  O   SER C  78     7652   4350   5925    550    771   -391       O  
ATOM   3345  CB  SER C  78      39.785  63.606  17.650  1.00 48.03           C  
ANISOU 3345  CB  SER C  78     7391   4974   5884    459   1059  -1188       C  
ATOM   3346  OG  SER C  78      39.039  64.343  16.702  1.00 45.69           O  
ANISOU 3346  OG  SER C  78     7168   4461   5734    993    960  -1245       O  
ATOM   3347  N   ILE C  79      40.618  61.321  15.730  1.00 32.72           N  
ANISOU 3347  N   ILE C  79     5232   3201   4001    199    818   -513       N  
ATOM   3348  CA  ILE C  79      40.430  60.602  14.479  1.00 35.05           C  
ANISOU 3348  CA  ILE C  79     5406   3562   4349    355    672   -365       C  
ATOM   3349  C   ILE C  79      39.201  59.704  14.572  1.00 31.84           C  
ANISOU 3349  C   ILE C  79     4569   3545   3985    385    661   -555       C  
ATOM   3350  O   ILE C  79      38.739  59.384  15.671  1.00 36.93           O  
ANISOU 3350  O   ILE C  79     5013   4423   4594    160    812   -696       O  
ATOM   3351  CB  ILE C  79      41.656  59.716  14.169  1.00 29.99           C  
ANISOU 3351  CB  ILE C  79     4823   2876   3696     46    628    -91       C  
ATOM   3352  CG1 ILE C  79      41.961  58.770  15.330  1.00 37.36           C  
ANISOU 3352  CG1 ILE C  79     5612   3990   4593   -355    693    -66       C  
ATOM   3353  CG2 ILE C  79      42.867  60.588  13.775  1.00 37.68           C  
ANISOU 3353  CG2 ILE C  79     6143   3521   4654      5    651     96       C  
ATOM   3354  CD1 ILE C  79      42.933  57.660  14.990  1.00 32.37           C  
ANISOU 3354  CD1 ILE C  79     4959   3343   3996   -551    601    159       C  
ATOM   3355  N   GLU C  80      38.669  59.278  13.432  1.00 33.27           N  
ANISOU 3355  N   GLU C  80     4589   3834   4219    627    493   -574       N  
ATOM   3356  CA  GLU C  80      37.656  58.217  13.453  1.00 33.27           C  
ANISOU 3356  CA  GLU C  80     4135   4192   4313    521    470   -766       C  
ATOM   3357  C   GLU C  80      38.394  56.908  13.213  1.00 31.70           C  
ANISOU 3357  C   GLU C  80     3938   3937   4170    167    421   -576       C  
ATOM   3358  O   GLU C  80      39.120  56.771  12.227  1.00 32.43           O  
ANISOU 3358  O   GLU C  80     4209   3878   4233    283    281   -435       O  
ATOM   3359  CB  GLU C  80      36.588  58.412  12.383  1.00 43.09           C  
ANISOU 3359  CB  GLU C  80     5136   5644   5594    981    264   -987       C  
ATOM   3360  CG  GLU C  80      35.514  57.329  12.436  1.00 61.24           C  
ANISOU 3360  CG  GLU C  80     6891   8338   8039    791    247  -1256       C  
ATOM   3361  CD  GLU C  80      34.595  57.331  11.225  1.00 70.38           C  
ANISOU 3361  CD  GLU C  80     7759   9762   9221   1222    -42  -1506       C  
ATOM   3362  OE1 GLU C  80      35.038  57.725  10.125  1.00 70.64           O  
ANISOU 3362  OE1 GLU C  80     8074   9653   9111   1585   -258  -1368       O  
ATOM   3363  OE2 GLU C  80      33.423  56.933  11.378  1.00 77.29           O  
ANISOU 3363  OE2 GLU C  80     8100  11035  10231   1185    -49  -1847       O  
ATOM   3364  N   MET C  81      38.208  55.952  14.109  1.00 31.30           N  
ANISOU 3364  N   MET C  81     3706   3998   4186   -245    548   -568       N  
ATOM   3365  CA  MET C  81      38.972  54.708  14.070  1.00 36.98           C  
ANISOU 3365  CA  MET C  81     4494   4566   4992   -563    500   -364       C  
ATOM   3366  C   MET C  81      38.664  53.939  12.779  1.00 34.28           C  
ANISOU 3366  C   MET C  81     3992   4238   4796   -435    289   -504       C  
ATOM   3367  O   MET C  81      37.505  53.909  12.342  1.00 35.68           O  
ANISOU 3367  O   MET C  81     3845   4659   5052   -310    223   -789       O  
ATOM   3368  CB  MET C  81      38.588  53.877  15.299  1.00 38.15           C  
ANISOU 3368  CB  MET C  81     4505   4816   5174  -1009    690   -299       C  
ATOM   3369  CG  MET C  81      39.464  52.686  15.572  1.00 52.99           C  
ANISOU 3369  CG  MET C  81     6553   6454   7126  -1315    649    -14       C  
ATOM   3370  SD  MET C  81      39.021  51.970  17.180  1.00 63.64           S  
ANISOU 3370  SD  MET C  81     7862   7923   8395  -1820    916    181       S  
ATOM   3371  CE  MET C  81      40.117  50.553  17.197  1.00107.86           C  
ANISOU 3371  CE  MET C  81    13735  13110  14138  -2022    760    549       C  
ATOM   3372  N   ALA C  82      39.686  53.341  12.150  1.00 33.38           N  
ANISOU 3372  N   ALA C  82     4065   3913   4707   -438    169   -362       N  
ATOM   3373  CA  ALA C  82      39.470  52.570  10.934  1.00 34.25           C  
ANISOU 3373  CA  ALA C  82     4046   4048   4918   -310    -36   -557       C  
ATOM   3374  C   ALA C  82      38.462  51.450  11.169  1.00 34.28           C  
ANISOU 3374  C   ALA C  82     3725   4112   5187   -624    -45   -774       C  
ATOM   3375  O   ALA C  82      38.567  50.714  12.151  1.00 34.49           O  
ANISOU 3375  O   ALA C  82     3778   3978   5349  -1024     95   -610       O  
ATOM   3376  CB  ALA C  82      40.798  51.954  10.414  1.00 33.33           C  
ANISOU 3376  CB  ALA C  82     4158   3702   4803   -295   -115   -407       C  
ATOM   3377  N   PHE C  83      37.510  51.343  10.251  1.00 33.30           N  
ANISOU 3377  N   PHE C  83     3307   4225   5119   -451   -217  -1128       N  
ATOM   3378  CA  PHE C  83      36.528  50.263  10.184  1.00 36.96           C  
ANISOU 3378  CA  PHE C  83     3400   4762   5879   -767   -269  -1434       C  
ATOM   3379  C   PHE C  83      35.661  50.221  11.426  1.00 49.81           C  
ANISOU 3379  C   PHE C  83     4773   6525   7626  -1161      0  -1412       C  
ATOM   3380  O   PHE C  83      35.249  49.155  11.859  1.00 41.90           O  
ANISOU 3380  O   PHE C  83     3615   5408   6898  -1645     96  -1449       O  
ATOM   3381  CB  PHE C  83      37.178  48.901   9.948  1.00 46.42           C  
ANISOU 3381  CB  PHE C  83     4746   5575   7315  -1029   -351  -1417       C  
ATOM   3382  CG  PHE C  83      38.052  48.863   8.722  1.00 36.07           C  
ANISOU 3382  CG  PHE C  83     3646   4201   5860   -640   -575  -1496       C  
ATOM   3383  CD1 PHE C  83      37.484  48.892   7.459  1.00 41.42           C  
ANISOU 3383  CD1 PHE C  83     4119   5167   6450   -340   -832  -1901       C  
ATOM   3384  CD2 PHE C  83      39.428  48.846   8.845  1.00 33.19           C  
ANISOU 3384  CD2 PHE C  83     3643   3570   5398   -558   -524  -1182       C  
ATOM   3385  CE1 PHE C  83      38.280  48.870   6.317  1.00 47.51           C  
ANISOU 3385  CE1 PHE C  83     5091   5959   7001     22  -1000  -1976       C  
ATOM   3386  CE2 PHE C  83      40.240  48.824   7.697  1.00 35.67           C  
ANISOU 3386  CE2 PHE C  83     4102   3907   5545   -208   -673  -1277       C  
ATOM   3387  CZ  PHE C  83      39.654  48.834   6.437  1.00 34.99           C  
ANISOU 3387  CZ  PHE C  83     3852   4110   5332     74   -891  -1664       C  
ATOM   3388  N   SER C  84      35.379  51.393  11.972  1.00 45.67           N  
ANISOU 3388  N   SER C  84     4221   6238   6894   -953    138  -1364       N  
ATOM   3389  CA  SER C  84      34.616  51.507  13.214  1.00 55.37           C  
ANISOU 3389  CA  SER C  84     5211   7682   8143  -1273    446  -1361       C  
ATOM   3390  C   SER C  84      33.899  52.853  13.224  1.00 54.99           C  
ANISOU 3390  C   SER C  84     4960   8006   7926   -826    463  -1583       C  
ATOM   3391  O   SER C  84      34.244  53.748  12.450  1.00 47.85           O  
ANISOU 3391  O   SER C  84     4258   7057   6865   -306    261  -1588       O  
ATOM   3392  CB  SER C  84      35.587  51.441  14.402  1.00 50.18           C  
ANISOU 3392  CB  SER C  84     4959   6763   7344  -1545    672   -921       C  
ATOM   3393  OG  SER C  84      34.953  51.795  15.626  1.00 54.43           O  
ANISOU 3393  OG  SER C  84     5333   7583   7763  -1767    991   -911       O  
ATOM   3394  N   ASP C  85      32.915  53.012  14.104  1.00 50.66           N  
ANISOU 3394  N   ASP C  85     4032   7814   7403  -1011    721  -1754       N  
ATOM   3395  CA  ASP C  85      32.313  54.327  14.296  1.00 51.37           C  
ANISOU 3395  CA  ASP C  85     3965   8211   7341   -539    763  -1974       C  
ATOM   3396  C   ASP C  85      32.908  55.069  15.495  1.00 56.39           C  
ANISOU 3396  C   ASP C  85     4948   8739   7738   -579   1034  -1752       C  
ATOM   3397  O   ASP C  85      32.475  56.173  15.825  1.00 55.93           O  
ANISOU 3397  O   ASP C  85     4817   8867   7566   -207   1107  -1956       O  
ATOM   3398  CB  ASP C  85      30.797  54.220  14.467  1.00 53.10           C  
ANISOU 3398  CB  ASP C  85     3458   9003   7714   -599    873  -2421       C  
ATOM   3399  CG  ASP C  85      30.396  53.249  15.566  1.00 70.80           C  
ANISOU 3399  CG  ASP C  85     5446  11400  10053  -1344   1271  -2355       C  
ATOM   3400  OD1 ASP C  85      31.248  52.897  16.407  1.00 71.38           O  
ANISOU 3400  OD1 ASP C  85     5957  11170   9994  -1710   1476  -1942       O  
ATOM   3401  OD2 ASP C  85      29.216  52.840  15.592  1.00 80.60           O  
ANISOU 3401  OD2 ASP C  85     6187  12998  11439  -1521   1334  -2636       O  
ATOM   3402  N   LEU C  86      33.885  54.458  16.154  1.00 47.89           N  
ANISOU 3402  N   LEU C  86     4241   7369   6585   -997   1157  -1374       N  
ATOM   3403  CA  LEU C  86      34.450  55.043  17.372  1.00 47.03           C  
ANISOU 3403  CA  LEU C  86     4428   7233   6208  -1093   1389  -1200       C  
ATOM   3404  C   LEU C  86      35.437  56.149  17.045  1.00 45.80           C  
ANISOU 3404  C   LEU C  86     4722   6758   5924   -684   1218  -1111       C  
ATOM   3405  O   LEU C  86      36.024  56.160  15.976  1.00 40.63           O  
ANISOU 3405  O   LEU C  86     4259   5829   5350   -469    963  -1008       O  
ATOM   3406  CB  LEU C  86      35.158  53.975  18.200  1.00 45.65           C  
ANISOU 3406  CB  LEU C  86     4489   6894   5963  -1645   1528   -803       C  
ATOM   3407  CG  LEU C  86      34.242  52.872  18.736  1.00 52.86           C  
ANISOU 3407  CG  LEU C  86     5048   8049   6987  -2174   1783   -795       C  
ATOM   3408  CD1 LEU C  86      35.054  51.805  19.442  1.00 56.97           C  
ANISOU 3408  CD1 LEU C  86     5945   8263   7437  -2605   1831   -300       C  
ATOM   3409  CD2 LEU C  86      33.196  53.474  19.670  1.00 62.71           C  
ANISOU 3409  CD2 LEU C  86     5929   9846   8052  -2218   2139  -1066       C  
ATOM   3410  N   ILE C  87      35.610  57.065  17.991  1.00 41.44           N  
ANISOU 3410  N   ILE C  87     4332   6254   5160   -616   1386  -1171       N  
ATOM   3411  CA  ILE C  87      36.522  58.177  17.855  1.00 43.26           C  
ANISOU 3411  CA  ILE C  87     4989   6147   5302   -329   1272  -1119       C  
ATOM   3412  C   ILE C  87      37.628  57.950  18.867  1.00 42.16           C  
ANISOU 3412  C   ILE C  87     5158   5904   4955   -706   1362   -864       C  
ATOM   3413  O   ILE C  87      37.366  57.488  19.984  1.00 42.69           O  
ANISOU 3413  O   ILE C  87     5123   6260   4839  -1028   1581   -847       O  
ATOM   3414  CB  ILE C  87      35.794  59.493  18.233  1.00 50.07           C  
ANISOU 3414  CB  ILE C  87     5787   7129   6108     73   1371  -1498       C  
ATOM   3415  CG1 ILE C  87      34.575  59.696  17.337  1.00 47.90           C  
ANISOU 3415  CG1 ILE C  87     5127   7058   6017    512   1253  -1780       C  
ATOM   3416  CG2 ILE C  87      36.731  60.686  18.151  1.00 49.55           C  
ANISOU 3416  CG2 ILE C  87     6211   6615   6002    302   1275  -1457       C  
ATOM   3417  CD1 ILE C  87      34.936  59.809  15.877  1.00 51.60           C  
ANISOU 3417  CD1 ILE C  87     5786   7216   6605    834    927  -1615       C  
ATOM   3418  N   ILE C  88      38.851  58.264  18.477  1.00 41.52           N  
ANISOU 3418  N   ILE C  88     5434   5464   4878   -668   1196   -665       N  
ATOM   3419  CA  ILE C  88      39.963  58.330  19.409  1.00 41.88           C  
ANISOU 3419  CA  ILE C  88     5746   5443   4722   -935   1220   -507       C  
ATOM   3420  C   ILE C  88      40.434  59.771  19.520  1.00 43.48           C  
ANISOU 3420  C   ILE C  88     6212   5420   4886   -735   1202   -698       C  
ATOM   3421  O   ILE C  88      40.626  60.456  18.514  1.00 41.22           O  
ANISOU 3421  O   ILE C  88     6071   4819   4772   -465   1088   -699       O  
ATOM   3422  CB  ILE C  88      41.126  57.449  18.966  1.00 46.12           C  
ANISOU 3422  CB  ILE C  88     6419   5778   5325  -1114   1044   -156       C  
ATOM   3423  CG1 ILE C  88      40.715  55.973  19.014  1.00 47.03           C  
ANISOU 3423  CG1 ILE C  88     6350   6011   5508  -1351   1061     31       C  
ATOM   3424  CG2 ILE C  88      42.332  57.684  19.855  1.00 42.57           C  
ANISOU 3424  CG2 ILE C  88     6198   5302   4673  -1315   1006    -46       C  
ATOM   3425  CD1 ILE C  88      41.740  55.062  18.332  1.00 44.15           C  
ANISOU 3425  CD1 ILE C  88     6096   5394   5287  -1401    856    306       C  
ATOM   3426  N   GLU C  89      40.595  60.248  20.745  1.00 44.20           N  
ANISOU 3426  N   GLU C  89     6391   5662   4739   -876   1321   -867       N  
ATOM   3427  CA  GLU C  89      40.945  61.643  20.935  1.00 46.88           C  
ANISOU 3427  CA  GLU C  89     6986   5741   5086   -717   1313  -1138       C  
ATOM   3428  C   GLU C  89      42.086  61.789  21.927  1.00 52.57           C  
ANISOU 3428  C   GLU C  89     7897   6497   5578  -1043   1274  -1138       C  
ATOM   3429  O   GLU C  89      42.159  61.073  22.923  1.00 48.05           O  
ANISOU 3429  O   GLU C  89     7243   6309   4706  -1294   1329  -1066       O  
ATOM   3430  CB  GLU C  89      39.709  62.435  21.395  1.00 47.89           C  
ANISOU 3430  CB  GLU C  89     6989   6033   5176   -416   1486  -1580       C  
ATOM   3431  CG  GLU C  89      39.990  63.902  21.682  1.00 58.33           C  
ANISOU 3431  CG  GLU C  89     8618   7005   6541   -227   1480  -1929       C  
ATOM   3432  CD  GLU C  89      38.729  64.716  21.877  1.00 68.45           C  
ANISOU 3432  CD  GLU C  89     9773   8367   7869    222   1612  -2388       C  
ATOM   3433  OE1 GLU C  89      38.847  65.931  22.139  1.00 81.25           O  
ANISOU 3433  OE1 GLU C  89    11668   9639   9563    427   1609  -2729       O  
ATOM   3434  OE2 GLU C  89      37.626  64.144  21.762  1.00 70.00           O  
ANISOU 3434  OE2 GLU C  89     9577   8963   8058    370   1713  -2441       O  
ATOM   3435  N   TRP C  90      42.982  62.725  21.649  1.00 46.74           N  
ANISOU 3435  N   TRP C  90     7417   5369   4973  -1050   1171  -1211       N  
ATOM   3436  CA  TRP C  90      44.078  63.013  22.554  1.00 47.31           C  
ANISOU 3436  CA  TRP C  90     7624   5491   4862  -1359   1094  -1312       C  
ATOM   3437  C   TRP C  90      43.732  64.253  23.371  1.00 54.96           C  
ANISOU 3437  C   TRP C  90     8748   6392   5743  -1274   1189  -1838       C  
ATOM   3438  O   TRP C  90      43.527  65.334  22.814  1.00 54.96           O  
ANISOU 3438  O   TRP C  90     8943   5918   6020  -1049   1209  -2037       O  
ATOM   3439  CB  TRP C  90      45.376  63.200  21.757  1.00 53.91           C  
ANISOU 3439  CB  TRP C  90     8580   5976   5928  -1518    939  -1100       C  
ATOM   3440  CG  TRP C  90      45.899  61.917  21.197  1.00 47.65           C  
ANISOU 3440  CG  TRP C  90     7618   5330   5158  -1606    831   -671       C  
ATOM   3441  CD1 TRP C  90      46.900  61.145  21.712  1.00 49.41           C  
ANISOU 3441  CD1 TRP C  90     7746   5801   5228  -1848    682   -498       C  
ATOM   3442  CD2 TRP C  90      45.421  61.227  20.023  1.00 47.07           C  
ANISOU 3442  CD2 TRP C  90     7444   5170   5268  -1404    836   -405       C  
ATOM   3443  NE1 TRP C  90      47.087  60.026  20.922  1.00 46.71           N  
ANISOU 3443  NE1 TRP C  90     7272   5471   5004  -1790    610   -144       N  
ATOM   3444  CE2 TRP C  90      46.194  60.055  19.887  1.00 44.52           C  
ANISOU 3444  CE2 TRP C  90     6992   4999   4925  -1546    708   -105       C  
ATOM   3445  CE3 TRP C  90      44.428  61.495  19.077  1.00 52.95           C  
ANISOU 3445  CE3 TRP C  90     8193   5744   6181  -1083    902   -425       C  
ATOM   3446  CZ2 TRP C  90      45.999  59.149  18.834  1.00 47.61           C  
ANISOU 3446  CZ2 TRP C  90     7273   5343   5473  -1408    669    129       C  
ATOM   3447  CZ3 TRP C  90      44.237  60.590  18.029  1.00 50.07           C  
ANISOU 3447  CZ3 TRP C  90     7696   5399   5929   -962    841   -180       C  
ATOM   3448  CH2 TRP C  90      45.017  59.435  17.924  1.00 48.12           C  
ANISOU 3448  CH2 TRP C  90     7337   5274   5672  -1142    739     70       C  
ATOM   3449  N   PHE C  91      43.637  64.089  24.693  1.00 55.61           N  
ANISOU 3449  N   PHE C  91     8771   6940   5419  -1424   1249  -2064       N  
ATOM   3450  CA  PHE C  91      43.300  65.186  25.586  1.00 57.00           C  
ANISOU 3450  CA  PHE C  91     9075   7136   5447  -1335   1346  -2651       C  
ATOM   3451  C   PHE C  91      44.445  65.448  26.562  1.00 68.18           C  
ANISOU 3451  C   PHE C  91    10612   8704   6589  -1683   1189  -2860       C  
ATOM   3452  O   PHE C  91      44.841  64.562  27.331  1.00 57.45           O  
ANISOU 3452  O   PHE C  91     9143   7868   4817  -1907   1119  -2667       O  
ATOM   3453  CB  PHE C  91      41.997  64.883  26.348  1.00 64.98           C  
ANISOU 3453  CB  PHE C  91     9868   8687   6134  -1161   1603  -2862       C  
ATOM   3454  CG  PHE C  91      41.646  65.906  27.412  1.00 74.64           C  
ANISOU 3454  CG  PHE C  91    11141  10040   7177  -1003   1669  -3426       C  
ATOM   3455  CD1 PHE C  91      41.276  67.193  27.062  1.00 73.91           C  
ANISOU 3455  CD1 PHE C  91    11200   9437   7444   -636   1645  -3799       C  
ATOM   3456  CD2 PHE C  91      41.666  65.565  28.763  1.00 75.38           C  
ANISOU 3456  CD2 PHE C  91    11133  10737   6773  -1154   1703  -3483       C  
ATOM   3457  CE1 PHE C  91      40.950  68.133  28.038  1.00 74.22           C  
ANISOU 3457  CE1 PHE C  91    11295   9551   7354   -436   1655  -4276       C  
ATOM   3458  CE2 PHE C  91      41.342  66.500  29.750  1.00 80.52           C  
ANISOU 3458  CE2 PHE C  91    11824  11507   7263   -963   1734  -3968       C  
ATOM   3459  CZ  PHE C  91      40.980  67.782  29.387  1.00 75.76           C  
ANISOU 3459  CZ  PHE C  91    11375  10382   7029   -609   1714  -4388       C  
ATOM   3460  N   LYS C  92      44.976  66.668  26.530  1.00 75.02           N  
ANISOU 3460  N   LYS C  92    11679   9108   7719  -1697   1093  -3200       N  
ATOM   3461  CA  LYS C  92      46.054  67.048  27.439  1.00 71.71           C  
ANISOU 3461  CA  LYS C  92    11266   8835   7146  -1973    882  -3405       C  
ATOM   3462  C   LYS C  92      45.514  67.675  28.728  1.00 71.77           C  
ANISOU 3462  C   LYS C  92    11267   9152   6849  -1804    918  -3891       C  
ATOM   3463  O   LYS C  92      44.843  68.708  28.704  1.00 72.13           O  
ANISOU 3463  O   LYS C  92    11440   8851   7115  -1505    996  -4250       O  
ATOM   3464  CB  LYS C  92      47.042  67.988  26.747  1.00 76.41           C  
ANISOU 3464  CB  LYS C  92    12002   8794   8238  -2130    739  -3433       C  
ATOM   3465  CG  LYS C  92      48.383  68.115  27.462  1.00 82.26           C  
ANISOU 3465  CG  LYS C  92    12641   9743   8870  -2494    490  -3560       C  
ATOM   3466  CD  LYS C  92      49.340  69.012  26.692  1.00 91.34           C  
ANISOU 3466  CD  LYS C  92    13861  10295  10547  -2691    406  -3532       C  
ATOM   3467  CE  LYS C  92      50.687  69.136  27.395  1.00 97.47           C  
ANISOU 3467  CE  LYS C  92    14454  11332  11246  -3053    153  -3708       C  
ATOM   3468  NZ  LYS C  92      51.428  67.844  27.401  1.00 95.06           N  
ANISOU 3468  NZ  LYS C  92    13875  11561  10681  -3230     16  -3357       N  
ATOM   3469  N   VAL C  93      45.813  67.040  29.855  1.00 72.73           N  
ANISOU 3469  N   VAL C  93    14671   7423   5541  -4440   2041  -1147       N  
ATOM   3470  CA  VAL C  93      45.339  67.515  31.152  1.00 75.64           C  
ANISOU 3470  CA  VAL C  93    15378   7661   5698  -4411   2098  -1271       C  
ATOM   3471  C   VAL C  93      46.038  68.814  31.564  1.00 82.39           C  
ANISOU 3471  C   VAL C  93    16585   8360   6360  -4518   2099  -1338       C  
ATOM   3472  O   VAL C  93      47.252  68.841  31.784  1.00 80.19           O  
ANISOU 3472  O   VAL C  93    16337   8144   5990  -4722   1945  -1305       O  
ATOM   3473  CB  VAL C  93      45.541  66.456  32.232  1.00 82.09           C  
ANISOU 3473  CB  VAL C  93    16188   8581   6420  -4506   1978  -1261       C  
ATOM   3474  CG1 VAL C  93      44.786  66.846  33.497  1.00 83.49           C  
ANISOU 3474  CG1 VAL C  93    16686   8641   6396  -4438   2073  -1391       C  
ATOM   3475  CG2 VAL C  93      45.064  65.105  31.725  1.00 80.88           C  
ANISOU 3475  CG2 VAL C  93    15689   8580   6461  -4449   1953  -1182       C  
ATOM   3476  N   GLU C  94      45.255  69.885  31.668  1.00 83.40           N  
ANISOU 3476  N   GLU C  94    16981   8292   6416  -4371   2271  -1440       N  
ATOM   3477  CA  GLU C  94      45.787  71.226  31.908  1.00 89.69           C  
ANISOU 3477  CA  GLU C  94    18144   8895   7041  -4460   2303  -1511       C  
ATOM   3478  C   GLU C  94      45.842  71.575  33.392  1.00 89.10           C  
ANISOU 3478  C   GLU C  94    18435   8710   6711  -4543   2291  -1625       C  
ATOM   3479  O   GLU C  94      45.048  71.070  34.186  1.00 86.78           O  
ANISOU 3479  O   GLU C  94    18171   8437   6365  -4435   2341  -1675       O  
ATOM   3480  CB  GLU C  94      44.931  72.262  31.176  1.00 93.15           C  
ANISOU 3480  CB  GLU C  94    18716   9149   7526  -4234   2506  -1558       C  
ATOM   3481  CG  GLU C  94      44.829  72.039  29.675  1.00 94.49           C  
ANISOU 3481  CG  GLU C  94    18555   9409   7939  -4145   2526  -1456       C  
ATOM   3482  CD  GLU C  94      43.568  72.643  29.080  1.00 99.68           C  
ANISOU 3482  CD  GLU C  94    19258   9946   8668  -3825   2726  -1508       C  
ATOM   3483  OE1 GLU C  94      43.393  72.570  27.844  1.00 98.90           O  
ANISOU 3483  OE1 GLU C  94    18919   9898   8758  -3730   2752  -1438       O  
ATOM   3484  OE2 GLU C  94      42.750  73.187  29.851  1.00104.57           O  
ANISOU 3484  OE2 GLU C  94    20151  10437   9143  -3651   2858  -1620       O  
ATOM   3485  N   LYS C  95      46.775  72.453  33.753  1.00 92.69           N  
ANISOU 3485  N   LYS C  95    19170   9052   6997  -4744   2227  -1672       N  
ATOM   3486  CA  LYS C  95      46.930  72.895  35.136  1.00 94.30           C  
ANISOU 3486  CA  LYS C  95    19752   9133   6944  -4856   2207  -1788       C  
ATOM   3487  C   LYS C  95      45.623  73.447  35.688  1.00 92.63           C  
ANISOU 3487  C   LYS C  95    19816   8735   6642  -4611   2429  -1900       C  
ATOM   3488  O   LYS C  95      44.979  74.285  35.061  1.00117.30           O  
ANISOU 3488  O   LYS C  95    23058  11703   9807  -4422   2604  -1930       O  
ATOM   3489  CB  LYS C  95      48.026  73.956  35.236  1.00100.66           C  
ANISOU 3489  CB  LYS C  95    20838   9817   7592  -5103   2134  -1837       C  
ATOM   3490  CG  LYS C  95      48.371  74.364  36.662  1.00106.31           C  
ANISOU 3490  CG  LYS C  95    21933  10425   8036  -5274   2077  -1956       C  
ATOM   3491  CD  LYS C  95      49.427  75.454  36.672  1.00110.68           C  
ANISOU 3491  CD  LYS C  95    22760  10854   8437  -5538   2010  -2012       C  
ATOM   3492  CE  LYS C  95      48.861  76.768  36.162  1.00111.94           C  
ANISOU 3492  CE  LYS C  95    23246  10723   8565  -5418   2232  -2069       C  
ATOM   3493  NZ  LYS C  95      47.860  77.322  37.115  1.00113.85           N  
ANISOU 3493  NZ  LYS C  95    23883  10731   8643  -5254   2413  -2190       N  
ATOM   3494  N   GLY C  96      45.227  72.960  36.858  1.00 94.32           N  
ANISOU 3494  N   GLY C  96    20132   8982   6725  -4598   2423  -1962       N  
ATOM   3495  CA  GLY C  96      44.013  73.424  37.503  1.00 99.09           C  
ANISOU 3495  CA  GLY C  96    20990   9449   7209  -4360   2632  -2078       C  
ATOM   3496  C   GLY C  96      42.794  72.568  37.207  1.00103.57           C  
ANISOU 3496  C   GLY C  96    21256  10178   7921  -4089   2740  -2053       C  
ATOM   3497  O   GLY C  96      41.720  72.805  37.758  1.00107.04           O  
ANISOU 3497  O   GLY C  96    21843  10573   8254  -3866   2915  -2149       O  
ATOM   3498  N   ALA C  97      42.950  71.572  36.338  1.00 89.90           N  
ANISOU 3498  N   ALA C  97    19097   8646   6415  -4106   2642  -1929       N  
ATOM   3499  CA  ALA C  97      41.849  70.666  36.027  1.00 87.45           C  
ANISOU 3499  CA  ALA C  97    18477   8512   6239  -3889   2723  -1905       C  
ATOM   3500  C   ALA C  97      41.518  69.790  37.233  1.00 88.73           C  
ANISOU 3500  C   ALA C  97    18664   8782   6266  -3927   2695  -1939       C  
ATOM   3501  O   ALA C  97      42.410  69.377  37.972  1.00 89.48           O  
ANISOU 3501  O   ALA C  97    18840   8895   6264  -4163   2529  -1916       O  
ATOM   3502  CB  ALA C  97      42.183  69.804  34.808  1.00 82.60           C  
ANISOU 3502  CB  ALA C  97    17428   8065   5893  -3932   2615  -1766       C  
ATOM   3503  N   LYS C  98      40.235  69.500  37.419  1.00 96.49           N  
ANISOU 3503  N   LYS C  98    19570   9860   7231  -3687   2855  -1993       N  
ATOM   3504  CA  LYS C  98      39.764  68.788  38.609  1.00 97.83           C  
ANISOU 3504  CA  LYS C  98    19806  10126   7240  -3701   2870  -2039       C  
ATOM   3505  C   LYS C  98      40.205  67.319  38.702  1.00 91.02           C  
ANISOU 3505  C   LYS C  98    18679   9437   6468  -3884   2692  -1930       C  
ATOM   3506  O   LYS C  98      40.119  66.706  39.766  1.00 89.95           O  
ANISOU 3506  O   LYS C  98    18644   9351   6182  -3964   2661  -1952       O  
ATOM   3507  CB  LYS C  98      38.238  68.885  38.706  1.00106.94           C  
ANISOU 3507  CB  LYS C  98    20913  11384   8335  -3383   3105  -2123       C  
ATOM   3508  CG  LYS C  98      37.720  70.303  38.910  1.00118.87           C  
ANISOU 3508  CG  LYS C  98    22751  12721   9694  -3168   3301  -2247       C  
ATOM   3509  CD  LYS C  98      36.206  70.372  38.763  1.00123.62           C  
ANISOU 3509  CD  LYS C  98    23215  13499  10257  -2804   3534  -2309       C  
ATOM   3510  CE  LYS C  98      35.695  71.794  38.950  1.00127.20           C  
ANISOU 3510  CE  LYS C  98    24005  13774  10551  -2555   3739  -2429       C  
ATOM   3511  NZ  LYS C  98      34.230  71.901  38.702  1.00126.75           N  
ANISOU 3511  NZ  LYS C  98    23767  13942  10450  -2161   3970  -2480       N  
ATOM   3512  N   SER C  99      40.676  66.760  37.593  1.00 86.86           N  
ANISOU 3512  N   SER C  99    17832   8993   6178  -3945   2581  -1812       N  
ATOM   3513  CA  SER C  99      41.073  65.353  37.550  1.00 81.67           C  
ANISOU 3513  CA  SER C  99    16921   8487   5622  -4091   2424  -1702       C  
ATOM   3514  C   SER C  99      42.489  65.124  38.082  1.00 82.15           C  
ANISOU 3514  C   SER C  99    17093   8517   5604  -4349   2204  -1643       C  
ATOM   3515  O   SER C  99      42.838  64.006  38.460  1.00 81.32           O  
ANISOU 3515  O   SER C  99    16889   8514   5496  -4459   2075  -1573       O  
ATOM   3516  CB  SER C  99      40.958  64.819  36.115  1.00 77.37           C  
ANISOU 3516  CB  SER C  99    15986   8052   5360  -4036   2403  -1606       C  
ATOM   3517  OG  SER C  99      41.266  65.848  35.195  1.00 77.89           O  
ANISOU 3517  OG  SER C  99    16059   8018   5519  -3984   2435  -1605       O  
ATOM   3518  N   ILE C 100      43.299  66.182  38.097  1.00 83.75           N  
ANISOU 3518  N   ILE C 100    17502   8589   5730  -4436   2161  -1674       N  
ATOM   3519  CA  ILE C 100      44.667  66.114  38.617  1.00 84.88           C  
ANISOU 3519  CA  ILE C 100    17750   8736   5765  -4671   1947  -1639       C  
ATOM   3520  C   ILE C 100      44.716  65.518  40.022  1.00 87.54           C  
ANISOU 3520  C   ILE C 100    18274   9099   5888  -4757   1872  -1676       C  
ATOM   3521  O   ILE C 100      44.073  66.028  40.935  1.00 90.78           O  
ANISOU 3521  O   ILE C 100    18968   9413   6114  -4702   1994  -1790       O  
ATOM   3522  CB  ILE C 100      45.311  67.506  38.694  1.00 92.55           C  
ANISOU 3522  CB  ILE C 100    19003   9546   6617  -4758   1947  -1713       C  
ATOM   3523  CG1 ILE C 100      45.295  68.193  37.325  1.00 95.63           C  
ANISOU 3523  CG1 ILE C 100    19254   9887   7193  -4679   2027  -1677       C  
ATOM   3524  CG2 ILE C 100      46.734  67.396  39.228  1.00 91.30           C  
ANISOU 3524  CG2 ILE C 100    18916   9439   6336  -5007   1706  -1690       C  
ATOM   3525  CD1 ILE C 100      46.447  67.817  36.438  1.00 95.45           C  
ANISOU 3525  CD1 ILE C 100    18964   9992   7311  -4821   1852  -1556       C  
ATOM   3526  N   GLY C 101      45.481  64.442  40.186  1.00 86.33           N  
ANISOU 3526  N   GLY C 101    17972   9078   5752  -4877   1675  -1581       N  
ATOM   3527  CA  GLY C 101      45.603  63.773  41.469  1.00 88.75           C  
ANISOU 3527  CA  GLY C 101    18447   9417   5858  -4957   1582  -1601       C  
ATOM   3528  C   GLY C 101      44.518  62.748  41.762  1.00 93.93           C  
ANISOU 3528  C   GLY C 101    19020  10137   6533  -4854   1687  -1584       C  
ATOM   3529  O   GLY C 101      44.475  62.179  42.858  1.00 90.20           O  
ANISOU 3529  O   GLY C 101    18710   9681   5880  -4910   1638  -1603       O  
ATOM   3530  N   ARG C 102      43.636  62.509  40.796  1.00 85.14           N  
ANISOU 3530  N   ARG C 102    17659   9065   5625  -4712   1829  -1554       N  
ATOM   3531  CA  ARG C 102      42.560  61.535  40.980  1.00 87.74           C  
ANISOU 3531  CA  ARG C 102    17883   9477   5975  -4630   1933  -1547       C  
ATOM   3532  C   ARG C 102      42.793  60.287  40.126  1.00 84.36           C  
ANISOU 3532  C   ARG C 102    17127   9164   5761  -4661   1829  -1414       C  
ATOM   3533  O   ARG C 102      43.418  60.359  39.072  1.00 86.64           O  
ANISOU 3533  O   ARG C 102    17207   9475   6236  -4674   1752  -1340       O  
ATOM   3534  CB  ARG C 102      41.197  62.162  40.665  1.00 90.55           C  
ANISOU 3534  CB  ARG C 102    18216   9827   6361  -4429   2184  -1641       C  
ATOM   3535  CG  ARG C 102      40.939  63.488  41.386  1.00 95.90           C  
ANISOU 3535  CG  ARG C 102    19230  10371   6835  -4361   2308  -1778       C  
ATOM   3536  CD  ARG C 102      39.448  63.799  41.488  1.00102.87           C  
ANISOU 3536  CD  ARG C 102    20121  11303   7664  -4132   2562  -1878       C  
ATOM   3537  NE  ARG C 102      38.755  62.877  42.388  1.00104.25           N  
ANISOU 3537  NE  ARG C 102    20322  11587   7702  -4144   2613  -1893       N  
ATOM   3538  CZ  ARG C 102      37.477  62.527  42.264  1.00105.04           C  
ANISOU 3538  CZ  ARG C 102    20267  11838   7806  -3982   2791  -1927       C  
ATOM   3539  NH1 ARG C 102      36.936  61.677  43.125  1.00107.73           N  
ANISOU 3539  NH1 ARG C 102    20653  12276   8005  -4029   2831  -1935       N  
ATOM   3540  NH2 ARG C 102      36.738  63.017  41.276  1.00 98.43           N  
ANISOU 3540  NH2 ARG C 102    19227  11072   7100  -3771   2927  -1949       N  
ATOM   3541  N   THR C 103      42.303  59.140  40.584  1.00 80.91           N  
ANISOU 3541  N   THR C 103    16660   8794   5288  -4680   1831  -1384       N  
ATOM   3542  CA  THR C 103      42.528  57.893  39.852  1.00 77.79           C  
ANISOU 3542  CA  THR C 103    16000   8482   5074  -4719   1732  -1266       C  
ATOM   3543  C   THR C 103      41.423  57.652  38.830  1.00 80.47           C  
ANISOU 3543  C   THR C 103    16069   8890   5617  -4612   1885  -1275       C  
ATOM   3544  O   THR C 103      40.329  58.202  38.952  1.00 76.67           O  
ANISOU 3544  O   THR C 103    15619   8425   5086  -4495   2071  -1373       O  
ATOM   3545  CB  THR C 103      42.612  56.685  40.808  1.00 79.25           C  
ANISOU 3545  CB  THR C 103    16308   8689   5114  -4807   1644  -1224       C  
ATOM   3546  OG1 THR C 103      41.297  56.314  41.243  1.00 80.53           O  
ANISOU 3546  OG1 THR C 103    16508   8882   5208  -4765   1822  -1287       O  
ATOM   3547  CG2 THR C 103      43.480  57.014  42.015  1.00 82.52           C  
ANISOU 3547  CG2 THR C 103    17026   9051   5276  -4891   1510  -1249       C  
ATOM   3548  N   LEU C 104      41.719  56.846  37.810  1.00 72.06           N  
ANISOU 3548  N   LEU C 104    14733   7879   4768  -4639   1801  -1179       N  
ATOM   3549  CA  LEU C 104      40.717  56.477  36.816  1.00 69.84           C  
ANISOU 3549  CA  LEU C 104    14180   7678   4677  -4560   1914  -1192       C  
ATOM   3550  C   LEU C 104      39.494  55.835  37.459  1.00 75.69           C  
ANISOU 3550  C   LEU C 104    14965   8489   5303  -4544   2043  -1253       C  
ATOM   3551  O   LEU C 104      38.368  56.040  37.007  1.00 71.57           O  
ANISOU 3551  O   LEU C 104    14299   8064   4831  -4429   2197  -1320       O  
ATOM   3552  CB  LEU C 104      41.313  55.532  35.772  1.00 66.41           C  
ANISOU 3552  CB  LEU C 104    13489   7280   4463  -4623   1782  -1083       C  
ATOM   3553  CG  LEU C 104      42.332  56.145  34.811  1.00 68.91           C  
ANISOU 3553  CG  LEU C 104    13671   7578   4933  -4619   1690  -1019       C  
ATOM   3554  CD1 LEU C 104      42.698  55.157  33.697  1.00 61.35           C  
ANISOU 3554  CD1 LEU C 104    12436   6673   4199  -4656   1594   -926       C  
ATOM   3555  CD2 LEU C 104      41.812  57.450  34.231  1.00 70.24           C  
ANISOU 3555  CD2 LEU C 104    13799   7727   5161  -4499   1826  -1098       C  
ATOM   3556  N   GLY C 105      39.725  55.059  38.515  1.00 79.61           N  
ANISOU 3556  N   GLY C 105    15661   8958   5631  -4654   1979  -1227       N  
ATOM   3557  CA  GLY C 105      38.650  54.414  39.251  1.00 80.29           C  
ANISOU 3557  CA  GLY C 105    15826   9107   5574  -4672   2100  -1278       C  
ATOM   3558  C   GLY C 105      37.769  55.420  39.964  1.00 93.53           C  
ANISOU 3558  C   GLY C 105    17652  10815   7068  -4556   2288  -1399       C  
ATOM   3559  O   GLY C 105      36.541  55.336  39.909  1.00 79.77           O  
ANISOU 3559  O   GLY C 105    15811   9205   5295  -4475   2459  -1462       O  
ATOM   3560  N   GLU C 106      38.405  56.376  40.635  1.00 80.67           N  
ANISOU 3560  N   GLU C 106    16265   9083   5303  -4544   2257  -1433       N  
ATOM   3561  CA  GLU C 106      37.695  57.452  41.307  1.00 83.76           C  
ANISOU 3561  CA  GLU C 106    16837   9475   5513  -4419   2431  -1556       C  
ATOM   3562  C   GLU C 106      36.893  58.309  40.332  1.00 82.73           C  
ANISOU 3562  C   GLU C 106    16504   9422   5506  -4214   2587  -1615       C  
ATOM   3563  O   GLU C 106      35.811  58.790  40.672  1.00 91.19           O  
ANISOU 3563  O   GLU C 106    17611  10589   6449  -4059   2783  -1709       O  
ATOM   3564  CB  GLU C 106      38.682  58.320  42.092  1.00 96.61           C  
ANISOU 3564  CB  GLU C 106    18767  10953   6986  -4471   2338  -1583       C  
ATOM   3565  CG  GLU C 106      39.313  57.605  43.275  1.00 97.09           C  
ANISOU 3565  CG  GLU C 106    19071  10965   6853  -4633   2204  -1547       C  
ATOM   3566  CD  GLU C 106      40.489  58.356  43.867  1.00103.10           C  
ANISOU 3566  CD  GLU C 106    20078  11609   7488  -4709   2057  -1560       C  
ATOM   3567  OE1 GLU C 106      41.015  59.270  43.192  1.00 97.88           O  
ANISOU 3567  OE1 GLU C 106    19365  10895   6930  -4675   2026  -1568       O  
ATOM   3568  OE2 GLU C 106      40.886  58.035  45.010  1.00101.52           O  
ANISOU 3568  OE2 GLU C 106    20127  11374   7071  -4811   1968  -1564       O  
ATOM   3569  N   LEU C 107      37.427  58.499  39.126  1.00 79.42           N  
ANISOU 3569  N   LEU C 107    15875   8979   5323  -4197   2502  -1557       N  
ATOM   3570  CA  LEU C 107      36.737  59.264  38.093  1.00 78.27           C  
ANISOU 3570  CA  LEU C 107    15530   8906   5305  -3994   2629  -1599       C  
ATOM   3571  C   LEU C 107      35.629  58.457  37.404  1.00 81.64           C  
ANISOU 3571  C   LEU C 107    15645   9541   5832  -3922   2717  -1590       C  
ATOM   3572  O   LEU C 107      34.699  59.034  36.842  1.00 77.35           O  
ANISOU 3572  O   LEU C 107    14954   9129   5306  -3708   2868  -1640       O  
ATOM   3573  CB  LEU C 107      37.732  59.786  37.043  1.00 79.00           C  
ANISOU 3573  CB  LEU C 107    15521   8894   5600  -4015   2507  -1539       C  
ATOM   3574  CG  LEU C 107      38.698  60.873  37.513  1.00 76.88           C  
ANISOU 3574  CG  LEU C 107    15535   8448   5230  -4059   2451  -1562       C  
ATOM   3575  CD1 LEU C 107      39.719  61.171  36.426  1.00 83.05           C  
ANISOU 3575  CD1 LEU C 107    16178   9165   6213  -4118   2324  -1481       C  
ATOM   3576  CD2 LEU C 107      37.938  62.127  37.885  1.00 79.89           C  
ANISOU 3576  CD2 LEU C 107    16107   8789   5457  -3862   2644  -1687       C  
ATOM   3577  N   ASP C 108      35.741  57.130  37.435  1.00 75.88           N  
ANISOU 3577  N   ASP C 108    14826   8851   5156  -4095   2620  -1524       N  
ATOM   3578  CA  ASP C 108      34.687  56.252  36.924  1.00 75.30           C  
ANISOU 3578  CA  ASP C 108    14494   8975   5141  -4078   2696  -1523       C  
ATOM   3579  C   ASP C 108      34.367  56.544  35.464  1.00 77.10           C  
ANISOU 3579  C   ASP C 108    14403   9304   5588  -3942   2710  -1512       C  
ATOM   3580  O   ASP C 108      33.209  56.463  35.039  1.00 76.03           O  
ANISOU 3580  O   ASP C 108    14060   9385   5441  -3810   2843  -1543       O  
ATOM   3581  CB  ASP C 108      33.417  56.382  37.783  1.00 79.02           C  
ANISOU 3581  CB  ASP C 108    15037   9614   5375  -3970   2906  -1606       C  
ATOM   3582  CG  ASP C 108      33.017  55.077  38.431  1.00 80.26           C  
ANISOU 3582  CG  ASP C 108    15224   9838   5433  -4155   2906  -1587       C  
ATOM   3583  OD1 ASP C 108      33.273  54.016  37.825  1.00 77.94           O  
ANISOU 3583  OD1 ASP C 108    14784   9536   5293  -4308   2786  -1522       O  
ATOM   3584  OD2 ASP C 108      32.446  55.114  39.553  1.00 83.74           O  
ANISOU 3584  OD2 ASP C 108    15853  10332   5632  -4150   3029  -1642       O  
ATOM   3585  N   VAL C 109      35.415  56.883  34.714  1.00 76.97           N  
ANISOU 3585  N   VAL C 109    14346   9147   5752  -3976   2573  -1461       N  
ATOM   3586  CA  VAL C 109      35.313  57.292  33.318  1.00 71.46           C  
ANISOU 3586  CA  VAL C 109    13384   8505   5262  -3853   2568  -1448       C  
ATOM   3587  C   VAL C 109      34.479  56.343  32.456  1.00 70.58           C  
ANISOU 3587  C   VAL C 109    12960   8591   5266  -3853   2576  -1437       C  
ATOM   3588  O   VAL C 109      33.477  56.755  31.870  1.00 73.84           O  
ANISOU 3588  O   VAL C 109    13187   9192   5678  -3653   2703  -1467       O  
ATOM   3589  CB  VAL C 109      36.719  57.470  32.708  1.00 73.08           C  
ANISOU 3589  CB  VAL C 109    13592   8533   5643  -3964   2391  -1377       C  
ATOM   3590  CG1 VAL C 109      36.637  57.885  31.240  1.00 61.77           C  
ANISOU 3590  CG1 VAL C 109    11897   7149   4423  -3848   2384  -1366       C  
ATOM   3591  CG2 VAL C 109      37.517  58.494  33.519  1.00 70.05           C  
ANISOU 3591  CG2 VAL C 109    13515   7978   5121  -3974   2384  -1390       C  
ATOM   3592  N   ARG C 110      34.874  55.077  32.387  1.00 64.38           N  
ANISOU 3592  N   ARG C 110    12125   7776   4562  -4066   2443  -1391       N  
ATOM   3593  CA  ARG C 110      34.186  54.155  31.488  1.00 63.69           C  
ANISOU 3593  CA  ARG C 110    11757   7851   4589  -4099   2426  -1390       C  
ATOM   3594  C   ARG C 110      32.743  53.915  31.909  1.00 72.73           C  
ANISOU 3594  C   ARG C 110    12837   9234   5562  -4029   2601  -1440       C  
ATOM   3595  O   ARG C 110      31.862  53.746  31.067  1.00 71.53           O  
ANISOU 3595  O   ARG C 110    12421   9295   5463  -3944   2655  -1451       O  
ATOM   3596  CB  ARG C 110      34.935  52.826  31.362  1.00 63.84           C  
ANISOU 3596  CB  ARG C 110    11780   7767   4711  -4339   2250  -1340       C  
ATOM   3597  CG  ARG C 110      34.288  51.831  30.398  1.00 61.65           C  
ANISOU 3597  CG  ARG C 110    11244   7635   4545  -4400   2214  -1358       C  
ATOM   3598  CD  ARG C 110      34.037  52.459  29.037  1.00 76.39           C  
ANISOU 3598  CD  ARG C 110    12836   9610   6578  -4238   2211  -1372       C  
ATOM   3599  NE  ARG C 110      33.659  51.452  28.048  1.00 90.07           N  
ANISOU 3599  NE  ARG C 110    14342  11457   8425  -4324   2129  -1389       N  
ATOM   3600  CZ  ARG C 110      32.419  51.017  27.852  1.00 90.13           C  
ANISOU 3600  CZ  ARG C 110    14194  11698   8352  -4312   2221  -1427       C  
ATOM   3601  NH1 ARG C 110      32.181  50.097  26.931  1.00 88.10           N  
ANISOU 3601  NH1 ARG C 110    13757  11528   8190  -4415   2124  -1449       N  
ATOM   3602  NH2 ARG C 110      31.416  51.499  28.575  1.00 90.25           N  
ANISOU 3602  NH2 ARG C 110    14234  11877   8178  -4199   2410  -1442       N  
ATOM   3603  N   GLN C 111      32.497  53.916  33.210  1.00 77.97           N  
ANISOU 3603  N   GLN C 111    13736   9884   6005  -4063   2693  -1467       N  
ATOM   3604  CA  GLN C 111      31.157  53.632  33.698  1.00 82.44           C  
ANISOU 3604  CA  GLN C 111    14245  10692   6386  -4018   2869  -1509       C  
ATOM   3605  C   GLN C 111      30.165  54.752  33.405  1.00 75.63           C  
ANISOU 3605  C   GLN C 111    13241  10053   5442  -3704   3060  -1541       C  
ATOM   3606  O   GLN C 111      29.105  54.511  32.832  1.00 76.51           O  
ANISOU 3606  O   GLN C 111    13093  10437   5541  -3616   3155  -1539       O  
ATOM   3607  CB  GLN C 111      31.154  53.323  35.191  1.00 74.99           C  
ANISOU 3607  CB  GLN C 111    13602   9678   5213  -4139   2922  -1531       C  
ATOM   3608  CG  GLN C 111      29.771  52.941  35.664  1.00 78.25           C  
ANISOU 3608  CG  GLN C 111    13940  10361   5432  -4121   3108  -1572       C  
ATOM   3609  CD  GLN C 111      29.740  52.439  37.099  1.00 81.27           C  
ANISOU 3609  CD  GLN C 111    14616  10674   5587  -4281   3153  -1593       C  
ATOM   3610  OE1 GLN C 111      30.611  52.760  37.901  1.00 81.66           O  
ANISOU 3610  OE1 GLN C 111    14951  10504   5574  -4320   3087  -1589       O  
ATOM   3611  NE2 GLN C 111      28.737  51.635  37.416  1.00 83.57           N  
ANISOU 3611  NE2 GLN C 111    14843  11163   5748  -4386   3262  -1612       N  
ATOM   3612  N   ASN C 112      30.513  55.972  33.797  1.00 74.50           N  
ANISOU 3612  N   ASN C 112    13277   9802   5229  -3530   3117  -1568       N  
ATOM   3613  CA  ASN C 112      29.601  57.097  33.654  1.00 76.62           C  
ANISOU 3613  CA  ASN C 112    13465  10266   5381  -3196   3314  -1601       C  
ATOM   3614  C   ASN C 112      29.583  57.783  32.283  1.00 90.72           C  
ANISOU 3614  C   ASN C 112    15020  12110   7340  -2989   3300  -1566       C  
ATOM   3615  O   ASN C 112      28.682  58.575  32.007  1.00 76.23           O  
ANISOU 3615  O   ASN C 112    13064  10494   5406  -2682   3469  -1573       O  
ATOM   3616  CB  ASN C 112      29.855  58.123  34.759  1.00 79.28           C  
ANISOU 3616  CB  ASN C 112    14133  10465   5526  -3090   3403  -1667       C  
ATOM   3617  CG  ASN C 112      29.602  57.557  36.147  1.00 84.83           C  
ANISOU 3617  CG  ASN C 112    15050  11174   6006  -3236   3462  -1707       C  
ATOM   3618  OD1 ASN C 112      28.756  56.680  36.323  1.00 84.79           O  
ANISOU 3618  OD1 ASN C 112    14911  11381   5923  -3307   3532  -1698       O  
ATOM   3619  ND2 ASN C 112      30.339  58.049  37.134  1.00 83.57           N  
ANISOU 3619  ND2 ASN C 112    15232  10784   5736  -3297   3431  -1748       N  
ATOM   3620  N   TYR C 113      30.556  57.480  31.425  1.00 74.97           N  
ANISOU 3620  N   TYR C 113    12961   9936   5588  -3138   3106  -1523       N  
ATOM   3621  CA  TYR C 113      30.645  58.158  30.133  1.00 78.85           C  
ANISOU 3621  CA  TYR C 113    13263  10452   6244  -2960   3084  -1490       C  
ATOM   3622  C   TYR C 113      30.709  57.223  28.919  1.00 76.40           C  
ANISOU 3622  C   TYR C 113    12664  10213   6153  -3084   2943  -1440       C  
ATOM   3623  O   TYR C 113      30.560  57.679  27.787  1.00 86.62           O  
ANISOU 3623  O   TYR C 113    13761  11586   7563  -2922   2940  -1406       O  
ATOM   3624  CB  TYR C 113      31.839  59.122  30.117  1.00 77.70           C  
ANISOU 3624  CB  TYR C 113    13344  10004   6174  -2963   3006  -1498       C  
ATOM   3625  CG  TYR C 113      31.740  60.239  31.136  1.00 78.96           C  
ANISOU 3625  CG  TYR C 113    13798  10085   6119  -2809   3147  -1564       C  
ATOM   3626  CD1 TYR C 113      32.167  60.051  32.448  1.00 78.42           C  
ANISOU 3626  CD1 TYR C 113    14021   9871   5905  -2977   3130  -1603       C  
ATOM   3627  CD2 TYR C 113      31.220  61.481  30.789  1.00 82.71           C  
ANISOU 3627  CD2 TYR C 113    14275  10628   6521  -2490   3297  -1590       C  
ATOM   3628  CE1 TYR C 113      32.077  61.066  33.386  1.00 85.26           C  
ANISOU 3628  CE1 TYR C 113    15175  10656   6565  -2847   3253  -1678       C  
ATOM   3629  CE2 TYR C 113      31.118  62.504  31.731  1.00 87.14           C  
ANISOU 3629  CE2 TYR C 113    15132  11101   6875  -2350   3429  -1671       C  
ATOM   3630  CZ  TYR C 113      31.553  62.291  33.024  1.00 86.99           C  
ANISOU 3630  CZ  TYR C 113    15402  10929   6721  -2538   3403  -1719       C  
ATOM   3631  OH  TYR C 113      31.460  63.301  33.960  1.00 80.44           O  
ANISOU 3631  OH  TYR C 113    14884  10000   5680  -2410   3528  -1810       O  
ATOM   3632  N   ASP C 114      30.907  55.927  29.155  1.00 69.62           N  
ANISOU 3632  N   ASP C 114    11795   9324   5333  -3364   2830  -1439       N  
ATOM   3633  CA  ASP C 114      31.188  54.967  28.085  1.00 67.32           C  
ANISOU 3633  CA  ASP C 114    11291   9040   5247  -3525   2663  -1415       C  
ATOM   3634  C   ASP C 114      32.417  55.391  27.280  1.00 68.59           C  
ANISOU 3634  C   ASP C 114    11462   8980   5621  -3546   2507  -1391       C  
ATOM   3635  O   ASP C 114      32.433  55.288  26.051  1.00 69.18           O  
ANISOU 3635  O   ASP C 114    11313   9115   5857  -3509   2429  -1375       O  
ATOM   3636  CB  ASP C 114      29.992  54.776  27.141  1.00 72.94           C  
ANISOU 3636  CB  ASP C 114    11681  10069   5965  -3390   2737  -1399       C  
ATOM   3637  CG  ASP C 114      28.808  54.124  27.818  1.00 87.40           C  
ANISOU 3637  CG  ASP C 114    13461  12145   7600  -3433   2871  -1417       C  
ATOM   3638  OD1 ASP C 114      28.993  53.517  28.893  1.00 92.15           O  
ANISOU 3638  OD1 ASP C 114    14270  12647   8098  -3629   2867  -1448       O  
ATOM   3639  OD2 ASP C 114      27.690  54.215  27.269  1.00 90.48           O  
ANISOU 3639  OD2 ASP C 114    13606  12840   7932  -3273   2984  -1392       O  
ATOM   3640  N   VAL C 115      33.435  55.880  27.976  1.00 68.79           N  
ANISOU 3640  N   VAL C 115    11745   8762   5631  -3612   2466  -1388       N  
ATOM   3641  CA  VAL C 115      34.694  56.251  27.333  1.00 71.79           C  
ANISOU 3641  CA  VAL C 115    12147   8937   6192  -3671   2322  -1357       C  
ATOM   3642  C   VAL C 115      35.830  55.458  27.961  1.00 71.60           C  
ANISOU 3642  C   VAL C 115    12285   8726   6193  -3930   2173  -1323       C  
ATOM   3643  O   VAL C 115      35.983  55.443  29.177  1.00 63.53           O  
ANISOU 3643  O   VAL C 115    11501   7629   5008  -3996   2211  -1322       O  
ATOM   3644  CB  VAL C 115      34.990  57.761  27.487  1.00 66.50           C  
ANISOU 3644  CB  VAL C 115    11641   8155   5469  -3499   2413  -1362       C  
ATOM   3645  CG1 VAL C 115      36.427  58.066  27.094  1.00 68.98           C  
ANISOU 3645  CG1 VAL C 115    12028   8247   5933  -3632   2267  -1321       C  
ATOM   3646  CG2 VAL C 115      34.012  58.583  26.653  1.00 62.42           C  
ANISOU 3646  CG2 VAL C 115    10954   7817   4948  -3206   2549  -1371       C  
ATOM   3647  N   THR C 116      36.624  54.787  27.135  1.00 57.44           N  
ANISOU 3647  N   THR C 116     9191   8109   4526  -1747   1230  -1562       N  
ATOM   3648  CA  THR C 116      37.742  54.016  27.656  1.00 51.19           C  
ANISOU 3648  CA  THR C 116     8588   7233   3629  -2085   1214  -1335       C  
ATOM   3649  C   THR C 116      39.041  54.800  27.509  1.00 58.31           C  
ANISOU 3649  C   THR C 116     9666   8040   4451  -2150   1036  -1175       C  
ATOM   3650  O   THR C 116      39.362  55.267  26.411  1.00 57.01           O  
ANISOU 3650  O   THR C 116     9446   7827   4387  -1978   1054  -1208       O  
ATOM   3651  CB  THR C 116      37.874  52.678  26.900  1.00 56.24           C  
ANISOU 3651  CB  THR C 116     9119   7868   4383  -2135   1366  -1317       C  
ATOM   3652  OG1 THR C 116      36.664  51.926  27.052  1.00 58.31           O  
