CNRS Nantes University UFIP UFIP
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***  4o6b  ***

elNémo ID: 20012722013310930

Job options:

ID        	=	 20012722013310930
JOBID     	=	 4o6b
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4o6b

HEADER    VIRAL PROTEIN                           20-DEC-13   4O6B              
TITLE     DENGUE TYPE2 VIRUS NON-STRUCTURAL PROTEIN 1 (NS1) FORM 1 CRYSTAL      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 1;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NS1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 2;                                 
SOURCE   3 ORGANISM_COMMON: DENV-2;                                             
SOURCE   4 ORGANISM_TAXID: 31634;                                               
SOURCE   5 STRAIN: THAILAND/16681/1984;                                         
SOURCE   6 GENE: NS1;                                                           
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PH-OP64-7                                 
KEYWDS    FLAVIVIRUS, NON-STRUCTURAL PROTEIN 1, NS1, VIRAL PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.L.AKEY,J.L.SMITH                                                    
REVDAT   3   22-NOV-17 4O6B    1       REMARK                                   
REVDAT   2   12-MAR-14 4O6B    1       JRNL                                     
REVDAT   1   19-FEB-14 4O6B    0                                                
JRNL        AUTH   D.L.AKEY,W.C.BROWN,S.DUTTA,J.KONWERSKI,J.JOSE,T.J.JURKIW,    
JRNL        AUTH 2 J.DELPROPOSTO,C.M.OGATA,G.SKINIOTIS,R.J.KUHN,J.L.SMITH       
JRNL        TITL   FLAVIVIRUS NS1 STRUCTURES REVEAL SURFACES FOR ASSOCIATIONS   
JRNL        TITL 2 WITH MEMBRANES AND THE IMMUNE SYSTEM.                        
JRNL        REF    SCIENCE                       V. 343   881 2014              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   24505133                                                     
JRNL        DOI    10.1126/SCIENCE.1247749                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 17724                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.360                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1836                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.0119 -  7.0478    0.87     1259   143  0.1507 0.2024        
REMARK   3     2  7.0478 -  5.5970    0.87     1259   139  0.1518 0.2080        
REMARK   3     3  5.5970 -  4.8903    0.87     1244   144  0.1516 0.1688        
REMARK   3     4  4.8903 -  4.4436    0.87     1274   135  0.1471 0.1499        
REMARK   3     5  4.4436 -  4.1253    0.86     1227   133  0.1572 0.1970        
REMARK   3     6  4.1253 -  3.8822    0.84     1223   138  0.1746 0.2139        
REMARK   3     7  3.8822 -  3.6878    0.79     1139   121  0.2186 0.2410        
REMARK   3     8  3.6878 -  3.5273    0.74     1053   117  0.3309 0.3531        
REMARK   3     9  3.5273 -  3.3916    0.86     1243   142  0.2416 0.2644        
REMARK   3    10  3.3916 -  3.2746    0.88     1308   142  0.2501 0.2811        
REMARK   3    11  3.2746 -  3.1722    0.87     1235   139  0.2556 0.2673        
REMARK   3    12  3.1722 -  3.0816    0.87     1252   140  0.2767 0.3318        
REMARK   3    13  3.0816 -  3.0005    0.83     1235   140  0.3137 0.3175        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 73.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.55                          
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: 0.5100                                                   
REMARK   3   OPERATOR: H,-H-K,-L                                                
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           5257                                  
REMARK   3   ANGLE     :  0.712           7127                                  
REMARK   3   CHIRALITY :  0.046            774                                  
REMARK   3   PLANARITY :  0.002            903                                  
REMARK   3   DIHEDRAL  : 12.102           1938                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 33 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0947 -16.2444 -22.1177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0478 T22:   0.1113                                     
REMARK   3      T33:   0.8563 T12:  -0.4173                                     
REMARK   3      T13:  -0.0038 T23:  -0.1364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5806 L22:   3.8425                                     
REMARK   3      L33:   1.6608 L12:   1.5963                                     
REMARK   3      L13:  -0.9792 L23:  -2.5114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3643 S12:  -0.3657 S13:   0.2352                       
REMARK   3      S21:   0.1093 S22:   0.3287 S23:   0.1174                       
REMARK   3      S31:  -1.0318 S32:   0.4446 S33:  -0.0028                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5535 -21.6114  -3.4427              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6042 T22:   0.7171                                     
REMARK   3      T33:   0.6157 T12:   0.1729                                     
REMARK   3      T13:   0.0310 T23:  -0.1529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3198 L22:   9.0765                                     
REMARK   3      L33:   5.9688 L12:   0.9110                                     
REMARK   3      L13:   0.4743 L23:   1.4553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2465 S12:  -0.6866 S13:   0.3523                       
REMARK   3      S21:  -0.0120 S22:  -0.0671 S23:   1.1540                       
REMARK   3      S31:  -0.9701 S32:  -0.7910 S33:  -0.0912                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -27.2796 -28.1855  -4.3907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7015 T22:   0.8156                                     
REMARK   3      T33:   0.5575 T12:  -0.2836                                     
REMARK   3      T13:   0.0716 T23:  -0.0814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2769 L22:   2.3326                                     
REMARK   3      L33:   3.3986 L12:  -1.5176                                     
REMARK   3      L13:  -2.9220 L23:   0.6782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0272 S12:   0.0415 S13:   0.1960                       
REMARK   3      S21:   0.1453 S22:  -0.0604 S23:   0.2781                       
REMARK   3      S31:   0.2938 S32:  -1.3350 S33:   0.1716                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 257 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2285 -34.7666 -18.7159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6609 T22:   0.2721                                     
REMARK   3      T33:   0.5368 T12:  -0.0560                                     
REMARK   3      T13:  -0.1603 T23:   0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2054 L22:   2.0962                                     
REMARK   3      L33:   4.9770 L12:  -1.0151                                     
REMARK   3      L13:  -2.6734 L23:   1.0250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2928 S12:  -0.3107 S13:   0.0553                       
REMARK   3      S21:  -0.0920 S22:   0.3506 S23:  -0.0220                       
REMARK   3      S31:   0.9224 S32:   0.1006 S33:  -0.0390                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 258 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0902 -40.6390  -1.6196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0481 T22:   0.7174                                     
REMARK   3      T33:   0.5346 T12:   0.2565                                     
REMARK   3      T13:  -0.1396 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8532 L22:   0.9414                                     
REMARK   3      L33:   3.6573 L12:   0.3133                                     
REMARK   3      L13:   0.8333 L23:  -0.4012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0227 S12:  -0.4055 S13:  -0.1235                       
REMARK   3      S21:   0.3147 S22:  -0.0984 S23:  -0.3967                       
REMARK   3      S31:   0.8896 S32:   1.1867 S33:   0.0674                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 31 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6065 -14.9323 -32.0921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1040 T22:   0.5456                                     
REMARK   3      T33:   1.0689 T12:  -0.4813                                     
REMARK   3      T13:   0.0997 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6914 L22:   3.0383                                     
REMARK   3      L33:   4.2082 L12:   0.2542                                     
REMARK   3      L13:   1.9398 L23:   2.9078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2315 S12:   0.1965 S13:   1.0823                       
REMARK   3      S21:  -0.3650 S22:  -0.2267 S23:   0.7485                       
REMARK   3      S31:  -1.9039 S32:   0.4781 S33:   0.1744                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 52 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5233 -35.4739 -48.5575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4675 T22:   1.4537                                     
REMARK   3      T33:   1.1886 T12:   0.1361                                     
REMARK   3      T13:  -0.1844 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8977 L22:   5.3205                                     
REMARK   3      L33:   8.1787 L12:   3.8029                                     
REMARK   3      L13:  -0.6701 L23:   0.1398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2313 S12:   0.3062 S13:  -0.8085                       
REMARK   3      S21:   0.1329 S22:  -0.6311 S23:  -0.8042                       
REMARK   3      S31:  -0.1069 S32:   2.4415 S33:   0.2116                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4832 -31.8409 -53.7997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6424 T22:   1.0352                                     
REMARK   3      T33:   0.8426 T12:  -0.1355                                     
REMARK   3      T13:  -0.0719 T23:   0.2433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1638 L22:   4.4241                                     
REMARK   3      L33:   6.6378 L12:  -4.5649                                     
REMARK   3      L13:  -1.2691 L23:   2.6080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2921 S12:  -0.7880 S13:   0.0164                       
REMARK   3      S21:  -0.7448 S22:   0.5071 S23:  -0.6805                       
REMARK   3      S31:  -0.4437 S32:   0.8956 S33:  -0.3958                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 135 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6976 -38.5548 -56.2173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6807 T22:   1.2994                                     
REMARK   3      T33:   0.7790 T12:   0.1748                                     
REMARK   3      T13:  -0.0160 T23:   0.3376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4287 L22:   3.5401                                     
REMARK   3      L33:   1.6719 L12:  -1.7438                                     
REMARK   3      L13:   0.7104 L23:   1.6566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2996 S12:   0.7667 S13:   0.9230                       
REMARK   3      S21:   0.2105 S22:  -0.6255 S23:  -1.3738                       
REMARK   3      S31:   0.6392 S32:   1.4431 S33:   0.3565                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 180 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4542 -36.0276 -45.6780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5104 T22:   0.6819                                     
REMARK   3      T33:   0.5494 T12:   0.1219                                     
REMARK   3      T13:   0.0809 T23:  -0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0426 L22:   5.4581                                     
REMARK   3      L33:   6.3769 L12:   0.1305                                     
REMARK   3      L13:   0.4889 L23:  -0.1477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4170 S12:   0.3874 S13:   0.0874                       
REMARK   3      S21:   0.1820 S22:  -0.3116 S23:  -0.0867                       
REMARK   3      S31:   0.5492 S32:   0.5284 S33:  -0.2869                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 196 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4987 -27.4109 -31.6552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7402 T22:   0.1873                                     
REMARK   3      T33:   0.7154 T12:  -0.2815                                     
REMARK   3      T13:  -0.1549 T23:   0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3574 L22:   2.5985                                     
REMARK   3      L33:   0.6164 L12:  -0.3636                                     
REMARK   3      L13:  -0.0707 L23:   0.2312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1726 S12:   0.1538 S13:   0.0374                       
REMARK   3      S21:  -0.1361 S22:   0.2320 S23:   0.1696                       
REMARK   3      S31:  -0.1332 S32:   0.0615 S33:   0.3926                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 197 THROUGH 237 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9734 -32.3032 -37.2360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5313 T22:   0.2864                                     
REMARK   3      T33:   0.4527 T12:  -0.1160                                     
REMARK   3      T13:  -0.0828 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8286 L22:   2.2456                                     
REMARK   3      L33:   5.2939 L12:   0.0679                                     
REMARK   3      L13:  -0.1209 L23:  -0.5664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0330 S12:  -0.1239 S13:   0.0250                       
REMARK   3      S21:  -0.0691 S22:   0.0687 S23:   0.2193                       
REMARK   3      S31:   0.2482 S32:   0.0389 S33:   0.1511                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 238 THROUGH 257 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.0767 -38.5709 -39.2806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8601 T22:   0.3894                                     
REMARK   3      T33:   0.6714 T12:  -0.2986                                     
REMARK   3      T13:   0.0267 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2023 L22:   0.2576                                     
REMARK   3      L33:   1.4494 L12:   0.2281                                     
REMARK   3      L13:   0.5373 L23:   0.6050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1829 S12:   0.1040 S13:   0.0886                       
REMARK   3      S21:   0.0187 S22:   0.2678 S23:  -0.3781                       
REMARK   3      S31:   1.0378 S32:  -0.7111 S33:   0.0068                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 258 THROUGH 292 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4816 -31.7645 -49.4165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6083 T22:   0.7435                                     
REMARK   3      T33:   0.6013 T12:  -0.0686                                     
REMARK   3      T13:  -0.2164 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6796 L22:   2.8691                                     
REMARK   3      L33:   2.8606 L12:   0.6455                                     
REMARK   3      L13:  -0.2640 L23:   0.3245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2839 S12:   1.0753 S13:  -0.1589                       
REMARK   3      S21:  -0.1715 S22:   0.0369 S23:   0.6310                       
REMARK   3      S31:   0.4216 S32:  -1.1397 S33:  -0.3319                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 293 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.7549 -32.0672 -56.0920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6806 T22:   1.0451                                     
REMARK   3      T33:   0.5984 T12:  -0.3982                                     
REMARK   3      T13:  -0.0995 T23:   0.1522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3354 L22:   1.2876                                     
REMARK   3      L33:   3.2267 L12:  -1.4349                                     
REMARK   3      L13:   0.4545 L23:   0.3991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2710 S12:   0.4256 S13:   0.2952                       
REMARK   3      S21:  -0.1621 S22:  -0.1918 S23:   0.2516                       
REMARK   3      S31:   0.5262 S32:  -1.1117 S33:  -0.0806                       
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 4O6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084096.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : K-B PAIR OF BIOMORPH MIRRORS       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17731                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61300                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4O6D                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 3350, 250 MM AMMONIUM FORMATE    
REMARK 280  PH 6.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 278K, PH 5.5     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       87.93950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.77189            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.13967            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       87.93950            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       50.77189            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       27.13967            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       87.93950            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       50.77189            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.13967            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.54379            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       54.27933            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      101.54379            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       54.27933            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      101.54379            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       54.27933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     VAL A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ASN A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     PHE A    -4                                                      
REMARK 465     GLN A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     TRP A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     PRO A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     LYS A   112                                                      
REMARK 465     TYR A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     TRP A   115                                                      
REMARK 465     LYS A   116                                                      
REMARK 465     THR A   117                                                      
REMARK 465     TRP A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     LYS A   122                                                      
REMARK 465     MET A   123                                                      
REMARK 465     LEU A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     THR A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     SER A   128                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     PHE A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     VAL A   162                                                      
REMARK 465     PHE A   163                                                      
REMARK 465     THR A   164                                                      
REMARK 465     THR A   165                                                      
REMARK 465     VAL A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     ALA A   352                                                      
REMARK 465     ALA B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     VAL B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     GLN B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     THR B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     LEU B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     TYR B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     TRP B   115                                                      
REMARK 465     LYS B   116                                                      
REMARK 465     THR B   117                                                      
REMARK 465     TRP B   118                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     LYS B   120                                                      
REMARK 465     ALA B   121                                                      
REMARK 465     LYS B   122                                                      
REMARK 465     MET B   123                                                      
REMARK 465     LEU B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     THR B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     SER B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     ASN B   130                                                      
REMARK 465     VAL B   162                                                      
REMARK 465     PHE B   163                                                      
REMARK 465     VAL B   350                                                      
REMARK 465     THR B   351                                                      
REMARK 465     ALA B   352                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   197     NZ   LYS A   221              2.14            
REMARK 500   O    TRP B    68     OG1  THR B    72              2.15            
REMARK 500   NZ   LYS B   172     OD1  ASP B   176              2.19            
REMARK 500   OG   SER B   297     O    TYR B   331              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 136     -144.51     53.83                                   
REMARK 500    ASP A 208      -39.76     68.47                                   
REMARK 500    HIS A 229       33.44    -97.26                                   
REMARK 500    TRP A 232       67.60     64.01                                   
REMARK 500    ASN A 255       27.89    -79.61                                   
REMARK 500    THR A 265       61.35   -106.17                                   
REMARK 500    SER A 315        3.63   -153.75                                   
REMARK 500    ASN A 347     -169.07   -127.76                                   
REMARK 500    HIS B  26       35.89    -91.10                                   
REMARK 500    GLU B  83       74.35     59.04                                   
REMARK 500    LYS B  85       62.00   -112.38                                   
REMARK 500    ASP B 136     -129.48     54.25                                   
REMARK 500    GLU B 156      -61.15    -95.89                                   
REMARK 500    ASP B 197     -159.76   -154.36                                   
REMARK 500    LEU B 206       78.98   -118.54                                   
REMARK 500    ASP B 208      -66.44     60.74                                   