ANISOU 3652  OG1 THR C 116     9223   8202   4728  -2162   1548  -1499       O  
ATOM   3653  CG2 THR C 116      39.046  51.867  27.438  1.00 54.36           C  
ANISOU 3653  CG2 THR C 116     9015   7510   4131  -2332   1268   -974       C  
ATOM   3654  N   VAL C 117      39.795  54.956  28.595  1.00 51.24           N  
ANISOU 3654  N   VAL C 117     8996   7108   3365  -2400    861  -1010       N  
ATOM   3655  CA  VAL C 117      41.154  55.479  28.442  1.00 54.70           C  
ANISOU 3655  CA  VAL C 117     9401   7428   3953  -2454    630   -796       C  
ATOM   3656  C   VAL C 117      42.029  54.327  27.961  1.00 47.37           C  
ANISOU 3656  C   VAL C 117     8227   6456   3314  -2426    599   -541       C  
ATOM   3657  O   VAL C 117      42.265  53.376  28.715  1.00 48.56           O  
ANISOU 3657  O   VAL C 117     8420   6608   3421  -2511    525   -387       O  
ATOM   3658  CB  VAL C 117      41.731  56.034  29.760  1.00 55.31           C  
ANISOU 3658  CB  VAL C 117     9701   7475   3839  -2665    357   -710       C  
ATOM   3659  CG1 VAL C 117      43.135  56.597  29.524  1.00 55.47           C  
ANISOU 3659  CG1 VAL C 117     9592   7401   4085  -2761    122   -549       C  
ATOM   3660  CG2 VAL C 117      40.814  57.105  30.335  1.00 59.42           C  
ANISOU 3660  CG2 VAL C 117    10452   8004   4121  -2618    390   -925       C  
ATOM   3661  N   ILE C 118      42.482  54.385  26.705  1.00 46.13           N  
ANISOU 3661  N   ILE C 118     7868   6244   3417  -2266    677   -496       N  
ATOM   3662  CA  ILE C 118      43.232  53.265  26.151  1.00 51.59           C  
ANISOU 3662  CA  ILE C 118     8334   6902   4365  -2179    679   -270       C  
ATOM   3663  C   ILE C 118      44.746  53.417  26.361  1.00 56.87           C  
ANISOU 3663  C   ILE C 118     8840   7546   5220  -2271    445    -22       C  
ATOM   3664  O   ILE C 118      45.496  52.441  26.263  1.00 48.50           O  
ANISOU 3664  O   ILE C 118     7613   6495   4319  -2198    375    188       O  
ATOM   3665  CB  ILE C 118      42.871  53.002  24.647  1.00 53.37           C  
ANISOU 3665  CB  ILE C 118     8427   7089   4762  -1906    910   -353       C  
ATOM   3666  CG1 ILE C 118      43.230  54.203  23.772  1.00 43.70           C  
ANISOU 3666  CG1 ILE C 118     7209   5782   3613  -1796    970   -401       C  
ATOM   3667  CG2 ILE C 118      41.383  52.679  24.516  1.00 49.78           C  
ANISOU 3667  CG2 ILE C 118     8048   6712   4152  -1826   1091   -647       C  
ATOM   3668  CD1 ILE C 118      43.173  53.913  22.210  1.00 47.10           C  
ANISOU 3668  CD1 ILE C 118     7549   6134   4211  -1460   1178   -421       C  
ATOM   3669  N   ALA C 119      45.181  54.634  26.680  1.00 48.97           N  
ANISOU 3669  N   ALA C 119     7889   6523   4195  -2429    317    -70       N  
ATOM   3670  CA  ALA C 119      46.595  54.904  26.942  1.00 56.06           C  
ANISOU 3670  CA  ALA C 119     8572   7431   5296  -2576     79     93       C  
ATOM   3671  C   ALA C 119      46.783  56.176  27.738  1.00 55.66           C  
ANISOU 3671  C   ALA C 119     8688   7349   5114  -2832   -109    -27       C  
ATOM   3672  O   ALA C 119      45.934  57.073  27.708  1.00 56.00           O  
ANISOU 3672  O   ALA C 119     9012   7316   4950  -2847     13   -219       O  
ATOM   3673  CB  ALA C 119      47.381  55.019  25.622  1.00 57.09           C  
ANISOU 3673  CB  ALA C 119     8416   7503   5772  -2473    255    197       C  
ATOM   3674  N   ILE C 120      47.913  56.264  28.432  1.00 57.12           N  
ANISOU 3674  N   ILE C 120     8697   7594   5411  -3011   -427     62       N  
ATOM   3675  CA  ILE C 120      48.319  57.505  29.086  1.00 59.04           C  
ANISOU 3675  CA  ILE C 120     9049   7785   5598  -3295   -638    -64       C  
ATOM   3676  C   ILE C 120      49.737  57.858  28.650  1.00 61.95           C  
ANISOU 3676  C   ILE C 120     8997   8171   6371  -3476   -729      6       C  
ATOM   3677  O   ILE C 120      50.657  57.048  28.767  1.00 71.59           O  
ANISOU 3677  O   ILE C 120     9848   9550   7801  -3424   -918    144       O  
ATOM   3678  CB  ILE C 120      48.239  57.394  30.631  1.00 61.11           C  
ANISOU 3678  CB  ILE C 120     9546   8123   5551  -3380  -1008   -106       C  
ATOM   3679  CG1 ILE C 120      46.796  57.141  31.072  1.00 58.81           C  
ANISOU 3679  CG1 ILE C 120     9667   7810   4867  -3245   -837   -193       C  
ATOM   3680  CG2 ILE C 120      48.801  58.655  31.303  1.00 64.37           C  
ANISOU 3680  CG2 ILE C 120    10053   8475   5931  -3685  -1285   -254       C  
ATOM   3681  CD1 ILE C 120      46.657  56.808  32.548  1.00 61.00           C  
ANISOU 3681  CD1 ILE C 120    10236   8139   4804  -3266  -1119   -191       C  
ATOM   3682  N   ILE C 121      49.909  59.061  28.118  1.00 62.81           N  
ANISOU 3682  N   ILE C 121     9169   8111   6584  -3678   -565    -99       N  
ATOM   3683  CA  ILE C 121      51.227  59.513  27.707  1.00 66.30           C  
ANISOU 3683  CA  ILE C 121     9207   8549   7434  -3933   -579    -66       C  
ATOM   3684  C   ILE C 121      51.718  60.596  28.656  1.00 70.25           C  
ANISOU 3684  C   ILE C 121     9796   8998   7898  -4335   -889   -246       C  
ATOM   3685  O   ILE C 121      51.087  61.643  28.797  1.00 70.00           O  
ANISOU 3685  O   ILE C 121    10220   8751   7627  -4463   -802   -399       O  
ATOM   3686  CB  ILE C 121      51.217  60.049  26.271  1.00 68.67           C  
ANISOU 3686  CB  ILE C 121     9528   8639   7924  -3898    -89    -37       C  
ATOM   3687  CG1 ILE C 121      50.614  59.006  25.322  1.00 67.33           C  
ANISOU 3687  CG1 ILE C 121     9335   8504   7743  -3464    187    101       C  
ATOM   3688  CG2 ILE C 121      52.627  60.443  25.842  1.00 81.52           C  
ANISOU 3688  CG2 ILE C 121    10693  10269  10011  -4201    -30      5       C  
ATOM   3689  CD1 ILE C 121      50.596  59.437  23.872  1.00 66.48           C  
ANISOU 3689  CD1 ILE C 121     9300   8184   7776  -3336    658    137       C  
ATOM   3690  N   LYS C 122      52.836  60.334  29.321  1.00 80.72           N  
ANISOU 3690  N   LYS C 122    10700  10528   9444  -4506  -1277   -251       N  
ATOM   3691  CA  LYS C 122      53.409  61.313  30.237  1.00 89.18           C  
ANISOU 3691  CA  LYS C 122    11798  11570  10518  -4907  -1634   -460       C  
ATOM   3692  C   LYS C 122      54.259  62.301  29.457  1.00 94.84           C  
ANISOU 3692  C   LYS C 122    12262  12132  11643  -5312  -1387   -539       C  
ATOM   3693  O   LYS C 122      54.721  61.988  28.361  1.00 96.98           O  
ANISOU 3693  O   LYS C 122    12180  12417  12253  -5255  -1034   -401       O  
ATOM   3694  CB  LYS C 122      54.221  60.622  31.334  1.00 89.87           C  
ANISOU 3694  CB  LYS C 122    11549  11961  10636  -4879  -2211   -484       C  
ATOM   3695  CG  LYS C 122      53.372  59.752  32.257  1.00 84.95           C  
ANISOU 3695  CG  LYS C 122    11315  11418   9543  -4519  -2431   -414       C  
ATOM   3696  CD  LYS C 122      54.168  59.273  33.458  1.00 97.64           C  
ANISOU 3696  CD  LYS C 122    12743  13269  11087  -4467  -3044   -476       C  
ATOM   3697  CE  LYS C 122      53.310  58.420  34.376  1.00 98.70           C  
ANISOU 3697  CE  LYS C 122    13369  13419  10713  -4110  -3187   -385       C  
ATOM   3698  NZ  LYS C 122      54.056  58.014  35.600  1.00 87.27           N  
ANISOU 3698  NZ  LYS C 122    11873  12169   9118  -3994  -3806   -457       N  
ATOM   3699  N   HIS C 123      54.459  63.490  30.024  1.00104.08           N  
ANISOU 3699  N   HIS C 123    13650  13128  12767  -5727  -1547   -762       N  
ATOM   3700  CA  HIS C 123      55.129  64.589  29.325  1.00109.64           C  
ANISOU 3700  CA  HIS C 123    14267  13586  13806  -6187  -1238   -863       C  
ATOM   3701  C   HIS C 123      56.513  64.227  28.780  1.00113.69           C  
ANISOU 3701  C   HIS C 123    13959  14315  14922  -6397  -1181   -821       C  
ATOM   3702  O   HIS C 123      57.005  64.868  27.853  1.00108.24           O  
ANISOU 3702  O   HIS C 123    13154  13419  14553  -6692   -730   -822       O  
ATOM   3703  CB  HIS C 123      55.215  65.836  30.221  1.00117.79           C  
ANISOU 3703  CB  HIS C 123    15657  14408  14690  -6636  -1515  -1141       C  
ATOM   3704  CG  HIS C 123      56.462  65.910  31.049  1.00117.14           C  
ANISOU 3704  CG  HIS C 123    15003  14564  14942  -6960  -2012  -1328       C  
ATOM   3705  ND1 HIS C 123      57.616  66.521  30.606  1.00117.38           N  
ANISOU 3705  ND1 HIS C 123    14543  14546  15511  -7324  -1846  -1436       N  
ATOM   3706  CD2 HIS C 123      56.734  65.457  32.296  1.00114.34           C  
ANISOU 3706  CD2 HIS C 123    14492  14493  14457  -6861  -2654  -1441       C  
ATOM   3707  CE1 HIS C 123      58.545  66.436  31.541  1.00118.77           C  
ANISOU 3707  CE1 HIS C 123    14229  14993  15906  -7457  -2392  -1641       C  
ATOM   3708  NE2 HIS C 123      58.035  65.795  32.577  1.00114.86           N  
ANISOU 3708  NE2 HIS C 123    13950  14701  14992  -7155  -2900  -1645       N  
ATOM   3709  N   ASN C 124      57.129  63.196  29.353  1.00120.37           N  
ANISOU 3709  N   ASN C 124    14264  15572  15898  -6216  -1614   -787       N  
ATOM   3710  CA  ASN C 124      58.433  62.725  28.900  1.00127.10           C  
ANISOU 3710  CA  ASN C 124    14273  16715  17303  -6322  -1607   -761       C  
ATOM   3711  C   ASN C 124      58.327  61.842  27.661  1.00126.70           C  
ANISOU 3711  C   ASN C 124    14048  16702  17390  -5921  -1121   -467       C  
ATOM   3712  O   ASN C 124      59.325  61.282  27.202  1.00126.17           O  
ANISOU 3712  O   ASN C 124    13296  16900  17743  -5891  -1069   -402       O  
ATOM   3713  CB  ASN C 124      59.147  61.964  30.021  1.00131.61           C  
ANISOU 3713  CB  ASN C 124    14372  17727  17908  -6195  -2310   -863       C  
ATOM   3714  CG  ASN C 124      58.517  60.611  30.307  1.00131.49           C  
ANISOU 3714  CG  ASN C 124    14535  17888  17536  -5556  -2482   -639       C  
ATOM   3715  OD1 ASN C 124      57.331  60.392  30.049  1.00130.60           O  
ANISOU 3715  OD1 ASN C 124    15008  17558  17055  -5281  -2207   -483       O  
ATOM   3716  ND2 ASN C 124      59.311  59.695  30.849  1.00134.07           N  
ANISOU 3716  ND2 ASN C 124    14366  18608  17966  -5314  -2939   -645       N  
ATOM   3717  N   GLN C 125      57.108  61.732  27.134  1.00125.84           N  
ANISOU 3717  N   GLN C 125    14556  16340  16920  -5596   -782   -317       N  
ATOM   3718  CA  GLN C 125      56.789  60.835  26.025  1.00124.12           C  
ANISOU 3718  CA  GLN C 125    14299  16129  16732  -5147   -377    -60       C  
ATOM   3719  C   GLN C 125      57.092  59.382  26.389  1.00127.62           C  
ANISOU 3719  C   GLN C 125    14352  16949  17189  -4740   -713     78       C  
ATOM   3720  O   GLN C 125      58.140  58.843  26.033  1.00135.04           O  
ANISOU 3720  O   GLN C 125    14662  18139  18510  -4695   -715    148       O  
ATOM   3721  CB  GLN C 125      57.519  61.247  24.740  1.00128.35           C  
ANISOU 3721  CB  GLN C 125    14543  16531  17695  -5323    184     13       C  
ATOM   3722  CG  GLN C 125      57.109  60.455  23.504  1.00126.26           C  
ANISOU 3722  CG  GLN C 125    14358  16205  17411  -4834    635    263       C  
ATOM   3723  CD  GLN C 125      58.036  60.693  22.322  1.00130.64           C  
ANISOU 3723  CD  GLN C 125    14541  16686  18410  -4967   1165    358       C  
ATOM   3724  OE1 GLN C 125      58.926  61.544  22.375  1.00134.68           O  
ANISOU 3724  OE1 GLN C 125    14755  17157  19259  -5486   1266    225       O  
ATOM   3725  NE2 GLN C 125      57.831  59.935  21.249  1.00127.68           N  
ANISOU 3725  NE2 GLN C 125    14191  16284  18039  -4511   1526    577       N  
ATOM   3726  N   GLU C 126      56.169  58.765  27.119  1.00122.65           N  
ANISOU 3726  N   GLU C 126    14128  16347  16125  -4440   -977    109       N  
ATOM   3727  CA  GLU C 126      56.269  57.357  27.486  1.00119.27           C  
ANISOU 3727  CA  GLU C 126    13526  16185  15606  -4018  -1249    256       C  
ATOM   3728  C   GLU C 126      54.860  56.794  27.640  1.00107.90           C  
ANISOU 3728  C   GLU C 126    12695  14600  13701  -3701  -1163    337       C  
ATOM   3729  O   GLU C 126      54.112  57.206  28.528  1.00107.07           O  
ANISOU 3729  O   GLU C 126    13033  14404  13243  -3793  -1350    215       O  
ATOM   3730  CB  GLU C 126      57.050  57.191  28.791  1.00124.53           C  
ANISOU 3730  CB  GLU C 126    13922  17133  16260  -4096  -1885    123       C  
ATOM   3731  CG  GLU C 126      57.299  55.743  29.184  1.00125.90           C  
ANISOU 3731  CG  GLU C 126    13954  17566  16318  -3618  -2178    275       C  
ATOM   3732  CD  GLU C 126      57.814  55.604  30.605  1.00130.43           C  
ANISOU 3732  CD  GLU C 126    14472  18367  16719  -3598  -2845    124       C  
ATOM   3733  OE1 GLU C 126      58.648  54.708  30.854  1.00132.54           O  
ANISOU 3733  OE1 GLU C 126    14356  18931  17072  -3290  -3161    171       O  
ATOM   3734  OE2 GLU C 126      57.379  56.386  31.476  1.00131.17           O  
ANISOU 3734  OE2 GLU C 126    14941  18339  16558  -3843  -3069    -51       O  
ATOM   3735  N   LYS C 127      54.497  55.852  26.776  1.00 95.21           N  
ANISOU 3735  N   LYS C 127    11101  12973  12100  -3338   -870    523       N  
ATOM   3736  CA  LYS C 127      53.104  55.422  26.682  1.00 82.87           C  
ANISOU 3736  CA  LYS C 127    10062  11254  10171  -3102   -689    553       C  
ATOM   3737  C   LYS C 127      52.777  54.205  27.548  1.00 76.67           C  
ANISOU 3737  C   LYS C 127     9440  10584   9108  -2840   -962    638       C  
ATOM   3738  O   LYS C 127      53.356  53.128  27.381  1.00 71.47           O  
ANISOU 3738  O   LYS C 127     8538  10059   8556  -2573  -1036    798       O  
ATOM   3739  CB  LYS C 127      52.711  55.177  25.216  1.00 77.42           C  
ANISOU 3739  CB  LYS C 127     9395  10421   9601  -2871   -198    656       C  
ATOM   3740  CG  LYS C 127      51.210  55.249  24.945  1.00 74.48           C  
ANISOU 3740  CG  LYS C 127     9533   9865   8901  -2731     34    570       C  
ATOM   3741  CD  LYS C 127      50.898  55.449  23.453  1.00 73.53           C  
ANISOU 3741  CD  LYS C 127     9472   9571   8894  -2540    489    594       C  
ATOM   3742  CE  LYS C 127      51.324  54.247  22.614  1.00 78.05           C  
ANISOU 3742  CE  LYS C 127     9785  10211   9660  -2210    620    793       C  
ATOM   3743  NZ  LYS C 127      50.933  54.357  21.173  1.00 70.27           N  
ANISOU 3743  NZ  LYS C 127     8932   9044   8724  -1955   1041    806       N  
ATOM   3744  N   LEU C 128      51.850  54.402  28.482  1.00 64.88           N  
ANISOU 3744  N   LEU C 128     8401   9016   7233  -2907  -1086    531       N  
ATOM   3745  CA  LEU C 128      51.285  53.318  29.276  1.00 64.21           C  
ANISOU 3745  CA  LEU C 128     8622   8955   6820  -2687  -1220    606       C  
ATOM   3746  C   LEU C 128      50.017  52.818  28.596  1.00 67.39           C  
ANISOU 3746  C   LEU C 128     9310   9210   7084  -2533   -816    620       C  
ATOM   3747  O   LEU C 128      49.025  53.543  28.513  1.00 57.77           O  
ANISOU 3747  O   LEU C 128     8356   7884   5709  -2644   -625    464       O  
ATOM   3748  CB  LEU C 128      50.963  53.809  30.690  1.00 65.94           C  
ANISOU 3748  CB  LEU C 128     9194   9170   6688  -2846  -1535    473       C  
ATOM   3749  CG  LEU C 128      50.065  52.950  31.596  1.00 65.23           C  
ANISOU 3749  CG  LEU C 128     9591   9025   6169  -2686  -1556    516       C  
ATOM   3750  CD1 LEU C 128      50.542  51.507  31.674  1.00 66.50           C  
ANISOU 3750  CD1 LEU C 128     9709   9244   6314  -2374  -1648    721       C  
ATOM   3751  CD2 LEU C 128      49.963  53.567  33.003  1.00 67.82           C  
ANISOU 3751  CD2 LEU C 128    10257   9353   6157  -2825  -1894    387       C  
ATOM   3752  N   LEU C 129      50.052  51.586  28.097  1.00 65.36           N  
ANISOU 3752  N   LEU C 129     8994   8957   6882  -2262   -699    781       N  
ATOM   3753  CA  LEU C 129      48.906  51.027  27.388  1.00 62.32           C  
ANISOU 3753  CA  LEU C 129     8826   8442   6411  -2129   -339    759       C  
ATOM   3754  C   LEU C 129      47.924  50.457  28.386  1.00 63.83           C  
ANISOU 3754  C   LEU C 129     9444   8576   6231  -2156   -347    712       C  
ATOM   3755  O   LEU C 129      48.324  49.940  29.433  1.00 59.85           O  
ANISOU 3755  O   LEU C 129     9091   8105   5544  -2126   -607    805       O  
ATOM   3756  CB  LEU C 129      49.329  49.909  26.425  1.00 55.15           C  
ANISOU 3756  CB  LEU C 129     7729   7522   5702  -1838   -200    938       C  
ATOM   3757  CG  LEU C 129      50.424  50.211  25.402  1.00 74.16           C  
ANISOU 3757  CG  LEU C 129     9696   9995   8486  -1751   -141   1033       C  
ATOM   3758  CD1 LEU C 129      50.489  49.100  24.361  1.00 54.93           C  
ANISOU 3758  CD1 LEU C 129     7199   7502   6170  -1419     70   1181       C  
ATOM   3759  CD2 LEU C 129      50.206  51.561  24.740  1.00 78.29           C  
ANISOU 3759  CD2 LEU C 129    10172  10447   9129  -1933     63    885       C  
ATOM   3760  N   ASN C 130      46.643  50.555  28.042  1.00 60.23           N  
ANISOU 3760  N   ASN C 130     9184   8040   5661  -2193    -48    552       N  
ATOM   3761  CA  ASN C 130      45.553  50.025  28.855  1.00 59.15           C  
ANISOU 3761  CA  ASN C 130     9418   7849   5208  -2260     62    472       C  
ATOM   3762  C   ASN C 130      45.704  50.284  30.349  1.00 60.37           C  
ANISOU 3762  C   ASN C 130     9850   8025   5063  -2387   -198    485       C  
ATOM   3763  O   ASN C 130      45.956  49.365  31.123  1.00 66.09           O  
ANISOU 3763  O   ASN C 130    10802   8702   5608  -2311   -308    631       O  
ATOM   3764  CB  ASN C 130      45.375  48.537  28.589  1.00 59.74           C  
ANISOU 3764  CB  ASN C 130     9588   7826   5284  -2110    218    599       C  
ATOM   3765  CG  ASN C 130      45.079  48.247  27.131  1.00 62.86           C  
ANISOU 3765  CG  ASN C 130     9768   8183   5932  -1966    470    547       C  
ATOM   3766  OD1 ASN C 130      44.293  48.952  26.484  1.00 54.25           O  
ANISOU 3766  OD1 ASN C 130     8609   7118   4886  -1995    647    327       O  
ATOM   3767  ND2 ASN C 130      45.726  47.220  26.597  1.00 52.57           N  
ANISOU 3767  ND2 ASN C 130     8389   6819   4766  -1757    466    740       N  
ATOM   3768  N   PRO C 131      45.577  51.552  30.753  1.00 55.50           N  
ANISOU 3768  N   PRO C 131     9274   7454   4360  -2549   -305    332       N  
ATOM   3769  CA  PRO C 131      45.574  51.864  32.183  1.00 58.08           C  
ANISOU 3769  CA  PRO C 131     9930   7784   4353  -2651   -545    309       C  
ATOM   3770  C   PRO C 131      44.334  51.309  32.870  1.00 66.05           C  
ANISOU 3770  C   PRO C 131    11346   8723   5026  -2684   -281    244       C  
ATOM   3771  O   PRO C 131      43.341  50.960  32.216  1.00 62.56           O  
ANISOU 3771  O   PRO C 131    10872   8262   4635  -2690     86    139       O  
ATOM   3772  CB  PRO C 131      45.557  53.394  32.209  1.00 74.63           C  
ANISOU 3772  CB  PRO C 131    11994   9910   6451  -2815   -642    126       C  
ATOM   3773  CG  PRO C 131      45.029  53.802  30.876  1.00 70.90           C  
ANISOU 3773  CG  PRO C 131    11318   9422   6198  -2780   -327     15       C  
ATOM   3774  CD  PRO C 131      45.538  52.766  29.921  1.00 53.84           C  
ANISOU 3774  CD  PRO C 131     8868   7260   4328  -2615   -228    185       C  
ATOM   3775  N   GLY C 132      44.404  51.222  34.191  1.00 62.16           N  
ANISOU 3775  N   GLY C 132    11232   8193   4191  -2704   -463    290       N  
ATOM   3776  CA  GLY C 132      43.307  50.713  34.985  1.00 61.87           C  
ANISOU 3776  CA  GLY C 132    11632   8069   3807  -2757   -177    248       C  
ATOM   3777  C   GLY C 132      42.882  51.712  36.037  1.00 63.85           C  
ANISOU 3777  C   GLY C 132    12199   8340   3720  -2853   -271    108       C  
ATOM   3778  O   GLY C 132      43.242  52.891  35.978  1.00 63.00           O  
ANISOU 3778  O   GLY C 132    11961   8305   3673  -2906   -511     -1       O  
ATOM   3779  N   ALA C 133      42.132  51.226  37.018  1.00 65.38           N  
ANISOU 3779  N   ALA C 133    12838   8437   3566  -2868    -58    114       N  
ATOM   3780  CA  ALA C 133      41.498  52.088  38.001  1.00 66.84           C  
ANISOU 3780  CA  ALA C 133    13174   8590   3633  -2839    -41    -27       C  
ATOM   3781  C   ALA C 133      42.485  52.796  38.926  1.00 76.07           C  
ANISOU 3781  C   ALA C 133    14543   9749   4611  -2767   -554     18       C  
ATOM   3782  O   ALA C 133      42.182  53.864  39.451  1.00 70.62           O  
ANISOU 3782  O   ALA C 133    13884   9060   3889  -2752   -623   -120       O  
ATOM   3783  CB  ALA C 133      40.501  51.290  38.812  1.00 68.98           C  
ANISOU 3783  CB  ALA C 133    13727   8719   3763  -2813    346    -17       C  
ATOM   3784  N   ASP C 134      43.660  52.205  39.123  1.00 71.55           N  
ANISOU 3784  N   ASP C 134    14087   9175   3924  -2691   -937    198       N  
ATOM   3785  CA  ASP C 134      44.633  52.755  40.064  1.00 75.01           C  
ANISOU 3785  CA  ASP C 134    14678   9624   4198  -2592  -1483    202       C  
ATOM   3786  C   ASP C 134      45.648  53.725  39.441  1.00 74.43           C  
ANISOU 3786  C   ASP C 134    14215   9707   4358  -2743  -1922    109       C  
ATOM   3787  O   ASP C 134      46.485  54.283  40.152  1.00 77.64           O  
ANISOU 3787  O   ASP C 134    14660  10143   4696  -2711  -2408     53       O  
ATOM   3788  CB  ASP C 134      45.349  51.632  40.826  1.00 78.78           C  
ANISOU 3788  CB  ASP C 134    15497  10020   4417  -2341  -1727    404       C  
ATOM   3789  CG  ASP C 134      44.412  50.860  41.753  1.00 96.79           C  
ANISOU 3789  CG  ASP C 134    18249  12079   6447  -2200  -1312    471       C  
ATOM   3790  OD1 ASP C 134      43.457  51.465  42.291  1.00 90.99           O  
ANISOU 3790  OD1 ASP C 134    17620  11289   5664  -2258  -1045    340       O  
ATOM   3791  OD2 ASP C 134      44.632  49.646  41.949  1.00 99.77           O  
ANISOU 3791  OD2 ASP C 134    18898  12327   6682  -2023  -1244    655       O  
ATOM   3792  N   SER C 135      45.576  53.937  38.128  1.00 73.88           N  
ANISOU 3792  N   SER C 135    13655   9700   4716  -2853  -1695     73       N  
ATOM   3793  CA  SER C 135      46.452  54.916  37.493  1.00 70.63           C  
ANISOU 3793  CA  SER C 135    12804   9371   4661  -2991  -1960    -20       C  
ATOM   3794  C   SER C 135      46.043  56.324  37.902  1.00 73.47           C  
ANISOU 3794  C   SER C 135    13387   9687   4841  -3165  -2030   -238       C  
ATOM   3795  O   SER C 135      44.888  56.718  37.743  1.00 73.14           O  
ANISOU 3795  O   SER C 135    13469   9585   4735  -3147  -1635   -334       O  
ATOM   3796  CB  SER C 135      46.438  54.780  35.970  1.00 67.03           C  
ANISOU 3796  CB  SER C 135    11866   8950   4653  -3021  -1649     11       C  
ATOM   3797  OG  SER C 135      47.213  53.670  35.557  1.00 71.65           O  
ANISOU 3797  OG  SER C 135    12176   9585   5461  -2859  -1715    206       O  
ATOM   3798  N   ILE C 136      46.995  57.076  38.442  1.00 76.02           N  
ANISOU 3798  N   ILE C 136    13680  10027   5178  -3268  -2510   -323       N  
ATOM   3799  CA  ILE C 136      46.736  58.444  38.861  1.00 78.05           C  
ANISOU 3799  CA  ILE C 136    14064  10174   5419  -3342  -2530   -503       C  
ATOM   3800  C   ILE C 136      46.984  59.388  37.696  1.00 83.76           C  
ANISOU 3800  C   ILE C 136    14496  10876   6452  -3599  -2439   -614       C  
ATOM   3801  O   ILE C 136      47.939  59.220  36.940  1.00 87.76           O  
ANISOU 3801  O   ILE C 136    14577  11461   7307  -3740  -2569   -572       O  
ATOM   3802  CB  ILE C 136      47.639  58.876  40.032  1.00 80.26           C  
ANISOU 3802  CB  ILE C 136    14444  10445   5606  -3321  -3061   -577       C  
ATOM   3803  CG1 ILE C 136      47.711  57.783  41.103  1.00 90.47           C  
ANISOU 3803  CG1 ILE C 136    16030  11762   6584  -3031  -3232   -451       C  
ATOM   3804  CG2 ILE C 136      47.132  60.181  40.633  1.00 81.40           C  
ANISOU 3804  CG2 ILE C 136    14822  10438   5668  -3317  -2995   -731       C  
ATOM   3805  CD1 ILE C 136      48.537  58.166  42.320  1.00 91.86           C  
ANISOU 3805  CD1 ILE C 136    16334  11943   6625  -2923  -3765   -555       C  
ATOM   3806  N   ILE C 137      46.121  60.384  37.560  1.00 72.05           N  
ANISOU 3806  N   ILE C 137    13167   9262   4949  -3556  -2135   -722       N  
ATOM   3807  CA  ILE C 137      46.258  61.367  36.499  1.00 74.60           C  
ANISOU 3807  CA  ILE C 137    13351   9498   5496  -3742  -1994   -825       C  
ATOM   3808  C   ILE C 137      47.107  62.551  36.961  1.00 78.08           C  
ANISOU 3808  C   ILE C 137    13830   9821   6017  -3960  -2319   -950       C  
ATOM   3809  O   ILE C 137      46.932  63.064  38.073  1.00 77.24           O  
ANISOU 3809  O   ILE C 137    13990   9644   5715  -3852  -2475  -1006       O  
ATOM   3810  CB  ILE C 137      44.882  61.833  36.018  1.00 69.51           C  
ANISOU 3810  CB  ILE C 137    12850   8775   4784  -3509  -1513   -880       C  
ATOM   3811  CG1 ILE C 137      44.128  60.637  35.430  1.00 76.20           C  
ANISOU 3811  CG1 ILE C 137    13560   9751   5641  -3341  -1194   -800       C  
ATOM   3812  CG2 ILE C 137      45.016  62.964  35.000  1.00 75.11           C  
ANISOU 3812  CG2 ILE C 137    13553   9340   5644  -3632  -1370   -985       C  
ATOM   3813  CD1 ILE C 137      42.878  60.999  34.695  1.00 75.79           C  
ANISOU 3813  CD1 ILE C 137    13478   9681   5639  -3096   -768   -893       C  
ATOM   3814  N   GLU C 138      48.040  62.972  36.114  1.00 75.60           N  
ANISOU 3814  N   GLU C 138    13234   9474   6017  -4286  -2400  -1004       N  
ATOM   3815  CA  GLU C 138      48.960  64.046  36.487  1.00 86.35           C  
ANISOU 3815  CA  GLU C 138    14554  10721   7535  -4561  -2687  -1144       C  
ATOM   3816  C   GLU C 138      48.905  65.207  35.503  1.00 88.51           C  
ANISOU 3816  C   GLU C 138    14915  10758   7956  -4766  -2375  -1234       C  
ATOM   3817  O   GLU C 138      48.335  65.090  34.413  1.00 76.04           O  
ANISOU 3817  O   GLU C 138    13364   9129   6399  -4696  -1981  -1191       O  
ATOM   3818  CB  GLU C 138      50.390  63.515  36.565  1.00 88.60           C  
ANISOU 3818  CB  GLU C 138    14326  11185   8153  -4807  -3115  -1150       C  
ATOM   3819  CG  GLU C 138      50.564  62.328  37.492  1.00 98.19           C  
ANISOU 3819  CG  GLU C 138    15506  12622   9181  -4556  -3466  -1055       C  
ATOM   3820  CD  GLU C 138      51.898  61.633  37.297  1.00110.82           C  
ANISOU 3820  CD  GLU C 138    16501  14459  11145  -4683  -3832  -1028       C  
ATOM   3821  OE1 GLU C 138      52.939  62.327  37.274  1.00113.48           O  
ANISOU 3821  OE1 GLU C 138    16481  14816  11819  -4995  -4082  -1191       O  
ATOM   3822  OE2 GLU C 138      51.900  60.390  37.155  1.00113.49           O  
ANISOU 3822  OE2 GLU C 138    16658  14958  11504  -4371  -3772   -825       O  
ATOM   3823  N   GLU C 139      49.503  66.326  35.893  1.00 86.89           N  
ANISOU 3823  N   GLU C 139    14794  10389   7832  -5000  -2546  -1374       N  
ATOM   3824  CA  GLU C 139      49.614  67.478  35.008  1.00 92.16           C  
ANISOU 3824  CA  GLU C 139    15603  10780   8634  -5233  -2252  -1455       C  
ATOM   3825  C   GLU C 139      50.437  67.120  33.775  1.00 95.75           C  
ANISOU 3825  C   GLU C 139    15592  11248   9542  -5529  -2071  -1407       C  
ATOM   3826  O   GLU C 139      51.393  66.347  33.860  1.00 86.03           O  
ANISOU 3826  O   GLU C 139    13814  10241   8633  -5689  -2331  -1369       O  
ATOM   3827  CB  GLU C 139      50.229  68.668  35.749  1.00 95.62           C  
ANISOU 3827  CB  GLU C 139    16191  11040   9101  -5477  -2498  -1624       C  
ATOM   3828  CG  GLU C 139      50.183  69.977  34.973  1.00 95.28           C  
ANISOU 3828  CG  GLU C 139    16469  10646   9088  -5675  -2155  -1700       C  
ATOM   3829  CD  GLU C 139      50.440  71.184  35.854  1.00103.63           C  
ANISOU 3829  CD  GLU C 139    17840  11501  10034  -5826  -2372  -1863       C  
ATOM   3830  OE1 GLU C 139      50.267  71.068  37.087  1.00105.17           O  
ANISOU 3830  OE1 GLU C 139    18138  11810  10011  -5646  -2723  -1904       O  
ATOM   3831  OE2 GLU C 139      50.816  72.246  35.313  1.00105.16           O  
ANISOU 3831  OE2 GLU C 139    18207  11401  10349  -6117  -2171  -1950       O  
ATOM   3832  N   ASN C 140      50.040  67.670  32.630  1.00 98.41           N  
ANISOU 3832  N   ASN C 140    16153  11345   9893  -5544  -1605  -1399       N  
ATOM   3833  CA  ASN C 140      50.704  67.416  31.350  1.00 94.36           C  
ANISOU 3833  CA  ASN C 140    15268  10776   9808  -5770  -1299  -1323       C  
ATOM   3834  C   ASN C 140      50.625  65.973  30.858  1.00 88.99           C  
ANISOU 3834  C   ASN C 140    14111  10403   9297  -5431  -1207  -1103       C  
ATOM   3835  O   ASN C 140      51.316  65.599  29.913  1.00 83.29           O  
ANISOU 3835  O   ASN C 140    12938   9720   8990  -5476   -971   -975       O  
ATOM   3836  CB  ASN C 140      52.160  67.895  31.365  1.00101.19           C  
ANISOU 3836  CB  ASN C 140    15663  11616  11170  -6226  -1420  -1382       C  
ATOM   3837  CG  ASN C 140      52.281  69.385  31.163  1.00108.33           C  
ANISOU 3837  CG  ASN C 140    16971  12138  12053  -6439  -1191  -1507       C  
ATOM   3838  OD1 ASN C 140      51.392  70.147  31.541  1.00108.77           O  
ANISOU 3838  OD1 ASN C 140    17665  12003  11661  -6249  -1158  -1578       O  
ATOM   3839  ND2 ASN C 140      53.381  69.811  30.556  1.00116.34           N  
ANISOU 3839  ND2 ASN C 140    17612  13043  13550  -6815  -1002  -1529       N  
ATOM   3840  N   ASP C 141      49.795  65.160  31.500  1.00 75.46           N  
ANISOU 3840  N   ASP C 141    12516   8893   7262  -5083  -1360  -1055       N  
ATOM   3841  CA  ASP C 141      49.520  63.839  30.969  1.00 74.37           C  
ANISOU 3841  CA  ASP C 141    12052   8979   7228  -4730  -1202   -857       C  
ATOM   3842  C   ASP C 141      48.652  64.020  29.742  1.00 74.09           C  
ANISOU 3842  C   ASP C 141    12236   8791   7126  -4463   -696   -834       C  
ATOM   3843  O   ASP C 141      47.862  64.957  29.655  1.00 67.71           O  
ANISOU 3843  O   ASP C 141    11944   7776   6008  -4403   -538   -979       O  
ATOM   3844  CB  ASP C 141      48.779  62.964  31.984  1.00 78.58           C  
ANISOU 3844  CB  ASP C 141    12734   9712   7409  -4468  -1428   -828       C  
ATOM   3845  CG  ASP C 141      49.716  62.156  32.864  1.00 84.63           C  
ANISOU 3845  CG  ASP C 141    13150  10704   8301  -4530  -1877   -755       C  
ATOM   3846  OD1 ASP C 141      50.937  62.168  32.610  1.00 88.05           O  
ANISOU 3846  OD1 ASP C 141    13111  11204   9139  -4747  -2022   -735       O  
ATOM   3847  OD2 ASP C 141      49.222  61.491  33.801  1.00 83.31           O  
ANISOU 3847  OD2 ASP C 141    13187  10652   7814  -4337  -2069   -727       O  
ATOM   3848  N   THR C 142      48.799  63.130  28.778  1.00 74.60           N  
ANISOU 3848  N   THR C 142    12938   8074   7331  -3378    551  -2675       N  
ATOM   3849  CA  THR C 142      47.863  63.120  27.671  1.00 71.86           C  
ANISOU 3849  CA  THR C 142    12429   7775   7101  -3091    755  -2467       C  
ATOM   3850  C   THR C 142      47.067  61.833  27.722  1.00 56.58           C  
ANISOU 3850  C   THR C 142    10194   6210   5095  -2851    539  -2270       C  
ATOM   3851  O   THR C 142      47.635  60.739  27.629  1.00 62.19           O  
ANISOU 3851  O   THR C 142    10519   7272   5838  -2842    159  -2167       O  
ATOM   3852  CB  THR C 142      48.573  63.301  26.326  1.00 70.44           C  
ANISOU 3852  CB  THR C 142    11933   7694   7138  -3099    682  -2399       C  
ATOM   3853  OG1 THR C 142      49.122  64.626  26.272  1.00 71.85           O  
ANISOU 3853  OG1 THR C 142    12436   7395   7469  -3324    986  -2583       O  
ATOM   3854  CG2 THR C 142      47.589  63.114  25.181  1.00 68.60           C  
ANISOU 3854  CG2 THR C 142    11593   7580   6890  -2856    851  -2225       C  
ATOM   3855  N   LEU C 143      45.756  61.960  27.916  1.00 55.81           N  
ANISOU 3855  N   LEU C 143    10290   5982   4934  -2634    820  -2237       N  
ATOM   3856  CA  LEU C 143      44.882  60.795  27.905  1.00 51.86           C  
ANISOU 3856  CA  LEU C 143     9487   5797   4419  -2412    638  -2092       C  
ATOM   3857  C   LEU C 143      44.476  60.494  26.470  1.00 49.43           C  
ANISOU 3857  C   LEU C 143     8763   5765   4255  -2142    514  -1980       C  
ATOM   3858  O   LEU C 143      44.034  61.388  25.753  1.00 59.70           O  
ANISOU 3858  O   LEU C 143    10415   6841   5427  -2216    983  -2018       O  
ATOM   3859  CB  LEU C 143      43.625  61.060  28.727  1.00 54.12           C  
ANISOU 3859  CB  LEU C 143    10176   5842   4543  -2291   1040  -2138       C  
ATOM   3860  CG  LEU C 143      43.827  61.707  30.102  1.00 74.09           C  
ANISOU 3860  CG  LEU C 143    13247   8022   6880  -2459   1265  -2308       C  
ATOM   3861  CD1 LEU C 143      42.487  61.870  30.785  1.00 63.29           C  
ANISOU 3861  CD1 LEU C 143    12361   6382   5306  -2341   1817  -2306       C  
ATOM   3862  CD2 LEU C 143      44.777  60.881  30.952  1.00 73.93           C  
ANISOU 3862  CD2 LEU C 143    13164   8202   6723  -2718    847  -2341       C  
ATOM   3863  N   VAL C 144      44.651  59.245  26.048  1.00 43.92           N  
ANISOU 3863  N   VAL C 144     7579   5458   3651  -2070    110  -1856       N  
ATOM   3864  CA  VAL C 144      44.171  58.788  24.755  1.00 46.13           C  
ANISOU 3864  CA  VAL C 144     7459   6057   4012  -1781    -84  -1776       C  
ATOM   3865  C   VAL C 144      42.807  58.153  24.977  1.00 48.48           C  
ANISOU 3865  C   VAL C 144     7678   6502   4241  -1606    -77  -1763       C  
ATOM   3866  O   VAL C 144      42.694  57.109  25.620  1.00 48.69           O  
ANISOU 3866  O   VAL C 144     7541   6597   4363  -1632   -267  -1707       O  
ATOM   3867  CB  VAL C 144      45.133  57.774  24.131  1.00 42.48           C  
ANISOU 3867  CB  VAL C 144     6569   5865   3706  -1794   -436  -1667       C  
ATOM   3868  CG1 VAL C 144      44.748  57.504  22.667  1.00 43.86           C  
ANISOU 3868  CG1 VAL C 144     6417   6332   3918  -1505   -614  -1595       C  
ATOM   3869  CG2 VAL C 144      46.568  58.310  24.222  1.00 48.90           C  
ANISOU 3869  CG2 VAL C 144     7499   6553   4527  -2048   -401  -1711       C  
ATOM   3870  N   LEU C 145      41.771  58.806  24.462  1.00 50.62           N  
ANISOU 3870  N   LEU C 145     8195   6848   4188  -1631    356  -1840       N  
ATOM   3871  CA  LEU C 145      40.404  58.444  24.802  1.00 43.75           C  
ANISOU 3871  CA  LEU C 145     7363   6139   3121  -1562    635  -1873       C  
ATOM   3872  C   LEU C 145      39.720  57.798  23.620  1.00 51.39           C  
ANISOU 3872  C   LEU C 145     7648   7839   4040  -1347    314  -1799       C  
ATOM   3873  O   LEU C 145      39.974  58.164  22.460  1.00 48.24           O  
ANISOU 3873  O   LEU C 145     6969   7716   3642  -1087    192  -1634       O  
ATOM   3874  CB  LEU C 145      39.608  59.680  25.243  1.00 49.22           C  
ANISOU 3874  CB  LEU C 145     8724   6368   3611  -1361   1653  -1821       C  
ATOM   3875  CG  LEU C 145      40.138  60.540  26.393  1.00 60.05           C  
ANISOU 3875  CG  LEU C 145    10726   7026   5064  -1549   1952  -1902       C  
ATOM   3876  CD1 LEU C 145      39.322  61.813  26.515  1.00 66.03           C  
ANISOU 3876  CD1 LEU C 145    12006   7250   5832  -1143   2962  -1729       C  
ATOM   3877  CD2 LEU C 145      40.113  59.779  27.711  1.00 60.50           C  
ANISOU 3877  CD2 LEU C 145    10810   7052   5127  -1743   1707  -1953       C  
ATOM   3878  N   SER C 146      38.842  56.840  23.902  1.00 44.30           N  
ANISOU 3878  N   SER C 146     6295   7196   3340  -1299    120  -1731       N  
ATOM   3879  CA  SER C 146      38.128  56.157  22.831  1.00 44.58           C  
ANISOU 3879  CA  SER C 146     5438   7862   3638   -977   -339  -1540       C  
ATOM   3880  C   SER C 146      36.653  55.943  23.135  1.00 47.42           C  
ANISOU 3880  C   SER C 146     5333   8297   4387   -660    -33  -1202       C  
ATOM   3881  O   SER C 146      36.304  55.393  24.167  1.00 50.73           O  
ANISOU 3881  O   SER C 146     5865   8490   4919   -901    125  -1253       O  
ATOM   3882  CB  SER C 146      38.803  54.825  22.469  1.00 46.42           C  
ANISOU 3882  CB  SER C 146     5433   7961   4245  -1085   -998  -1546       C  
ATOM   3883  OG  SER C 146      37.959  54.076  21.610  1.00 50.92           O  
ANISOU 3883  OG  SER C 146     5373   8861   5114   -839  -1293  -1402       O  
ATOM   3884  N   GLY C 147      35.792  56.387  22.228  1.00 49.87           N  
ANISOU 3884  N   GLY C 147     5095   8949   4906    -94     67   -815       N  
ATOM   3885  CA  GLY C 147      34.359  56.219  22.386  1.00 53.86           C  
ANISOU 3885  CA  GLY C 147     4994   9599   5870    249    324   -454       C  
ATOM   3886  C   GLY C 147      33.547  56.933  21.320  1.00 71.18           C  
ANISOU 3886  C   GLY C 147     6638  12190   8217    953    426     11       C  
ATOM   3887  O   GLY C 147      34.085  57.413  20.319  1.00 57.94           O  
ANISOU 3887  O   GLY C 147     4998  10763   6252   1189    204     61       O  
ATOM   3888  N   GLU C 148      32.239  57.003  21.526  1.00 63.62           N  
ANISOU 3888  N   GLU C 148     5138  11316   7717   1327    781    402       N  
ATOM   3889  CA  GLU C 148      31.376  57.678  20.569  1.00 75.54           C  
ANISOU 3889  CA  GLU C 148     6056  13243   9401   2064    863    907       C  
ATOM   3890  C   GLU C 148      31.530  59.177  20.721  1.00 83.40           C  
ANISOU 3890  C   GLU C 148     7767  13712  10208   2509   1755   1266       C  
ATOM   3891  O   GLU C 148      31.937  59.655  21.779  1.00 70.78           O  
ANISOU 3891  O   GLU C 148     7007  11394   8492   2262   2416   1130       O  
ATOM   3892  CB  GLU C 148      29.930  57.248  20.752  1.00 80.46           C  
ANISOU 3892  CB  GLU C 148     5765  14139  10665   2312    939   1220       C  
ATOM   3893  CG  GLU C 148      29.739  55.760  20.559  1.00 86.97           C  
ANISOU 3893  CG  GLU C 148     5841  15411  11793   1833     57    850       C  
ATOM   3894  CD  GLU C 148      28.380  55.277  21.015  1.00100.65           C  
ANISOU 3894  CD  GLU C 148     6843  17132  14267   1864    248   1093       C  
ATOM   3895  OE1 GLU C 148      27.467  56.115  21.186  1.00107.15           O  
ANISOU 3895  OE1 GLU C 148     7494  17863  15356   2408    923   1602       O  
ATOM   3896  OE2 GLU C 148      28.233  54.051  21.207  1.00104.41           O  
ANISOU 3896  OE2 GLU C 148     7118  17461  15093   1298   -246    730       O  
ATOM   3897  N   ARG C 149      31.232  59.910  19.651  1.00 87.73           N  
ANISOU 3897  N   ARG C 149     8017  14608  10708   3170   1753   1709       N  
ATOM   3898  CA  ARG C 149      31.449  61.351  19.633  1.00 86.09           C  
ANISOU 3898  CA  ARG C 149     8487  13858  10364   3622   2585   2089       C  
ATOM   3899  C   ARG C 149      30.685  62.045  20.754  1.00 88.01           C  
ANISOU 3899  C   ARG C 149     9062  13425  10952   3862   3620   2342       C  
ATOM   3900  O   ARG C 149      31.263  62.824  21.512  1.00 85.58           O  
ANISOU 3900  O   ARG C 149     9714  12315  10489   3698   4319   2199       O  
ATOM   3901  CB  ARG C 149      31.049  61.953  18.284  1.00 91.78           C  
ANISOU 3901  CB  ARG C 149     8718  15135  11019   4414   2428   2663       C  
ATOM   3902  CG  ARG C 149      31.438  63.414  18.147  1.00 96.70           C  
ANISOU 3902  CG  ARG C 149    10089  15139  11512   4851   3269   3080       C  
ATOM   3903  CD  ARG C 149      30.935  64.015  16.846  1.00114.94           C  
ANISOU 3903  CD  ARG C 149    11903  18019  13748   5743   3172   3778       C  
ATOM   3904  NE  ARG C 149      29.528  64.398  16.931  1.00127.85           N  
ANISOU 3904  NE  ARG C 149    13081  19690  15808   6283   3476   4294       N  
ATOM   3905  CZ  ARG C 149      28.528  63.703  16.400  1.00131.92           C  
ANISOU 3905  CZ  ARG C 149    12787  20894  16444   6270   2736   4311       C  
ATOM   3906  NH1 ARG C 149      27.281  64.133  16.533  1.00137.34           N  
ANISOU 3906  NH1 ARG C 149    13165  21504  17514   6627   3049   4726       N  
ATOM   3907  NH2 ARG C 149      28.773  62.582  15.733  1.00128.71           N  
ANISOU 3907  NH2 ARG C 149    11947  21162  15792   5836   1706   3836       N  
ATOM   3908  N   LYS C 150      29.391  61.753  20.862  1.00 88.10           N  
ANISOU 3908  N   LYS C 150     8266  13761  11446   4243   3718   2683       N  
ATOM   3909  CA  LYS C 150      28.547  62.431  21.845  1.00 95.22           C  
ANISOU 3909  CA  LYS C 150     9389  14086  12706   4607   4782   2999       C  
ATOM   3910  C   LYS C 150      29.014  62.184  23.281  1.00 92.61           C  
ANISOU 3910  C   LYS C 150     9898  13073  12215   3966   5236   2505       C  
ATOM   3911  O   LYS C 150      28.881  63.051  24.141  1.00 96.43           O  
ANISOU 3911  O   LYS C 150    11139  12809  12691   4109   6120   2553       O  
ATOM   3912  CB  LYS C 150      27.066  62.062  21.669  1.00100.03           C  
ANISOU 3912  CB  LYS C 150     8996  15140  13872   4918   4582   3390       C  
ATOM   3913  CG  LYS C 150      26.726  60.595  21.890  1.00 97.61           C  
ANISOU 3913  CG  LYS C 150     7903  15329  13855   4405   3936   3087       C  
ATOM   3914  CD  LYS C 150      25.211  60.416  21.991  1.00105.49           C  
ANISOU 3914  CD  LYS C 150     8164  16470  15446   4595   3962   3414       C  
ATOM   3915  CE  LYS C 150      24.834  59.017  22.456  1.00105.25           C  
ANISOU 3915  CE  LYS C 150     7505  16676  15808   4010   3534   3109       C  
ATOM   3916  NZ  LYS C 150      23.369  58.898  22.705  1.00119.70           N  
ANISOU 3916  NZ  LYS C 150     8689  18546  18244   4174   3726   3414       N  
ATOM   3917  N   HIS C 151      29.592  61.013  23.528  1.00 89.88           N  
ANISOU 3917  N   HIS C 151     9499  12955  11695   3228   4519   1997       N  
ATOM   3918  CA  HIS C 151      30.092  60.693  24.860  1.00 86.43           C  
ANISOU 3918  CA  HIS C 151     9855  11972  11015   2637   4836   1554       C  
ATOM   3919  C   HIS C 151      31.425  61.376  25.151  1.00 85.69           C  
ANISOU 3919  C   HIS C 151    10900  11292  10365   2278   4965   1127       C  
ATOM   3920  O   HIS C 151      31.661  61.832  26.265  1.00 80.12           O  
ANISOU 3920  O   HIS C 151    11077   9934   9432   2111   5619    897       O  
ATOM   3921  CB  HIS C 151      30.206  59.184  25.040  1.00 77.50           C  
ANISOU 3921  CB  HIS C 151     8240  11256   9952   2024   4053   1237       C  
ATOM   3922  CG  HIS C 151      28.885  58.494  25.152  1.00 82.20           C  
ANISOU 3922  CG  HIS C 151     7838  12212  11182   2223   4115   1589       C  
ATOM   3923  ND1 HIS C 151      28.673  57.211  24.698  1.00 86.01           N  
ANISOU 3923  ND1 HIS C 151     7440  13255  11983   1881   3250   1463       N  
ATOM   3924  CD2 HIS C 151      27.706  58.908  25.674  1.00 91.76           C  
ANISOU 3924  CD2 HIS C 151     8758  13273  12833   2716   4969   2059       C  
ATOM   3925  CE1 HIS C 151      27.419  56.864  24.933  1.00 90.04           C  
ANISOU 3925  CE1 HIS C 151     7123  13943  13145   2105   3542   1842       C  
ATOM   3926  NE2 HIS C 151      26.811  57.878  25.524  1.00 93.38           N  
ANISOU 3926  NE2 HIS C 151     7862  13971  13649   2631   4596   2233       N  
ATOM   3927  N   LEU C 152      32.296  61.452  24.149  1.00 79.92           N  
ANISOU 3927  N   LEU C 152    10141  10809   9417   2159   4344   1009       N  
ATOM   3928  CA  LEU C 152      33.568  62.144  24.318  1.00 72.55           C  
ANISOU 3928  CA  LEU C 152    10158   9331   8076   1804   4460    645       C  
ATOM   3929  C   LEU C 152      33.353  63.627  24.605  1.00 94.11           C  
ANISOU 3929  C   LEU C 152    13564  11313  10880   2264   5493    891       C  
ATOM   3930  O   LEU C 152      34.072  64.224  25.408  1.00 79.33           O  
ANISOU 3930  O   LEU C 152    12651   8730   8761   1918   5905    497       O  
ATOM   3931  CB  LEU C 152      34.454  61.978  23.077  1.00 68.50           C  
ANISOU 3931  CB  LEU C 152     9376   9266   7385   1683   3702    585       C  
ATOM   3932  CG  LEU C 152      35.223  60.667  22.946  1.00 61.86           C  
ANISOU 3932  CG  LEU C 152     8265   8897   6341   1051   2726    111       C  
ATOM   3933  CD1 LEU C 152      36.022  60.673  21.635  1.00 59.40           C  
ANISOU 3933  CD1 LEU C 152     7709   9020   5840   1084   2146    118       C  
ATOM   3934  CD2 LEU C 152      36.153  60.439  24.125  1.00 80.41           C  
ANISOU 3934  CD2 LEU C 152    11402  10752   8397    354   2737   -446       C  
ATOM   3935  N   LYS C 153      32.372  64.215  23.926  1.00 98.72           N  
ANISOU 3935  N   LYS C 153    13634  12055  11820   3053   5876   1526       N  
ATOM   3936  CA  LYS C 153      32.020  65.612  24.139  1.00101.05           C  
ANISOU 3936  CA  LYS C 153    14481  11596  12318   3531   6736   1837       C  
ATOM   3937  C   LYS C 153      31.713  65.847  25.612  1.00 94.26           C  
ANISOU 3937  C   LYS C 153    14285  10048  11480   3286   7209   1550       C  
ATOM   3938  O   LYS C 153      32.255  66.765  26.223  1.00 97.00           O  
ANISOU 3938  O   LYS C 153    15548   9578  11731   3083   7600   1295       O  
ATOM   3939  CB  LYS C 153      30.813  66.005  23.282  1.00109.49           C  
ANISOU 3939  CB  LYS C 153    14753  13040  13807   4408   6888   2619       C  
ATOM   3940  CG  LYS C 153      31.103  66.160  21.790  1.00111.99           C  
ANISOU 3940  CG  LYS C 153    14575  13933  14044   4823   6505   3018       C  
ATOM   3941  CD  LYS C 153      32.016  67.352  21.508  1.00111.95           C  
ANISOU 3941  CD  LYS C 153    15419  13202  13917   4833   6940   3068       C  
ATOM   3942  CE  LYS C 153      31.684  68.010  20.173  1.00108.22           C  
ANISOU 3942  CE  LYS C 153    14512  13069  13537   5631   6957   3845       C  
ATOM   3943  NZ  LYS C 153      31.729  67.043  19.042  1.00100.14           N  
ANISOU 3943  NZ  LYS C 153    12572  13213  12263   5752   6025   3951       N  
ATOM   3944  N   LYS C 154      30.868  64.991  26.178  1.00101.30           N  
ANISOU 3944  N   LYS C 154    14694  11293  12500   3292   7164   1596       N  
ATOM   3945  CA  LYS C 154      30.437  65.132  27.569  1.00 98.64           C  
ANISOU 3945  CA  LYS C 154    14906  10423  12148   3162   7635   1422       C  
ATOM   3946  C   LYS C 154      31.618  65.107  28.539  1.00102.21           C  
ANISOU 3946  C   LYS C 154    16336  10401  12097   2430   7478    724       C  
ATOM   3947  O   LYS C 154      31.766  66.008  29.361  1.00107.04           O  
ANISOU 3947  O   LYS C 154    17771  10281  12619   2374   7931    553       O  
ATOM   3948  CB  LYS C 154      29.422  64.045  27.937  1.00 99.16           C  
ANISOU 3948  CB  LYS C 154    14206  11024  12448   3229   7574   1617       C  
ATOM   3949  CG  LYS C 154      28.788  64.227  29.309  1.00107.99           C  
ANISOU 3949  CG  LYS C 154    15807  11651  13573   3250   8160   1586       C  
ATOM   3950  CD  LYS C 154      28.060  65.559  29.404  1.00118.95           C  
ANISOU 3950  CD  LYS C 154    17492  12461  15243   3855   8888   1976       C  
ATOM   3951  CE  LYS C 154      27.472  65.784  30.791  1.00124.21           C  
ANISOU 3951  CE  LYS C 154    18704  12635  15855   3900   9516   1924       C  
ATOM   3952  NZ  LYS C 154      26.428  64.778  31.135  1.00122.07           N  
ANISOU 3952  NZ  LYS C 154    17655  12855  15870   4009   9563   2210       N  
ATOM   3953  N   LEU C 155      32.461  64.084  28.425  1.00 92.12           N  
ANISOU 3953  N   LEU C 155    14941   9563  10496   1865   6800    338       N  
ATOM   3954  CA  LEU C 155      33.626  63.941  29.295  1.00 90.48           C  
ANISOU 3954  CA  LEU C 155    15521   9035   9823   1148   6455   -289       C  
ATOM   3955  C   LEU C 155      34.560  65.139  29.199  1.00 87.53           C  
ANISOU 3955  C   LEU C 155    15866   8016   9376    965   6571   -514       C  
ATOM   3956  O   LEU C 155      35.009  65.671  30.215  1.00 90.94           O  
ANISOU 3956  O   LEU C 155    17040   7905   9608    634   6707   -835       O  
ATOM   3957  CB  LEU C 155      34.401  62.667  28.957  1.00 77.76           C  
ANISOU 3957  CB  LEU C 155    13573   8034   7939    624   5644   -585       C  
ATOM   3958  CG  LEU C 155      35.665  62.437  29.787  1.00 75.13           C  
ANISOU 3958  CG  LEU C 155    13870   7478   7197   -102   5088  -1150       C  
ATOM   3959  CD1 LEU C 155      35.308  62.290  31.266  1.00 79.29           C  
ANISOU 3959  CD1 LEU C 155    14838   7739   7549   -190   5330  -1239       C  
ATOM   3960  CD2 LEU C 155      36.427  61.220  29.275  1.00 67.74           C  
ANISOU 3960  CD2 LEU C 155    12519   7137   6083   -552   4229  -1375       C  
ATOM   3961  N   ILE C 156      34.855  65.552  27.970  1.00 95.11           N  
ANISOU 3961  N   ILE C 156    16565   9078  10496   1175   6534   -306       N  
ATOM   3962  CA  ILE C 156      35.712  66.707  27.736  1.00100.11           C  
ANISOU 3962  CA  ILE C 156    17815   9067  11154   1021   6759   -433       C  
ATOM   3963  C   ILE C 156      35.072  67.961  28.318  1.00102.25           C  
ANISOU 3963  C   ILE C 156    18637   8554  11659   1388   7612   -220       C  
ATOM   3964  O   ILE C 156      35.735  68.746  28.997  1.00107.18           O  
ANISOU 3964  O   ILE C 156    20011   8549  12162    981   7813   -548       O  
ATOM   3965  CB  ILE C 156      36.001  66.914  26.234  1.00100.35           C  
ANISOU 3965  CB  ILE C 156    17414   9389  11328   1323   6685    -99       C  
ATOM   3966  CG1 ILE C 156      36.827  65.750  25.681  1.00101.79           C  
ANISOU 3966  CG1 ILE C 156    17174  10304  11196    859   5839   -382       C  
ATOM   3967  CG2 ILE C 156      36.740  68.224  26.008  1.00103.40           C  
ANISOU 3967  CG2 ILE C 156    18462   8975  11851   1243   7146   -124       C  
ATOM   3968  CD1 ILE C 156      38.195  65.615  26.310  1.00102.14           C  
ANISOU 3968  CD1 ILE C 156    17755  10077  10975     -5   5334  -1032       C  
ATOM   3969  N   HIS C 157      33.778  68.134  28.061  1.00103.92           N  
ANISOU 3969  N   HIS C 157    18408   8874  12204   2131   8079    352       N  
ATOM   3970  CA  HIS C 157      33.018  69.247  28.624  1.00115.23           C  
ANISOU 3970  CA  HIS C 157    20297   9614  13870   2544   8911    620       C  
ATOM   3971  C   HIS C 157      33.099  69.244  30.149  1.00121.50           C  
ANISOU 3971  C   HIS C 157    21772  10045  14345   2115   9045    154       C  
ATOM   3972  O   HIS C 157      33.270  70.293  30.772  1.00131.99           O  
ANISOU 3972  O   HIS C 157    23843  10680  15627   2022   9560     16       O  
ATOM   3973  CB  HIS C 157      31.556  69.181  28.173  1.00120.15           C  
ANISOU 3973  CB  HIS C 157    20160  10591  14899   3373   9234   1328       C  
ATOM   3974  CG  HIS C 157      30.706  70.293  28.704  1.00130.83           C  
ANISOU 3974  CG  HIS C 157    21926  11278  16507   3844  10103   1666       C  
ATOM   3975  ND1 HIS C 157      30.868  71.605  28.318  1.00139.73           N  
ANISOU 3975  ND1 HIS C 157    23523  11743  17827   4091  10682   1929       N  
ATOM   3976  CD2 HIS C 157      29.681  70.287  29.593  1.00130.48           C  
ANISOU 3976  CD2 HIS C 157    21896  11129  16553   4114  10546   1810       C  
ATOM   3977  CE1 HIS C 157      29.984  72.361  28.944  1.00147.24           C  
ANISOU 3977  CE1 HIS C 157    24762  12228  18956   4483  11423   2197       C  
ATOM   3978  NE2 HIS C 157      29.252  71.584  29.723  1.00138.74           N  
ANISOU 3978  NE2 HIS C 157    23418  11478  17818   4519  11351   2125       N  
ATOM   3979  N   ASP C 158      32.982  68.060  30.743  1.00115.13           N  
ANISOU 3979  N   ASP C 158    20696   9755  13293   1864   8589    -65       N  
ATOM   3980  CA  ASP C 158      33.089  67.918  32.190  1.00118.68           C  
ANISOU 3980  CA  ASP C 158    21741   9989  13364   1503   8638   -456       C  
ATOM   3981  C   ASP C 158      34.551  67.892  32.623  1.00116.81           C  
ANISOU 3981  C   ASP C 158    22017   9669  12697    706   8052  -1056       C  
ATOM   3982  O   ASP C 158      35.011  68.789  33.331  1.00122.24           O  
ANISOU 3982  O   ASP C 158    23401   9844  13200    465   8299  -1335       O  
ATOM   3983  CB  ASP C 158      32.368  66.653  32.666  1.00111.82           C  
ANISOU 3983  CB  ASP C 158    20367   9694  12427   1586   8449   -360       C  
ATOM   3984  CG  ASP C 158      30.855  66.774  32.585  1.00118.46           C  
ANISOU 3984  CG  ASP C 158    20720  10586  13704   2326   9096    229       C  
ATOM   3985  OD1 ASP C 158      30.360  67.780  32.034  1.00120.48           O  
ANISOU 3985  OD1 ASP C 158    20956  10499  14321   2825   9609    607       O  
ATOM   3986  OD2 ASP C 158      30.159  65.857  33.067  1.00115.59           O  
ANISOU 3986  OD2 ASP C 158    19954  10612  13354   2406   9099    360       O  
TER    3987      ASP C 158                                                      
ATOM   3988  N   GLY D   0      64.093  40.191  12.684  1.00 95.66           N  
ANISOU 3988  N   GLY D   0    12898   7917  15533   2152  -3043   1082       N  
ATOM   3989  CA  GLY D   0      63.519  40.162  11.351  1.00 89.81           C  
ANISOU 3989  CA  GLY D   0    12372   7006  14744   2104  -2711    778       C  
ATOM   3990  C   GLY D   0      63.645  41.492  10.627  1.00 83.89           C  
ANISOU 3990  C   GLY D   0    11334   6566  13975   2036  -2585    588       C  
ATOM   3991  O   GLY D   0      64.141  41.549   9.496  1.00 83.79           O  
ANISOU 3991  O   GLY D   0    11220   6460  14157   2269  -2253    360       O  
ATOM   3992  N   LEU D   1      63.191  42.564  11.274  1.00 70.54           N  
ANISOU 3992  N   LEU D   1     9528   5238  12035   1725  -2813    680       N  
ATOM   3993  CA  LEU D   1      63.284  43.903  10.697  1.00 66.66           C  
ANISOU 3993  CA  LEU D   1     8763   5032  11531   1640  -2711    541       C  
ATOM   3994  C   LEU D   1      64.357  44.775  11.347  1.00 69.38           C  
ANISOU 3994  C   LEU D   1     8614   5671  12076   1706  -2887    666       C  
ATOM   3995  O   LEU D   1      64.452  44.876  12.570  1.00 66.54           O  
ANISOU 3995  O   LEU D   1     8225   5456  11602   1580  -3201    864       O  
ATOM   3996  CB  LEU D   1      61.938  44.641  10.762  1.00 62.28           C  
ANISOU 3996  CB  LEU D   1     8458   4672  10535   1230  -2774    517       C  
ATOM   3997  CG  LEU D   1      60.778  44.116   9.906  1.00 59.59           C  
ANISOU 3997  CG  LEU D   1     8551   4143   9946   1063  -2579    352       C  
ATOM   3998  CD1 LEU D   1      59.600  45.091   9.935  1.00 49.31           C  
ANISOU 3998  CD1 LEU D   1     7373   3130   8231    687  -2621    364       C  
ATOM   3999  CD2 LEU D   1      61.214  43.853   8.475  1.00 61.12           C  
ANISOU 3999  CD2 LEU D   1     8754   4118  10350   1308  -2206     52       C  
ATOM   4000  N   ASN D   2      65.162  45.407  10.506  1.00 59.78           N  
ANISOU 4000  N   ASN D   2     7018   4552  11144   1881  -2655    537       N  
ATOM   4001  CA  ASN D   2      66.030  46.482  10.953  1.00 62.25           C  
ANISOU 4001  CA  ASN D   2     6855   5182  11615   1828  -2789    620       C  
ATOM   4002  C   ASN D   2      65.252  47.762  10.728  1.00 60.67           C  
ANISOU 4002  C   ASN D   2     6688   5206  11158   1510  -2764    529       C  
ATOM   4003  O   ASN D   2      64.869  48.039   9.598  1.00 57.80           O  
ANISOU 4003  O   ASN D   2     6363   4804  10795   1544  -2450    350       O  
ATOM   4004  CB  ASN D   2      67.313  46.502  10.123  1.00 65.12           C  
ANISOU 4004  CB  ASN D   2     6751   5561  12429   2165  -2495    554       C  
ATOM   4005  CG  ASN D   2      68.235  47.635  10.502  1.00 84.66           C  
ANISOU 4005  CG  ASN D   2     8716   8364  15088   2053  -2614    639       C  
ATOM   4006  OD1 ASN D   2      68.572  47.815  11.673  1.00 98.09           O  
ANISOU 4006  OD1 ASN D   2    10340  10188  16742   1918  -2988    808       O  
ATOM   4007  ND2 ASN D   2      68.648  48.414   9.511  1.00 89.21           N  
ANISOU 4007  ND2 ASN D   2     8965   9079  15851   2085  -2275    515       N  
ATOM   4008  N   ILE D   3      64.987  48.517  11.793  1.00 52.72           N  
ANISOU 4008  N   ILE D   3     5714   4418   9898   1215  -3058    640       N  
ATOM   4009  CA  ILE D   3      64.255  49.775  11.670  1.00 48.15           C  
ANISOU 4009  CA  ILE D   3     5194   4051   9051    926  -3022    572       C  
ATOM   4010  C   ILE D   3      65.090  50.945  12.172  1.00 56.07           C  
ANISOU 4010  C   ILE D   3     5849   5289  10165    793  -3126    599       C  
ATOM   4011  O   ILE D   3      65.662  50.883  13.262  1.00 51.59           O  
ANISOU 4011  O   ILE D   3     5238   4771   9595    750  -3388    711       O  
ATOM   4012  CB  ILE D   3      62.924  49.742  12.447  1.00 51.46           C  
ANISOU 4012  CB  ILE D   3     6092   4512   8947    644  -3163    634       C  
ATOM   4013  CG1 ILE D   3      62.126  48.481  12.080  1.00 52.83           C  
ANISOU 4013  CG1 ILE D   3     6627   4436   9011    714  -3095    633       C  
ATOM   4014  CG2 ILE D   3      62.107  51.011  12.180  1.00 45.89           C  
ANISOU 4014  CG2 ILE D   3     5469   4021   7948    396  -3047    565       C  
ATOM   4015  CD1 ILE D   3      60.956  48.222  12.979  1.00 60.37           C  
ANISOU 4015  CD1 ILE D   3     7974   5450   9513    445  -3212    736       C  
ATOM   4016  N   LYS D   4      65.161  51.999  11.362  1.00 47.12           N  
ANISOU 4016  N   LYS D   4     4488   4288   9129    724  -2908    497       N  
ATOM   4017  CA  LYS D   4      65.853  53.229  11.732  1.00 47.89           C  
ANISOU 4017  CA  LYS D   4     4309   4575   9311    538  -2963    504       C  
ATOM   4018  C   LYS D   4      64.862  54.375  11.666  1.00 48.48           C  
ANISOU 4018  C   LYS D   4     4616   4778   9024    265  -2876    439       C  
ATOM   4019  O   LYS D   4      64.213  54.578  10.640  1.00 53.89           O  
ANISOU 4019  O   LYS D   4     5316   5488   9674    282  -2626    362       O  
ATOM   4020  CB  LYS D   4      67.012  53.524  10.780  1.00 56.27           C  
ANISOU 4020  CB  LYS D   4     4828   5687  10865    693  -2698    468       C  
ATOM   4021  CG  LYS D   4      68.346  52.954  11.196  1.00 82.37           C  
ANISOU 4021  CG  LYS D   4     7792   8978  14526    876  -2832    575       C  
ATOM   4022  CD  LYS D   4      69.477  53.820  10.656  1.00 94.39           C  
ANISOU 4022  CD  LYS D   4     8792  10653  16420    848  -2635    577       C  
ATOM   4023  CE  LYS D   4      69.280  55.282  11.055  1.00 94.35           C  
ANISOU 4023  CE  LYS D   4     8834  10781  16233    473  -2728    549       C  
ATOM   4024  NZ  LYS D   4      70.393  56.160  10.590  1.00 97.54           N  
ANISOU 4024  NZ  LYS D   4     8754  11314  16994    394  -2555    573       N  
ATOM   4025  N   GLU D   5      64.734  55.112  12.762  1.00 44.33           N  
ANISOU 4025  N   GLU D   5     4288   4336   8218     49  -3053    469       N  
ATOM   4026  CA  GLU D   5      63.845  56.265  12.790  1.00 46.67           C  
ANISOU 4026  CA  GLU D   5     4828   4744   8161   -166  -2921    413       C  
ATOM   4027  C   GLU D   5      64.727  57.518  12.816  1.00 45.08           C  
ANISOU 4027  C   GLU D   5     4340   4621   8167   -297  -2907    374       C  
ATOM   4028  O   GLU D   5      65.736  57.557  13.527  1.00 47.03           O  
ANISOU 4028  O   GLU D   5     4403   4868   8600   -306  -3133    414       O  
ATOM   4029  CB  GLU D   5      62.912  56.221  14.010  1.00 42.77           C  
ANISOU 4029  CB  GLU D   5     4812   4268   7170   -271  -3029    463       C  
ATOM   4030  CG  GLU D   5      61.926  57.404  14.074  1.00 50.29           C  
ANISOU 4030  CG  GLU D   5     6020   5337   7751   -429  -2837    415       C  
ATOM   4031  CD  GLU D   5      60.981  57.366  15.284  1.00 51.92           C  
ANISOU 4031  CD  GLU D   5     6632   5579   7514   -488  -2855    464       C  
ATOM   4032  OE1 GLU D   5      61.007  56.388  16.059  1.00 49.16           O  
ANISOU 4032  OE1 GLU D   5     6391   5171   7115   -439  -3009    537       O  
ATOM   4033  OE2 GLU D   5      60.189  58.320  15.449  1.00 47.36           O  
ANISOU 4033  OE2 GLU D   5     6244   5089   6661   -576  -2695    432       O  
ATOM   4034  N   ASN D   6      64.363  58.512  12.010  1.00 44.99           N  
ANISOU 4034  N   ASN D   6     4279   4678   8136   -409  -2645    307       N  
ATOM   4035  CA  ASN D   6      65.080  59.779  11.964  1.00 48.20           C  
ANISOU 4035  CA  ASN D   6     4461   5128   8726   -573  -2590    272       C  
ATOM   4036  C   ASN D   6      64.101  60.935  12.051  1.00 38.41           C  
ANISOU 4036  C   ASN D   6     3543   3929   7121   -750  -2458    216       C  
ATOM   4037  O   ASN D   6      63.023  60.871  11.517  1.00 38.87           O  
ANISOU 4037  O   ASN D   6     3813   4022   6934   -736  -2267    211       O  
ATOM   4038  CB  ASN D   6      65.902  59.911  10.671  1.00 50.35           C  
ANISOU 4038  CB  ASN D   6     4233   5419   9480   -517  -2290    271       C  
ATOM   4039  CG  ASN D   6      67.222  59.176  10.738  1.00 67.52           C  
ANISOU 4039  CG  ASN D   6     5998   7572  12083   -359  -2405    334       C  
ATOM   4040  OD1 ASN D   6      67.470  58.251   9.965  1.00 73.45           O  
ANISOU 4040  OD1 ASN D   6     6530   8300  13079   -122  -2227    348       O  
ATOM   4041  ND2 ASN D   6      68.081  59.585  11.665  1.00 79.73           N  
ANISOU 4041  ND2 ASN D   6     7439   9135  13718   -474  -2691    368       N  
ATOM   4042  N   ASP D   7      64.496  62.004  12.734  1.00 42.85           N  
ANISOU 4042  N   ASP D   7     4137   4484   7659   -918  -2571    173       N  
ATOM   4043  CA  ASP D   7      63.640  63.183  12.831  1.00 44.12           C  
ANISOU 4043  CA  ASP D   7     4595   4643   7524  -1067  -2436    109       C  
ATOM   4044  C   ASP D   7      63.700  63.987  11.527  1.00 40.06           C  
ANISOU 4044  C   ASP D   7     3856   4114   7249  -1157  -2072    103       C  
ATOM   4045  O   ASP D   7      64.770  64.131  10.937  1.00 43.38           O  
ANISOU 4045  O   ASP D   7     3867   4524   8090  -1186  -1979    128       O  
ATOM   4046  CB  ASP D   7      64.149  64.075  13.978  1.00 47.99           C  
ANISOU 4046  CB  ASP D   7     5184   5093   7959  -1229  -2687     35       C  
ATOM   4047  CG  ASP D   7      63.187  65.197  14.314  1.00 52.50           C  
ANISOU 4047  CG  ASP D   7     6138   5620   8191  -1344  -2586    -50       C  
ATOM   4048  OD1 ASP D   7      61.986  64.907  14.465  1.00 51.99           O  
ANISOU 4048  OD1 ASP D   7     6402   5595   7756  -1244  -2498    -20       O  
ATOM   4049  OD2 ASP D   7      63.630  66.365  14.417  1.00 51.05           O  
ANISOU 4049  OD2 ASP D   7     5923   5346   8127  -1537  -2584   -142       O  
ATOM   4050  N   LEU D   8      62.565  64.530  11.098  1.00 34.52           N  
ANISOU 4050  N   LEU D   8     3419   3414   6282  -1199  -1837    100       N  
ATOM   4051  CA  LEU D   8      62.540  65.499  10.016  1.00 44.19           C  
ANISOU 4051  CA  LEU D   8     4514   4593   7682  -1307  -1458    128       C  
ATOM   4052  C   LEU D   8      62.007  66.771  10.657  1.00 35.74           C  
ANISOU 4052  C   LEU D   8     3788   3408   6382  -1459  -1474     64       C  
ATOM   4053  O   LEU D   8      60.789  66.928  10.774  1.00 35.81           O  
ANISOU 4053  O   LEU D   8     4157   3414   6034  -1429  -1401     81       O  
ATOM   4054  CB  LEU D   8      61.606  65.033   8.891  1.00 32.02           C  
ANISOU 4054  CB  LEU D   8     3012   3133   6021  -1206  -1124    216       C  
ATOM   4055  CG  LEU D   8      61.895  63.647   8.319  1.00 32.84           C  
ANISOU 4055  CG  LEU D   8     2911   3346   6220   -996  -1079    230       C  
ATOM   4056  CD1 LEU D   8      60.839  63.237   7.286  1.00 32.19           C  
ANISOU 4056  CD1 LEU D   8     3042   3416   5774   -838   -700    275       C  
ATOM   4057  CD2 LEU D   8      63.328  63.620   7.738  1.00 39.26           C  
ANISOU 4057  CD2 LEU D   8     3185   4131   7600   -993   -976    246       C  
ATOM   4058  N   PRO D   9      62.914  67.650  11.114  1.00 38.18           N  
ANISOU 4058  N   PRO D   9     4001   3613   6893  -1624  -1582    -10       N  
ATOM   4059  CA  PRO D   9      62.547  68.798  11.953  1.00 48.26           C  
ANISOU 4059  CA  PRO D   9     5633   4737   7967  -1770  -1663   -126       C  
ATOM   4060  C   PRO D   9      61.487  69.670  11.317  1.00 47.07           C  
ANISOU 4060  C   PRO D   9     5756   4459   7668  -1785  -1303    -79       C  
ATOM   4061  O   PRO D   9      61.701  70.164  10.210  1.00 42.76           O  
ANISOU 4061  O   PRO D   9     5021   3863   7364  -1831   -954     30       O  
ATOM   4062  CB  PRO D   9      63.854  69.587  12.055  1.00 49.90           C  
ANISOU 4062  CB  PRO D   9     5574   4847   8538  -1988  -1739   -181       C  
ATOM   4063  CG  PRO D   9      64.914  68.557  11.936  1.00 54.15           C  
ANISOU 4063  CG  PRO D   9     5679   5534   9361  -1909  -1906   -111       C  
ATOM   4064  CD  PRO D   9      64.385  67.544  10.954  1.00 42.13           C  
ANISOU 4064  CD  PRO D   9     4049   4131   7829  -1686  -1667      8       C  
ATOM   4065  N   GLY D  10      60.379  69.864  12.029  1.00 38.87           N  
ANISOU 4065  N   GLY D  10     5168   3377   6223  -1722  -1366   -126       N  
ATOM   4066  CA  GLY D  10      59.293  70.707  11.567  1.00 42.26           C  
ANISOU 4066  CA  GLY D  10     5926   3662   6470  -1695  -1038    -47       C  
ATOM   4067  C   GLY D  10      58.386  69.973  10.589  1.00 39.81           C  
ANISOU 4067  C   GLY D  10     5582   3591   5954  -1477   -735    156       C  
ATOM   4068  O   GLY D  10      57.392  70.521  10.132  1.00 35.95           O  
ANISOU 4068  O   GLY D  10     5310   3134   5215  -1329   -389    274       O  
ATOM   4069  N   ILE D  11      58.723  68.732  10.259  1.00 32.52           N  
ANISOU 4069  N   ILE D  11     4372   2874   5110  -1408   -836    192       N  
ATOM   4070  CA  ILE D  11      58.006  68.019   9.190  1.00 28.30           C  
ANISOU 4070  CA  ILE D  11     3768   2597   4389  -1201   -522    345       C  
ATOM   4071  C   ILE D  11      57.329  66.717   9.675  1.00 36.76           C  
ANISOU 4071  C   ILE D  11     4959   3865   5142  -1077   -737    348       C  
ATOM   4072  O   ILE D  11      56.141  66.468   9.398  1.00 35.47           O  
ANISOU 4072  O   ILE D  11     4980   3883   4613   -942   -562    457       O  
ATOM   4073  CB  ILE D  11      58.946  67.710   7.989  1.00 33.61           C  
ANISOU 4073  CB  ILE D  11     4010   3321   5438  -1203   -305    401       C  
ATOM   4074  CG1 ILE D  11      59.381  68.998   7.286  1.00 37.90           C  
ANISOU 4074  CG1 ILE D  11     4450   3709   6243  -1311     22    482       C  
ATOM   4075  CG2 ILE D  11      58.263  66.710   7.014  1.00 35.09           C  
ANISOU 4075  CG2 ILE D  11     4177   3778   5377  -1002    -81    493       C  
ATOM   4076  CD1 ILE D  11      60.448  68.778   6.208  1.00 37.17           C  
ANISOU 4076  CD1 ILE D  11     3907   3666   6550  -1330    255    550       C  
ATOM   4077  N   GLY D  12      58.078  65.893  10.412  1.00 32.97           N  
ANISOU 4077  N   GLY D  12     4362   3347   4817  -1132  -1128    255       N  
ATOM   4078  CA  GLY D  12      57.562  64.609  10.872  1.00 30.44           C  
ANISOU 4078  CA  GLY D  12     4151   3162   4255  -1032  -1338    283       C  
ATOM   4079  C   GLY D  12      58.699  63.653  11.183  1.00 28.13           C  
ANISOU 4079  C   GLY D  12     3588   2814   4286  -1038  -1661    227       C  
ATOM   4080  O   GLY D  12      59.726  64.070  11.702  1.00 31.84           O  
ANISOU 4080  O   GLY D  12     3908   3195   4996  -1083  -1802    157       O  
ATOM   4081  N   LYS D  13      58.533  62.388  10.819  1.00 31.76           N  
ANISOU 4081  N   LYS D  13     3990   3356   4720   -918  -1676    274       N  
ATOM   4082  CA  LYS D  13      59.566  61.383  11.055  1.00 33.26           C  
ANISOU 4082  CA  LYS D  13     3950   3487   5198   -818  -1877    253       C  
ATOM   4083  C   LYS D  13      59.708  60.516   9.818  1.00 28.73           C  
ANISOU 4083  C   LYS D  13     3167   2940   4809   -710  -1673    255       C  
ATOM   4084  O   LYS D  13      58.754  60.315   9.059  1.00 31.19           O  
ANISOU 4084  O   LYS D  13     3650   3362   4841   -663  -1394    283       O  
ATOM   4085  CB  LYS D  13      59.209  60.445  12.223  1.00 32.64           C  
ANISOU 4085  CB  LYS D  13     4137   3404   4861   -716  -2070    309       C  
ATOM   4086  CG  LYS D  13      58.991  61.089  13.562  1.00 40.20           C  
ANISOU 4086  CG  LYS D  13     5343   4350   5581   -760  -2174    306       C  
ATOM   4087  CD  LYS D  13      60.278  61.584  14.146  1.00 39.15           C  
ANISOU 4087  CD  LYS D  13     5022   4139   5716   -819  -2400    239       C  
ATOM   4088  CE  LYS D  13      60.157  61.799  15.634  1.00 45.79           C  
ANISOU 4088  CE  LYS D  13     6124   4965   6308   -844  -2581    232       C  
ATOM   4089  NZ  LYS D  13      61.381  62.513  16.126  1.00 51.16           N  
ANISOU 4089  NZ  LYS D  13     6627   5591   7220   -954  -2815    147       N  
ATOM   4090  N   LYS D  14      60.911  59.989   9.650  1.00 38.28           N  
ANISOU 4090  N   LYS D  14     4027   4067   6451   -626  -1763    225       N  
ATOM   4091  CA  LYS D  14      61.200  59.049   8.597  1.00 32.76           C  
ANISOU 4091  CA  LYS D  14     3173   3365   5909   -438  -1515    198       C  
ATOM   4092  C   LYS D  14      61.582  57.726   9.238  1.00 30.77           C  
ANISOU 4092  C   LYS D  14     2911   2989   5793   -296  -1849    214       C  
ATOM   4093  O   LYS D  14      62.422  57.688  10.132  1.00 33.68           O  
ANISOU 4093  O   LYS D  14     3087   3287   6421   -301  -2211    253       O  
ATOM   4094  CB  LYS D  14      62.380  59.557   7.762  1.00 36.93           C  
ANISOU 4094  CB  LYS D  14     3252   3893   6885   -399  -1251    176       C  
ATOM   4095  CG  LYS D  14      63.009  58.490   6.879  1.00 40.67           C  
ANISOU 4095  CG  LYS D  14     3515   4333   7605   -146  -1037    130       C  
ATOM   4096  CD  LYS D  14      63.943  59.110   5.856  1.00 52.37           C  
ANISOU 4096  CD  LYS D  14     4590   5876   9433   -104   -635    136       C  
ATOM   4097  CE  LYS D  14      65.231  59.556   6.507  1.00 56.34           C  
ANISOU 4097  CE  LYS D  14     4619   6330  10459   -177   -878    199       C  
ATOM   4098  NZ  LYS D  14      66.371  59.310   5.592  1.00 75.58           N  
ANISOU 4098  NZ  LYS D  14     6571   8796  13349     16   -537    219       N  
ATOM   4099  N   PHE D  15      60.981  56.644   8.755  1.00 33.48           N  
ANISOU 4099  N   PHE D  15     3464   3292   5967   -175  -1739    193       N  
ATOM   4100  CA  PHE D  15      61.348  55.303   9.184  1.00 38.54           C  
ANISOU 4100  CA  PHE D  15     4120   3753   6771     -6  -1989    217       C  
ATOM   4101  C   PHE D  15      61.928  54.562   7.992  1.00 34.05           C  
ANISOU 4101  C   PHE D  15     3384   3094   6459    227  -1661    108       C  
ATOM   4102  O   PHE D  15      61.296  54.475   6.947  1.00 36.17           O  
ANISOU 4102  O   PHE D  15     3822   3421   6498    227  -1314     11       O  
ATOM   4103  CB  PHE D  15      60.110  54.547   9.696  1.00 32.15           C  
ANISOU 4103  CB  PHE D  15     3759   2906   5552    -80  -2145    282       C  
ATOM   4104  CG  PHE D  15      59.551  55.105  10.983  1.00 34.47           C  
ANISOU 4104  CG  PHE D  15     4258   3283   5556   -255  -2425    398       C  
ATOM   4105  CD1 PHE D  15      58.746  56.253  10.967  1.00 33.79           C  
ANISOU 4105  CD1 PHE D  15     4313   3380   5144   -411  -2210    395       C  
ATOM   4106  CD2 PHE D  15      59.848  54.508  12.201  1.00 37.52           C  
ANISOU 4106  CD2 PHE D  15     4761   3564   5929   -232  -2613    474       C  
ATOM   4107  CE1 PHE D  15      58.243  56.782  12.136  1.00 34.32           C  
ANISOU 4107  CE1 PHE D  15     4611   3504   4927   -488  -2176    451       C  
ATOM   4108  CE2 PHE D  15      59.336  55.031  13.378  1.00 42.64           C  
ANISOU 4108  CE2 PHE D  15     5642   4299   6260   -355  -2586    523       C  
ATOM   4109  CZ  PHE D  15      58.530  56.182  13.335  1.00 31.51           C  
ANISOU 4109  CZ  PHE D  15     4349   3054   4570   -464  -2358    501       C  
ATOM   4110  N   GLU D  16      63.127  54.027   8.150  1.00 37.75           N  
ANISOU 4110  N   GLU D  16     3524   3431   7388    442  -1771    127       N  
ATOM   4111  CA  GLU D  16      63.705  53.179   7.120  1.00 40.44           C  
ANISOU 4111  CA  GLU D  16     3741   3648   7978    730  -1450     18       C  
ATOM   4112  C   GLU D  16      63.710  51.746   7.611  1.00 44.27           C  
ANISOU 4112  C   GLU D  16     4421   3854   8547    926  -1697     46       C  
ATOM   4113  O   GLU D  16      64.336  51.431   8.626  1.00 44.89           O  
ANISOU 4113  O   GLU D  16     4333   3838   8883   1012  -2087    194       O  
ATOM   4114  CB  GLU D  16      65.117  53.643   6.772  1.00 52.10           C  
ANISOU 4114  CB  GLU D  16     4639   5184   9973    883  -1292     39       C  
ATOM   4115  CG  GLU D  16      65.153  55.082   6.315  1.00 59.40           C  
ANISOU 4115  CG  GLU D  16     5377   6337  10854    662  -1047     43       C  
ATOM   4116  CD  GLU D  16      66.387  55.408   5.509  1.00 78.54           C  
ANISOU 4116  CD  GLU D  16     7268   8829  13744    821   -695     50       C  
ATOM   4117  OE1 GLU D  16      67.222  54.499   5.313  1.00 84.15           O  
ANISOU 4117  OE1 GLU D  16     7735   9425  14814   1139   -631     42       O  
ATOM   4118  OE2 GLU D  16      66.513  56.570   5.064  1.00 81.25           O  
ANISOU 4118  OE2 GLU D  16     7434   9332  14105    641   -456     81       O  
ATOM   4119  N   ILE D  17      63.005  50.889   6.883  1.00 45.78           N  
ANISOU 4119  N   ILE D  17     4978   3904   8512    983  -1485    -88       N  
ATOM   4120  CA  ILE D  17      62.768  49.508   7.293  1.00 45.14           C  
ANISOU 4120  CA  ILE D  17     5199   3500   8452   1112  -1696    -67       C  
ATOM   4121  C   ILE D  17      63.401  48.514   6.335  1.00 47.98           C  
ANISOU 4121  C   ILE D  17     5551   3600   9081   1464  -1384   -242       C  
ATOM   4122  O   ILE D  17      63.266  48.626   5.124  1.00 51.88           O  
ANISOU 4122  O   ILE D  17     6114   4158   9439   1499   -960   -452       O  
ATOM   4123  CB  ILE D  17      61.262  49.239   7.368  1.00 40.82           C  
ANISOU 4123  CB  ILE D  17     5164   2951   7396    824  -1764    -78       C  
ATOM   4124  CG1 ILE D  17      60.611  50.284   8.276  1.00 41.92           C  
ANISOU 4124  CG1 ILE D  17     5318   3362   7248    524  -1997     88       C  
ATOM   4125  CG2 ILE D  17      60.995  47.833   7.854  1.00 43.08           C  
ANISOU 4125  CG2 ILE D  17     5777   2867   7725    904  -1994    -22       C  
ATOM   4126  CD1 ILE D  17      59.149  50.538   7.957  1.00 43.58           C  
ANISOU 4126  CD1 ILE D  17     5870   3735   6952    236  -1888     66       C  
ATOM   4127  N   GLU D  18      64.096  47.534   6.881  1.00 51.85           N  
ANISOU 4127  N   GLU D  18     5976   3789   9936   1750  -1588   -151       N  
ATOM   4128  CA  GLU D  18      64.775  46.565   6.046  1.00 57.68           C  
ANISOU 4128  CA  GLU D  18     6709   4238  10968   2148  -1274   -316       C  
ATOM   4129  C   GLU D  18      64.472  45.156   6.525  1.00 58.95           C  
ANISOU 4129  C   GLU D  18     7289   4060  11048   2205  -1448   -266       C  
ATOM   4130  O   GLU D  18      64.524  44.881   7.717  1.00 65.86           O  
ANISOU 4130  O   GLU D  18     8156   4944  11922   2125  -1824    -14       O  
ATOM   4131  CB  GLU D  18      66.274  46.842   6.068  1.00 68.89           C  
ANISOU 4131  CB  GLU D  18     7533   5833  12807   2413  -1152   -211       C  
ATOM   4132  CG  GLU D  18      67.092  45.991   5.131  1.00 91.61           C  
ANISOU 4132  CG  GLU D  18    10372   8546  15889   2827   -720   -358       C  
ATOM   4133  CD  GLU D  18      68.403  46.658   4.780  1.00103.64           C  
ANISOU 4133  CD  GLU D  18    11277  10363  17740   3006   -469   -287       C  
ATOM   4134  OE1 GLU D  18      69.462  46.019   4.953  1.00110.33           O  
ANISOU 4134  OE1 GLU D  18    11889  11162  18870   3320   -447   -181       O  
ATOM   4135  OE2 GLU D  18      68.367  47.822   4.322  1.00103.45           O  
ANISOU 4135  OE2 GLU D  18    11003  10620  17683   2823   -287   -321       O  
ATOM   4136  N   THR D  19      64.130  44.279   5.586  1.00 66.01           N  
ANISOU 4136  N   THR D  19     8573   4664  11842   2318  -1152   -517       N  
ATOM   4137  CA  THR D  19      63.857  42.886   5.887  1.00 74.23           C  
ANISOU 4137  CA  THR D  19    10035   5332  12838   2368  -1241   -489       C  
ATOM   4138  C   THR D  19      65.140  42.074   5.715  1.00 76.62           C  
ANISOU 4138  C   THR D  19    10153   5442  13517   2855  -1031   -471       C  
ATOM   4139  O   THR D  19      66.154  42.588   5.231  1.00 73.60           O  
ANISOU 4139  O   THR D  19     9335   5252  13380   3126   -784   -506       O  
ATOM   4140  CB  THR D  19      62.770  42.296   4.953  1.00 71.12           C  
ANISOU 4140  CB  THR D  19    10219   4702  12103   2179  -1046   -789       C  
ATOM   4141  OG1 THR D  19      63.264  42.236   3.608  1.00 70.32           O  
ANISOU 4141  OG1 THR D  19    10135   4535  12046   2454   -565  -1118       O  
ATOM   4142  CG2 THR D  19      61.502  43.122   4.993  1.00 72.53           C  
ANISOU 4142  CG2 THR D  19    10563   5122  11872   1713  -1220   -801       C  
ATOM   4143  N   ARG D  20      65.105  40.808   6.107  1.00 80.52           N  
ANISOU 4143  N   ARG D  20    10966   5572  14056   2968  -1107   -394       N  
ATOM   4144  CA  ARG D  20      66.247  39.932   5.868  1.00 85.37           C  
ANISOU 4144  CA  ARG D  20    11493   5951  14994   3476   -874   -384       C  
ATOM   4145  C   ARG D  20      66.392  39.611   4.382  1.00 86.41           C  
ANISOU 4145  C   ARG D  20    11866   5901  15064   3722   -344   -763       C  
ATOM   4146  O   ARG D  20      67.483  39.301   3.910  1.00 88.87           O  
ANISOU 4146  O   ARG D  20    11989   6176  15602   4193    -65   -807       O  
ATOM   4147  CB  ARG D  20      66.150  38.650   6.696  1.00 95.34           C  
ANISOU 4147  CB  ARG D  20    13064   6835  16326   3547  -1074   -184       C  
ATOM   4148  CG  ARG D  20      66.634  38.827   8.120  1.00100.69           C  
ANISOU 4148  CG  ARG D  20    13388   7723  17148   3542  -1514    212       C  
ATOM   4149  CD  ARG D  20      66.666  37.511   8.872  1.00111.59           C  
ANISOU 4149  CD  ARG D  20    15057   8724  18618   3689  -1652    426       C  
ATOM   4150  NE  ARG D  20      65.729  37.519   9.990  1.00114.26           N  
ANISOU 4150  NE  ARG D  20    15570   9141  18703   3269  -2054    647       N  
ATOM   4151  CZ  ARG D  20      65.813  36.713  11.042  1.00118.39           C  
ANISOU 4151  CZ  ARG D  20    16198   9507  19278   3331  -2297    945       C  
ATOM   4152  NH1 ARG D  20      64.912  36.794  12.014  1.00113.78           N  
ANISOU 4152  NH1 ARG D  20    15775   9046  18409   2939  -2615   1130       N  
ATOM   4153  NH2 ARG D  20      66.801  35.830  11.125  1.00125.71           N  
ANISOU 4153  NH2 ARG D  20    17069  10169  20524   3808  -2200   1068       N  
ATOM   4154  N   SER D  21      65.289  39.714   3.645  1.00 86.35           N  
ANISOU 4154  N   SER D  21    12277   5829  14705   3397   -221  -1043       N  
ATOM   4155  CA  SER D  21      65.310  39.537   2.196  1.00 99.98           C  
ANISOU 4155  CA  SER D  21    14286   7449  16253   3562    269  -1441       C  
ATOM   4156  C   SER D  21      65.941  40.755   1.529  1.00106.69           C  
ANISOU 4156  C   SER D  21    14649   8767  17123   3703    506  -1523       C  
ATOM   4157  O   SER D  21      66.072  40.819   0.305  1.00113.29           O  
ANISOU 4157  O   SER D  21    15621   9665  17759   3865    886  -1847       O  
ATOM   4158  CB  SER D  21      63.888  39.336   1.668  1.00 98.21           C  
ANISOU 4158  CB  SER D  21    14593   7087  15637   3075    276  -1707       C  
ATOM   4159  OG  SER D  21      63.886  39.133   0.264  1.00108.44           O  
ANISOU 4159  OG  SER D  21    16149   8295  16760   3168    764  -2118       O  
ATOM   4160  N   HIS D  22      66.352  41.704   2.363  1.00 99.61           N  
ANISOU 4160  N   HIS D  22    13170   8219  16459   3615    260  -1225       N  
ATOM   4161  CA  HIS D  22      66.763  43.037   1.942  1.00102.17           C  
ANISOU 4161  CA  HIS D  22    12980   9008  16833   3575    448  -1223       C  
ATOM   4162  C   HIS D  22      65.743  43.720   1.030  1.00 95.54           C  
ANISOU 4162  C   HIS D  22    12400   8311  15588   3271    656  -1498       C  
ATOM   4163  O   HIS D  22      66.095  44.409   0.075  1.00101.18           O  
ANISOU 4163  O   HIS D  22    12909   9313  16222   3352   1068  -1628       O  
ATOM   4164  CB  HIS D  22      68.173  43.079   1.339  1.00115.49           C  
ANISOU 4164  CB  HIS D  22    14224  10868  18789   4018    823  -1223       C  
ATOM   4165  CG  HIS D  22      68.675  44.476   1.127  1.00124.82           C  
ANISOU 4165  CG  HIS D  22    14810  12539  20077   3899    976  -1114       C  
ATOM   4166  ND1 HIS D  22      69.382  44.857   0.007  1.00131.86           N  
ANISOU 4166  ND1 HIS D  22    15468  13682  20952   4098   1476  -1239       N  
ATOM   4167  CD2 HIS D  22      68.519  45.593   1.871  1.00123.14           C  
ANISOU 4167  CD2 HIS D  22    14236  12602  19950   3565    694   -893       C  
ATOM   4168  CE1 HIS D  22      69.652  46.149   0.079  1.00129.58           C  
ANISOU 4168  CE1 HIS D  22    14692  13788  20754   3873   1511  -1068       C  
ATOM   4169  NE2 HIS D  22      69.149  46.619   1.204  1.00124.68           N  
ANISOU 4169  NE2 HIS D  22    13988  13176  20209   3557   1036   -873       N  
ATOM   4170  N   GLU D  23      64.467  43.521   1.329  1.00 77.62           N  
ANISOU 4170  N   GLU D  23    10583   5883  13026   2898    366  -1563       N  
ATOM   4171  CA  GLU D  23      63.463  44.403   0.779  1.00 67.16           C  
ANISOU 4171  CA  GLU D  23     9405   4884  11230   2499    427  -1681       C  
ATOM   4172  C   GLU D  23      63.528  45.627   1.666  1.00 64.81           C  
ANISOU 4172  C   GLU D  23     8637   4985  11001   2272    167  -1348       C  
ATOM   4173  O   GLU D  23      63.680  45.510   2.888  1.00 60.66           O  
ANISOU 4173  O   GLU D  23     7961   4365  10720   2246   -250  -1088       O  
ATOM   4174  CB  GLU D  23      62.081  43.757   0.809  1.00 63.45           C  
ANISOU 4174  CB  GLU D  23     9557   4225  10328   2119    174  -1796       C  
ATOM   4175  CG  GLU D  23      61.935  42.591  -0.172  1.00 81.72           C  
ANISOU 4175  CG  GLU D  23    12415   6122  12512   2274    422  -2190       C  
ATOM   4176  CD  GLU D  23      61.840  43.057  -1.619  1.00 87.60           C  
ANISOU 4176  CD  GLU D  23    13279   7150  12855   2281    887  -2499       C  
ATOM   4177  OE1 GLU D  23      61.640  44.270  -1.852  1.00 90.35           O  
ANISOU 4177  OE1 GLU D  23    13342   8014  12971   2087    974  -2377       O  
ATOM   4178  OE2 GLU D  23      61.955  42.211  -2.526  1.00 88.37           O  
ANISOU 4178  OE2 GLU D  23    13653   7068  12854   2412   1103  -2819       O  
ATOM   4179  N   LYS D  24      63.460  46.798   1.047  1.00 56.75           N  
ANISOU 4179  N   LYS D  24     7405   4393   9764   2124    421  -1354       N  
ATOM   4180  CA  LYS D  24      63.565  48.053   1.773  1.00 53.04           C  
ANISOU 4180  CA  LYS D  24     6519   4271   9362   1909    228  -1080       C  
ATOM   4181  C   LYS D  24      62.271  48.844   1.624  1.00 49.30           C  
ANISOU 4181  C   LYS D  24     6298   4092   8341   1475    162  -1062       C  
ATOM   4182  O   LYS D  24      61.664  48.876   0.555  1.00 48.49           O  
ANISOU 4182  O   LYS D  24     6474   4103   7849   1393    439  -1253       O  
ATOM   4183  CB  LYS D  24      64.761  48.862   1.260  1.00 72.96           C  
ANISOU 4183  CB  LYS D  24     8485   7021  12215   2132    596  -1036       C  
ATOM   4184  CG  LYS D  24      65.058  50.132   2.043  1.00 72.43           C  
ANISOU 4184  CG  LYS D  24     7968   7242  12312   1914    382   -769       C  
ATOM   4185  CD  LYS D  24      66.217  50.911   1.415  1.00 74.80           C  
ANISOU 4185  CD  LYS D  24     7711   7752  12956   2087    784   -719       C  
ATOM   4186  CE  LYS D  24      66.440  52.248   2.120  1.00 73.89           C  
ANISOU 4186  CE  LYS D  24     7206   7890  12980   1799    569   -486       C  
ATOM   4187  NZ  LYS D  24      66.887  53.320   1.183  1.00 74.47           N  
ANISOU 4187  NZ  LYS D  24     6968   8234  13092   1761   1042   -457       N  
ATOM   4188  N   MET D  25      61.844  49.450   2.722  1.00 44.57           N  
ANISOU 4188  N   MET D  25     5612   3620   7703   1217   -216   -828       N  
ATOM   4189  CA  MET D  25      60.671  50.297   2.734  1.00 46.57           C  
ANISOU 4189  CA  MET D  25     6033   4163   7498    852   -280   -758       C  
ATOM   4190  C   MET D  25      61.051  51.558   3.504  1.00 44.81           C  
ANISOU 4190  C   MET D  25     5432   4166   7426    746   -410   -540       C  
ATOM   4191  O   MET D  25      61.715  51.479   4.538  1.00 46.21           O  
ANISOU 4191  O   MET D  25     5390   4232   7936    816   -706   -403       O  
ATOM   4192  CB  MET D  25      59.511  49.563   3.427  1.00 49.59           C  
ANISOU 4192  CB  MET D  25     6822   4405   7615    618   -638   -704       C  
ATOM   4193  CG  MET D  25      58.172  50.288   3.400  1.00 54.65           C  
ANISOU 4193  CG  MET D  25     7639   5351   7775    266   -689   -620       C  
ATOM   4194  SD  MET D  25      56.848  49.383   4.270  1.00 50.42           S  
ANISOU 4194  SD  MET D  25     7504   4670   6985    -21  -1084   -504       S  
ATOM   4195  CE  MET D  25      56.673  47.945   3.222  1.00 51.57           C  
ANISOU 4195  CE  MET D  25     8037   4484   7073     31   -959   -803       C  
ATOM   4196  N   THR D  26      60.651  52.722   3.001  1.00 35.60           N  
ANISOU 4196  N   THR D  26     4206   3301   6018    580   -202   -506       N  
ATOM   4197  CA  THR D  26      60.814  53.953   3.769  1.00 33.58           C  
ANISOU 4197  CA  THR D  26     3697   3210   5850    427   -345   -322       C  
ATOM   4198  C   THR D  26      59.427  54.516   3.975  1.00 33.37           C  
ANISOU 4198  C   THR D  26     3963   3368   5349    153   -436   -241       C  
ATOM   4199  O   THR D  26      58.683  54.647   3.008  1.00 35.04           O  
ANISOU 4199  O   THR D  26     4356   3737   5221     93   -188   -303       O  
ATOM   4200  CB  THR D  26      61.718  54.963   3.038  1.00 40.37           C  
ANISOU 4200  CB  THR D  26     4174   4225   6939    497     16   -309       C  
ATOM   4201  OG1 THR D  26      63.029  54.396   2.895  1.00 41.50           O  
ANISOU 4201  OG1 THR D  26     3983   4221   7564    775    111   -354       O  
ATOM   4202  CG2 THR D  26      61.832  56.277   3.822  1.00 40.11           C  
ANISOU 4202  CG2 THR D  26     3938   4308   6995    290   -145   -145       C  
ATOM   4203  N   ILE D  27      59.071  54.825   5.221  1.00 30.21           N  
ANISOU 4203  N   ILE D  27     3608   2966   4907      7   -786    -97       N  
ATOM   4204  CA  ILE D  27      57.759  55.447   5.480  1.00 27.64           C  
ANISOU 4204  CA  ILE D  27     3520   2834   4150   -213   -831      7       C  
ATOM   4205  C   ILE D  27      58.000  56.838   6.026  1.00 33.22           C  
ANISOU 4205  C   ILE D  27     4057   3648   4919   -299   -847    109       C  
ATOM   4206  O   ILE D  27      58.728  56.989   7.003  1.00 30.19           O  
ANISOU 4206  O   ILE D  27     3530   3154   4789   -295  -1111    146       O  
ATOM   4207  CB  ILE D  27      56.942  54.644   6.507  1.00 32.36           C  
ANISOU 4207  CB  ILE D  27     4389   3342   4564   -319  -1180     97       C  
ATOM   4208  CG1 ILE D  27      56.598  53.256   5.947  1.00 34.66           C  
ANISOU 4208  CG1 ILE D  27     4902   3474   4793   -286  -1173     -9       C  
ATOM   4209  CG2 ILE D  27      55.618  55.348   6.830  1.00 29.32           C  
ANISOU 4209  CG2 ILE D  27     4186   3190   3764   -514  -1189    235       C  
ATOM   4210  CD1 ILE D  27      55.946  52.317   6.989  1.00 32.04           C  
ANISOU 4210  CD1 ILE D  27     4820   2990   4365   -394  -1517    113       C  
ATOM   4211  N   ILE D  28      57.415  57.856   5.390  1.00 27.96           N  
ANISOU 4211  N   ILE D  28     3419   3181   4024   -375   -580    154       N  
ATOM   4212  CA  ILE D  28      57.515  59.206   5.915  1.00 28.74           C  
ANISOU 4212  CA  ILE D  28     3434   3326   4161   -467   -582    243       C  
ATOM   4213  C   ILE D  28      56.171  59.510   6.574  1.00 33.22           C  
ANISOU 4213  C   ILE D  28     4290   4011   4320   -577   -695    356       C  
ATOM   4214  O   ILE D  28      55.113  59.302   5.956  1.00 31.04           O  
ANISOU 4214  O   ILE D  28     4171   3904   3717   -598   -554    405       O  
ATOM   4215  CB  ILE D  28      57.756  60.253   4.792  1.00 28.92           C  
ANISOU 4215  CB  ILE D  28     3304   3462   4221   -453   -171    266       C  
ATOM   4216  CG1 ILE D  28      58.940  59.870   3.890  1.00 41.94           C  
ANISOU 4216  CG1 ILE D  28     4669   5056   6210   -316     56    174       C  
ATOM   4217  CG2 ILE D  28      57.948  61.657   5.414  1.00 33.40           C  
ANISOU 4217  CG2 ILE D  28     3812   3987   4891   -566   -192    346       C  
ATOM   4218  CD1 ILE D  28      60.304  59.911   4.582  1.00 42.36           C  
ANISOU 4218  CD1 ILE D  28     4386   4937   6774   -297   -130    153       C  
ATOM   4219  N   ILE D  29      56.201  59.972   7.819  1.00 30.34           N  
ANISOU 4219  N   ILE D  29     3992   3577   3961   -644   -949    399       N  
ATOM   4220  CA  ILE D  29      54.955  60.347   8.493  1.00 30.67           C  
ANISOU 4220  CA  ILE D  29     4299   3740   3615   -710   -998    516       C  
ATOM   4221  C   ILE D  29      54.980  61.837   8.740  1.00 29.90           C  
ANISOU 4221  C   ILE D  29     4215   3635   3510   -741   -877    539       C  
ATOM   4222  O   ILE D  29      55.844  62.324   9.469  1.00 33.46           O  
ANISOU 4222  O   ILE D  29     4606   3924   4183   -790  -1059    466       O  
ATOM   4223  CB  ILE D  29      54.784  59.621   9.802  1.00 32.76           C  
ANISOU 4223  CB  ILE D  29     4706   3914   3829   -714  -1269    529       C  
ATOM   4224  CG1 ILE D  29      54.755  58.109   9.566  1.00 34.83           C  
ANISOU 4224  CG1 ILE D  29     4980   4111   4142   -679  -1345    513       C  
ATOM   4225  CG2 ILE D  29      53.492  60.070  10.524  1.00 34.25           C  
ANISOU 4225  CG2 ILE D  29     5006   4205   3802   -679  -1033    539       C  
ATOM   4226  CD1 ILE D  29      54.731  57.356  10.867  1.00 42.66           C  
ANISOU 4226  CD1 ILE D  29     6060   4974   5174   -652  -1462    527       C  
ATOM   4227  N   HIS D  30      54.073  62.559   8.080  1.00 31.18           N  
ANISOU 4227  N   HIS D  30     4452   3959   3436   -713   -579    641       N  
ATOM   4228  CA  HIS D  30      53.991  64.011   8.224  1.00 27.98           C  
ANISOU 4228  CA  HIS D  30     4106   3504   3021   -713   -412    680       C  
ATOM   4229  C   HIS D  30      53.133  64.375   9.416  1.00 35.80           C  
ANISOU 4229  C   HIS D  30     5326   4506   3771   -677   -508    687       C  
ATOM   4230  O   HIS D  30      52.235  63.630   9.791  1.00 34.88           O  
ANISOU 4230  O   HIS D  30     5138   4500   3612   -545   -475    609       O  
ATOM   4231  CB  HIS D  30      53.382  64.657   6.988  1.00 27.59           C  
ANISOU 4231  CB  HIS D  30     4020   3618   2845   -639    -26    810       C  
ATOM   4232  CG  HIS D  30      54.252  64.588   5.775  1.00 30.18           C  
ANISOU 4232  CG  HIS D  30     4112   3939   3418   -630    177    771       C  
ATOM   4233  ND1 HIS D  30      55.145  65.582   5.443  1.00 29.39           N  
ANISOU 4233  ND1 HIS D  30     3869   3683   3614   -661    354    765       N  
ATOM   4234  CD2 HIS D  30      54.382  63.629   4.823  1.00 32.79           C  
ANISOU 4234  CD2 HIS D  30     4337   4388   3735   -593    251    732       C  
ATOM   4235  CE1 HIS D  30      55.764  65.254   4.318  1.00 36.84           C  
ANISOU 4235  CE1 HIS D  30     4606   4687   4703   -625    561    755       C  
ATOM   4236  NE2 HIS D  30      55.328  64.074   3.930  1.00 35.50           N  
ANISOU 4236  NE2 HIS D  30     4475   4678   4334   -570    503    714       N  
ATOM   4237  N   ASP D  31      53.368  65.552   9.978  1.00 34.52           N  
ANISOU 4237  N   ASP D  31     4888   2902   5326   -394  -1112   -606       N  
ATOM   4238  CA  ASP D  31      52.580  65.979  11.123  1.00 33.61           C  
ANISOU 4238  CA  ASP D  31     4976   2791   5001   -186  -1103   -834       C  
ATOM   4239  C   ASP D  31      51.114  66.263  10.833  1.00 38.62           C  
ANISOU 4239  C   ASP D  31     5660   3441   5574    199   -918   -782       C  
ATOM   4240  O   ASP D  31      50.294  66.269  11.763  1.00 36.23           O  
ANISOU 4240  O   ASP D  31     5411   3292   5062    419   -840   -937       O  
ATOM   4241  CB  ASP D  31      53.241  67.155  11.804  1.00 37.08           C  
ANISOU 4241  CB  ASP D  31     5720   2884   5484   -344  -1215  -1118       C  
ATOM   4242  CG  ASP D  31      54.381  66.711  12.659  1.00 46.76           C  
ANISOU 4242  CG  ASP D  31     6851   4272   6643   -650  -1454  -1249       C  
ATOM   4243  OD1 ASP D  31      54.294  65.578  13.192  1.00 44.23           O  
ANISOU 4243  OD1 ASP D  31     6344   4336   6126   -600  -1509  -1178       O  
ATOM   4244  OD2 ASP D  31      55.357  67.463  12.769  1.00 42.28           O  
ANISOU 4244  OD2 ASP D  31     6384   3450   6231   -949  -1602  -1396       O  
ATOM   4245  N   ASP D  32      50.779  66.504   9.566  1.00 34.51           N  
ANISOU 4245  N   ASP D  32     5103   2797   5210    291   -847   -560       N  
ATOM   4246  CA  ASP D  32      49.368  66.714   9.203  1.00 38.69           C  
ANISOU 4246  CA  ASP D  32     5595   3402   5703    682   -725   -476       C  
ATOM   4247  C   ASP D  32      48.675  65.380   8.951  1.00 34.79           C  
ANISOU 4247  C   ASP D  32     4744   3374   5099    715   -695   -310       C  
ATOM   4248  O   ASP D  32      47.492  65.340   8.623  1.00 40.17           O  
ANISOU 4248  O   ASP D  32     5278   4228   5756    988   -623   -223       O  
ATOM   4249  CB  ASP D  32      49.182  67.634   7.985  1.00 39.08           C  
ANISOU 4249  CB  ASP D  32     5801   3119   5927    813   -710   -289       C  
ATOM   4250  CG  ASP D  32      49.817  67.073   6.708  1.00 43.24           C  
ANISOU 4250  CG  ASP D  32     6204   3708   6517    565   -745    -14       C  
ATOM   4251  OD1 ASP D  32      50.363  65.961   6.740  1.00 36.76           O  
ANISOU 4251  OD1 ASP D  32     5156   3165   5645    333   -774      4       O  
ATOM   4252  OD2 ASP D  32      49.772  67.755   5.661  1.00 50.01           O  
ANISOU 4252  OD2 ASP D  32     7220   4323   7458    623   -733    187       O  
ATOM   4253  N   GLY D  33      49.417  64.290   9.081  1.00 29.38           N  
ANISOU 4253  N   GLY D  33     3912   2878   4374    435   -764   -265       N  
ATOM   4254  CA  GLY D  33      48.805  62.986   8.888  1.00 30.95           C  
ANISOU 4254  CA  GLY D  33     3835   3436   4487    419   -742   -124       C  
ATOM   4255  C   GLY D  33      49.163  62.286   7.578  1.00 33.10           C  
ANISOU 4255  C   GLY D  33     3986   3738   4853    272   -788     67       C  
ATOM   4256  O   GLY D  33      48.910  61.098   7.432  1.00 28.30           O  
ANISOU 4256  O   GLY D  33     3201   3356   4196    184   -799    146       O  
ATOM   4257  N   ARG D  34      49.715  63.004   6.603  1.00 29.66           N  
ANISOU 4257  N   ARG D  34     3675   3062   4531    236   -797    140       N  
ATOM   4258  CA  ARG D  34      50.096  62.354   5.345  1.00 29.71           C  
ANISOU 4258  CA  ARG D  34     3602   3125   4559    103   -801    294       C  
ATOM   4259  C   ARG D  34      51.191  61.331   5.585  1.00 26.29           C  
ANISOU 4259  C   ARG D  34     3062   2760   4169   -126   -823    251       C  
ATOM   4260  O   ARG D  34      52.082  61.544   6.431  1.00 27.33           O  
ANISOU 4260  O   ARG D  34     3220   2799   4366   -236   -867    143       O  
ATOM   4261  CB  ARG D  34      50.599  63.390   4.300  1.00 25.98           C  
ANISOU 4261  CB  ARG D  34     3325   2386   4162     77   -762    410       C  
ATOM   4262  CG  ARG D  34      49.570  64.402   3.919  1.00 37.73           C  
ANISOU 4262  CG  ARG D  34     4953   3757   5627    357   -773    505       C  
ATOM   4263  CD  ARG D  34      50.175  65.448   2.968  1.00 49.41           C  
ANISOU 4263  CD  ARG D  34     6700   4904   7168    294   -729    670       C  
ATOM   4264  NE  ARG D  34      51.066  66.387   3.660  1.00 57.65           N  
ANISOU 4264  NE  ARG D  34     7944   5584   8377    141   -695    551       N  
ATOM   4265  CZ  ARG D  34      52.288  66.715   3.248  1.00 68.01           C  
ANISOU 4265  CZ  ARG D  34     9342   6703   9797   -176   -625    608       C  
ATOM   4266  NH1 ARG D  34      53.008  67.582   3.951  1.00 68.79           N  
ANISOU 4266  NH1 ARG D  34     9602   6473  10061   -355   -634    471       N  
ATOM   4267  NH2 ARG D  34      52.793  66.182   2.138  1.00 67.63           N  
ANISOU 4267  NH2 ARG D  34     9212   6803   9683   -334   -536    783       N  
ATOM   4268  N   ARG D  35      51.094  60.204   4.884  1.00 26.80           N  
ANISOU 4268  N   ARG D  35     3006   2982   4193   -180   -818    320       N  