REMARK 500    ASP B 281      106.66    -56.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O6C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O6D   RELATED DB: PDB                                   
DBREF  4O6B A    0   352  UNP    P29990   POLG_DEN26     775   1127             
DBREF  4O6B B    0   352  UNP    P29990   POLG_DEN26     775   1127             
SEQADV 4O6B ALA A  -23  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -22  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -21  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -20  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -19  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -18  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS A  -17  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER A  -16  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER A  -15  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLY A  -14  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B VAL A  -13  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASP A  -12  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B LEU A  -11  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLY A  -10  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B THR A   -9  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLU A   -8  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASN A   -7  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B LEU A   -6  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B TYR A   -5  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B PHE A   -4  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLN A   -3  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER A   -2  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASN A   -1  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ALA B  -23  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -22  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -21  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -20  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -19  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -18  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B HIS B  -17  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER B  -16  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER B  -15  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLY B  -14  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B VAL B  -13  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASP B  -12  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B LEU B  -11  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLY B  -10  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B THR B   -9  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLU B   -8  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASN B   -7  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B LEU B   -6  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B TYR B   -5  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B PHE B   -4  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B GLN B   -3  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B SER B   -2  UNP  P29990              EXPRESSION TAG                 
SEQADV 4O6B ASN B   -1  UNP  P29990              EXPRESSION TAG                 
SEQRES   1 A  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP SER          
SEQRES   3 A  376  GLY CYS VAL VAL SER TRP LYS ASN LYS GLU LEU LYS CYS          
SEQRES   4 A  376  GLY SER GLY ILE PHE ILE THR ASP ASN VAL HIS THR TRP          
SEQRES   5 A  376  THR GLU GLN TYR LYS PHE GLN PRO GLU SER PRO SER LYS          
SEQRES   6 A  376  LEU ALA SER ALA ILE GLN LYS ALA HIS GLU GLU GLY ILE          
SEQRES   7 A  376  CYS GLY ILE ARG SER VAL THR ARG LEU GLU ASN LEU MET          
SEQRES   8 A  376  TRP LYS GLN ILE THR PRO GLU LEU ASN HIS ILE LEU SER          
SEQRES   9 A  376  GLU ASN GLU VAL LYS LEU THR ILE MET THR GLY ASP ILE          
SEQRES  10 A  376  LYS GLY ILE MET GLN ALA GLY LYS ARG SER LEU ARG PRO          
SEQRES  11 A  376  GLN PRO THR GLU LEU LYS TYR SER TRP LYS THR TRP GLY          
SEQRES  12 A  376  LYS ALA LYS MET LEU SER THR GLU SER HIS ASN GLN THR          
SEQRES  13 A  376  PHE LEU ILE ASP GLY PRO GLU THR ALA GLU CYS PRO ASN          
SEQRES  14 A  376  THR ASN ARG ALA TRP ASN SER LEU GLU VAL GLU ASP TYR          
SEQRES  15 A  376  GLY PHE GLY VAL PHE THR THR ASN ILE TRP LEU LYS LEU          
SEQRES  16 A  376  LYS GLU LYS GLN ASP VAL PHE CYS ASP SER LYS LEU MET          
SEQRES  17 A  376  SER ALA ALA ILE LYS ASP ASN ARG ALA VAL HIS ALA ASP          
SEQRES  18 A  376  MET GLY TYR TRP ILE GLU SER ALA LEU ASN ASP THR TRP          
SEQRES  19 A  376  LYS ILE GLU LYS ALA SER PHE ILE GLU VAL LYS ASN CYS          
SEQRES  20 A  376  HIS TRP PRO LYS SER HIS THR LEU TRP SER ASN GLY VAL          
SEQRES  21 A  376  LEU GLU SER GLU MET ILE ILE PRO LYS ASN LEU ALA GLY          
SEQRES  22 A  376  PRO VAL SER GLN HIS ASN TYR ARG PRO GLY TYR HIS THR          
SEQRES  23 A  376  GLN ILE THR GLY PRO TRP HIS LEU GLY LYS LEU GLU MET          
SEQRES  24 A  376  ASP PHE ASP PHE CYS ASP GLY THR THR VAL VAL VAL THR          
SEQRES  25 A  376  GLU ASP CYS GLY ASN ARG GLY PRO SER LEU ARG THR THR          
SEQRES  26 A  376  THR ALA SER GLY LYS LEU ILE THR GLU TRP CYS CYS ARG          
SEQRES  27 A  376  SER CYS THR LEU PRO PRO LEU ARG TYR ARG GLY GLU ASP          
SEQRES  28 A  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO LEU LYS GLU          
SEQRES  29 A  376  LYS GLU GLU ASN LEU VAL ASN SER LEU VAL THR ALA              
SEQRES   1 B  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP SER          
SEQRES   3 B  376  GLY CYS VAL VAL SER TRP LYS ASN LYS GLU LEU LYS CYS          
SEQRES   4 B  376  GLY SER GLY ILE PHE ILE THR ASP ASN VAL HIS THR TRP          
SEQRES   5 B  376  THR GLU GLN TYR LYS PHE GLN PRO GLU SER PRO SER LYS          
SEQRES   6 B  376  LEU ALA SER ALA ILE GLN LYS ALA HIS GLU GLU GLY ILE          
SEQRES   7 B  376  CYS GLY ILE ARG SER VAL THR ARG LEU GLU ASN LEU MET          
SEQRES   8 B  376  TRP LYS GLN ILE THR PRO GLU LEU ASN HIS ILE LEU SER          
SEQRES   9 B  376  GLU ASN GLU VAL LYS LEU THR ILE MET THR GLY ASP ILE          
SEQRES  10 B  376  LYS GLY ILE MET GLN ALA GLY LYS ARG SER LEU ARG PRO          
SEQRES  11 B  376  GLN PRO THR GLU LEU LYS TYR SER TRP LYS THR TRP GLY          
SEQRES  12 B  376  LYS ALA LYS MET LEU SER THR GLU SER HIS ASN GLN THR          
SEQRES  13 B  376  PHE LEU ILE ASP GLY PRO GLU THR ALA GLU CYS PRO ASN          
SEQRES  14 B  376  THR ASN ARG ALA TRP ASN SER LEU GLU VAL GLU ASP TYR          
SEQRES  15 B  376  GLY PHE GLY VAL PHE THR THR ASN ILE TRP LEU LYS LEU          
SEQRES  16 B  376  LYS GLU LYS GLN ASP VAL PHE CYS ASP SER LYS LEU MET          
SEQRES  17 B  376  SER ALA ALA ILE LYS ASP ASN ARG ALA VAL HIS ALA ASP          
SEQRES  18 B  376  MET GLY TYR TRP ILE GLU SER ALA LEU ASN ASP THR TRP          
SEQRES  19 B  376  LYS ILE GLU LYS ALA SER PHE ILE GLU VAL LYS ASN CYS          
SEQRES  20 B  376  HIS TRP PRO LYS SER HIS THR LEU TRP SER ASN GLY VAL          
SEQRES  21 B  376  LEU GLU SER GLU MET ILE ILE PRO LYS ASN LEU ALA GLY          
SEQRES  22 B  376  PRO VAL SER GLN HIS ASN TYR ARG PRO GLY TYR HIS THR          
SEQRES  23 B  376  GLN ILE THR GLY PRO TRP HIS LEU GLY LYS LEU GLU MET          
SEQRES  24 B  376  ASP PHE ASP PHE CYS ASP GLY THR THR VAL VAL VAL THR          
SEQRES  25 B  376  GLU ASP CYS GLY ASN ARG GLY PRO SER LEU ARG THR THR          
SEQRES  26 B  376  THR ALA SER GLY LYS LEU ILE THR GLU TRP CYS CYS ARG          
SEQRES  27 B  376  SER CYS THR LEU PRO PRO LEU ARG TYR ARG GLY GLU ASP          
SEQRES  28 B  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO LEU LYS GLU          
SEQRES  29 B  376  LYS GLU GLU ASN LEU VAL ASN SER LEU VAL THR ALA              
MODRES 4O6B ASN A  207  ASN  GLYCOSYLATION SITE                                 
MODRES 4O6B ASN B  207  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 401      14                                                       
HET    NAG  B 401      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  NAG    2(C8 H15 N O6)                                               
HELIX    1   1 SER A   38  GLU A   52  1                                  15    
HELIX    2   2 THR A   61  ASN A   82  1                                  22    
HELIX    3   3 PRO A  144  ARG A  148  5                                   5    
HELIX    4   4 PRO A  244  ALA A  248  5                                   5    
HELIX    5   5 PRO A  267  GLY A  271  5                                   5    
HELIX    6   6 LYS A  341  LEU A  345  5                                   5    
HELIX    7   7 SER B   38  GLY B   53  1                                  16    
HELIX    8   8 THR B   61  ASN B   82  1                                  22    
HELIX    9   9 PRO B  144  THR B  146  5                                   3    
HELIX   10  10 ASP B  180  MET B  184  5                                   5    
HELIX   11  11 PRO B  244  ALA B  248  5                                   5    
HELIX   12  12 LYS B  341  LEU B  345  5                                   5    
SHEET    1   A 5 ASP A   1  VAL A   6  0                                        
SHEET    2   A 5 LEU A  13  THR A  22 -1  O  LYS A  14   N  VAL A   5           
SHEET    3   A 5 GLU B  12  THR B  22 -1  O  ILE B  19   N  ILE A  21           
SHEET    4   A 5 SER B   2  SER B   7 -1  N  SER B   7   O  GLU B  12           
SHEET    5   A 5 ASP A   1  VAL A   6 -1  N  VAL A   6   O  SER B   2           
SHEET    1   B 3 PHE A  34  GLN A  35  0                                        
SHEET    2   B 3 ILE A 167  LEU A 171  1  O  LEU A 169   N  GLN A  35           
SHEET    3   B 3 LEU A 153  ASP A 157 -1  N  GLU A 154   O  LYS A 170           
SHEET    1   C 2 THR A  87  THR A  90  0                                        
SHEET    2   C 2 THR A 132  ILE A 135  1  O  PHE A 133   N  MET A  89           
SHEET    1   D 2 ILE A  96  MET A  97  0                                        
SHEET    2   D 2 VAL A 220  LYS A 221  1  O  VAL A 220   N  MET A  97           
SHEET    1   E15 LEU A 298  ARG A 299  0                                        
SHEET    2   E15 CYS A 329  TYR A 331 -1  O  TYR A 331   N  LEU A 298           
SHEET    3   E15 LEU A 321  ARG A 324 -1  N  TYR A 323   O  TRP A 330           
SHEET    4   E15 LEU A 273  PHE A 277 -1  N  ASP A 276   O  ARG A 322           
SHEET    5   E15 TRP A 210  PHE A 217 -1  N  PHE A 217   O  LEU A 273           
SHEET    6   E15 TYR A 200  LEU A 206 -1  N  GLU A 203   O  GLU A 213           
SHEET    7   E15 ARG A 192  ALA A 196 -1  N  HIS A 195   O  ILE A 202           
SHEET    8   E15 SER A 185  LYS A 189 -1  N  ALA A 187   O  VAL A 194           
SHEET    9   E15 SER B 185  LYS B 189 -1  O  ALA B 186   N  ILE A 188           
SHEET   10   E15 ARG B 192  ALA B 196 -1  O  ALA B 196   N  SER B 185           
SHEET   11   E15 TYR B 200  LEU B 206 -1  O  SER B 204   N  ALA B 193           
SHEET   12   E15 TRP B 210  PHE B 217 -1  O  GLU B 213   N  GLU B 203           
SHEET   13   E15 LEU B 273  PHE B 277 -1  O  LEU B 273   N  PHE B 217           
SHEET   14   E15 LEU B 321  ARG B 324 -1  O  ARG B 322   N  ASP B 276           
SHEET   15   E15 CYS B 329  TYR B 331 -1  O  TRP B 330   N  TYR B 323           
SHEET    1   F 3 THR A 284  VAL A 287  0                                        
SHEET    2   F 3 GLU A 310  CYS A 313  1  O  TRP A 311   N  THR A 284           
SHEET    3   F 3 ILE A 335  PRO A 337 -1  O  ARG A 336   N  CYS A 312           
SHEET    1   G 2 TYR B  32  PHE B  34  0                                        
SHEET    2   G 2 THR B 165  ILE B 167  1  O  THR B 165   N  LYS B  33           
SHEET    1   H 4 THR B  87  THR B  90  0                                        
SHEET    2   H 4 THR B 132  ILE B 135  1  O  PHE B 133   N  THR B  87           
SHEET    3   H 4 GLY B  56  ILE B  57  1  N  ILE B  57   O  LEU B 134           
SHEET    4   H 4 ARG B 148  ALA B 149  1  O  ALA B 149   N  GLY B  56           
SHEET    1   I 2 ILE B  96  MET B  97  0                                        
SHEET    2   I 2 VAL B 220  LYS B 221  1  O  VAL B 220   N  MET B  97           
SHEET    1   J 2 LEU B 153  GLU B 154  0                                        
SHEET    2   J 2 LYS B 170  LEU B 171 -1  O  LYS B 170   N  GLU B 154           
SHEET    1   K 3 THR B 284  VAL B 287  0                                        
SHEET    2   K 3 GLU B 310  CYS B 313  1  O  TRP B 311   N  THR B 284           
SHEET    3   K 3 ARG B 336  PRO B 337 -1  O  ARG B 336   N  CYS B 312           
SSBOND   1 CYS A    4    CYS A   15                          1555   1555  2.03  
SSBOND   2 CYS A   55    CYS A  143                          1555   1555  2.03  
SSBOND   3 CYS A  179    CYS A  223                          1555   1555  2.03  
SSBOND   4 CYS A  280    CYS A  329                          1555   1555  2.03  
SSBOND   5 CYS A  291    CYS A  312                          1555   1555  2.03  
SSBOND   6 CYS A  313    CYS A  316                          1555   1555  2.03  
SSBOND   7 CYS B    4    CYS B   15                          1555   1555  2.03  
SSBOND   8 CYS B   55    CYS B  143                          1555   1555  2.03  
SSBOND   9 CYS B  179    CYS B  223                          1555   1555  2.03  
SSBOND  10 CYS B  280    CYS B  329                          1555   1555  2.03  
SSBOND  11 CYS B  291    CYS B  312                          1555   1555  2.03  
SSBOND  12 CYS B  313    CYS B  316                          1555   1555  2.02  
LINK         ND2 ASN A 207                 C1  NAG A 401     1555   1555  1.45  
LINK         ND2 ASN B 207                 C1  NAG B 401     1555   1555  1.46  
CISPEP   1 LEU A  318    PRO A  319          0        -1.53                     
CISPEP   2 LEU B  318    PRO B  319          0        -0.05                     
SITE     1 AC1  2 ASN A 207  ASP A 208                                          
SITE     1 AC2  1 ASN B 207                                                     
CRYST1  175.879  175.879   81.419  90.00  90.00 120.00 H 3          18          
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      0.005686  0.003283  0.000000        0.00000                         
SCALE2      0.000000  0.006565  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012282        0.00000                         
ATOM      1  N   ALA A   0     -14.523 -16.148 -34.110  1.00 87.67           N  
ANISOU    1  N   ALA A   0    13388   7036  12885  -2271   -537   1429       N  
ATOM      2  CA  ALA A   0     -13.199 -16.571 -33.664  1.00 85.79           C  
ANISOU    2  CA  ALA A   0    13130   6868  12599  -2300   -488   1059       C  
ATOM      3  C   ALA A   0     -12.522 -15.503 -32.814  1.00 85.84           C  
ANISOU    3  C   ALA A   0    13087   6758  12771  -2229   -210    944       C  
ATOM      4  O   ALA A   0     -12.959 -14.353 -32.769  1.00 87.84           O  
ANISOU    4  O   ALA A   0    13340   6851  13184  -2181    -22   1132       O  
ATOM      5  CB  ALA A   0     -12.325 -16.930 -34.851  1.00 85.95           C  
ANISOU    5  CB  ALA A   0    13251   7000  12406  -2506   -632    901       C  
ATOM      6  N   ASP A   1     -11.445 -15.893 -32.145  1.00 84.12           N  
ANISOU    6  N   ASP A   1    12815   6617  12531  -2228   -202    647       N  
ATOM      7  CA  ASP A   1     -10.702 -14.978 -31.294  1.00 83.80           C  
ANISOU    7  CA  ASP A   1    12720   6500  12619  -2193    -52    521       C  
ATOM      8  C   ASP A   1      -9.415 -14.547 -31.978  1.00 83.89           C  
ANISOU    8  C   ASP A   1    12813   6579  12483  -2343    -85    343       C  
ATOM      9  O   ASP A   1      -8.496 -15.347 -32.161  1.00 82.52           O  
ANISOU    9  O   ASP A   1    12650   6553  12153  -2408   -173    124       O  
ATOM     10  CB  ASP A   1     -10.395 -15.642 -29.953  1.00 82.32           C  
ANISOU   10  CB  ASP A   1    12431   6371  12477  -2098    -49    349       C  
ATOM     11  CG  ASP A   1     -11.648 -16.064 -29.214  1.00 81.94           C  
ANISOU   11  CG  ASP A   1    12333   6259  12542  -1949     21    528       C  
ATOM     12  OD1 ASP A   1     -12.738 -16.026 -29.821  1.00 83.07           O  
ANISOU   12  OD1 ASP A   1    12539   6345  12677  -1920     26    777       O  
ATOM     13  OD2 ASP A   1     -11.543 -16.441 -28.028  1.00 80.69           O  
ANISOU   13  OD2 ASP A   1    12096   6119  12443  -1871     60    435       O  
ATOM     14  N   SER A   2      -9.358 -13.280 -32.367  1.00 85.72           N  
ANISOU   14  N   SER A   2    13098   6691  12781  -2394      9    456       N  
ATOM     15  CA  SER A   2      -8.182 -12.753 -33.049  1.00 86.28           C  
ANISOU   15  CA  SER A   2    13273   6817  12693  -2543     13    319       C  
ATOM     16  C   SER A   2      -7.364 -11.883 -32.106  1.00 85.49           C  
ANISOU   16  C   SER A   2    13188   6671  12624  -2536     99    174       C  
ATOM     17  O   SER A   2      -7.909 -11.039 -31.397  1.00 86.87           O  
ANISOU   17  O   SER A   2    13341   6687  12978  -2462    173    289       O  
ATOM     18  CB  SER A   2      -8.590 -11.952 -34.287  1.00 88.81           C  
ANISOU   18  CB  SER A   2    13668   7054  13021  -2645     51    557       C  
ATOM     19  OG  SER A   2      -7.465 -11.644 -35.089  1.00 89.41           O  
ANISOU   19  OG  SER A   2    13854   7209  12908  -2807     55    426       O  
ATOM     20  N   GLY A   3      -6.054 -12.095 -32.096  1.00 83.54           N  
ANISOU   20  N   GLY A   3    12991   6559  12192  -2624     90    -69       N  
ATOM     21  CA  GLY A   3      -5.189 -11.361 -31.198  1.00 64.64           C  
ANISOU   21  CA  GLY A   3    10643   4153   9766  -2649    172   -221       C  
ATOM     22  C   GLY A   3      -3.725 -11.720 -31.318  1.00 75.61           C  
ANISOU   22  C   GLY A   3    12052   5702  10972  -2751    172   -448       C  
ATOM     23  O   GLY A   3      -3.295 -12.337 -32.298  1.00 64.09           O  
ANISOU   23  O   GLY A   3    10599   4341   9412  -2819    129   -486       O  
ATOM     24  N   CYS A   4      -2.960 -11.322 -30.305  1.00 76.27           N  
ANISOU   24  N   CYS A   4    12153   5806  11020  -2774    230   -591       N  
ATOM     25  CA  CYS A   4      -1.517 -11.535 -30.285  1.00 76.93           C  
ANISOU   25  CA  CYS A   4    12227   6023  10981  -2877    246   -772       C  
ATOM     26  C   CYS A   4      -1.024 -12.158 -28.978  1.00 76.77           C  
ANISOU   26  C   CYS A   4    12118   6097  10956  -2846    198   -904       C  
ATOM     27  O   CYS A   4      -1.475 -11.803 -27.885  1.00 76.23           O  
ANISOU   27  O   CYS A   4    12073   5971  10921  -2804    222   -905       O  
ATOM     28  CB  CYS A   4      -0.771 -10.227 -30.557  1.00 78.60           C  
ANISOU   28  CB  CYS A   4    12550   6164  11150  -3008    379   -799       C  
ATOM     29  SG  CYS A   4      -0.806  -9.690 -32.281  1.00160.73           S  
ANISOU   29  SG  CYS A   4    23030  16510  21530  -3104    425   -667       S  
ATOM     30  N   VAL A   5      -0.095 -13.100 -29.114  1.00 77.29           N  
ANISOU   30  N   VAL A   5    12080   6298  10989  -2878    135  -1005       N  
ATOM     31  CA  VAL A   5       0.459 -13.826 -27.976  1.00 77.07           C  
ANISOU   31  CA  VAL A   5    11928   6363  10990  -2865     63  -1099       C  
ATOM     32  C   VAL A   5       1.979 -13.937 -28.131  1.00 78.04           C  
ANISOU   32  C   VAL A   5    11997   6575  11080  -2991     79  -1208       C  
ATOM     33  O   VAL A   5       2.500 -13.974 -29.258  1.00 78.56           O  
ANISOU   33  O   VAL A   5    12082   6654  11114  -3047    120  -1218       O  
ATOM     34  CB  VAL A   5      -0.174 -15.241 -27.851  1.00 88.40           C  
ANISOU   34  CB  VAL A   5    13211   7844  12533  -2735    -70  -1065       C  
ATOM     35  CG1 VAL A   5       0.343 -15.973 -26.623  1.00 87.82           C  
ANISOU   35  CG1 VAL A   5    12991   7851  12525  -2727   -152  -1133       C  
ATOM     36  CG2 VAL A   5      -1.689 -15.154 -27.793  1.00 87.72           C  
ANISOU   36  CG2 VAL A   5    13159   7661  12510  -2619    -81   -932       C  
ATOM     37  N   VAL A   6       2.684 -13.971 -27.000  1.00 78.45           N  
ANISOU   37  N   VAL A   6    11982   6682  11142  -3051     49  -1280       N  
ATOM     38  CA  VAL A   6       4.136 -14.139 -26.987  1.00 79.94           C  
ANISOU   38  CA  VAL A   6    12078   6946  11349  -3179     42  -1357       C  
ATOM     39  C   VAL A   6       4.574 -15.205 -25.978  1.00 79.28           C  
ANISOU   39  C   VAL A   6    11799   6946  11376  -3170    -94  -1380       C  
ATOM     40  O   VAL A   6       4.133 -15.207 -24.829  1.00 78.99           O  
ANISOU   40  O   VAL A   6    11754   6925  11333  -3154   -142  -1380       O  
ATOM     41  CB  VAL A   6       4.861 -12.801 -26.697  1.00 83.13           C  
ANISOU   41  CB  VAL A   6    12596   7317  11672  -3342    145  -1410       C  
ATOM     42  CG1 VAL A   6       4.162 -12.035 -25.582  1.00 83.95           C  
ANISOU   42  CG1 VAL A   6    12821   7365  11712  -3345    177  -1425       C  
ATOM     43  CG2 VAL A   6       6.328 -13.039 -26.365  1.00 84.49           C  
ANISOU   43  CG2 VAL A   6    12634   7568  11899  -3487    103  -1469       C  
ATOM     44  N   SER A   7       5.437 -16.114 -26.420  1.00 78.84           N  
ANISOU   44  N   SER A   7    11586   6934  11436  -3190   -150  -1392       N  
ATOM     45  CA  SER A   7       5.940 -17.181 -25.562  1.00 78.17           C  
ANISOU   45  CA  SER A   7    11279   6905  11515  -3193   -290  -1382       C  
ATOM     46  C   SER A   7       7.225 -16.765 -24.857  1.00 79.64           C  
ANISOU   46  C   SER A   7    11384   7145  11730  -3382   -306  -1409       C  
ATOM     47  O   SER A   7       8.272 -17.387 -25.046  1.00 79.82           O  
ANISOU   47  O   SER A   7    11232   7185  11910  -3453   -358  -1386       O  
ATOM     48  CB  SER A   7       6.195 -18.443 -26.382  1.00 77.46           C  
ANISOU   48  CB  SER A   7    11053   6798  11580  -3125   -351  -1361       C  
ATOM     49  OG  SER A   7       7.095 -18.181 -27.445  1.00 78.54           O  
ANISOU   49  OG  SER A   7    11235   6921  11687  -3218   -246  -1395       O  
ATOM     50  N   LYS A  11      11.505 -17.577 -27.013  1.00113.57           N  
ANISOU   50  N   LYS A  11    15283  11418  16450  -3765   -216  -1335       N  
ATOM     51  CA  LYS A  11      11.061 -16.193 -27.131  1.00114.15           C  
ANISOU   51  CA  LYS A  11    15586  11484  16302  -3789   -105  -1409       C  
ATOM     52  C   LYS A  11      10.550 -15.903 -28.537  1.00114.75           C  
ANISOU   52  C   LYS A  11    15852  11508  16238  -3715     54  -1451       C  
ATOM     53  O   LYS A  11      11.229 -15.260 -29.337  1.00116.22           O  
ANISOU   53  O   LYS A  11    16095  11670  16394  -3821    182  -1464       O  
ATOM     54  CB  LYS A  11      12.197 -15.233 -26.777  1.00115.44           C  
ANISOU   54  CB  LYS A  11    15709  11659  16493  -4001    -84  -1403       C  
ATOM     55  CG  LYS A  11      12.806 -15.458 -25.400  1.00115.63           C  
ANISOU   55  CG  LYS A  11    15530  11749  16654  -4122   -246  -1357       C  
ATOM     56  CD  LYS A  11      13.998 -14.538 -25.187  1.00117.39           C  
ANISOU   56  CD  LYS A  11    15700  11979  16925  -4355   -233  -1344       C  
ATOM     57  CE  LYS A  11      14.824 -14.943 -23.977  1.00118.49           C  
ANISOU   57  CE  LYS A  11    15564  12197  17257  -4508   -396  -1270       C  
ATOM     58  NZ  LYS A  11      16.122 -14.209 -23.918  1.00121.18           N  
ANISOU   58  NZ  LYS A  11    15794  12539  17709  -4748   -395  -1226       N  
ATOM     59  N   GLU A  12       9.346 -16.378 -28.832  1.00113.75           N  
ANISOU   59  N   GLU A  12    15813  11368  16039  -3549     39  -1460       N  
ATOM     60  CA  GLU A  12       8.766 -16.215 -30.157  1.00114.09           C  
ANISOU   60  CA  GLU A  12    16022  11373  15954  -3495    162  -1485       C  
ATOM     61  C   GLU A  12       7.469 -15.426 -30.064  1.00113.71           C  
ANISOU   61  C   GLU A  12    16149  11299  15757  -3415    172  -1458       C  
ATOM     62  O   GLU A  12       6.719 -15.573 -29.101  1.00112.84           O  
ANISOU   62  O   GLU A  12    16015  11196  15662  -3329     74  -1433       O  
ATOM     63  CB  GLU A  12       8.504 -17.584 -30.782  1.00113.31           C  
ANISOU   63  CB  GLU A  12    15862  11262  15927  -3395    130  -1505       C  
ATOM     64  CG  GLU A  12       7.951 -17.552 -32.201  1.00113.71           C  
ANISOU   64  CG  GLU A  12    16085  11285  15835  -3373    248  -1544       C  
ATOM     65  CD  GLU A  12       7.584 -18.936 -32.705  1.00113.56           C  
ANISOU   65  CD  GLU A  12    16026  11244  15877  -3281    203  -1590       C  
ATOM     66  OE1 GLU A  12       7.746 -19.908 -31.938  1.00113.12           O  
ANISOU   66  OE1 GLU A  12    15805  11183  15993  -3224     78  -1572       O  
ATOM     67  OE2 GLU A  12       7.135 -19.051 -33.866  1.00114.08           O  
ANISOU   67  OE2 GLU A  12    16234  11292  15820  -3284    285  -1638       O  
ATOM     68  N   LEU A  13       7.208 -14.588 -31.062  1.00114.77           N  
ANISOU   68  N   LEU A  13    16451  11392  15765  -3454    295  -1446       N  
ATOM     69  CA  LEU A  13       5.974 -13.804 -31.104  1.00114.44           C  
ANISOU   69  CA  LEU A  13    16566  11294  15621  -3391    311  -1383       C  
ATOM     70  C   LEU A  13       5.044 -14.290 -32.217  1.00113.04           C  
ANISOU   70  C   LEU A  13    16468  11097  15383  -3316    311  -1342       C  
ATOM     71  O   LEU A  13       5.497 -14.558 -33.330  1.00113.80           O  
ANISOU   71  O   LEU A  13    16600  11206  15433  -3382    383  -1374       O  
ATOM     72  CB  LEU A  13       6.286 -12.319 -31.310  1.00117.26           C  
ANISOU   72  CB  LEU A  13    17053  11587  15912  -3513    429  -1364       C  
ATOM     73  CG  LEU A  13       6.940 -11.521 -30.179  1.00119.31           C  
ANISOU   73  CG  LEU A  13    17295  11837  16202  -3610    430  -1404       C  
ATOM     74  CD1 LEU A  13       8.441 -11.763 -30.116  1.00120.92           C  
ANISOU   74  CD1 LEU A  13    17361  12096  16486  -3745    430  -1455       C  
ATOM     75  CD2 LEU A  13       6.643 -10.038 -30.338  1.00120.96           C  
ANISOU   75  CD2 LEU A  13    17669  11931  16358  -3678    536  -1369       C  
ATOM     76  N   LYS A  14       3.747 -14.401 -31.926  1.00110.58           N  
ANISOU   76  N   LYS A  14    16190  10752  15073  -3197    235  -1270       N  
ATOM     77  CA  LYS A  14       2.790 -14.813 -32.961  1.00108.56           C  
ANISOU   77  CA  LYS A  14    16010  10473  14766  -3152    211  -1211       C  
ATOM     78  C   LYS A  14       1.422 -14.139 -32.842  1.00105.58           C  
ANISOU   78  C   LYS A  14    15721  10009  14386  -3087    187  -1073       C  
ATOM     79  O   LYS A  14       0.950 -13.850 -31.741  1.00104.79           O  
ANISOU   79  O   LYS A  14    15586   9873  14354  -3012    157  -1042       O  
ATOM     80  CB  LYS A  14       2.628 -16.337 -32.999  1.00108.25           C  
ANISOU   80  CB  LYS A  14    15851  10478  14802  -3064    104  -1267       C  
ATOM     81  CG  LYS A  14       3.628 -17.060 -33.893  1.00109.60           C  
ANISOU   81  CG  LYS A  14    16005  10684  14953  -3144    163  -1379       C  
ATOM     82  CD  LYS A  14       3.051 -18.373 -34.409  1.00109.72           C  
ANISOU   82  CD  LYS A  14    15990  10695  15003  -3075     76  -1421       C  
ATOM     83  CE  LYS A  14       4.062 -19.143 -35.242  1.00111.34           C  
ANISOU   83  CE  LYS A  14    16192  10911  15200  -3154    163  -1559       C  
ATOM     84  NZ  LYS A  14       5.034 -19.904 -34.410  1.00111.54           N  
ANISOU   84  NZ  LYS A  14    16023  10938  15418  -3119    131  -1617       N  
ATOM     85  N   CYS A  15       0.790 -13.902 -33.988  1.00103.68           N  
ANISOU   85  N   CYS A  15    15596   9727  14073  -3130    203   -981       N  
ATOM     86  CA  CYS A  15      -0.491 -13.209 -34.034  1.00100.85           C  
ANISOU   86  CA  CYS A  15    15306   9258  13753  -3086    185   -807       C  
ATOM     87  C   CYS A  15      -1.410 -13.834 -35.062  1.00 97.04           C  
ANISOU   87  C   CYS A  15    14871   8775  13226  -3093    106   -710       C  
ATOM     88  O   CYS A  15      -0.952 -14.454 -36.020  1.00 97.34           O  
ANISOU   88  O   CYS A  15    14956   8883  13144  -3183    104   -787       O  
ATOM     89  CB  CYS A  15      -0.282 -11.739 -34.389  1.00103.11           C  
ANISOU   89  CB  CYS A  15    15702   9449  14027  -3186    305   -726       C  
ATOM     90  SG  CYS A  15       0.638 -10.812 -33.158  1.00 67.24           S  
ANISOU   90  SG  CYS A  15    11141   4878   9531  -3209    398   -831       S  
ATOM     91  N   GLY A  16      -2.711 -13.661 -34.868  1.00 93.10           N  
ANISOU   91  N   GLY A  16    14365   8186  12821  -3012     48   -538       N  
ATOM     92  CA  GLY A  16      -3.667 -14.148 -35.839  1.00 90.08           C  
ANISOU   92  CA  GLY A  16    14037   7796  12392  -3047    -39   -408       C  
ATOM     93  C   GLY A  16      -4.996 -14.470 -35.204  1.00 86.08           C  
ANISOU   93  C   GLY A  16    13447   7222  12039  -2908   -120   -259       C  
ATOM     94  O   GLY A  16      -5.275 -14.057 -34.081  1.00 86.15           O  
ANISOU   94  O   GLY A  16    13374   7160  12198  -2791    -80   -230       O  
ATOM     95  N   SER A  17      -5.820 -15.211 -35.933  1.00 82.76           N  
ANISOU   95  N   SER A  17    13059   6822  11565  -2938   -231   -164       N  
ATOM     96  CA  SER A  17      -7.123 -15.613 -35.435  1.00 78.96           C  
ANISOU   96  CA  SER A  17    12500   6284  11218  -2818   -306      2       C  
ATOM     97  C   SER A  17      -7.072 -17.069 -34.997  1.00 75.21           C  
ANISOU   97  C   SER A  17    11929   5902  10747  -2746   -405   -154       C  
ATOM     98  O   SER A  17      -6.210 -17.828 -35.440  1.00 61.95           O  
ANISOU   98  O   SER A  17    10261   4315   8963  -2813   -433   -354       O  
ATOM     99  CB  SER A  17      -8.178 -15.429 -36.523  1.00 80.67           C  
ANISOU   99  CB  SER A  17    12853   6455  11344  -2933   -400    271       C  
ATOM    100  OG  SER A  17      -9.462 -15.793 -36.059  1.00 80.25           O  
ANISOU  100  OG  SER A  17    12703   6352  11437  -2802   -462    463       O  
ATOM    101  N   GLY A  18      -7.989 -17.454 -34.117  1.00 71.72           N  
ANISOU  101  N   GLY A  18    11381   5420  10449  -2605   -434    -53       N  
ATOM    102  CA  GLY A  18      -8.054 -18.825 -33.652  1.00 67.68           C  
ANISOU  102  CA  GLY A  18    10763   4980   9971  -2533   -520   -163       C  
ATOM    103  C   GLY A  18      -8.754 -18.936 -32.317  1.00 64.15           C  
ANISOU  103  C   GLY A  18    10194   4490   9689  -2368   -480    -76       C  
ATOM    104  O   GLY A  18      -9.693 -18.195 -32.044  1.00 63.46           O  
ANISOU  104  O   GLY A  18    10128   4302   9683  -2308   -426    137       O  
ATOM    105  N   ILE A  19      -8.296 -19.867 -31.485  1.00 62.20           N  
ANISOU  105  N   ILE A  19     9817   4313   9505  -2299   -484   -229       N  
ATOM    106  CA  ILE A  19      -8.862 -20.051 -30.151  1.00 61.01           C  
ANISOU  106  CA  ILE A  19     9569   4140   9471  -2165   -435   -161       C  
ATOM    107  C   ILE A  19      -7.763 -19.947 -29.093  1.00 60.15           C  
ANISOU  107  C   ILE A  19     9348   4073   9431  -2144   -352   -349       C  
ATOM    108  O   ILE A  19      -6.675 -20.497 -29.270  1.00 59.76           O  
ANISOU  108  O   ILE A  19     9231   4103   9371  -2196   -380   -535       O  
ATOM    109  CB  ILE A  19      -9.598 -21.408 -30.017  1.00 60.53           C  
ANISOU  109  CB  ILE A  19     9464   4132   9401  -2108   -566    -94       C  
ATOM    110  CG1 ILE A  19     -10.652 -21.573 -31.113  1.00 61.91           C  
ANISOU  110  CG1 ILE A  19     9742   4281   9501  -2152   -735    105       C  
ATOM    111  CG2 ILE A  19     -10.259 -21.528 -28.657  1.00 59.37           C  
ANISOU  111  CG2 ILE A  19     9256   3970   9334  -1975   -524     18       C  
ATOM    112  CD1 ILE A  19     -11.809 -20.595 -31.006  1.00 62.95           C  
ANISOU  112  CD1 ILE A  19     9930   4309   9678  -2092   -704    385       C  
ATOM    113  N   PHE A  20      -8.051 -19.239 -28.002  1.00 60.13           N  
ANISOU  113  N   PHE A  20     9325   4005   9515  -2075   -264   -290       N  
ATOM    114  CA  PHE A  20      -7.075 -19.035 -26.934  1.00 60.21           C  
ANISOU  114  CA  PHE A  20     9257   4056   9564  -2083   -242   -441       C  
ATOM    115  C   PHE A  20      -7.525 -19.639 -25.606  1.00 58.88           C  
ANISOU  115  C   PHE A  20     8997   3902   9471  -2002   -202   -413       C  
ATOM    116  O   PHE A  20      -8.555 -19.256 -25.057  1.00 58.40           O  
ANISOU  116  O   PHE A  20     8974   3744   9473  -1921   -128   -261       O  
ATOM    117  CB  PHE A  20      -6.785 -17.545 -26.752  1.00 62.51           C  
ANISOU  117  CB  PHE A  20     9659   4262   9828  -2126   -198   -431       C  
ATOM    118  CG  PHE A  20      -5.691 -17.263 -25.768  1.00 63.83           C  
ANISOU  118  CG  PHE A  20     9824   4493   9938  -2183   -213   -585       C  
ATOM    119  CD1 PHE A  20      -4.471 -17.905 -25.877  1.00 64.36           C  
ANISOU  119  CD1 PHE A  20     9813   4685   9956  -2251   -273   -738       C  
ATOM    120  CD2 PHE A  20      -5.879 -16.355 -24.738  1.00 65.14           C  
ANISOU  120  CD2 PHE A  20    10078   4582  10089  -2184   -158   -569       C  
ATOM    121  CE1 PHE A  20      -3.456 -17.654 -24.974  1.00 65.34           C  
ANISOU  121  CE1 PHE A  20     9935   4873  10019  -2327   -284   -850       C  
ATOM    122  CE2 PHE A  20      -4.866 -16.095 -23.830  1.00 66.13           C  
ANISOU  122  CE2 PHE A  20    10244   4782  10102  -2277   -158   -717       C  
ATOM    123  CZ  PHE A  20      -3.653 -16.746 -23.949  1.00 66.13           C  
ANISOU  123  CZ  PHE A  20    10148   4921  10056  -2353   -226   -845       C  
ATOM    124  N   ILE A  21      -6.733 -20.574 -25.091  1.00 58.46           N  
ANISOU  124  N   ILE A  21     8829   3964   9420  -2029   -231   -548       N  
ATOM    125  CA  ILE A  21      -7.062 -21.287 -23.859  1.00 57.79           C  
ANISOU  125  CA  ILE A  21     8690   3923   9345  -1988   -196   -514       C  
ATOM    126  C   ILE A  21      -6.274 -20.730 -22.679  1.00 59.71           C  
ANISOU  126  C   ILE A  21     8868   4196   9622  -2027   -204   -610       C  
ATOM    127  O   ILE A  21      -5.062 -20.879 -22.626  1.00 60.56           O  
ANISOU  127  O   ILE A  21     8893   4393   9723  -2106   -267   -748       O  
ATOM    128  CB  ILE A  21      -6.762 -22.796 -23.995  1.00 55.57           C  
ANISOU  128  CB  ILE A  21     8352   3765   8996  -2010   -262   -548       C  
ATOM    129  CG1 ILE A  21      -7.459 -23.370 -25.231  1.00 54.94           C  
ANISOU  129  CG1 ILE A  21     8337   3670   8869  -1977   -367   -454       C  
ATOM    130  CG2 ILE A  21      -7.170 -23.543 -22.736  1.00 54.22           C  
ANISOU  130  CG2 ILE A  21     8160   3654   8786  -1969   -316   -440       C  
ATOM    131  CD1 ILE A  21      -8.946 -23.136 -25.256  1.00 54.63           C  
ANISOU  131  CD1 ILE A  21     8388   3555   8814  -1873   -433   -211       C  
ATOM    132  N   THR A  22      -6.967 -20.104 -21.730  1.00 60.77           N  
ANISOU  132  N   THR A  22     9053   4244   9793  -1981   -164   -521       N  
ATOM    133  CA  THR A  22      -6.298 -19.424 -20.621  1.00 61.98           C  
ANISOU  133  CA  THR A  22     9232   4387   9929  -2066   -224   -610       C  
ATOM    134  C   THR A  22      -6.157 -20.292 -19.371  1.00 62.15           C  
ANISOU  134  C   THR A  22     9144   4518   9952  -2091   -224   -625       C  
ATOM    135  O   THR A  22      -6.930 -21.223 -19.157  1.00 61.52           O  
ANISOU  135  O   THR A  22     9037   4471   9865  -2022   -144   -516       O  
ATOM    136  CB  THR A  22      -7.007 -18.103 -20.254  1.00 62.97           C  
ANISOU  136  CB  THR A  22     9550   4354  10022  -2043   -184   -529       C  
ATOM    137  OG1 THR A  22      -8.287 -18.382 -19.678  1.00 62.44           O  
ANISOU  137  OG1 THR A  22     9439   4194  10092  -1913   -113   -355       O  
ATOM    138  CG2 THR A  22      -7.196 -17.240 -21.484  1.00 63.61           C  
ANISOU  138  CG2 THR A  22     9745   4345  10078  -2033   -151   -483       C  
ATOM    139  N   ASP A  23      -5.152 -19.984 -18.558  1.00 63.57           N  
ANISOU  139  N   ASP A  23     9329   4761  10063  -2231   -312   -745       N  
ATOM    140  CA  ASP A  23      -4.979 -20.628 -17.262  1.00 64.58           C  
ANISOU  140  CA  ASP A  23     9428   4976  10134  -2340   -353   -739       C  
ATOM    141  C   ASP A  23      -5.478 -19.677 -16.186  1.00 68.50           C  
ANISOU  141  C   ASP A  23    10212   5372  10441  -2433   -339   -715       C  
ATOM    142  O   ASP A  23      -4.841 -18.665 -15.903  1.00 70.58           O  
ANISOU  142  O   ASP A  23    10677   5650  10490  -2578   -311   -847       O  
ATOM    143  CB  ASP A  23      -3.506 -20.973 -17.036  1.00 64.52           C  
ANISOU  143  CB  ASP A  23     9298   5137  10079  -2502   -451   -865       C  
ATOM    144  CG  ASP A  23      -3.202 -21.364 -15.603  1.00 65.76           C  
ANISOU  144  CG  ASP A  23     9486   5412  10090  -2708   -549   -835       C  
ATOM    145  OD1 ASP A  23      -4.094 -21.877 -14.902  1.00 56.28           O  
ANISOU  145  OD1 ASP A  23     8327   4187   8870  -2701   -561   -697       O  
ATOM    146  OD2 ASP A  23      -2.051 -21.163 -15.176  1.00 67.45           O  
ANISOU  146  OD2 ASP A  23     9681   5755  10193  -2897   -632   -922       O  
ATOM    147  N   ASN A  24      -6.625 -20.003 -15.598  1.00 69.86           N  
ANISOU  147  N   ASN A  24    10443   5441  10659  -2365   -291   -558       N  
ATOM    148  CA  ASN A  24      -7.224 -19.158 -14.574  1.00 73.57           C  
ANISOU  148  CA  ASN A  24    11235   5782  10935  -2452   -197   -546       C  
ATOM    149  C   ASN A  24      -7.001 -19.727 -13.180  1.00 77.83           C  
ANISOU  149  C   ASN A  24    11863   6426  11284  -2678   -257   -540       C  
ATOM    150  O   ASN A  24      -7.534 -19.219 -12.195  1.00 80.48           O  
ANISOU  150  O   ASN A  24    12501   6664  11413  -2790   -120   -547       O  
ATOM    151  CB  ASN A  24      -8.722 -18.992 -14.823  1.00 71.64           C  
ANISOU  151  CB  ASN A  24    11017   5318  10884  -2221    -92   -330       C  
ATOM    152  CG  ASN A  24      -9.052 -18.814 -16.287  1.00 68.76           C  
ANISOU  152  CG  ASN A  24    10464   4907  10756  -2023    -86   -264       C  
ATOM    153  OD1 ASN A  24      -8.821 -17.753 -16.864  1.00 69.42           O  
ANISOU  153  OD1 ASN A  24    10665   4941  10768  -2037    -57   -343       O  
ATOM    154  ND2 ASN A  24      -9.607 -19.853 -16.895  1.00 65.82           N  
ANISOU  154  ND2 ASN A  24     9869   4589  10549  -1869    -24   -134       N  
ATOM    155  N   VAL A  25      -6.205 -20.785 -13.110  1.00 79.47           N  
ANISOU  155  N   VAL A  25    11811   6839  11544  -2763   -439   -523       N  
ATOM    156  CA  VAL A  25      -5.911 -21.439 -11.846  1.00 83.56           C  
ANISOU  156  CA  VAL A  25    12331   7520  11897  -3015   -584   -451       C  
ATOM    157  C   VAL A  25      -4.719 -20.785 -11.146  1.00 89.65           C  
ANISOU  157  C   VAL A  25    13246   8485  12333  -3346   -606   -662       C  
ATOM    158  O   VAL A  25      -4.774 -20.484  -9.955  1.00 91.88           O  
ANISOU  158  O   VAL A  25    13774   8843  12295  -3627   -577   -701       O  
ATOM    159  CB  VAL A  25      -5.654 -22.945 -12.059  1.00 81.68           C  
ANISOU  159  CB  VAL A  25    11710   7447  11880  -2944   -792   -272       C  
ATOM    160  CG1 VAL A  25      -5.209 -23.614 -10.773  1.00 83.17           C  
ANISOU  160  CG1 VAL A  25    11793   7873  11936  -3221  -1030   -126       C  
ATOM    161  CG2 VAL A  25      -6.901 -23.613 -12.599  1.00 79.65           C  
ANISOU  161  CG2 VAL A  25    11377   7048  11837  -2649   -768    -49       C  
ATOM    162  N   HIS A  26      -3.649 -20.549 -11.896  1.00 93.17           N  
ANISOU  162  N   HIS A  26    13551   9017  12833  -3330   -634   -797       N  
ATOM    163  CA  HIS A  26      -2.423 -20.012 -11.316  1.00 99.90           C  
ANISOU  163  CA  HIS A  26    14478  10068  13409  -3627   -675   -954       C  
ATOM    164  C   HIS A  26      -2.495 -18.511 -11.042  1.00109.78           C  
ANISOU  164  C   HIS A  26    16140  11218  14353  -3744   -448  -1167       C  
ATOM    165  O   HIS A  26      -1.675 -17.969 -10.299  1.00112.69           O  
ANISOU  165  O   HIS A  26    16652  11749  14417  -4042   -447  -1307       O  
ATOM    166  CB  HIS A  26      -1.221 -20.332 -12.208  1.00 95.63           C  
ANISOU  166  CB  HIS A  26    13633   9625  13077  -3563   -769   -986       C  
ATOM    167  CG  HIS A  26      -0.955 -21.797 -12.357  1.00 90.73           C  
ANISOU  167  CG  HIS A  26    12620   9124  12728  -3493   -925   -824       C  
ATOM    168  ND1 HIS A  26       0.116 -22.290 -13.072  1.00 88.77           N  
ANISOU  168  ND1 HIS A  26    12090   8951  12686  -3451   -958   -854       N  
ATOM    169  CD2 HIS A  26      -1.620 -22.877 -11.882  1.00 88.19           C  
ANISOU  169  CD2 HIS A  26    12152   8855  12502  -3462  -1031   -620       C  
ATOM    170  CE1 HIS A  26       0.099 -23.609 -13.032  1.00 86.88           C  
ANISOU  170  CE1 HIS A  26    11573   8811  12627  -3402  -1039   -703       C  
ATOM    171  NE2 HIS A  26      -0.945 -23.991 -12.317  1.00 86.53           N  
ANISOU  171  NE2 HIS A  26    11591   8766  12521  -3396  -1115   -538       N  
ATOM    172  N   THR A  27      -3.474 -17.843 -11.640  1.00116.50           N  
ANISOU  172  N   THR A  27    17161  11808  15295  -3514   -251  -1177       N  
ATOM    173  CA  THR A  27      -3.649 -16.414 -11.422  1.00126.94           C  
ANISOU  173  CA  THR A  27    18855  12995  16381  -3591     14  -1366       C  
ATOM    174  C   THR A  27      -4.081 -16.125  -9.987  1.00136.85           C  
ANISOU  174  C   THR A  27    20462  14256  17280  -3856    174  -1471       C  
ATOM    175  O   THR A  27      -5.132 -16.589  -9.541  1.00137.75           O  
ANISOU  175  O   THR A  27    20657  14254  17428  -3792    240  -1352       O  
ATOM    176  CB  THR A  27      -4.674 -15.821 -12.396  1.00126.34           C  
ANISOU  176  CB  THR A  27    18829  12647  16528  -3277    179  -1294       C  
ATOM    177  OG1 THR A  27      -5.977 -16.336 -12.095  1.00125.45           O  
ANISOU  177  OG1 THR A  27    18753  12380  16531  -3131    238  -1124       O  
ATOM    178  CG2 THR A  27      -4.310 -16.184 -13.822  1.00123.67           C  
ANISOU  178  CG2 THR A  27    18162  12334  16494  -3059     16  -1195       C  
ATOM    179  N   TRP A  28      -3.257 -15.359  -9.273  1.00145.92           N  
ANISOU  179  N   TRP A  28    21822  15537  18083  -4168    245  -1690       N  
ATOM    180  CA  TRP A  28      -3.543 -14.975  -7.890  1.00155.40           C  
ANISOU  180  CA  TRP A  28    23400  16778  18868  -4482    426  -1853       C  
ATOM    181  C   TRP A  28      -4.866 -14.227  -7.776  1.00158.06           C  
ANISOU  181  C   TRP A  28    24085  16763  19210  -4314    825  -1919       C  
ATOM    182  O   TRP A  28      -5.524 -14.253  -6.735  1.00161.35           O  
ANISOU  182  O   TRP A  28    24797  17131  19379  -4471   1017  -1991       O  
ATOM    183  CB  TRP A  28      -2.408 -14.112  -7.325  1.00163.50           C  
ANISOU  183  CB  TRP A  28    24587  17986  19549  -4823    449  -2086       C  
ATOM    184  CG  TRP A  28      -1.258 -14.904  -6.777  1.00167.67           C  
ANISOU  184  CG  TRP A  28    24868  18911  19928  -5121     99  -2011       C  
ATOM    185  CD1 TRP A  28      -1.007 -15.183  -5.464  1.00172.16           C  
ANISOU  185  CD1 TRP A  28    25552  19775  20087  -5523      5  -2050       C  
ATOM    186  CD2 TRP A  28      -0.206 -15.522  -7.526  1.00167.44           C  
ANISOU  186  CD2 TRP A  28    24414  19040  20167  -5043   -196  -1860       C  
ATOM    187  NE1 TRP A  28       0.136 -15.936  -5.350  1.00173.18           N  
ANISOU  187  NE1 TRP A  28    25315  20249  20236  -5691   -357  -1888       N  
ATOM    188  CE2 TRP A  28       0.648 -16.158  -6.602  1.00170.34           C  
ANISOU  188  CE2 TRP A  28    24630  19781  20309  -5388   -460  -1781       C  
ATOM    189  CE3 TRP A  28       0.098 -15.599  -8.888  1.00165.26           C  
ANISOU  189  CE3 TRP A  28    23871  18630  20290  -4723   -247  -1778       C  
ATOM    190  CZ2 TRP A  28       1.784 -16.862  -6.998  1.00170.35           C  
ANISOU  190  CZ2 TRP A  28    24214  19984  20525  -5391   -743  -1616       C  
ATOM    191  CZ3 TRP A  28       1.227 -16.299  -9.278  1.00164.89           C  
ANISOU  191  CZ3 TRP A  28    23452  18774  20424  -4742   -504  -1659       C  
ATOM    192  CH2 TRP A  28       2.055 -16.921  -8.337  1.00167.37           C  
ANISOU  192  CH2 TRP A  28    23614  19419  20559  -5060   -736  -1576       C  
ATOM    193  N   THR A  29      -5.247 -13.562  -8.860  1.00151.15           N  
ANISOU  193  N   THR A  29    23163  15647  18622  -4001    956  -1879       N  
ATOM    194  CA  THR A  29      -6.497 -12.822  -8.910  1.00148.57           C  
ANISOU  194  CA  THR A  29    23085  14974  18389  -3788   1330  -1879       C  
ATOM    195  C   THR A  29      -7.664 -13.732  -9.273  1.00143.61           C  
ANISOU  195  C   THR A  29    22283  14197  18085  -3479   1278  -1575       C  
ATOM    196  O   THR A  29      -7.508 -14.690 -10.032  1.00140.30           O  
ANISOU  196  O   THR A  29    21490  13892  17927  -3332    947  -1361       O  
ATOM    197  CB  THR A  29      -6.414 -11.676  -9.929  1.00147.61           C  
ANISOU  197  CB  THR A  29    22950  14689  18448  -3615   1458  -1914       C  
ATOM    198  OG1 THR A  29      -6.078 -12.206 -11.218  1.00143.45           O  
ANISOU  198  OG1 THR A  29    22028  14248  18229  -3408   1144  -1718       O  
ATOM    199  CG2 THR A  29      -5.350 -10.675  -9.510  1.00150.69           C  
ANISOU  199  CG2 THR A  29    23534  15171  18551  -3915   1545  -2193       C  
ATOM    200  N   GLU A  30      -8.830 -13.427  -8.714  1.00143.76           N  
ANISOU  200  N   GLU A  30    22566  13952  18105  -3372   1628  -1547       N  
ATOM    201  CA  GLU A  30     -10.048 -14.163  -9.019  1.00139.75           C  
ANISOU  201  CA  GLU A  30    21888  13269  17939  -3044   1616  -1203       C  
ATOM    202  C   GLU A  30     -10.839 -13.430 -10.095  1.00136.24           C  
ANISOU  202  C   GLU A  30    21329  12603  17833  -2691   1738  -1045       C  
ATOM    203  O   GLU A  30     -11.590 -12.500  -9.802  1.00138.76           O  