ATOM   4269  CA  ARG D  35      52.219  59.230   4.833  1.00 23.39           C  
ANISOU 4269  CA  ARG D  35     2484   2563   3841   -332   -818    292       C  
ATOM   4270  C   ARG D  35      52.690  59.141   3.380  1.00 28.66           C  
ANISOU 4270  C   ARG D  35     3171   3209   4510   -389   -717    356       C  
ATOM   4271  O   ARG D  35      51.874  59.223   2.465  1.00 29.73           O  
ANISOU 4271  O   ARG D  35     3374   3408   4516   -327   -705    432       O  
ATOM   4272  CB  ARG D  35      51.736  57.828   5.216  1.00 26.06           C  
ANISOU 4272  CB  ARG D  35     2729   3048   4124   -339   -868    292       C  
ATOM   4273  CG  ARG D  35      51.737  57.533   6.694  1.00 33.57           C  
ANISOU 4273  CG  ARG D  35     3666   4043   5047   -338   -944    258       C  
ATOM   4274  CD  ARG D  35      50.709  58.357   7.463  1.00 30.92           C  
ANISOU 4274  CD  ARG D  35     3378   3778   4591   -232   -923    228       C  
ATOM   4275  NE  ARG D  35      50.388  57.653   8.695  1.00 25.92           N  
ANISOU 4275  NE  ARG D  35     2734   3275   3838   -252   -948    237       N  
ATOM   4276  CZ  ARG D  35      49.492  58.032   9.600  1.00 34.21           C  
ANISOU 4276  CZ  ARG D  35     3805   4460   4734   -166   -883    203       C  
ATOM   4277  NH1 ARG D  35      49.275  57.244  10.646  1.00 29.03           N  
ANISOU 4277  NH1 ARG D  35     3160   3942   3929   -227   -878    257       N  
ATOM   4278  NH2 ARG D  35      48.817  59.176   9.467  1.00 26.43           N  
ANISOU 4278  NH2 ARG D  35     2842   3465   3735      0   -804    128       N  
ATOM   4279  N   GLU D  36      53.991  58.937   3.175  1.00 29.12           N  
ANISOU 4279  N   GLU D  36     3151   3221   4692   -499   -645    325       N  
ATOM   4280  CA  GLU D  36      54.485  58.475   1.876  1.00 28.92           C  
ANISOU 4280  CA  GLU D  36     3118   3241   4628   -540   -494    349       C  
ATOM   4281  C   GLU D  36      55.254  57.203   2.147  1.00 31.70           C  
ANISOU 4281  C   GLU D  36     3309   3639   5095   -528   -491    250       C  
ATOM   4282  O   GLU D  36      55.953  57.101   3.151  1.00 32.40           O  
ANISOU 4282  O   GLU D  36     3259   3706   5344   -538   -580    212       O  
ATOM   4283  CB  GLU D  36      55.416  59.503   1.246  1.00 32.10           C  
ANISOU 4283  CB  GLU D  36     3545   3556   5097   -666   -332    420       C  
ATOM   4284  CG  GLU D  36      54.676  60.694   0.635  1.00 41.65           C  
ANISOU 4284  CG  GLU D  36     4994   4658   6171   -646   -314    571       C  
ATOM   4285  CD  GLU D  36      54.642  61.900   1.551  1.00 61.57           C  
ANISOU 4285  CD  GLU D  36     7602   6965   8826   -671   -399    574       C  
ATOM   4286  OE1 GLU D  36      53.570  62.544   1.643  1.00 70.15           O  
ANISOU 4286  OE1 GLU D  36     8856   7971   9827   -511   -484    632       O  
ATOM   4287  OE2 GLU D  36      55.687  62.218   2.161  1.00 64.69           O  
ANISOU 4287  OE2 GLU D  36     7892   7272   9416   -841   -388    501       O  
ATOM   4288  N   ILE D  37      55.127  56.232   1.258  1.00 28.83           N  
ANISOU 4288  N   ILE D  37     2987   3326   4641   -488   -412    202       N  
ATOM   4289  CA  ILE D  37      55.873  54.997   1.405  1.00 27.15           C  
ANISOU 4289  CA  ILE D  37     2664   3089   4563   -419   -389     99       C  
ATOM   4290  C   ILE D  37      56.688  54.842   0.113  1.00 32.58           C  
ANISOU 4290  C   ILE D  37     3336   3828   5217   -407   -129     29       C  
ATOM   4291  O   ILE D  37      56.150  55.050  -0.976  1.00 31.40           O  
ANISOU 4291  O   ILE D  37     3369   3738   4825   -444    -33     38       O  
ATOM   4292  CB  ILE D  37      54.903  53.788   1.546  1.00 30.57           C  
ANISOU 4292  CB  ILE D  37     3221   3478   4917   -383   -511     54       C  
ATOM   4293  CG1 ILE D  37      53.943  53.978   2.736  1.00 33.62           C  
ANISOU 4293  CG1 ILE D  37     3618   3878   5278   -418   -698    145       C  
ATOM   4294  CG2 ILE D  37      55.685  52.486   1.726  1.00 28.50           C  
ANISOU 4294  CG2 ILE D  37     2910   3095   4822   -270   -497    -40       C  
ATOM   4295  CD1 ILE D  37      52.807  52.924   2.761  1.00 37.40           C  
ANISOU 4295  CD1 ILE D  37     4198   4342   5671   -474   -787    137       C  
ATOM   4296  N   TYR D  38      57.963  54.481   0.245  1.00 31.04           N  
ANISOU 4296  N   TYR D  38     2909   3644   5242   -340    -17    -36       N  
ATOM   4297  CA  TYR D  38      58.840  54.249  -0.896  1.00 29.13           C  
ANISOU 4297  CA  TYR D  38     2595   3489   4983   -296    296   -127       C  
ATOM   4298  C   TYR D  38      59.367  52.833  -0.809  1.00 33.36           C  
ANISOU 4298  C   TYR D  38     3048   3953   5676    -65    321   -292       C  
ATOM   4299  O   TYR D  38      59.750  52.376   0.274  1.00 34.98           O  
ANISOU 4299  O   TYR D  38     3082   4082   6127     44    130   -272       O  
ATOM   4300  CB  TYR D  38      60.028  55.216  -0.848  1.00 33.01           C  
ANISOU 4300  CB  TYR D  38     2790   4088   5664   -415    458    -53       C  
ATOM   4301  CG  TYR D  38      59.599  56.657  -0.955  1.00 32.10           C  
ANISOU 4301  CG  TYR D  38     2815   3950   5431   -645    448    118       C  
ATOM   4302  CD1 TYR D  38      59.451  57.266  -2.201  1.00 33.48           C  
ANISOU 4302  CD1 TYR D  38     3187   4182   5353   -750    694    209       C  
ATOM   4303  CD2 TYR D  38      59.303  57.397   0.185  1.00 39.51           C  
ANISOU 4303  CD2 TYR D  38     3745   4786   6481   -733    189    188       C  
ATOM   4304  CE1 TYR D  38      59.042  58.591  -2.308  1.00 38.75           C  
ANISOU 4304  CE1 TYR D  38     4035   4758   5930   -923    669    403       C  
ATOM   4305  CE2 TYR D  38      58.906  58.727   0.090  1.00 35.28           C  
ANISOU 4305  CE2 TYR D  38     3386   4152   5867   -901    183    322       C  
ATOM   4306  CZ  TYR D  38      58.766  59.308  -1.147  1.00 39.71           C  
ANISOU 4306  CZ  TYR D  38     4141   4724   6224   -985    413    446       C  
ATOM   4307  OH  TYR D  38      58.374  60.614  -1.222  1.00 41.86           O  
ANISOU 4307  OH  TYR D  38     4629   4834   6444  -1115    390    612       O  
ATOM   4308  N   ARG D  39      59.449  52.162  -1.951  1.00 32.62           N  
ANISOU 4308  N   ARG D  39     3095   3871   5428     30    557   -457       N  
ATOM   4309  CA  ARG D  39      60.004  50.808  -1.974  1.00 34.93           C  
ANISOU 4309  CA  ARG D  39     3352   4030   5889    301    621   -652       C  
ATOM   4310  C   ARG D  39      61.255  50.723  -2.841  1.00 39.14           C  
ANISOU 4310  C   ARG D  39     3656   4723   6490    455   1026   -793       C  
ATOM   4311  O   ARG D  39      61.268  51.221  -3.968  1.00 41.17           O  
ANISOU 4311  O   ARG D  39     4026   5152   6465    346   1315   -829       O  
ATOM   4312  CB  ARG D  39      58.936  49.824  -2.471  1.00 37.34           C  
ANISOU 4312  CB  ARG D  39     4072   4145   5970    308    535   -808       C  
ATOM   4313  CG  ARG D  39      57.817  49.604  -1.448  1.00 48.29           C  
ANISOU 4313  CG  ARG D  39     5595   5373   7380    185    166   -675       C  
ATOM   4314  CD  ARG D  39      58.231  48.550  -0.430  1.00 48.32           C  
ANISOU 4314  CD  ARG D  39     5539   5126   7695    384     14   -668       C  
ATOM   4315  NE  ARG D  39      58.280  47.231  -1.053  1.00 50.46           N  
ANISOU 4315  NE  ARG D  39     6056   5131   7987    549    105   -908       N  
ATOM   4316  CZ  ARG D  39      59.392  46.574  -1.360  1.00 56.07           C  
ANISOU 4316  CZ  ARG D  39     6660   5747   8897    872    305  -1074       C  
ATOM   4317  NH1 ARG D  39      59.315  45.384  -1.928  1.00 60.98           N  
ANISOU 4317  NH1 ARG D  39     7584   6063   9521   1028    383  -1328       N  
ATOM   4318  NH2 ARG D  39      60.578  47.099  -1.096  1.00 54.89           N  
ANISOU 4318  NH2 ARG D  39     6089   5803   8964   1041    425  -1003       N  
ATOM   4319  N   PHE D  40      62.296  50.099  -2.294  1.00 41.58           N  
ANISOU 4319  N   PHE D  40     3632   5002   7164    723   1047   -852       N  
ATOM   4320  CA  PHE D  40      63.546  49.869  -2.997  1.00 49.21           C  
ANISOU 4320  CA  PHE D  40     4282   6146   8271    942   1450  -1007       C  
ATOM   4321  C   PHE D  40      63.889  48.393  -2.833  1.00 50.46           C  
ANISOU 4321  C   PHE D  40     4468   6050   8654   1376   1431  -1215       C  
ATOM   4322  O   PHE D  40      63.427  47.748  -1.887  1.00 54.67           O  
ANISOU 4322  O   PHE D  40     5144   6299   9329   1463   1061  -1144       O  
ATOM   4323  CB  PHE D  40      64.660  50.702  -2.371  1.00 47.68           C  
ANISOU 4323  CB  PHE D  40     3503   6205   8408    872   1464   -846       C  
ATOM   4324  CG  PHE D  40      64.279  52.130  -2.107  1.00 44.61           C  
ANISOU 4324  CG  PHE D  40     3126   5923   7900    445   1347   -614       C  
ATOM   4325  CD1 PHE D  40      64.487  53.108  -3.066  1.00 59.76           C  
ANISOU 4325  CD1 PHE D  40     5036   8046   9622    184   1695   -549       C  
ATOM   4326  CD2 PHE D  40      63.736  52.498  -0.893  1.00 41.27           C  
ANISOU 4326  CD2 PHE D  40     2753   5376   7553    316    909   -460       C  
ATOM   4327  CE1 PHE D  40      64.141  54.420  -2.818  1.00 55.90           C  
ANISOU 4327  CE1 PHE D  40     4613   7568   9059   -184   1580   -330       C  
ATOM   4328  CE2 PHE D  40      63.388  53.814  -0.641  1.00 45.60           C  
ANISOU 4328  CE2 PHE D  40     3351   5967   8008    -33    814   -290       C  
ATOM   4329  CZ  PHE D  40      63.582  54.768  -1.611  1.00 50.59           C  
ANISOU 4329  CZ  PHE D  40     3999   6735   8488   -274   1138   -224       C  
ATOM   4330  N   ASN D  41      64.686  47.869  -3.752  1.00 54.46           N  
ANISOU 4330  N   ASN D  41     4867   6641   9183   1654   1849  -1464       N  
ATOM   4331  CA  ASN D  41      65.246  46.529  -3.629  1.00 80.87           C  
ANISOU 4331  CA  ASN D  41     8180   9731  12817   2154   1887  -1680       C  
ATOM   4332  C   ASN D  41      66.744  46.581  -3.390  1.00 81.92           C  
ANISOU 4332  C   ASN D  41     7664  10150  13313   2441   2050  -1640       C  
ATOM   4333  O   ASN D  41      67.281  47.624  -3.004  1.00 68.33           O  
ANISOU 4333  O   ASN D  41     5509   8771  11682   2192   2009  -1413       O  
ATOM   4334  CB  ASN D  41      64.965  45.696  -4.881  1.00 89.34           C  
ANISOU 4334  CB  ASN D  41     9710  10644  13592   2318   2221  -2058       C  
ATOM   4335  CG  ASN D  41      64.257  44.398  -4.563  1.00 94.73           C  
ANISOU 4335  CG  ASN D  41    10885  10775  14334   2501   1941  -2206       C  
ATOM   4336  OD1 ASN D  41      64.395  43.857  -3.465  1.00 99.15           O  
ANISOU 4336  OD1 ASN D  41    11345  11068  15260   2695   1613  -2051       O  
ATOM   4337  ND2 ASN D  41      63.489  43.891  -5.521  1.00 97.33           N  
ANISOU 4337  ND2 ASN D  41    11772  10921  14286   2409   2051  -2495       N  
ATOM   4338  N   ASP D  42      67.406  45.453  -3.648  1.00 90.43           N  
ANISOU 4338  N   ASP D  42     8785  11112  14463   2897   2159  -1806       N  
ATOM   4339  CA  ASP D  42      68.837  45.294  -3.386  1.00100.84           C  
ANISOU 4339  CA  ASP D  42     9573  12729  16014   3208   2214  -1717       C  
ATOM   4340  C   ASP D  42      69.741  45.589  -4.584  1.00116.71           C  
ANISOU 4340  C   ASP D  42    11308  15170  17868   3280   2774  -1874       C  
ATOM   4341  O   ASP D  42      70.820  46.160  -4.416  1.00127.07           O  
ANISOU 4341  O   ASP D  42    12037  16913  19330   3257   2854  -1720       O  
ATOM   4342  CB  ASP D  42      69.134  43.884  -2.856  1.00104.33           C  
ANISOU 4342  CB  ASP D  42    10177  12812  16652   3735   1998  -1753       C  
ATOM   4343  CG  ASP D  42      68.764  42.791  -3.840  1.00111.12           C  
ANISOU 4343  CG  ASP D  42    11585  13314  17321   4026   2265  -2108       C  
ATOM   4344  OD1 ASP D  42      67.902  43.045  -4.709  1.00118.76           O  
ANISOU 4344  OD1 ASP D  42    12936  14215  17971   3749   2468  -2316       O  
ATOM   4345  OD2 ASP D  42      69.331  41.677  -3.735  1.00 99.21           O  
ANISOU 4345  OD2 ASP D  42    10155  11586  15954   4533   2255  -2181       O  
ATOM   4346  N   ARG D  43      69.313  45.185  -5.780  1.00116.69           N  
ANISOU 4346  N   ARG D  43    11739  15069  17529   3348   3147  -2179       N  
ATOM   4347  CA  ARG D  43      70.122  45.344  -6.993  1.00114.86           C  
ANISOU 4347  CA  ARG D  43    11334  15250  17059   3449   3705  -2342       C  
ATOM   4348  C   ARG D  43      70.489  46.805  -7.227  1.00114.94           C  
ANISOU 4348  C   ARG D  43    10936  15757  16980   2965   3911  -2097       C  
ATOM   4349  O   ARG D  43      71.568  47.123  -7.723  1.00119.84           O  
ANISOU 4349  O   ARG D  43    11113  16826  17594   3020   4257  -2062       O  
ATOM   4350  CB  ARG D  43      69.396  44.760  -8.215  1.00108.25           C  
ANISOU 4350  CB  ARG D  43    11158  14220  15753   3511   3998  -2712       C  
ATOM   4351  CG  ARG D  43      69.671  45.472  -9.548  1.00102.98           C  
ANISOU 4351  CG  ARG D  43    10485  14022  14619   3304   4541  -2790       C  
ATOM   4352  CD  ARG D  43      71.077  45.213 -10.091  1.00114.97           C  
ANISOU 4352  CD  ARG D  43    11540  15958  16186   3688   4954  -2875       C  
ATOM   4353  NE  ARG D  43      71.274  43.833 -10.516  1.00115.64           N  
ANISOU 4353  NE  ARG D  43    11927  15793  16220   4272   5050  -3261       N  
ATOM   4354  CZ  ARG D  43      72.428  43.350 -10.964  1.00128.30           C  
ANISOU 4354  CZ  ARG D  43    13184  17692  17873   4744   5394  -3411       C  
ATOM   4355  NH1 ARG D  43      73.495  44.136 -11.044  1.00128.90           N  
ANISOU 4355  NH1 ARG D  43    12565  18356  18057   4663   5677  -3188       N  
ATOM   4356  NH2 ARG D  43      72.518  42.079 -11.330  1.00136.63           N  
ANISOU 4356  NH2 ARG D  43    14586  18452  18875   5293   5449  -3791       N  
ATOM   4357  N   ASP D  44      69.584  47.701  -6.867  1.00101.78           N  
ANISOU 4357  N   ASP D  44     9430  13998  15243   2486   3699  -1914       N  
ATOM   4358  CA  ASP D  44      69.899  49.113  -6.927  1.00105.33           C  
ANISOU 4358  CA  ASP D  44     9552  14820  15649   2001   3812  -1633       C  
ATOM   4359  C   ASP D  44      69.140  49.828  -5.822  1.00100.27           C  
ANISOU 4359  C   ASP D  44     8940  13977  15182   1651   3332  -1395       C  
ATOM   4360  O   ASP D  44      68.025  50.302  -6.033  1.00 98.09           O  
ANISOU 4360  O   ASP D  44     9066  13539  14664   1360   3310  -1372       O  
ATOM   4361  CB  ASP D  44      69.557  49.684  -8.303  1.00109.88           C  
ANISOU 4361  CB  ASP D  44    10459  15593  15696   1736   4292  -1685       C  
ATOM   4362  CG  ASP D  44      70.131  51.071  -8.520  1.00115.48           C  
ANISOU 4362  CG  ASP D  44    10832  16689  16355   1270   4479  -1365       C  
ATOM   4363  OD1 ASP D  44      70.640  51.669  -7.547  1.00110.35           O  
ANISOU 4363  OD1 ASP D  44     9737  16113  16078   1089   4187  -1135       O  
ATOM   4364  OD2 ASP D  44      70.066  51.564  -9.666  1.00123.45           O  
ANISOU 4364  OD2 ASP D  44    12072  17915  16919   1068   4888  -1335       O  
ATOM   4365  N   PRO D  45      69.747  49.897  -4.626  1.00 93.20           N  
ANISOU 4365  N   PRO D  45     7630  13116  14666   1693   2934  -1222       N  
ATOM   4366  CA  PRO D  45      69.125  50.527  -3.456  1.00 75.92           C  
ANISOU 4366  CA  PRO D  45     5475  10757  12616   1399   2432  -1009       C  
ATOM   4367  C   PRO D  45      68.753  51.989  -3.702  1.00 77.55           C  
ANISOU 4367  C   PRO D  45     5733  11087  12646    836   2518   -818       C  
ATOM   4368  O   PRO D  45      67.947  52.538  -2.965  1.00 72.16           O  
ANISOU 4368  O   PRO D  45     5228  10213  11977    591   2172   -687       O  
ATOM   4369  CB  PRO D  45      70.211  50.414  -2.382  1.00 77.90           C  
ANISOU 4369  CB  PRO D  45     5235  11178  13185   1538   2098   -879       C  
ATOM   4370  CG  PRO D  45      71.037  49.236  -2.809  1.00 86.02           C  
ANISOU 4370  CG  PRO D  45     6097  12278  14310   2082   2319  -1058       C  
ATOM   4371  CD  PRO D  45      71.064  49.319  -4.306  1.00 87.73           C  
ANISOU 4371  CD  PRO D  45     6440  12650  14245   2062   2923  -1231       C  
ATOM   4372  N   ASP D  46      69.331  52.606  -4.727  1.00 87.85           N  
ANISOU 4372  N   ASP D  46     6920  12694  13764    643   2973   -782       N  
ATOM   4373  CA  ASP D  46      68.988  53.978  -5.088  1.00 81.90           C  
ANISOU 4373  CA  ASP D  46     6311  12002  12805    116   3082   -560       C  
ATOM   4374  C   ASP D  46      67.898  53.998  -6.159  1.00 77.08           C  
ANISOU 4374  C   ASP D  46     6267  11271  11751     45   3387   -624       C  
ATOM   4375  O   ASP D  46      67.489  55.059  -6.628  1.00 72.70           O  
ANISOU 4375  O   ASP D  46     5952  10734  10939   -345   3506   -415       O  
ATOM   4376  CB  ASP D  46      70.227  54.738  -5.578  1.00 97.31           C  
ANISOU 4376  CB  ASP D  46     7855  14350  14769   -119   3380   -414       C  
ATOM   4377  CG  ASP D  46      71.280  54.903  -4.494  1.00103.96           C  
ANISOU 4377  CG  ASP D  46     8139  15364  15995   -144   3048   -338       C  
ATOM   4378  OD1 ASP D  46      70.947  54.720  -3.304  1.00101.53           O  
ANISOU 4378  OD1 ASP D  46     7854  14845  15876    -77   2544   -340       O  
ATOM   4379  OD2 ASP D  46      72.441  55.224  -4.827  1.00112.23           O  
ANISOU 4379  OD2 ASP D  46     8732  16789  17122   -243   3287   -267       O  
ATOM   4380  N   GLU D  47      67.431  52.817  -6.550  1.00 71.02           N  
ANISOU 4380  N   GLU D  47     5765  10366  10855    423   3486   -912       N  
ATOM   4381  CA  GLU D  47      66.393  52.721  -7.561  1.00 62.52           C  
ANISOU 4381  CA  GLU D  47     5355   9199   9201    368   3601   -981       C  
ATOM   4382  C   GLU D  47      65.062  52.492  -6.878  1.00 56.42           C  
ANISOU 4382  C   GLU D  47     5031   8069   8338    348   3018   -945       C  
ATOM   4383  O   GLU D  47      64.901  51.554  -6.100  1.00 54.86           O  
ANISOU 4383  O   GLU D  47     4814   7640   8391    615   2713  -1077       O  
ATOM   4384  CB  GLU D  47      66.676  51.589  -8.552  1.00 72.52           C  
ANISOU 4384  CB  GLU D  47     6767  10535  10251    747   4013  -1349       C  
ATOM   4385  CG  GLU D  47      65.539  51.332  -9.535  1.00 74.03           C  
ANISOU 4385  CG  GLU D  47     7699  10624   9806    696   4008  -1474       C  
ATOM   4386  CD  GLU D  47      65.827  51.896 -10.916  1.00 93.76           C  
ANISOU 4386  CD  GLU D  47    10367  13475  11783    528   4574  -1448       C  
ATOM   4387  OE1 GLU D  47      65.009  52.697 -11.417  1.00 97.84           O  
ANISOU 4387  OE1 GLU D  47    11310  14018  11848    210   4470  -1220       O  
ATOM   4388  OE2 GLU D  47      66.870  51.531 -11.503  1.00 99.04           O  
ANISOU 4388  OE2 GLU D  47    10785  14396  12450    743   4958  -1577       O  
ATOM   4389  N   LEU D  48      64.118  53.376  -7.164  1.00 53.59           N  
ANISOU 4389  N   LEU D  48     5061   7672   7629     35   2878   -736       N  
ATOM   4390  CA  LEU D  48      62.807  53.339  -6.557  1.00 48.35           C  
ANISOU 4390  CA  LEU D  48     4756   6743   6872    -21   2368   -669       C  
ATOM   4391  C   LEU D  48      61.909  52.396  -7.353  1.00 48.70           C  
ANISOU 4391  C   LEU D  48     5293   6695   6517    118   2336   -906       C  
ATOM   4392  O   LEU D  48      61.827  52.508  -8.586  1.00 51.92           O  
ANISOU 4392  O   LEU D  48     5977   7274   6476     68   2633   -968       O  
ATOM   4393  CB  LEU D  48      62.235  54.743  -6.593  1.00 46.31           C  
ANISOU 4393  CB  LEU D  48     4663   6497   6436   -365   2257   -350       C  
ATOM   4394  CG  LEU D  48      60.825  54.874  -6.054  1.00 42.28           C  
ANISOU 4394  CG  LEU D  48     4479   5777   5808   -413   1782   -264       C  
ATOM   4395  CD1 LEU D  48      60.850  54.733  -4.522  1.00 39.54           C  
ANISOU 4395  CD1 LEU D  48     3870   5262   5891   -363   1424   -245       C  
ATOM   4396  CD2 LEU D  48      60.223  56.198  -6.516  1.00 41.37           C  
ANISOU 4396  CD2 LEU D  48     4622   5682   5416   -661   1760     25       C  
ATOM   4397  N   LEU D  49      61.283  51.434  -6.679  1.00 46.37           N  
ANISOU 4397  N   LEU D  49     5121   6134   6363    269   1989  -1045       N  
ATOM   4398  CA  LEU D  49      60.447  50.456  -7.376  1.00 47.38           C  
ANISOU 4398  CA  LEU D  49     5706   6132   6164    347   1922  -1308       C  
ATOM   4399  C   LEU D  49      59.019  50.959  -7.458  1.00 44.17           C  
ANISOU 4399  C   LEU D  49     5628   5709   5445     92   1569  -1154       C  
ATOM   4400  O   LEU D  49      58.359  50.844  -8.491  1.00 45.97           O  
ANISOU 4400  O   LEU D  49     6228   6026   5213     15   1583  -1264       O  
ATOM   4401  CB  LEU D  49      60.449  49.116  -6.641  1.00 47.39           C  
ANISOU 4401  CB  LEU D  49     5710   5803   6494    597   1729  -1517       C  
ATOM   4402  CG  LEU D  49      61.793  48.405  -6.549  1.00 54.89           C  
ANISOU 4402  CG  LEU D  49     6341   6725   7790    962   2028  -1702       C  
ATOM   4403  CD1 LEU D  49      61.717  47.281  -5.519  1.00 56.05           C  
ANISOU 4403  CD1 LEU D  49     6491   6483   8323   1196   1722  -1768       C  
ATOM   4404  CD2 LEU D  49      62.205  47.873  -7.912  1.00 56.93           C  
ANISOU 4404  CD2 LEU D  49     6814   7087   7731   1134   2484  -2047       C  
ATOM   4405  N   SER D  50      58.531  51.494  -6.349  1.00 39.96           N  
ANISOU 4405  N   SER D  50     4946   5084   5152    -17   1237   -913       N  
ATOM   4406  CA  SER D  50      57.183  52.020  -6.326  1.00 37.34           C  
ANISOU 4406  CA  SER D  50     4835   4763   4589   -206    914   -757       C  
ATOM   4407  C   SER D  50      57.068  52.985  -5.161  1.00 33.79           C  
ANISOU 4407  C   SER D  50     4147   4278   4414   -291    717   -479       C  
ATOM   4408  O   SER D  50      57.940  53.052  -4.299  1.00 33.23           O  
ANISOU 4408  O   SER D  50     3775   4152   4699   -230    757   -441       O  
ATOM   4409  CB  SER D  50      56.190  50.863  -6.131  1.00 36.80           C  
ANISOU 4409  CB  SER D  50     4978   4510   4496   -204    623   -946       C  
ATOM   4410  OG  SER D  50      56.322  50.327  -4.817  1.00 34.70           O  
ANISOU 4410  OG  SER D  50     4515   4022   4648   -129    454   -915       O  
ATOM   4411  N   ASN D  51      55.976  53.739  -5.139  1.00 31.98           N  
ANISOU 4411  N   ASN D  51     4053   4090   4009   -414    488   -301       N  
ATOM   4412  CA  ASN D  51      55.745  54.662  -4.030  1.00 33.19           C  
ANISOU 4412  CA  ASN D  51     4041   4180   4388   -467    307    -87       C  
ATOM   4413  C   ASN D  51      54.274  54.998  -4.013  1.00 34.84           C  
ANISOU 4413  C   ASN D  51     4404   4424   4411   -512     23     16       C  
ATOM   4414  O   ASN D  51      53.596  54.847  -5.031  1.00 33.93           O  
ANISOU 4414  O   ASN D  51     4501   4427   3964   -537    -24    -14       O  
ATOM   4415  CB  ASN D  51      56.575  55.944  -4.181  1.00 34.71           C  
ANISOU 4415  CB  ASN D  51     4141   4415   4633   -556    512    100       C  
ATOM   4416  CG  ASN D  51      56.073  56.834  -5.308  1.00 43.21           C  
ANISOU 4416  CG  ASN D  51     5492   5589   5338   -634    580    277       C  
ATOM   4417  OD1 ASN D  51      56.337  56.587  -6.492  1.00 45.13           O  
ANISOU 4417  OD1 ASN D  51     5900   5972   5275   -642    803    227       O  
ATOM   4418  ND2 ASN D  51      55.345  57.875  -4.946  1.00 42.33           N  
ANISOU 4418  ND2 ASN D  51     5457   5400   5227   -664    389    487       N  
ATOM   4419  N   ILE D  52      53.779  55.433  -2.859  1.00 31.06           N  
ANISOU 4419  N   ILE D  52     3799   3874   4128   -509   -172    122       N  
ATOM   4420  CA  ILE D  52      52.362  55.739  -2.744  1.00 31.30           C  
ANISOU 4420  CA  ILE D  52     3886   3974   4032   -509   -417    211       C  
ATOM   4421  C   ILE D  52      52.180  56.826  -1.677  1.00 31.69           C  
ANISOU 4421  C   ILE D  52     3830   3950   4261   -467   -491    359       C  
ATOM   4422  O   ILE D  52      52.955  56.915  -0.722  1.00 32.82           O  
ANISOU 4422  O   ILE D  52     3847   3985   4638   -476   -445    335       O  
ATOM   4423  CB  ILE D  52      51.557  54.452  -2.421  1.00 31.62           C  
ANISOU 4423  CB  ILE D  52     3903   4021   4090   -553   -590     66       C  
ATOM   4424  CG1 ILE D  52      50.055  54.690  -2.579  1.00 37.68           C  
ANISOU 4424  CG1 ILE D  52     4660   4954   4704   -581   -828    142       C  
ATOM   4425  CG2 ILE D  52      51.972  53.868  -1.060  1.00 33.21           C  
ANISOU 4425  CG2 ILE D  52     3954   4074   4591   -540   -607     33       C  
ATOM   4426  CD1 ILE D  52      49.252  53.399  -2.739  1.00 35.20           C  
ANISOU 4426  CD1 ILE D  52     4357   4678   4338   -724   -987    -16       C  
ATOM   4427  N   SER D  53      51.230  57.719  -1.905  1.00 31.20           N  
ANISOU 4427  N   SER D  53     3838   3944   4075   -401   -607    503       N  
ATOM   4428  CA  SER D  53      50.934  58.763  -0.921  1.00 30.02           C  
ANISOU 4428  CA  SER D  53     3637   3690   4078   -315   -667    597       C  
ATOM   4429  C   SER D  53      49.547  58.456  -0.379  1.00 26.32           C  
ANISOU 4429  C   SER D  53     3043   3366   3592   -229   -855    583       C  
ATOM   4430  O   SER D  53      48.654  58.137  -1.164  1.00 32.56           O  
ANISOU 4430  O   SER D  53     3831   4333   4206   -215   -980    608       O  
ATOM   4431  CB  SER D  53      50.895  60.124  -1.618  1.00 45.43           C  
ANISOU 4431  CB  SER D  53     5777   5549   5934   -247   -631    794       C  
ATOM   4432  OG  SER D  53      52.168  60.449  -2.157  1.00 48.70           O  
ANISOU 4432  OG  SER D  53     6286   5856   6363   -386   -412    837       O  
ATOM   4433  N   LEU D  54      49.382  58.574   0.939  1.00 29.85           N  
ANISOU 4433  N   LEU D  54     3374   3769   4197   -188   -871    541       N  
ATOM   4434  CA  LEU D  54      48.157  58.195   1.638  1.00 30.21           C  
ANISOU 4434  CA  LEU D  54     3247   3987   4243   -138   -974    525       C  
ATOM   4435  C   LEU D  54      47.830  59.310   2.624  1.00 31.92           C  
ANISOU 4435  C   LEU D  54     3450   4141   4539     41   -948    542       C  
ATOM   4436  O   LEU D  54      48.740  59.884   3.199  1.00 31.25           O  
ANISOU 4436  O   LEU D  54     3476   3856   4544     29   -877    500       O  
ATOM   4437  CB  LEU D  54      48.441  56.937   2.468  1.00 26.87           C  
ANISOU 4437  CB  LEU D  54     2744   3567   3898   -293   -958    430       C  
ATOM   4438  CG  LEU D  54      48.894  55.698   1.692  1.00 27.43           C  
ANISOU 4438  CG  LEU D  54     2873   3607   3940   -447   -961    355       C  
ATOM   4439  CD1 LEU D  54      49.253  54.586   2.662  1.00 33.50           C  
ANISOU 4439  CD1 LEU D  54     3614   4288   4826   -545   -953    308       C  
ATOM   4440  CD2 LEU D  54      47.742  55.274   0.814  1.00 26.77           C  
ANISOU 4440  CD2 LEU D  54     2744   3712   3714   -511  -1089    353       C  
ATOM   4441  N   ASP D  55      46.550  59.617   2.819  1.00 29.53           N  
ANISOU 4441  N   ASP D  55     2997   4014   4207    208  -1006    580       N  
ATOM   4442  CA  ASP D  55      46.185  60.498   3.930  1.00 29.15           C  
ANISOU 4442  CA  ASP D  55     2933   3920   4224    408   -936    532       C  
ATOM   4443  C   ASP D  55      46.111  59.697   5.228  1.00 37.79           C  
ANISOU 4443  C   ASP D  55     3909   5135   5314    293   -863    436       C  
ATOM   4444  O   ASP D  55      46.327  58.487   5.211  1.00 28.16           O  
ANISOU 4444  O   ASP D  55     2632   3989   4080     66   -886    440       O  
ATOM   4445  CB  ASP D  55      44.908  61.308   3.626  1.00 27.52           C  
ANISOU 4445  CB  ASP D  55     2599   3847   4011    721   -991    611       C  
ATOM   4446  CG  ASP D  55      43.647  60.454   3.458  1.00 39.06           C  
ANISOU 4446  CG  ASP D  55     3700   5709   5434    694  -1073    645       C  
ATOM   4447  OD1 ASP D  55      43.536  59.342   3.998  1.00 35.07           O  
ANISOU 4447  OD1 ASP D  55     3046   5359   4919    451  -1032    590       O  
ATOM   4448  OD2 ASP D  55      42.708  60.962   2.819  1.00 41.26           O  
ANISOU 4448  OD2 ASP D  55     3826   6146   5704    925  -1192    743       O  
ATOM   4449  N   ASP D  56      45.834  60.362   6.346  1.00 27.21           N  
ANISOU 4449  N   ASP D  56     3361   2736   4241    188   -153   -146       N  
ATOM   4450  CA  ASP D  56      45.790  59.678   7.634  1.00 24.58           C  
ANISOU 4450  CA  ASP D  56     3041   2488   3809    205   -302   -286       C  
ATOM   4451  C   ASP D  56      44.799  58.511   7.676  1.00 27.07           C  
ANISOU 4451  C   ASP D  56     3299   3087   3901    250   -300   -199       C  
ATOM   4452  O   ASP D  56      45.143  57.431   8.145  1.00 26.12           O  
ANISOU 4452  O   ASP D  56     3152   3042   3731    180   -394   -255       O  
ATOM   4453  CB  ASP D  56      45.459  60.664   8.764  1.00 27.65           C  
ANISOU 4453  CB  ASP D  56     3624   2729   4153    320   -321   -410       C  
ATOM   4454  CG  ASP D  56      45.287  59.959  10.096  1.00 35.79           C  
ANISOU 4454  CG  ASP D  56     4753   3859   4988    342   -450   -532       C  
ATOM   4455  OD1 ASP D  56      46.304  59.505  10.645  1.00 32.37           O  
ANISOU 4455  OD1 ASP D  56     4316   3380   4605    214   -656   -649       O  
ATOM   4456  OD2 ASP D  56      44.146  59.863  10.586  1.00 32.35           O  
ANISOU 4456  OD2 ASP D  56     4390   3544   4357    491   -340   -494       O  
ATOM   4457  N  ASER D  57      43.582  58.732   7.195  0.59 25.01           N  
ANISOU 4457  N  ASER D  57     3003   2969   3530    362   -205    -48       N  
ATOM   4458  N  BSER D  57      43.579  58.730   7.200  0.41 25.56           N  
ANISOU 4458  N  BSER D  57     3073   3039   3599    362   -205    -48       N  
ATOM   4459  CA ASER D  57      42.559  57.672   7.239  0.59 26.70           C  
ANISOU 4459  CA ASER D  57     3122   3457   3567    355   -205     34       C  
ATOM   4460  CA BSER D  57      42.567  57.663   7.226  0.41 27.29           C  
ANISOU 4460  CA BSER D  57     3195   3532   3642    353   -205     34       C  
ATOM   4461  C  ASER D  57      42.920  56.475   6.332  0.59 30.12           C  
ANISOU 4461  C  ASER D  57     3497   3991   3956    160   -235     70       C  
ATOM   4462  C  BSER D  57      42.974  56.471   6.356  0.41 29.48           C  
ANISOU 4462  C  BSER D  57     3419   3902   3880    159   -236     63       C  
ATOM   4463  O  ASER D  57      42.711  55.311   6.694  0.59 27.56           O  
ANISOU 4463  O  ASER D  57     3163   3780   3530     76   -260     44       O  
ATOM   4464  O  BSER D  57      42.830  55.310   6.756  0.41 26.35           O  
ANISOU 4464  O  BSER D  57     3017   3606   3387     76   -264     31       O  
ATOM   4465  CB ASER D  57      41.177  58.245   6.897  0.59 33.07           C  
ANISOU 4465  CB ASER D  57     3821   4412   4331    517   -130    205       C  
ATOM   4466  CB BSER D  57      41.197  58.184   6.784  0.41 32.00           C  
ANISOU 4466  CB BSER D  57     3679   4288   4193    501   -136    214       C  
ATOM   4467  OG ASER D  57      41.131  58.718   5.569  0.59 38.45           O  
ANISOU 4467  OG ASER D  57     4466   5099   5045    508   -141    364       O  
ATOM   4468  OG BSER D  57      40.243  57.131   6.811  0.41 29.92           O  
ANISOU 4468  OG BSER D  57     3270   4296   3802    433   -148    285       O  
ATOM   4469  N   GLU D  58      43.485  56.761   5.168  1.00 24.99           N  
ANISOU 4469  N   GLU D  58     2860   3263   3373     85   -193    124       N  
ATOM   4470  CA  GLU D  58      43.931  55.705   4.266  1.00 27.54           C  
ANISOU 4470  CA  GLU D  58     3201   3623   3642    -93   -156    125       C  
ATOM   4471  C   GLU D  58      45.044  54.888   4.889  1.00 26.52           C  
ANISOU 4471  C   GLU D  58     3068   3366   3643   -148   -164    -19       C  
ATOM   4472  O   GLU D  58      45.064  53.650   4.751  1.00 25.20           O  
ANISOU 4472  O   GLU D  58     2927   3249   3400   -243   -143    -41       O  
ATOM   4473  CB  GLU D  58      44.394  56.281   2.936  1.00 23.99           C  
ANISOU 4473  CB  GLU D  58     2826   3078   3209   -155    -48    207       C  
ATOM   4474  CG  GLU D  58      43.273  56.922   2.137  1.00 30.41           C  
ANISOU 4474  CG  GLU D  58     3663   4038   3852    -97    -94    404       C  
ATOM   4475  CD  GLU D  58      43.785  57.547   0.860  1.00 43.97           C  
ANISOU 4475  CD  GLU D  58     5540   5631   5536   -154     21    510       C  
ATOM   4476  OE1 GLU D  58      44.850  58.214   0.884  1.00 33.58           O  
ANISOU 4476  OE1 GLU D  58     4267   4060   4430   -154    163    454       O  
ATOM   4477  OE2 GLU D  58      43.130  57.352  -0.174  1.00 51.63           O  
ANISOU 4477  OE2 GLU D  58     6605   6756   6257   -225    -35    653       O  
ATOM   4478  N   ALA D  59      45.995  55.579   5.537  1.00 22.22           N  
ANISOU 4478  N   ALA D  59     2492   2639   3310    -94   -208   -111       N  
ATOM   4479  CA  ALA D  59      47.122  54.854   6.123  1.00 24.12           C  
ANISOU 4479  CA  ALA D  59     2670   2773   3723   -121   -279   -214       C  
ATOM   4480  C   ALA D  59      46.630  53.932   7.232  1.00 27.70           C  
ANISOU 4480  C   ALA D  59     3185   3325   4013    -74   -409   -235       C  
ATOM   4481  O   ALA D  59      47.127  52.818   7.408  1.00 25.22           O  
ANISOU 4481  O   ALA D  59     2865   2979   3738    -92   -433   -247       O  
ATOM   4482  CB  ALA D  59      48.166  55.828   6.680  1.00 21.80           C  
ANISOU 4482  CB  ALA D  59     2299   2294   3690   -113   -377   -308       C  
ATOM   4483  N   ARG D  60      45.700  54.428   8.030  1.00 27.81           N  
ANISOU 4483  N   ARG D  60     3282   3426   3859      6   -462   -232       N  
ATOM   4484  CA  ARG D  60      45.224  53.639   9.151  1.00 25.55           C  
ANISOU 4484  CA  ARG D  60     3102   3215   3390     41   -535   -241       C  
ATOM   4485  C   ARG D  60      44.379  52.465   8.692  1.00 24.46           C  
ANISOU 4485  C   ARG D  60     2969   3222   3102    -49   -426   -153       C  
ATOM   4486  O   ARG D  60      44.325  51.432   9.379  1.00 27.58           O  
ANISOU 4486  O   ARG D  60     3464   3617   3399    -68   -453   -145       O  
ATOM   4487  CB  ARG D  60      44.405  54.514  10.135  1.00 24.36           C  
ANISOU 4487  CB  ARG D  60     3067   3101   3087    153   -532   -273       C  
ATOM   4488  CG  ARG D  60      45.369  55.392  10.998  1.00 24.32           C  
ANISOU 4488  CG  ARG D  60     3166   2910   3164    192   -706   -415       C  
ATOM   4489  CD  ARG D  60      44.630  56.148  12.143  1.00 26.27           C  
ANISOU 4489  CD  ARG D  60     3643   3141   3199    301   -669   -492       C  
ATOM   4490  NE  ARG D  60      43.772  57.184  11.554  1.00 28.15           N  
ANISOU 4490  NE  ARG D  60     3826   3384   3487    398   -465   -446       N  
ATOM   4491  CZ  ARG D  60      42.467  57.061  11.347  1.00 33.97           C  
ANISOU 4491  CZ  ARG D  60     4484   4292   4132    486   -268   -326       C  
ATOM   4492  NH1 ARG D  60      41.808  58.051  10.783  1.00 32.49           N  
ANISOU 4492  NH1 ARG D  60     4216   4093   4038    613   -129   -253       N  
ATOM   4493  NH2 ARG D  60      41.819  55.953  11.709  1.00 33.33           N  
ANISOU 4493  NH2 ARG D  60     4388   4385   3891    447   -213   -262       N  
ATOM   4494  N   GLN D  61      43.670  52.633   7.591  1.00 23.44           N  
ANISOU 4494  N   GLN D  61     2761   3210   2937   -118   -323    -80       N  
ATOM   4495  CA  GLN D  61      42.910  51.496   7.045  1.00 25.28           C  
ANISOU 4495  CA  GLN D  61     3003   3572   3029   -275   -257    -21       C  
ATOM   4496  C   GLN D  61      43.848  50.394   6.570  1.00 27.17           C  
ANISOU 4496  C   GLN D  61     3330   3661   3332   -374   -215    -72       C  
ATOM   4497  O   GLN D  61      43.624  49.191   6.834  1.00 25.65           O  
ANISOU 4497  O   GLN D  61     3240   3451   3055   -465   -179    -71       O  
ATOM   4498  CB  GLN D  61      41.995  51.932   5.918  1.00 29.34           C  
ANISOU 4498  CB  GLN D  61     3419   4259   3468   -349   -234     74       C  
ATOM   4499  CG  GLN D  61      40.792  52.792   6.355  1.00 30.20           C  
ANISOU 4499  CG  GLN D  61     3386   4543   3546   -225   -242    166       C  
ATOM   4500  CD  GLN D  61      39.878  53.103   5.207  1.00 45.31           C  
ANISOU 4500  CD  GLN D  61     5162   6652   5401   -287   -291    304       C  
ATOM   4501  OE1 GLN D  61      40.320  53.551   4.155  1.00 48.47           O  
ANISOU 4501  OE1 GLN D  61     5618   7000   5797   -309   -320    341       O  
ATOM   4502  NE2 GLN D  61      38.589  52.842   5.389  1.00 58.35           N  
ANISOU 4502  NE2 GLN D  61     6627   8539   7005   -327   -305    399       N  
ATOM   4503  N   ILE D  62      44.867  50.800   5.835  1.00 27.08           N  
ANISOU 4503  N   ILE D  62     3288   3516   3486   -355   -171   -110       N  
ATOM   4504  CA  ILE D  62      45.842  49.850   5.345  1.00 25.34           C  
ANISOU 4504  CA  ILE D  62     3124   3121   3384   -400    -61   -160       C  
ATOM   4505  C   ILE D  62      46.543  49.189   6.544  1.00 27.01           C  
ANISOU 4505  C   ILE D  62     3338   3204   3720   -277   -167   -180       C  
ATOM   4506  O   ILE D  62      46.759  47.972   6.525  1.00 25.65           O  
ANISOU 4506  O   ILE D  62     3273   2920   3554   -300    -90   -180       O  
ATOM   4507  CB  ILE D  62      46.830  50.478   4.344  1.00 27.20           C  
ANISOU 4507  CB  ILE D  62     3298   3233   3806   -399     75   -188       C  
ATOM   4508  CG1 ILE D  62      46.110  50.757   3.019  1.00 26.75           C  
ANISOU 4508  CG1 ILE D  62     3353   3284   3528   -545    183   -141       C  
ATOM   4509  CG2 ILE D  62      48.002  49.538   4.091  1.00 28.21           C  
ANISOU 4509  CG2 ILE D  62     3423   3146   4150   -373    231   -245       C  
ATOM   4510  CD1 ILE D  62      46.870  51.709   2.099  1.00 32.25           C  
ANISOU 4510  CD1 ILE D  62     4035   3875   4344   -542    332   -126       C  
ATOM   4511  N   ALA D  63      46.884  49.975   7.568  1.00 24.20           N  
ANISOU 4511  N   ALA D  63     2907   2846   3443   -151   -353   -191       N  
ATOM   4512  CA  ALA D  63      47.563  49.428   8.751  1.00 25.19           C  
ANISOU 4512  CA  ALA D  63     3063   2871   3639    -33   -536   -186       C  
ATOM   4513  C   ALA D  63      46.680  48.405   9.494  1.00 25.87           C  
ANISOU 4513  C   ALA D  63     3365   3004   3461    -55   -533   -121       C  
ATOM   4514  O   ALA D  63      47.176  47.401  10.012  1.00 24.93           O  
ANISOU 4514  O   ALA D  63     3342   2753   3377     14   -589    -71       O  
ATOM   4515  CB  ALA D  63      47.999  50.519   9.693  1.00 26.35           C  
ANISOU 4515  CB  ALA D  63     3154   3017   3841     51   -772   -235       C  
ATOM   4516  N   ALA D  64      45.388  48.677   9.559  1.00 26.53           N  
ANISOU 4516  N   ALA D  64     3509   3260   3310   -141   -456   -101       N  
ATOM   4517  CA  ALA D  64      44.478  47.746  10.251  1.00 29.29           C  
ANISOU 4517  CA  ALA D  64     4041   3656   3433   -205   -395    -32       C  
ATOM   4518  C   ALA D  64      44.399  46.407   9.496  1.00 25.41           C  
ANISOU 4518  C   ALA D  64     3639   3066   2950   -352   -243    -10       C  
ATOM   4519  O   ALA D  64      44.391  45.333  10.125  1.00 30.41           O  
ANISOU 4519  O   ALA D  64     4469   3574   3510   -357   -218     52       O  
ATOM   4520  CB  ALA D  64      43.095  48.360  10.395  1.00 24.74           C  
ANISOU 4520  CB  ALA D  64     3420   3299   2682   -269   -302    -10       C  
ATOM   4521  N   ILE D  65      44.346  46.464   8.171  1.00 26.10           N  
ANISOU 4521  N   ILE D  65     3643   3177   3095   -477   -132    -59       N  
ATOM   4522  CA  ILE D  65      44.328  45.223   7.381  1.00 30.75           C  
ANISOU 4522  CA  ILE D  65     4389   3630   3665   -642     32    -83       C  
ATOM   4523  C   ILE D  65      45.654  44.480   7.539  1.00 27.16           C  
ANISOU 4523  C   ILE D  65     4013   2881   3426   -473     63    -88       C  
ATOM   4524  O   ILE D  65      45.688  43.270   7.818  1.00 26.47           O  
ANISOU 4524  O   ILE D  65     4135   2602   3319   -491    149    -53       O  
ATOM   4525  CB  ILE D  65      44.062  45.532   5.896  1.00 29.48           C  
ANISOU 4525  CB  ILE D  65     4188   3554   3459   -816    127   -148       C  
ATOM   4526  CG1 ILE D  65      42.635  46.074   5.702  1.00 28.56           C  
ANISOU 4526  CG1 ILE D  65     3960   3739   3151   -979     57   -100       C  
ATOM   4527  CG2 ILE D  65      44.285  44.269   4.981  1.00 28.65           C  
ANISOU 4527  CG2 ILE D  65     4328   3239   3319   -990    326   -227       C  
ATOM   4528  CD1 ILE D  65      42.378  46.569   4.240  1.00 28.97           C  
ANISOU 4528  CD1 ILE D  65     3985   3908   3114  -1124     61   -123       C  
ATOM   4529  N   LEU D  66      46.759  45.211   7.367  1.00 25.66           N  
ANISOU 4529  N   LEU D  66     3633   2637   3479   -301      4   -118       N  
ATOM   4530  CA  LEU D  66      48.086  44.588   7.428  1.00 25.03           C  
ANISOU 4530  CA  LEU D  66     3515   2298   3697   -109     37   -106       C  
ATOM   4531  C   LEU D  66      48.341  43.975   8.808  1.00 27.83           C  
ANISOU 4531  C   LEU D  66     3961   2557   4055     63   -168     12       C  
ATOM   4532  O   LEU D  66      48.964  42.912   8.945  1.00 30.93           O  
ANISOU 4532  O   LEU D  66     4450   2704   4597    195   -109     76       O  
ATOM   4533  CB  LEU D  66      49.175  45.666   7.134  1.00 27.30           C  
ANISOU 4533  CB  LEU D  66     3495   2591   4288     12    -19   -145       C  
ATOM   4534  CG  LEU D  66      50.607  45.141   7.085  1.00 35.55           C  
ANISOU 4534  CG  LEU D  66     4370   3397   5741    220     34   -123       C  
ATOM   4535  CD1 LEU D  66      50.745  44.110   5.962  1.00 38.74           C  
ANISOU 4535  CD1 LEU D  66     4944   3586   6190    175    431   -177       C  
ATOM   4536  CD2 LEU D  66      51.613  46.305   6.892  1.00 30.26           C  
ANISOU 4536  CD2 LEU D  66     3337   2760   5402    282    -34   -157       C  
ATOM   4537  N   GLY D  67      47.854  44.661   9.833  1.00 25.56           N  
ANISOU 4537  N   GLY D  67     2633   2849   4230   -259  -1241   -306       N  
ATOM   4538  CA  GLY D  67      48.121  44.303  11.213  1.00 30.56           C  
ANISOU 4538  CA  GLY D  67     3771   3384   4458   -349  -1330   -371       C  
ATOM   4539  C   GLY D  67      47.203  43.234  11.802  1.00 28.75           C  
ANISOU 4539  C   GLY D  67     3790   3206   3927   -363   -944   -433       C  
ATOM   4540  O   GLY D  67      47.323  42.917  13.002  1.00 31.08           O  
ANISOU 4540  O   GLY D  67     4497   3474   3838   -399   -957   -457       O  
ATOM   4541  N   GLY D  68      46.296  42.702  10.997  1.00 28.40           N  
ANISOU 4541  N   GLY D  68     3489   3235   4069   -334   -637   -423       N  
ATOM   4542  CA  GLY D  68      45.459  41.580  11.421  1.00 33.50           C  
ANISOU 4542  CA  GLY D  68     4269   3897   4564   -390   -344   -361       C  
ATOM   4543  C   GLY D  68      44.229  41.999  12.221  1.00 38.08           C  
ANISOU 4543  C   GLY D  68     4996   4514   4959   -391     47   -475       C  
ATOM   4544  O   GLY D  68      43.602  41.179  12.907  1.00 35.76           O  
ANISOU 4544  O   GLY D  68     4837   4268   4482   -436    290   -329       O  
ATOM   4545  N   MET D  69      43.864  43.270  12.099  1.00 28.38           N  
ANISOU 4545  N   MET D  69     3705   3278   3798   -309    115   -686       N  
ATOM   4546  CA  MET D  69      42.729  43.851  12.816  1.00 34.96           C  
ANISOU 4546  CA  MET D  69     4683   4179   4420   -203    500   -808       C  
ATOM   4547  C   MET D  69      41.412  43.732  12.048  1.00 36.30           C  
ANISOU 4547  C   MET D  69     4465   4435   4892   -220    888   -731       C  
ATOM   4548  O   MET D  69      40.352  44.000  12.604  1.00 35.20           O  
ANISOU 4548  O   MET D  69     4371   4410   4594   -115   1282   -717       O  
ATOM   4549  CB  MET D  69      42.990  45.328  13.132  1.00 39.45           C  
ANISOU 4549  CB  MET D  69     5441   4641   4908    -63    328  -1106       C  
ATOM   4550  CG  MET D  69      44.163  45.563  14.045  1.00 44.85           C  
ANISOU 4550  CG  MET D  69     6556   5201   5283    -50   -111  -1197       C  
ATOM   4551  SD  MET D  69      43.850  44.826  15.666  1.00 57.69           S  
ANISOU 4551  SD  MET D  69     8713   6987   6220     84    129  -1150       S  
ATOM   4552  CE  MET D  69      45.357  45.272  16.530  1.00138.85           C  
ANISOU 4552  CE  MET D  69    19472  17072  16212     82   -532  -1303       C  
ATOM   4553  N   VAL D  70      41.465  43.367  10.775  1.00 33.36           N  
ANISOU 4553  N   VAL D  70     3713   4031   4932   -308    770   -665       N  
ATOM   4554  CA  VAL D  70      40.227  43.124  10.022  1.00 34.47           C  
ANISOU 4554  CA  VAL D  70     3490   4226   5381   -356   1056   -573       C  
ATOM   4555  C   VAL D  70      40.021  41.625   9.895  1.00 33.09           C  
ANISOU 4555  C   VAL D  70     3268   3996   5309   -506   1007   -324       C  
ATOM   4556  O   VAL D  70      39.031  41.061  10.394  1.00 35.74           O  
ANISOU 4556  O   VAL D  70     3563   4369   5645   -595   1283    -93       O  
ATOM   4557  CB  VAL D  70      40.264  43.773   8.620  1.00 30.52           C  
ANISOU 4557  CB  VAL D  70     2598   3727   5271   -309    934   -688       C  
ATOM   4558  CG1 VAL D  70      38.931  43.510   7.869  1.00 37.85           C  
ANISOU 4558  CG1 VAL D  70     3443   4682   6255   -310   1002   -517       C  
ATOM   4559  CG2 VAL D  70      40.522  45.291   8.758  1.00 32.16           C  
ANISOU 4559  CG2 VAL D  70     2838   3923   5460   -186    912   -895       C  
ATOM   4560  N   TYR D  71      40.983  40.972   9.260  1.00 30.81           N  
ANISOU 4560  N   TYR D  71     2981   3613   5114   -510    635   -328       N  
ATOM   4561  CA  TYR D  71      41.001  39.515   9.283  1.00 34.20           C  
ANISOU 4561  CA  TYR D  71     3479   3912   5605   -621    488   -129       C  
ATOM   4562  C   TYR D  71      42.187  39.062  10.118  1.00 30.01           C  
ANISOU 4562  C   TYR D  71     3299   3354   4750   -605    283    -69       C  
ATOM   4563  O   TYR D  71      43.322  39.383   9.827  1.00 28.98           O  
ANISOU 4563  O   TYR D  71     3221   3243   4547   -490     21   -165       O  
ATOM   4564  CB  TYR D  71      41.099  38.940   7.888  1.00 32.68           C  
ANISOU 4564  CB  TYR D  71     3066   3614   5735   -558    199   -188       C  
ATOM   4565  CG  TYR D  71      41.186  37.434   7.881  1.00 34.45           C  
ANISOU 4565  CG  TYR D  71     3426   3616   6048   -637    -57    -33       C  
ATOM   4566  CD1 TYR D  71      40.057  36.662   8.113  1.00 37.35           C  
ANISOU 4566  CD1 TYR D  71     3709   3828   6656   -859     23    190       C  
ATOM   4567  CD2 TYR D  71      42.401  36.787   7.649  1.00 30.69           C  
ANISOU 4567  CD2 TYR D  71     3142   3070   5449   -479   -401    -62       C  
ATOM   4568  CE1 TYR D  71      40.124  35.274   8.091  1.00 40.28           C  
ANISOU 4568  CE1 TYR D  71     4204   3912   7190   -954   -293    348       C  
ATOM   4569  CE2 TYR D  71      42.481  35.391   7.641  1.00 33.20           C  
ANISOU 4569  CE2 TYR D  71     3623   3128   5865   -519   -674     57       C  
ATOM   4570  CZ  TYR D  71      41.328  34.649   7.862  1.00 40.79           C  
ANISOU 4570  CZ  TYR D  71     4516   3872   7110   -774   -643    246       C  
ATOM   4571  OH  TYR D  71      41.343  33.266   7.844  1.00 43.81           O  
ANISOU 4571  OH  TYR D  71     5050   3915   7681   -847   -987    386       O  
ATOM   4572  N   LYS D  72      41.909  38.332  11.182  1.00 31.34           N  
ANISOU 4572  N   LYS D  72     3670   3505   4732   -718    413    153       N  
ATOM   4573  CA  LYS D  72      42.975  37.752  11.995  1.00 30.46           C  
ANISOU 4573  CA  LYS D  72     3884   3368   4320   -716    216    251       C  
ATOM   4574  C   LYS D  72      43.372  36.398  11.408  1.00 42.60           C  
ANISOU 4574  C   LYS D  72     5408   4700   6077   -756    -92    385       C  
ATOM   4575  O   LYS D  72      42.517  35.549  11.151  1.00 39.11           O  
ANISOU 4575  O   LYS D  72     4837   4103   5921   -883    -77    548       O  
ATOM   4576  CB  LYS D  72      42.448  37.552  13.421  1.00 39.76           C  