ANISOU  203  O   GLU A  30    21893  12671  18158  -2590   2144  -1089       O  
ATOM    204  CB  GLU A  30     -10.894 -14.345  -7.759  1.00143.43           C  
ANISOU  204  CB  GLU A  30    22674  13577  18248  -3106   1939  -1190       C  
ATOM    205  CG  GLU A  30     -10.233 -15.222  -6.711  1.00144.76           C  
ANISOU  205  CG  GLU A  30    22921  14001  18080  -3506   1747  -1272       C  
ATOM    206  CD  GLU A  30      -9.961 -16.620  -7.221  1.00141.29           C  
ANISOU  206  CD  GLU A  30    22017  13774  17894  -3449   1245   -958       C  
ATOM    207  OE1 GLU A  30      -8.857 -17.145  -6.967  1.00141.08           O  
ANISOU  207  OE1 GLU A  30    21851  14080  17673  -3766    920  -1045       O  
ATOM    208  OE2 GLU A  30     -10.855 -17.195  -7.876  1.00138.83           O  
ANISOU  208  OE2 GLU A  30    21439  13317  17992  -3076   1170   -604       O  
ATOM    209  N   GLN A  31     -10.661 -13.862 -11.341  1.00130.20           N  
ANISOU  209  N   GLN A  31    20183  11942  17346  -2524   1387   -859       N  
ATOM    210  CA  GLN A  31     -11.247 -13.183 -12.493  1.00127.09           C  
ANISOU  210  CA  GLN A  31    19652  11409  17228  -2273   1405   -704       C  
ATOM    211  C   GLN A  31     -12.729 -13.505 -12.682  1.00124.84           C  
ANISOU  211  C   GLN A  31    19230  10954  17248  -1964   1440   -345       C  
ATOM    212  O   GLN A  31     -13.474 -12.702 -13.246  1.00126.22           O  
ANISOU  212  O   GLN A  31    19398  10966  17595  -1791   1577   -220       O  
ATOM    213  CB  GLN A  31     -10.485 -13.547 -13.772  1.00123.24           C  
ANISOU  213  CB  GLN A  31    18835  11108  16881  -2252   1026   -654       C  
ATOM    214  CG  GLN A  31      -8.969 -13.466 -13.662  1.00122.89           C  
ANISOU  214  CG  GLN A  31    18820  11281  16593  -2515    923   -927       C  
ATOM    215  CD  GLN A  31      -8.452 -12.044 -13.605  1.00125.56           C  
ANISOU  215  CD  GLN A  31    19415  11542  16752  -2650   1171  -1164       C  
ATOM    216  OE1 GLN A  31      -7.341 -11.798 -13.137  1.00126.91           O  
ANISOU  216  OE1 GLN A  31    19686  11860  16672  -2901   1162  -1395       O  
ATOM    217  NE2 GLN A  31      -9.249 -11.100 -14.091  1.00126.71           N  
ANISOU  217  NE2 GLN A  31    19639  11458  17048  -2493   1379  -1082       N  
ATOM    218  N   TYR A  32     -13.152 -14.677 -12.218  1.00121.11           N  
ANISOU  218  N   TYR A  32    18624  10537  16856  -1903   1294   -147       N  
ATOM    219  CA  TYR A  32     -14.514 -15.142 -12.468  1.00117.71           C  
ANISOU  219  CA  TYR A  32    17980  10013  16730  -1605   1225    254       C  
ATOM    220  C   TYR A  32     -15.338 -15.319 -11.199  1.00117.03           C  
ANISOU  220  C   TYR A  32    18077   9791  16596  -1526   1554    357       C  
ATOM    221  O   TYR A  32     -14.825 -15.747 -10.166  1.00117.87           O  
ANISOU  221  O   TYR A  32    18381   9937  16466  -1729   1657    209       O  
ATOM    222  CB  TYR A  32     -14.491 -16.459 -13.242  1.00114.14           C  
ANISOU  222  CB  TYR A  32    17116   9745  16507  -1535    718    502       C  
ATOM    223  CG  TYR A  32     -13.810 -16.371 -14.587  1.00112.39           C  
ANISOU  223  CG  TYR A  32    16682   9638  16382  -1569    447    437       C  
ATOM    224  CD1 TYR A  32     -14.540 -16.125 -15.739  1.00111.77           C  
ANISOU  224  CD1 TYR A  32    16445   9521  16500  -1425    254    667       C  
ATOM    225  CD2 TYR A  32     -12.437 -16.534 -14.704  1.00111.46           C  
ANISOU  225  CD2 TYR A  32    16546   9683  16122  -1766    382    154       C  
ATOM    226  CE1 TYR A  32     -13.924 -16.044 -16.971  1.00110.31           C  
ANISOU  226  CE1 TYR A  32    16067   9450  16396  -1456     84    605       C  
ATOM    227  CE2 TYR A  32     -11.812 -16.454 -15.932  1.00110.00           C  
ANISOU  227  CE2 TYR A  32    16166   9598  16032  -1768    219     95       C  
ATOM    228  CZ  TYR A  32     -12.560 -16.208 -17.062  1.00109.30           C  
ANISOU  228  CZ  TYR A  32    15909   9439  16183  -1611    108    313       C  
ATOM    229  OH  TYR A  32     -11.944 -16.126 -18.288  1.00108.03           O  
ANISOU  229  OH  TYR A  32    15577   9393  16075  -1620     28    241       O  
ATOM    230  N   LYS A  33     -16.622 -14.986 -11.294  1.00115.60           N  
ANISOU  230  N   LYS A  33    17829   9468  16626  -1247   1717    627       N  
ATOM    231  CA  LYS A  33     -17.572 -15.205 -10.208  1.00115.49           C  
ANISOU  231  CA  LYS A  33    17904   9337  16640  -1085   2046    805       C  
ATOM    232  C   LYS A  33     -18.853 -15.802 -10.776  1.00113.21           C  
ANISOU  232  C   LYS A  33    17236   9124  16655   -779   1773   1265       C  
ATOM    233  O   LYS A  33     -19.166 -15.598 -11.948  1.00111.71           O  
ANISOU  233  O   LYS A  33    16869   8989  16586   -716   1484   1378       O  
ATOM    234  CB  LYS A  33     -17.885 -13.894  -9.484  1.00119.37           C  
ANISOU  234  CB  LYS A  33    18787   9556  17012  -1069   2697    585       C  
ATOM    235  CG  LYS A  33     -16.686 -13.237  -8.822  1.00121.02           C  
ANISOU  235  CG  LYS A  33    19454   9715  16813  -1439   2960     72       C  
ATOM    236  CD  LYS A  33     -17.087 -11.979  -8.067  1.00125.49           C  
ANISOU  236  CD  LYS A  33    20433   9989  17257  -1430   3629   -161       C  
ATOM    237  CE  LYS A  33     -15.871 -11.302  -7.455  1.00127.23           C  
ANISOU  237  CE  LYS A  33    21103  10218  17019  -1859   3813   -703       C  
ATOM    238  NZ  LYS A  33     -16.233 -10.065  -6.710  1.00132.10           N  
ANISOU  238  NZ  LYS A  33    22143  10547  17503  -1881   4477   -970       N  
ATOM    239  N   PHE A  34     -19.592 -16.538  -9.951  1.00 96.98           N  
ANISOU  239  N   PHE A  34    15102  10792  10953   -273   1285  -2044       N  
ATOM    240  CA  PHE A  34     -20.836 -17.162 -10.398  1.00 95.46           C  
ANISOU  240  CA  PHE A  34    14914  10654  10703     95    992  -1847       C  
ATOM    241  C   PHE A  34     -22.063 -16.323 -10.029  1.00 97.53           C  
ANISOU  241  C   PHE A  34    15355  10735  10967    442    795  -1775       C  
ATOM    242  O   PHE A  34     -22.155 -15.808  -8.913  1.00 97.65           O  
ANISOU  242  O   PHE A  34    15224  10796  11081    488    827  -1908       O  
ATOM    243  CB  PHE A  34     -20.970 -18.577  -9.821  1.00 90.93           C  
ANISOU  243  CB  PHE A  34    13759  10504  10285    187    831  -1855       C  
ATOM    244  CG  PHE A  34     -20.160 -19.619 -10.553  1.00 88.98           C  
ANISOU  244  CG  PHE A  34    13384  10377  10047      6    930  -1878       C  
ATOM    245  CD1 PHE A  34     -19.390 -19.277 -11.653  1.00 90.58           C  
ANISOU  245  CD1 PHE A  34    13955  10358  10101   -236   1202  -1906       C  
ATOM    246  CD2 PHE A  34     -20.183 -20.946 -10.145  1.00 86.08           C  
ANISOU  246  CD2 PHE A  34    12556  10317   9833     78    780  -1876       C  
ATOM    247  CE1 PHE A  34     -18.651 -20.235 -12.326  1.00 90.11           C  
ANISOU  247  CE1 PHE A  34    13768  10409  10061   -380   1353  -1975       C  
ATOM    248  CE2 PHE A  34     -19.447 -21.907 -10.816  1.00 85.53           C  
ANISOU  248  CE2 PHE A  34    12375  10317   9807    -43    877  -1931       C  
ATOM    249  CZ  PHE A  34     -18.681 -21.549 -11.907  1.00 87.61           C  
ANISOU  249  CZ  PHE A  34    12969  10383   9935   -260   1178  -2001       C  
ATOM    250  N   GLN A  35     -22.997 -16.184 -10.970  1.00 99.76           N  
ANISOU  250  N   GLN A  35    15956  10807  11142    698    577  -1584       N  
ATOM    251  CA  GLN A  35     -24.243 -15.459 -10.715  1.00102.23           C  
ANISOU  251  CA  GLN A  35    16365  10944  11532   1101    347  -1519       C  
ATOM    252  C   GLN A  35     -25.485 -16.211 -11.199  1.00103.13           C  
ANISOU  252  C   GLN A  35    16282  11187  11716   1444    -31  -1357       C  
ATOM    253  O   GLN A  35     -25.466 -16.857 -12.252  1.00103.31           O  
ANISOU  253  O   GLN A  35    16460  11203  11589   1387   -170  -1232       O  
ATOM    254  CB  GLN A  35     -24.206 -14.059 -11.338  1.00105.64           C  
ANISOU  254  CB  GLN A  35    17490  10831  11816   1118    391  -1454       C  
ATOM    255  CG  GLN A  35     -23.686 -12.971 -10.410  1.00106.59           C  
ANISOU  255  CG  GLN A  35    17730  10763  12008    985    641  -1652       C  
ATOM    256  CD  GLN A  35     -22.176 -12.935 -10.339  1.00105.83           C  
ANISOU  256  CD  GLN A  35    17674  10695  11843    447    997  -1792       C  
ATOM    257  OE1 GLN A  35     -21.492 -13.227 -11.317  1.00106.25           O  
ANISOU  257  OE1 GLN A  35    17943  10690  11738    175   1134  -1706       O  
ATOM    258  NE2 GLN A  35     -21.646 -12.574  -9.178  1.00105.53           N  
ANISOU  258  NE2 GLN A  35    17418  10751  11927    285   1152  -2032       N  
ATOM    259  N   PRO A  36     -26.575 -16.127 -10.420  1.00104.61           N  
ANISOU  259  N   PRO A  36    16117  11494  12138   1784   -184  -1385       N  
ATOM    260  CA  PRO A  36     -27.866 -16.724 -10.774  1.00105.76           C  
ANISOU  260  CA  PRO A  36    15983  11760  12442   2114   -555  -1261       C  
ATOM    261  C   PRO A  36     -28.659 -15.807 -11.694  1.00110.72           C  
ANISOU  261  C   PRO A  36    17056  11972  13041   2446   -873  -1121       C  
ATOM    262  O   PRO A  36     -28.368 -14.617 -11.750  1.00113.40           O  
ANISOU  262  O   PRO A  36    17871  11927  13288   2479   -764  -1137       O  
ATOM    263  CB  PRO A  36     -28.572 -16.813  -9.424  1.00105.48           C  
ANISOU  263  CB  PRO A  36    15387  12004  12687   2300   -466  -1392       C  
ATOM    264  CG  PRO A  36     -28.056 -15.631  -8.680  1.00106.70           C  
ANISOU  264  CG  PRO A  36    15799  11949  12795   2269   -179  -1560       C  
ATOM    265  CD  PRO A  36     -26.607 -15.507  -9.083  1.00105.16           C  
ANISOU  265  CD  PRO A  36    15988  11623  12344   1843     23  -1577       C  
ATOM    266  N   GLU A  37     -29.641 -16.356 -12.402  1.00112.29           N  
ANISOU  266  N   GLU A  37    17119  12223  13325   2681  -1298   -985       N  
ATOM    267  CA  GLU A  37     -30.534 -15.556 -13.232  1.00117.37           C  
ANISOU  267  CA  GLU A  37    18121  12491  13984   3066  -1723   -840       C  
ATOM    268  C   GLU A  37     -31.832 -15.312 -12.481  1.00119.92           C  
ANISOU  268  C   GLU A  37    17873  12919  14770   3523  -1896   -921       C  
ATOM    269  O   GLU A  37     -32.486 -14.280 -12.647  1.00125.35           O  
ANISOU  269  O   GLU A  37    18772  13259  15595   3920  -2112   -890       O  
ATOM    270  CB  GLU A  37     -30.822 -16.273 -14.548  1.00118.20           C  
ANISOU  270  CB  GLU A  37    18452  12573  13884   3046  -2158   -659       C  
ATOM    271  CG  GLU A  37     -29.627 -16.377 -15.473  1.00117.08           C  
ANISOU  271  CG  GLU A  37    18976  12263  13246   2641  -1965   -585       C  
ATOM    272  CD  GLU A  37     -29.941 -17.183 -16.708  1.00118.03           C  
ANISOU  272  CD  GLU A  37    19332  12394  13121   2613  -2375   -452       C  
ATOM    273  OE1 GLU A  37     -30.875 -18.007 -16.649  1.00117.90           O  
ANISOU  273  OE1 GLU A  37    18790  12639  13370   2785  -2740   -463       O  
ATOM    274  OE2 GLU A  37     -29.267 -16.991 -17.737  1.00119.47           O  
ANISOU  274  OE2 GLU A  37    20240  12318  12836   2396  -2320   -350       O  
ATOM    275  N   SER A  38     -32.194 -16.275 -11.643  1.00116.30           N  
ANISOU  275  N   SER A  38    16693  12928  14567   3464  -1775  -1028       N  
ATOM    276  CA  SER A  38     -33.416 -16.177 -10.866  1.00117.45           C  
ANISOU  276  CA  SER A  38    16206  13246  15172   3837  -1830  -1134       C  
ATOM    277  C   SER A  38     -33.243 -16.815  -9.500  1.00112.18           C  
ANISOU  277  C   SER A  38    14991  13012  14619   3625  -1372  -1301       C  
ATOM    278  O   SER A  38     -33.484 -18.010  -9.331  1.00110.60           O  
ANISOU  278  O   SER A  38    14329  13176  14520   3447  -1397  -1267       O  
ATOM    279  CB  SER A  38     -34.574 -16.838 -11.607  1.00121.04           C  
ANISOU  279  CB  SER A  38    16289  13811  15889   4061  -2371  -1020       C  
ATOM    280  OG  SER A  38     -35.776 -16.698 -10.876  1.00124.76           O  
ANISOU  280  OG  SER A  38    16076  14453  16874   4423  -2386  -1146       O  
ATOM    281  N   PRO A  39     -32.819 -16.011  -8.516  1.00109.16           N  
ANISOU  281  N   PRO A  39    14718  12565  14194   3626   -966  -1478       N  
ATOM    282  CA  PRO A  39     -32.713 -16.457  -7.125  1.00105.95           C  
ANISOU  282  CA  PRO A  39    13883  12540  13833   3460   -540  -1644       C  
ATOM    283  C   PRO A  39     -34.084 -16.873  -6.603  1.00107.82           C  
ANISOU  283  C   PRO A  39    13416  13066  14485   3728   -549  -1699       C  
ATOM    284  O   PRO A  39     -34.182 -17.659  -5.661  1.00106.96           O  
ANISOU  284  O   PRO A  39    12889  13343  14408   3532   -265  -1753       O  
ATOM    285  CB  PRO A  39     -32.229 -15.202  -6.395  1.00107.15           C  
ANISOU  285  CB  PRO A  39    14398  12442  13874   3524   -220  -1849       C  
ATOM    286  CG  PRO A  39     -31.560 -14.381  -7.446  1.00107.92           C  
ANISOU  286  CG  PRO A  39    15187  12056  13764   3499   -406  -1746       C  
ATOM    287  CD  PRO A  39     -32.345 -14.627  -8.693  1.00110.52           C  
ANISOU  287  CD  PRO A  39    15516  12258  14218   3743   -898  -1528       C  
ATOM    288  N   SER A  40     -35.131 -16.339  -7.224  1.00111.21           N  
ANISOU  288  N   SER A  40    13719  13296  15239   4168   -881  -1679       N  
ATOM    289  CA  SER A  40     -36.499 -16.713  -6.898  1.00113.84           C  
ANISOU  289  CA  SER A  40    13299  13892  16062   4438   -933  -1741       C  
ATOM    290  C   SER A  40     -36.794 -18.148  -7.332  1.00110.77           C  
ANISOU  290  C   SER A  40    12502  13824  15761   4165  -1176  -1576       C  
ATOM    291  O   SER A  40     -37.292 -18.949  -6.542  1.00111.26           O  
ANISOU  291  O   SER A  40    11982  14268  16022   4019   -920  -1626       O  
ATOM    292  CB  SER A  40     -37.476 -15.749  -7.568  1.00120.06           C  
ANISOU  292  CB  SER A  40    14057  14343  17216   5013  -1328  -1759       C  
ATOM    293  OG  SER A  40     -37.205 -15.641  -8.953  1.00120.21           O  
ANISOU  293  OG  SER A  40    14596  14034  17043   5036  -1884  -1531       O  
ATOM    294  N   LYS A  41     -36.486 -18.462  -8.589  1.00107.83           N  
ANISOU  294  N   LYS A  41    12485  13270  15216   4077  -1650  -1386       N  
ATOM    295  CA  LYS A  41     -36.668 -19.814  -9.113  1.00104.42           C  
ANISOU  295  CA  LYS A  41    11781  13071  14824   3800  -1919  -1253       C  
ATOM    296  C   LYS A  41     -35.830 -20.799  -8.326  1.00 98.57           C  
ANISOU  296  C   LYS A  41    10985  12616  13852   3328  -1509  -1248       C  
ATOM    297  O   LYS A  41     -36.257 -21.918  -8.054  1.00 98.45           O  
ANISOU  297  O   LYS A  41    10500  12890  14017   3117  -1498  -1206       O  
ATOM    298  CB  LYS A  41     -36.272 -19.889 -10.589  1.00103.06           C  
ANISOU  298  CB  LYS A  41    12175  12612  14371   3759  -2433  -1086       C  
ATOM    299  CG  LYS A  41     -37.359 -19.455 -11.554  1.00107.99           C  
ANISOU  299  CG  LYS A  41    12727  13035  15268   4171  -3061  -1024       C  
ATOM    300  CD  LYS A  41     -36.984 -19.781 -12.992  1.00107.10           C  
ANISOU  300  CD  LYS A  41    13206  12699  14788   4046  -3569   -853       C  
ATOM    301  CE  LYS A  41     -38.103 -19.406 -13.948  1.00113.01           C  
ANISOU  301  CE  LYS A  41    13900  13257  15783   4458  -4299   -777       C  
ATOM    302  NZ  LYS A  41     -38.465 -17.967 -13.830  1.00117.04           N  
ANISOU  302  NZ  LYS A  41    14583  13441  16448   4957  -4358   -796       N  
ATOM    303  N   LEU A  42     -34.628 -20.368  -7.972  1.00 94.48           N  
ANISOU  303  N   LEU A  42    10958  11988  12951   3159  -1202  -1286       N  
ATOM    304  CA  LEU A  42     -33.716 -21.177  -7.183  1.00 89.58           C  
ANISOU  304  CA  LEU A  42    10333  11601  12102   2759   -863  -1284       C  
ATOM    305  C   LEU A  42     -34.338 -21.498  -5.836  1.00 89.57           C  
ANISOU  305  C   LEU A  42     9809  11934  12291   2730   -494  -1369       C  
ATOM    306  O   LEU A  42     -34.406 -22.658  -5.428  1.00 88.21           O  
ANISOU  306  O   LEU A  42     9340  12021  12153   2457   -418  -1284       O  
ATOM    307  CB  LEU A  42     -32.412 -20.417  -6.980  1.00 87.89           C  
ANISOU  307  CB  LEU A  42    10673  11199  11521   2638   -628  -1356       C  
ATOM    308  CG  LEU A  42     -31.316 -21.158  -6.228  1.00 84.75           C  
ANISOU  308  CG  LEU A  42    10308  11006  10887   2255   -364  -1362       C  
ATOM    309  CD1 LEU A  42     -31.071 -22.505  -6.877  1.00 82.78           C  
ANISOU  309  CD1 LEU A  42     9971  10853  10629   2021   -582  -1215       C  
ATOM    310  CD2 LEU A  42     -30.050 -20.324  -6.222  1.00 83.59           C  
ANISOU  310  CD2 LEU A  42    10667  10645  10449   2134   -209  -1454       C  
ATOM    311  N   ALA A  43     -34.793 -20.451  -5.157  1.00 91.46           N  
ANISOU  311  N   ALA A  43     9981  12134  12636   3009   -243  -1539       N  
ATOM    312  CA  ALA A  43     -35.448 -20.589  -3.866  1.00 92.83           C  
ANISOU  312  CA  ALA A  43     9707  12613  12954   3011    190  -1660       C  
ATOM    313  C   ALA A  43     -36.621 -21.553  -3.953  1.00 95.34           C  
ANISOU  313  C   ALA A  43     9358  13187  13680   2985     95  -1578       C  
ATOM    314  O   ALA A  43     -36.783 -22.418  -3.098  1.00 95.60           O  
ANISOU  314  O   ALA A  43     9098  13521  13703   2705    397  -1538       O  
ATOM    315  CB  ALA A  43     -35.913 -19.237  -3.370  1.00 96.32           C  
ANISOU  315  CB  ALA A  43    10175  12908  13514   3403    426  -1898       C  
ATOM    316  N   SER A  44     -37.431 -21.398  -4.996  1.00 97.85           N  
ANISOU  316  N   SER A  44     9461  13367  14351   3255   -351  -1544       N  
ATOM    317  CA  SER A  44     -38.595 -22.250  -5.207  1.00101.10           C  
ANISOU  317  CA  SER A  44     9189  13998  15226   3227   -525  -1491       C  
ATOM    318  C   SER A  44     -38.178 -23.698  -5.421  1.00 98.39           C  
ANISOU  318  C   SER A  44     8851  13790  14745   2753   -649  -1299       C  
ATOM    319  O   SER A  44     -38.871 -24.631  -5.005  1.00100.34           O  
ANISOU  319  O   SER A  44     8573  14293  15258   2528   -527  -1254       O  
ATOM    320  CB  SER A  44     -39.393 -21.758  -6.414  1.00104.60           C  
ANISOU  320  CB  SER A  44     9498  14220  16024   3617  -1121  -1488       C  
ATOM    321  OG  SER A  44     -39.754 -20.398  -6.261  1.00108.11           O  
ANISOU  321  OG  SER A  44     9985  14469  16623   4103  -1050  -1656       O  
ATOM    322  N   ALA A  45     -37.035 -23.874  -6.073  1.00 94.39           N  
ANISOU  322  N   ALA A  45     8943  13082  13838   2596   -864  -1197       N  
ATOM    323  CA  ALA A  45     -36.501 -25.199  -6.335  1.00 91.84           C  
ANISOU  323  CA  ALA A  45     8705  12818  13372   2196   -989  -1044       C  
ATOM    324  C   ALA A  45     -36.006 -25.825  -5.042  1.00 90.51           C  
ANISOU  324  C   ALA A  45     8500  12874  13015   1881   -511  -1005       C  
ATOM    325  O   ALA A  45     -36.031 -27.042  -4.887  1.00 90.06           O  
ANISOU  325  O   ALA A  45     8286  12929  13003   1562   -522   -875       O  
ATOM    326  CB  ALA A  45     -35.384 -25.126  -7.351  1.00 88.40           C  
ANISOU  326  CB  ALA A  45     8905  12109  12573   2151  -1270   -992       C  
ATOM    327  N   ILE A  46     -35.550 -24.987  -4.116  1.00 90.51           N  
ANISOU  327  N   ILE A  46     8697  12909  12785   1967   -122  -1115       N  
ATOM    328  CA  ILE A  46     -35.113 -25.473  -2.816  1.00 90.33           C  
ANISOU  328  CA  ILE A  46     8702  13101  12520   1693    301  -1080       C  
ATOM    329  C   ILE A  46     -36.322 -25.828  -1.952  1.00 96.30           C  
ANISOU  329  C   ILE A  46     8897  14137  13556   1632    645  -1090       C  
ATOM    330  O   ILE A  46     -36.284 -26.793  -1.189  1.00 96.92           O  
ANISOU  330  O   ILE A  46     8899  14393  13532   1298    867   -954       O  
ATOM    331  CB  ILE A  46     -34.232 -24.446  -2.088  1.00 88.48           C  
ANISOU  331  CB  ILE A  46     8891  12812  11914   1776    574  -1226       C  
ATOM    332  CG1 ILE A  46     -33.052 -24.039  -2.962  1.00 84.18           C  
ANISOU  332  CG1 ILE A  46     8850  11990  11144   1796    291  -1230       C  
ATOM    333  CG2 ILE A  46     -33.710 -25.018  -0.789  1.00 88.15           C  
ANISOU  333  CG2 ILE A  46     8955  12985  11555   1478    908  -1170       C  
ATOM    334  CD1 ILE A  46     -32.072 -23.140  -2.255  1.00 83.06           C  
ANISOU  334  CD1 ILE A  46     9110  11786  10661   1790    521  -1377       C  
ATOM    335  N   GLN A  47     -37.391 -25.044  -2.077  1.00101.23           N  
ANISOU  335  N   GLN A  47     9132  14786  14547   1959    698  -1250       N  
ATOM    336  CA  GLN A  47     -38.647 -25.338  -1.396  1.00107.55           C  
ANISOU  336  CA  GLN A  47     9285  15862  15719   1921   1049  -1299       C  
ATOM    337  C   GLN A  47     -39.155 -26.687  -1.869  1.00109.58           C  
ANISOU  337  C   GLN A  47     9171  16198  16264   1596    804  -1104       C  
ATOM    338  O   GLN A  47     -39.615 -27.504  -1.076  1.00111.86           O  
ANISOU  338  O   GLN A  47     9161  16714  16627   1270   1160  -1017       O  
ATOM    339  CB  GLN A  47     -39.699 -24.274  -1.715  1.00111.92           C  
ANISOU  339  CB  GLN A  47     9414  16376  16734   2401   1020  -1523       C  
ATOM    340  CG  GLN A  47     -39.351 -22.868  -1.263  1.00112.14           C  
ANISOU  340  CG  GLN A  47     9790  16266  16554   2760   1270  -1751       C  
ATOM    341  CD  GLN A  47     -40.315 -21.828  -1.809  1.00116.70           C  
ANISOU  341  CD  GLN A  47    10014  16699  17628   3303   1096  -1947       C  
ATOM    342  OE1 GLN A  47     -40.191 -20.637  -1.522  1.00118.00           O  
ANISOU  342  OE1 GLN A  47    10425  16692  17718   3650   1269  -2153       O  
ATOM    343  NE2 GLN A  47     -41.280 -22.276  -2.603  1.00119.66           N  
ANISOU  343  NE2 GLN A  47     9816  17118  18533   3389    709  -1889       N  
ATOM    344  N   LYS A  48     -39.065 -26.902  -3.176  1.00109.62           N  
ANISOU  344  N   LYS A  48     9251  15992  16406   1666    199  -1042       N  
ATOM    345  CA  LYS A  48     -39.485 -28.152  -3.790  1.00112.13           C  
ANISOU  345  CA  LYS A  48     9296  16321  16989   1364   -130   -893       C  
ATOM    346  C   LYS A  48     -38.607 -29.300  -3.306  1.00110.22           C  
ANISOU  346  C   LYS A  48     9403  16078  16396    920      1   -691       C  
ATOM    347  O   LYS A  48     -39.101 -30.374  -2.972  1.00112.40           O  
ANISOU  347  O   LYS A  48     9382  16464  16862    562    106   -562       O  
ATOM    348  CB  LYS A  48     -39.404 -28.029  -5.313  1.00111.61           C  
ANISOU  348  CB  LYS A  48     9409  15993  17002   1553   -820   -898       C  
ATOM    349  CG  LYS A  48     -39.972 -29.208  -6.081  1.00114.00           C  
ANISOU  349  CG  LYS A  48     9421  16277  17616   1281  -1245   -807       C  
ATOM    350  CD  LYS A  48     -39.903 -28.956  -7.581  1.00114.12           C  
ANISOU  350  CD  LYS A  48     9705  16034  17620   1498  -1932   -838       C  
ATOM    351  CE  LYS A  48     -40.666 -30.013  -8.358  1.00117.61           C  
ANISOU  351  CE  LYS A  48     9800  16463  18422   1257  -2412   -807       C  
ATOM    352  NZ  LYS A  48     -40.586 -29.785  -9.826  1.00117.91           N  
ANISOU  352  NZ  LYS A  48    10196  16249  18356   1453  -3106   -841       N  
ATOM    353  N   ALA A  49     -37.302 -29.054  -3.261  1.00106.77           N  
ANISOU  353  N   ALA A  49     9589  15498  15479    947    -12   -665       N  
ATOM    354  CA  ALA A  49     -36.329 -30.050  -2.825  1.00105.41           C  
ANISOU  354  CA  ALA A  49     9780  15288  14984    611     44   -487       C  
ATOM    355  C   ALA A  49     -36.590 -30.503  -1.393  1.00109.89           C  
ANISOU  355  C   ALA A  49    10223  16087  15444    341    558   -381       C  
ATOM    356  O   ALA A  49     -36.583 -31.696  -1.098  1.00110.89           O  
ANISOU  356  O   ALA A  49    10347  16211  15577    -13    575   -178       O  
ATOM    357  CB  ALA A  49     -34.924 -29.497  -2.955  1.00100.58           C  
ANISOU  357  CB  ALA A  49     9754  14519  13944    735    -30   -532       C  
ATOM    358  N   HIS A  50     -36.810 -29.540  -0.507  1.00113.49           N  
ANISOU  358  N   HIS A  50    10635  16713  15771    504    985   -520       N  
ATOM    359  CA  HIS A  50     -37.148 -29.837   0.876  1.00118.38           C  
ANISOU  359  CA  HIS A  50    11182  17574  16224    259   1540   -449       C  
ATOM    360  C   HIS A  50     -38.489 -30.558   0.921  1.00123.74           C  
ANISOU  360  C   HIS A  50    11229  18406  17381     32   1713   -383       C  
ATOM    361  O   HIS A  50     -38.696 -31.457   1.734  1.00126.39           O  
ANISOU  361  O   HIS A  50    11548  18852  17622   -360   2027   -189       O  
ATOM    362  CB  HIS A  50     -37.208 -28.546   1.692  1.00121.78           C  
ANISOU  362  CB  HIS A  50    11690  18139  16444    523   1966   -687       C  
ATOM    363  CG  HIS A  50     -37.351 -28.765   3.165  1.00126.84           C  
ANISOU  363  CG  HIS A  50    12431  19018  16745    268   2559   -635       C  
ATOM    364  ND1 HIS A  50     -36.911 -29.912   3.794  1.00127.72           N  
ANISOU  364  ND1 HIS A  50    12823  19153  16553   -146   2611   -344       N  
ATOM    365  CD2 HIS A  50     -37.883 -27.986   4.135  1.00131.98           C  
ANISOU  365  CD2 HIS A  50    12995  19875  17275    370   3133   -838       C  
ATOM    366  CE1 HIS A  50     -37.167 -29.827   5.086  1.00132.31           C  
ANISOU  366  CE1 HIS A  50    13522  19954  16795   -311   3181   -344       C  
ATOM    367  NE2 HIS A  50     -37.758 -28.668   5.320  1.00134.94           N  
ANISOU  367  NE2 HIS A  50    13630  20416  17226     -9   3534   -662       N  
ATOM    368  N   GLU A  51     -39.395 -30.160   0.032  1.00125.62           N  
ANISOU  368  N   GLU A  51    10955  18636  18138    267   1484   -537       N  
ATOM    369  CA  GLU A  51     -40.687 -30.824  -0.106  1.00131.13           C  
ANISOU  369  CA  GLU A  51    10950  19471  19401     55   1547   -512       C  
ATOM    370  C   GLU A  51     -40.493 -32.217  -0.702  1.00129.02           C  
ANISOU  370  C   GLU A  51    10769  19029  19224   -338   1151   -276       C  
ATOM    371  O   GLU A  51     -41.251 -33.141  -0.404  1.00133.62           O  
ANISOU  371  O   GLU A  51    10970  19704  20097   -735   1332   -154       O  
ATOM    372  CB  GLU A  51     -41.631 -29.983  -0.975  1.00134.51           C  
ANISOU  372  CB  GLU A  51    10817  19910  20381    466   1273   -752       C  
ATOM    373  CG  GLU A  51     -43.023 -30.573  -1.182  1.00141.62           C  
ANISOU  373  CG  GLU A  51    10866  20973  21971    276   1275   -778       C  
ATOM    374  CD  GLU A  51     -43.115 -31.456  -2.414  1.00141.34           C  
ANISOU  374  CD  GLU A  51    10761  20737  22205    103    566   -675       C  
ATOM    375  OE1 GLU A  51     -42.889 -30.950  -3.533  1.00139.21           O  
ANISOU  375  OE1 GLU A  51    10665  20268  21960    445    -36   -759       O  
ATOM    376  OE2 GLU A  51     -43.415 -32.658  -2.261  1.00143.86           O  
ANISOU  376  OE2 GLU A  51    10902  21074  22683   -393    616   -511       O  
ATOM    377  N   GLU A  52     -39.468 -32.359  -1.539  1.00122.48           N  
ANISOU  377  N   GLU A  52    10454  17932  18153   -241    644   -229       N  
ATOM    378  CA  GLU A  52     -39.120 -33.656  -2.112  1.00119.54           C  
ANISOU  378  CA  GLU A  52    10269  17338  17811   -566    271    -44       C  
ATOM    379  C   GLU A  52     -38.178 -34.432  -1.191  1.00115.37           C  
ANISOU  379  C   GLU A  52    10253  16744  16837   -856    502    194       C  
ATOM    380  O   GLU A  52     -37.650 -35.475  -1.570  1.00113.43           O  
ANISOU  380  O   GLU A  52    10284  16260  16554  -1072    207    347       O  
ATOM    381  CB  GLU A  52     -38.500 -33.491  -3.506  1.00116.50           C  
ANISOU  381  CB  GLU A  52    10187  16688  17388   -322   -351   -136       C  
ATOM    382  CG  GLU A  52     -39.493 -33.058  -4.582  1.00119.81           C  
ANISOU  382  CG  GLU A  52    10156  17106  18260   -109   -753   -306       C  
ATOM    383  CD  GLU A  52     -38.836 -32.764  -5.921  1.00116.76           C  
ANISOU  383  CD  GLU A  52    10200  16458  17706    139  -1318   -390       C  
ATOM    384  OE1 GLU A  52     -37.593 -32.654  -5.975  1.00112.14           O  
ANISOU  384  OE1 GLU A  52    10203  15728  16679    203  -1306   -362       O  
ATOM    385  OE2 GLU A  52     -39.568 -32.641  -6.924  1.00119.40           O  
ANISOU  385  OE2 GLU A  52    10282  16738  18349    261  -1776   -491       O  
ATOM    386  N   GLY A  53     -37.973 -33.913   0.018  1.00114.02           N  
ANISOU  386  N   GLY A  53    10232  16766  16322   -840   1002    212       N  
ATOM    387  CA  GLY A  53     -37.171 -34.592   1.021  1.00111.55           C  
ANISOU  387  CA  GLY A  53    10412  16416  15558  -1105   1202    455       C  
ATOM    388  C   GLY A  53     -35.675 -34.436   0.835  1.00104.27           C  
ANISOU  388  C   GLY A  53    10084  15304  14229   -913    887    461       C  
ATOM    389  O   GLY A  53     -34.971 -35.404   0.551  1.00102.66           O  
ANISOU  389  O   GLY A  53    10174  14860  13973  -1055    579    627       O  
ATOM    390  N   ILE A  54     -35.183 -33.214   1.005  1.00100.22           N  
ANISOU  390  N   ILE A  54     9730  14883  13465   -591    975    262       N  
ATOM    391  CA  ILE A  54     -33.762 -32.945   0.823  1.00 94.28           C  
ANISOU  391  CA  ILE A  54     9463  13978  12383   -424    706    226       C  
ATOM    392  C   ILE A  54     -33.197 -32.076   1.944  1.00 94.57           C  
ANISOU  392  C   ILE A  54     9797  14176  11962   -336   1006    149       C  
ATOM    393  O   ILE A  54     -33.637 -30.946   2.146  1.00 95.88           O  
ANISOU  393  O   ILE A  54     9833  14483  12114   -130   1262    -70       O  
ATOM    394  CB  ILE A  54     -33.489 -32.292  -0.544  1.00 89.33           C  
ANISOU  394  CB  ILE A  54     8810  13193  11940   -121    342     18       C  
ATOM    395  CG1 ILE A  54     -33.603 -33.337  -1.654  1.00 87.88           C  
ANISOU  395  CG1 ILE A  54     8548  12789  12055   -237    -56     97       C  
ATOM    396  CG2 ILE A  54     -32.116 -31.662  -0.568  1.00 85.45           C  
ANISOU  396  CG2 ILE A  54     8742  12611  11114     52    228    -83       C  
ATOM    397  CD1 ILE A  54     -33.336 -32.794  -3.029  1.00 84.93           C  
ANISOU  397  CD1 ILE A  54     8240  12249  11779     20   -409    -86       C  
ATOM    398  N   CYS A  55     -32.223 -32.621   2.669  1.00 93.95           N  
ANISOU  398  N   CYS A  55    10131  14050  11516   -481    936    318       N  
ATOM    399  CA  CYS A  55     -31.580 -31.914   3.771  1.00 94.29           C  
ANISOU  399  CA  CYS A  55    10522  14233  11072   -441   1130    251       C  
ATOM    400  C   CYS A  55     -30.885 -30.655   3.278  1.00 90.82           C  
ANISOU  400  C   CYS A  55    10173  13748  10586   -134   1002    -48       C  
ATOM    401  O   CYS A  55     -31.115 -29.564   3.795  1.00 91.45           O  
ANISOU  401  O   CYS A  55    10287  13962  10498     -5   1289   -257       O  
ATOM    402  CB  CYS A  55     -30.567 -32.826   4.458  1.00 94.45           C  
ANISOU  402  CB  CYS A  55    10965  14162  10761   -623    909    504       C  
ATOM    403  SG  CYS A  55     -29.534 -33.745   3.301  1.00154.01           S  
ANISOU  403  SG  CYS A  55    18557  21372  18587   -558    321    587       S  
ATOM    404  N   GLY A  56     -30.034 -30.817   2.272  1.00 87.71           N  
ANISOU  404  N   GLY A  56     9839  13143  10343    -33    602    -78       N  
ATOM    405  CA  GLY A  56     -29.300 -29.701   1.709  1.00 85.18           C  
ANISOU  405  CA  GLY A  56     9632  12740   9992    197    491   -333       C  
ATOM    406  C   GLY A  56     -28.677 -30.057   0.377  1.00 81.85           C  
ANISOU  406  C   GLY A  56     9199  12087   9812    268    135   -349       C  
ATOM    407  O   GLY A  56     -29.036 -31.057  -0.231  1.00 81.64           O  
ANISOU  407  O   GLY A  56     9034  11961  10023    185    -25   -209       O  
ATOM    408  N   ILE A  57     -27.740 -29.237  -0.081  1.00 80.04           N  
ANISOU  408  N   ILE A  57     9137  11761   9515    395     39   -538       N  
ATOM    409  CA  ILE A  57     -27.097 -29.468  -1.368  1.00 78.01           C  
ANISOU  409  CA  ILE A  57     8910  11293   9438    453   -212   -589       C  
ATOM    410  C   ILE A  57     -25.583 -29.383  -1.251  1.00 77.78           C  
ANISOU  410  C   ILE A  57     9064  11205   9284    426   -330   -677       C  
ATOM    411  O   ILE A  57     -25.056 -28.668  -0.398  1.00 78.67           O  
ANISOU  411  O   ILE A  57     9299  11416   9175    408   -243   -774       O  
ATOM    412  CB  ILE A  57     -27.571 -28.449  -2.410  1.00 76.83           C  
ANISOU  412  CB  ILE A  57     8752  11038   9403    635   -190   -751       C  
ATOM    413  CG1 ILE A  57     -27.232 -27.032  -1.957  1.00 76.75           C  
ANISOU  413  CG1 ILE A  57     8911  11047   9204    733     -5   -943       C  
ATOM    414  CG2 ILE A  57     -29.067 -28.567  -2.627  1.00 78.75           C  
ANISOU  414  CG2 ILE A  57     8724  11336   9860    695   -154   -685       C  
ATOM    415  CD1 ILE A  57     -28.035 -25.966  -2.654  1.00 77.27           C  
ANISOU  415  CD1 ILE A  57     8975  11005   9377    946     49  -1057       C  
ATOM    416  N   ARG A  58     -24.881 -30.118  -2.104  1.00 77.45           N  
ANISOU  416  N   ARG A  58     9021  11002   9403    419   -529   -671       N  
ATOM    417  CA  ARG A  58     -23.424 -30.043  -2.124  1.00 78.01           C  
ANISOU  417  CA  ARG A  58     9164  11020   9455    410   -625   -792       C  
ATOM    418  C   ARG A  58     -22.925 -29.484  -3.447  1.00 76.83           C  
ANISOU  418  C   ARG A  58     9073  10709   9409    469   -582   -986       C  
ATOM    419  O   ARG A  58     -23.412 -29.853  -4.516  1.00 75.76           O  
ANISOU  419  O   ARG A  58     8950  10444   9393    511   -622   -971       O  
ATOM    420  CB  ARG A  58     -22.790 -31.406  -1.846  1.00 79.91           C  
ANISOU  420  CB  ARG A  58     9354  11202   9805    367   -857   -649       C  
ATOM    421  CG  ARG A  58     -23.172 -31.985  -0.498  1.00 83.16           C  
ANISOU  421  CG  ARG A  58     9810  11741  10046    274   -908   -414       C  
ATOM    422  CD  ARG A  58     -22.133 -32.971   0.017  1.00 85.61           C  
ANISOU  422  CD  ARG A  58    10149  11978  10401    271  -1201   -304       C  
ATOM    423  NE  ARG A  58     -20.936 -32.291   0.502  1.00 86.85           N  
ANISOU  423  NE  ARG A  58    10315  12222  10465    300  -1301   -474       N  
ATOM    424  CZ  ARG A  58     -20.797 -31.819   1.736  1.00 89.24           C  
ANISOU  424  CZ  ARG A  58    10758  12699  10450    229  -1335   -443       C  
ATOM    425  NH1 ARG A  58     -19.675 -31.213   2.093  1.00 90.30           N  
ANISOU  425  NH1 ARG A  58    10871  12898  10542    233  -1482   -631       N  
ATOM    426  NH2 ARG A  58     -21.781 -31.951   2.615  1.00 90.92           N  
ANISOU  426  NH2 ARG A  58    11135  13027  10383    132  -1209   -244       N  
ATOM    427  N   SER A  59     -21.952 -28.585  -3.358  1.00 77.45           N  
ANISOU  427  N   SER A  59     9219  10790   9418    440   -500  -1171       N  
ATOM    428  CA  SER A  59     -21.430 -27.896  -4.527  1.00 77.45           C  
ANISOU  428  CA  SER A  59     9332  10632   9463    441   -380  -1349       C  
ATOM    429  C   SER A  59     -20.530 -28.806  -5.348  1.00 77.96           C  
ANISOU  429  C   SER A  59     9320  10587   9716    426   -439  -1409       C  
ATOM    430  O   SER A  59     -19.892 -29.708  -4.812  1.00 78.71           O  
ANISOU  430  O   SER A  59     9243  10726   9938    425   -593  -1373       O  
ATOM    431  CB  SER A  59     -20.660 -26.650  -4.095  1.00 78.17           C  
ANISOU  431  CB  SER A  59     9508  10744   9449    356   -243  -1534       C  
ATOM    432  OG  SER A  59     -21.405 -25.902  -3.153  1.00 78.62           O  
ANISOU  432  OG  SER A  59     9645  10900   9327    385   -184  -1514       O  
ATOM    433  N   VAL A  60     -20.490 -28.564  -6.653  1.00 78.59           N  
ANISOU  433  N   VAL A  60     9558  10503   9799    431   -317  -1506       N  
ATOM    434  CA  VAL A  60     -19.639 -29.333  -7.548  1.00 80.02           C  
ANISOU  434  CA  VAL A  60     9705  10567  10132    420   -283  -1622       C  
ATOM    435  C   VAL A  60     -18.266 -28.693  -7.600  1.00 80.86           C  
ANISOU  435  C   VAL A  60     9733  10680  10308    308    -78  -1844       C  
ATOM    436  O   VAL A  60     -17.248 -29.382  -7.596  1.00 82.26           O  
ANISOU  436  O   VAL A  60     9676  10865  10715    311    -87  -1960       O  
ATOM    437  CB  VAL A  60     -20.211 -29.361  -8.968  1.00 81.24           C  
ANISOU  437  CB  VAL A  60    10138  10545  10186    444   -221  -1642       C  
ATOM    438  CG1 VAL A  60     -19.534 -30.444  -9.795  1.00 82.75           C  
ANISOU  438  CG1 VAL A  60    10307  10615  10520    457   -195  -1764       C  
ATOM    439  CG2 VAL A  60     -21.693 -29.590  -8.919  1.00 81.09           C  
ANISOU  439  CG2 VAL A  60    10167  10535  10108    526   -429  -1449       C  
ATOM    440  N   THR A  61     -18.252 -27.365  -7.649  1.00 79.77           N  
ANISOU  440  N   THR A  61     9775  10522  10012    209    104  -1913       N  
ATOM    441  CA  THR A  61     -17.007 -26.615  -7.727  1.00 80.26           C  
ANISOU  441  CA  THR A  61     9772  10572  10151     32    332  -2132       C  
ATOM    442  C   THR A  61     -16.893 -25.589  -6.605  1.00 79.76           C  
ANISOU  442  C   THR A  61     9687  10605  10013    -62    299  -2166       C  
ATOM    443  O   THR A  61     -17.844 -25.365  -5.858  1.00 78.34           O  
ANISOU  443  O   THR A  61     9598  10490   9678     31    161  -2029       O  
ATOM    444  CB  THR A  61     -16.876 -25.898  -9.077  1.00 80.94           C  
ANISOU  444  CB  THR A  61    10200  10454  10098    -83    657  -2224       C  
ATOM    445  OG1 THR A  61     -15.796 -24.956  -9.016  1.00 83.09           O  
ANISOU  445  OG1 THR A  61    10427  10705  10437   -320    919  -2419       O  
ATOM    446  CG2 THR A  61     -18.160 -25.163  -9.413  1.00 79.62           C  
ANISOU  446  CG2 THR A  61    10435  10163   9653      2    609  -2061       C  
ATOM    447  N   ARG A  62     -15.720 -24.971  -6.498  1.00 81.33           N  
ANISOU  447  N   ARG A  62     9756  10810  10335   -263    448  -2378       N  
ATOM    448  CA  ARG A  62     -15.465 -23.969  -5.471  1.00 81.87           C  
ANISOU  448  CA  ARG A  62     9826  10942  10339   -398    404  -2468       C  
ATOM    449  C   ARG A  62     -16.314 -22.726  -5.700  1.00 79.54           C  
ANISOU  449  C   ARG A  62     9969  10469   9785   -418    566  -2431       C  
ATOM    450  O   ARG A  62     -16.906 -22.188  -4.764  1.00 79.51           O  
ANISOU  450  O   ARG A  62    10070  10512   9629   -365    459  -2403       O  
ATOM    451  CB  ARG A  62     -13.977 -23.599  -5.450  1.00 86.26           C  
ANISOU  451  CB  ARG A  62    10105  11523  11149   -654    523  -2732       C  
ATOM    452  CG  ARG A  62     -13.596 -22.555  -4.410  1.00 89.42           C  
ANISOU  452  CG  ARG A  62    10510  11969  11498   -846    439  -2875       C  
ATOM    453  CD  ARG A  62     -13.238 -21.225  -5.055  1.00 92.51           C  
ANISOU  453  CD  ARG A  62    11161  12130  11860  -1131    801  -3032       C  
ATOM    454  NE  ARG A  62     -11.800 -21.067  -5.262  1.00 96.89           N  
ANISOU  454  NE  ARG A  62    11351  12712  12749  -1432    954  -3290       N  
ATOM    455  CZ  ARG A  62     -11.237 -19.989  -5.800  1.00100.27           C  
ANISOU  455  CZ  ARG A  62    11934  12943  13221  -1772   1305  -3452       C  
ATOM    456  NH1 ARG A  62      -9.921 -19.927  -5.947  1.00104.40           N  
ANISOU  456  NH1 ARG A  62    12030  13526  14110  -2068   1462  -3704       N  
ATOM    457  NH2 ARG A  62     -11.987 -18.970  -6.193  1.00 99.95           N  
ANISOU  457  NH2 ARG A  62    12464  12626  12887  -1819   1500  -3360       N  
ATOM    458  N   LEU A  63     -16.378 -22.286  -6.951  1.00 78.22           N  
ANISOU  458  N   LEU A  63    10090  10077   9555   -477    825  -2433       N  
ATOM    459  CA  LEU A  63     -17.103 -21.069  -7.294  1.00 77.25           C  
ANISOU  459  CA  LEU A  63    10427   9713   9211   -473    950  -2384       C  
ATOM    460  C   LEU A  63     -18.594 -21.198  -6.996  1.00 73.93           C  
ANISOU  460  C   LEU A  63    10123   9316   8651   -167    740  -2190       C  
ATOM    461  O   LEU A  63     -19.241 -20.228  -6.606  1.00 74.97           O  
ANISOU  461  O   LEU A  63    10483   9333   8668    -91    747  -2186       O  
ATOM    462  CB  LEU A  63     -16.885 -20.694  -8.760  1.00 79.02           C  
ANISOU  462  CB  LEU A  63    11007   9675   9342   -594   1233  -2378       C  
ATOM    463  CG  LEU A  63     -15.453 -20.569  -9.281  1.00 82.02           C  
ANISOU  463  CG  LEU A  63    11274  10017   9873   -930   1564  -2580       C  
ATOM    464  CD1 LEU A  63     -15.440 -19.805 -10.594  1.00 84.34           C  
ANISOU  464  CD1 LEU A  63    12113   9988   9944  -1091   1896  -2539       C  
ATOM    465  CD2 LEU A  63     -14.536 -19.913  -8.267  1.00 84.20           C  
ANISOU  465  CD2 LEU A  63    11290  10368  10332  -1177   1585  -2787       C  
ATOM    466  N   GLU A  64     -19.131 -22.398  -7.180  1.00 70.25           N  
ANISOU  466  N   GLU A  64     9477   8983   8233      2    568  -2050       N  
ATOM    467  CA  GLU A  64     -20.522 -22.664  -6.846  1.00 67.52           C  
ANISOU  467  CA  GLU A  64     9125   8702   7828    251    381  -1878       C  
ATOM    468  C   GLU A  64     -20.744 -22.446  -5.358  1.00 66.20           C  
ANISOU  468  C   GLU A  64     8800   8720   7633    278    318  -1906       C  
ATOM    469  O   GLU A  64     -21.705 -21.803  -4.950  1.00 66.30           O  
ANISOU  469  O   GLU A  64     8923   8705   7562    425    329  -1879       O  
ATOM    470  CB  GLU A  64     -20.893 -24.095  -7.229  1.00 66.18           C  
ANISOU  470  CB  GLU A  64     8758   8635   7753    347    209  -1747       C  
ATOM    471  CG  GLU A  64     -22.301 -24.500  -6.838  1.00 65.57           C  
ANISOU  471  CG  GLU A  64     8581   8653   7679    542     29  -1577       C  
ATOM    472  CD  GLU A  64     -22.657 -25.888  -7.322  1.00 64.79           C  
ANISOU  472  CD  GLU A  64     8331   8596   7691    583   -146  -1459       C  
ATOM    473  OE1 GLU A  64     -21.837 -26.487  -8.044  1.00 64.78           O  
ANISOU  473  OE1 GLU A  64     8352   8524   7739    502   -120  -1525       O  
ATOM    474  OE2 GLU A  64     -23.755 -26.377  -6.980  1.00 64.60           O  
ANISOU  474  OE2 GLU A  64     8159   8664   7723    684   -286  -1322       O  
ATOM    475  N   ASN A  65     -19.837 -22.987  -4.557  1.00 65.70           N  
ANISOU  475  N   ASN A  65     8489   8838   7636    149    245  -1974       N  
ATOM    476  CA  ASN A  65     -19.870 -22.804  -3.113  1.00 65.83           C  
ANISOU  476  CA  ASN A  65     8431   9035   7546    130    165  -2015       C  
ATOM    477  C   ASN A  65     -19.829 -21.322  -2.749  1.00 67.85           C  
ANISOU  477  C   ASN A  65     8949   9156   7674     62    318  -2196       C  
ATOM    478  O   ASN A  65     -20.623 -20.857  -1.932  1.00 68.79           O  
ANISOU  478  O   ASN A  65     9170   9323   7642    171    348  -2209       O  
ATOM    479  CB  ASN A  65     -18.707 -23.569  -2.466  1.00 65.19           C  
ANISOU  479  CB  ASN A  65     8082   9125   7562     -3    -14  -2065       C  
ATOM    480  CG  ASN A  65     -18.669 -23.424  -0.960  1.00 65.53           C  
ANISOU  480  CG  ASN A  65     8126   9356   7416    -45   -154  -2097       C  
ATOM    481  OD1 ASN A  65     -17.615 -23.167  -0.379  1.00 66.47           O  
ANISOU  481  OD1 ASN A  65     8168   9538   7551   -208   -274  -2259       O  
ATOM    482  ND2 ASN A  65     -19.815 -23.596  -0.318  1.00 65.42           N  
ANISOU  482  ND2 ASN A  65     8199   9441   7216     85   -138  -1957       N  
ATOM    483  N   LEU A  66     -18.918 -20.582  -3.377  1.00 69.25           N  
ANISOU  483  N   LEU A  66     9249   9144   7919   -129    450  -2349       N  
ATOM    484  CA  LEU A  66     -18.804 -19.152  -3.119  1.00 72.17           C  
ANISOU  484  CA  LEU A  66     9916   9309   8194   -234    595  -2529       C  
ATOM    485  C   LEU A  66     -20.105 -18.438  -3.466  1.00 74.14           C  
ANISOU  485  C   LEU A  66    10472   9352   8347     23    685  -2445       C  
ATOM    486  O   LEU A  66     -20.517 -17.501  -2.778  1.00 76.12           O  
ANISOU  486  O   LEU A  66    10923   9505   8493     84    750  -2567       O  
ATOM    487  CB  LEU A  66     -17.635 -18.543  -3.895  1.00 73.05           C  
ANISOU  487  CB  LEU A  66    10116   9216   8425   -532    765  -2676       C  
ATOM    488  CG  LEU A  66     -16.239 -19.081  -3.578  1.00 73.83           C  
ANISOU  488  CG  LEU A  66     9833   9504   8717   -790    687  -2823       C  
ATOM    489  CD1 LEU A  66     -15.159 -18.188  -4.172  1.00 76.53           C  
ANISOU  489  CD1 LEU A  66    10257   9628   9191  -1143    932  -3020       C  
ATOM    490  CD2 LEU A  66     -16.040 -19.239  -2.084  1.00 74.84           C  
ANISOU  490  CD2 LEU A  66     9786   9878   8771   -808    423  -2916       C  
ATOM    491  N   MET A  67     -20.756 -18.897  -4.528  1.00 74.34           N  
ANISOU  491  N   MET A  67    10527   9300   8420    190    662  -2256       N  
ATOM    492  CA  MET A  67     -22.038 -18.338  -4.926  1.00 76.82           C  
ANISOU  492  CA  MET A  67    11057   9430   8700    480    658  -2159       C  
ATOM    493  C   MET A  67     -23.085 -18.587  -3.852  1.00 78.52           C  
ANISOU  493  C   MET A  67    11061   9868   8903    704    609  -2141       C  
ATOM    494  O   MET A  67     -23.759 -17.660  -3.413  1.00 80.40           O  
ANISOU  494  O   MET A  67    11457   9982   9110    876    696  -2235       O  
ATOM    495  CB  MET A  67     -22.499 -18.947  -6.247  1.00 75.93           C  
ANISOU  495  CB  MET A  67    10988   9235   8626    594    557  -1964       C  