ANISOU 4576  CB  LYS D  72     5273   4664   5169   -770    518    473       C  
ATOM   4577  CG  LYS D  72      43.271  36.572  14.244  1.00 50.78           C  
ANISOU 4577  CG  LYS D  72     6949   6018   6326   -817    341    688       C  
ATOM   4578  CD  LYS D  72      42.518  36.125  15.493  1.00 50.00           C  
ANISOU 4578  CD  LYS D  72     6950   6071   5976   -856    682   1032       C  
ATOM   4579  CE  LYS D  72      43.281  35.050  16.220  1.00 53.41           C  
ANISOU 4579  CE  LYS D  72     7608   6452   6235   -920    500   1297       C  
ATOM   4580  NZ  LYS D  72      43.278  33.802  15.431  1.00 58.02           N  
ANISOU 4580  NZ  LYS D  72     8019   6732   7293  -1084    236   1478       N  
ATOM   4581  N   PRO D  73      44.669  36.167  11.223  1.00 32.57           N  
ANISOU 4581  N   PRO D  73     4276   3407   4691   -635   -407    346       N  
ATOM   4582  CA  PRO D  73      45.137  34.861  10.736  1.00 30.92           C  
ANISOU 4582  CA  PRO D  73     4128   2995   4625   -583   -715    451       C  
ATOM   4583  C   PRO D  73      44.664  33.770  11.715  1.00 34.15           C  
ANISOU 4583  C   PRO D  73     4695   3257   5023   -792   -650    751       C  
ATOM   4584  O   PRO D  73      44.893  33.862  12.913  1.00 37.00           O  
ANISOU 4584  O   PRO D  73     5248   3747   5063   -865   -500    905       O  
ATOM   4585  CB  PRO D  73      46.653  35.011  10.792  1.00 34.81           C  
ANISOU 4585  CB  PRO D  73     4759   3590   4878   -405   -956    452       C  
ATOM   4586  CG  PRO D  73      46.859  36.533  10.554  1.00 37.22           C  
ANISOU 4586  CG  PRO D  73     4902   4102   5139   -337   -877    282       C  
ATOM   4587  CD  PRO D  73      45.773  37.132  11.396  1.00 40.05           C  
ANISOU 4587  CD  PRO D  73     5307   4499   5410   -517   -534    232       C  
ATOM   4588  N   GLN D  74      43.987  32.767  11.184  1.00 35.24           N  
ANISOU 4588  N   GLN D  74     4741   3120   5528   -878   -799    851       N  
ATOM   4589  CA  GLN D  74      43.229  31.830  11.999  1.00 38.79           C  
ANISOU 4589  CA  GLN D  74     5202   3414   6122  -1131   -721   1230       C  
ATOM   4590  C   GLN D  74      44.104  30.988  12.920  1.00 44.29           C  
ANISOU 4590  C   GLN D  74     6177   4060   6591  -1148   -846   1471       C  
ATOM   4591  O   GLN D  74      43.643  30.526  13.960  1.00 45.26           O  
ANISOU 4591  O   GLN D  74     6314   4212   6668  -1329   -660   1851       O  
ATOM   4592  CB  GLN D  74      42.400  30.947  11.061  1.00 45.78           C  
ANISOU 4592  CB  GLN D  74     5919   3919   7554  -1233  -1010   1271       C  
ATOM   4593  CG  GLN D  74      41.648  29.803  11.702  1.00 67.49           C  
ANISOU 4593  CG  GLN D  74     8615   6400  10629  -1529  -1076   1748       C  
ATOM   4594  CD  GLN D  74      40.856  29.014  10.675  1.00 79.91           C  
ANISOU 4594  CD  GLN D  74    10029   7626  12708  -1574  -1453   1681       C  
ATOM   4595  OE1 GLN D  74      40.053  29.580   9.930  1.00 81.69           O  
ANISOU 4595  OE1 GLN D  74    10018   7924  13095  -1564  -1385   1515       O  
ATOM   4596  NE2 GLN D  74      41.094  27.707  10.614  1.00 82.74           N  
ANISOU 4596  NE2 GLN D  74    10522   7701  13215  -1550  -1849   1747       N  
ATOM   4597  N   ALA D  75      45.370  30.795  12.570  1.00 38.22           N  
ANISOU 4597  N   ALA D  75     5597   3259   5666   -933  -1135   1312       N  
ATOM   4598  CA  ALA D  75      46.194  29.857  13.335  1.00 44.70           C  
ANISOU 4598  CA  ALA D  75     6665   3991   6328   -942  -1296   1563       C  
ATOM   4599  C   ALA D  75      46.905  30.460  14.545  1.00 48.45           C  
ANISOU 4599  C   ALA D  75     7317   4794   6297   -947  -1099   1661       C  
ATOM   4600  O   ALA D  75      47.532  29.738  15.322  1.00 49.84           O  
ANISOU 4600  O   ALA D  75     7686   4946   6303   -975  -1191   1911       O  
ATOM   4601  CB  ALA D  75      47.187  29.109  12.418  1.00 45.94           C  
ANISOU 4601  CB  ALA D  75     6953   3925   6577   -667  -1731   1426       C  
ATOM   4602  N   LEU D  76      46.782  31.772  14.725  1.00 44.69           N  
ANISOU 4602  N   LEU D  76     6797   4597   5587   -914   -866   1459       N  
ATOM   4603  CA  LEU D  76      47.467  32.453  15.825  1.00 44.20           C  
ANISOU 4603  CA  LEU D  76     6961   4797   5036   -886   -785   1472       C  
ATOM   4604  C   LEU D  76      46.598  32.527  17.079  1.00 46.65           C  
ANISOU 4604  C   LEU D  76     7355   5292   5079   -982   -417   1691       C  
ATOM   4605  O   LEU D  76      45.466  32.981  17.021  1.00 58.53           O  
ANISOU 4605  O   LEU D  76     8689   6874   6677  -1011   -114   1674       O  
ATOM   4606  CB  LEU D  76      47.893  33.854  15.377  1.00 49.49           C  
ANISOU 4606  CB  LEU D  76     7580   5614   5608   -765   -829   1135       C  
ATOM   4607  CG  LEU D  76      48.877  33.860  14.213  1.00 52.53           C  
ANISOU 4607  CG  LEU D  76     7834   5933   6193   -599  -1156   1030       C  
ATOM   4608  CD1 LEU D  76      49.345  35.283  13.911  1.00 58.68           C  
ANISOU 4608  CD1 LEU D  76     8513   6865   6920   -519  -1223    822       C  
ATOM   4609  CD2 LEU D  76      50.068  32.945  14.487  1.00 50.62           C  
ANISOU 4609  CD2 LEU D  76     7760   5644   5829   -530  -1432   1258       C  
ATOM   4610  N   GLU D  77      47.121  32.076  18.213  1.00 46.13           N  
ANISOU 4610  N   GLU D  77     7533   5339   4655   -989   -424   1938       N  
ATOM   4611  CA  GLU D  77      46.330  32.057  19.440  1.00 50.52           C  
ANISOU 4611  CA  GLU D  77     8164   6148   4885   -991    -48   2219       C  
ATOM   4612  C   GLU D  77      46.767  33.155  20.407  1.00 55.90           C  
ANISOU 4612  C   GLU D  77     9175   7128   4937   -802     13   1998       C  
ATOM   4613  O   GLU D  77      45.989  33.601  21.263  1.00 56.19           O  
ANISOU 4613  O   GLU D  77     9298   7444   4608   -662    373   2071       O  
ATOM   4614  CB  GLU D  77      46.409  30.674  20.099  1.00 57.86           C  
ANISOU 4614  CB  GLU D  77     9114   7012   5858  -1106    -74   2731       C  
ATOM   4615  CG  GLU D  77      45.380  30.435  21.196  1.00 78.64           C  
ANISOU 4615  CG  GLU D  77    11676   9926   8279  -1099    363   3194       C  
ATOM   4616  CD  GLU D  77      45.876  30.818  22.580  1.00 88.10           C  
ANISOU 4616  CD  GLU D  77    13226  11516   8732   -890    497   3256       C  
ATOM   4617  OE1 GLU D  77      45.032  30.952  23.492  1.00 91.42           O  
ANISOU 4617  OE1 GLU D  77    13625  12293   8818   -741    920   3559       O  
ATOM   4618  OE2 GLU D  77      47.103  30.974  22.761  1.00 89.29           O  
ANISOU 4618  OE2 GLU D  77    13669  11639   8617   -844    167   3034       O  
ATOM   4619  N   SER D  78      48.018  33.582  20.262  1.00 50.77           N  
ANISOU 4619  N   SER D  78     7208   4854   7227    450     88   1939       N  
ATOM   4620  CA  SER D  78      48.541  34.713  21.019  1.00 42.59           C  
ANISOU 4620  CA  SER D  78     6100   4234   5848    448   -321   2013       C  
ATOM   4621  C   SER D  78      49.696  35.350  20.253  1.00 50.50           C  
ANISOU 4621  C   SER D  78     6912   5116   7158    606   -388   1927       C  
ATOM   4622  O   SER D  78      50.343  34.692  19.438  1.00 46.63           O  
ANISOU 4622  O   SER D  78     6289   4212   7214    766   -148   1999       O  
ATOM   4623  CB  SER D  78      49.014  34.259  22.411  1.00 46.14           C  
ANISOU 4623  CB  SER D  78     6483   4871   6178    396   -622   2620       C  
ATOM   4624  OG  SER D  78      50.218  33.514  22.335  1.00 61.32           O  
ANISOU 4624  OG  SER D  78     8127   6488   8681    618   -670   3130       O  
ATOM   4625  N   ILE D  79      49.947  36.632  20.504  1.00 41.61           N  
ANISOU 4625  N   ILE D  79     5797   4317   5696    533   -646   1743       N  
ATOM   4626  CA  ILE D  79      51.090  37.308  19.894  1.00 43.62           C  
ANISOU 4626  CA  ILE D  79     5866   4496   6212    619   -722   1684       C  
ATOM   4627  C   ILE D  79      51.806  38.187  20.916  1.00 50.17           C  
ANISOU 4627  C   ILE D  79     6609   5721   6731    449  -1146   1839       C  
ATOM   4628  O   ILE D  79      51.191  38.630  21.891  1.00 49.06           O  
ANISOU 4628  O   ILE D  79     6675   5918   6048    239  -1309   1779       O  
ATOM   4629  CB  ILE D  79      50.646  38.216  18.713  1.00 41.46           C  
ANISOU 4629  CB  ILE D  79     5758   4142   5852    632   -509   1146       C  
ATOM   4630  CG1 ILE D  79      49.562  39.181  19.179  1.00 42.62           C  
ANISOU 4630  CG1 ILE D  79     6155   4594   5445    514   -578    850       C  
ATOM   4631  CG2 ILE D  79      50.153  37.362  17.551  1.00 45.26           C  
ANISOU 4631  CG2 ILE D  79     6301   4285   6611    703   -120    978       C  
ATOM   4632  CD1 ILE D  79      49.178  40.263  18.162  1.00 40.57           C  
ANISOU 4632  CD1 ILE D  79     6030   4287   5096    570   -438    445       C  
ATOM   4633  N   GLU D  80      53.101  38.423  20.710  1.00 45.43           N  
ANISOU 4633  N   GLU D  80     5702   5100   6458    488  -1296   2017       N  
ATOM   4634  CA  GLU D  80      53.769  39.522  21.414  1.00 53.45           C  
ANISOU 4634  CA  GLU D  80     6668   6507   7134    217  -1666   1995       C  
ATOM   4635  C   GLU D  80      53.524  40.828  20.669  1.00 48.06           C  
ANISOU 4635  C   GLU D  80     6237   5746   6279    142  -1490   1413       C  
ATOM   4636  O   GLU D  80      53.879  40.966  19.495  1.00 42.25           O  
ANISOU 4636  O   GLU D  80     5426   4709   5917    297  -1245   1246       O  
ATOM   4637  CB  GLU D  80      55.274  39.310  21.569  1.00 61.69           C  
ANISOU 4637  CB  GLU D  80     7203   7648   8589    229  -1944   2458       C  
ATOM   4638  CG  GLU D  80      55.886  40.289  22.587  1.00 76.35           C  
ANISOU 4638  CG  GLU D  80     9008  10043   9958   -199  -2421   2497       C  
ATOM   4639  CD  GLU D  80      57.208  40.916  22.143  1.00 81.59           C  
ANISOU 4639  CD  GLU D  80     9281  10765  10953   -296  -2547   2513       C  
ATOM   4640  OE1 GLU D  80      57.198  42.084  21.679  1.00 77.84           O  
ANISOU 4640  OE1 GLU D  80     9044  10233  10297   -487  -2414   1993       O  
ATOM   4641  OE2 GLU D  80      58.257  40.251  22.283  1.00 73.76           O  
ANISOU 4641  OE2 GLU D  80     7723   9873  10430   -180  -2765   3079       O  
ATOM   4642  N   MET D  81      52.925  41.786  21.362  1.00 43.66           N  
ANISOU 4642  N   MET D  81     6000   5432   5158   -101  -1571   1121       N  
ATOM   4643  CA  MET D  81      52.507  43.046  20.752  1.00 44.97           C  
ANISOU 4643  CA  MET D  81     6459   5456   5171   -124  -1350    612       C  
ATOM   4644  C   MET D  81      53.725  43.793  20.219  1.00 43.61           C  
ANISOU 4644  C   MET D  81     6129   5202   5238   -234  -1409    551       C  
ATOM   4645  O   MET D  81      54.796  43.765  20.827  1.00 48.19           O  
ANISOU 4645  O   MET D  81     6432   6027   5851   -463  -1726    806       O  
ATOM   4646  CB  MET D  81      51.781  43.884  21.796  1.00 49.05           C  
ANISOU 4646  CB  MET D  81     7332   6208   5097   -379  -1372    343       C  
ATOM   4647  CG  MET D  81      50.698  44.784  21.257  1.00 53.73           C  
ANISOU 4647  CG  MET D  81     8250   6584   5581   -226  -1014    -95       C  
ATOM   4648  SD  MET D  81      50.049  45.775  22.623  1.00 73.41           S  
ANISOU 4648  SD  MET D  81    11152   9292   7449   -550   -936   -434       S  
ATOM   4649  CE  MET D  81      48.992  46.893  21.703  1.00 72.59           C  
ANISOU 4649  CE  MET D  81    11305   8799   7478   -217   -467   -840       C  
ATOM   4650  N   ALA D  82      53.579  44.440  19.073  1.00 41.87           N  
ANISOU 4650  N   ALA D  82     6052   4676   5182    -97  -1121    258       N  
ATOM   4651  CA  ALA D  82      54.710  45.133  18.470  1.00 39.56           C  
ANISOU 4651  CA  ALA D  82     5627   4269   5134   -220  -1106    195       C  
ATOM   4652  C   ALA D  82      55.118  46.303  19.356  1.00 39.36           C  
ANISOU 4652  C   ALA D  82     5768   4441   4747   -640  -1289      0       C  
ATOM   4653  O   ALA D  82      54.265  47.006  19.895  1.00 41.83           O  
ANISOU 4653  O   ALA D  82     6478   4763   4653   -736  -1200   -284       O  
ATOM   4654  CB  ALA D  82      54.350  45.627  17.054  1.00 44.15           C  
ANISOU 4654  CB  ALA D  82     6413   4490   5874    -18   -740    -54       C  
ATOM   4655  N   PHE D  83      56.426  46.501  19.493  1.00 46.71           N  
ANISOU 4655  N   PHE D  83     6378   5523   5845   -914  -1503    137       N  
ATOM   4656  CA  PHE D  83      56.994  47.602  20.266  1.00 55.09           C  
ANISOU 4656  CA  PHE D  83     7570   6795   6565  -1444  -1684    -77       C  
ATOM   4657  C   PHE D  83      56.501  47.633  21.709  1.00 59.85           C  
ANISOU 4657  C   PHE D  83     8390   7779   6570  -1757  -1934   -110       C  
ATOM   4658  O   PHE D  83      56.311  48.696  22.285  1.00 57.67           O  
ANISOU 4658  O   PHE D  83     8523   7524   5865  -2147  -1864   -508       O  
ATOM   4659  CB  PHE D  83      56.740  48.934  19.555  1.00 52.66           C  
ANISOU 4659  CB  PHE D  83     7709   6078   6221  -1502  -1305   -540       C  
ATOM   4660  CG  PHE D  83      57.205  48.938  18.125  1.00 53.86           C  
ANISOU 4660  CG  PHE D  83     7709   5891   6864  -1255  -1042   -497       C  
ATOM   4661  CD1 PHE D  83      58.558  48.866  17.826  1.00 62.70           C  
ANISOU 4661  CD1 PHE D  83     8380   7111   8334  -1457  -1150   -327       C  
ATOM   4662  CD2 PHE D  83      56.292  48.993  17.080  1.00 39.79           C  
ANISOU 4662  CD2 PHE D  83     6202   3743   5175   -853   -689   -603       C  
ATOM   4663  CE1 PHE D  83      59.000  48.858  16.509  1.00 62.99           C  
ANISOU 4663  CE1 PHE D  83     8302   6840   8793  -1269   -837   -315       C  
ATOM   4664  CE2 PHE D  83      56.729  48.967  15.753  1.00 44.62           C  
ANISOU 4664  CE2 PHE D  83     6720   4092   6143   -697   -440   -563       C  
ATOM   4665  CZ  PHE D  83      58.082  48.913  15.471  1.00 52.56           C  
ANISOU 4665  CZ  PHE D  83     7338   5151   7481   -910   -477   -446       C  
ATOM   4666  N   SER D  84      56.296  46.454  22.285  1.00 59.59           N  
ANISOU 4666  N   SER D  84     8120   8016   6506  -1610  -2175    302       N  
ATOM   4667  CA  SER D  84      55.753  46.342  23.632  1.00 59.89           C  
ANISOU 4667  CA  SER D  84     8385   8441   5929  -1904  -2385    322       C  
ATOM   4668  C   SER D  84      56.109  44.973  24.193  1.00 61.93           C  
ANISOU 4668  C   SER D  84     8197   9042   6291  -1803  -2773    986       C  
ATOM   4669  O   SER D  84      56.427  44.048  23.438  1.00 60.77           O  
ANISOU 4669  O   SER D  84     7659   8682   6749  -1376  -2725   1345       O  
ATOM   4670  CB  SER D  84      54.228  46.510  23.606  1.00 49.32           C  
ANISOU 4670  CB  SER D  84     7536   6845   4358  -1658  -1975    -25       C  
ATOM   4671  OG  SER D  84      53.655  46.250  24.876  1.00 65.85           O  
ANISOU 4671  OG  SER D  84     9836   9305   5878  -1920  -2105     13       O  
ATOM   4672  N   ASP D  85      56.059  44.844  25.513  1.00 64.53           N  
ANISOU 4672  N   ASP D  85     8614   9875   6028  -2208  -3118   1158       N  
ATOM   4673  CA  ASP D  85      56.281  43.553  26.148  1.00 69.39           C  
ANISOU 4673  CA  ASP D  85     8865  10806   6692  -2102  -3480   1867       C  
ATOM   4674  C   ASP D  85      54.953  42.863  26.431  1.00 67.71           C  
ANISOU 4674  C   ASP D  85     8989  10464   6273  -1861  -3227   1870       C  
ATOM   4675  O   ASP D  85      54.921  41.744  26.930  1.00 70.81           O  
ANISOU 4675  O   ASP D  85     9176  10936   6793  -1686  -3299   2359       O  
ATOM   4676  CB  ASP D  85      57.100  43.704  27.434  1.00 79.48           C  
ANISOU 4676  CB  ASP D  85     9987  12602   7612  -2565  -3778   2058       C  
ATOM   4677  CG  ASP D  85      58.582  43.870  27.159  1.00 95.42           C  
ANISOU 4677  CG  ASP D  85    11437  14800  10018  -2685  -4079   2334       C  
ATOM   4678  OD1 ASP D  85      59.067  43.274  26.174  1.00 94.86           O  
ANISOU 4678  OD1 ASP D  85    10909  14474  10660  -2253  -4073   2655       O  
ATOM   4679  OD2 ASP D  85      59.263  44.594  27.919  1.00107.33           O  
ANISOU 4679  OD2 ASP D  85    12942  16689  11149  -3213  -4273   2220       O  
ATOM   4680  N   LEU D  86      53.861  43.541  26.095  1.00 61.89           N  
ANISOU 4680  N   LEU D  86     8729   9423   5361  -1783  -2761   1257       N  
ATOM   4681  CA  LEU D  86      52.521  43.005  26.298  1.00 60.35           C  
ANISOU 4681  CA  LEU D  86     8815   9122   4994  -1580  -2462   1187       C  
ATOM   4682  C   LEU D  86      52.208  41.840  25.360  1.00 56.19           C  
ANISOU 4682  C   LEU D  86     8033   8217   5101  -1040  -2274   1477       C  
ATOM   4683  O   LEU D  86      52.688  41.789  24.229  1.00 56.40           O  
ANISOU 4683  O   LEU D  86     7827   7906   5695   -751  -2158   1459       O  
ATOM   4684  CB  LEU D  86      51.470  44.102  26.092  1.00 60.36           C  
ANISOU 4684  CB  LEU D  86     9286   8890   4756  -1581  -1990    490       C  
ATOM   4685  CG  LEU D  86      51.288  45.139  27.204  1.00 70.81           C  
ANISOU 4685  CG  LEU D  86    11033  10484   5386  -2109  -1933     76       C  
ATOM   4686  CD1 LEU D  86      50.159  46.098  26.842  1.00 73.43           C  
ANISOU 4686  CD1 LEU D  86    11771  10449   5680  -1939  -1357   -540       C  
ATOM   4687  CD2 LEU D  86      51.017  44.462  28.532  1.00 76.58           C  
ANISOU 4687  CD2 LEU D  86    11747  11585   5767  -2309  -2018    344       C  
ATOM   4688  N   ILE D  87      51.382  40.920  25.847  1.00 53.07           N  
ANISOU 4688  N   ILE D  87     7725   7872   4566   -969  -2198   1705       N  
ATOM   4689  CA  ILE D  87      50.871  39.808  25.055  1.00 47.95           C  
ANISOU 4689  CA  ILE D  87     6944   6846   4427   -563  -1939   1883       C  
ATOM   4690  C   ILE D  87      49.399  40.032  24.774  1.00 45.07           C  
ANISOU 4690  C   ILE D  87     6882   6354   3889   -476  -1521   1424       C  
ATOM   4691  O   ILE D  87      48.670  40.547  25.618  1.00 56.67           O  
ANISOU 4691  O   ILE D  87     8636   8078   4820   -711  -1443   1194       O  
ATOM   4692  CB  ILE D  87      51.005  38.463  25.815  1.00 56.60           C  
ANISOU 4692  CB  ILE D  87     7891   8053   5562   -560  -2133   2559       C  
ATOM   4693  CG1 ILE D  87      52.442  38.239  26.285  1.00 62.13           C  
ANISOU 4693  CG1 ILE D  87     8198   8969   6438   -628  -2567   3083       C  
ATOM   4694  CG2 ILE D  87      50.503  37.303  24.966  1.00 55.18           C  
ANISOU 4694  CG2 ILE D  87     7628   7396   5941   -203  -1786   2681       C  
ATOM   4695  CD1 ILE D  87      53.475  38.336  25.196  1.00 68.82           C  
ANISOU 4695  CD1 ILE D  87     8667   9539   7943   -370  -2596   3161       C  
ATOM   4696  N   ILE D  88      48.970  39.674  23.568  1.00 43.72           N  
ANISOU 4696  N   ILE D  88     6628   5816   4167   -165  -1234   1281       N  
ATOM   4697  CA  ILE D  88      47.564  39.640  23.239  1.00 45.41           C  
ANISOU 4697  CA  ILE D  88     6997   5970   4288    -77   -893    973       C  
ATOM   4698  C   ILE D  88      47.223  38.184  22.975  1.00 54.28           C  
ANISOU 4698  C   ILE D  88     8007   6906   5713     15   -768   1269       C  
ATOM   4699  O   ILE D  88      47.926  37.500  22.233  1.00 45.71           O  
ANISOU 4699  O   ILE D  88     6741   5517   5110    171   -753   1463       O  
ATOM   4700  CB  ILE D  88      47.267  40.464  22.001  1.00 47.89           C  
ANISOU 4700  CB  ILE D  88     7321   6074   4802    126   -687    568       C  
ATOM   4701  CG1 ILE D  88      47.574  41.945  22.269  1.00 45.44           C  
ANISOU 4701  CG1 ILE D  88     7181   5843   4240     33   -730    267       C  
ATOM   4702  CG2 ILE D  88      45.819  40.271  21.555  1.00 39.16           C  
ANISOU 4702  CG2 ILE D  88     6245   4971   3665    229   -395    357       C  
ATOM   4703  CD1 ILE D  88      47.523  42.793  20.993  1.00 46.23           C  
ANISOU 4703  CD1 ILE D  88     7290   5685   4589    253   -563    -13       C  
ATOM   4704  N   GLU D  89      46.165  37.702  23.612  1.00 53.61           N  
ANISOU 4704  N   GLU D  89     8042   6969   5358   -109   -622   1290       N  
ATOM   4705  CA  GLU D  89      45.772  36.312  23.455  1.00 49.35           C  
ANISOU 4705  CA  GLU D  89     7452   6222   5079   -100   -456   1553       C  
ATOM   4706  C   GLU D  89      44.283  36.221  23.143  1.00 51.08           C  
ANISOU 4706  C   GLU D  89     7724   6511   5174   -160   -136   1222       C  
ATOM   4707  O   GLU D  89      43.473  36.986  23.687  1.00 51.68           O  
ANISOU 4707  O   GLU D  89     7887   6891   4858   -243    -57    973       O  
ATOM   4708  CB  GLU D  89      46.124  35.526  24.733  1.00 57.38           C  
ANISOU 4708  CB  GLU D  89     8518   7373   5911   -265   -643   2107       C  
ATOM   4709  CG  GLU D  89      45.878  34.031  24.632  1.00 58.17           C  
ANISOU 4709  CG  GLU D  89     8601   7143   6358   -246   -440   2466       C  
ATOM   4710  CD  GLU D  89      46.528  33.247  25.751  1.00 75.47           C  
ANISOU 4710  CD  GLU D  89    10795   9390   8492   -319   -681   3175       C  
ATOM   4711  OE1 GLU D  89      46.422  32.002  25.734  1.00 77.97           O  
ANISOU 4711  OE1 GLU D  89    11122   9350   9151   -278   -488   3549       O  
ATOM   4712  OE2 GLU D  89      47.136  33.869  26.651  1.00 77.54           O  
ANISOU 4712  OE2 GLU D  89    11059  10052   8352   -448  -1059   3379       O  
ATOM   4713  N   TRP D  90      43.928  35.302  22.252  1.00 49.02           N  
ANISOU 4713  N   TRP D  90     7391   5973   5261   -140     80   1199       N  
ATOM   4714  CA  TRP D  90      42.532  35.062  21.917  1.00 50.12           C  
ANISOU 4714  CA  TRP D  90     7504   6235   5304   -272    345    933       C  
ATOM   4715  C   TRP D  90      42.051  33.806  22.625  1.00 53.00           C  
ANISOU 4715  C   TRP D  90     7950   6533   5653   -506    512   1219       C  
ATOM   4716  O   TRP D  90      42.619  32.728  22.446  1.00 61.22           O  
ANISOU 4716  O   TRP D  90     9033   7181   7046   -518    584   1505       O  
ATOM   4717  CB  TRP D  90      42.357  34.885  20.409  1.00 44.18           C  
ANISOU 4717  CB  TRP D  90     6650   5285   4850   -232    479    664       C  
ATOM   4718  CG  TRP D  90      42.560  36.135  19.617  1.00 47.69           C  
ANISOU 4718  CG  TRP D  90     7029   5827   5265    -31    361    394       C  
ATOM   4719  CD1 TRP D  90      41.593  36.953  19.104  1.00 50.06           C  
ANISOU 4719  CD1 TRP D  90     7215   6405   5401     19    396    119       C  
ATOM   4720  CD2 TRP D  90      43.818  36.714  19.246  1.00 42.70           C  
ANISOU 4720  CD2 TRP D  90     6419   5003   4801    153    202    428       C  
ATOM   4721  NE1 TRP D  90      42.177  38.004  18.433  1.00 42.57           N  
ANISOU 4721  NE1 TRP D  90     6274   5403   4499    232    275      1       N  
ATOM   4722  CE2 TRP D  90      43.539  37.884  18.519  1.00 42.52           C  
ANISOU 4722  CE2 TRP D  90     6362   5115   4677    284    168    155       C  
ATOM   4723  CE3 TRP D  90      45.153  36.362  19.477  1.00 47.25           C  
ANISOU 4723  CE3 TRP D  90     6998   5321   5633    223     88    707       C  
ATOM   4724  CZ2 TRP D  90      44.546  38.697  18.007  1.00 49.22           C  
ANISOU 4724  CZ2 TRP D  90     7241   5819   5640    433     56    110       C  
ATOM   4725  CZ3 TRP D  90      46.147  37.169  18.969  1.00 51.32           C  
ANISOU 4725  CZ3 TRP D  90     7474   5747   6277    368    -35    644       C  
ATOM   4726  CH2 TRP D  90      45.840  38.319  18.235  1.00 43.81           C  
ANISOU 4726  CH2 TRP D  90     6552   4905   5190    446    -35    327       C  
ATOM   4727  N   PHE D  91      41.011  33.941  23.437  1.00 52.04           N  
ANISOU 4727  N   PHE D  91     7860   6755   5159   -688    632   1153       N  
ATOM   4728  CA  PHE D  91      40.479  32.784  24.151  1.00 56.96           C  
ANISOU 4728  CA  PHE D  91     8586   7331   5724   -962    827   1432       C  
ATOM   4729  C   PHE D  91      39.000  32.571  23.866  1.00 57.99           C  
ANISOU 4729  C   PHE D  91     8583   7674   5776  -1192   1136   1124       C  
ATOM   4730  O   PHE D  91      38.187  33.471  24.061  1.00 59.02           O  
ANISOU 4730  O   PHE D  91     8580   8204   5642  -1170   1196    844       O  
ATOM   4731  CB  PHE D  91      40.710  32.915  25.652  1.00 58.43           C  
ANISOU 4731  CB  PHE D  91     8959   7768   5472  -1079    700   1765       C  
ATOM   4732  CG  PHE D  91      40.369  31.679  26.416  1.00 64.53           C  
ANISOU 4732  CG  PHE D  91     9887   8440   6192  -1350    873   2179       C  
ATOM   4733  CD1 PHE D  91      41.105  30.521  26.240  1.00 72.38           C  
ANISOU 4733  CD1 PHE D  91    10944   8944   7615  -1301    867   2640       C  
ATOM   4734  CD2 PHE D  91      39.313  31.671  27.310  1.00 69.89           C  
ANISOU 4734  CD2 PHE D  91    10655   9472   6430  -1644   1102   2126       C  
ATOM   4735  CE1 PHE D  91      40.797  29.375  26.941  1.00 71.42           C  
ANISOU 4735  CE1 PHE D  91    11000   8653   7482  -1539   1060   3079       C  
ATOM   4736  CE2 PHE D  91      38.996  30.524  28.026  1.00 71.85           C  
ANISOU 4736  CE2 PHE D  91    11081   9611   6609  -1932   1288   2543       C  
ATOM   4737  CZ  PHE D  91      39.739  29.377  27.840  1.00 74.61           C  
ANISOU 4737  CZ  PHE D  91    11522   9439   7387  -1877   1253   3039       C  
ATOM   4738  N   LYS D  92      38.657  31.373  23.403  1.00 69.53           N  
ANISOU 4738  N   LYS D  92    10061   8855   7502  -1426   1363   1179       N  
ATOM   4739  CA  LYS D  92      37.273  31.046  23.078  1.00 63.47           C  
ANISOU 4739  CA  LYS D  92     9116   8323   6678  -1741   1636    901       C  
ATOM   4740  C   LYS D  92      36.546  30.410  24.257  1.00 66.91           C  
ANISOU 4740  C   LYS D  92     9656   8898   6869  -2061   1878   1121       C  
ATOM   4741  O   LYS D  92      36.998  29.411  24.819  1.00 68.80           O  
ANISOU 4741  O   LYS D  92    10161   8781   7198  -2196   1964   1526       O  
ATOM   4742  CB  LYS D  92      37.217  30.128  21.855  1.00 65.60           C  
ANISOU 4742  CB  LYS D  92     9376   8241   7308  -1953   1794    738       C  
ATOM   4743  CG  LYS D  92      35.810  29.814  21.375  1.00 69.95           C  
ANISOU 4743  CG  LYS D  92     9682   9118   7777  -2367   2011    423       C  
ATOM   4744  CD  LYS D  92      35.845  29.194  19.988  1.00 78.70           C  
ANISOU 4744  CD  LYS D  92    10799   9971   9132  -2617   2102    147       C  
ATOM   4745  CE  LYS D  92      34.457  28.786  19.529  1.00 89.41           C  
ANISOU 4745  CE  LYS D  92    11887  11718  10367  -3150   2273   -144       C  
ATOM   4746  NZ  LYS D  92      34.482  28.116  18.199  1.00 93.87           N  
ANISOU 4746  NZ  LYS D  92    12530  12064  11073  -3536   2382   -461       N  
ATOM   4747  N   VAL D  93      35.420  31.005  24.634  1.00 71.64           N  
ANISOU 4747  N   VAL D  93    12816   6869   7535  -3088   1089   -105       N  
ATOM   4748  CA  VAL D  93      34.614  30.496  25.737  1.00 74.21           C  
ANISOU 4748  CA  VAL D  93    13085   7180   7930  -3478   1387    -55       C  
ATOM   4749  C   VAL D  93      33.752  29.338  25.232  1.00 76.78           C  
ANISOU 4749  C   VAL D  93    13401   7185   8585  -3786   1506   -296       C  
ATOM   4750  O   VAL D  93      32.835  29.543  24.440  1.00 68.61           O  
ANISOU 4750  O   VAL D  93    12102   6246   7722  -3890   1355   -714       O  
ATOM   4751  CB  VAL D  93      33.721  31.613  26.322  1.00 63.47           C  
ANISOU 4751  CB  VAL D  93    11385   6222   6506  -3583   1415   -247       C  
ATOM   4752  CG1 VAL D  93      33.007  31.141  27.564  1.00 67.56           C  
ANISOU 4752  CG1 VAL D  93    11881   6734   7053  -3926   1769   -119       C  
ATOM   4753  CG2 VAL D  93      34.556  32.869  26.629  1.00 59.87           C  
ANISOU 4753  CG2 VAL D  93    10936   6052   5760  -3284   1263   -113       C  
ATOM   4754  N   GLU D  94      34.062  28.122  25.678  1.00 79.24           N  
ANISOU 4754  N   GLU D  94    13990   7118   8998  -3932   1773    -22       N  
ATOM   4755  CA  GLU D  94      33.365  26.922  25.218  1.00 80.44           C  
ANISOU 4755  CA  GLU D  94    14183   6873   9506  -4247   1921   -242       C  
ATOM   4756  C   GLU D  94      32.229  26.497  26.153  1.00 90.80           C  
ANISOU 4756  C   GLU D  94    15284   8166  11050  -4678   2243   -254       C  
ATOM   4757  O   GLU D  94      31.773  27.272  26.995  1.00 89.44           O  
ANISOU 4757  O   GLU D  94    14887   8346  10751  -4724   2317   -192       O  
ATOM   4758  CB  GLU D  94      34.353  25.761  25.054  1.00 76.90           C  
ANISOU 4758  CB  GLU D  94    14119   5991   9111  -4080   2069     61       C  
ATOM   4759  CG  GLU D  94      35.420  25.977  23.985  1.00 83.77           C  
ANISOU 4759  CG  GLU D  94    15252   6749   9829  -3695   1828     76       C  
ATOM   4760  CD  GLU D  94      34.900  25.773  22.569  1.00 83.31           C  
ANISOU 4760  CD  GLU D  94    15203   6530   9920  -3753   1611   -464       C  
ATOM   4761  OE1 GLU D  94      35.497  26.340  21.626  1.00 82.14           O  
ANISOU 4761  OE1 GLU D  94    15124   6488   9597  -3380   1338   -551       O  
ATOM   4762  OE2 GLU D  94      33.904  25.040  22.394  1.00 92.13           O  
ANISOU 4762  OE2 GLU D  94    16192   7490  11322  -4109   1689   -789       O  
ATOM   4763  N   LYS D  95      31.786  25.254  25.998  1.00 98.67           N  
ANISOU 4763  N   LYS D  95    16277   8823  12390  -4855   2408   -328       N  
ATOM   4764  CA  LYS D  95      30.675  24.716  26.780  1.00 98.83           C  
ANISOU 4764  CA  LYS D  95    16020   8821  12711  -5171   2693   -328       C  
ATOM   4765  C   LYS D  95      31.038  24.537  28.249  1.00 97.19           C  
ANISOU 4765  C   LYS D  95    15885   8700  12340  -5049   3019    198       C  
ATOM   4766  O   LYS D  95      32.147  24.120  28.581  1.00 98.65           O  
ANISOU 4766  O   LYS D  95    16333   8802  12347  -4746   3069    582       O  
ATOM   4767  CB  LYS D  95      30.214  23.376  26.205  1.00108.79           C  
ANISOU 4767  CB  LYS D  95    17268   9664  14402  -5359   2767   -523       C  
ATOM   4768  CG  LYS D  95      31.261  22.273  26.295  1.00112.27           C  
ANISOU 4768  CG  LYS D  95    18070   9736  14852  -5118   2950   -180       C  
ATOM   4769  CD  LYS D  95      30.623  20.894  26.336  1.00116.42           C  
ANISOU 4769  CD  LYS D  95    18530   9862  15843  -5363   3197   -235       C  
ATOM   4770  CE  LYS D  95      31.652  19.833  26.694  1.00118.14           C  
ANISOU 4770  CE  LYS D  95    19054   9767  16069  -5094   3457    203       C  
ATOM   4771  NZ  LYS D  95      32.328  20.135  27.991  1.00116.83           N  
ANISOU 4771  NZ  LYS D  95    18913   9867  15610  -4824   3625    775       N  
ATOM   4772  N   GLY D  96      30.096  24.862  29.127  1.00 90.21           N  
ANISOU 4772  N   GLY D  96    14735   8027  11516  -5247   3224    222       N  
ATOM   4773  CA  GLY D  96      30.268  24.629  30.548  1.00 99.18           C  
ANISOU 4773  CA  GLY D  96    15918   9267  12499  -5132   3534    684       C  
ATOM   4774  C   GLY D  96      31.210  25.591  31.243  1.00 92.61           C  
ANISOU 4774  C   GLY D  96    15257   8806  11126  -4831   3430    957       C  
ATOM   4775  O   GLY D  96      31.557  25.394  32.408  1.00 93.78           O  
ANISOU 4775  O   GLY D  96    15470   9088  11075  -4670   3606   1350       O  
ATOM   4776  N   ALA D  97      31.636  26.631  30.532  1.00 83.55           N  
ANISOU 4776  N   ALA D  97    14163   7837   9746  -4747   3118    747       N  
ATOM   4777  CA  ALA D  97      32.464  27.657  31.140  1.00 83.86           C  
ANISOU 4777  CA  ALA D  97    14321   8241   9301  -4492   2978    943       C  
ATOM   4778  C   ALA D  97      31.665  28.379  32.216  1.00 90.02           C  
ANISOU 4778  C   ALA D  97    14944   9345   9914  -4615   3190    938       C  
ATOM   4779  O   ALA D  97      30.594  28.916  31.940  1.00 92.91           O  
ANISOU 4779  O   ALA D  97    15064   9790  10446  -4862   3266    621       O  
ATOM   4780  CB  ALA D  97      32.936  28.636  30.088  1.00 83.64           C  
ANISOU 4780  CB  ALA D  97    14344   8300   9135  -4405   2634    704       C  
ATOM   4781  N   LYS D  98      32.189  28.381  33.440  1.00 93.10           N  
ANISOU 4781  N   LYS D  98    15446   9939   9988  -4416   3278   1288       N  
ATOM   4782  CA  LYS D  98      31.556  29.060  34.569  1.00 92.42           C  
ANISOU 4782  CA  LYS D  98    15286  10164   9667  -4467   3489   1305       C  
ATOM   4783  C   LYS D  98      31.199  30.516  34.268  1.00 87.66           C  
ANISOU 4783  C   LYS D  98    14592   9834   8881  -4534   3379    957       C  
ATOM   4784  O   LYS D  98      30.224  31.050  34.797  1.00 88.13           O  
ANISOU 4784  O   LYS D  98    14493  10057   8935  -4660   3627    828       O  
ATOM   4785  CB  LYS D  98      32.481  29.029  35.789  1.00100.40           C  
ANISOU 4785  CB  LYS D  98    16469  11411  10267  -4190   3458   1696       C  
ATOM   4786  CG  LYS D  98      32.742  27.650  36.367  1.00105.15           C  
ANISOU 4786  CG  LYS D  98    17099  11830  11023  -4094   3651   2121       C  
ATOM   4787  CD  LYS D  98      33.749  27.726  37.508  1.00104.38           C  
ANISOU 4787  CD  LYS D  98    17111  12051  10497  -3805   3554   2513       C  
ATOM   4788  CE  LYS D  98      33.911  26.380  38.202  1.00106.33           C  
ANISOU 4788  CE  LYS D  98    17332  12181  10888  -3704   3798   2993       C  
ATOM   4789  NZ  LYS D  98      32.644  25.923  38.836  1.00109.79           N  
ANISOU 4789  NZ  LYS D  98    17675  12531  11508  -3904   4237   3029       N  
ATOM   4790  N   SER D  99      31.992  31.155  33.416  1.00 80.81           N  
ANISOU 4790  N   SER D  99    13806   9008   7889  -4416   3036    833       N  
ATOM   4791  CA  SER D  99      31.840  32.581  33.157  1.00 77.01           C  
ANISOU 4791  CA  SER D  99    13220   8804   7236  -4380   2904    539       C  
ATOM   4792  C   SER D  99      30.703  32.895  32.181  1.00 80.85           C  
ANISOU 4792  C   SER D  99    13301   9272   8146  -4461   2867    128       C  
ATOM   4793  O   SER D  99      30.346  34.059  31.987  1.00 73.87           O  
ANISOU 4793  O   SER D  99    12215   8629   7225  -4356   2790   -130       O  
ATOM   4794  CB  SER D  99      33.158  33.171  32.652  1.00 77.34           C  
ANISOU 4794  CB  SER D  99    13409   8920   7057  -4097   2492    576       C  
ATOM   4795  OG  SER D  99      33.568  32.548  31.444  1.00 80.15           O  
ANISOU 4795  OG  SER D  99    13754   9003   7696  -4000   2267    551       O  
ATOM   4796  N   ILE D 100      30.140  31.859  31.565  1.00 84.08           N  
ANISOU 4796  N   ILE D 100    13583   9398   8966  -4650   2922     71       N  
ATOM   4797  CA  ILE D 100      29.010  32.041  30.656  1.00 81.91           C  
ANISOU 4797  CA  ILE D 100    12888   9139   9093  -4770   2854   -303       C  
ATOM   4798  C   ILE D 100      27.816  32.654  31.388  1.00 81.48           C  
ANISOU 4798  C   ILE D 100    12544   9309   9106  -4907   3180   -378       C  
ATOM   4799  O   ILE D 100      27.387  32.151  32.422  1.00 82.45           O  
ANISOU 4799  O   ILE D 100    12732   9370   9226  -5087   3576   -155       O  
ATOM   4800  CB  ILE D 100      28.599  30.711  29.995  1.00 91.79           C  
ANISOU 4800  CB  ILE D 100    14081  10022  10772  -5023   2870   -364       C  
ATOM   4801  CG1 ILE D 100      29.521  30.402  28.813  1.00 84.40           C  
ANISOU 4801  CG1 ILE D 100    13326   8905   9836  -4836   2489   -457       C  
ATOM   4802  CG2 ILE D 100      27.145  30.752  29.531  1.00 82.13           C  
ANISOU 4802  CG2 ILE D 100    12369   8857   9978  -5277   2918   -676       C  
ATOM   4803  CD1 ILE D 100      29.242  29.056  28.188  1.00 93.59           C  
ANISOU 4803  CD1 ILE D 100    14528   9653  11380  -5087   2521   -545       C  
ATOM   4804  N   GLY D 101      27.305  33.760  30.856  1.00 77.34           N  
ANISOU 4804  N   GLY D 101    11705   9040   8640  -4782   3050   -654       N  
ATOM   4805  CA  GLY D 101      26.166  34.432  31.447  1.00 79.73           C  
ANISOU 4805  CA  GLY D 101    11707   9549   9036  -4863   3380   -716       C  
ATOM   4806  C   GLY D 101      26.548  35.561  32.383  1.00 78.50           C  
ANISOU 4806  C   GLY D 101    11759   9626   8440  -4664   3543   -655       C  
ATOM   4807  O   GLY D 101      25.692  36.339  32.791  1.00 80.09           O  
ANISOU 4807  O   GLY D 101    11742  10006   8684  -4656   3824   -734       O  
ATOM   4808  N   ARG D 102      27.834  35.658  32.713  1.00 76.07           N  
ANISOU 4808  N   ARG D 102    11868   9312   7722  -4510   3370   -517       N  
ATOM   4809  CA  ARG D 102      28.321  36.710  33.604  1.00 79.11           C  
ANISOU 4809  CA  ARG D 102    12494   9910   7654  -4359   3464   -501       C  
ATOM   4810  C   ARG D 102      28.841  37.905  32.818  1.00 80.12           C  
ANISOU 4810  C   ARG D 102    12535  10165   7741  -4091   3148   -734       C  
ATOM   4811  O   ARG D 102      29.267  37.767  31.670  1.00 74.70           O  
ANISOU 4811  O   ARG D 102    11741   9398   7242  -3968   2793   -808       O  
ATOM   4812  CB  ARG D 102      29.421  36.187  34.538  1.00 75.83           C  
ANISOU 4812  CB  ARG D 102    12554   9465   6792  -4367   3449   -192       C  
ATOM   4813  CG  ARG D 102      29.095  34.875  35.250  1.00 79.74           C  
ANISOU 4813  CG  ARG D 102    13167   9796   7335  -4585   3761    119       C  
ATOM   4814  CD  ARG D 102      27.637  34.794  35.683  1.00 87.90           C  
ANISOU 4814  CD  ARG D 102    13913  10834   8651  -4734   4194     68       C  
ATOM   4815  NE  ARG D 102      27.284  35.797  36.681  1.00 92.32           N  
ANISOU 4815  NE  ARG D 102    14528  11629   8919  -4593   4415      0       N  
ATOM   4816  CZ  ARG D 102      26.042  36.036  37.089  1.00 93.92           C  
ANISOU 4816  CZ  ARG D 102    14480  11874   9331  -4638   4801    -48       C  
ATOM   4817  NH1 ARG D 102      25.812  36.968  38.004  1.00 90.33           N  
ANISOU 4817  NH1 ARG D 102    14136  11597   8589  -4472   4997   -110       N  
ATOM   4818  NH2 ARG D 102      25.029  35.352  36.576  1.00 90.61           N  
ANISOU 4818  NH2 ARG D 102    13684  11304   9439  -4842   4974    -36       N  
ATOM   4819  N   THR D 103      28.810  39.080  33.439  1.00 71.49           N  
ANISOU 4819  N   THR D 103    11506   9251   6404  -3989   3310   -848       N  
ATOM   4820  CA  THR D 103      29.313  40.293  32.801  1.00 68.21           C  
ANISOU 4820  CA  THR D 103    11016   8926   5976  -3731   3080  -1051       C  
ATOM   4821  C   THR D 103      30.771  40.536  33.184  1.00 66.33           C  
ANISOU 4821  C   THR D 103    11168   8691   5344  -3642   2814   -953       C  
ATOM   4822  O   THR D 103      31.228  40.049  34.218  1.00 68.29           O  
ANISOU 4822  O   THR D 103    11754   8960   5234  -3776   2885   -758       O  
ATOM   4823  CB  THR D 103      28.472  41.520  33.196  1.00 76.74           C  
ANISOU 4823  CB  THR D 103    11936  10152   7071  -3663   3436  -1254       C  
ATOM   4824  OG1 THR D 103      28.562  41.727  34.613  1.00 81.74           O  
ANISOU 4824  OG1 THR D 103    12935  10848   7275  -3774   3742  -1204       O  
ATOM   4825  CG2 THR D 103      27.008  41.312  32.814  1.00 75.56           C  
ANISOU 4825  CG2 THR D 103    11330  10032   7348  -3741   3698  -1299       C  
ATOM   4826  N   LEU D 104      31.504  41.281  32.356  1.00 62.92           N  
ANISOU 4826  N   LEU D 104    10667   8255   4986  -3407   2506  -1057       N  
ATOM   4827  CA  LEU D 104      32.884  41.625  32.684  1.00 61.46           C  
ANISOU 4827  CA  LEU D 104    10784   8079   4490  -3331   2239   -962       C  
ATOM   4828  C   LEU D 104      33.013  42.223  34.093  1.00 64.35           C  
ANISOU 4828  C   LEU D 104    11454   8586   4411  -3467   2446  -1014       C  
ATOM   4829  O   LEU D 104      33.961  41.925  34.817  1.00 73.25           O  
ANISOU 4829  O   LEU D 104    12820   9732   5278  -3492   2224   -821       O  
ATOM   4830  CB  LEU D 104      33.458  42.608  31.665  1.00 58.04           C  
ANISOU 4830  CB  LEU D 104    10175   7619   4259  -3047   1988  -1097       C  
ATOM   4831  CG  LEU D 104      33.848  42.016  30.312  1.00 65.71           C  
ANISOU 4831  CG  LEU D 104    10985   8461   5522  -2856   1678   -991       C  
ATOM   4832  CD1 LEU D 104      34.782  42.984  29.602  1.00 53.50           C  
ANISOU 4832  CD1 LEU D 104     9376   6886   4065  -2561   1434  -1022       C  
ATOM   4833  CD2 LEU D 104      34.477  40.632  30.469  1.00 58.80           C  
ANISOU 4833  CD2 LEU D 104    10349   7460   4531  -2973   1528   -688       C  
ATOM   4834  N   GLY D 105      32.053  43.060  34.467  1.00 66.26           N  
ANISOU 4834  N   GLY D 105    11580   8890   4704  -3467   2793  -1251       N  
ATOM   4835  CA  GLY D 105      32.049  43.693  35.783  1.00 69.63           C  
ANISOU 4835  CA  GLY D 105    12192   9370   4893  -3484   2913  -1321       C  
ATOM   4836  C   GLY D 105      31.816  42.734  36.945  1.00 73.40           C  
ANISOU 4836  C   GLY D 105    12878   9896   5113  -3633   3050  -1101       C  
ATOM   4837  O   GLY D 105      32.408  42.883  38.021  1.00 77.78           O  
ANISOU 4837  O   GLY D 105    13683  10532   5338  -3644   2949  -1050       O  
ATOM   4838  N   GLU D 106      30.943  41.752  36.746  1.00 86.98           N  
ANISOU 4838  N   GLU D 106    14477  11576   6995  -3747   3296   -967       N  
ATOM   4839  CA  GLU D 106      30.737  40.725  37.765  1.00 95.23           C  
ANISOU 4839  CA  GLU D 106    15688  12635   7858  -3853   3448   -704       C  
ATOM   4840  C   GLU D 106      31.997  39.872  37.899  1.00 77.12           C  
ANISOU 4840  C   GLU D 106    13599  10334   5369  -3846   3070   -411       C  
ATOM   4841  O   GLU D 106      32.420  39.537  38.999  1.00 80.17           O  
ANISOU 4841  O   GLU D 106    14196  10820   5444  -3831   3039   -225       O  
ATOM   4842  CB  GLU D 106      29.519  39.855  37.437  1.00 79.35           C  
ANISOU 4842  CB  GLU D 106    13442  10533   6174  -3993   3803   -612       C  
ATOM   4843  CG  GLU D 106      28.188  40.584  37.528  1.00 81.40           C  
ANISOU 4843  CG  GLU D 106    13451  10826   6653  -3976   4224   -810       C  
ATOM   4844  CD  GLU D 106      27.055  39.821  36.869  1.00 88.00           C  
ANISOU 4844  CD  GLU D 106    13915  11575   7945  -4138   4483   -744       C  
ATOM   4845  OE1 GLU D 106      27.333  38.872  36.101  1.00 80.53           O  
ANISOU 4845  OE1 GLU D 106    12903  10520   7175  -4281   4303   -629       O  
ATOM   4846  OE2 GLU D 106      25.882  40.172  37.112  1.00 85.01           O  
ANISOU 4846  OE2 GLU D 106    13291  11222   7787  -4125   4857   -801       O  
ATOM   4847  N   LEU D 107      32.611  39.539  36.770  1.00 73.30           N  
ANISOU 4847  N   LEU D 107    13037   9744   5070  -3824   2790   -351       N  
ATOM   4848  CA  LEU D 107      33.842  38.765  36.790  1.00 78.12           C  
ANISOU 4848  CA  LEU D 107    13794  10318   5569  -3763   2439    -41       C  
ATOM   4849  C   LEU D 107      35.002  39.629  37.264  1.00 80.91           C  
ANISOU 4849  C   LEU D 107    14268  10812   5664  -3648   2101    -75       C  
ATOM   4850  O   LEU D 107      35.984  39.122  37.802  1.00 86.48           O  
ANISOU 4850  O   LEU D 107    15090  11583   6184  -3594   1862    202       O  
ATOM   4851  CB  LEU D 107      34.134  38.202  35.401  1.00 68.82           C  
ANISOU 4851  CB  LEU D 107    12513   8952   4683  -3743   2266     33       C  
ATOM   4852  CG  LEU D 107      33.064  37.252  34.869  1.00 81.95           C  
ANISOU 4852  CG  LEU D 107    14044  10447   6645  -3921   2566     61       C  
ATOM   4853  CD1 LEU D 107      33.325  36.943  33.410  1.00 77.00           C  
ANISOU 4853  CD1 LEU D 107    13237   9623   6395  -3806   2292     11       C  
ATOM   4854  CD2 LEU D 107      33.029  35.983  35.707  1.00 78.79           C  
ANISOU 4854  CD2 LEU D 107    13751   9959   6226  -3977   2704    391       C  
ATOM   4855  N   ASP D 108      34.872  40.936  37.054  1.00 81.86           N  
ANISOU 4855  N   ASP D 108    14321  10972   5810  -3610   2101   -408       N  
ATOM   4856  CA  ASP D 108      35.888  41.910  37.454  1.00 81.30           C  
ANISOU 4856  CA  ASP D 108    14335  10998   5556  -3548   1814   -502       C  
ATOM   4857  C   ASP D 108      37.295  41.538  36.984  1.00 68.83           C  
ANISOU 4857  C   ASP D 108    12759   9394   3998  -3459   1372   -237       C  
ATOM   4858  O   ASP D 108      38.242  41.515  37.769  1.00 77.83           O  
ANISOU 4858  O   ASP D 108    14012  10669   4891  -3464   1133    -80       O  
ATOM   4859  CB  ASP D 108      35.858  42.131  38.969  1.00 90.43           C  
ANISOU 4859  CB  ASP D 108    15700  12334   6325  -3618   1910   -522       C  
ATOM   4860  CG  ASP D 108      35.529  43.561  39.332  1.00 97.66           C  
ANISOU 4860  CG  ASP D 108    16643  13276   7189  -3621   2046   -909       C  
ATOM   4861  OD1 ASP D 108      36.359  44.441  39.037  1.00 76.02           O  
ANISOU 4861  OD1 ASP D 108    13879  10519   4486  -3587   1785  -1046       O  
ATOM   4862  OD2 ASP D 108      34.446  43.812  39.903  1.00101.33           O  
ANISOU 4862  OD2 ASP D 108    17146  13752   7603  -3648   2436  -1060       O  
ATOM   4863  N   VAL D 109      37.405  41.234  35.696  1.00 64.98           N  
ANISOU 4863  N   VAL D 109    12139   8746   3805  -3365   1280   -175       N  
ATOM   4864  CA  VAL D 109      38.644  40.741  35.100  1.00 70.40           C  
ANISOU 4864  CA  VAL D 109    12808   9355   4585  -3230    919    129       C  
ATOM   4865  C   VAL D 109      39.889  41.603  35.357  1.00 68.18           C  
ANISOU 4865  C   VAL D 109    12534   9167   4203  -3174    580    144       C  
ATOM   4866  O   VAL D 109      40.870  41.121  35.920  1.00 74.01           O  
ANISOU 4866  O   VAL D 109    13316   9995   4809  -3153    346    440       O  
ATOM   4867  CB  VAL D 109      38.456  40.517  33.586  1.00 67.31           C  
ANISOU 4867  CB  VAL D 109    12296   8768   4512  -3106    906    119       C  
ATOM   4868  CG1 VAL D 109      39.766  40.086  32.925  1.00 60.86           C  
ANISOU 4868  CG1 VAL D 109    11455   7834   3836  -2902    562    448       C  
ATOM   4869  CG2 VAL D 109      37.346  39.490  33.358  1.00 62.76           C  
ANISOU 4869  CG2 VAL D 109    11721   8094   4030  -3227   1207    141       C  
ATOM   4870  N   ARG D 110      39.856  42.867  34.949  1.00 65.98           N  
ANISOU 4870  N   ARG D 110    12187   8870   4012  -3148    570   -167       N  
ATOM   4871  CA  ARG D 110      41.037  43.727  35.088  1.00 71.85           C  
ANISOU 4871  CA  ARG D 110    12931   9666   4704  -3136    255   -171       C  
ATOM   4872  C   ARG D 110      41.428  43.984  36.542  1.00 80.07           C  
ANISOU 4872  C   ARG D 110    14120  10921   5382  -3314    169   -200       C  
ATOM   4873  O   ARG D 110      42.612  44.043  36.874  1.00 67.40           O  
ANISOU 4873  O   ARG D 110    12526   9416   3669  -3339   -170    -11       O  
ATOM   4874  CB  ARG D 110      40.835  45.058  34.367  1.00 71.25           C  
ANISOU 4874  CB  ARG D 110    12750   9490   4832  -3064    326   -528       C  
ATOM   4875  CG  ARG D 110      42.069  45.954  34.349  1.00 71.34           C  
ANISOU 4875  CG  ARG D 110    12755   9502   4849  -3075      2   -539       C  
ATOM   4876  CD  ARG D 110      41.740  47.263  33.653  1.00 82.66           C  
ANISOU 4876  CD  ARG D 110    14078  10792   6536  -2984    157   -923       C  
ATOM   4877  NE  ARG D 110      40.445  47.770  34.104  1.00 86.47           N  
ANISOU 4877  NE  ARG D 110    14547  11282   7026  -3025    581  -1272       N  
ATOM   4878  CZ  ARG D 110      39.557  48.372  33.319  1.00 78.28           C  
ANISOU 4878  CZ  ARG D 110    13339  10124   6280  -2861    889  -1514       C  
ATOM   4879  NH1 ARG D 110      38.403  48.788  33.830  1.00 67.55           N  
ANISOU 4879  NH1 ARG D 110    11956   8784   4926  -2897   1276  -1757       N  
ATOM   4880  NH2 ARG D 110      39.819  48.557  32.026  1.00 64.00           N  
ANISOU 4880  NH2 ARG D 110    11289   8164   4865  -2579    807  -1432       N  
ATOM   4881  N   GLN D 111      40.438  44.143  37.412  1.00 69.12           N  
ANISOU 4881  N   GLN D 111    12843   9617   3801  -3426    474   -426       N  
ATOM   4882  CA  GLN D 111      40.736  44.438  38.811  1.00 74.14           C  
ANISOU 4882  CA  GLN D 111    13659  10470   4041  -3571    412   -489       C  
ATOM   4883  C   GLN D 111      41.443  43.261  39.466  1.00 79.49           C  
ANISOU 4883  C   GLN D 111    14398  11320   4483  -3565    209    -58       C  
ATOM   4884  O   GLN D 111      42.388  43.437  40.236  1.00 82.25           O  