ATOM    496  CG  MET A  67     -23.886 -18.507  -6.669  1.00 77.20           C  
ANISOU  496  CG  MET A  67    11291   9239   8805    930    444  -1850       C  
ATOM    497  SD  MET A  67     -24.581 -19.582  -7.931  1.00183.52           S  
ANISOU  497  SD  MET A  67    24689  22729  22313   1062    197  -1631       S  
ATOM    498  CE  MET A  67     -24.537 -21.157  -7.080  1.00 48.10           C  
ANISOU  498  CE  MET A  67     6997   6000   5280    980    131  -1595       C  
ATOM    499  N   TRP A  68     -23.211 -19.843  -3.434  1.00 78.70           N  
ANISOU  499  N   TRP A  68    10745  10200   8958    695    500  -2028       N  
ATOM    500  CA  TRP A  68     -24.170 -20.214  -2.403  1.00 81.02           C  
ANISOU  500  CA  TRP A  68    10835  10730   9217    841    514  -1987       C  
ATOM    501  C   TRP A  68     -23.967 -19.378  -1.156  1.00 84.21           C  
ANISOU  501  C   TRP A  68    11380  11177   9441    789    657  -2199       C  
ATOM    502  O   TRP A  68     -24.926 -18.954  -0.523  1.00 86.18           O  
ANISOU  502  O   TRP A  68    11634  11464   9645    977    797  -2260       O  
ATOM    503  CB  TRP A  68     -24.049 -21.696  -2.053  1.00 79.92           C  
ANISOU  503  CB  TRP A  68    10394  10870   9101    746    381  -1825       C  
ATOM    504  CG  TRP A  68     -24.587 -22.582  -3.110  1.00 78.96           C  
ANISOU  504  CG  TRP A  68    10130  10719   9153    830    246  -1638       C  
ATOM    505  CD1 TRP A  68     -23.898 -23.506  -3.835  1.00 77.64           C  
ANISOU  505  CD1 TRP A  68     9896  10536   9068    717    112  -1562       C  
ATOM    506  CD2 TRP A  68     -25.935 -22.621  -3.583  1.00 79.99           C  
ANISOU  506  CD2 TRP A  68    10160  10820   9412   1049    211  -1537       C  
ATOM    507  NE1 TRP A  68     -24.738 -24.127  -4.727  1.00 77.40           N  
ANISOU  507  NE1 TRP A  68     9790  10457   9162    830     -9  -1423       N  
ATOM    508  CE2 TRP A  68     -25.996 -23.599  -4.592  1.00 78.95           C  
ANISOU  508  CE2 TRP A  68     9943  10653   9401   1025     20  -1398       C  
ATOM    509  CE3 TRP A  68     -27.099 -21.926  -3.248  1.00 82.25           C  
ANISOU  509  CE3 TRP A  68    10392  11102   9755   1275    314  -1577       C  
ATOM    510  CZ2 TRP A  68     -27.177 -23.898  -5.271  1.00 79.85           C  
ANISOU  510  CZ2 TRP A  68     9928  10737   9675   1187   -123  -1289       C  
ATOM    511  CZ3 TRP A  68     -28.266 -22.223  -3.919  1.00 83.20           C  
ANISOU  511  CZ3 TRP A  68    10318  11206  10088   1464    185  -1466       C  
ATOM    512  CH2 TRP A  68     -28.299 -23.200  -4.918  1.00 81.93           C  
ANISOU  512  CH2 TRP A  68    10081  11018  10029   1403    -58  -1318       C  
ATOM    513  N   LYS A  69     -22.707 -19.144  -0.815  1.00 85.79           N  
ANISOU  513  N   LYS A  69    11678  11368   9551    529    623  -2339       N  
ATOM    514  CA  LYS A  69     -22.380 -18.301   0.322  1.00 89.76           C  
ANISOU  514  CA  LYS A  69    12371  11879   9852    432    706  -2581       C  
ATOM    515  C   LYS A  69     -22.879 -16.873   0.108  1.00 92.85           C  
ANISOU  515  C   LYS A  69    13090  11937  10253    578    890  -2754       C  
ATOM    516  O   LYS A  69     -23.625 -16.337   0.928  1.00 95.00           O  
ANISOU  516  O   LYS A  69    13465  12223  10407    741   1040  -2888       O  
ATOM    517  CB  LYS A  69     -20.871 -18.310   0.561  1.00 90.96           C  
ANISOU  517  CB  LYS A  69    12516  12062   9982    103    567  -2711       C  
ATOM    518  CG  LYS A  69     -20.335 -19.661   1.001  1.00 90.50           C  
ANISOU  518  CG  LYS A  69    12157  12312   9918      7    335  -2568       C  
ATOM    519  CD  LYS A  69     -18.818 -19.699   0.992  1.00 91.80           C  
ANISOU  519  CD  LYS A  69    12206  12486  10188   -272    160  -2702       C  
ATOM    520  CE  LYS A  69     -18.316 -20.974   1.643  1.00 92.19           C  
ANISOU  520  CE  LYS A  69    11988  12816  10223   -308   -135  -2572       C  
ATOM    521  NZ  LYS A  69     -16.869 -21.216   1.386  1.00 93.28           N  
ANISOU  521  NZ  LYS A  69    11872  12966  10604   -510   -328  -2683       N  
ATOM    522  N   GLN A  70     -22.482 -16.270  -1.008  1.00 93.41           N  
ANISOU  522  N   GLN A  70    13352  11683  10457    528    898  -2748       N  
ATOM    523  CA  GLN A  70     -22.803 -14.872  -1.277  1.00 96.92           C  
ANISOU  523  CA  GLN A  70    14188  11720  10918    644   1033  -2890       C  
ATOM    524  C   GLN A  70     -24.283 -14.630  -1.563  1.00 97.99           C  
ANISOU  524  C   GLN A  70    14326  11749  11157   1082   1074  -2800       C  
ATOM    525  O   GLN A  70     -24.721 -13.484  -1.641  1.00101.56           O  
ANISOU  525  O   GLN A  70    15089  11852  11648   1271   1166  -2924       O  
ATOM    526  CB  GLN A  70     -21.956 -14.343  -2.439  1.00 97.66           C  
ANISOU  526  CB  GLN A  70    14541  11472  11093    429   1046  -2862       C  
ATOM    527  CG  GLN A  70     -20.460 -14.283  -2.155  1.00 98.72           C  
ANISOU  527  CG  GLN A  70    14649  11651  11209    -20   1053  -3027       C  
ATOM    528  CD  GLN A  70     -19.664 -13.722  -3.321  1.00100.13           C  
ANISOU  528  CD  GLN A  70    15081  11488  11477   -275   1167  -3006       C  
ATOM    529  OE1 GLN A  70     -20.185 -13.566  -4.425  1.00100.20           O  
ANISOU  529  OE1 GLN A  70    15315  11254  11503   -118   1203  -2818       O  
ATOM    530  NE2 GLN A  70     -18.393 -13.415  -3.079  1.00101.92           N  
ANISOU  530  NE2 GLN A  70    15279  11695  11753   -690   1220  -3200       N  
ATOM    531  N   ILE A  71     -25.053 -15.702  -1.718  1.00 95.82           N  
ANISOU  531  N   ILE A  71    13688  11751  10967   1246    987  -2595       N  
ATOM    532  CA  ILE A  71     -26.458 -15.566  -2.092  1.00 96.98           C  
ANISOU  532  CA  ILE A  71    13727  11827  11296   1651    975  -2509       C  
ATOM    533  C   ILE A  71     -27.408 -16.056  -1.000  1.00 96.28           C  
ANISOU  533  C   ILE A  71    13289  12080  11212   1809   1120  -2554       C  
ATOM    534  O   ILE A  71     -28.585 -15.700  -0.988  1.00 98.46           O  
ANISOU  534  O   ILE A  71    13432  12306  11672   2158   1195  -2588       O  
ATOM    535  CB  ILE A  71     -26.762 -16.304  -3.413  1.00 97.18           C  
ANISOU  535  CB  ILE A  71    13629  11828  11468   1719    739  -2237       C  
ATOM    536  CG1 ILE A  71     -28.025 -15.738  -4.065  1.00100.63           C  
ANISOU  536  CG1 ILE A  71    14087  12033  12115   2141    630  -2177       C  
ATOM    537  CG2 ILE A  71     -26.885 -17.803  -3.184  1.00 95.31           C  
ANISOU  537  CG2 ILE A  71    12961  11998  11255   1608    658  -2082       C  
ATOM    538  CD1 ILE A  71     -28.515 -16.532  -5.256  1.00 99.96           C  
ANISOU  538  CD1 ILE A  71    13861  11967  12152   2227    337  -1928       C  
ATOM    539  N   THR A  72     -26.884 -16.866  -0.085  1.00 93.19           N  
ANISOU  539  N   THR A  72    12754  12029  10627   1550   1164  -2555       N  
ATOM    540  CA  THR A  72     -27.671 -17.429   1.016  1.00 92.35           C  
ANISOU  540  CA  THR A  72    12385  12264  10440   1610   1352  -2568       C  
ATOM    541  C   THR A  72     -28.555 -16.420   1.774  1.00 94.09           C  
ANISOU  541  C   THR A  72    12686  12412  10652   1884   1664  -2830       C  
ATOM    542  O   THR A  72     -29.734 -16.698   2.007  1.00 95.16           O  
ANISOU  542  O   THR A  72    12497  12712  10948   2108   1835  -2806       O  
ATOM    543  CB  THR A  72     -26.783 -18.224   2.009  1.00137.78           C  
ANISOU  543  CB  THR A  72    18149  18316  15885   1270   1324  -2546       C  
ATOM    544  OG1 THR A  72     -26.116 -19.283   1.312  1.00134.24           O  
ANISOU  544  OG1 THR A  72    17547  17937  15523   1088   1054  -2309       O  
ATOM    545  CG2 THR A  72     -27.619 -18.819   3.129  1.00140.03           C  
ANISOU  545  CG2 THR A  72    18254  18932  16018   1292   1557  -2521       C  
ATOM    546  N   PRO A  73     -28.001 -15.249   2.156  1.00 94.17           N  
ANISOU  546  N   PRO A  73    13109  12164  10507   1862   1757  -3107       N  
ATOM    547  CA  PRO A  73     -28.871 -14.298   2.854  1.00 97.45           C  
ANISOU  547  CA  PRO A  73    13618  12474  10935   2163   2077  -3395       C  
ATOM    548  C   PRO A  73     -30.055 -13.874   2.001  1.00 97.61           C  
ANISOU  548  C   PRO A  73    13431  12273  11383   2621   2069  -3350       C  
ATOM    549  O   PRO A  73     -31.185 -13.878   2.485  1.00100.82           O  
ANISOU  549  O   PRO A  73    13536  12828  11943   2904   2327  -3448       O  
ATOM    550  CB  PRO A  73     -27.951 -13.097   3.100  1.00 99.56           C  
ANISOU  550  CB  PRO A  73    14419  12389  11021   2035   2084  -3679       C  
ATOM    551  CG  PRO A  73     -26.840 -13.246   2.125  1.00 96.33           C  
ANISOU  551  CG  PRO A  73    14131  11816  10653   1755   1770  -3498       C  
ATOM    552  CD  PRO A  73     -26.633 -14.718   2.017  1.00 92.93           C  
ANISOU  552  CD  PRO A  73    13325  11791  10194   1564   1612  -3208       C  
ATOM    553  N   GLU A  74     -29.793 -13.522   0.748  1.00 94.70           N  
ANISOU  553  N   GLU A  74    13220  11558  11203   2688   1773  -3203       N  
ATOM    554  CA  GLU A  74     -30.849 -13.109  -0.159  1.00 95.60           C  
ANISOU  554  CA  GLU A  74    13196  11423  11706   3135   1642  -3127       C  
ATOM    555  C   GLU A  74     -31.864 -14.227  -0.329  1.00 93.57           C  
ANISOU  555  C   GLU A  74    12322  11537  11692   3254   1589  -2931       C  
ATOM    556  O   GLU A  74     -33.065 -13.986  -0.323  1.00 97.36           O  
ANISOU  556  O   GLU A  74    12470  12016  12508   3651   1664  -3003       O  
ATOM    557  CB  GLU A  74     -30.266 -12.720  -1.513  1.00 94.39           C  
ANISOU  557  CB  GLU A  74    13404  10863  11597   3095   1301  -2940       C  
ATOM    558  CG  GLU A  74     -31.280 -12.129  -2.466  1.00 98.09           C  
ANISOU  558  CG  GLU A  74    13866  10991  12413   3578   1077  -2855       C  
ATOM    559  CD  GLU A  74     -30.643 -11.608  -3.732  1.00 98.01           C  
ANISOU  559  CD  GLU A  74    14378  10524  12336   3506    783  -2671       C  
ATOM    560  OE1 GLU A  74     -29.950 -12.390  -4.412  1.00 94.20           O  
ANISOU  560  OE1 GLU A  74    13925  10167  11699   3175    625  -2454       O  
ATOM    561  OE2 GLU A  74     -30.829 -10.414  -4.045  1.00102.15           O  
ANISOU  561  OE2 GLU A  74    15318  10542  12953   3776    734  -2746       O  
ATOM    562  N   LEU A  75     -31.369 -15.452  -0.464  1.00 87.99           N  
ANISOU  562  N   LEU A  75    11444  11134  10854   2905   1460  -2702       N  
ATOM    563  CA  LEU A  75     -32.233 -16.613  -0.617  1.00 86.26           C  
ANISOU  563  CA  LEU A  75    10674  11247  10854   2926   1398  -2507       C  
ATOM    564  C   LEU A  75     -33.117 -16.811   0.602  1.00 88.46           C  
ANISOU  564  C   LEU A  75    10589  11851  11171   3004   1817  -2660       C  
ATOM    565  O   LEU A  75     -34.323 -16.997   0.476  1.00 91.42           O  
ANISOU  565  O   LEU A  75    10481  12337  11918   3260   1870  -2652       O  
ATOM    566  CB  LEU A  75     -31.402 -17.868  -0.860  1.00 81.98           C  
ANISOU  566  CB  LEU A  75    10103  10915  10130   2518   1212  -2266       C  
ATOM    567  CG  LEU A  75     -30.697 -17.962  -2.209  1.00 79.30           C  
ANISOU  567  CG  LEU A  75    10011  10324   9795   2431    841  -2095       C  
ATOM    568  CD1 LEU A  75     -30.104 -19.347  -2.390  1.00 75.80           C  
ANISOU  568  CD1 LEU A  75     9426  10115   9258   2098    698  -1890       C  
ATOM    569  CD2 LEU A  75     -31.662 -17.639  -3.334  1.00 81.14           C  
ANISOU  569  CD2 LEU A  75    10146  10337  10348   2780    570  -2009       C  
ATOM    570  N   ASN A  76     -32.507 -16.781   1.781  1.00 87.54           N  
ANISOU  570  N   ASN A  76    10705  11894  10662   2762   2114  -2806       N  
ATOM    571  CA  ASN A  76     -33.257 -16.855   3.027  1.00 90.54           C  
ANISOU  571  CA  ASN A  76    10875  12567  10961   2801   2596  -2982       C  
ATOM    572  C   ASN A  76     -34.203 -15.677   3.147  1.00 95.04           C  
ANISOU  572  C   ASN A  76    11363  12931  11817   3277   2851  -3290       C  
ATOM    573  O   ASN A  76     -35.314 -15.805   3.653  1.00 98.81           O  
ANISOU  573  O   ASN A  76    11399  13627  12519   3465   3206  -3399       O  
ATOM    574  CB  ASN A  76     -32.307 -16.872   4.224  1.00 89.82           C  
ANISOU  574  CB  ASN A  76    11204  12618  10304   2463   2795  -3104       C  
ATOM    575  CG  ASN A  76     -31.893 -18.271   4.620  1.00 86.38           C  
ANISOU  575  CG  ASN A  76    10671  12529   9621   2062   2722  -2822       C  
ATOM    576  OD1 ASN A  76     -32.725 -19.169   4.735  1.00 86.89           O  
ANISOU  576  OD1 ASN A  76    10322  12851   9841   2025   2861  -2653       O  
ATOM    577  ND2 ASN A  76     -30.599 -18.464   4.835  1.00 83.34           N  
ANISOU  577  ND2 ASN A  76    10655  12128   8882   1757   2492  -2771       N  
ATOM    578  N   HIS A  77     -33.745 -14.523   2.681  1.00 95.55           N  
ANISOU  578  N   HIS A  77    11853  12554  11899   3467   2687  -3436       N  
ATOM    579  CA  HIS A  77     -34.567 -13.330   2.686  1.00101.83           C  
ANISOU  579  CA  HIS A  77    12639  13047  13006   3974   2856  -3725       C  
ATOM    580  C   HIS A  77     -35.756 -13.561   1.769  1.00104.86           C  
ANISOU  580  C   HIS A  77    12442  13422  13977   4355   2640  -3577       C  
ATOM    581  O   HIS A  77     -36.902 -13.375   2.168  1.00 96.38           O  
ANISOU  581  O   HIS A  77    10936  12433  13250   4625   2925  -3691       O  
ATOM    582  CB  HIS A  77     -33.756 -12.126   2.213  1.00101.47           C  
ANISOU  582  CB  HIS A  77    13232  12454  12866   4049   2645  -3839       C  
ATOM    583  CG  HIS A  77     -34.321 -10.813   2.648  1.00107.58           C  
ANISOU  583  CG  HIS A  77    14172  12856  13847   4317   2896  -4095       C  
ATOM    584  ND1 HIS A  77     -35.061 -10.008   1.810  1.00110.88           N  
ANISOU  584  ND1 HIS A  77    14526  12861  14741   4764   2688  -4064       N  
ATOM    585  CD2 HIS A  77     -34.255 -10.164   3.835  1.00 99.24           C  
ANISOU  585  CD2 HIS A  77    13358  11760  12588   4197   3319  -4395       C  
ATOM    586  CE1 HIS A  77     -35.426  -8.918   2.461  1.00116.46           C  
ANISOU  586  CE1 HIS A  77    15397  13286  15566   4926   2995  -4341       C  
ATOM    587  NE2 HIS A  77     -34.951  -8.988   3.691  1.00116.57           N  
ANISOU  587  NE2 HIS A  77    15595  13522  15176   4579   3393  -4570       N  
ATOM    588  N   ILE A  78     -35.468 -13.985   0.543  1.00102.26           N  
ANISOU  588  N   ILE A  78    12131  12968  13756   4281   2119  -3258       N  
ATOM    589  CA  ILE A  78     -36.501 -14.332  -0.425  1.00105.09           C  
ANISOU  589  CA  ILE A  78    11976  13331  14624   4578   1784  -3085       C  
ATOM    590  C   ILE A  78     -37.422 -15.416   0.124  1.00108.82           C  
ANISOU  590  C   ILE A  78    11718  14312  15315   4480   2038  -3050       C  
ATOM    591  O   ILE A  78     -38.645 -15.319   0.019  1.00113.80           O  
ANISOU  591  O   ILE A  78    11764  15010  16465   4847   2076  -3141       O  
ATOM    592  CB  ILE A  78     -35.881 -14.818  -1.744  1.00 99.42           C  
ANISOU  592  CB  ILE A  78    11488  12458  13830   4388   1215  -2745       C  
ATOM    593  CG1 ILE A  78     -35.259 -13.642  -2.498  1.00 99.50           C  
ANISOU  593  CG1 ILE A  78    12163  11905  13736   4555    957  -2754       C  
ATOM    594  CG2 ILE A  78     -36.923 -15.498  -2.610  1.00100.50           C  
ANISOU  594  CG2 ILE A  78    11057  12715  14415   4573    846  -2558       C  
ATOM    595  CD1 ILE A  78     -34.574 -14.034  -3.783  1.00 95.51           C  
ANISOU  595  CD1 ILE A  78    11981  11232  13076   4339    488  -2446       C  
ATOM    596  N   LEU A  79     -36.821 -16.442   0.716  1.00107.36           N  
ANISOU  596  N   LEU A  79    11567  14467  14758   3978   2207  -2917       N  
ATOM    597  CA  LEU A  79     -37.576 -17.531   1.322  1.00111.14           C  
ANISOU  597  CA  LEU A  79    11459  15404  15367   3781   2498  -2848       C  
ATOM    598  C   LEU A  79     -38.495 -16.989   2.410  1.00120.14           C  
ANISOU  598  C   LEU A  79    12286  16706  16656   4025   3121  -3183       C  
ATOM    599  O   LEU A  79     -39.609 -17.476   2.602  1.00124.14           O  
ANISOU  599  O   LEU A  79    12148  17468  17552   4067   3340  -3166       O  
ATOM    600  CB  LEU A  79     -36.619 -18.568   1.904  1.00106.34           C  
ANISOU  600  CB  LEU A  79    11113  15044  14246   3221   2579  -2656       C  
ATOM    601  CG  LEU A  79     -37.132 -20.000   1.970  1.00105.77           C  
ANISOU  601  CG  LEU A  79    10557  15321  14309   2910   2604  -2407       C  
ATOM    602  CD1 LEU A  79     -37.842 -20.339   0.685  1.00105.58           C  
ANISOU  602  CD1 LEU A  79    10094  15205  14816   3083   2129  -2257       C  
ATOM    603  CD2 LEU A  79     -35.968 -20.938   2.191  1.00100.71           C  
ANISOU  603  CD2 LEU A  79    10303  14767  13195   2435   2471  -2169       C  
ATOM    604  N   SER A  80     -38.017 -15.969   3.115  1.00124.15           N  
ANISOU  604  N   SER A  80    13305  17022  16846   4122   3404  -3448       N  
ATOM    605  CA  SER A  80     -38.825 -15.278   4.107  1.00133.31           C  
ANISOU  605  CA  SER A  80    14403  18176  18071   4297   3947  -3640       C  
ATOM    606  C   SER A  80     -39.839 -14.367   3.420  1.00140.43           C  
ANISOU  606  C   SER A  80    15012  18757  19589   4840   3779  -3689       C  
ATOM    607  O   SER A  80     -40.950 -14.179   3.915  1.00146.92           O  
ANISOU  607  O   SER A  80    15416  19706  20700   5059   4135  -3762       O  
ATOM    608  CB  SER A  80     -37.931 -14.463   5.041  1.00133.83           C  
ANISOU  608  CB  SER A  80    15214  18072  17563   4183   4216  -3860       C  
ATOM    609  OG  SER A  80     -38.703 -13.674   5.926  1.00141.06           O  
ANISOU  609  OG  SER A  80    16144  18950  18503   4445   4697  -4066       O  
ATOM    610  N   GLU A  81     -39.449 -13.803   2.278  1.00139.81           N  
ANISOU  610  N   GLU A  81    15179  18269  19675   5064   3219  -3631       N  
ATOM    611  CA  GLU A  81     -40.340 -12.937   1.509  1.00146.45           C  
ANISOU  611  CA  GLU A  81    15818  18755  21071   5576   2944  -3623       C  
ATOM    612  C   GLU A  81     -41.543 -13.725   1.016  1.00150.26           C  
ANISOU  612  C   GLU A  81    15477  19525  22092   5679   2768  -3442       C  
ATOM    613  O   GLU A  81     -42.634 -13.180   0.851  1.00156.97           O  
ANISOU  613  O   GLU A  81    15943  20277  23422   6076   2755  -3471       O  
ATOM    614  CB  GLU A  81     -39.608 -12.312   0.320  1.00143.66           C  
ANISOU  614  CB  GLU A  81    15985  17910  20689   5719   2328  -3522       C  
ATOM    615  CG  GLU A  81     -38.589 -11.247   0.692  1.00143.28           C  
ANISOU  615  CG  GLU A  81    16736  17462  20241   5664   2464  -3713       C  
ATOM    616  CD  GLU A  81     -37.830 -10.727  -0.511  1.00140.57           C  
ANISOU  616  CD  GLU A  81    16944  16648  19819   5729   1888  -3558       C  
ATOM    617  OE1 GLU A  81     -38.226 -11.050  -1.650  1.00140.14           O  
ANISOU  617  OE1 GLU A  81    16684  16528  20034   5905   1372  -3310       O  
ATOM    618  OE2 GLU A  81     -36.835  -9.998  -0.317  1.00139.40           O  
ANISOU  618  OE2 GLU A  81    17464  16186  19316   5566   1951  -3671       O  
ATOM    619  N   ASN A  82     -41.332 -15.013   0.779  1.00129.61           N  
ANISOU  619  N   ASN A  82    12792  20971  15482    717   2673   -644       N  
ATOM    620  CA  ASN A  82     -42.412 -15.900   0.385  1.00131.94           C  
ANISOU  620  CA  ASN A  82    12761  21870  15500    536   2521   -563       C  
ATOM    621  C   ASN A  82     -43.050 -16.524   1.616  1.00133.26           C  
ANISOU  621  C   ASN A  82    12862  22250  15521    232   2575   -757       C  
ATOM    622  O   ASN A  82     -43.950 -17.358   1.508  1.00134.67           O  
ANISOU  622  O   ASN A  82    12773  22897  15497     -1   2488   -749       O  
ATOM    623  CB  ASN A  82     -41.895 -16.979  -0.564  1.00130.15           C  
ANISOU  623  CB  ASN A  82    12626  21702  15123    233   2240   -517       C  
ATOM    624  CG  ASN A  82     -41.294 -16.398  -1.829  1.00130.31           C  
ANISOU  624  CG  ASN A  82    12704  21557  15252    550   2195   -300       C  
ATOM    625  OD1 ASN A  82     -41.757 -15.375  -2.335  1.00133.08           O  
ANISOU  625  OD1 ASN A  82    12856  22011  15700   1018   2337    -96       O  
ATOM    626  ND2 ASN A  82     -40.255 -17.045  -2.343  1.00127.55           N  
ANISOU  626  ND2 ASN A  82    12632  20945  14887    321   2022   -320       N  
ATOM    627  N   GLU A  83     -42.561 -16.109   2.782  1.00133.07           N  
ANISOU  627  N   GLU A  83    13076  21885  15601    235   2735   -947       N  
ATOM    628  CA  GLU A  83     -43.111 -16.518   4.072  1.00134.50           C  
ANISOU  628  CA  GLU A  83    13226  22240  15640     29   2842  -1119       C  
ATOM    629  C   GLU A  83     -43.122 -18.034   4.246  1.00133.26           C  
ANISOU  629  C   GLU A  83    13131  22259  15245   -469   2678  -1158       C  
ATOM    630  O   GLU A  83     -43.968 -18.585   4.948  1.00134.97           O  
ANISOU  630  O   GLU A  83    13186  22786  15309   -656   2765  -1206       O  
ATOM    631  CB  GLU A  83     -44.515 -15.938   4.261  1.00138.61           C  
ANISOU  631  CB  GLU A  83    13337  23179  16149    281   3029  -1051       C  
ATOM    632  CG  GLU A  83     -44.901 -15.668   5.708  1.00140.33           C  
ANISOU  632  CG  GLU A  83    13574  23413  16334    284   3259  -1244       C  
ATOM    633  CD  GLU A  83     -46.217 -14.927   5.825  1.00144.45           C  
ANISOU  633  CD  GLU A  83    13694  24298  16893    602   3473  -1165       C  
ATOM    634  OE1 GLU A  83     -46.869 -15.028   6.885  1.00146.44           O  
ANISOU  634  OE1 GLU A  83    13858  24743  17041    532   3639  -1287       O  
ATOM    635  OE2 GLU A  83     -46.598 -14.238   4.855  1.00145.95           O  
ANISOU  635  OE2 GLU A  83    13654  24594  17205    949   3488   -965       O  
ATOM    636  N   VAL A  84     -42.174 -18.703   3.598  1.00130.51           N  
ANISOU  636  N   VAL A  84    13018  21684  14884   -676   2476  -1130       N  
ATOM    637  CA  VAL A  84     -42.031 -20.143   3.737  1.00129.21           C  
ANISOU  637  CA  VAL A  84    12966  21587  14541  -1139   2357  -1165       C  
ATOM    638  C   VAL A  84     -41.036 -20.446   4.848  1.00126.76           C  
ANISOU  638  C   VAL A  84    13046  20926  14188  -1282   2391  -1304       C  
ATOM    639  O   VAL A  84     -39.918 -19.934   4.844  1.00124.75           O  
ANISOU  639  O   VAL A  84    13058  20283  14057  -1149   2344  -1364       O  
ATOM    640  CB  VAL A  84     -41.544 -20.782   2.434  1.00127.69           C  
ANISOU  640  CB  VAL A  84    12819  21354  14345  -1290   2129  -1069       C  
ATOM    641  CG1 VAL A  84     -41.681 -22.294   2.509  1.00127.59           C  
ANISOU  641  CG1 VAL A  84    12842  21462  14175  -1776   2062  -1110       C  
ATOM    642  CG2 VAL A  84     -42.331 -20.233   1.260  1.00129.87           C  
ANISOU  642  CG2 VAL A  84    12725  21975  14643  -1030   2076   -927       C  
ATOM    643  N   LYS A  85     -41.450 -21.276   5.799  1.00127.44           N  
ANISOU  643  N   LYS A  85    13149  21174  14097  -1540   2486  -1351       N  
ATOM    644  CA  LYS A  85     -40.609 -21.596   6.946  1.00126.06           C  
ANISOU  644  CA  LYS A  85    13315  20765  13815  -1632   2531  -1459       C  
ATOM    645  C   LYS A  85     -39.434 -22.503   6.579  1.00122.11           C  
ANISOU  645  C   LYS A  85    13138  19968  13291  -1862   2355  -1423       C  
ATOM    646  O   LYS A  85     -39.600 -23.710   6.403  1.00121.79           O  
ANISOU  646  O   LYS A  85    13122  20001  13151  -2186   2334  -1336       O  
ATOM    647  CB  LYS A  85     -41.446 -22.220   8.070  1.00129.55           C  
ANISOU  647  CB  LYS A  85    13680  21488  14056  -1797   2727  -1470       C  
ATOM    648  CG  LYS A  85     -42.416 -23.304   7.616  1.00131.97           C  
ANISOU  648  CG  LYS A  85    13751  22088  14305  -2125   2758  -1354       C  
ATOM    649  CD  LYS A  85     -43.143 -23.926   8.800  1.00135.25           C  
ANISOU  649  CD  LYS A  85    14125  22719  14547  -2288   3003  -1348       C  
ATOM    650  CE  LYS A  85     -44.091 -25.033   8.359  1.00137.47           C  
ANISOU  650  CE  LYS A  85    14154  23253  14825  -2659   3074  -1269       C  
ATOM    651  NZ  LYS A  85     -44.798 -25.651   9.517  1.00140.36           N  
ANISOU  651  NZ  LYS A  85    14484  23795  15051  -2820   3367  -1237       N  
ATOM    652  N   LEU A  86     -38.249 -21.906   6.464  1.00119.00           N  
ANISOU  652  N   LEU A  86    12977  19222  13013  -1697   2254  -1500       N  
ATOM    653  CA  LEU A  86     -37.021 -22.651   6.181  1.00114.98           C  
ANISOU  653  CA  LEU A  86    12779  18413  12493  -1867   2093  -1475       C  
ATOM    654  C   LEU A  86     -35.774 -21.796   6.404  1.00112.67           C  
ANISOU  654  C   LEU A  86    12702  17775  12334  -1651   2033  -1626       C  
ATOM    655  O   LEU A  86     -35.731 -20.632   6.007  1.00113.35           O  
ANISOU  655  O   LEU A  86    12689  17743  12634  -1389   2065  -1688       O  
ATOM    656  CB  LEU A  86     -37.028 -23.189   4.748  1.00112.53           C  
ANISOU  656  CB  LEU A  86    12406  18083  12266  -2012   1945  -1334       C  
ATOM    657  CG  LEU A  86     -35.793 -23.983   4.322  1.00108.42           C  
ANISOU  657  CG  LEU A  86    12195  17245  11756  -2185   1792  -1297       C  
ATOM    658  CD1 LEU A  86     -35.532 -25.118   5.295  1.00107.95           C  
ANISOU  658  CD1 LEU A  86    12348  17167  11503  -2427   1855  -1281       C  
ATOM    659  CD2 LEU A  86     -35.948 -24.517   2.905  1.00107.04           C  
ANISOU  659  CD2 LEU A  86    11926  17108  11634  -2331   1666  -1188       C  
ATOM    660  N   THR A  87     -34.765 -22.381   7.041  1.00110.27           N  
ANISOU  660  N   THR A  87    12677  17309  11910  -1756   1966  -1685       N  
ATOM    661  CA  THR A  87     -33.505 -21.689   7.285  1.00108.04           C  
ANISOU  661  CA  THR A  87    12575  16729  11746  -1597   1892  -1871       C  
ATOM    662  C   THR A  87     -32.384 -22.307   6.455  1.00103.49           C  
ANISOU  662  C   THR A  87    12206  15866  11250  -1722   1710  -1781       C  
ATOM    663  O   THR A  87     -32.055 -23.480   6.623  1.00102.86           O  
ANISOU  663  O   THR A  87    12293  15796  10995  -1930   1652  -1671       O  
ATOM    664  CB  THR A  87     -33.122 -21.733   8.773  1.00110.63           C  
ANISOU  664  CB  THR A  87    13032  17157  11847  -1557   1943  -2058       C  
ATOM    665  OG1 THR A  87     -34.193 -21.199   9.561  1.00113.67           O  
ANISOU  665  OG1 THR A  87    13230  17820  12140  -1443   2131  -2143       O  
ATOM    666  CG2 THR A  87     -31.862 -20.925   9.026  1.00110.54           C  
ANISOU  666  CG2 THR A  87    13142  16882  11975  -1402   1863  -2324       C  
ATOM    667  N   ILE A  88     -31.804 -21.515   5.558  1.00100.03           N  
ANISOU  667  N   ILE A  88    11761  15157  11088  -1580   1654  -1812       N  
ATOM    668  CA  ILE A  88     -30.735 -22.000   4.687  1.00 95.47           C  
ANISOU  668  CA  ILE A  88    11365  14298  10610  -1673   1498  -1728       C  
ATOM    669  C   ILE A  88     -29.365 -21.794   5.315  1.00 93.92           C  
ANISOU  669  C   ILE A  88    11365  13863  10456  -1623   1427  -1928       C  
ATOM    670  O   ILE A  88     -29.002 -20.677   5.679  1.00 94.54           O  
ANISOU  670  O   ILE A  88    11395  13813  10712  -1435   1490  -2158       O  
ATOM    671  CB  ILE A  88     -30.754 -21.299   3.324  1.00 93.47           C  
ANISOU  671  CB  ILE A  88    11009  13882  10625  -1533   1489  -1627       C  
ATOM    672  CG1 ILE A  88     -32.122 -21.457   2.661  1.00 94.32           C  
ANISOU  672  CG1 ILE A  88    10871  14307  10661  -1550   1533  -1449       C  
ATOM    673  CG2 ILE A  88     -29.658 -21.847   2.434  1.00 90.45           C  
ANISOU  673  CG2 ILE A  88    10818  13222  10325  -1633   1343  -1538       C  
ATOM    674  CD1 ILE A  88     -32.355 -20.502   1.513  1.00 94.49           C  
ANISOU  674  CD1 ILE A  88    10734  14266  10901  -1297   1572  -1340       C  
ATOM    675  N   MET A  89     -28.604 -22.876   5.432  1.00 92.46           N  
ANISOU  675  N   MET A  89    11385  13623  10122  -1789   1309  -1852       N  
ATOM    676  CA  MET A  89     -27.284 -22.815   6.044  1.00 92.38           C  
ANISOU  676  CA  MET A  89    11535  13457  10107  -1740   1215  -2032       C  
ATOM    677  C   MET A  89     -26.214 -23.345   5.098  1.00 90.99           C  
ANISOU  677  C   MET A  89    11521  12989  10064  -1824   1080  -1919       C  
ATOM    678  O   MET A  89     -26.258 -24.500   4.680  1.00 90.37           O  
ANISOU  678  O   MET A  89    11556  12919   9860  -2001   1035  -1697       O  
ATOM    679  CB  MET A  89     -27.270 -23.603   7.352  1.00 93.51           C  
ANISOU  679  CB  MET A  89    11778  13863   9888  -1789   1219  -2048       C  
ATOM    680  CG  MET A  89     -28.219 -23.062   8.403  1.00 96.13           C  
ANISOU  680  CG  MET A  89    11964  14497  10063  -1688   1362  -2187       C  
ATOM    681  SD  MET A  89     -28.219 -24.057   9.900  1.00117.36           S  
ANISOU  681  SD  MET A  89    14787  17526  12280  -1710   1396  -2142       S  
ATOM    682  CE  MET A  89     -26.467 -24.132  10.244  1.00 71.92           C  
ANISOU  682  CE  MET A  89     9201  11639   6485  -1621   1196  -2311       C  
ATOM    683  N   THR A  90     -25.254 -22.491   4.763  1.00 91.24           N  
ANISOU  683  N   THR A  90    11555  12743  10369  -1703   1043  -2087       N  
ATOM    684  CA  THR A  90     -24.203 -22.854   3.825  1.00 90.28           C  
ANISOU  684  CA  THR A  90    11569  12327  10408  -1757    936  -1992       C  
ATOM    685  C   THR A  90     -22.895 -23.114   4.551  1.00 91.44           C  
ANISOU  685  C   THR A  90    11839  12408  10495  -1750    821  -2159       C  
ATOM    686  O   THR A  90     -22.447 -22.293   5.343  1.00 93.36           O  
ANISOU  686  O   THR A  90    12004  12669  10800  -1634    829  -2466       O  
ATOM    687  CB  THR A  90     -23.977 -21.748   2.788  1.00 90.09           C  
ANISOU  687  CB  THR A  90    11456  12009  10767  -1621   1005  -2023       C  
ATOM    688  OG1 THR A  90     -25.196 -21.507   2.075  1.00 90.58           O  
ANISOU  688  OG1 THR A  90    11379  12189  10847  -1579   1101  -1842       O  
ATOM    689  CG2 THR A  90     -22.892 -22.152   1.805  1.00 88.10           C  
ANISOU  689  CG2 THR A  90    11345  11462  10668  -1673    912  -1912       C  
ATOM    690  N   GLY A  91     -22.282 -24.259   4.277  1.00 90.26           N  
ANISOU  690  N   GLY A  91    11867  12201  10227  -1867    719  -1974       N  
ATOM    691  CA  GLY A  91     -21.023 -24.602   4.910  1.00 91.59           C  
ANISOU  691  CA  GLY A  91    12139  12347  10314  -1831    598  -2089       C  
ATOM    692  C   GLY A  91     -19.834 -24.400   3.991  1.00 90.72           C  
ANISOU  692  C   GLY A  91    12077  11888  10505  -1821    526  -2115       C  
ATOM    693  O   GLY A  91     -19.985 -23.958   2.852  1.00 90.36           O  
ANISOU  693  O   GLY A  91    12001  11607  10727  -1828    584  -2033       O  
ATOM    694  N   ASP A  92     -18.646 -24.723   4.492  1.00 89.90           N  
ANISOU  694  N   ASP A  92    12037  11778  10341  -1783    406  -2220       N  
ATOM    695  CA  ASP A  92     -17.426 -24.599   3.706  1.00 87.04           C  
ANISOU  695  CA  ASP A  92    11710  11099  10260  -1775    342  -2254       C  
ATOM    696  C   ASP A  92     -17.124 -25.876   2.942  1.00 85.11           C  
ANISOU  696  C   ASP A  92    11671  10729   9936  -1881    301  -1920       C  
ATOM    697  O   ASP A  92     -17.727 -26.918   3.186  1.00 85.22           O  
ANISOU  697  O   ASP A  92    11806  10903   9672  -1963    321  -1693       O  
ATOM    698  CB  ASP A  92     -16.238 -24.258   4.605  1.00 88.34           C  
ANISOU  698  CB  ASP A  92    11794  11349  10424  -1677    227  -2578       C  
ATOM    699  CG  ASP A  92     -16.105 -22.776   4.854  1.00 91.05           C  
ANISOU  699  CG  ASP A  92    11921  11609  11065  -1607    296  -2986       C  
ATOM    700  OD1 ASP A  92     -16.306 -21.997   3.902  1.00 91.24           O  
ANISOU  700  OD1 ASP A  92    11896  11316  11454  -1612    432  -2972       O  
ATOM    701  OD2 ASP A  92     -15.798 -22.388   6.000  1.00 94.26           O  
ANISOU  701  OD2 ASP A  92    12204  12270  11340  -1535    234  -3324       O  
ATOM    702  N   ILE A  93     -16.178 -25.778   2.017  1.00 83.21           N  
ANISOU  702  N   ILE A  93    11469  10180   9966  -1881    273  -1903       N  
ATOM    703  CA  ILE A  93     -15.695 -26.928   1.266  1.00 81.38           C  
ANISOU  703  CA  ILE A  93    11434   9792   9696  -1966    242  -1633       C  
ATOM    704  C   ILE A  93     -14.270 -27.266   1.699  1.00 81.36           C  
ANISOU  704  C   ILE A  93    11469   9754   9692  -1886    125  -1715       C  
ATOM    705  O   ILE A  93     -13.445 -26.374   1.886  1.00 82.09           O  
ANISOU  705  O   ILE A  93    11413   9777   9999  -1800     80  -1992       O  
ATOM    706  CB  ILE A  93     -15.705 -26.652  -0.249  1.00 80.38           C  
ANISOU  706  CB  ILE A  93    11329   9359   9851  -2011    310  -1513       C  
ATOM    707  CG1 ILE A  93     -14.965 -25.350  -0.562  1.00 80.58           C  
ANISOU  707  CG1 ILE A  93    11210   9156  10252  -1895    345  -1739       C  
ATOM    708  CG2 ILE A  93     -17.132 -26.571  -0.771  1.00 80.64           C  
ANISOU  708  CG2 ILE A  93    11322   9499   9818  -2080    402  -1382       C  
ATOM    709  CD1 ILE A  93     -14.621 -25.157  -2.015  1.00 49.58           C  
ANISOU  709  CD1 ILE A  93     7332   4910   6595  -1890    421  -1593       C  
ATOM    710  N   LYS A  94     -13.984 -28.551   1.872  1.00 80.20           N  
ANISOU  710  N   LYS A  94    11502   9654   9314  -1911     94  -1483       N  
ATOM    711  CA  LYS A  94     -12.631 -28.998   2.199  1.00 79.58           C  
ANISOU  711  CA  LYS A  94    11461   9563   9213  -1804    -14  -1503       C  
ATOM    712  C   LYS A  94     -12.354 -30.354   1.556  1.00 77.69           C  
ANISOU  712  C   LYS A  94    11466   9142   8910  -1870     33  -1164       C  
ATOM    713  O   LYS A  94     -13.197 -31.249   1.597  1.00 78.10           O  
ANISOU  713  O   LYS A  94    11667   9244   8765  -1969    133   -931       O  
ATOM    714  CB  LYS A  94     -12.425 -29.065   3.716  1.00 81.62           C  
ANISOU  714  CB  LYS A  94    11640  10220   9151  -1652   -109  -1636       C  
ATOM    715  CG  LYS A  94     -12.213 -27.711   4.379  1.00 82.69           C  
ANISOU  715  CG  LYS A  94    11510  10513   9394  -1570   -182  -2074       C  
ATOM    716  CD  LYS A  94     -12.060 -27.831   5.885  1.00 85.78           C  
ANISOU  716  CD  LYS A  94    11818  11376   9401  -1407   -287  -2222       C  
ATOM    717  CE  LYS A  94     -11.917 -26.457   6.528  1.00 87.87           C  
ANISOU  717  CE  LYS A  94    11805  11798   9785  -1358   -343  -2726       C  
ATOM    718  NZ  LYS A  94     -11.774 -26.531   8.008  1.00 91.49           N  
ANISOU  718  NZ  LYS A  94    12159  12782   9821  -1185   -460  -2916       N  
ATOM    719  N   GLY A  95     -11.176 -30.500   0.957  1.00 75.71           N  
ANISOU  719  N   GLY A  95    11248   8667   8852  -1825    -14  -1153       N  
ATOM    720  CA  GLY A  95     -10.832 -31.726   0.261  1.00 73.89           C  
ANISOU  720  CA  GLY A  95    11250   8219   8605  -1881     53   -859       C  
ATOM    721  C   GLY A  95     -11.776 -32.002  -0.891  1.00 71.95           C  
ANISOU  721  C   GLY A  95    11118   7773   8445  -2084    181   -714       C  
ATOM    722  O   GLY A  95     -12.338 -31.081  -1.476  1.00 71.28           O  
ANISOU  722  O   GLY A  95    10915   7647   8520  -2137    197   -832       O  
ATOM    723  N   ILE A  96     -11.959 -33.278  -1.204  1.00 71.84           N  
ANISOU  723  N   ILE A  96    11324   7651   8320  -2186    286   -465       N  
ATOM    724  CA  ILE A  96     -12.811 -33.687  -2.313  1.00 71.09           C  
ANISOU  724  CA  ILE A  96    11325   7404   8281  -2400    400   -367       C  
ATOM    725  C   ILE A  96     -14.271 -33.326  -2.077  1.00 71.17           C  
ANISOU  725  C   ILE A  96    11227   7641   8175  -2517    442   -420       C  
ATOM    726  O   ILE A  96     -14.838 -33.645  -1.035  1.00 72.74           O  
ANISOU  726  O   ILE A  96    11425   8052   8159  -2517    482   -378       O  
ATOM    727  CB  ILE A  96     -12.716 -35.202  -2.550  1.00 72.26           C  
ANISOU  727  CB  ILE A  96    11727   7382   8346  -2508    540   -134       C  
ATOM    728  CG1 ILE A  96     -11.253 -35.630  -2.650  1.00 72.52           C  
ANISOU  728  CG1 ILE A  96    11866   7217   8472  -2353    511    -55       C  
ATOM    729  CG2 ILE A  96     -13.488 -35.602  -3.799  1.00 71.37           C  
ANISOU  729  CG2 ILE A  96    11683   7128   8305  -2749    644   -112       C  
ATOM    730  CD1 ILE A  96     -11.066 -37.100  -2.904  1.00 73.70           C  
ANISOU  730  CD1 ILE A  96    12279   7146   8580  -2430    685    181       C  
ATOM    731  N   MET A  97     -14.876 -32.666  -3.056  1.00 69.77           N  
ANISOU  731  N   MET A  97    10949   7434   8127  -2593    445   -493       N  
ATOM    732  CA  MET A  97     -16.286 -32.335  -2.967  1.00 70.28           C  
ANISOU  732  CA  MET A  97    10884   7729   8092  -2694    486   -534       C  
ATOM    733  C   MET A  97     -17.099 -33.574  -3.290  1.00 71.42           C  
ANISOU  733  C   MET A  97    11150   7881   8106  -2937    610   -406       C  
ATOM    734  O   MET A  97     -17.209 -33.968  -4.449  1.00 71.40           O  
ANISOU  734  O   MET A  97    11202   7755   8173  -3067    644   -383       O  
ATOM    735  CB  MET A  97     -16.629 -31.198  -3.923  1.00 69.35           C  
ANISOU  735  CB  MET A  97    10601   7605   8142  -2643    458   -627       C  
ATOM    736  CG  MET A  97     -15.703 -30.004  -3.783  1.00 68.81           C  
ANISOU  736  CG  MET A  97    10427   7425   8291  -2431    395   -763       C  
ATOM    737  SD  MET A  97     -16.225 -28.577  -4.736  1.00 56.00           S  
ANISOU  737  SD  MET A  97     8614   5783   6880  -2319    439   -823       S  
ATOM    738  CE  MET A  97     -14.760 -27.580  -4.609  1.00 62.11           C  
ANISOU  738  CE  MET A  97     9333   6287   7977  -2132    427   -974       C  
ATOM    739  N   GLN A  98     -17.649 -34.199  -2.255  1.00 72.66           N  
ANISOU  739  N   GLN A  98    11347   8183   8080  -2999    698   -338       N  
ATOM    740  CA  GLN A  98     -18.443 -35.406  -2.430  1.00 74.16           C  
ANISOU  740  CA  GLN A  98    11642   8349   8187  -3255    870   -235       C  
ATOM    741  C   GLN A  98     -19.724 -35.106  -3.200  1.00 75.05           C  
ANISOU  741  C   GLN A  98    11571   8638   8306  -3440    882   -343       C  
ATOM    742  O   GLN A  98     -20.308 -34.034  -3.056  1.00 74.59           O  
ANISOU  742  O   GLN A  98    11301   8804   8235  -3343    801   -443       O  
ATOM    743  CB  GLN A  98     -18.769 -36.033  -1.075  1.00 75.51           C  
ANISOU  743  CB  GLN A  98    11881   8640   8168  -3247   1000   -112       C  
ATOM    744  CG  GLN A  98     -17.555 -36.573  -0.325  1.00 75.54           C  
ANISOU  744  CG  GLN A  98    12073   8519   8110  -3048   1010     41       C  
ATOM    745  CD  GLN A  98     -17.015 -37.854  -0.927  1.00 75.44           C  
ANISOU  745  CD  GLN A  98    12307   8172   8184  -3161   1164    205       C  
ATOM    746  OE1 GLN A  98     -17.651 -38.466  -1.781  1.00 75.55           O  
ANISOU  746  OE1 GLN A  98    12364   8056   8287  -3431   1291    185       O  
ATOM    747  NE2 GLN A  98     -15.835 -38.267  -0.481  1.00 75.62           N  
ANISOU  747  NE2 GLN A  98    12480   8073   8180  -2950   1157    350       N  
ATOM    748  N   ALA A  99     -20.148 -36.060  -4.022  1.00 77.01           N  
ANISOU  748  N   ALA A  99    11890   8796   8576  -3698    992   -337       N  
ATOM    749  CA  ALA A  99     -21.323 -35.886  -4.865  1.00 78.68           C  
ANISOU  749  CA  ALA A  99    11900   9226   8770  -3880    987   -467       C  
ATOM    750  C   ALA A  99     -22.605 -36.231  -4.122  1.00 81.88           C  
ANISOU  750  C   ALA A  99    12179   9869   9064  -4064   1119   -486       C  
ATOM    751  O   ALA A  99     -22.582 -36.952  -3.129  1.00 82.68           O  
ANISOU  751  O   ALA A  99    12412   9889   9111  -4113   1276   -372       O  
ATOM    752  CB  ALA A  99     -21.196 -36.730  -6.115  1.00 78.93           C  
ANISOU  752  CB  ALA A  99    11978   9153   8859  -3939   1006   -512       C  
ATOM    753  N   GLY A 100     -23.724 -35.713  -4.616  1.00 84.17           N  
ANISOU  753  N   GLY A 100    12202  10465   9313  -4144   1070   -614       N  
ATOM    754  CA  GLY A 100     -25.026 -35.999  -4.043  1.00 87.18           C  
ANISOU  754  CA  GLY A 100    12412  11103   9610  -4338   1198   -659       C  
ATOM    755  C   GLY A 100     -25.918 -36.729  -5.028  1.00 90.20           C  
ANISOU  755  C   GLY A 100    12661  11607  10003  -4675   1266   -815       C  
ATOM    756  O   GLY A 100     -25.973 -36.377  -6.205  1.00 90.14           O  
ANISOU  756  O   GLY A 100    12536  11717   9995  -4661   1127   -926       O  
ATOM    757  N   LYS A 101     -26.623 -37.746  -4.551  1.00 93.07           N  
ANISOU  757  N   LYS A 101    13024  11967  10372  -4892   1474   -832       N  
ATOM    758  CA  LYS A 101     -27.424 -38.569  -5.445  1.00 98.10           C  
ANISOU  758  CA  LYS A 101    13522  12712  11042  -5087   1525  -1024       C  
ATOM    759  C   LYS A 101     -28.715 -37.882  -5.857  1.00100.45           C  
ANISOU  759  C   LYS A 101    13424  13493  11249  -5246   1444  -1205       C  
ATOM    760  O   LYS A 101     -29.207 -38.090  -6.965  1.00102.28           O  
ANISOU  760  O   LYS A 101    13479  13926  11456  -5359   1372  -1401       O  
ATOM    761  CB  LYS A 101     -27.693 -39.941  -4.830  1.00102.79           C  
ANISOU  761  CB  LYS A 101    14244  13086  11726  -5207   1790   -992       C  
ATOM    762  CG  LYS A 101     -26.425 -40.745  -4.626  1.00103.43           C  
ANISOU  762  CG  LYS A 101    14670  12727  11901  -5032   1868   -820       C  
ATOM    763  CD  LYS A 101     -25.576 -40.708  -5.885  1.00102.28           C  
ANISOU  763  CD  LYS A 101    14595  12479  11788  -4918   1705   -891       C  
ATOM    764  CE  LYS A 101     -24.116 -40.981  -5.585  1.00100.13           C  
ANISOU  764  CE  LYS A 101    14615  11851  11578  -4658   1702   -687       C  
ATOM    765  NZ  LYS A 101     -23.276 -40.762  -6.793  1.00 97.80           N  
ANISOU  765  NZ  LYS A 101    14361  11488  11310  -4523   1539   -742       N  
ATOM    766  N   ARG A 102     -29.256 -37.054  -4.971  1.00101.08           N  
ANISOU  766  N   ARG A 102    13341  13802  11264  -5218   1452  -1142       N  
ATOM    767  CA  ARG A 102     -30.429 -36.264  -5.317  1.00103.73           C  
ANISOU  767  CA  ARG A 102    13273  14630  11508  -5186   1338  -1273       C  
ATOM    768  C   ARG A 102     -30.027 -35.183  -6.303  1.00105.19           C  
ANISOU  768  C   ARG A 102    13373  14954  11641  -4868   1077  -1270       C  
ATOM    769  O   ARG A 102     -28.844 -35.011  -6.599  1.00102.71           O  
ANISOU  769  O   ARG A 102    13311  14335  11378  -4688    998  -1171       O  
ATOM    770  CB  ARG A 102     -31.048 -35.628  -4.073  1.00102.37           C  
ANISOU  770  CB  ARG A 102    12979  14635  11283  -5040   1406  -1175       C  
ATOM    771  CG  ARG A 102     -31.550 -36.631  -3.055  1.00103.71           C  
ANISOU  771  CG  ARG A 102    13212  14707  11486  -5320   1700  -1141       C  
ATOM    772  CD  ARG A 102     -32.602 -37.543  -3.652  1.00106.44           C  
ANISOU  772  CD  ARG A 102    13338  15216  11889  -5687   1817  -1360       C  
ATOM    773  NE  ARG A 102     -33.937 -36.965  -3.554  1.00107.93           N  
ANISOU  773  NE  ARG A 102    13091  15909  12010  -5770   1811  -1481       N  
ATOM    774  CZ  ARG A 102     -34.795 -37.243  -2.580  1.00109.79           C  
ANISOU  774  CZ  ARG A 102    13223  16234  12259  -5863   2024  -1455       C  
ATOM    775  NH1 ARG A 102     -34.458 -38.095  -1.623  1.00110.14           N  
ANISOU  775  NH1 ARG A 102    13573  15902  12373  -5887   2264  -1297       N  
ATOM    776  NH2 ARG A 102     -35.991 -36.673  -2.561  1.00111.61           N  
ANISOU  776  NH2 ARG A 102    13032  16944  12429  -5905   2004  -1569       N  
ATOM    777  N   SER A 103     -31.013 -34.457  -6.815  1.00110.08           N  
ANISOU  777  N   SER A 103    13627  16036  12162  -4784    964  -1361       N  
ATOM    778  CA  SER A 103     -30.743 -33.362  -7.735  1.00111.59           C  
ANISOU  778  CA  SER A 103    13719  16386  12296  -4433    760  -1310       C  
ATOM    779  C   SER A 103     -31.950 -32.437  -7.816  1.00113.83           C  
ANISOU  779  C   SER A 103    13593  17187  12472  -4262    694  -1333       C  
ATOM    780  O   SER A 103     -33.091 -32.895  -7.805  1.00116.84           O  
ANISOU  780  O   SER A 103    13689  17921  12784  -4511    741  -1490       O  
ATOM    781  CB  SER A 103     -30.391 -33.903  -9.123  1.00113.85           C  
ANISOU  781  CB  SER A 103    14037  16686  12534  -4547    670  -1425       C  
ATOM    782  OG  SER A 103     -29.830 -32.890  -9.941  1.00113.62           O  
ANISOU  782  OG  SER A 103    14010  16693  12467  -4163    517  -1305       O  
ATOM    783  N   LEU A 104     -31.692 -31.136  -7.893  1.00112.80           N  
ANISOU  783  N   LEU A 104    13424  17086  12349  -3834    608  -1181       N  
ATOM    784  CA  LEU A 104     -32.760 -30.141  -7.936  1.00115.62           C  
ANISOU  784  CA  LEU A 104    13412  17895  12622  -3593    571  -1155       C  
ATOM    785  C   LEU A 104     -33.611 -30.261  -9.200  1.00118.97           C  
ANISOU  785  C   LEU A 104    13493  18846  12864  -3626    449  -1269       C  
ATOM    786  O   LEU A 104     -33.109 -30.627 -10.260  1.00119.15           O  
ANISOU  786  O   LEU A 104    13595  18852  12823  -3659    355  -1311       O  
ATOM    787  CB  LEU A 104     -32.169 -28.735  -7.838  1.00115.99           C  
ANISOU  787  CB  LEU A 104    13530  17777  12765  -3117    553   -961       C  