ANISOU 4884  O   GLN D 111    14815  11871   4567  -3633    -75     30       O  
ATOM   4885  CB  GLN D 111      39.457  44.766  39.570  1.00 77.09           C  
ANISOU 4885  CB  GLN D 111    14153  10875   4262  -3639    830   -774       C  
ATOM   4886  CG  GLN D 111      39.680  45.172  41.012  1.00 82.83           C  
ANISOU 4886  CG  GLN D 111    15109  11823   4539  -3762    797   -891       C  
ATOM   4887  CD  GLN D 111      38.454  45.826  41.603  1.00113.65           C  
ANISOU 4887  CD  GLN D 111    19129  15697   8355  -3791   1234  -1230       C  
ATOM   4888  OE1 GLN D 111      37.431  45.174  41.815  1.00115.58           O  
ANISOU 4888  OE1 GLN D 111    19397  15935   8582  -3761   1569  -1151       O  
ATOM   4889  NE2 GLN D 111      38.542  47.128  41.855  1.00113.32           N  
ANISOU 4889  NE2 GLN D 111    19153  15616   8289  -3845   1258  -1598       N  
ATOM   4890  N   ASN D 112      40.979  42.060  39.137  1.00 77.97           N  
ANISOU 4890  N   ASN D 112    14165  11047   4414  -3476    366    210       N  
ATOM   4891  CA  ASN D 112      41.467  40.835  39.756  1.00 82.55           C  
ANISOU 4891  CA  ASN D 112    14780  11758   4829  -3415    285    639       C  
ATOM   4892  C   ASN D 112      42.727  40.252  39.130  1.00 82.47           C  
ANISOU 4892  C   ASN D 112    14614  11697   5022  -3260    -46   1025       C  
ATOM   4893  O   ASN D 112      43.539  39.638  39.825  1.00 78.56           O  
ANISOU 4893  O   ASN D 112    14118  11385   4344  -3196   -210   1358       O  
ATOM   4894  CB  ASN D 112      40.357  39.785  39.760  1.00 84.32           C  
ANISOU 4894  CB  ASN D 112    15029  11883   5126  -3392    662    752       C  
ATOM   4895  CG  ASN D 112      39.230  40.152  40.701  1.00 93.45           C  
ANISOU 4895  CG  ASN D 112    16340  13145   6021  -3509   1010    496       C  
ATOM   4896  OD1 ASN D 112      39.428  40.931  41.629  1.00 84.67           O  
ANISOU 4896  OD1 ASN D 112    15364  12229   4575  -3578    950    317       O  
ATOM   4897  ND2 ASN D 112      38.044  39.603  40.464  1.00 98.26           N  
ANISOU 4897  ND2 ASN D 112    16927  13615   6793  -3532   1385    475       N  
ATOM   4898  N   TYR D 113      42.885  40.446  37.822  1.00 70.89           N  
ANISOU 4898  N   TYR D 113    13005   9993   3938  -3160   -118    996       N  
ATOM   4899  CA  TYR D 113      43.952  39.784  37.075  1.00 72.45           C  
ANISOU 4899  CA  TYR D 113    13034  10080   4414  -2943   -345   1379       C  
ATOM   4900  C   TYR D 113      44.948  40.708  36.380  1.00 68.71           C  
ANISOU 4900  C   TYR D 113    12434   9553   4118  -2890   -658   1356       C  
ATOM   4901  O   TYR D 113      45.942  40.235  35.834  1.00 73.17           O  
ANISOU 4901  O   TYR D 113    12832  10040   4930  -2677   -837   1692       O  
ATOM   4902  CB  TYR D 113      43.349  38.840  36.032  1.00 67.49           C  
ANISOU 4902  CB  TYR D 113    12341   9175   4127  -2791   -132   1477       C  
ATOM   4903  CG  TYR D 113      42.583  37.702  36.653  1.00 68.31           C  
ANISOU 4903  CG  TYR D 113    12535   9290   4130  -2827    158   1616       C  
ATOM   4904  CD1 TYR D 113      43.229  36.534  37.025  1.00 82.79           C  
ANISOU 4904  CD1 TYR D 113    14316  11153   5987  -2656    153   2046       C  
ATOM   4905  CD2 TYR D 113      41.218  37.801  36.881  1.00 71.36           C  
ANISOU 4905  CD2 TYR D 113    13034   9658   4423  -3009    476   1340       C  
ATOM   4906  CE1 TYR D 113      42.537  35.486  37.608  1.00 83.40           C  
ANISOU 4906  CE1 TYR D 113    14472  11224   5993  -2675    452   2209       C  
ATOM   4907  CE2 TYR D 113      40.510  36.755  37.465  1.00 71.76           C  
ANISOU 4907  CE2 TYR D 113    13155   9701   4408  -3049    766   1499       C  
ATOM   4908  CZ  TYR D 113      41.178  35.601  37.823  1.00 81.39           C  
ANISOU 4908  CZ  TYR D 113    14340  10935   5651  -2886    748   1938       C  
ATOM   4909  OH  TYR D 113      40.493  34.557  38.399  1.00 81.57           O  
ANISOU 4909  OH  TYR D 113    14421  10932   5641  -2908   1068   2130       O  
ATOM   4910  N   ASP D 114      44.690  42.013  36.405  1.00 70.90           N  
ANISOU 4910  N   ASP D 114    12775   9859   4304  -3053   -682    969       N  
ATOM   4911  CA  ASP D 114      45.436  42.967  35.575  1.00 68.86           C  
ANISOU 4911  CA  ASP D 114    12406   9495   4262  -3002   -916    916       C  
ATOM   4912  C   ASP D 114      45.439  42.570  34.091  1.00 73.13           C  
ANISOU 4912  C   ASP D 114    12807   9757   5223  -2719   -872   1080       C  
ATOM   4913  O   ASP D 114      46.425  42.787  33.382  1.00 69.20           O  
ANISOU 4913  O   ASP D 114    12158   9157   4978  -2548  -1099   1299       O  
ATOM   4914  CB  ASP D 114      46.871  43.190  36.080  1.00 66.50           C  
ANISOU 4914  CB  ASP D 114    12023   9358   3884  -3052  -1315   1166       C  
ATOM   4915  CG  ASP D 114      46.917  43.827  37.466  1.00 95.38           C  
ANISOU 4915  CG  ASP D 114    15836  13298   7106  -3343  -1405    922       C  
ATOM   4916  OD1 ASP D 114      45.900  44.416  37.890  1.00 95.67           O  
ANISOU 4916  OD1 ASP D 114    16030  13349   6970  -3479  -1147    497       O  
ATOM   4917  OD2 ASP D 114      47.974  43.745  38.132  1.00 98.31           O  
ANISOU 4917  OD2 ASP D 114    16152  13878   7323  -3412  -1720   1152       O  
ATOM   4918  N   VAL D 115      44.333  41.986  33.632  1.00 68.56           N  
ANISOU 4918  N   VAL D 115    12267   9055   4727  -2663   -574    979       N  
ATOM   4919  CA  VAL D 115      44.126  41.711  32.210  1.00 59.27           C  
ANISOU 4919  CA  VAL D 115    10996   7628   3897  -2413   -505   1035       C  
ATOM   4920  C   VAL D 115      42.990  42.569  31.657  1.00 54.22           C  
ANISOU 4920  C   VAL D 115    10402   6946   3254  -2467   -280    615       C  
ATOM   4921  O   VAL D 115      41.931  42.666  32.265  1.00 56.07           O  
ANISOU 4921  O   VAL D 115    10708   7277   3318  -2655    -24    333       O  
ATOM   4922  CB  VAL D 115      43.797  40.232  31.968  1.00 64.15           C  
ANISOU 4922  CB  VAL D 115    11602   8127   4645  -2299   -355   1253       C  
ATOM   4923  CG1 VAL D 115      43.309  40.019  30.536  1.00 55.26           C  
ANISOU 4923  CG1 VAL D 115    10436   6758   3804  -2101   -254   1194       C  
ATOM   4924  CG2 VAL D 115      45.007  39.358  32.281  1.00 62.63           C  
ANISOU 4924  CG2 VAL D 115    11283   7960   4552  -2120   -512   1673       C  
ATOM   4925  N   THR D 116      43.224  43.214  30.517  1.00 50.42           N  
ANISOU 4925  N   THR D 116     9760   6310   3089  -2214   -343    563       N  
ATOM   4926  CA  THR D 116      42.194  44.003  29.845  1.00 49.28           C  
ANISOU 4926  CA  THR D 116     9424   6103   3196  -2093   -108    162       C  
ATOM   4927  C   THR D 116      41.549  43.199  28.724  1.00 56.75           C  
ANISOU 4927  C   THR D 116    10270   6912   4380  -1879     -1    203       C  
ATOM   4928  O   THR D 116      42.248  42.691  27.840  1.00 51.47           O  
ANISOU 4928  O   THR D 116     9571   6088   3896  -1622   -152    483       O  
ATOM   4929  CB  THR D 116      42.797  45.321  29.263  1.00 47.44           C  
ANISOU 4929  CB  THR D 116     8979   5779   3268  -1878   -204     55       C  
ATOM   4930  OG1 THR D 116      43.277  46.135  30.342  1.00 56.40           O  
ANISOU 4930  OG1 THR D 116    10216   7028   4186  -2141   -295    -82       O  
ATOM   4931  CG2 THR D 116      41.763  46.100  28.491  1.00 48.07           C  
ANISOU 4931  CG2 THR D 116     8834   5804   3627  -1688     62   -280       C  
ATOM   4932  N   VAL D 117      40.224  43.059  28.755  1.00 50.96           N  
ANISOU 4932  N   VAL D 117     9487   6233   3640  -1990    259    -72       N  
ATOM   4933  CA  VAL D 117      39.523  42.544  27.585  1.00 51.90           C  
ANISOU 4933  CA  VAL D 117     9451   6254   4016  -1799    324   -129       C  
ATOM   4934  C   VAL D 117      39.402  43.681  26.576  1.00 45.23           C  
ANISOU 4934  C   VAL D 117     8323   5394   3467  -1474    332   -307       C  
ATOM   4935  O   VAL D 117      38.629  44.617  26.776  1.00 49.01           O  
ANISOU 4935  O   VAL D 117     8647   5975   3998  -1507    530   -592       O  
ATOM   4936  CB  VAL D 117      38.120  42.009  27.931  1.00 51.83           C  
ANISOU 4936  CB  VAL D 117     9417   6321   3953  -2043    583   -339       C  
ATOM   4937  CG1 VAL D 117      37.475  41.401  26.682  1.00 46.19           C  
ANISOU 4937  CG1 VAL D 117     8536   5519   3496  -1885    573   -408       C  
ATOM   4938  CG2 VAL D 117      38.207  40.973  29.030  1.00 55.80           C  
ANISOU 4938  CG2 VAL D 117    10195   6838   4168  -2348    642   -139       C  
ATOM   4939  N   ILE D 118      40.179  43.628  25.497  1.00 51.37           N  
ANISOU 4939  N   ILE D 118     9035   6036   4445  -1129    156   -109       N  
ATOM   4940  CA  ILE D 118      40.193  44.736  24.545  1.00 51.01           C  
ANISOU 4940  CA  ILE D 118     8723   5977   4680   -769    180   -207       C  
ATOM   4941  C   ILE D 118      39.140  44.549  23.450  1.00 45.99           C  
ANISOU 4941  C   ILE D 118     7886   5402   4186   -571    264   -376       C  
ATOM   4942  O   ILE D 118      38.810  45.489  22.732  1.00 42.66           O  
ANISOU 4942  O   ILE D 118     7203   5040   3968   -286    349   -488       O  
ATOM   4943  CB  ILE D 118      41.599  44.949  23.913  1.00 43.37           C  
ANISOU 4943  CB  ILE D 118     7753   4844   3880   -442    -20    120       C  
ATOM   4944  CG1 ILE D 118      42.008  43.715  23.102  1.00 44.48           C  
ANISOU 4944  CG1 ILE D 118     8034   4848   4018   -258   -146    387       C  
ATOM   4945  CG2 ILE D 118      42.644  45.245  24.998  1.00 47.31           C  
ANISOU 4945  CG2 ILE D 118     8382   5328   4263   -663   -153    281       C  
ATOM   4946  CD1 ILE D 118      43.374  43.827  22.447  1.00 51.65           C  
ANISOU 4946  CD1 ILE D 118     8943   5577   5105    103   -295    768       C  
ATOM   4947  N   ALA D 119      38.591  43.341  23.341  1.00 42.26           N  
ANISOU 4947  N   ALA D 119     7523   4923   3612   -733    244   -391       N  
ATOM   4948  CA  ALA D 119      37.543  43.085  22.358  1.00 43.56           C  
ANISOU 4948  CA  ALA D 119     7490   5179   3883   -618    271   -585       C  
ATOM   4949  C   ALA D 119      36.780  41.805  22.660  1.00 45.66           C  
ANISOU 4949  C   ALA D 119     7873   5427   4047   -967    299   -670       C  
ATOM   4950  O   ALA D 119      37.330  40.881  23.247  1.00 44.55           O  
ANISOU 4950  O   ALA D 119     8018   5133   3776  -1164    266   -485       O  
ATOM   4951  CB  ALA D 119      38.145  43.003  20.937  1.00 41.61           C  
ANISOU 4951  CB  ALA D 119     7215   4844   3751   -160    102   -449       C  
ATOM   4952  N   ILE D 120      35.513  41.754  22.259  1.00 44.54           N  
ANISOU 4952  N   ILE D 120     7486   5440   3996  -1042    371   -923       N  
ATOM   4953  CA  ILE D 120      34.780  40.485  22.245  1.00 46.01           C  
ANISOU 4953  CA  ILE D 120     7737   5573   4172  -1344    367  -1019       C  
ATOM   4954  C   ILE D 120      34.338  40.135  20.827  1.00 56.09           C  
ANISOU 4954  C   ILE D 120     8867   6897   5548  -1143    187  -1170       C  
ATOM   4955  O   ILE D 120      33.731  40.958  20.138  1.00 58.38           O  
ANISOU 4955  O   ILE D 120     8825   7423   5933   -921    167  -1311       O  
ATOM   4956  CB  ILE D 120      33.584  40.474  23.209  1.00 50.91           C  
ANISOU 4956  CB  ILE D 120     8206   6328   4811  -1730    609  -1179       C  
ATOM   4957  CG1 ILE D 120      34.082  40.630  24.650  1.00 48.57           C  
ANISOU 4957  CG1 ILE D 120     8147   5982   4325  -1941    775  -1031       C  
ATOM   4958  CG2 ILE D 120      32.787  39.164  23.054  1.00 55.47           C  
ANISOU 4958  CG2 ILE D 120     8790   6821   5465  -2041    602  -1283       C  
ATOM   4959  CD1 ILE D 120      32.968  40.862  25.706  1.00 51.78           C  
ANISOU 4959  CD1 ILE D 120     8432   6530   4712  -2252   1086  -1165       C  
ATOM   4960  N   ILE D 121      34.671  38.922  20.386  1.00 53.77           N  
ANISOU 4960  N   ILE D 121     8835   6380   5215  -1203     65  -1131       N  
ATOM   4961  CA  ILE D 121      34.279  38.453  19.062  1.00 50.74           C  
ANISOU 4961  CA  ILE D 121     8391   6025   4864  -1055   -128  -1322       C  
ATOM   4962  C   ILE D 121      33.197  37.395  19.180  1.00 62.32           C  
ANISOU 4962  C   ILE D 121     9811   7457   6410  -1505   -114  -1563       C  
ATOM   4963  O   ILE D 121      33.445  36.287  19.659  1.00 60.30           O  
ANISOU 4963  O   ILE D 121     9851   6908   6150  -1780    -40  -1489       O  
ATOM   4964  CB  ILE D 121      35.474  37.858  18.287  1.00 57.40           C  
ANISOU 4964  CB  ILE D 121     9598   6594   5617   -751   -259  -1138       C  
ATOM   4965  CG1 ILE D 121      36.653  38.829  18.293  1.00 58.58           C  
ANISOU 4965  CG1 ILE D 121     9784   6727   5746   -342   -251   -835       C  
ATOM   4966  CG2 ILE D 121      35.080  37.520  16.843  1.00 53.66           C  
ANISOU 4966  CG2 ILE D 121     9092   6189   5109   -543   -465  -1375       C  
ATOM   4967  CD1 ILE D 121      37.917  38.216  17.761  1.00 56.42           C  
ANISOU 4967  CD1 ILE D 121     9869   6152   5417    -59   -315   -559       C  
ATOM   4968  N   LYS D 122      31.990  37.742  18.748  1.00 70.72           N  
ANISOU 4968  N   LYS D 122    10475   8818   7579  -1578   -171  -1826       N  
ATOM   4969  CA  LYS D 122      30.896  36.788  18.737  1.00 76.28           C  
ANISOU 4969  CA  LYS D 122    11057   9509   8416  -2016   -194  -2074       C  
ATOM   4970  C   LYS D 122      31.170  35.699  17.710  1.00 84.11           C  
ANISOU 4970  C   LYS D 122    12322  10282   9353  -2008   -421  -2229       C  
ATOM   4971  O   LYS D 122      32.020  35.861  16.833  1.00 84.33           O  
ANISOU 4971  O   LYS D 122    12553  10265   9224  -1593   -571  -2165       O  
ATOM   4972  CB  LYS D 122      29.574  37.486  18.427  1.00 81.36           C  
ANISOU 4972  CB  LYS D 122    11148  10567   9199  -2060   -236  -2281       C  
ATOM   4973  CG  LYS D 122      29.138  38.511  19.462  1.00 78.98           C  
ANISOU 4973  CG  LYS D 122    10581  10449   8980  -2094     58  -2161       C  
ATOM   4974  CD  LYS D 122      27.651  38.813  19.325  1.00 85.72           C  
ANISOU 4974  CD  LYS D 122    10883  11640  10044  -2268     82  -2334       C  
ATOM   4975  CE  LYS D 122      26.820  37.545  19.463  1.00 93.10           C  
ANISOU 4975  CE  LYS D 122    11766  12452  11156  -2786     46  -2508       C  
ATOM   4976  NZ  LYS D 122      25.382  37.766  19.137  1.00101.97           N  
ANISOU 4976  NZ  LYS D 122    12294  13932  12518  -2952     -6  -2669       N  
ATOM   4977  N   HIS D 123      30.450  34.588  17.827  1.00 92.24           N  
ANISOU 4977  N   HIS D 123    13370  11149  10528  -2467   -414  -2432       N  
ATOM   4978  CA  HIS D 123      30.593  33.474  16.898  1.00 97.22           C  
ANISOU 4978  CA  HIS D 123    14287  11526  11128  -2538   -599  -2651       C  
ATOM   4979  C   HIS D 123      30.339  33.929  15.459  1.00 96.90           C  
ANISOU 4979  C   HIS D 123    14077  11803  10938  -2212   -946  -2904       C  
ATOM   4980  O   HIS D 123      30.986  33.457  14.526  1.00 92.87           O  
ANISOU 4980  O   HIS D 123    13915  11120  10251  -1978  -1098  -2983       O  
ATOM   4981  CB  HIS D 123      29.629  32.350  17.279  1.00103.24           C  
ANISOU 4981  CB  HIS D 123    14983  12097  12147  -3141   -527  -2878       C  
ATOM   4982  CG  HIS D 123      30.126  30.982  16.948  1.00108.17           C  
ANISOU 4982  CG  HIS D 123    16089  12222  12790  -3304   -510  -2969       C  
ATOM   4983  ND1 HIS D 123      29.372  30.053  16.278  1.00114.72           N  
ANISOU 4983  ND1 HIS D 123    16901  12928  13758  -3661   -674  -3379       N  
ATOM   4984  CD2 HIS D 123      31.323  30.379  17.204  1.00106.81           C  
ANISOU 4984  CD2 HIS D 123    16433  11621  12531  -3155   -325  -2688       C  
ATOM   4985  CE1 HIS D 123      30.066  28.934  16.129  1.00116.70           C  
ANISOU 4985  CE1 HIS D 123    17671  12659  14012  -3727   -559  -3377       C  
ATOM   4986  NE2 HIS D 123      31.252  29.117  16.687  1.00112.03           N  
ANISOU 4986  NE2 HIS D 123    17396  11883  13287  -3403   -335  -2930       N  
ATOM   4987  N   ASN D 124      29.408  34.867  15.299  1.00100.29           N  
ANISOU 4987  N   ASN D 124    13976  12707  11424  -2166  -1042  -2999       N  
ATOM   4988  CA  ASN D 124      29.037  35.405  13.990  1.00101.51           C  
ANISOU 4988  CA  ASN D 124    13881  13264  11423  -1839  -1369  -3195       C  
ATOM   4989  C   ASN D 124      30.099  36.309  13.351  1.00 98.63           C  
ANISOU 4989  C   ASN D 124    13669  12985  10821  -1165  -1395  -2955       C  
ATOM   4990  O   ASN D 124      29.874  36.848  12.265  1.00 94.16           O  
ANISOU 4990  O   ASN D 124    12906  12776  10096   -807  -1629  -3052       O  
ATOM   4991  CB  ASN D 124      27.709  36.161  14.095  1.00108.72           C  
ANISOU 4991  CB  ASN D 124    14129  14670  12509  -1972  -1414  -3285       C  
ATOM   4992  CG  ASN D 124      27.753  37.277  15.126  1.00107.67           C  
ANISOU 4992  CG  ASN D 124    13774  14643  12491  -1841  -1079  -2971       C  
ATOM   4993  OD1 ASN D 124      28.824  37.767  15.476  1.00100.29           O  
ANISOU 4993  OD1 ASN D 124    13120  13532  11452  -1533   -912  -2708       O  
ATOM   4994  ND2 ASN D 124      26.587  37.682  15.618  1.00112.46           N  
ANISOU 4994  ND2 ASN D 124    13875  15529  13325  -2084   -974  -3003       N  
ATOM   4995  N   GLN D 125      31.216  36.492  14.065  1.00 94.52           N  
ANISOU 4995  N   GLN D 125    13460  12160  10294  -1003  -1150  -2620       N  
ATOM   4996  CA  GLN D 125      32.427  37.208  13.612  1.00 84.53           C  
ANISOU 4996  CA  GLN D 125    12393  10851   8875   -408  -1122  -2330       C  
ATOM   4997  C   GLN D 125      32.502  38.716  13.924  1.00 78.44           C  
ANISOU 4997  C   GLN D 125    11272  10357   8177    -81   -984  -2098       C  
ATOM   4998  O   GLN D 125      33.554  39.331  13.741  1.00 72.28           O  
ANISOU 4998  O   GLN D 125    10634   9483   7346    356   -914  -1823       O  
ATOM   4999  CB  GLN D 125      32.751  36.942  12.133  1.00 90.64           C  
ANISOU 4999  CB  GLN D 125    13367  11669   9405    -13  -1371  -2458       C  
ATOM   5000  CG  GLN D 125      34.228  36.756  11.859  1.00 91.28           C  
ANISOU 5000  CG  GLN D 125    13931  11384   9365    392  -1274  -2162       C  
ATOM   5001  CD  GLN D 125      34.796  35.554  12.588  1.00 97.12           C  
ANISOU 5001  CD  GLN D 125    15115  11612  10174     41  -1118  -2086       C  
ATOM   5002  OE1 GLN D 125      34.382  34.417  12.348  1.00108.96           O  
ANISOU 5002  OE1 GLN D 125    16827  12918  11654   -291  -1191  -2372       O  
ATOM   5003  NE2 GLN D 125      35.741  35.799  13.491  1.00 86.82           N  
ANISOU 5003  NE2 GLN D 125    13940  10087   8962    106   -900  -1693       N  
ATOM   5004  N   GLU D 126      31.409  39.308  14.396  1.00 69.63           N  
ANISOU 5004  N   GLU D 126     9698   9547   7212   -291   -913  -2195       N  
ATOM   5005  CA  GLU D 126      31.404  40.736  14.684  1.00 67.16           C  
ANISOU 5005  CA  GLU D 126     9065   9459   6995      8   -731  -2005       C  
ATOM   5006  C   GLU D 126      32.152  41.003  15.991  1.00 65.98           C  
ANISOU 5006  C   GLU D 126     9124   9027   6918   -129   -457  -1780       C  
ATOM   5007  O   GLU D 126      31.984  40.283  16.978  1.00 64.63           O  
ANISOU 5007  O   GLU D 126     9106   8667   6784   -587   -350  -1813       O  
ATOM   5008  CB  GLU D 126      29.971  41.291  14.728  1.00 75.83           C  
ANISOU 5008  CB  GLU D 126     9600  10973   8239   -134   -703  -2153       C  
ATOM   5009  CG  GLU D 126      29.123  40.792  15.886  1.00 88.83           C  
ANISOU 5009  CG  GLU D 126    11141  12553  10056   -724   -536  -2258       C  
ATOM   5010  CD  GLU D 126      27.651  41.161  15.753  1.00101.25           C  
ANISOU 5010  CD  GLU D 126    12128  14541  11800   -864   -540  -2391       C  
ATOM   5011  OE1 GLU D 126      26.995  40.674  14.806  1.00 99.67           O  
ANISOU 5011  OE1 GLU D 126    11730  14576  11565   -912   -850  -2596       O  
ATOM   5012  OE2 GLU D 126      27.152  41.936  16.602  1.00106.67           O  
ANISOU 5012  OE2 GLU D 126    12553  15322  12654   -927   -231  -2288       O  
ATOM   5013  N   LYS D 127      33.000  42.025  15.989  1.00 56.15           N  
ANISOU 5013  N   LYS D 127     7887   7755   5691    269   -348  -1546       N  
ATOM   5014  CA  LYS D 127      33.827  42.290  17.147  1.00 65.95           C  
ANISOU 5014  CA  LYS D 127     9345   8749   6964    146   -155  -1350       C  
ATOM   5015  C   LYS D 127      33.438  43.589  17.827  1.00 61.40           C  
ANISOU 5015  C   LYS D 127     8469   8334   6528    175     96  -1334       C  
ATOM   5016  O   LYS D 127      33.347  44.637  17.192  1.00 63.14           O  
ANISOU 5016  O   LYS D 127     8411   8732   6847    573    149  -1287       O  
ATOM   5017  CB  LYS D 127      35.319  42.262  16.794  1.00 68.82           C  
ANISOU 5017  CB  LYS D 127    10032   8848   7267    488   -224  -1077       C  
ATOM   5018  CG  LYS D 127      35.764  43.255  15.741  1.00 71.94           C  
ANISOU 5018  CG  LYS D 127    10260   9358   7718   1084   -246   -939       C  
ATOM   5019  CD  LYS D 127      37.262  43.113  15.487  1.00 75.83           C  
ANISOU 5019  CD  LYS D 127    11072   9548   8193   1386   -285   -626       C  
ATOM   5020  CE  LYS D 127      38.049  43.116  16.796  1.00 72.17           C  
ANISOU 5020  CE  LYS D 127    10795   8851   7775   1095   -186   -450       C  
ATOM   5021  NZ  LYS D 127      39.518  42.936  16.587  1.00 76.51           N  
ANISOU 5021  NZ  LYS D 127    11605   9121   8346   1367   -235    -93       N  
ATOM   5022  N   LEU D 128      33.168  43.486  19.122  1.00 54.69           N  
ANISOU 5022  N   LEU D 128     7689   7411   5680   -240    281  -1372       N  
ATOM   5023  CA  LEU D 128      32.905  44.639  19.957  1.00 49.73           C  
ANISOU 5023  CA  LEU D 128     6889   6860   5147   -263    566  -1377       C  
ATOM   5024  C   LEU D 128      34.229  45.117  20.529  1.00 53.54           C  
ANISOU 5024  C   LEU D 128     7648   7112   5583   -174    598  -1195       C  
ATOM   5025  O   LEU D 128      34.960  44.354  21.161  1.00 47.46           O  
ANISOU 5025  O   LEU D 128     7220   6145   4668   -401    515  -1089       O  
ATOM   5026  CB  LEU D 128      31.922  44.271  21.078  1.00 52.52           C  
ANISOU 5026  CB  LEU D 128     7204   7261   5488   -744    770  -1512       C  
ATOM   5027  CG  LEU D 128      31.777  45.209  22.280  1.00 58.73           C  
ANISOU 5027  CG  LEU D 128     7987   8045   6284   -873   1107  -1532       C  
ATOM   5028  CD1 LEU D 128      31.262  46.585  21.868  1.00 57.74           C  
ANISOU 5028  CD1 LEU D 128     7483   8097   6360   -543   1319  -1570       C  
ATOM   5029  CD2 LEU D 128      30.849  44.584  23.335  1.00 61.28           C  
ANISOU 5029  CD2 LEU D 128     8333   8394   6557  -1335   1310  -1624       C  
ATOM   5030  N   LEU D 129      34.545  46.382  20.288  1.00 53.25           N  
ANISOU 5030  N   LEU D 129     7440   7100   5693    160    720  -1138       N  
ATOM   5031  CA  LEU D 129      35.785  46.956  20.776  1.00 50.65           C  
ANISOU 5031  CA  LEU D 129     7310   6557   5379    233    735   -983       C  
ATOM   5032  C   LEU D 129      35.568  47.620  22.131  1.00 47.08           C  
ANISOU 5032  C   LEU D 129     6911   6085   4893    -83    988  -1114       C  
ATOM   5033  O   LEU D 129      34.504  48.164  22.397  1.00 49.58           O  
ANISOU 5033  O   LEU D 129     7008   6546   5283   -149   1247  -1286       O  
ATOM   5034  CB  LEU D 129      36.318  47.983  19.779  1.00 44.33           C  
ANISOU 5034  CB  LEU D 129     6304   5739   4801    764    758   -845       C  
ATOM   5035  CG  LEU D 129      36.619  47.474  18.363  1.00 45.92           C  
ANISOU 5035  CG  LEU D 129     6480   5971   4998   1169    537   -697       C  
ATOM   5036  CD1 LEU D 129      37.035  48.626  17.464  1.00 61.62           C  
ANISOU 5036  CD1 LEU D 129     8228   7964   7222   1725    642   -532       C  
ATOM   5037  CD2 LEU D 129      37.709  46.447  18.401  1.00 45.98           C  
ANISOU 5037  CD2 LEU D 129     6859   5747   4866   1097    311   -514       C  
ATOM   5038  N   ASN D 130      36.606  47.585  22.957  1.00 57.06           N  
ANISOU 5038  N   ASN D 130    10419   7088   4172  -2470    210   -802       N  
ATOM   5039  CA  ASN D 130      36.569  48.120  24.314  1.00 62.82           C  
ANISOU 5039  CA  ASN D 130    11406   7578   4886  -2676    720  -1080       C  
ATOM   5040  C   ASN D 130      35.275  47.813  25.052  1.00 66.40           C  
ANISOU 5040  C   ASN D 130    11560   7923   5746  -2526   1062  -1284       C  
ATOM   5041  O   ASN D 130      34.517  48.726  25.393  1.00 67.22           O  
ANISOU 5041  O   ASN D 130    11659   7666   6217  -2323   1379  -1414       O  
ATOM   5042  CB  ASN D 130      36.845  49.615  24.311  1.00 68.68           C  
ANISOU 5042  CB  ASN D 130    12494   7883   5718  -2670    896  -1097       C  
ATOM   5043  CG  ASN D 130      38.208  49.945  23.737  1.00 70.90           C  
ANISOU 5043  CG  ASN D 130    13026   8294   5617  -2900    622   -882       C  
ATOM   5044  OD1 ASN D 130      39.198  49.250  24.003  1.00 63.86           O  
ANISOU 5044  OD1 ASN D 130    11696   7715   4853  -2922    476   -688       O  
ATOM   5045  ND2 ASN D 130      38.268  51.001  22.941  1.00 70.05           N  
ANISOU 5045  ND2 ASN D 130    13106   7855   5654  -2767    547   -699       N  
ATOM   5046  N   PRO D 131      35.015  46.518  25.282  1.00 65.04           N  
ANISOU 5046  N   PRO D 131    11138   8054   5521  -2618   1017  -1300       N  
ATOM   5047  CA  PRO D 131      33.875  46.075  26.086  1.00 65.40           C  
ANISOU 5047  CA  PRO D 131    10886   8070   5894  -2571   1377  -1472       C  
ATOM   5048  C   PRO D 131      33.904  46.710  27.461  1.00 61.13           C  
ANISOU 5048  C   PRO D 131    10619   7378   5230  -2718   1917  -1730       C  
ATOM   5049  O   PRO D 131      34.976  47.103  27.942  1.00 58.76           O  
ANISOU 5049  O   PRO D 131    10714   7106   4505  -2962   1969  -1780       O  
ATOM   5050  CB  PRO D 131      34.111  44.569  26.220  1.00 68.27           C  
ANISOU 5050  CB  PRO D 131    11141   8758   6040  -2790   1257  -1409       C  
ATOM   5051  CG  PRO D 131      35.559  44.380  25.931  1.00 62.94           C  
ANISOU 5051  CG  PRO D 131    10660   8235   5019  -2861    936  -1175       C  
ATOM   5052  CD  PRO D 131      35.868  45.385  24.888  1.00 63.58           C  
ANISOU 5052  CD  PRO D 131    10898   8219   5039  -2740    665  -1108       C  
ATOM   5053  N   GLY D 132      32.740  46.811  28.094  1.00 64.86           N  
ANISOU 5053  N   GLY D 132    10825   7739   6080  -2563   2301  -1894       N  
ATOM   5054  CA  GLY D 132      32.653  47.428  29.406  1.00 68.72           C  
ANISOU 5054  CA  GLY D 132    11547   8111   6454  -2658   2844  -2185       C  
ATOM   5055  C   GLY D 132      32.146  46.481  30.477  1.00 64.71           C  
ANISOU 5055  C   GLY D 132    10842   7873   5872  -2813   3204  -2269       C  
ATOM   5056  O   GLY D 132      32.108  45.269  30.295  1.00 68.53           O  
ANISOU 5056  O   GLY D 132    11114   8605   6319  -2937   3038  -2087       O  
ATOM   5057  N   ALA D 133      31.744  47.041  31.609  1.00 68.62           N  
ANISOU 5057  N   ALA D 133    11424   8301   6346  -2803   3730  -2548       N  
ATOM   5058  CA  ALA D 133      31.323  46.219  32.732  1.00 70.10           C  
ANISOU 5058  CA  ALA D 133    11428   8773   6433  -2940   4081  -2570       C  
ATOM   5059  C   ALA D 133      30.106  45.346  32.425  1.00 89.55           C  
ANISOU 5059  C   ALA D 133    13334  11340   9352  -2834   4149  -2447       C  
ATOM   5060  O   ALA D 133      30.008  44.227  32.922  1.00 78.45           O  
ANISOU 5060  O   ALA D 133    11797  10190   7821  -3056   4277  -2318       O  
ATOM   5061  CB  ALA D 133      31.041  47.102  33.963  1.00 74.89           C  
ANISOU 5061  CB  ALA D 133    12107   9281   7067  -2840   4466  -2817       C  
ATOM   5062  N   ASP D 134      29.180  45.858  31.617  1.00 73.66           N  
ANISOU 5062  N   ASP D 134    10958   9129   7899  -2487   4032  -2448       N  
ATOM   5063  CA  ASP D 134      27.902  45.170  31.401  1.00 76.27           C  
ANISOU 5063  CA  ASP D 134    10649   9605   8724  -2383   4093  -2370       C  
ATOM   5064  C   ASP D 134      27.887  44.222  30.194  1.00 73.33           C  
ANISOU 5064  C   ASP D 134     9990   9336   8535  -2460   3543  -2134       C  
ATOM   5065  O   ASP D 134      26.855  43.621  29.887  1.00 75.77           O  
ANISOU 5065  O   ASP D 134     9739   9787   9265  -2435   3528  -2096       O  
ATOM   5066  CB  ASP D 134      26.753  46.173  31.283  1.00 81.57           C  
ANISOU 5066  CB  ASP D 134    10970  10128   9895  -1924   4313  -2513       C  
ATOM   5067  CG  ASP D 134      26.472  46.901  32.591  1.00 95.22           C  
ANISOU 5067  CG  ASP D 134    12868  11800  11512  -1836   4954  -2804       C  
ATOM   5068  OD1 ASP D 134      26.419  46.248  33.658  1.00 99.60           O  
ANISOU 5068  OD1 ASP D 134    13417  12612  11815  -2107   5333  -2855       O  
ATOM   5069  OD2 ASP D 134      26.301  48.136  32.550  1.00 99.70           O  
ANISOU 5069  OD2 ASP D 134    13589  12055  12237  -1476   5095  -2979       O  
ATOM   5070  N   SER D 135      29.017  44.095  29.504  1.00 68.63           N  
ANISOU 5070  N   SER D 135     9755   8704   7617  -2566   3098  -2005       N  
ATOM   5071  CA  SER D 135      29.108  43.124  28.410  1.00 66.01           C  
ANISOU 5071  CA  SER D 135     9210   8491   7381  -2652   2591  -1830       C  
ATOM   5072  C   SER D 135      28.979  41.712  28.983  1.00 69.63           C  
ANISOU 5072  C   SER D 135     9563   9101   7791  -3006   2758  -1767       C  
ATOM   5073  O   SER D 135      29.711  41.339  29.898  1.00 64.62           O  
ANISOU 5073  O   SER D 135     9307   8520   6727  -3231   3003  -1722       O  
ATOM   5074  CB  SER D 135      30.430  43.271  27.652  1.00 61.31           C  
ANISOU 5074  CB  SER D 135     9047   7869   6378  -2682   2134  -1705       C  
ATOM   5075  OG  SER D 135      30.650  44.615  27.267  1.00 63.76           O  
ANISOU 5075  OG  SER D 135     9542   7980   6705  -2415   2061  -1729       O  
ATOM   5076  N   ILE D 136      28.035  40.937  28.463  1.00 68.06           N  
ANISOU 5076  N   ILE D 136     8844   8983   8032  -3060   2642  -1756       N  
ATOM   5077  CA  ILE D 136      27.840  39.576  28.943  1.00 71.55           C  
ANISOU 5077  CA  ILE D 136     9193   9480   8514  -3427   2825  -1681       C  
ATOM   5078  C   ILE D 136      28.702  38.600  28.146  1.00 73.06           C  
ANISOU 5078  C   ILE D 136     9619   9636   8505  -3591   2368  -1565       C  
ATOM   5079  O   ILE D 136      28.799  38.696  26.922  1.00 71.71           O  
ANISOU 5079  O   ILE D 136     9327   9489   8430  -3449   1856  -1595       O  
ATOM   5080  CB  ILE D 136      26.362  39.138  28.844  1.00 76.08           C  
ANISOU 5080  CB  ILE D 136     9067  10154   9688  -3500   2973  -1763       C  
ATOM   5081  CG1 ILE D 136      25.434  40.225  29.395  1.00 83.80           C  
ANISOU 5081  CG1 ILE D 136     9728  11208  10902  -3211   3360  -1891       C  
ATOM   5082  CG2 ILE D 136      26.138  37.820  29.583  1.00 78.22           C  
ANISOU 5082  CG2 ILE D 136     9298  10410  10012  -3931   3309  -1660       C  
ATOM   5083  CD1 ILE D 136      23.964  39.878  29.290  1.00 83.89           C  
ANISOU 5083  CD1 ILE D 136     8968  11421  11485  -3254   3507  -1967       C  
ATOM   5084  N   ILE D 137      29.342  37.670  28.846  1.00 68.39           N  
ANISOU 5084  N   ILE D 137     9370   9009   7606  -3848   2566  -1419       N  
ATOM   5085  CA  ILE D 137      30.063  36.594  28.186  1.00 66.44           C  
ANISOU 5085  CA  ILE D 137     9338   8692   7213  -3981   2212  -1313       C  
ATOM   5086  C   ILE D 137      29.089  35.508  27.740  1.00 67.64           C  
ANISOU 5086  C   ILE D 137     9063   8740   7899  -4226   2171  -1382       C  
ATOM   5087  O   ILE D 137      28.331  34.958  28.551  1.00 69.38           O  
ANISOU 5087  O   ILE D 137     9083   8903   8376  -4471   2622  -1341       O  
ATOM   5088  CB  ILE D 137      31.140  35.984  29.095  1.00 71.93           C  
ANISOU 5088  CB  ILE D 137    10570   9393   7369  -4100   2449  -1089       C  
ATOM   5089  CG1 ILE D 137      32.220  37.021  29.405  1.00 78.48           C  
ANISOU 5089  CG1 ILE D 137    11800  10391   7628  -3921   2406  -1070       C  
ATOM   5090  CG2 ILE D 137      31.745  34.751  28.443  1.00 70.37           C  
ANISOU 5090  CG2 ILE D 137    10570   9069   7098  -4195   2147   -977       C  
ATOM   5091  CD1 ILE D 137      33.531  36.425  29.876  1.00 77.81           C  
ANISOU 5091  CD1 ILE D 137    12074  10330   7159  -3757   2194   -871       C  
ATOM   5092  N   GLU D 138      29.107  35.209  26.444  1.00 66.02           N  
ANISOU 5092  N   GLU D 138     8706   8534   7845  -4185   1637  -1499       N  
ATOM   5093  CA  GLU D 138      28.202  34.229  25.852  1.00 68.11           C  
ANISOU 5093  CA  GLU D 138     8539   8725   8614  -4455   1515  -1655       C  
ATOM   5094  C   GLU D 138      28.983  33.049  25.285  1.00 66.68           C  
ANISOU 5094  C   GLU D 138     8709   8345   8283  -4600   1238  -1641       C  
ATOM   5095  O   GLU D 138      30.139  33.197  24.893  1.00 67.33           O  
ANISOU 5095  O   GLU D 138     9218   8465   7898  -4379    950  -1555       O  
ATOM   5096  CB  GLU D 138      27.401  34.870  24.722  1.00 86.43           C  
ANISOU 5096  CB  GLU D 138    10294  11288  11259  -4268   1096  -1878       C  
ATOM   5097  CG  GLU D 138      26.580  36.077  25.131  1.00100.11           C  
ANISOU 5097  CG  GLU D 138    11656  13203  13180  -4024   1338  -1897       C  
ATOM   5098  CD  GLU D 138      26.442  37.085  24.005  1.00111.15           C  
ANISOU 5098  CD  GLU D 138    12798  14829  14603  -3614    865  -1968       C  
ATOM   5099  OE1 GLU D 138      25.471  37.872  24.022  1.00118.76           O  
ANISOU 5099  OE1 GLU D 138    13282  15968  15873  -3395    974  -2023       O  
ATOM   5100  OE2 GLU D 138      27.312  37.093  23.107  1.00110.90           O  
ANISOU 5100  OE2 GLU D 138    13045  14823  14270  -3479    400  -1939       O  
ATOM   5101  N   GLU D 139      28.345  31.883  25.235  1.00 70.87           N  
ANISOU 5101  N   GLU D 139     9051   8655   9219  -4976   1343  -1737       N  
ATOM   5102  CA  GLU D 139      28.987  30.685  24.703  1.00 77.79           C  
ANISOU 5102  CA  GLU D 139    10275   9254  10026  -5100   1125  -1764       C  
ATOM   5103  C   GLU D 139      29.527  30.943  23.294  1.00 76.41           C  
ANISOU 5103  C   GLU D 139    10107   9275   9648  -4825    457  -1961       C  
ATOM   5104  O   GLU D 139      28.858  31.566  22.472  1.00 70.05           O  
ANISOU 5104  O   GLU D 139     8812   8758   9047  -4738    124  -2183       O  
ATOM   5105  CB  GLU D 139      28.026  29.485  24.711  1.00 76.90           C  
ANISOU 5105  CB  GLU D 139     9881   8874  10464  -5386   1266  -1849       C  
ATOM   5106  CG  GLU D 139      28.730  28.142  24.501  1.00 93.89           C  
ANISOU 5106  CG  GLU D 139    12503  10619  12550  -5420   1207  -1788       C  
ATOM   5107  CD  GLU D 139      27.807  26.942  24.648  1.00106.88           C  
ANISOU 5107  CD  GLU D 139    13940  11921  14748  -5752   1407  -1839       C  
ATOM   5108  OE1 GLU D 139      28.311  25.797  24.622  1.00108.72           O  
ANISOU 5108  OE1 GLU D 139    14579  11736  14992  -5809   1457  -1771       O  
ATOM   5109  OE2 GLU D 139      26.580  27.136  24.788  1.00112.74           O  
ANISOU 5109  OE2 GLU D 139    14118  12808  15911  -5964   1522  -1943       O  
ATOM   5110  N   ASN D 140      30.756  30.490  23.057  1.00 75.12           N  
ANISOU 5110  N   ASN D 140    10485   9013   9045  -4635    284  -1838       N  
ATOM   5111  CA  ASN D 140      31.443  30.628  21.770  1.00 76.50           C  
ANISOU 5111  CA  ASN D 140    10712   9402   8954  -4256   -297  -1935       C  
ATOM   5112  C   ASN D 140      31.922  32.036  21.404  1.00 72.46           C  
ANISOU 5112  C   ASN D 140    10175   9280   8078  -3896   -553  -1840       C  
ATOM   5113  O   ASN D 140      32.305  32.286  20.256  1.00 66.33           O  
ANISOU 5113  O   ASN D 140     9307   8720   7177  -3508   -997  -1865       O  
ATOM   5114  CB  ASN D 140      30.641  29.988  20.627  1.00 80.61           C  
ANISOU 5114  CB  ASN D 140    10801   9917   9911  -4276   -657  -2256       C  
ATOM   5115  CG  ASN D 140      30.812  28.487  20.576  1.00 91.62           C  
ANISOU 5115  CG  ASN D 140    12450  10889  11471  -4449   -578  -2335       C  
ATOM   5116  OD1 ASN D 140      30.493  27.782  21.531  1.00 98.93           O  
ANISOU 5116  OD1 ASN D 140    13508  11452  12631  -4786   -119  -2233       O  
ATOM   5117  ND2 ASN D 140      31.315  27.988  19.457  1.00 99.31           N  
ANISOU 5117  ND2 ASN D 140    13500  11893  12340  -4189   -995  -2502       N  
ATOM   5118  N   ASP D 141      31.915  32.946  22.379  1.00 62.99           N  
ANISOU 5118  N   ASP D 141     9054   8138   6741  -3959   -224  -1698       N  
ATOM   5119  CA  ASP D 141      32.591  34.229  22.218  1.00 67.40           C  
ANISOU 5119  CA  ASP D 141     9743   8960   6905  -3637   -384  -1562       C  
ATOM   5120  C   ASP D 141      34.095  33.997  22.248  1.00 58.24           C  
ANISOU 5120  C   ASP D 141     9050   7841   5239  -3332   -430  -1266       C  
ATOM   5121  O   ASP D 141      34.582  33.097  22.934  1.00 60.77           O  
ANISOU 5121  O   ASP D 141     9706   8000   5382  -3486   -193  -1162       O  
ATOM   5122  CB  ASP D 141      32.239  35.206  23.357  1.00 64.48           C  
ANISOU 5122  CB  ASP D 141     9343   8584   6572  -3631     72  -1448       C  
ATOM   5123  CG  ASP D 141      30.903  35.902  23.156  1.00 75.29           C  
ANISOU 5123  CG  ASP D 141    10138  10023   8445  -3584    103  -1601       C  
ATOM   5124  OD1 ASP D 141      30.349  35.842  22.039  1.00 76.22           O  
ANISOU 5124  OD1 ASP D 141     9868  10284   8809  -3510   -300  -1764       O  
ATOM   5125  OD2 ASP D 141      30.411  36.527  24.123  1.00 80.23           O  
ANISOU 5125  OD2 ASP D 141    10686  10608   9188  -3591    533  -1562       O  
ATOM   5126  N   THR D 142      34.838  34.820  21.523  1.00 56.71           N  
ANISOU 5126  N   THR D 142     9197   5634   6716  -3593   1576   -837       N  
ATOM   5127  CA  THR D 142      36.276  34.871  21.726  1.00 60.85           C  
ANISOU 5127  CA  THR D 142    10032   6125   6964  -3546   1614   -915       C  
ATOM   5128  C   THR D 142      36.657  36.182  22.398  1.00 59.44           C  
ANISOU 5128  C   THR D 142     9510   6554   6520  -3431   1740   -778       C  
ATOM   5129  O   THR D 142      36.456  37.256  21.835  1.00 60.35           O  
ANISOU 5129  O   THR D 142     9104   7188   6638  -3237   1735   -911       O  
ATOM   5130  CB  THR D 142      37.044  34.724  20.402  1.00 65.99           C  
ANISOU 5130  CB  THR D 142    10722   6746   7606  -3405   1478  -1396       C  
ATOM   5131  OG1 THR D 142      36.698  33.475  19.801  1.00 64.23           O  
ANISOU 5131  OG1 THR D 142    10890   5909   7607  -3329   1222  -1627       O  
ATOM   5132  CG2 THR D 142      38.537  34.755  20.651  1.00 64.80           C  
ANISOU 5132  CG2 THR D 142    10620   6823   7177  -2785   1348  -1300       C  
ATOM   5133  N   LEU D 143      37.187  36.094  23.615  1.00 55.68           N  
ANISOU 5133  N   LEU D 143     9368   5949   5839  -3466   1771   -514       N  
ATOM   5134  CA  LEU D 143      37.696  37.271  24.309  1.00 50.65           C  
ANISOU 5134  CA  LEU D 143     8467   5793   4985  -3332   1755   -452       C  
ATOM   5135  C   LEU D 143      39.105  37.599  23.827  1.00 55.11           C  
ANISOU 5135  C   LEU D 143     8924   6630   5384  -3289   1740   -492       C  
ATOM   5136  O   LEU D 143      39.962  36.722  23.790  1.00 52.76           O  
ANISOU 5136  O   LEU D 143     8904   6116   5025  -2864   1485   -441       O  
ATOM   5137  CB  LEU D 143      37.730  37.016  25.813  1.00 59.61           C  
ANISOU 5137  CB  LEU D 143    10024   6728   5898  -3382   1782   -133       C  
ATOM   5138  CG  LEU D 143      36.461  36.419  26.419  1.00 65.18           C  
ANISOU 5138  CG  LEU D 143    10848   7130   6788  -3424   1880     49       C  
ATOM   5139  CD1 LEU D 143      36.648  36.153  27.901  1.00 73.61           C  
ANISOU 5139  CD1 LEU D 143    12344   8042   7581  -3415   1953    400       C  
ATOM   5140  CD2 LEU D 143      35.296  37.360  26.187  1.00 67.60           C  
ANISOU 5140  CD2 LEU D 143    10604   7747   7333  -3284   1876    -70       C  
ATOM   5141  N   VAL D 144      39.355  38.852  23.455  1.00 47.96           N  
ANISOU 5141  N   VAL D 144     7379   6268   4577  -3053   1640   -640       N  
ATOM   5142  CA  VAL D 144      40.708  39.247  23.065  1.00 45.91           C  
ANISOU 5142  CA  VAL D 144     6787   6424   4231  -2780   1555   -614       C  
ATOM   5143  C   VAL D 144      41.329  39.907  24.288  1.00 47.51           C  
ANISOU 5143  C   VAL D 144     7027   6805   4218  -2816   1410   -417       C  
ATOM   5144  O   VAL D 144      40.841  40.938  24.757  1.00 49.51           O  
ANISOU 5144  O   VAL D 144     7058   7140   4615  -2864   1344   -494       O  
ATOM   5145  CB  VAL D 144      40.710  40.214  21.875  1.00 45.70           C  
ANISOU 5145  CB  VAL D 144     6038   6797   4527  -2503   1514   -799       C  
ATOM   5146  CG1 VAL D 144      42.137  40.489  21.418  1.00 50.30           C  
ANISOU 5146  CG1 VAL D 144     6176   7846   5091  -2092   1452   -711       C  
ATOM   5147  CG2 VAL D 144      39.890  39.641  20.732  1.00 50.97           C  
ANISOU 5147  CG2 VAL D 144     6729   7323   5314  -2528   1620  -1032       C  
ATOM   5148  N   LEU D 145      42.378  39.285  24.822  1.00 51.67           N  
ANISOU 5148  N   LEU D 145     7819   7232   4581  -2427   1066   -229       N  
ATOM   5149  CA  LEU D 145      42.892  39.623  26.155  1.00 45.95           C  
ANISOU 5149  CA  LEU D 145     7320   6582   3555  -2466    836    -37       C  
ATOM   5150  C   LEU D 145      44.282  40.229  26.045  1.00 50.78           C  
ANISOU 5150  C   LEU D 145     7425   7592   4276  -2090    442     37       C  
ATOM   5151  O   LEU D 145      45.132  39.721  25.309  1.00 53.14           O  
ANISOU 5151  O   LEU D 145     7504   7935   4752  -1605    281    127       O  
ATOM   5152  CB  LEU D 145      42.969  38.374  27.044  1.00 51.04           C  
ANISOU 5152  CB  LEU D 145     8694   6789   3911  -2333    721    221       C  
ATOM   5153  CG  LEU D 145      41.712  37.526  27.265  1.00 52.48           C  
ANISOU 5153  CG  LEU D 145     9405   6461   4073  -2652   1068    281       C  
ATOM   5154  CD1 LEU D 145      42.039  36.208  27.973  1.00 58.13           C  
ANISOU 5154  CD1 LEU D 145    10741   6733   4613  -2389    931    600       C  
ATOM   5155  CD2 LEU D 145      40.667  38.299  28.052  1.00 60.05           C  
ANISOU 5155  CD2 LEU D 145    10483   7483   4852  -3149   1393    305       C  
ATOM   5156  N   SER D 146      44.521  41.309  26.779  1.00 45.98           N  
ANISOU 5156  N   SER D 146     6631   7249   3591  -2295    279     16       N  
ATOM   5157  CA  SER D 146      45.835  41.933  26.762  1.00 47.13           C  
ANISOU 5157  CA  SER D 146     6241   7729   3936  -2009   -165    123       C  
ATOM   5158  C   SER D 146      46.404  42.039  28.172  1.00 51.67           C  
ANISOU 5158  C   SER D 146     7188   8308   4136  -2040   -627    240       C  
ATOM   5159  O   SER D 146      45.718  42.454  29.101  1.00 52.28           O  
ANISOU 5159  O   SER D 146     7681   8321   3862  -2397   -547    110       O  
ATOM   5160  CB  SER D 146      45.771  43.307  26.102  1.00 47.41           C  
ANISOU 5160  CB  SER D 146     5515   8108   4392  -2194    -33    -42       C  
ATOM   5161  OG  SER D 146      47.026  43.959  26.191  1.00 45.88           O  
ANISOU 5161  OG  SER D 146     4764   8183   4484  -1977   -497    109       O  
ATOM   5162  N   GLY D 147      47.663  41.658  28.327  1.00 57.39           N  
ANISOU 5162  N   GLY D 147     7768   9127   4908  -1625  -1109    506       N  
ATOM   5163  CA  GLY D 147      48.303  41.675  29.631  1.00 60.62           C  
ANISOU 5163  CA  GLY D 147     8516   9581   4936  -1600  -1642    641       C  
ATOM   5164  C   GLY D 147      49.655  41.001  29.603  1.00 66.21           C  
ANISOU 5164  C   GLY D 147     9027  10370   5761  -1075  -2111   1030       C  
ATOM   5165  O   GLY D 147      50.160  40.655  28.533  1.00 63.66           O  
ANISOU 5165  O   GLY D 147     8245  10090   5853   -705  -2000   1190       O  
ATOM   5166  N   GLU D 148      50.235  40.821  30.787  1.00 77.16           N  
ANISOU 5166  N   GLU D 148    10770  11799   6749  -1004  -2624   1203       N  
ATOM   5167  CA  GLU D 148      51.518  40.148  30.962  1.00 79.17           C  
ANISOU 5167  CA  GLU D 148    10880  12143   7060   -511  -3111   1645       C  
ATOM   5168  C   GLU D 148      51.296  38.653  30.881  1.00 77.82           C  
ANISOU 5168  C   GLU D 148    11277  11630   6660   -170  -2789   1901       C  
ATOM   5169  O   GLU D 148      50.242  38.169  31.287  1.00 76.94           O  
ANISOU 5169  O   GLU D 148    11835  11228   6172   -386  -2409   1783       O  
ATOM   5170  CB  GLU D 148      52.105  40.488  32.331  1.00 97.81           C  
ANISOU 5170  CB  GLU D 148    13481  14683   8999   -585  -3806   1717       C  
ATOM   5171  CG  GLU D 148      52.215  41.975  32.622  1.00108.33           C  
ANISOU 5171  CG  GLU D 148    14416  16248  10498   -990  -4193   1372       C  
ATOM   5172  CD  GLU D 148      53.557  42.553  32.215  1.00120.83           C  
ANISOU 5172  CD  GLU D 148    15066  18096  12746   -818  -4787   1610       C  
ATOM   5173  OE1 GLU D 148      53.722  42.898  31.024  1.00120.38           O  
ANISOU 5173  OE1 GLU D 148    14269  18101  13367   -733  -4499   1670       O  
ATOM   5174  OE2 GLU D 148      54.446  42.661  33.089  1.00129.01           O  
ANISOU 5174  OE2 GLU D 148    16089  19276  13653   -735  -5510   1757       O  
ATOM   5175  N   ARG D 149      52.290  37.923  30.375  1.00 81.07           N  
ANISOU 5175  N   ARG D 149    11414  12048   7342    375  -2927   2288       N  
ATOM   5176  CA  ARG D 149      52.159  36.479  30.176  1.00 87.37           C  
ANISOU 5176  CA  ARG D 149    12723  12454   8021    754  -2614   2522       C  
ATOM   5177  C   ARG D 149      51.759  35.776  31.467  1.00 94.72           C  
ANISOU 5177  C   ARG D 149    14473  13165   8352    670  -2672   2682       C  
ATOM   5178  O   ARG D 149      50.912  34.880  31.463  1.00 85.57           O  
ANISOU 5178  O   ARG D 149    13890  11570   7052    638  -2227   2672       O  
ATOM   5179  CB  ARG D 149      53.461  35.872  29.645  1.00 93.68           C  
ANISOU 5179  CB  ARG D 149    13116  13331   9146   1427  -2819   2985       C  
ATOM   5180  CG  ARG D 149      53.298  34.458  29.091  1.00100.60           C  
ANISOU 5180  CG  ARG D 149    14449  13739  10037   1866  -2401   3127       C  
ATOM   5181  CD  ARG D 149      52.954  34.486  27.605  1.00103.24           C  
ANISOU 5181  CD  ARG D 149    14492  13980  10754   2008  -1946   2835       C  
ATOM   5182  NE  ARG D 149      52.058  33.401  27.204  1.00108.85           N  
ANISOU 5182  NE  ARG D 149    15860  14118  11378   2038  -1494   2631       N  
ATOM   5183  CZ  ARG D 149      51.671  33.178  25.949  1.00106.21           C  
ANISOU 5183  CZ  ARG D 149    15463  13615  11276   2205  -1128   2333       C  
ATOM   5184  NH1 ARG D 149      50.850  32.172  25.671  1.00108.08           N  
ANISOU 5184  NH1 ARG D 149    16329  13270  11466   2176   -821   2120       N  
ATOM   5185  NH2 ARG D 149      52.108  33.957  24.967  1.00 96.81           N  
ANISOU 5185  NH2 ARG D 149    13573  12833  10378   2417  -1088   2261       N  
ATOM   5186  N   LYS D 150      52.369  36.204  32.569  1.00 95.33           N  
ANISOU 5186  N   LYS D 150    14581  13547   8093    644  -3240   2843       N  
ATOM   5187  CA  LYS D 150      52.084  35.642  33.881  1.00 94.93           C  
ANISOU 5187  CA  LYS D 150    15287  13399   7383    639  -3338   3046       C  
ATOM   5188  C   LYS D 150      50.615  35.823  34.249  1.00 96.79           C  
ANISOU 5188  C   LYS D 150    16083  13411   7280    172  -2835   2722       C  
ATOM   5189  O   LYS D 150      49.976  34.901  34.760  1.00 94.55           O  
ANISOU 5189  O   LYS D 150    16441  12796   6689    228  -2497   2939       O  
ATOM   5190  CB  LYS D 150      52.978  36.299  34.933  1.00103.96           C  
ANISOU 5190  CB  LYS D 150    16319  14990   8190    661  -4122   3166       C  
ATOM   5191  CG  LYS D 150      54.461  36.209  34.608  1.00107.44           C  
ANISOU 5191  CG  LYS D 150    16091  15684   9046   1091  -4668   3565       C  
ATOM   5192  CD  LYS D 150      55.317  36.848  35.688  1.00113.60           C  
ANISOU 5192  CD  LYS D 150    16728  16886   9548   1069  -5492   3641       C  
ATOM   5193  CE  LYS D 150      56.799  36.640  35.409  1.00117.72           C  
ANISOU 5193  CE  LYS D 150    16508  17620  10599   1550  -5861   4045       C  
ATOM   5194  NZ  LYS D 150      57.656  37.173  36.503  1.00126.54           N  
ANISOU 5194  NZ  LYS D 150    17431  19097  11550   1568  -6480   3979       N  
ATOM   5195  N   HIS D 151      50.082  37.010  33.972  1.00 91.82           N  
ANISOU 5195  N   HIS D 151    15168  12950   6771   -269  -2753   2260       N  
ATOM   5196  CA  HIS D 151      48.702  37.334  34.317  1.00 84.98           C  
ANISOU 5196  CA  HIS D 151    14753  11922   5615   -707  -2262   1983       C  
ATOM   5197  C   HIS D 151      47.698  36.637  33.413  1.00 85.29           C  
ANISOU 5197  C   HIS D 151    14890  11521   5995   -822  -1579   1931       C  
ATOM   5198  O   HIS D 151      46.664  36.162  33.878  1.00 81.77           O  
ANISOU 5198  O   HIS D 151    14994  10774   5301   -997  -1149   2013       O  
ATOM   5199  CB  HIS D 151      48.479  38.846  34.298  1.00 81.73           C  
ANISOU 5199  CB  HIS D 151    13988  11807   5257  -1115  -2381   1523       C  
ATOM   5200  CG  HIS D 151      49.177  39.570  35.407  1.00 94.16           C  
ANISOU 5200  CG  HIS D 151    15664  13724   6387  -1105  -3061   1472       C  
ATOM   5201  ND1 HIS D 151      49.294  40.943  35.445  1.00 85.52           N  
ANISOU 5201  ND1 HIS D 151    14205  12873   5418  -1412  -3357   1065       N  
ATOM   5202  CD2 HIS D 151      49.791  39.108  36.521  1.00102.61           C  
ANISOU 5202  CD2 HIS D 151    17175  14922   6890   -819  -3541   1762       C  
ATOM   5203  CE1 HIS D 151      49.953  41.295  36.534  1.00103.99           C  
ANISOU 5203  CE1 HIS D 151    16711  15427   7372  -1298  -3972   1033       C  
ATOM   5204  NE2 HIS D 151      50.264  40.202  37.207  1.00106.07           N  
ANISOU 5204  NE2 HIS D 151    17404  15661   7237   -914  -4055   1439       N  
ATOM   5205  N   LEU D 152      47.993  36.594  32.117  1.00 81.87           N  
ANISOU 5205  N   LEU D 152    13911  11054   6141   -711  -1493   1811       N  
ATOM   5206  CA  LEU D 152      47.154  35.861  31.181  1.00 78.19           C  
ANISOU 5206  CA  LEU D 152    13546  10162   6001   -772   -965   1718       C  
ATOM   5207  C   LEU D 152      47.064  34.393  31.581  1.00 85.74           C  
ANISOU 5207  C   LEU D 152    15109  10635   6832   -504   -835   2092       C  
ATOM   5208  O   LEU D 152      45.977  33.815  31.616  1.00 79.27           O  
ANISOU 5208  O   LEU D 152    14695   9383   6041   -744   -406   2096       O  
ATOM   5209  CB  LEU D 152      47.706  35.970  29.761  1.00 71.11           C  
ANISOU 5209  CB  LEU D 152    12017   9363   5637   -529   -971   1564       C  
ATOM   5210  CG  LEU D 152      47.559  37.322  29.065  1.00 65.69           C  
ANISOU 5210  CG  LEU D 152    10670   9061   5230   -806   -926   1213       C  
ATOM   5211  CD1 LEU D 152      48.135  37.228  27.667  1.00 63.66           C  
ANISOU 5211  CD1 LEU D 152     9850   8897   5439   -425   -874   1172       C  
ATOM   5212  CD2 LEU D 152      46.102  37.749  29.019  1.00 62.56           C  
ANISOU 5212  CD2 LEU D 152    10448   8530   4792  -1359   -460    914       C  
ATOM   5213  N   LYS D 153      48.214  33.799  31.880  1.00 90.92           N  
ANISOU 5213  N   LYS D 153    15785  11350   7412     -6  -1203   2451       N  
ATOM   5214  CA  LYS D 153      48.277  32.388  32.239  1.00102.35           C  
ANISOU 5214  CA  LYS D 153    17763  12329   8795    324  -1088   2862       C  
ATOM   5215  C   LYS D 153      47.403  32.058  33.445  1.00 99.42           C  
ANISOU 5215  C   LYS D 153    18038  11754   7984     95   -862   3101       C  
ATOM   5216  O   LYS D 153      46.733  31.027  33.464  1.00 98.16           O  
ANISOU 5216  O   LYS D 153    18300  11032   7964     90   -490   3299       O  
ATOM   5217  CB  LYS D 153      49.724  31.964  32.501  1.00115.19           C  
ANISOU 5217  CB  LYS D 153    19248  14155  10365    911  -1548   3277       C  
ATOM   5218  CG  LYS D 153      50.529  31.689  31.237  1.00117.41           C  
ANISOU 5218  CG  LYS D 153    19059  14404  11148   1340  -1579   3242       C  
ATOM   5219  CD  LYS D 153      49.987  30.477  30.491  1.00118.39           C  
ANISOU 5219  CD  LYS D 153    19562  13850  11573   1501  -1142   3199       C  
ATOM   5220  CE  LYS D 153      50.920  30.045  29.370  1.00117.73           C  
ANISOU 5220  CE  LYS D 153    19150  13722  11860   2103  -1171   3235       C  
ATOM   5221  NZ  LYS D 153      50.473  28.773  28.734  1.00117.68           N  
ANISOU 5221  NZ  LYS D 153    19626  12983  12105   2321   -819   3164       N  
ATOM   5222  N   LYS D 154      47.398  32.945  34.436  1.00 93.17           N  
ANISOU 5222  N   LYS D 154    17323  11399   6679    -76  -1079   3086       N  
ATOM   5223  CA  LYS D 154      46.644  32.709  35.668  1.00102.77           C  
ANISOU 5223  CA  LYS D 154    19171  12518   7359   -182   -851   3367       C  
ATOM   5224  C   LYS D 154      45.144  32.923  35.466  1.00 93.68           C  
ANISOU 5224  C   LYS D 154    18168  11076   6348   -682   -244   3168       C  
ATOM   5225  O   LYS D 154      44.324  32.231  36.063  1.00 97.01           O  
ANISOU 5225  O   LYS D 154    19006  11154   6699   -723    163   3491       O  
ATOM   5226  CB  LYS D 154      47.160  33.607  36.794  1.00100.12           C  
ANISOU 5226  CB  LYS D 154    18936  12760   6346   -133  -1323   3364       C  
ATOM   5227  CG  LYS D 154      46.670  33.220  38.181  1.00106.27           C  
ANISOU 5227  CG  LYS D 154    20104  13578   6696     -8  -1108   3649       C  
ATOM   5228  CD  LYS D 154      47.243  31.877  38.613  1.00114.13           C  
ANISOU 5228  CD  LYS D 154    21338  14366   7660    463  -1157   4248       C  
ATOM   5229  CE  LYS D 154      46.978  31.601  40.093  1.00123.00           C  
ANISOU 5229  CE  LYS D 154    22750  15701   8285    646  -1055   4571       C  
ATOM   5230  NZ  LYS D 154      45.524  31.535  40.405  1.00119.40           N  
ANISOU 5230  NZ  LYS D 154    22493  14981   7892    375   -384   4582       N  
ATOM   5231  N   LEU D 155      44.791  33.886  34.621  1.00 87.38           N  
ANISOU 5231  N   LEU D 155    16907  10442   5850  -1039   -170   2668       N  
ATOM   5232  CA  LEU D 155      43.391  34.137  34.298  1.00 83.88           C  
ANISOU 5232  CA  LEU D 155    16496   9758   5618  -1521    388   2491       C  
ATOM   5233  C   LEU D 155      42.822  32.964  33.516  1.00 94.05           C  
ANISOU 5233  C   LEU D 155    17863  10405   7465  -1561    716   2601       C  
ATOM   5234  O   LEU D 155      41.710  32.506  33.781  1.00 96.70           O  
ANISOU 5234  O   LEU D 155    18474  10346   7923  -1815   1161   2803       O  
ATOM   5235  CB  LEU D 155      43.249  35.425  33.486  1.00 77.33           C  
ANISOU 5235  CB  LEU D 155    15087   9275   5021  -1842    367   1960       C  
ATOM   5236  CG  LEU D 155      41.886  35.683  32.837  1.00 77.75           C  
ANISOU 5236  CG  LEU D 155    15010   9105   5428  -2324    911   1759       C  
ATOM   5237  CD1 LEU D 155      40.793  35.826  33.882  1.00 75.48           C  
ANISOU 5237  CD1 LEU D 155    14808   8765   5106  -2401   1247   1847       C  
ATOM   5238  CD2 LEU D 155      41.954  36.925  31.937  1.00 72.63           C  
ANISOU 5238  CD2 LEU D 155    13711   8842   5043  -2542    850   1280       C  
ATOM   5239  N   ILE D 156      43.603  32.480  32.557  1.00 90.54           N  
ANISOU 5239  N   ILE D 156    17151   9850   7400  -1279    477   2470       N  
ATOM   5240  CA  ILE D 156      43.200  31.358  31.719  1.00 91.49           C  
ANISOU 5240  CA  ILE D 156    17382   9329   8052  -1260    686   2469       C  
ATOM   5241  C   ILE D 156      43.156  30.045  32.502  1.00 99.03           C  
ANISOU 5241  C   ILE D 156    18904   9747   8977  -1028    804   3018       C  
ATOM   5242  O   ILE D 156      42.282  29.207  32.275  1.00103.93           O  
ANISOU 5242  O   ILE D 156    19757   9726  10006  -1231   1116   3120       O  
ATOM   5243  CB  ILE D 156      44.109  31.242  30.483  1.00 86.84           C  
ANISOU 5243  CB  ILE D 156    16402   8801   7790   -912    421   2167       C  
ATOM   5244  CG1 ILE D 156      43.834  32.413  29.540  1.00 75.57           C  
ANISOU 5244  CG1 ILE D 156    14403   7781   6528  -1196    450   1664       C  
ATOM   5245  CG2 ILE D 156      43.888  29.924  29.758  1.00 85.21           C  
ANISOU 5245  CG2 ILE D 156    16463   7875   8037   -755    550   2164       C  
ATOM   5246  CD1 ILE D 156      44.540  32.305  28.246  1.00 86.61           C  
ANISOU 5246  CD1 ILE D 156    15426   9244   8239   -835    298   1394       C  
ATOM   5247  N   HIS D 157      44.088  29.874  33.433  1.00105.45           N  
ANISOU 5247  N   HIS D 157    19910  10814   9341   -611    536   3400       N  
ATOM   5248  CA  HIS D 157      44.058  28.724  34.337  1.00107.56           C  
ANISOU 5248  CA  HIS D 157    20706  10660   9502   -353    680   4017       C  
ATOM   5249  C   HIS D 157      42.773  28.734  35.162  1.00109.78           C  
ANISOU 5249  C   HIS D 157    21204  10797   9710   -714   1135   4249       C  
ATOM   5250  O   HIS D 157      42.169  27.688  35.402  1.00115.90           O  
ANISOU 5250  O   HIS D 157    22114  11042  10883   -714   1427   4571       O  
ATOM   5251  CB  HIS D 157      45.281  28.727  35.257  1.00108.23           C  
ANISOU 5251  CB  HIS D 157    20893  11203   9028    157    267   4384       C  
ATOM   5252  CG  HIS D 157      45.283  27.622  36.267  1.00117.62           C  
ANISOU 5252  CG  HIS D 157    22505  12095  10089    468    422   5035       C  
ATOM   5253  ND1 HIS D 157      44.854  27.799  37.565  1.00125.70           N  
ANISOU 5253  ND1 HIS D 157    23580  13462  10717    436    546   5279       N  
ATOM   5254  CD2 HIS D 157      45.663  26.325  36.171  1.00122.42           C  
ANISOU 5254  CD2 HIS D 157    23303  12171  11041    840    484   5419       C  
ATOM   5255  CE1 HIS D 157      44.970  26.660  38.226  1.00128.43           C  
ANISOU 5255  CE1 HIS D 157    24119  13531  11146    752    673   5830       C  
ATOM   5256  NE2 HIS D 157      45.458  25.750  37.402  1.00128.77           N  
ANISOU 5256  NE2 HIS D 157    24234  13028  11664    981    640   5919       N  
ATOM   5257  N   ASP D 158      42.360  29.924  35.590  1.00108.14           N  
ANISOU 5257  N   ASP D 158    20765  11152   9172   -970   1164   3991       N  
ATOM   5258  CA  ASP D 158      41.115  30.084  36.337  1.00109.01           C  
ANISOU 5258  CA  ASP D 158    20770  11297   9351  -1212   1578   4087       C  
ATOM   5259  C   ASP D 158      39.917  29.945  35.405  1.00107.99           C  
ANISOU 5259  C   ASP D 158    20362  10736   9933  -1671   1917   3851       C  
ATOM   5260  O   ASP D 158      38.830  29.551  35.832  1.00111.59           O  
ANISOU 5260  O   ASP D 158    20695  10991  10714  -1812   2255   4088       O  
ATOM   5261  CB  ASP D 158      41.081  31.438  37.046  1.00104.13           C  
ANISOU 5261  CB  ASP D 158    19999  11371   8196  -1259   1485   3833       C  
ATOM   5262  CG  ASP D 158      42.102  31.539  38.164  1.00111.26           C  
ANISOU 5262  CG  ASP D 158    21142  12728   8404   -819   1108   4064       C  
ATOM   5263  OD1 ASP D 158      42.902  30.593  38.339  1.00115.19           O  
ANISOU 5263  OD1 ASP D 158    21861  13065   8840   -459    909   4443       O  
ATOM   5264  OD2 ASP D 158      42.109  32.574  38.862  1.00105.76           O  
ANISOU 5264  OD2 ASP D 158    20388  12544   7252   -816    987   3848       O  
ATOM   5265  N   PHE D 159      40.126  30.278  34.133  1.00 98.73           N  
ANISOU 5265  N   PHE D 159    19033   9474   9006  -1879   1782   3407       N  
ATOM   5266  CA  PHE D 159      39.137  30.033  33.090  1.00102.34           C  
ANISOU 5266  CA  PHE D 159    19209   9521  10153  -2270   1981   3130       C  
ATOM   5267  C   PHE D 159      39.004  28.529  32.864  1.00108.40           C  
ANISOU 5267  C   PHE D 159    20230   9513  11445  -2176   2031   3409       C  
ATOM   5268  O   PHE D 159      37.912  27.966  32.949  1.00110.50           O  
ANISOU 5268  O   PHE D 159    20292   9454  12239  -2394   2250   3548       O  
ATOM   5269  CB  PHE D 159      39.560  30.707  31.785  1.00103.52           C  
ANISOU 5269  CB  PHE D 159    19173   9798  10363  -2433   1796   2614       C  
ATOM   5270  CG  PHE D 159      38.762  31.935  31.438  1.00105.39           C  
ANISOU 5270  CG  PHE D 159    18840  10510  10693  -2783   1921   2194       C  
ATOM   5271  CD1 PHE D 159      37.406  32.002  31.715  1.00108.75           C  
ANISOU 5271  CD1 PHE D 159    18912  10932  11474  -2982   2183   2212       C  
ATOM   5272  CD2 PHE D 159      39.370  33.020  30.823  1.00100.84           C  
ANISOU 5272  CD2 PHE D 159    18014  10404   9895  -2841   1757   1836       C  
ATOM   5273  CE1 PHE D 159      36.675  33.130  31.388  1.00103.76           C  
ANISOU 5273  CE1 PHE D 159    17733  10732  10961  -3163   2254   1862       C  
ATOM   5274  CE2 PHE D 159      38.644  34.151  30.495  1.00 95.48           C  
ANISOU 5274  CE2 PHE D 159    16754  10143   9382  -3079   1864   1457       C  
ATOM   5275  CZ  PHE D 159      37.295  34.205  30.777  1.00 95.18           C  
ANISOU 5275  CZ  PHE D 159    16416  10068   9681  -3200   2096   1462       C  
TER    5276      PHE D 159                                                      
ATOM   5277  N   SER E  -1       2.663  89.514   5.437  1.00 67.98           N  
ANISOU 5277  N   SER E  -1     8372   6554  10903   1753  -1278  -1125       N  
ATOM   5278  CA  SER E  -1       2.735  90.648   4.514  1.00 79.26           C  
ANISOU 5278  CA  SER E  -1    10286   7567  12264   1881  -1458   -940       C  
ATOM   5279  C   SER E  -1       3.759  90.437   3.385  1.00 74.54           C  
ANISOU 5279  C   SER E  -1     9989   6741  11591   1570  -1474   -598       C  
ATOM   5280  O   SER E  -1       4.864  91.001   3.413  1.00 67.11           O  
ANISOU 5280  O   SER E  -1     9392   5500  10608   1275  -1411   -466       O  
ATOM   5281  CB  SER E  -1       3.039  91.940   5.285  1.00 81.96           C  
ANISOU 5281  CB  SER E  -1    10962   7564  12617   1926  -1448  -1060       C  
ATOM   5282  OG  SER E  -1       3.168  93.053   4.415  1.00 91.02           O  
ANISOU 5282  OG  SER E  -1    12613   8280  13692   1997  -1607   -864       O  
ATOM   5283  N   GLY E   0       3.389  89.641   2.385  1.00 62.37           N  
ANISOU 5283  N   GLY E   0     8318   5380   9999   1603  -1554   -458       N  
ATOM   5284  CA  GLY E   0       4.268  89.429   1.245  1.00 62.91           C  
ANISOU 5284  CA  GLY E   0     8667   5282   9955   1328  -1566   -142       C  
ATOM   5285  C   GLY E   0       4.264  88.080   0.534  1.00 62.31           C  
ANISOU 5285  C   GLY E   0     8359   5486   9829   1210  -1530    -37       C  
ATOM   5286  O   GLY E   0       3.781  87.975  -0.595  1.00 80.70           O  
ANISOU 5286  O   GLY E   0    10785   7826  12053   1322  -1705    104       O  
ATOM   5287  N   LEU E   1       4.812  87.054   1.175  1.00 59.62           N  
ANISOU 5287  N   LEU E   1     7731   5445   9478    945  -1266    -99       N  
ATOM   5288  CA  LEU E   1       5.175  85.821   0.476  1.00 53.15           C  
ANISOU 5288  CA  LEU E   1     6808   4876   8509    729  -1139     28       C  
ATOM   5289  C   LEU E   1       3.995  84.959   0.033  1.00 48.99           C  
ANISOU 5289  C   LEU E   1     6037   4635   7943    880  -1248    -56       C  
ATOM   5290  O   LEU E   1       3.010  84.822   0.770  1.00 46.76           O  
ANISOU 5290  O   LEU E   1     5448   4558   7762   1053  -1295   -273       O  
ATOM   5291  CB  LEU E   1       6.092  84.961   1.348  1.00 44.49           C  
ANISOU 5291  CB  LEU E   1     5511   3982   7413    462   -856    -15       C  
ATOM   5292  CG  LEU E   1       7.327  85.644   1.934  1.00 51.80           C  
ANISOU 5292  CG  LEU E   1     6577   4754   8352    243   -726     46       C  
ATOM   5293  CD1 LEU E   1       8.008  84.710   2.903  1.00 45.14           C  
ANISOU 5293  CD1 LEU E   1     5458   4182   7510     65   -494    -19       C  
ATOM   5294  CD2 LEU E   1       8.275  86.067   0.842  1.00 43.77           C  
ANISOU 5294  CD2 LEU E   1     5876   3581   7173     41   -718    303       C  
ATOM   5295  N   ASN E   2       4.107  84.390  -1.168  1.00 40.00           N  
ANISOU 5295  N   ASN E   2     5026   3545   6628    782  -1280    105       N  
ATOM   5296  CA  ASN E   2       3.325  83.206  -1.529  1.00 34.86           C  
ANISOU 5296  CA  ASN E   2     4156   3202   5885    755  -1304     28       C  
ATOM   5297  C   ASN E   2       4.124  81.992  -1.140  1.00 34.68           C  
ANISOU 5297  C   ASN E   2     4060   3306   5809    488  -1034     12       C  
ATOM   5298  O   ASN E   2       5.292  81.842  -1.543  1.00 30.46           O  
ANISOU 5298  O   ASN E   2     3720   2675   5177    337   -881    152       O  
ATOM   5299  CB  ASN E   2       3.026  83.124  -3.028  1.00 42.69           C  
ANISOU 5299  CB  ASN E   2     5354   4189   6678    772  -1482    183       C  
ATOM   5300  CG  ASN E   2       2.002  84.118  -3.468  1.00 59.74           C  
ANISOU 5300  CG  ASN E   2     7549   6284   8866   1094  -1809    200       C  
ATOM   5301  OD1 ASN E   2       0.838  84.054  -3.066  1.00 73.02           O  
ANISOU 5301  OD1 ASN E   2     8912   8205  10628   1300  -1949     22       O  
ATOM   5302  ND2 ASN E   2       2.414  85.039  -4.323  1.00 54.83           N  
ANISOU 5302  ND2 ASN E   2     7313   5366   8155   1144  -1944    422       N  
ATOM   5303  N   ILE E   3       3.497  81.102  -0.383  1.00 28.52           N  
ANISOU 5303  N   ILE E   3     3004   2763   5069    432   -981   -154       N  
ATOM   5304  CA  ILE E   3       4.193  79.920   0.085  1.00 27.24           C  
ANISOU 5304  CA  ILE E   3     2822   2669   4858    218   -759   -164       C  
ATOM   5305  C   ILE E   3       3.326  78.723  -0.228  1.00 31.36           C  
ANISOU 5305  C   ILE E   3     3272   3382   5262     96   -811   -245       C  
ATOM   5306  O   ILE E   3       2.119  78.751   0.020  1.00 28.24           O  
ANISOU 5306  O   ILE E   3     2639   3199   4892    123   -949   -372       O  
ATOM   5307  CB  ILE E   3       4.402  79.968   1.601  1.00 30.62           C  
ANISOU 5307  CB  ILE E   3     3044   3161   5428    180   -627   -270       C  
ATOM   5308  CG1 ILE E   3       5.180  81.224   2.001  1.00 37.26           C  
ANISOU 5308  CG1 ILE E   3     3966   3815   6376    254   -596   -223       C  
ATOM   5309  CG2 ILE E   3       5.124  78.721   2.060  1.00 28.70           C  
ANISOU 5309  CG2 ILE E   3     2820   2965   5119     -2   -437   -246       C  
ATOM   5310  CD1 ILE E   3       5.133  81.502   3.496  1.00 36.49           C  
ANISOU 5310  CD1 ILE E   3     3656   3803   6404    243   -516   -373       C  
ATOM   5311  N   LYS E   4       3.923  77.710  -0.847  1.00 26.27           N  
ANISOU 5311  N   LYS E   4     2841   2676   4466    -37   -710   -184       N  
ATOM   5312  CA  LYS E   4       3.216  76.469  -1.096  1.00 27.06           C  
ANISOU 5312  CA  LYS E   4     2964   2888   4429   -219   -749   -269       C  
ATOM   5313  C   LYS E   4       4.010  75.354  -0.407  1.00 27.84           C  
ANISOU 5313  C   LYS E   4     3178   2894   4508   -344   -547   -272       C  
ATOM   5314  O   LYS E   4       5.218  75.249  -0.584  1.00 30.43           O  
ANISOU 5314  O   LYS E   4     3675   3076   4812   -261   -398   -186       O  
ATOM   5315  CB  LYS E   4       3.124  76.224  -2.602  1.00 35.86           C  
ANISOU 5315  CB  LYS E   4     4325   3963   5337   -235   -850   -216       C  
ATOM   5316  CG  LYS E   4       2.408  74.931  -2.997  1.00 47.70           C  
ANISOU 5316  CG  LYS E   4     5923   5546   6655   -474   -909   -318       C  
ATOM   5317  CD  LYS E   4       2.180  74.895  -4.503  1.00 64.06           C  
ANISOU 5317  CD  LYS E   4     8210   7626   8503   -486  -1047   -285       C  
ATOM   5318  CE  LYS E   4       3.166  73.974  -5.204  1.00 76.52           C  
ANISOU 5318  CE  LYS E   4    10174   9005   9895   -533   -881   -280       C  
ATOM   5319  NZ  LYS E   4       2.638  72.575  -5.327  1.00 71.39           N  
ANISOU 5319  NZ  LYS E   4     9716   8330   9080   -797   -905   -419       N  
ATOM   5320  N   GLU E   5       3.329  74.532   0.382  1.00 29.70           N  
ANISOU 5320  N   GLU E   5     3317   3236   4733   -542   -551   -364       N  
ATOM   5321  CA  GLU E   5       3.966  73.419   1.069  1.00 28.56           C  
ANISOU 5321  CA  GLU E   5     3341   2961   4550   -656   -406   -346       C  
ATOM   5322  C   GLU E   5       3.457  72.122   0.472  1.00 33.00           C  
ANISOU 5322  C   GLU E   5     4181   3442   4914   -885   -464   -398       C  
ATOM   5323  O   GLU E   5       2.259  71.962   0.236  1.00 29.49           O  
ANISOU 5323  O   GLU E   5     3632   3182   4389  -1102   -610   -483       O  
ATOM   5324  CB  GLU E   5       3.649  73.470   2.583  1.00 28.98           C  
ANISOU 5324  CB  GLU E   5     3136   3166   4708   -770   -362   -385       C  
ATOM   5325  CG  GLU E   5       4.127  72.240   3.325  1.00 32.47           C  
ANISOU 5325  CG  GLU E   5     3791   3469   5077   -920   -263   -339       C  
ATOM   5326  CD  GLU E   5       3.829  72.279   4.826  1.00 41.76           C  
ANISOU 5326  CD  GLU E   5     4732   4826   6309  -1075   -219   -358       C  
ATOM   5327  OE1 GLU E   5       4.324  71.374   5.531  1.00 37.15           O  
ANISOU 5327  OE1 GLU E   5     4341   4112   5662  -1173   -154   -279       O  
ATOM   5328  OE2 GLU E   5       3.116  73.204   5.298  1.00 43.52           O  
ANISOU 5328  OE2 GLU E   5     4598   5318   6618  -1075   -254   -454       O  
ATOM   5329  N   ASN E   6       4.375  71.187   0.197  1.00 27.70           N  
ANISOU 5329  N   ASN E   6     3874   2505   4148   -830   -357   -362       N  
ATOM   5330  CA  ASN E   6       4.010  69.857  -0.286  1.00 30.02           C  
ANISOU 5330  CA  ASN E   6     4547   2619   4241  -1048   -405   -429       C  
ATOM   5331  C   ASN E   6       4.663  68.794   0.572  1.00 30.48           C  
ANISOU 5331  C   ASN E   6     4879   2422   4282  -1060   -306   -387       C  
ATOM   5332  O   ASN E   6       5.730  69.021   1.140  1.00 31.78           O  
ANISOU 5332  O   ASN E   6     4986   2535   4554   -795   -180   -301       O  
ATOM   5333  CB  ASN E   6       4.497  69.680  -1.722  1.00 36.65           C  
ANISOU 5333  CB  ASN E   6     5684   3316   4925   -895   -394   -460       C  
ATOM   5334  CG  ASN E   6       3.597  70.367  -2.724  1.00 43.70           C  
ANISOU 5334  CG  ASN E   6     6436   4425   5742   -978   -559   -497       C  
ATOM   5335  OD1 ASN E   6       3.762  71.547  -3.022  1.00 49.38           O  
ANISOU 5335  OD1 ASN E   6     6927   5283   6552   -788   -577   -428       O  
ATOM   5336  ND2 ASN E   6       2.632  69.622  -3.251  1.00 45.19           N  
ANISOU 5336  ND2 ASN E   6     6788   4637   5744  -1284   -703   -599       N  
ATOM   5337  N   ASP E   7       4.006  67.654   0.716  1.00 33.97           N  
ANISOU 5337  N   ASP E   7     5620   2713   4573  -1390   -382   -434       N  
ATOM   5338  CA  ASP E   7       4.609  66.546   1.450  1.00 49.76           C  
ANISOU 5338  CA  ASP E   7     8000   4382   6525  -1390   -326   -371       C  
ATOM   5339  C   ASP E   7       5.626  65.809   0.589  1.00 44.74           C  
ANISOU 5339  C   ASP E   7     7837   3378   5784  -1061   -257   -408       C  
ATOM   5340  O   ASP E   7       5.428  65.660  -0.612  1.00 41.52           O  
ANISOU 5340  O   ASP E   7     7624   2912   5241  -1068   -292   -521       O  
ATOM   5341  CB  ASP E   7       3.551  65.539   1.904  1.00 52.75           C  
ANISOU 5341  CB  ASP E   7     8594   4704   6743  -1891   -436   -388       C  
ATOM   5342  CG  ASP E   7       4.158  64.386   2.678  1.00 52.08           C  
ANISOU 5342  CG  ASP E   7     8883   4315   6590  -1811   -395   -278       C  
ATOM   5343  OD1 ASP E   7       4.694  64.637   3.783  1.00 58.32           O  
ANISOU 5343  OD1 ASP E   7     9539   5123   7497  -1715   -339   -161       O  
ATOM   5344  OD2 ASP E   7       4.123  63.238   2.175  1.00 63.57           O  
ANISOU 5344  OD2 ASP E   7    10782   5509   7864  -1839   -435   -306       O  
ATOM   5345  N   LEU E   8       6.715  65.354   1.208  1.00 41.94           N  
ANISOU 5345  N   LEU E   8     7651   2812   5474   -751   -164   -323       N  
ATOM   5346  CA  LEU E   8       7.668  64.467   0.540  1.00 39.78           C  
ANISOU 5346  CA  LEU E   8     7853   2179   5080   -386   -100   -384       C  
ATOM   5347  C   LEU E   8       7.752  63.158   1.333  1.00 52.45           C  
ANISOU 5347  C   LEU E   8     9774   3551   6603   -416   -157   -305       C  
ATOM   5348  O   LEU E   8       8.466  63.091   2.332  1.00 53.66           O  
ANISOU 5348  O   LEU E   8     9867   3673   6847   -209   -125   -174       O  
ATOM   5349  CB  LEU E   8       9.039  65.130   0.498  1.00 39.87           C  
ANISOU 5349  CB  LEU E   8     7574   2374   5201    136     65   -333       C  
ATOM   5350  CG  LEU E   8       9.129  66.471  -0.232  1.00 41.24           C  
ANISOU 5350  CG  LEU E   8     7296   2933   5441    188    134   -347       C  
ATOM   5351  CD1 LEU E   8      10.455  67.130   0.094  1.00 41.57           C  
ANISOU 5351  CD1 LEU E   8     7007   3200   5586    568    288   -256       C  
ATOM   5352  CD2 LEU E   8       8.998  66.262  -1.721  1.00 44.17           C  
ANISOU 5352  CD2 LEU E   8     7925   3235   5623    218    142   -497       C  
ATOM   5353  N   PRO E   9       7.007  62.129   0.900  1.00 61.34           N  
ANISOU 5353  N   PRO E   9    11253   4517   7538   -691   -255   -373       N  
ATOM   5354  CA  PRO E   9       6.913  60.797   1.524  1.00 67.86           C  
ANISOU 5354  CA  PRO E   9    12480   5073   8231   -795   -336   -302       C  
ATOM   5355  C   PRO E   9       8.236  60.288   2.094  1.00 75.71           C  
ANISOU 5355  C   PRO E   9    13634   5859   9272   -289   -287   -216       C  
ATOM   5356  O   PRO E   9       9.216  60.177   1.346  1.00 68.86           O  
ANISOU 5356  O   PRO E   9    12850   4920   8395    186   -200   -307       O  
ATOM   5357  CB  PRO E   9       6.500  59.894   0.359  1.00 64.32           C  
ANISOU 5357  CB  PRO E   9    12458   4422   7559   -902   -390   -449       C  
ATOM   5358  CG  PRO E   9       6.325  60.807  -0.852  1.00 68.35           C  
ANISOU 5358  CG  PRO E   9    12750   5140   8081   -877   -342   -593       C  
ATOM   5359  CD  PRO E   9       6.197  62.194  -0.324  1.00 57.10           C  
ANISOU 5359  CD  PRO E   9    10785   4044   6866   -930   -307   -523       C  
ATOM   5360  N   GLY E  10       8.256  59.996   3.395  1.00 68.79           N  
ANISOU 5360  N   GLY E  10    12771   4940   8425   -389   -343    -46       N  
ATOM   5361  CA  GLY E  10       9.434  59.457   4.055  1.00 63.02           C  
ANISOU 5361  CA  GLY E  10    12188   4034   7721     68   -339     61       C  
ATOM   5362  C   GLY E  10      10.675  60.323   3.955  1.00 77.88           C  
ANISOU 5362  C   GLY E  10    13697   6125   9770    610   -208     64       C  
ATOM   5363  O   GLY E  10      11.796  59.847   4.144  1.00 85.66           O  
ANISOU 5363  O   GLY E  10    14760   7034  10753   1095   -192    100       O  
ATOM   5364  N   ILE E  11      10.477  61.604   3.662  1.00 67.54           N  
ANISOU 5364  N   ILE E  11    11964   5111   8587    525   -119     27       N  
ATOM   5365  CA  ILE E  11      11.581  62.537   3.532  1.00 57.07           C  
ANISOU 5365  CA  ILE E  11    10255   4042   7389    975     18     35       C  
ATOM   5366  C   ILE E  11      11.339  63.740   4.438  1.00 49.25           C  
ANISOU 5366  C   ILE E  11     8861   3292   6561    778     41    161       C  
ATOM   5367  O   ILE E  11      12.152  64.074   5.303  1.00 49.24           O  
ANISOU 5367  O   ILE E  11     8573   3497   6640   1005     70    293       O  
ATOM   5368  CB  ILE E  11      11.749  62.959   2.053  1.00 66.98           C  
ANISOU 5368  CB  ILE E  11    11452   5401   8595   1134    133   -153       C  
ATOM   5369  CG1 ILE E  11      12.275  61.769   1.240  1.00 82.30           C  
ANISOU 5369  CG1 ILE E  11    13781   7126  10363   1434    137   -282       C  
ATOM   5370  CG2 ILE E  11      12.657  64.169   1.923  1.00 60.25           C  
ANISOU 5370  CG2 ILE E  11    10126   4908   7856   1453    295   -131       C  
ATOM   5371  CD1 ILE E  11      11.953  61.815  -0.243  1.00 83.81           C  
ANISOU 5371  CD1 ILE E  11    14115   7308  10420   1388    194   -481       C  
ATOM   5372  N   GLY E  12      10.191  64.378   4.269  1.00 41.63           N  
ANISOU 5372  N   GLY E  12     7698   2491   5626    302     12    107       N  
ATOM   5373  CA  GLY E  12       9.896  65.575   5.034  1.00 35.86           C  
ANISOU 5373  CA  GLY E  12     6394   2188   5043     87     37    172       C  
ATOM   5374  C   GLY E  12       8.874  66.419   4.295  1.00 36.07           C  
ANISOU 5374  C   GLY E  12     6176   2425   5103   -210     27     50       C  
ATOM   5375  O   GLY E  12       7.824  65.917   3.891  1.00 39.67           O  
ANISOU 5375  O   GLY E  12     6869   2749   5455   -544    -66    -28       O  
ATOM   5376  N   LYS E  13       9.196  67.692   4.101  1.00 35.36           N  
ANISOU 5376  N   LYS E  13     5634   2661   5141    -91    104     40       N  
ATOM   5377  CA  LYS E  13       8.295  68.644   3.461  1.00 30.66           C  
ANISOU 5377  CA  LYS E  13     4791   2269   4591   -293     68    -50       C  
ATOM   5378  C   LYS E  13       9.070  69.592   2.567  1.00 31.48           C  
ANISOU 5378  C   LYS E  13     4707   2518   4738    -27    159    -59       C  
ATOM   5379  O   LYS E  13      10.213  69.938   2.853  1.00 31.08           O  
ANISOU 5379  O   LYS E  13     4500   2572   4735    219    264     13       O  
ATOM   5380  CB  LYS E  13       7.599  69.502   4.526  1.00 29.91           C  
ANISOU 5380  CB  LYS E  13     4299   2448   4617   -529     33    -35       C  
ATOM   5381  CG  LYS E  13       6.665  68.731   5.471  1.00 36.48           C  
ANISOU 5381  CG  LYS E  13     5230   3257   5373   -897    -44    -25       C  
ATOM   5382  CD  LYS E  13       5.474  68.120   4.738  1.00 46.05           C  
ANISOU 5382  CD  LYS E  13     6646   4401   6449  -1218   -153   -124       C  
ATOM   5383  CE  LYS E  13       4.373  67.675   5.719  1.00 57.40           C  
ANISOU 5383  CE  LYS E  13     8031   5981   7799  -1690   -218   -124       C  
ATOM   5384  NZ  LYS E  13       3.079  67.322   5.022  1.00 64.46           N  
ANISOU 5384  NZ  LYS E  13     8973   6965   8553  -2072   -332   -239       N  
ATOM   5385  N   LYS E  14       8.399  70.065   1.526  1.00 29.46           N  
ANISOU 5385  N   LYS E  14     4440   2311   4442   -124    103   -133       N  
ATOM   5386  CA  LYS E  14       8.949  71.022   0.593  1.00 25.84           C  
ANISOU 5386  CA  LYS E  14     3850   1985   3983     37    164   -120       C  
ATOM   5387  C   LYS E  14       8.118  72.312   0.677  1.00 27.95           C  
ANISOU 5387  C   LYS E  14     3817   2433   4370   -113     64   -115       C  
ATOM   5388  O   LYS E  14       6.897  72.251   0.634  1.00 29.29           O  
ANISOU 5388  O   LYS E  14     3966   2631   4531   -312    -73   -183       O  
ATOM   5389  CB  LYS E  14       8.833  70.447  -0.819  1.00 29.06           C  
ANISOU 5389  CB  LYS E  14     4578   2269   4194     74    154   -205       C  
ATOM   5390  CG  LYS E  14       9.381  71.404  -1.883  1.00 34.68           C  
ANISOU 5390  CG  LYS E  14     5193   3139   4846    192    218   -172       C  
ATOM   5391  CD  LYS E  14       9.529  70.722  -3.219  1.00 45.25           C  
ANISOU 5391  CD  LYS E  14     6863   4387   5944    268    253   -268       C  
ATOM   5392  CE  LYS E  14       8.224  70.672  -3.993  1.00 55.68           C  
ANISOU 5392  CE  LYS E  14     8323   5672   7160     17     65   -339       C  
ATOM   5393  NZ  LYS E  14       8.436  70.068  -5.339  1.00 67.37           N  
ANISOU 5393  NZ  LYS E  14    10144   7085   8368     76    106   -447       N  
ATOM   5394  N   PHE E  15       8.791  73.446   0.852  1.00 24.44           N  
ANISOU 5394  N   PHE E  15     3146   2114   4023    -17    124    -42       N  
ATOM   5395  CA  PHE E  15       8.178  74.760   0.815  1.00 26.59           C  
ANISOU 5395  CA  PHE E  15     3222   2480   4401    -79     24    -37       C  
ATOM   5396  C   PHE E  15       8.703  75.517  -0.386  1.00 33.67           C  
ANISOU 5396  C   PHE E  15     4202   3379   5212     -2     40     37       C  
ATOM   5397  O   PHE E  15       9.913  75.744  -0.498  1.00 32.27           O  
ANISOU 5397  O   PHE E  15     4009   3256   4994     73    184    116       O  
ATOM   5398  CB  PHE E  15       8.513  75.550   2.101  1.00 25.17           C  
ANISOU 5398  CB  PHE E  15     2786   2392   4386    -89     65    -14       C  
ATOM   5399  CG  PHE E  15       7.916  74.925   3.376  1.00 28.14           C  
ANISOU 5399  CG  PHE E  15     3058   2818   4817   -208     48    -79       C  
ATOM   5400  CD1 PHE E  15       8.539  73.848   3.996  1.00 30.26           C  
ANISOU 5400  CD1 PHE E  15     3425   3042   5031   -198    131    -35       C  
ATOM   5401  CD2 PHE E  15       6.738  75.416   3.927  1.00 22.05           C  
ANISOU 5401  CD2 PHE E  15     2097   2158   4125   -315    -55   -180       C  
ATOM   5402  CE1 PHE E  15       8.000  73.257   5.155  1.00 28.86           C  
ANISOU 5402  CE1 PHE E  15     3201   2905   4859   -358    107    -59       C  
ATOM   5403  CE2 PHE E  15       6.163  74.814   5.090  1.00 27.71           C  
ANISOU 5403  CE2 PHE E  15     2704   2985   4840   -484    -50   -239       C  
ATOM   5404  CZ  PHE E  15       6.816  73.730   5.700  1.00 30.97           C  
ANISOU 5404  CZ  PHE E  15     3263   3325   5180   -536     30   -160       C  
ATOM   5405  N   GLU E  16       7.807  75.910  -1.281  1.00 27.39           N  
ANISOU 5405  N   GLU E  16     3479   2567   4361    -41   -113     23       N  
ATOM   5406  CA  GLU E  16       8.182  76.813  -2.378  1.00 29.10           C  
ANISOU 5406  CA  GLU E  16     3798   2778   4479     -9   -136    129       C  
ATOM   5407  C   GLU E  16       7.718  78.206  -2.018  1.00 33.00           C  
ANISOU 5407  C   GLU E  16     4171   3242   5127     -1   -273    174       C  
ATOM   5408  O   GLU E  16       6.546  78.423  -1.704  1.00 27.81           O  
ANISOU 5408  O   GLU E  16     3403   2600   4565     21   -442     92       O  
ATOM   5409  CB  GLU E  16       7.585  76.355  -3.690  1.00 30.45           C  
ANISOU 5409  CB  GLU E  16     4184   2940   4447    -35   -239    104       C  
ATOM   5410  CG  GLU E  16       8.085  74.969  -4.105  1.00 45.65           C  
ANISOU 5410  CG  GLU E  16     6311   4838   6198    -17    -99     22       C  
ATOM   5411  CD  GLU E  16       7.997  74.746  -5.607  1.00 71.31           C  
ANISOU 5411  CD  GLU E  16     9815   8101   9178    -39   -134     14       C  
ATOM   5412  OE1 GLU E  16       7.422  75.616  -6.301  1.00 76.43           O  
ANISOU 5412  OE1 GLU E  16    10475   8790   9773    -89   -301     95       O  
ATOM   5413  OE2 GLU E  16       8.515  73.714  -6.088  1.00 73.92           O  
ANISOU 5413  OE2 GLU E  16    10355   8396   9333     16     -4    -78       O  
ATOM   5414  N   ILE E  17       8.654  79.141  -2.022  1.00 32.39           N  
ANISOU 5414  N   ILE E  17     4113   3134   5059    -22   -198    292       N  
ATOM   5415  CA  ILE E  17       8.405  80.495  -1.555  1.00 29.06           C  
ANISOU 5415  CA  ILE E  17     3658   2602   4784    -14   -315    327       C  
ATOM   5416  C   ILE E  17       8.642  81.545  -2.663  1.00 29.12           C  
ANISOU 5416  C   ILE E  17     3916   2481   4665    -56   -411    500       C  
ATOM   5417  O   ILE E  17       9.681  81.552  -3.294  1.00 31.02           O  
ANISOU 5417  O   ILE E  17     4264   2784   4736   -182   -270    622       O  
ATOM   5418  CB  ILE E  17       9.343  80.791  -0.362  1.00 34.19           C  
ANISOU 5418  CB  ILE E  17     4156   3288   5546    -89   -162    321       C  
ATOM   5419  CG1 ILE E  17       9.040  79.823   0.801  1.00 31.48           C  
ANISOU 5419  CG1 ILE E  17     3599   3058   5305    -59    -99    180       C  
ATOM   5420  CG2 ILE E  17       9.216  82.237   0.098  1.00 36.62           C  
ANISOU 5420  CG2 ILE E  17     4511   3426   5978   -108   -273    338       C  
ATOM   5421  CD1 ILE E  17      10.197  79.673   1.782  1.00 36.15           C  
ANISOU 5421  CD1 ILE E  17     4049   3762   5924   -128     74    202       C  
ATOM   5422  N   GLU E  18       7.704  82.453  -2.872  1.00 29.37           N  
ANISOU 5422  N   GLU E  18     4042   2354   4764     53   -651    516       N  
ATOM   5423  CA  GLU E  18       7.920  83.497  -3.867  1.00 36.37           C  
ANISOU 5423  CA  GLU E  18     5238   3060   5519      3   -775    716       C  
ATOM   5424  C   GLU E  18       7.686  84.852  -3.214  1.00 35.87           C  
ANISOU 5424  C   GLU E  18     5278   2723   5630     78   -925    727       C  
ATOM   5425  O   GLU E  18       6.656  85.075  -2.586  1.00 40.89           O  
ANISOU 5425  O   GLU E  18     5780   3312   6443    313  -1077    572       O  
ATOM   5426  CB  GLU E  18       6.970  83.291  -5.055  1.00 42.64           C  
ANISOU 5426  CB  GLU E  18     6163   3875   6162    112   -988    761       C  
ATOM   5427  CG  GLU E  18       7.366  84.050  -6.316  1.00 58.54           C  
ANISOU 5427  CG  GLU E  18     8540   5764   7937      1  -1081   1011       C  
ATOM   5428  CD  GLU E  18       6.176  84.407  -7.189  1.00 68.05           C  
ANISOU 5428  CD  GLU E  18     9894   6899   9063    190  -1417   1076       C  
ATOM   5429  OE1 GLU E  18       5.191  83.635  -7.220  1.00 63.62           O  
ANISOU 5429  OE1 GLU E  18     9126   6522   8525    327  -1517    923       O  
ATOM   5430  OE2 GLU E  18       6.222  85.472  -7.841  1.00 77.45           O  
ANISOU 5430  OE2 GLU E  18    11419   7859  10150    182  -1598   1293       O  
ATOM   5431  N   THR E  19       8.660  85.746  -3.324  1.00 43.59           N  
ANISOU 5431  N   THR E  19     4385   3757   8422   -340     12   2108       N  
ATOM   5432  CA  THR E  19       8.551  87.065  -2.733  1.00 48.37           C  
ANISOU 5432  CA  THR E  19     4787   4109   9483   -288      2   2054       C  
ATOM   5433  C   THR E  19       7.731  87.985  -3.632  1.00 62.75           C  
ANISOU 5433  C   THR E  19     6524   5868  11450   -321   -103   2334       C  
ATOM   5434  O   THR E  19       7.391  87.638  -4.767  1.00 62.15           O  
ANISOU 5434  O   THR E  19     6544   5965  11104   -400   -163   2575       O  
ATOM   5435  CB  THR E  19       9.939  87.711  -2.552  1.00 49.03           C  
ANISOU 5435  CB  THR E  19     4804   4059   9766   -349     82   1975       C  
ATOM   5436  OG1 THR E  19      10.526  87.909  -3.841  1.00 57.25           O  
ANISOU 5436  OG1 THR E  19     5906   5191  10655   -489     79   2254       O  
ATOM   5437  CG2 THR E  19      10.842  86.823  -1.715  1.00 46.51           C  
ANISOU 5437  CG2 THR E  19     4538   3809   9325   -328    188   1715       C  
ATOM   5438  N   ARG E  20       7.425  89.167  -3.119  1.00 74.91           N  
ANISOU 5438  N   ARG E  20     7869   7151  13441   -265   -126   2295       N  
ATOM   5439  CA  ARG E  20       6.633  90.137  -3.864  1.00 92.45           C  
ANISOU 5439  CA  ARG E  20     9970   9269  15889   -283   -227   2569       C  
ATOM   5440  C   ARG E  20       7.269  90.497  -5.210  1.00 89.16           C  
ANISOU 5440  C   ARG E  20     9593   8921  15363   -425   -258   2896       C  
ATOM   5441  O   ARG E  20       6.569  90.663  -6.211  1.00 88.17           O  
ANISOU 5441  O   ARG E  20     9452   8888  15162   -473   -351   3195       O  
ATOM   5442  CB  ARG E  20       6.418  91.385  -3.012  1.00102.78           C  
ANISOU 5442  CB  ARG E  20    11055  10240  17758   -202   -230   2428       C  
ATOM   5443  CG  ARG E  20       5.664  91.097  -1.724  1.00105.09           C  
ANISOU 5443  CG  ARG E  20    11286  10485  18161    -71   -192   2118       C  
ATOM   5444  CD  ARG E  20       6.129  92.000  -0.596  1.00108.41           C  
ANISOU 5444  CD  ARG E  20    11550  10612  19030    -13   -141   1786       C  
ATOM   5445  NE  ARG E  20       6.231  93.394  -1.017  1.00111.48           N  
ANISOU 5445  NE  ARG E  20    11782  10712  19864    -45   -203   1923       N  
ATOM   5446  CZ  ARG E  20       5.195  94.220  -1.125  1.00114.58           C  
ANISOU 5446  CZ  ARG E  20    12026  10919  20590      8   -271   2034       C  
ATOM   5447  NH1 ARG E  20       5.383  95.475  -1.513  1.00118.65           N  
ANISOU 5447  NH1 ARG E  20    12394  11147  21539    -26   -333   2173       N  
ATOM   5448  NH2 ARG E  20       3.970  93.791  -0.851  1.00116.91           N  
ANISOU 5448  NH2 ARG E  20    12314  11306  20801     93   -280   2023       N  
ATOM   5449  N   SER E  21       8.595  90.585  -5.233  1.00 83.65           N  
ANISOU 5449  N   SER E  21     8933   8202  14649   -503   -178   2850       N  
ATOM   5450  CA  SER E  21       9.315  90.965  -6.443  1.00 85.96           C  
ANISOU 5450  CA  SER E  21     9239   8572  14851   -654   -184   3167       C  
ATOM   5451  C   SER E  21       9.620  89.770  -7.339  1.00 85.94           C  
ANISOU 5451  C   SER E  21     9437   8921  14296   -746   -144   3267       C  
ATOM   5452  O   SER E  21      10.413  89.882  -8.272  1.00 83.72           O  
ANISOU 5452  O   SER E  21     9176   8767  13866   -882   -108   3489       O  
ATOM   5453  CB  SER E  21      10.624  91.653  -6.081  1.00 83.78           C  
ANISOU 5453  CB  SER E  21     8883   8115  14834   -718   -109   3089       C  
ATOM   5454  OG  SER E  21      11.627  90.695  -5.819  1.00 70.14           O  
ANISOU 5454  OG  SER E  21     7286   6558  12806   -759      9   2904       O  
ATOM   5455  N   HIS E  22       9.007  88.631  -7.030  1.00 89.48           N  
ANISOU 5455  N   HIS E  22    10018   9522  14459   -678   -146   3098       N  
ATOM   5456  CA  HIS E  22       9.142  87.400  -7.816  1.00 90.12           C  
ANISOU 5456  CA  HIS E  22    10292   9908  14042   -754   -120   3148       C  
ATOM   5457  C   HIS E  22      10.475  86.663  -7.677  1.00 78.31           C  
ANISOU 5457  C   HIS E  22     8901   8521  12334   -811     27   3006       C  
ATOM   5458  O   HIS E  22      10.879  85.938  -8.586  1.00 81.89           O  
ANISOU 5458  O   HIS E  22     9470   9221  12423   -910     73   3118       O  
ATOM   5459  CB  HIS E  22       8.796  87.633  -9.295  1.00103.49           C  
ANISOU 5459  CB  HIS E  22    11982  11783  15556   -872   -199   3518       C  
ATOM   5460  CG  HIS E  22       7.327  87.720  -9.559  1.00110.76           C  
ANISOU 5460  CG  HIS E  22    12853  12719  16511   -827   -347   3638       C  
ATOM   5461  ND1 HIS E  22       6.640  86.760 -10.268  1.00112.08           N  
ANISOU 5461  ND1 HIS E  22    13140  13134  16309   -872   -415   3702       N  
ATOM   5462  CD2 HIS E  22       6.406  88.643  -9.186  1.00114.84           C  
ANISOU 5462  CD2 HIS E  22    13193  13032  17408   -745   -438   3702       C  
ATOM   5463  CE1 HIS E  22       5.362  87.091 -10.333  1.00115.60           C  
ANISOU 5463  CE1 HIS E  22    13481  13543  16901   -829   -546   3812       C  
ATOM   5464  NE2 HIS E  22       5.196  88.229  -9.683  1.00116.76           N  
ANISOU 5464  NE2 HIS E  22    13444  13420  17501   -747   -554   3819       N  
ATOM   5465  N   GLU E  23      11.150  86.828  -6.542  1.00 55.06           N  
ANISOU 5465  N   GLU E  23     5894   5408   9619   -749    104   2757       N  
ATOM   5466  CA  GLU E  23      12.307  85.991  -6.244  1.00 43.93           C  
ANISOU 5466  CA  GLU E  23     4556   4106   8029   -784    242   2595       C  
ATOM   5467  C   GLU E  23      11.843  84.717  -5.561  1.00 45.09           C  
ANISOU 5467  C   GLU E  23     4826   4326   7980   -680    247   2372       C  
ATOM   5468  O   GLU E  23      10.867  84.737  -4.808  1.00 46.60           O  
ANISOU 5468  O   GLU E  23     4989   4414   8302   -564    168   2254       O  
ATOM   5469  CB  GLU E  23      13.331  86.748  -5.397  1.00 48.61           C  
ANISOU 5469  CB  GLU E  23     4999   4506   8964   -789    316   2444       C  
ATOM   5470  CG  GLU E  23      14.044  87.860  -6.183  1.00 54.59           C  
ANISOU 5470  CG  GLU E  23     5644   5216   9882   -929    327   2694       C  
ATOM   5471  CD  GLU E  23      14.836  87.315  -7.371  1.00 75.86           C  
ANISOU 5471  CD  GLU E  23     8407   8218  12199  -1077    427   2910       C  
ATOM   5472  OE1 GLU E  23      15.458  86.233  -7.238  1.00 80.41           O  
ANISOU 5472  OE1 GLU E  23     9060   8982  12510  -1082    547   2770       O  
ATOM   5473  OE2 GLU E  23      14.834  87.966  -8.441  1.00 87.67           O  
ANISOU 5473  OE2 GLU E  23     9857   9785  13667  -1185    394   3229       O  
ATOM   5474  N   LYS E  24      12.517  83.605  -5.851  1.00 44.41           N  
ANISOU 5474  N   LYS E  24     4858   4428   7589   -725    345   2339       N  
ATOM   5475  CA  LYS E  24      12.020  82.292  -5.477  1.00 50.67           C  
ANISOU 5475  CA  LYS E  24     5789   5297   8166   -647    330   2200       C  
ATOM   5476  C   LYS E  24      13.036  81.540  -4.651  1.00 45.59           C  
ANISOU 5476  C   LYS E  24     5132   4659   7532   -601    470   2001       C  
ATOM   5477  O   LYS E  24      14.222  81.524  -4.963  1.00 44.58           O  
ANISOU 5477  O   LYS E  24     4951   4626   7363   -678    616   2031       O  
ATOM   5478  CB  LYS E  24      11.735  81.463  -6.728  1.00 65.56           C  
ANISOU 5478  CB  LYS E  24     7838   7408   9662   -737    306   2370       C  
ATOM   5479  CG  LYS E  24      10.582  81.954  -7.581  1.00 79.97           C  
ANISOU 5479  CG  LYS E  24     9675   9270  11439   -779    155   2569       C  
ATOM   5480  CD  LYS E  24      10.642  81.331  -8.971  1.00 91.52           C  
ANISOU 5480  CD  LYS E  24    11261  11006  12505   -907    157   2762       C  
ATOM   5481  CE  LYS E  24      10.845  79.821  -8.895  1.00100.25           C  
ANISOU 5481  CE  LYS E  24    12538  12231  13323   -898    202   2630       C  
ATOM   5482  NZ  LYS E  24      11.197  79.236 -10.221  1.00105.64           N  
ANISOU 5482  NZ  LYS E  24    13325  13249  13566  -1033    244   2792       N  
ATOM   5483  N   MET E  25      12.567  80.912  -3.594  1.00 38.35           N  
ANISOU 5483  N   MET E  25     4233   3668   6670   -474    439   1813       N  
ATOM   5484  CA  MET E  25      13.414  79.960  -2.902  1.00 40.79           C  
ANISOU 5484  CA  MET E  25     4548   4025   6925   -403    558   1625       C  
ATOM   5485  C   MET E  25      12.623  78.706  -2.596  1.00 42.69           C  
ANISOU 5485  C   MET E  25     4942   4323   6954   -296    469   1532       C  
ATOM   5486  O   MET E  25      11.401  78.733  -2.501  1.00 38.32           O  
ANISOU 5486  O   MET E  25     4421   3695   6442   -287    340   1624       O  
ATOM   5487  CB  MET E  25      14.070  80.566  -1.653  1.00 46.60           C  
ANISOU 5487  CB  MET E  25     5099   4670   7938   -333    612   1381       C  
ATOM   5488  CG  MET E  25      13.217  80.647  -0.413  1.00 51.67           C  
ANISOU 5488  CG  MET E  25     5681   5200   8752   -206    531   1225       C  
ATOM   5489  SD  MET E  25      14.105  81.460   0.941  1.00 53.58           S  
ANISOU 5489  SD  MET E  25     5689   5395   9273   -149    588    892       S  
ATOM   5490  CE  MET E  25      14.886  80.138   1.748  1.00 46.92           C  
ANISOU 5490  CE  MET E  25     4870   4834   8121     -5    634    645       C  
ATOM   5491  N   THR E  26      13.321  77.593  -2.470  1.00 28.74           N  
ANISOU 5491  N   THR E  26     3258   2703   4959   -208    525   1338       N  
ATOM   5492  CA  THR E  26      12.682  76.356  -2.064  1.00 28.10           C  
ANISOU 5492  CA  THR E  26     3304   2631   4740   -109    435   1252       C  
ATOM   5493  C   THR E  26      13.397  75.810  -0.872  1.00 33.73           C  
ANISOU 5493  C   THR E  26     3941   3393   5483     46    487   1019       C  
ATOM   5494  O   THR E  26      14.614  75.695  -0.886  1.00 34.22           O  
ANISOU 5494  O   THR E  26     3951   3560   5491     89    602    886       O  
ATOM   5495  CB  THR E  26      12.742  75.347  -3.208  1.00 34.76           C  
ANISOU 5495  CB  THR E  26     4346   3581   5281   -147    419   1257       C  
ATOM   5496  OG1 THR E  26      11.990  75.872  -4.307  1.00 40.09           O  
ANISOU 5496  OG1 THR E  26     5077   4266   5888   -304    346   1501       O  
ATOM   5497  CG2 THR E  26      12.181  73.991  -2.779  1.00 34.04           C  
ANISOU 5497  CG2 THR E  26     4383   3441   5108    -58    314   1156       C  
ATOM   5498  N   ILE E  27      12.654  75.473   0.174  1.00 28.68           N  
ANISOU 5498  N   ILE E  27     3268   2714   4917    130    404    994       N  
ATOM   5499  CA  ILE E  27      13.275  74.909   1.367  1.00 30.38           C  
ANISOU 5499  CA  ILE E  27     3391   3024   5127    277    436    819       C  
ATOM   5500  C   ILE E  27      12.793  73.498   1.510  1.00 32.16           C  
ANISOU 5500  C   ILE E  27     3749   3241   5230    343    346    856       C  
ATOM   5501  O   ILE E  27      11.584  73.252   1.521  1.00 28.76           O  
ANISOU 5501  O   ILE E  27     3375   2738   4814    298    234    998       O  
ATOM   5502  CB  ILE E  27      12.901  75.718   2.640  1.00 29.65           C  
ANISOU 5502  CB  ILE E  27     3104   2953   5208    327    423    752       C  
ATOM   5503  CG1 ILE E  27      13.416  77.144   2.544  1.00 30.27           C  
ANISOU 5503  CG1 ILE E  27     3044   2973   5485    254    494    682       C  
ATOM   5504  CG2 ILE E  27      13.486  75.066   3.886  1.00 30.22           C  
ANISOU 5504  CG2 ILE E  27     3071   3198   5213    472    436    608       C  
ATOM   5505  CD1 ILE E  27      12.977  78.036   3.724  1.00 30.40           C  
ANISOU 5505  CD1 ILE E  27     2870   2983   5696    308    476    547       C  
ATOM   5506  N   ILE E  28      13.730  72.558   1.593  1.00 28.52           N  
ANISOU 5506  N   ILE E  28     3323   2835   4678    448    389    742       N  
ATOM   5507  CA  ILE E  28      13.397  71.167   1.882  1.00 29.62           C  
ANISOU 5507  CA  ILE E  28     3564   2915   4774    528    295    777       C  
ATOM   5508  C   ILE E  28      13.703  70.905   3.357  1.00 34.79           C  
ANISOU 5508  C   ILE E  28     4047   3693   5478    663    291    763       C  
ATOM   5509  O   ILE E  28      14.811  71.161   3.817  1.00 36.41           O  
ANISOU 5509  O   ILE E  28     4119   4033   5682    750    380    633       O  
ATOM   5510  CB  ILE E  28      14.197  70.196   0.981  1.00 31.02           C  
ANISOU 5510  CB  ILE E  28     3890   3046   4851    584    332    657       C  
ATOM   5511  CG1 ILE E  28      14.000  70.535  -0.503  1.00 38.77           C  
ANISOU 5511  CG1 ILE E  28     5016   4006   5708    445    351    652       C  
ATOM   5512  CG2 ILE E  28      13.858  68.718   1.268  1.00 35.88           C  
ANISOU 5512  CG2 ILE E  28     4614   3518   5502    666    213    687       C  
ATOM   5513  CD1 ILE E  28      12.620  70.285  -1.015  1.00 45.91           C  
ANISOU 5513  CD1 ILE E  28     6063   4791   6591    312    195    793       C  
ATOM   5514  N   ILE E  29      12.723  70.411   4.106  1.00 31.93           N  
ANISOU 5514  N   ILE E  29     3664   3324   5143    670    184    915       N  
ATOM   5515  CA  ILE E  29      12.980  70.004   5.485  1.00 30.10           C  
ANISOU 5515  CA  ILE E  29     3266   3265   4906    795    170    952       C  
ATOM   5516  C   ILE E  29      12.864  68.494   5.622  1.00 33.03           C  
ANISOU 5516  C   ILE E  29     3728   3522   5300    857     70   1098       C  
ATOM   5517  O   ILE E  29      11.796  67.936   5.380  1.00 37.69           O  
ANISOU 5517  O   ILE E  29     4420   3966   5933    769    -40   1263       O  
ATOM   5518  CB  ILE E  29      11.972  70.651   6.469  1.00 39.40           C  
ANISOU 5518  CB  ILE E  29     4283   4599   6087    769    142   1040       C  
ATOM   5519  CG1 ILE E  29      11.882  72.152   6.243  1.00 41.82           C  
ANISOU 5519  CG1 ILE E  29     4516   4921   6453    703    216    897       C  
ATOM   5520  CG2 ILE E  29      12.352  70.338   7.916  1.00 35.05           C  
ANISOU 5520  CG2 ILE E  29     3530   4328   5461    896    141   1064       C  
ATOM   5521  CD1 ILE E  29      10.977  72.842   7.238  1.00 42.55           C  
ANISOU 5521  CD1 ILE E  29     4429   5175   6564    718    208    908       C  
ATOM   5522  N   HIS E  30      13.956  67.861   6.041  1.00 32.68           N  
ANISOU 5522  N   HIS E  30     3623   3535   5259   1006     97   1050       N  
ATOM   5523  CA  HIS E  30      14.043  66.427   6.250  1.00 35.83           C  
ANISOU 5523  CA  HIS E  30     4079   3789   5744   1098      1   1192       C  
ATOM   5524  C   HIS E  30      13.636  66.050   7.669  1.00 37.20           C  
ANISOU 5524  C   HIS E  30     4087   4173   5876   1115    -73   1409       C  
ATOM   5525  O   HIS E  30      13.877  66.804   8.614  1.00 40.42           O  
ANISOU 5525  O   HIS E  30     4282   4893   6182   1165    -19   1398       O  
ATOM   5526  CB  HIS E  30      15.488  65.964   6.009  1.00 44.45           C  
ANISOU 5526  CB  HIS E  30     5161   4863   6866   1267     73   1030       C  
ATOM   5527  CG  HIS E  30      15.942  66.115   4.589  1.00 53.60           C  
ANISOU 5527  CG  HIS E  30     6490   5873   8003   1237    158    794       C  
ATOM   5528  ND1 HIS E  30      15.961  65.066   3.699  1.00 52.80           N  
ANISOU 5528  ND1 HIS E  30     6585   5497   7979   1275    113    723       N  
ATOM   5529  CD2 HIS E  30      16.394  67.198   3.907  1.00 48.04           C  
ANISOU 5529  CD2 HIS E  30     5774   5281   7200   1169    287    618       C  
ATOM   5530  CE1 HIS E  30      16.399  65.493   2.525  1.00 56.51           C  
ANISOU 5530  CE1 HIS E  30     7154   5971   8347   1239    221    500       C  
ATOM   5531  NE2 HIS E  30      16.668  66.781   2.627  1.00 49.42           N  
ANISOU 5531  NE2 HIS E  30     6128   5306   7345   1167    328    468       N  
ATOM   5532  N   ASP E  31      13.070  64.860   7.833  1.00 41.34           N  
ANISOU 5532  N   ASP E  31     5270   3076   7360    348    932   1247       N  
ATOM   5533  CA  ASP E  31      12.687  64.410   9.164  1.00 43.70           C  
ANISOU 5533  CA  ASP E  31     5627   3285   7691    343    950   1449       C  
ATOM   5534  C   ASP E  31      13.880  64.208  10.103  1.00 48.03           C  
ANISOU 5534  C   ASP E  31     6055   3963   8231    665    944   1834       C  
ATOM   5535  O   ASP E  31      13.727  64.288  11.314  1.00 47.66           O  
ANISOU 5535  O   ASP E  31     5969   4031   8107    613    860   2043       O  
ATOM   5536  CB  ASP E  31      11.804  63.171   9.090  1.00 48.50           C  
ANISOU 5536  CB  ASP E  31     6560   3455   8412    224   1182   1333       C  
ATOM   5537  CG  ASP E  31      10.365  63.513   8.732  1.00 50.81           C  
ANISOU 5537  CG  ASP E  31     6880   3742   8684   -180   1098   1034       C  
ATOM   5538  OD1 ASP E  31       9.890  64.594   9.147  1.00 47.52           O  
ANISOU 5538  OD1 ASP E  31     6241   3595   8219   -336    887   1031       O  
ATOM   5539  OD2 ASP E  31       9.719  62.710   8.033  1.00 55.39           O  
ANISOU 5539  OD2 ASP E  31     7685   4052   9309   -354   1265    804       O  
ATOM   5540  N   ASP E  32      15.066  63.983   9.546  1.00 46.07           N  
ANISOU 5540  N   ASP E  32     5725   3728   8051    972   1027   1935       N  
ATOM   5541  CA  ASP E  32      16.264  63.849  10.373  1.00 53.99           C  
ANISOU 5541  CA  ASP E  32     6524   4929   9060   1292    978   2344       C  
ATOM   5542  C   ASP E  32      16.836  65.195  10.830  1.00 48.79           C  
ANISOU 5542  C   ASP E  32     5522   4825   8192   1212    701   2407       C  
ATOM   5543  O   ASP E  32      17.762  65.245  11.639  1.00 50.29           O  
ANISOU 5543  O   ASP E  32     5491   5303   8314   1385    593   2746       O  
ATOM   5544  CB  ASP E  32      17.340  63.002   9.680  1.00 50.75           C  
ANISOU 5544  CB  ASP E  32     6118   4287   8880   1680   1227   2462       C  
ATOM   5545  CG  ASP E  32      17.904  63.651   8.420  1.00 56.66           C  
ANISOU 5545  CG  ASP E  32     6755   5151   9621   1683   1252   2185       C  
ATOM   5546  OD1 ASP E  32      17.596  64.821   8.117  1.00 50.71           O  
ANISOU 5546  OD1 ASP E  32     5890   4702   8677   1430   1044   1966       O  
ATOM   5547  OD2 ASP E  32      18.685  62.977   7.726  1.00 57.80           O  
ANISOU 5547  OD2 ASP E  32     6932   5056   9973   1946   1520   2199       O  
ATOM   5548  N   GLY E  33      16.279  66.284  10.313  1.00 42.25           N  
ANISOU 5548  N   GLY E  33     4639   4151   7262    934    598   2096       N  
ATOM   5549  CA  GLY E  33      16.708  67.608  10.722  1.00 42.17           C  
ANISOU 5549  CA  GLY E  33     4346   4603   7073    803    414   2099       C  
ATOM   5550  C   GLY E  33      17.472  68.430   9.690  1.00 38.54           C  
ANISOU 5550  C   GLY E  33     3715   4330   6597    865    403   1938       C  
ATOM   5551  O   GLY E  33      17.611  69.652   9.845  1.00 43.04           O  
ANISOU 5551  O   GLY E  33     4096   5221   7037    689    304   1853       O  
ATOM   5552  N  AARG E  34      17.959  67.786   8.637  0.45 43.26           N  
ANISOU 5552  N  AARG E  34     4401   4706   7331   1085    552   1875       N  
ATOM   5553  N  BARG E  34      17.973  67.782   8.645  0.55 43.04           N  
ANISOU 5553  N  BARG E  34     4371   4680   7303   1088    552   1878       N  
ATOM   5554  CA AARG E  34      18.697  68.511   7.606  0.45 38.99           C  
ANISOU 5554  CA AARG E  34     3734   4317   6763   1126    575   1710       C  
ATOM   5555  CA BARG E  34      18.687  68.507   7.593  0.55 43.78           C  
ANISOU 5555  CA BARG E  34     4344   4920   7370   1125    576   1707       C  
ATOM   5556  C  AARG E  34      17.783  69.440   6.803  0.45 39.53           C  
ANISOU 5556  C  AARG E  34     3882   4390   6746    830    513   1418       C  
ATOM   5557  C  BARG E  34      17.757  69.480   6.870  0.55 38.71           C  
ANISOU 5557  C  BARG E  34     3770   4299   6638    821    504   1424       C  
ATOM   5558  O  AARG E  34      16.618  69.122   6.560  0.45 39.68           O  
ANISOU 5558  O  AARG E  34     4101   4179   6795    655    512   1296       O  
ATOM   5559  O  BARG E  34      16.558  69.231   6.753  0.55 35.31           O  
ANISOU 5559  O  BARG E  34     3523   3659   6233    634    490   1315       O  
ATOM   5560  CB AARG E  34      19.427  67.544   6.677  0.45 49.40           C  
ANISOU 5560  CB AARG E  34     5154   5360   8255   1399    812   1690       C  
ATOM   5561  CB BARG E  34      19.330  67.546   6.588  0.55 47.78           C  
ANISOU 5561  CB BARG E  34     4974   5132   8047   1376    817   1661       C  
ATOM   5562  CG AARG E  34      20.406  66.630   7.403  0.45 55.22           C  
ANISOU 5562  CG AARG E  34     5753   6069   9158   1763    899   2050       C  
ATOM   5563  CG BARG E  34      20.656  66.958   7.064  0.55 55.96           C  
ANISOU 5563  CG BARG E  34     5793   6240   9230   1754    901   1974       C  
ATOM   5564  CD AARG E  34      21.618  66.346   6.538  0.45 61.60           C  
ANISOU 5564  CD AARG E  34     6450   6812  10142   2046   1117   2038       C  
ATOM   5565  CD BARG E  34      21.182  65.883   6.118  0.55 62.66           C  
ANISOU 5565  CD BARG E  34     6793   6683  10334   2007   1243   1920       C  
ATOM   5566  NE AARG E  34      22.341  67.572   6.215  0.45 56.33           N  
ANISOU 5566  NE AARG E  34     5519   6555   9330   1972   1000   1927       N  
ATOM   5567  NE BARG E  34      20.332  64.695   6.109  0.55 64.13           N  
ANISOU 5567  NE BARG E  34     7322   6390  10654   1994   1440   1898       N  
ATOM   5568  CZ AARG E  34      23.400  68.017   6.885  0.45 55.93           C  
ANISOU 5568  CZ AARG E  34     5085   6913   9254   2114    878   2162       C  
ATOM   5569  CZ BARG E  34      19.588  64.316   5.077  0.55 63.51           C  
ANISOU 5569  CZ BARG E  34     7576   5984  10570   1778   1630   1552       C  
ATOM   5570  NH1AARG E  34      23.988  69.145   6.511  0.45 45.59           N  
ANISOU 5570  NH1AARG E  34     3574   5940   7808   1995    821   2000       N  
ATOM   5571  NH1BARG E  34      18.844  63.223   5.162  0.55 58.14           N  
ANISOU 5571  NH1BARG E  34     7198   4885  10008   1734   1834   1522       N  
ATOM   5572  NH2AARG E  34      23.874  67.333   7.922  0.45 50.26           N  
ANISOU 5572  NH2AARG E  34     4256   6288   8553   2264    798   2498       N  
ATOM   5573  NH2BARG E  34      19.592  65.030   3.957  0.55 70.42           N  
ANISOU 5573  NH2BARG E  34     8489   6970  11297   1574   1620   1239       N  
ATOM   5574  N   ARG E  35      18.322  70.589   6.400  1.00 36.39           N  
ANISOU 5574  N   ARG E  35     3306   4266   6254    775    466   1332       N  
ATOM   5575  CA  ARG E  35      17.595  71.513   5.541  1.00 32.55           C  
ANISOU 5575  CA  ARG E  35     2870   3788   5711    548    418   1129       C  
ATOM   5576  C   ARG E  35      18.439  71.728   4.288  1.00 36.29           C  
ANISOU 5576  C   ARG E  35     3360   4291   6139    633    515   1002       C  
ATOM   5577  O   ARG E  35      19.679  71.794   4.351  1.00 38.20           O  
ANISOU 5577  O   ARG E  35     3444   4688   6383    816    593   1057       O  
ATOM   5578  CB  ARG E  35      17.412  72.882   6.204  1.00 35.72           C  
ANISOU 5578  CB  ARG E  35     3068   4454   6049    364    339   1138       C  
ATOM   5579  CG  ARG E  35      16.208  73.032   7.071  1.00 34.57           C  
ANISOU 5579  CG  ARG E  35     2942   4236   5957    160    284   1161       C  
ATOM   5580  CD  ARG E  35      16.383  72.276   8.402  1.00 33.53           C  
ANISOU 5580  CD  ARG E  35     2803   4133   5803    207    276   1334       C  
ATOM   5581  NE  ARG E  35      15.578  72.942   9.408  1.00 32.35           N  
ANISOU 5581  NE  ARG E  35     2598   4045   5649    -57    273   1324       N  
ATOM   5582  CZ  ARG E  35      15.363  72.469  10.631  1.00 38.68           C  
ANISOU 5582  CZ  ARG E  35     3432   4864   6400   -137    268   1448       C  
ATOM   5583  NH1 ARG E  35      14.607  73.151  11.482  1.00 34.21           N  
ANISOU 5583  NH1 ARG E  35     2833   4332   5834   -428    324   1387       N  
ATOM   5584  NH2 ARG E  35      15.869  71.301  10.983  1.00 33.05           N  
ANISOU 5584  NH2 ARG E  35     2799   4102   5656     68    241   1641       N  
ATOM   5585  N   GLU E  36      17.765  71.831   3.154  1.00 32.85           N  
ANISOU 5585  N   GLU E  36     3103   3729   5648    476    507    841       N  
ATOM   5586  CA  GLU E  36      18.395  72.359   1.948  1.00 38.64           C  
ANISOU 5586  CA  GLU E  36     3869   4538   6274    459    580    711       C  
ATOM   5587  C   GLU E  36      17.613  73.541   1.447  1.00 33.75           C  
ANISOU 5587  C   GLU E  36     3225   4036   5563    234    442    686       C  
ATOM   5588  O   GLU E  36      16.379  73.499   1.432  1.00 32.80           O  
ANISOU 5588  O   GLU E  36     3164   3833   5464     70    310    705       O  
ATOM   5589  CB  GLU E  36      18.464  71.312   0.849  1.00 37.89           C  
ANISOU 5589  CB  GLU E  36     4049   4197   6151    450    738    553       C  
ATOM   5590  CG  GLU E  36      19.454  70.221   1.156  1.00 48.15           C  
ANISOU 5590  CG  GLU E  36     5351   5331   7612    730    968    595       C  
ATOM   5591  CD  GLU E  36      18.786  69.071   1.836  1.00 62.47           C  
ANISOU 5591  CD  GLU E  36     7293   6884   9560    772   1001    674       C  
ATOM   5592  OE1 GLU E  36      17.806  68.549   1.257  1.00 66.73           O  
ANISOU 5592  OE1 GLU E  36     8088   7226  10043    549   1018    522       O  
ATOM   5593  OE2 GLU E  36      19.228  68.699   2.945  1.00 67.67           O  
ANISOU 5593  OE2 GLU E  36     7795   7558  10357   1000   1005    897       O  
ATOM   5594  N   ILE E  37      18.336  74.586   1.060  1.00 30.95           N  
ANISOU 5594  N   ILE E  37     2762   3865   5133    238    489    664       N  
ATOM   5595  CA  ILE E  37      17.729  75.758   0.449  1.00 33.99           C  
ANISOU 5595  CA  ILE E  37     3129   4331   5454     65    405    687       C  
ATOM   5596  C   ILE E  37      18.252  75.911  -0.981  1.00 31.44           C  
ANISOU 5596  C   ILE E  37     2972   4029   4946     13    476    582       C  
ATOM   5597  O   ILE E  37      19.462  75.801  -1.226  1.00 35.30           O  
ANISOU 5597  O   ILE E  37     3460   4561   5394    128    653    481       O  
ATOM   5598  CB  ILE E  37      18.064  77.049   1.229  1.00 36.27           C  
ANISOU 5598  CB  ILE E  37     3179   4794   5807     58    462    750       C  
ATOM   5599  CG1 ILE E  37      17.680  76.905   2.709  1.00 39.30           C  
ANISOU 5599  CG1 ILE E  37     3421   5188   6323     53    434    823       C  
ATOM   5600  CG2 ILE E  37      17.334  78.229   0.604  1.00 30.73           C  
ANISOU 5600  CG2 ILE E  37     2463   4099   5116    -83    421    826       C  
ATOM   5601  CD1 ILE E  37      18.226  78.037   3.578  1.00 39.80           C  
ANISOU 5601  CD1 ILE E  37     3270   5450   6402    -14    557    822       C  
ATOM   5602  N   TYR E  38      17.334  76.150  -1.915  1.00 32.19           N  
ANISOU 5602  N   TYR E  38     3194   4112   4923   -179    336    618       N  
ATOM   5603  CA  TYR E  38      17.652  76.389  -3.318  1.00 33.90           C  
ANISOU 5603  CA  TYR E  38     3601   4382   4897   -308    370    548       C  
ATOM   5604  C   TYR E  38      17.102  77.750  -3.719  1.00 34.43           C  
ANISOU 5604  C   TYR E  38     3577   4573   4931   -408    247    745       C  
ATOM   5605  O   TYR E  38      15.946  78.059  -3.408  1.00 35.40           O  
ANISOU 5605  O   TYR E  38     3580   4693   5179   -468     60    927       O  
ATOM   5606  CB  TYR E  38      16.993  75.319  -4.185  1.00 36.20           C  
ANISOU 5606  CB  TYR E  38     4155   4587   5013   -512    295    446       C  
ATOM   5607  CG  TYR E  38      17.406  73.912  -3.829  1.00 37.09           C  
ANISOU 5607  CG  TYR E  38     4387   4494   5210   -415    479    267       C  
ATOM   5608  CD1 TYR E  38      16.744  73.193  -2.835  1.00 41.11           C  
ANISOU 5608  CD1 TYR E  38     4835   4875   5910   -351    417    316       C  
ATOM   5609  CD2 TYR E  38      18.486  73.316  -4.463  1.00 39.61           C  
ANISOU 5609  CD2 TYR E  38     4880   4714   5456   -373    762     64       C  
ATOM   5610  CE1 TYR E  38      17.141  71.896  -2.501  1.00 38.17           C  
ANISOU 5610  CE1 TYR E  38     4583   4272   5647   -233    623    198       C  
ATOM   5611  CE2 TYR E  38      18.900  72.039  -4.132  1.00 42.51           C  
ANISOU 5611  CE2 TYR E  38     5338   4839   5977   -239    991    -59       C  
ATOM   5612  CZ  TYR E  38      18.230  71.330  -3.154  1.00 43.92           C  
ANISOU 5612  CZ  TYR E  38     5464   4884   6341   -159    918     26       C  
ATOM   5613  OH  TYR E  38      18.653  70.040  -2.854  1.00 43.58           O  
ANISOU 5613  OH  TYR E  38     5528   4555   6474     -4   1185    -56       O  
ATOM   5614  N   ARG E  39      17.919  78.559  -4.399  1.00 34.13           N  
ANISOU 5614  N   ARG E  39     3587   4620   4761   -416    381    726       N  
ATOM   5615  CA  ARG E  39      17.478  79.852  -4.931  1.00 35.12           C  
ANISOU 5615  CA  ARG E  39     3665   4826   4853   -497    312    950       C  
ATOM   5616  C   ARG E  39      17.427  79.794  -6.443  1.00 37.41           C  
ANISOU 5616  C   ARG E  39     4220   5199   4793   -704    232    967       C  
ATOM   5617  O   ARG E  39      18.378  79.353  -7.085  1.00 39.68           O  
ANISOU 5617  O   ARG E  39     4714   5487   4875   -754    412    740       O  
ATOM   5618  CB  ARG E  39      18.421  81.009  -4.504  1.00 33.92           C  
ANISOU 5618  CB  ARG E  39     3377   4703   4807   -389    567    934       C  
ATOM   5619  CG  ARG E  39      18.141  81.481  -3.058  1.00 47.20           C  
ANISOU 5619  CG  ARG E  39     4785   6346   6803   -292    624    990       C  
ATOM   5620  CD  ARG E  39      17.030  82.562  -3.006  1.00 35.93           C  
ANISOU 5620  CD  ARG E  39     3228   4850   5573   -332    568   1275       C  
ATOM   5621  NE  ARG E  39      17.534  83.827  -3.537  1.00 48.59           N  
ANISOU 5621  NE  ARG E  39     4849   6457   7155   -347    775   1356       N  
ATOM   5622  CZ  ARG E  39      17.022  84.463  -4.579  1.00 49.93           C  
ANISOU 5622  CZ  ARG E  39     5099   6619   7254   -396    688   1619       C  
ATOM   5623  NH1 ARG E  39      17.567  85.600  -4.994  1.00 45.84           N  
ANISOU 5623  NH1 ARG E  39     4619   6070   6728   -400    929   1690       N  
ATOM   5624  NH2 ARG E  39      15.965  83.966  -5.203  1.00 44.55           N  
ANISOU 5624  NH2 ARG E  39     4451   5978   6499   -460    360   1828       N  
ATOM   5625  N   PHE E  40      16.326  80.250  -7.019  1.00 39.05           N  
ANISOU 5625  N   PHE E  40     4411   5495   4933   -842    -27   1251       N  
ATOM   5626  CA  PHE E  40      16.185  80.242  -8.469  1.00 42.37           C  
ANISOU 5626  CA  PHE E  40     5082   6066   4951  -1101   -155   1321       C  
ATOM   5627  C   PHE E  40      15.956  81.625  -9.067  1.00 57.51           C  
ANISOU 5627  C   PHE E  40     6944   8077   6829  -1112   -219   1684       C  
ATOM   5628  O   PHE E  40      15.424  82.528  -8.413  1.00 54.91           O  
ANISOU 5628  O   PHE E  40     6345   7682   6838   -944   -238   1954       O  
ATOM   5629  CB  PHE E  40      15.029  79.344  -8.914  1.00 44.60           C  
ANISOU 5629  CB  PHE E  40     5427   6455   5062  -1349   -472   1373       C  
ATOM   5630  CG  PHE E  40      15.207  77.901  -8.543  1.00 52.67           C  
ANISOU 5630  CG  PHE E  40     6581   7350   6083  -1389   -366   1017       C  
ATOM   5631  CD1 PHE E  40      15.869  77.024  -9.398  1.00 57.67           C  
ANISOU 5631  CD1 PHE E  40     7555   7966   6393  -1599   -190    704       C  
ATOM   5632  CD2 PHE E  40      14.720  77.422  -7.342  1.00 41.85           C  
ANISOU 5632  CD2 PHE E  40     5011   5841   5048  -1226   -391    996       C  
ATOM   5633  CE1 PHE E  40      16.038  75.692  -9.064  1.00 52.77           C  
ANISOU 5633  CE1 PHE E  40     7061   7161   5829  -1614    -20    396       C  
ATOM   5634  CE2 PHE E  40      14.877  76.073  -7.005  1.00 43.20           C  
ANISOU 5634  CE2 PHE E  40     5322   5857   5235  -1246   -264    708       C  
ATOM   5635  CZ  PHE E  40      15.540  75.212  -7.874  1.00 45.07           C  
ANISOU 5635  CZ  PHE E  40     5886   6047   5191  -1425    -67    417       C  
ATOM   5636  N   ASN E  41      16.359  81.742 -10.326  1.00 64.03           N  
ANISOU 5636  N   ASN E  41     8049   9033   7245  -1328   -215   1686       N  
ATOM   5637  CA  ASN E  41      16.091  82.890 -11.179  1.00 81.01           C  
ANISOU 5637  CA  ASN E  41    10227  11306   9248  -1398   -317   2080       C  
ATOM   5638  C   ASN E  41      14.605  83.244 -11.187  1.00 86.21           C  
ANISOU 5638  C   ASN E  41    10626  12083  10046  -1406   -709   2565       C  
ATOM   5639  O   ASN E  41      13.748  82.363 -11.247  1.00 82.59           O  
ANISOU 5639  O   ASN E  41    10129  11753   9500  -1569   -998   2559       O  
ATOM   5640  CB  ASN E  41      16.527  82.538 -12.606  1.00 86.46           C  
ANISOU 5640  CB  ASN E  41    11314  12176   9361  -1746   -334   1974       C  
ATOM   5641  CG  ASN E  41      17.210  83.687 -13.325  1.00 86.83           C  
ANISOU 5641  CG  ASN E  41    11511  12236   9246  -1757   -149   2141       C  
ATOM   5642  OD1 ASN E  41      16.589  84.708 -13.622  1.00 95.65           O  
ANISOU 5642  OD1 ASN E  41    12513  13420  10408  -1712   -312   2630       O  
ATOM   5643  ND2 ASN E  41      18.489  83.508 -13.642  1.00 82.52           N  
ANISOU 5643  ND2 ASN E  41    11217  11610   8525  -1818    215   1750       N  
ATOM   5644  N   ASP E  42      14.293  84.534 -11.134  1.00100.21           N  
ANISOU 5644  N   ASP E  42    12206  13802  12067  -1233   -690   2989       N  
ATOM   5645  CA  ASP E  42      12.914  84.965 -11.322  1.00107.87           C  
ANISOU 5645  CA  ASP E  42    12897  14897  13190  -1223  -1055   3534       C  
ATOM   5646  C   ASP E  42      12.462  84.617 -12.742  1.00105.28           C  
ANISOU 5646  C   ASP E  42    12764  14948  12289  -1585  -1449   3762       C  
ATOM   5647  O   ASP E  42      11.321  84.208 -12.962  1.00 98.22           O  
ANISOU 5647  O   ASP E  42    11688  14288  11344  -1732  -1858   4013       O  
ATOM   5648  CB  ASP E  42      12.763  86.468 -11.047  1.00120.92           C  
ANISOU 5648  CB  ASP E  42    14323  16355  15268   -944   -865   3967       C  
ATOM   5649  CG  ASP E  42      13.679  87.323 -11.908  1.00131.58           C  
ANISOU 5649  CG  ASP E  42    15947  17695  16352   -980   -642   4062       C  
ATOM   5650  OD1 ASP E  42      14.704  86.799 -12.392  1.00134.47           O  
ANISOU 5650  OD1 ASP E  42    16660  18130  16304  -1164   -505   3657       O  
ATOM   5651  OD2 ASP E  42      13.375  88.523 -12.093  1.00135.70           O  
ANISOU 5651  OD2 ASP E  42    16337  18113  17112   -820   -563   4547       O  
ATOM   5652  N   ARG E  43      13.385  84.758 -13.691  1.00108.56           N  
ANISOU 5652  N   ARG E  43    13553  15444  12250  -1770  -1309   3647       N  
ATOM   5653  CA  ARG E  43      13.124  84.478 -15.098  1.00112.60           C  
ANISOU 5653  CA  ARG E  43    14326  16336  12119  -2191  -1627   3821       C  
ATOM   5654  C   ARG E  43      13.052  82.981 -15.382  1.00108.24           C  
ANISOU 5654  C   ARG E  43    13998  15951  11177  -2570  -1743   3357       C  
ATOM   5655  O   ARG E  43      11.980  82.445 -15.662  1.00106.18           O  
ANISOU 5655  O   ARG E  43    13614  15976  10753  -2815  -2153   3531       O  
ATOM   5656  CB  ARG E  43      14.205  85.125 -15.969  1.00121.63           C  
ANISOU 5656  CB  ARG E  43    15837  17467  12908  -2291  -1358   3795       C  
ATOM   5657  CG  ARG E  43      14.330  86.628 -15.767  1.00125.61           C  
ANISOU 5657  CG  ARG E  43    16176  17770  13780  -1951  -1170   4239       C  
ATOM   5658  CD  ARG E  43      12.973  87.286 -15.925  1.00131.71           C  
ANISOU 5658  CD  ARG E  43    16581  18692  14771  -1838  -1577   4949       C  
ATOM   5659  NE  ARG E  43      12.958  88.676 -15.482  1.00132.23           N  
ANISOU 5659  NE  ARG E  43    16413  18428  15399  -1424  -1295   5252       N  
ATOM   5660  CZ  ARG E  43      11.868  89.437 -15.477  1.00136.16           C  
ANISOU 5660  CZ  ARG E  43    16527  18901  16305  -1198  -1467   5688       C  
ATOM   5661  NH1 ARG E  43      10.711  88.936 -15.888  1.00138.78           N  
ANISOU 5661  NH1 ARG E  43    16630  19553  16548  -1351  -1942   5893       N  
ATOM   5662  NH2 ARG E  43      11.932  90.695 -15.061  1.00137.19           N  
ANISOU 5662  NH2 ARG E  43    16498  18688  16941   -850  -1121   5891       N  
ATOM   5663  N   ASP E  44      14.198  82.310 -15.304  1.00102.65           N  
ANISOU 5663  N   ASP E  44    13600  15054  10348  -2623  -1350   2768       N  
ATOM   5664  CA  ASP E  44      14.284  80.893 -15.641  1.00 97.13           C  
ANISOU 5664  CA  ASP E  44    13175  14427   9303  -2987  -1327   2289       C  
ATOM   5665  C   ASP E  44      14.269  79.989 -14.410  1.00 90.66           C  
ANISOU 5665  C   ASP E  44    12190  13333   8922  -2755  -1172   1929       C  
ATOM   5666  O   ASP E  44      15.247  79.929 -13.666  1.00 90.85           O  
ANISOU 5666  O   ASP E  44    12216  13056   9248  -2462   -789   1627       O  
ATOM   5667  CB  ASP E  44      15.538  80.620 -16.471  1.00100.19           C  
ANISOU 5667  CB  ASP E  44    14028  14761   9277  -3227   -948   1879       C  
ATOM   5668  CG  ASP E  44      15.749  79.143 -16.739  1.00104.43           C  
ANISOU 5668  CG  ASP E  44    14863  15263   9553  -3571   -779   1328       C  
ATOM   5669  OD1 ASP E  44      14.750  78.392 -16.795  1.00 96.69           O  
ANISOU 5669  OD1 ASP E  44    13834  14459   8443  -3830  -1069   1338       O  
ATOM   5670  OD2 ASP E  44      16.919  78.733 -16.896  1.00112.46           O  
ANISOU 5670  OD2 ASP E  44    16152  16057  10520  -3588   -317    878       O  
ATOM   5671  N   PRO E  45      13.163  79.257 -14.215  1.00 88.88           N  
ANISOU 5671  N   PRO E  45    11823  13239   8709  -2915  -1475   1970       N  
ATOM   5672  CA  PRO E  45      12.954  78.371 -13.061  1.00 92.28           C  
ANISOU 5672  CA  PRO E  45    12103  13425   9535  -2730  -1368   1690       C  
ATOM   5673  C   PRO E  45      13.888  77.161 -13.042  1.00 92.03           C  
ANISOU 5673  C   PRO E  45    12407  13165   9397  -2828   -969   1104       C  
ATOM   5674  O   PRO E  45      14.042  76.531 -11.998  1.00 87.30           O  
ANISOU 5674  O   PRO E  45    11704  12296   9169  -2580   -788    888       O  
ATOM   5675  CB  PRO E  45      11.506  77.901 -13.244  1.00 95.23           C  
ANISOU 5675  CB  PRO E  45    12310  14073   9799  -3018  -1805   1886       C  
ATOM   5676  CG  PRO E  45      11.261  78.008 -14.711  1.00 98.63           C  
ANISOU 5676  CG  PRO E  45    12968  14917   9588  -3511  -2062   2047       C  
ATOM   5677  CD  PRO E  45      12.023  79.224 -15.148  1.00 94.50           C  
ANISOU 5677  CD  PRO E  45    12508  14387   9012  -3330  -1956   2307       C  
ATOM   5678  N   ASP E  46      14.488  76.833 -14.181  1.00 97.90           N  
ANISOU 5678  N   ASP E  46    13547  14002   9651  -3192   -811    870       N  
ATOM   5679  CA  ASP E  46      15.389  75.687 -14.258  1.00 97.93           C  
ANISOU 5679  CA  ASP E  46    13870  13743   9598  -3290   -358    320       C  
ATOM   5680  C   ASP E  46      16.824  76.064 -13.911  1.00 81.73           C  
ANISOU 5680  C   ASP E  46    11838  11422   7796  -2926     70    149       C  
ATOM   5681  O   ASP E  46      17.664  75.192 -13.696  1.00 75.86           O  
ANISOU 5681  O   ASP E  46    11236  10399   7186  -2849    479   -244       O  
ATOM   5682  CB  ASP E  46      15.338  75.038 -15.646  1.00111.57           C  
ANISOU 5682  CB  ASP E  46    16039  15669  10684  -3927   -309     73       C  
ATOM   5683  CG  ASP E  46      14.113  74.168 -15.838  1.00121.73           C  
ANISOU 5683  CG  ASP E  46    17348  17154  11749  -4346   -587     31       C  
ATOM   5684  OD1 ASP E  46      13.057  74.491 -15.254  1.00124.13           O  
ANISOU 5684  OD1 ASP E  46    17284  17609  12270  -4209   -998    387       O  
ATOM   5685  OD2 ASP E  46      14.206  73.158 -16.570  1.00127.93           O  
ANISOU 5685  OD2 ASP E  46    18517  17935  12155  -4838   -355   -381       O  
ATOM   5686  N   GLU E  47      17.107  77.362 -13.864  1.00 72.19           N  
ANISOU 5686  N   GLU E  47    10468  10293   6670  -2707     -1    454       N  
ATOM   5687  CA  GLU E  47      18.447  77.810 -13.513  1.00 68.47           C  
ANISOU 5687  CA  GLU E  47     9972   9617   6426  -2397    390    295       C  
ATOM   5688  C   GLU E  47      18.603  78.099 -12.016  1.00 61.74           C  
ANISOU 5688  C   GLU E  47     8726   8592   6141  -1909    427    376       C  
ATOM   5689  O   GLU E  47      17.977  79.006 -11.468  1.00 50.65           O  
ANISOU 5689  O   GLU E  47     7045   7257   4941  -1738    198    722       O  
ATOM   5690  CB  GLU E  47      18.855  79.023 -14.348  1.00 76.86           C  
ANISOU 5690  CB  GLU E  47    11145  10830   7227  -2487    403    499       C  
ATOM   5691  CG  GLU E  47      20.296  78.959 -14.844  1.00 84.72           C  
ANISOU 5691  CG  GLU E  47    12388  11685   8116  -2521    886    132       C  
ATOM   5692  CD  GLU E  47      20.558  79.891 -16.011  1.00 96.27           C  
ANISOU 5692  CD  GLU E  47    14107  13322   9149  -2786    902    284       C  
ATOM   5693  OE1 GLU E  47      19.892  79.736 -17.059  1.00100.49           O  
ANISOU 5693  OE1 GLU E  47    14907  14094   9178  -3225    671    397       O  
ATOM   5694  OE2 GLU E  47      21.429  80.779 -15.880  1.00 95.51           O  
ANISOU 5694  OE2 GLU E  47    13951  13143   9195  -2585   1147    294       O  
ATOM   5695  N   LEU E  48      19.461  77.315 -11.377  1.00 49.31           N  
ANISOU 5695  N   LEU E  48     7127   6792   4816  -1704    745     61       N  
ATOM   5696  CA  LEU E  48      19.756  77.449  -9.961  1.00 52.05           C  
ANISOU 5696  CA  LEU E  48     7129   7018   5628  -1298    800    105       C  
ATOM   5697  C   LEU E  48      20.792  78.547  -9.760  1.00 50.43           C  
ANISOU 5697  C   LEU E  48     6787   6840   5534  -1107   1005    128       C  
ATOM   5698  O   LEU E  48      21.835  78.556 -10.420  1.00 46.58           O  
ANISOU 5698  O   LEU E  48     6464   6325   4910  -1167   1300    -88       O  
ATOM   5699  CB  LEU E  48      20.307  76.128  -9.424  1.00 45.49           C  
ANISOU 5699  CB  LEU E  48     6319   5965   5001  -1158   1049   -182       C  
ATOM   5700  CG  LEU E  48      20.610  76.033  -7.933  1.00 42.42           C  
ANISOU 5700  CG  LEU E  48     5591   5487   5039   -776   1079   -122       C  
ATOM   5701  CD1 LEU E  48      19.298  76.063  -7.134  1.00 40.70           C  
ANISOU 5701  CD1 LEU E  48     5208   5302   4955   -760    744    110       C  
ATOM   5702  CD2 LEU E  48      21.383  74.760  -7.646  1.00 46.18           C  
ANISOU 5702  CD2 LEU E  48     6111   5739   5698   -623   1381   -358       C  
ATOM   5703  N   LEU E  49      20.505  79.477  -8.860  1.00 45.64           N  
ANISOU 5703  N   LEU E  49     5887   6276   5179   -914    892    361       N  
ATOM   5704  CA  LEU E  49      21.450  80.558  -8.584  1.00 49.19           C  
ANISOU 5704  CA  LEU E  49     6199   6755   5737   -780   1120    355       C  
ATOM   5705  C   LEU E  49      22.424  80.147  -7.489  1.00 46.18           C  
ANISOU 5705  C   LEU E  49     5583   6329   5635   -535   1327    158       C  
ATOM   5706  O   LEU E  49      23.610  80.467  -7.550  1.00 44.89           O  
ANISOU 5706  O   LEU E  49     5370   6197   5487   -478   1603    -10       O  
ATOM   5707  CB  LEU E  49      20.720  81.838  -8.194  1.00 44.91           C  
ANISOU 5707  CB  LEU E  49     5475   6255   5332   -738    984    682       C  
ATOM   5708  CG  LEU E  49      19.764  82.452  -9.221  1.00 44.11           C  
ANISOU 5708  CG  LEU E  49     5522   6231   5008   -927    755   1002       C  
ATOM   5709  CD1 LEU E  49      18.988  83.593  -8.556  1.00 56.91           C  
ANISOU 5709  CD1 LEU E  49     6880   7812   6930   -799    679   1345       C  
ATOM   5710  CD2 LEU E  49      20.497  82.942 -10.457  1.00 51.10           C  
ANISOU 5710  CD2 LEU E  49     6689   7174   5552  -1102    926    958       C  
ATOM   5711  N   SER E  50      21.916  79.411  -6.504  1.00 39.98           N  
ANISOU 5711  N   SER E  50     4641   5490   5058   -405   1186    195       N  
ATOM   5712  CA  SER E  50      22.714  78.964  -5.373  1.00 39.16           C  
ANISOU 5712  CA  SER E  50     4289   5389   5202   -175   1312     96       C  
ATOM   5713  C   SER E  50      21.924  77.955  -4.549  1.00 40.23           C  
ANISOU 5713  C   SER E  50     4367   5429   5490    -90   1130    167       C  
ATOM   5714  O   SER E  50      20.695  77.882  -4.631  1.00 35.05           O  
ANISOU 5714  O   SER E  50     3787   4730   4799   -205    901    299       O  
ATOM   5715  CB  SER E  50      23.068  80.141  -4.461  1.00 38.26           C  
ANISOU 5715  CB  SER E  50     3893   5416   5227   -111   1370    170       C  
ATOM   5716  OG  SER E  50      21.918  80.693  -3.837  1.00 37.79           O  
ANISOU 5716  OG  SER E  50     3742   5343   5272   -151   1178    379       O  
ATOM   5717  N   ASN E  51      22.638  77.186  -3.743  1.00 38.18           N  
ANISOU 5717  N   ASN E  51     3951   5146   5410    115   1235    104       N  
ATOM   5718  CA  ASN E  51      21.984  76.291  -2.797  1.00 35.67           C  
ANISOU 5718  CA  ASN E  51     3569   4734   5252    215   1093    200       C  
ATOM   5719  C   ASN E  51      22.899  76.122  -1.604  1.00 44.77           C  
ANISOU 5719  C   ASN E  51     4419   5999   6592    442   1165    248       C  
ATOM   5720  O   ASN E  51      24.123  76.315  -1.710  1.00 39.10           O  
ANISOU 5720  O   ASN E  51     3562   5396   5899    542   1350    166       O  
ATOM   5721  CB  ASN E  51      21.670  74.938  -3.423  1.00 36.75           C  
ANISOU 5721  CB  ASN E  51     3971   4635   5358    182   1149     92       C  
ATOM   5722  CG  ASN E  51      22.923  74.140  -3.728  1.00 55.03           C  
ANISOU 5722  CG  ASN E  51     6305   6836   7768    349   1466    -65       C  
ATOM   5723  OD1 ASN E  51      23.608  74.390  -4.719  1.00 56.51           O  
ANISOU 5723  OD1 ASN E  51     6613   7027   7831    266   1667   -229       O  
ATOM   5724  ND2 ASN E  51      23.228  73.177  -2.875  1.00 58.35           N  
ANISOU 5724  ND2 ASN E  51     6599   7141   8430    591   1534      6       N  
ATOM   5725  N   ILE E  52      22.306  75.782  -0.465  1.00 39.14           N  
ANISOU 5725  N   ILE E  52     3590   5285   5996    499   1011    392       N  
ATOM   5726  CA  ILE E  52      23.082  75.595   0.741  1.00 43.99           C  
ANISOU 5726  CA  ILE E  52     3915   6067   6733    672   1021    495       C  
ATOM   5727  C   ILE E  52      22.486  74.445   1.525  1.00 37.88           C  
ANISOU 5727  C   ILE E  52     3178   5135   6079    780    921    632       C  
ATOM   5728  O   ILE E  52      21.277  74.260   1.544  1.00 36.76           O  
ANISOU 5728  O   ILE E  52     3203   4838   5924    653    798    650       O  
ATOM   5729  CB  ILE E  52      23.151  76.901   1.571  1.00 37.61           C  
ANISOU 5729  CB  ILE E  52     2876   5539   5876    536    971    534       C  
ATOM   5730  CG1 ILE E  52      24.273  76.821   2.625  1.00 44.92           C  
ANISOU 5730  CG1 ILE E  52     3468   6760   6838    650    993    611       C  
ATOM   5731  CG2 ILE E  52      21.795  77.301   2.132  1.00 35.35           C  
ANISOU 5731  CG2 ILE E  52     2646   5181   5605    370    822    617       C  
ATOM   5732  CD1 ILE E  52      24.371  78.089   3.455  1.00 45.81           C  
ANISOU 5732  CD1 ILE E  52     3495   7100   6811    398    947    531       C  
ATOM   5733  N   SER E  53      23.345  73.637   2.129  1.00 36.01           N  
ANISOU 5733  N   SER E  53     2777   4931   5975   1022    986    747       N  
ATOM   5734  CA  SER E  53      22.861  72.542   2.976  1.00 45.78           C  
ANISOU 5734  CA  SER E  53     4049   6012   7334   1146    914    927       C  
ATOM   5735  C   SER E  53      23.185  72.817   4.441  1.00 45.62           C  
ANISOU 5735  C   SER E  53     3728   6307   7299   1178    765   1150       C  
ATOM   5736  O   SER E  53      24.310  73.229   4.758  1.00 47.35           O  
ANISOU 5736  O   SER E  53     3650   6839   7501   1256    782   1210       O  
ATOM   5737  CB  SER E  53      23.535  71.231   2.564  1.00 53.11           C  
ANISOU 5737  CB  SER E  53     5041   6677   8462   1424   1136    958       C  
ATOM   5738  OG  SER E  53      23.313  70.965   1.194  1.00 61.42           O  
ANISOU 5738  OG  SER E  53     6396   7459   9480   1322   1321    706       O  
ATOM   5739  N   LEU E  54      22.219  72.563   5.324  1.00 42.09           N  
ANISOU 5739  N   LEU E  54     3355   5800   6838   1083    626   1265       N  
ATOM   5740  CA  LEU E  54      22.356  72.894   6.735  1.00 36.97           C  
ANISOU 5740  CA  LEU E  54     2480   5467   6101   1007    484   1451       C  
ATOM   5741  C   LEU E  54      21.910  71.726   7.601  1.00 44.42           C  
ANISOU 5741  C   LEU E  54     3507   6250   7122   1125    419   1690       C  
ATOM   5742  O   LEU E  54      20.995  71.000   7.248  1.00 41.90           O  
ANISOU 5742  O   LEU E  54     3464   5558   6896   1130    465   1638       O  
ATOM   5743  CB  LEU E  54      21.450  74.077   7.078  1.00 34.39           C  
ANISOU 5743  CB  LEU E  54     2182   5235   5650    662    427   1317       C  
ATOM   5744  CG  LEU E  54      21.630  75.364   6.271  1.00 39.65           C  
ANISOU 5744  CG  LEU E  54     2813   5998   6254    508    518   1103       C  
ATOM   5745  CD1 LEU E  54      20.445  76.314   6.561  1.00 37.86           C  
ANISOU 5745  CD1 LEU E  54     2658   5709   6019    219    514   1019       C  
ATOM   5746  CD2 LEU E  54      22.973  75.970   6.649  1.00 38.79           C  
ANISOU 5746  CD2 LEU E  54     2481   6251   6008    488    543   1071       C  
ATOM   5747  N   ASP E  55      22.545  71.546   8.746  1.00 44.01           N  
ANISOU 5747  N   ASP E  55     3217   6498   7006   1190    310   1962       N  
ATOM   5748  CA  ASP E  55      21.977  70.620   9.720  1.00 41.15           C  
ANISOU 5748  CA  ASP E  55     2962   6011   6663   1231    234   2212       C  
ATOM   5749  C   ASP E  55      21.001  71.374  10.603  1.00 40.04           C  
ANISOU 5749  C   ASP E  55     2885   5996   6331    844    136   2131       C  
ATOM   5750  O   ASP E  55      20.840  72.587  10.447  1.00 41.93           O  
ANISOU 5750  O   ASP E  55     3063   6401   6466    583    153   1902       O  
ATOM   5751  CB  ASP E  55      23.071  69.875  10.513  1.00 46.45           C  
ANISOU 5751  CB  ASP E  55     3365   6916   7366   1515    156   2630       C  
ATOM   5752  CG  ASP E  55      23.966  70.793  11.338  1.00 56.12           C  
ANISOU 5752  CG  ASP E  55     4278   8738   8308   1310     -9   2692       C  
ATOM   5753  OD1 ASP E  55      23.516  71.854  11.797  1.00 53.74           O  
ANISOU 5753  OD1 ASP E  55     3916   8704   7800    947    -72   2544       O  
ATOM   5754  OD2 ASP E  55      25.142  70.419  11.569  1.00 66.70           O  
ANISOU 5754  OD2 ASP E  55     5448  10263   9631   1477    -47   2874       O  
ATOM   5755  N   ASP E  56      20.330  70.663  11.508  1.00 38.96           N  
ANISOU 5755  N   ASP E  56     4808   5346   4647     55   -723   1967       N  
ATOM   5756  CA  ASP E  56      19.305  71.266  12.350  1.00 40.94           C  
ANISOU 5756  CA  ASP E  56     5145   5617   4792   -201   -746   1843       C  
ATOM   5757  C   ASP E  56      19.823  72.447  13.175  1.00 47.65           C  
ANISOU 5757  C   ASP E  56     5850   6681   5573   -310   -926   1887       C  
ATOM   5758  O   ASP E  56      19.194  73.503  13.216  1.00 37.59           O  
ANISOU 5758  O   ASP E  56     4531   5468   4284   -486   -934   1732       O  
ATOM   5759  CB  ASP E  56      18.701  70.223  13.281  1.00 37.18           C  
ANISOU 5759  CB  ASP E  56     4945   4977   4204   -252   -678   1889       C  
ATOM   5760  CG  ASP E  56      17.754  70.837  14.297  1.00 40.92           C  
ANISOU 5760  CG  ASP E  56     5503   5495   4551   -505   -687   1784       C  
ATOM   5761  OD1 ASP E  56      16.634  71.219  13.880  1.00 44.60           O  
ANISOU 5761  OD1 ASP E  56     5968   5928   5051   -653   -582   1581       O  
ATOM   5762  OD2 ASP E  56      18.118  70.942  15.494  1.00 40.10           O  
ANISOU 5762  OD2 ASP E  56     5462   5466   4307   -552   -796   1903       O  
ATOM   5763  N   SER E  57      20.965  72.267  13.834  1.00 45.07           N  
ANISOU 5763  N   SER E  57     5457   6467   5202   -206  -1072   2098       N  
ATOM   5764  CA  SER E  57      21.533  73.337  14.645  1.00 50.28           C  
ANISOU 5764  CA  SER E  57     5996   7315   5794   -336  -1229   2085       C  
ATOM   5765  C   SER E  57      21.856  74.580  13.802  1.00 47.02           C  
ANISOU 5765  C   SER E  57     5357   7013   5495   -395  -1244   1969       C  
ATOM   5766  O   SER E  57      21.580  75.717  14.202  1.00 41.28           O  
ANISOU 5766  O   SER E  57     4615   6354   4715   -592  -1296   1857       O  
ATOM   5767  CB  SER E  57      22.782  72.843  15.387  1.00 57.33           C  
ANISOU 5767  CB  SER E  57     6837   8281   6666   -199  -1326   2226       C  
ATOM   5768  OG  SER E  57      23.400  73.905  16.090  1.00 57.23           O  
ANISOU 5768  OG  SER E  57     6706   8437   6601   -348  -1458   2184       O  
ATOM   5769  N   GLU E  58      22.428  74.362  12.624  1.00 36.80           N  
ANISOU 5769  N   GLU E  58     3916   5716   4349   -224  -1176   1994       N  
ATOM   5770  CA  GLU E  58      22.745  75.474  11.731  1.00 40.34           C  
ANISOU 5770  CA  GLU E  58     4184   6243   4898   -276  -1156   1894       C  
ATOM   5771  C   GLU E  58      21.498  76.190  11.254  1.00 43.90           C  
ANISOU 5771  C   GLU E  58     4694   6644   5343   -418  -1116   1746       C  
ATOM   5772  O   GLU E  58      21.445  77.419  11.242  1.00 38.58           O  
ANISOU 5772  O   GLU E  58     3967   6017   4675   -561  -1137   1638       O  
ATOM   5773  CB  GLU E  58      23.561  75.003  10.534  1.00 45.66           C  
ANISOU 5773  CB  GLU E  58     4719   6923   5708    -62  -1066   1955       C  
ATOM   5774  CG  GLU E  58      24.957  74.567  10.894  1.00 59.35           C  
ANISOU 5774  CG  GLU E  58     6330   8749   7473     76  -1108   2090       C  
ATOM   5775  CD  GLU E  58      25.682  73.978   9.716  1.00 60.04           C  
ANISOU 5775  CD  GLU E  58     6298   8830   7684    307   -989   2156       C  
ATOM   5776  OE1 GLU E  58      25.008  73.421   8.829  1.00 47.50           O  
ANISOU 5776  OE1 GLU E  58     4799   7117   6130    409   -873   2133       O  
ATOM   5777  OE2 GLU E  58      26.921  74.078   9.666  1.00 60.04           O  
ANISOU 5777  OE2 GLU E  58     6119   8955   7740    381  -1006   2235       O  
ATOM   5778  N   ALA E  59      20.492  75.423  10.855  1.00 32.76           N  
ANISOU 5778  N   ALA E  59     3429   5085   3935   -380   -996   1677       N  
ATOM   5779  CA  ALA E  59      19.255  76.015  10.405  1.00 29.97           C  
ANISOU 5779  CA  ALA E  59     3131   4660   3596   -501   -908   1475       C  
ATOM   5780  C   ALA E  59      18.614  76.879  11.481  1.00 33.87           C  
ANISOU 5780  C   ALA E  59     3695   5181   3992   -699   -955   1384       C  
ATOM   5781  O   ALA E  59      18.091  77.954  11.169  1.00 33.71           O  
ANISOU 5781  O   ALA E  59     3632   5173   4002   -789   -940   1258       O  
ATOM   5782  CB  ALA E  59      18.274  74.929   9.939  1.00 32.48           C  
ANISOU 5782  CB  ALA E  59     3602   4813   3926   -461   -760   1390       C  
ATOM   5783  N   ARG E  60      18.624  76.391  12.724  1.00 35.71           N  
ANISOU 5783  N   ARG E  60     4058   5410   4101   -755   -997   1450       N  
ATOM   5784  CA  ARG E  60      18.015  77.121  13.839  1.00 32.80           C  
ANISOU 5784  CA  ARG E  60     3794   5059   3607   -946  -1018   1358       C  
ATOM   5785  C   ARG E  60      18.803  78.391  14.205  1.00 45.39           C  
ANISOU 5785  C   ARG E  60     5293   6788   5167  -1050  -1162   1371       C  
ATOM   5786  O   ARG E  60      18.207  79.394  14.596  1.00 35.86           O  
ANISOU 5786  O   ARG E  60     4145   5567   3913  -1194  -1139   1232       O  
ATOM   5787  CB  ARG E  60      17.789  76.212  15.066  1.00 32.64           C  
ANISOU 5787  CB  ARG E  60     3972   4996   3433   -991  -1011   1429       C  
ATOM   5788  CG  ARG E  60      16.583  75.290  14.900  1.00 36.43           C  
ANISOU 5788  CG  ARG E  60     4592   5321   3927   -996   -829   1342       C  
ATOM   5789  CD  ARG E  60      16.288  74.453  16.151  1.00 41.77           C  
ANISOU 5789  CD  ARG E  60     5495   5939   4436  -1069   -798   1414       C  
ATOM   5790  NE  ARG E  60      17.351  73.485  16.404  1.00 43.82           N  
ANISOU 5790  NE  ARG E  60     5798   6193   4658   -922   -895   1641       N  
ATOM   5791  CZ  ARG E  60      18.334  73.656  17.283  1.00 46.61           C  
ANISOU 5791  CZ  ARG E  60     6147   6671   4890   -917  -1073   1799       C  
ATOM   5792  NH1 ARG E  60      18.394  74.753  18.013  1.00 43.92           N  
ANISOU 5792  NH1 ARG E  60     5794   6457   4437  -1082  -1168   1737       N  
ATOM   5793  NH2 ARG E  60      19.261  72.722  17.431  1.00 47.35           N  
ANISOU 5793  NH2 ARG E  60     6255   6764   4970   -743  -1157   2023       N  
ATOM   5794  N   GLN E  61      20.132  78.353  14.085  1.00 37.33           N  
ANISOU 5794  N   GLN E  61     4128   5881   4176   -979  -1289   1525       N  
ATOM   5795  CA  GLN E  61      20.934  79.546  14.323  1.00 41.38           C  
ANISOU 5795  CA  GLN E  61     4564   6458   4700  -1081  -1343   1480       C  
ATOM   5796  C   GLN E  61      20.647  80.624  13.269  1.00 36.85           C  
ANISOU 5796  C   GLN E  61     3919   5843   4241  -1103  -1270   1362       C  
ATOM   5797  O   GLN E  61      20.502  81.803  13.590  1.00 40.77           O  
ANISOU 5797  O   GLN E  61     4464   6329   4698  -1251  -1286   1265       O  
ATOM   5798  CB  GLN E  61      22.435  79.218  14.330  1.00 44.27           C  
ANISOU 5798  CB  GLN E  61     4785   6913   5121   -976  -1400   1615       C  
ATOM   5799  CG  GLN E  61      22.895  78.384  15.501  1.00 52.83           C  
ANISOU 5799  CG  GLN E  61     5934   8050   6089   -956  -1496   1733       C  
ATOM   5800  CD  GLN E  61      24.396  78.153  15.467  1.00 66.07           C  
ANISOU 5800  CD  GLN E  61     7430   9843   7832   -847  -1563   1861       C  
ATOM   5801  OE1 GLN E  61      24.895  77.382  14.652  1.00 77.15           O  
ANISOU 5801  OE1 GLN E  61     8720  11242   9353   -641  -1506   1946       O  
ATOM   5802  NE2 GLN E  61      25.123  78.838  16.342  1.00 60.19           N  
ANISOU 5802  NE2 GLN E  61     6658   9207   7003   -991  -1684   1874       N  
ATOM   5803  N   ILE E  62      20.579  80.221  12.002  1.00 34.99           N  
ANISOU 5803  N   ILE E  62     3588   5571   4134   -952  -1187   1374       N  
ATOM   5804  CA  ILE E  62      20.264  81.147  10.945  1.00 30.96           C  
ANISOU 5804  CA  ILE E  62     3033   5013   3718   -950  -1113   1277       C  
ATOM   5805  C   ILE E  62      18.843  81.685  11.070  1.00 39.05           C  
ANISOU 5805  C   ILE E  62     4150   5971   4716  -1045  -1079   1133       C  
ATOM   5806  O   ILE E  62      18.593  82.870  10.813  1.00 38.83           O  
ANISOU 5806  O   ILE E  62     4135   5901   4718  -1109  -1056   1044       O  
ATOM   5807  CB  ILE E  62      20.470  80.495   9.583  1.00 33.53           C  
ANISOU 5807  CB  ILE E  62     3261   5323   4154   -773  -1032   1321       C  
ATOM   5808  CG1 ILE E  62      21.964  80.197   9.397  1.00 40.29           C  
ANISOU 5808  CG1 ILE E  62     3998   6259   5051