ATOM    788  CG  LEU A 104     -31.388 -28.428  -6.560  1.00116.36           C  
ANISOU  788  CG  LEU A 104    13846  17394  12971  -3045    652   -902       C  
ATOM    789  CD1 LEU A 104     -30.758 -27.046  -6.617  1.00116.09           C  
ANISOU  789  CD1 LEU A 104    13862  17170  13078  -2613    655   -771       C  
ATOM    790  CD2 LEU A 104     -32.295 -28.548  -5.351  1.00119.07           C  
ANISOU  790  CD2 LEU A 104    14053  17911  13278  -3171    766   -961       C  
ATOM    791  N   ARG A 105     -34.901 -29.959  -9.075  1.00121.51           N  
ANISOU  791  N   ARG A 105    13417  19667  13084  -3607    448  -1330       N  
ATOM    792  CA  ARG A 105     -35.803 -29.918 -10.223  1.00124.31           C  
ANISOU  792  CA  ARG A 105    13369  20637  13226  -3571    308  -1440       C  
ATOM    793  C   ARG A 105     -36.297 -28.494 -10.454  1.00122.40           C  
ANISOU  793  C   ARG A 105    12869  20727  12910  -3040    260  -1231       C  
ATOM    794  O   ARG A 105     -36.754 -27.835  -9.521  1.00121.51           O  
ANISOU  794  O   ARG A 105    12668  20617  12881  -2889    364  -1142       O  
ATOM    795  CB  ARG A 105     -37.002 -30.849 -10.016  1.00129.67           C  
ANISOU  795  CB  ARG A 105    13719  21709  13842  -4012    351  -1719       C  
ATOM    796  CG  ARG A 105     -36.833 -32.255 -10.584  1.00132.02           C  
ANISOU  796  CG  ARG A 105    14089  21943  14129  -4507    353  -2001       C  
ATOM    797  CD  ARG A 105     -35.939 -33.121  -9.709  1.00130.38           C  
ANISOU  797  CD  ARG A 105    14338  21061  14139  -4799    539  -1979       C  
ATOM    798  NE  ARG A 105     -35.744 -34.455 -10.274  1.00132.66           N  
ANISOU  798  NE  ARG A 105    14718  21228  14457  -5256    587  -2240       N  
ATOM    799  CZ  ARG A 105     -36.557 -35.487 -10.065  1.00136.88           C  
ANISOU  799  CZ  ARG A 105    15068  21888  15052  -5738    733  -2514       C  
ATOM    800  NH1 ARG A 105     -37.632 -35.349  -9.300  1.00139.56           N  
ANISOU  800  NH1 ARG A 105    15129  22486  15412  -5795    835  -2538       N  
ATOM    801  NH2 ARG A 105     -36.293 -36.661 -10.622  1.00138.55           N  
ANISOU  801  NH2 ARG A 105    15493  21827  15323  -5932    820  -2684       N  
ATOM    802  N   PRO A 106     -36.208 -28.014 -11.704  1.00121.92           N  
ANISOU  802  N   PRO A 106    12690  20948  12684  -2733    126  -1141       N  
ATOM    803  CA  PRO A 106     -36.692 -26.671 -12.043  1.00121.91           C  
ANISOU  803  CA  PRO A 106    12440  21273  12607  -2179    115   -898       C  
ATOM    804  C   PRO A 106     -38.217 -26.620 -12.079  1.00124.47           C  
ANISOU  804  C   PRO A 106    12229  22319  12744  -2183     63  -1008       C  
ATOM    805  O   PRO A 106     -38.852 -27.617 -12.421  1.00126.56           O  
ANISOU  805  O   PRO A 106    12257  22969  12860  -2576    -31  -1298       O  
ATOM    806  CB  PRO A 106     -36.123 -26.444 -13.445  1.00122.53           C  
ANISOU  806  CB  PRO A 106    12565  21469  12523  -1901     -2   -777       C  
ATOM    807  CG  PRO A 106     -35.993 -27.812 -14.017  1.00123.43           C  
ANISOU  807  CG  PRO A 106    12714  21676  12509  -2381   -115  -1082       C  
ATOM    808  CD  PRO A 106     -35.612 -28.698 -12.865  1.00121.45           C  
ANISOU  808  CD  PRO A 106    12744  20903  12497  -2858      6  -1241       C  
ATOM    809  N   GLN A 107     -38.795 -25.476 -11.725  1.00124.35           N  
ANISOU  809  N   GLN A 107    12013  22477  12758  -1760    142   -799       N  
ATOM    810  CA  GLN A 107     -40.246 -25.325 -11.733  1.00127.44           C  
ANISOU  810  CA  GLN A 107    11870  23572  12978  -1705    102   -873       C  
ATOM    811  C   GLN A 107     -40.687 -24.242 -12.715  1.00130.50           C  
ANISOU  811  C   GLN A 107    11956  24464  13163  -1087     36   -609       C  
ATOM    812  O   GLN A 107     -40.828 -23.075 -12.348  1.00130.80           O  
ANISOU  812  O   GLN A 107    11968  24414  13316   -624    180   -333       O  
ATOM    813  CB  GLN A 107     -40.762 -25.004 -10.330  1.00125.76           C  
ANISOU  813  CB  GLN A 107    11623  23200  12961  -1755    286   -868       C  
ATOM    814  CG  GLN A 107     -42.264 -25.149 -10.189  1.00128.91           C  
ANISOU  814  CG  GLN A 107    11472  24290  13216  -1846    264  -1016       C  
ATOM    815  CD  GLN A 107     -42.730 -26.558 -10.482  1.00129.87           C  
ANISOU  815  CD  GLN A 107    11402  24718  13223  -2442    159  -1391       C  
ATOM    816  OE1 GLN A 107     -42.170 -27.527  -9.969  1.00127.38           O  
ANISOU  816  OE1 GLN A 107    11401  23945  13053  -2911    233  -1557       O  
ATOM    817  NE2 GLN A 107     -43.753 -26.683 -11.319  1.00133.92           N  
ANISOU  817  NE2 GLN A 107    11386  26014  13482  -2418      2  -1536       N  
ATOM    818  N   HIS A 129     -37.398 -25.932  16.018  1.00139.79           N  
ANISOU  818  N   HIS A 129    16811  22824  13480  -1817   3214  -1454       N  
ATOM    819  CA  HIS A 129     -38.430 -25.101  15.410  1.00138.92           C  
ANISOU  819  CA  HIS A 129    16381  22771  13633  -1823   3257  -1563       C  
ATOM    820  C   HIS A 129     -38.308 -25.059  13.893  1.00134.03           C  
ANISOU  820  C   HIS A 129    15671  21882  13371  -1976   3064  -1528       C  
ATOM    821  O   HIS A 129     -38.765 -25.966  13.199  1.00133.73           O  
ANISOU  821  O   HIS A 129    15576  21804  13430  -2248   3105  -1326       O  
ATOM    822  CB  HIS A 129     -38.374 -23.678  15.967  1.00139.81           C  
ANISOU  822  CB  HIS A 129    16399  22984  13737  -1516   3239  -1899       C  
ATOM    823  CG  HIS A 129     -38.955 -23.544  17.337  1.00 98.99           C  
ANISOU  823  CG  HIS A 129    11204  18167   8242  -1364   3478  -1962       C  
ATOM    824  ND1 HIS A 129     -40.256 -23.147  17.556  1.00101.40           N  
ANISOU  824  ND1 HIS A 129    11242  18703   8582  -1332   3709  -1967       N  
ATOM    825  CD2 HIS A 129     -38.414 -23.757  18.559  1.00100.98           C  
ANISOU  825  CD2 HIS A 129    11652  18615   8101  -1214   3527  -2018       C  
ATOM    826  CE1 HIS A 129     -40.492 -23.120  18.855  1.00104.59           C  
ANISOU  826  CE1 HIS A 129    11695  19404   8640  -1181   3903  -2026       C  
ATOM    827  NE2 HIS A 129     -39.390 -23.486  19.487  1.00106.96           N  
ANISOU  827  NE2 HIS A 129    12277  19705   8660  -1099   3793  -2058       N  
ATOM    828  N   ASN A 130     -37.693 -23.992  13.389  1.00130.40           N  
ANISOU  828  N   ASN A 130    15193  21245  13108  -1798   2876  -1740       N  
ATOM    829  CA  ASN A 130     -37.562 -23.778  11.953  1.00125.38           C  
ANISOU  829  CA  ASN A 130    14466  20380  12792  -1871   2706  -1705       C  
ATOM    830  C   ASN A 130     -36.739 -24.864  11.276  1.00121.47           C  
ANISOU  830  C   ASN A 130    14188  19646  12319  -2096   2559  -1537       C  
ATOM    831  O   ASN A 130     -35.813 -25.415  11.870  1.00120.56           O  
ANISOU  831  O   ASN A 130    14339  19442  12026  -2098   2516  -1512       O  
ATOM    832  CB  ASN A 130     -36.936 -22.413  11.670  1.00122.90           C  
ANISOU  832  CB  ASN A 130    14133  19874  12690  -1608   2590  -1949       C  
ATOM    833  CG  ASN A 130     -37.623 -21.290  12.417  1.00123.93           C  
ANISOU  833  CG  ASN A 130    14083  20188  12818  -1364   2763  -2153       C  
ATOM    834  OD1 ASN A 130     -38.108 -21.474  13.533  1.00125.68           O  
ANISOU  834  OD1 ASN A 130    14298  20675  12781  -1336   2928  -2187       O  
ATOM    835  ND2 ASN A 130     -37.670 -20.115  11.801  1.00123.01           N  
ANISOU  835  ND2 ASN A 130    13826  19920  12994  -1167   2755  -2278       N  
ATOM    836  N   GLN A 131     -37.074 -25.168  10.028  1.00119.43           N  
ANISOU  836  N   GLN A 131    13806  19309  12264  -2268   2484  -1427       N  
ATOM    837  CA  GLN A 131     -36.348 -26.192   9.293  1.00116.61           C  
ANISOU  837  CA  GLN A 131    13642  18714  11951  -2492   2362  -1289       C  
ATOM    838  C   GLN A 131     -34.987 -25.684   8.846  1.00112.85           C  
ANISOU  838  C   GLN A 131    13358  17926  11594  -2347   2139  -1386       C  
ATOM    839  O   GLN A 131     -34.732 -24.482   8.852  1.00113.10           O  
ANISOU  839  O   GLN A 131    13324  17905  11743  -2102   2084  -1563       O  
ATOM    840  CB  GLN A 131     -37.162 -26.683   8.099  1.00117.04           C  
ANISOU  840  CB  GLN A 131    13479  18831  12160  -2731   2351  -1192       C  
ATOM    841  CG  GLN A 131     -38.340 -27.550   8.493  1.00120.21           C  
ANISOU  841  CG  GLN A 131    13719  19487  12469  -2980   2585  -1094       C  
ATOM    842  CD  GLN A 131     -37.925 -28.713   9.370  1.00121.20           C  
ANISOU  842  CD  GLN A 131    14127  19508  12415  -3136   2743   -953       C  
ATOM    843  OE1 GLN A 131     -36.884 -29.333   9.147  1.00119.46           O  
ANISOU  843  OE1 GLN A 131    14187  19009  12194  -3200   2648   -880       O  
ATOM    844  NE2 GLN A 131     -38.733 -29.010  10.380  1.00124.36           N  
ANISOU  844  NE2 GLN A 131    14456  20133  12661  -3172   3009   -889       N  
ATOM    845  N   THR A 132     -34.115 -26.606   8.458  1.00109.63           N  
ANISOU  845  N   THR A 132    13182  17292  11182  -2502   2042  -1274       N  
ATOM    846  CA  THR A 132     -32.748 -26.248   8.116  1.00105.76           C  
ANISOU  846  CA  THR A 132    12881  16510  10793  -2381   1846  -1358       C  
ATOM    847  C   THR A 132     -32.295 -26.875   6.801  1.00100.77           C  
ANISOU  847  C   THR A 132    12325  15635  10327  -2559   1718  -1239       C  
ATOM    848  O   THR A 132     -32.429 -28.082   6.603  1.00101.15           O  
ANISOU  848  O   THR A 132    12465  15654  10314  -2807   1776  -1080       O  
ATOM    849  CB  THR A 132     -31.789 -26.642   9.249  1.00107.95           C  
ANISOU  849  CB  THR A 132    13410  16768  10839  -2299   1838  -1377       C  
ATOM    850  OG1 THR A 132     -31.983 -25.756  10.359  1.00110.38           O  
ANISOU  850  OG1 THR A 132    13639  17291  11010  -2075   1905  -1577       O  
ATOM    851  CG2 THR A 132     -30.351 -26.555   8.788  1.00106.24           C  
ANISOU  851  CG2 THR A 132    13377  16253  10737  -2236   1634  -1436       C  
ATOM    852  N   PHE A 133     -31.768 -26.043   5.904  1.00 95.68           N  
ANISOU  852  N   PHE A 133    11645  14805   9903  -2427   1575  -1321       N  
ATOM    853  CA  PHE A 133     -31.247 -26.519   4.626  1.00 90.51           C  
ANISOU  853  CA  PHE A 133    11068  13929   9392  -2553   1449  -1225       C  
ATOM    854  C   PHE A 133     -29.728 -26.373   4.567  1.00 86.48           C  
ANISOU  854  C   PHE A 133    10794  13102   8964  -2449   1312  -1279       C  
ATOM    855  O   PHE A 133     -29.202 -25.265   4.456  1.00 85.20           O  
ANISOU  855  O   PHE A 133    10595  12810   8966  -2235   1257  -1421       O  
ATOM    856  CB  PHE A 133     -31.894 -25.773   3.459  1.00 89.02           C  
ANISOU  856  CB  PHE A 133    10635  13808   9379  -2474   1410  -1222       C  
ATOM    857  CG  PHE A 133     -31.813 -26.510   2.156  1.00 86.54           C  
ANISOU  857  CG  PHE A 133    10337  13420   9124  -2661   1317  -1114       C  
ATOM    858  CD1 PHE A 133     -32.684 -27.551   1.887  1.00 87.31           C  
ANISOU  858  CD1 PHE A 133    10335  13714   9124  -2949   1377  -1049       C  
ATOM    859  CD2 PHE A 133     -30.867 -26.168   1.204  1.00 84.15           C  
ANISOU  859  CD2 PHE A 133    10139  12854   8980  -2558   1188  -1100       C  
ATOM    860  CE1 PHE A 133     -32.618 -28.236   0.694  1.00 86.39           C  
ANISOU  860  CE1 PHE A 133    10220  13554   9052  -3137   1293  -1007       C  
ATOM    861  CE2 PHE A 133     -30.794 -26.853   0.006  1.00 82.99           C  
ANISOU  861  CE2 PHE A 133    10008  12668   8855  -2719   1106  -1018       C  
ATOM    862  CZ  PHE A 133     -31.673 -27.888  -0.249  1.00 84.28           C  
ANISOU  862  CZ  PHE A 133    10068  13051   8904  -3011   1150   -989       C  
ATOM    863  N   LEU A 134     -29.031 -27.503   4.628  1.00 84.34           N  
ANISOU  863  N   LEU A 134    10752  12692   8602  -2604   1283  -1168       N  
ATOM    864  CA  LEU A 134     -27.581 -27.498   4.776  1.00 81.53           C  
ANISOU  864  CA  LEU A 134    10609  12089   8281  -2503   1162  -1214       C  
ATOM    865  C   LEU A 134     -26.822 -27.542   3.453  1.00 78.81           C  
ANISOU  865  C   LEU A 134    10336  11453   8154  -2539   1040  -1171       C  
ATOM    866  O   LEU A 134     -26.604 -28.611   2.891  1.00 78.14           O  
ANISOU  866  O   LEU A 134    10389  11249   8053  -2726   1034  -1026       O  
ATOM    867  CB  LEU A 134     -27.134 -28.660   5.669  1.00 81.23           C  
ANISOU  867  CB  LEU A 134    10789  12070   8006  -2579   1215  -1088       C  
ATOM    868  CG  LEU A 134     -27.774 -28.756   7.056  1.00 82.56           C  
ANISOU  868  CG  LEU A 134    10926  12539   7904  -2520   1359  -1089       C  
ATOM    869  CD1 LEU A 134     -28.991 -29.674   7.046  1.00 83.72           C  
ANISOU  869  CD1 LEU A 134    11020  12821   7968  -2756   1559   -908       C  
ATOM    870  CD2 LEU A 134     -26.760 -29.219   8.088  1.00 82.64           C  
ANISOU  870  CD2 LEU A 134    11142  12572   7685  -2388   1332  -1058       C  
ATOM    871  N   ILE A 135     -26.405 -26.378   2.968  1.00 77.91           N  
ANISOU  871  N   ILE A 135    10138  11207   8258  -2354    975  -1297       N  
ATOM    872  CA  ILE A 135     -25.559 -26.308   1.784  1.00 76.23           C  
ANISOU  872  CA  ILE A 135    10004  10706   8253  -2343    879  -1254       C  
ATOM    873  C   ILE A 135     -24.110 -26.549   2.171  1.00 76.08           C  
ANISOU  873  C   ILE A 135    10185  10466   8257  -2300    790  -1310       C  
ATOM    874  O   ILE A 135     -23.580 -25.859   3.036  1.00 77.02           O  
ANISOU  874  O   ILE A 135    10281  10593   8390  -2149    771  -1500       O  
ATOM    875  CB  ILE A 135     -25.629 -24.931   1.128  1.00 76.17           C  
ANISOU  875  CB  ILE A 135     9835  10609   8498  -2134    897  -1336       C  
ATOM    876  CG1 ILE A 135     -27.071 -24.577   0.776  1.00 77.56           C  
ANISOU  876  CG1 ILE A 135     9776  11054   8640  -2112    982  -1272       C  
ATOM    877  CG2 ILE A 135     -24.751 -24.893  -0.104  1.00 74.59           C  
ANISOU  877  CG2 ILE A 135     9726  10117   8498  -2109    828  -1259       C  
ATOM    878  CD1 ILE A 135     -27.204 -23.238   0.101  1.00 77.83           C  
ANISOU  878  CD1 ILE A 135     9655  11001   8917  -1856   1041  -1292       C  
ATOM    879  N   ASP A 136     -23.474 -27.521   1.526  1.00 75.33           N  
ANISOU  879  N   ASP A 136    10265  10191   8165  -2429    737  -1169       N  
ATOM    880  CA  ASP A 136     -22.076 -27.848   1.805  1.00 75.09           C  
ANISOU  880  CA  ASP A 136    10411   9964   8154  -2378    651  -1192       C  
ATOM    881  C   ASP A 136     -21.809 -28.124   3.279  1.00 77.88           C  
ANISOU  881  C   ASP A 136    10818  10502   8268  -2308    650  -1253       C  
ATOM    882  O   ASP A 136     -22.652 -28.682   3.977  1.00 79.27           O  
ANISOU  882  O   ASP A 136    10998  10905   8216  -2378    747  -1164       O  
ATOM    883  CB  ASP A 136     -21.143 -26.743   1.304  1.00 73.12           C  
ANISOU  883  CB  ASP A 136    10108   9481   8195  -2215    586  -1348       C  
ATOM    884  CG  ASP A 136     -20.802 -26.892  -0.158  1.00 70.70           C  
ANISOU  884  CG  ASP A 136     9860   8927   8077  -2263    568  -1219       C  
ATOM    885  OD1 ASP A 136     -20.424 -28.006  -0.571  1.00 69.49           O  
ANISOU  885  OD1 ASP A 136     9875   8676   7851  -2399    541  -1071       O  
ATOM    886  OD2 ASP A 136     -20.911 -25.894  -0.895  1.00 70.34           O  
ANISOU  886  OD2 ASP A 136     9695   8780   8251  -2149    604  -1258       O  
ATOM    887  N   GLY A 137     -20.631 -27.718   3.743  1.00 79.36           N  
ANISOU  887  N   GLY A 137    11032  10619   8503  -2159    549  -1410       N  
ATOM    888  CA  GLY A 137     -20.209 -28.000   5.100  1.00 82.97           C  
ANISOU  888  CA  GLY A 137    11531  11304   8689  -2050    516  -1475       C  
ATOM    889  C   GLY A 137     -19.656 -29.404   5.198  1.00 84.97           C  
ANISOU  889  C   GLY A 137    12008  11510   8767  -2099    518  -1214       C  
ATOM    890  O   GLY A 137     -19.409 -30.045   4.179  1.00 83.68           O  
ANISOU  890  O   GLY A 137    11964  11087   8744  -2225    530  -1045       O  
ATOM    891  N   PRO A 138     -19.460 -29.891   6.429  1.00 88.60           N  
ANISOU  891  N   PRO A 138    12529  12228   8909  -1980    528  -1170       N  
ATOM    892  CA  PRO A 138     -18.948 -31.244   6.650  1.00 90.67           C  
ANISOU  892  CA  PRO A 138    13013  12451   8987  -1972    577   -876       C  
ATOM    893  C   PRO A 138     -20.069 -32.270   6.670  1.00 93.59           C  
ANISOU  893  C   PRO A 138    13496  12832   9232  -2150    805   -592       C  
ATOM    894  O   PRO A 138     -21.244 -31.905   6.655  1.00 94.03           O  
ANISOU  894  O   PRO A 138    13428  13000   9299  -2262    896   -643       O  
ATOM    895  CB  PRO A 138     -18.331 -31.142   8.040  1.00 92.81           C  
ANISOU  895  CB  PRO A 138    13258  13068   8938  -1711    499   -967       C  
ATOM    896  CG  PRO A 138     -19.209 -30.164   8.741  1.00 93.64           C  
ANISOU  896  CG  PRO A 138    13174  13455   8951  -1671    520  -1210       C  
ATOM    897  CD  PRO A 138     -19.627 -29.154   7.693  1.00 91.03           C  
ANISOU  897  CD  PRO A 138    12697  12889   9002  -1807    500  -1403       C  
ATOM    898  N   GLU A 139     -19.699 -33.545   6.712  1.00 96.25           N  
ANISOU  898  N   GLU A 139    14054  13044   9473  -2172    917   -298       N  
ATOM    899  CA  GLU A 139     -20.672 -34.631   6.744  1.00 99.79           C  
ANISOU  899  CA  GLU A 139    14621  13443   9849  -2364   1187    -31       C  
ATOM    900  C   GLU A 139     -21.480 -34.639   8.040  1.00105.03           C  
ANISOU  900  C   GLU A 139    15240  14461  10205  -2268   1331     29       C  
ATOM    901  O   GLU A 139     -21.112 -33.984   9.014  1.00106.66           O  
ANISOU  901  O   GLU A 139    15365  14971  10189  -2012   1214   -107       O  
ATOM    902  CB  GLU A 139     -19.963 -35.973   6.567  1.00100.25           C  
ANISOU  902  CB  GLU A 139    14945  13241   9902  -2373   1318    272       C  
ATOM    903  CG  GLU A 139     -19.191 -36.104   5.260  1.00 97.40           C  
ANISOU  903  CG  GLU A 139    14652  12520   9837  -2479   1213    234       C  
ATOM    904  CD  GLU A 139     -20.092 -36.318   4.055  1.00 95.96           C  
ANISOU  904  CD  GLU A 139    14437  12130   9894  -2820   1307    193       C  
ATOM    905  OE1 GLU A 139     -21.301 -36.572   4.237  1.00 97.31           O  
ANISOU  905  OE1 GLU A 139    14547  12408  10019  -3002   1483    225       O  
ATOM    906  OE2 GLU A 139     -19.583 -36.238   2.918  1.00 93.95           O  
ANISOU  906  OE2 GLU A 139    14202  11633   9863  -2901   1206    119       O  
ATOM    907  N   THR A 140     -22.582 -35.383   8.040  1.00108.64           N  
ANISOU  907  N   THR A 140    15737  14888  10652  -2481   1598    209       N  
ATOM    908  CA  THR A 140     -23.420 -35.533   9.228  1.00113.92           C  
ANISOU  908  CA  THR A 140    16381  15863  11040  -2408   1798    317       C  
ATOM    909  C   THR A 140     -24.318 -36.760   9.121  1.00117.41           C  
ANISOU  909  C   THR A 140    16939  16140  11532  -2668   2159    595       C  
ATOM    910  O   THR A 140     -24.516 -37.298   8.035  1.00116.70           O  
ANISOU  910  O   THR A 140    16883  15739  11718  -2954   2226    610       O  
ATOM    911  CB  THR A 140     -24.307 -34.300   9.459  1.00114.74           C  
ANISOU  911  CB  THR A 140    16215  16248  11134  -2406   1714     31       C  
ATOM    912  OG1 THR A 140     -25.218 -34.566  10.531  1.00118.19           O  
ANISOU  912  OG1 THR A 140    16634  16960  11311  -2369   1952    160       O  
ATOM    913  CG2 THR A 140     -25.097 -33.974   8.205  1.00113.14           C  
ANISOU  913  CG2 THR A 140    15855  15878  11255  -2696   1692   -103       C  
ATOM    914  N   ALA A 141     -24.864 -37.196  10.250  1.00121.43           N  
ANISOU  914  N   ALA A 141    17498  16862  11777  -2572   2412    798       N  
ATOM    915  CA  ALA A 141     -25.779 -38.332  10.257  1.00124.94           C  
ANISOU  915  CA  ALA A 141    18035  17140  12297  -2829   2816   1054       C  
ATOM    916  C   ALA A 141     -27.205 -37.882   9.948  1.00126.00           C  
ANISOU  916  C   ALA A 141    17907  17399  12570  -3113   2891    863       C  
ATOM    917  O   ALA A 141     -28.005 -38.654   9.423  1.00127.46           O  
ANISOU  917  O   ALA A 141    18077  17388  12964  -3454   3147    928       O  
ATOM    918  CB  ALA A 141     -25.722 -39.062  11.594  1.00128.89           C  
ANISOU  918  CB  ALA A 141    18719  17793  12460  -2579   3109   1411       C  
ATOM    919  N   GLU A 142     -27.514 -36.630  10.277  1.00125.40           N  
ANISOU  919  N   GLU A 142    17607  17653  12387  -2970   2679    609       N  
ATOM    920  CA  GLU A 142     -28.838 -36.074  10.018  1.00125.50           C  
ANISOU  920  CA  GLU A 142    17339  17831  12513  -3177   2728    427       C  
ATOM    921  C   GLU A 142     -29.088 -35.916   8.524  1.00121.80           C  
ANISOU  921  C   GLU A 142    16731  17162  12386  -3461   2586    241       C  
ATOM    922  O   GLU A 142     -30.232 -35.981   8.069  1.00122.87           O  
ANISOU  922  O   GLU A 142    16662  17363  12661  -3726   2703    164       O  
ATOM    923  CB  GLU A 142     -29.005 -34.717  10.704  1.00125.78           C  
ANISOU  923  CB  GLU A 142    17183  18236  12371  -2917   2544    193       C  
ATOM    924  CG  GLU A 142     -28.165 -33.606  10.105  1.00122.88           C  
ANISOU  924  CG  GLU A 142    16739  17827  12123  -2772   2174    -85       C  
ATOM    925  CD  GLU A 142     -28.491 -32.248  10.681  1.00123.32           C  
ANISOU  925  CD  GLU A 142    16582  18191  12083  -2569   2053   -357       C  
ATOM    926  OE1 GLU A 142     -29.347 -31.548  10.102  1.00122.63           O  
ANISOU  926  OE1 GLU A 142    16263  18153  12179  -2677   2029   -517       O  
ATOM    927  OE2 GLU A 142     -27.882 -31.878  11.707  1.00124.80           O  
ANISOU  927  OE2 GLU A 142    16825  18586  12009  -2290   1987   -421       O  
ATOM    928  N   CYS A 143     -28.015 -35.699   7.767  1.00117.34           N  
ANISOU  928  N   CYS A 143    16258  16388  11938  -3390   2333    163       N  
ATOM    929  CA  CYS A 143     -28.115 -35.542   6.323  1.00112.73           C  
ANISOU  929  CA  CYS A 143    15564  15632  11634  -3607   2188      5       C  
ATOM    930  C   CYS A 143     -27.023 -36.311   5.594  1.00109.17           C  
ANISOU  930  C   CYS A 143    15356  14814  11310  -3659   2143    101       C  
ATOM    931  O   CYS A 143     -25.854 -35.941   5.645  1.00106.99           O  
ANISOU  931  O   CYS A 143    15194  14456  11000  -3421   1946     89       O  
ATOM    932  CB  CYS A 143     -28.058 -34.071   5.923  1.00110.47           C  
ANISOU  932  CB  CYS A 143    15065  15500  11409  -3437   1898   -251       C  
ATOM    933  SG  CYS A 143     -27.707 -33.852   4.176  1.00 81.31           S  
ANISOU  933  SG  CYS A 143    11316  11578   7999  -3571   1690   -379       S  
ATOM    934  N   PRO A 144     -27.410 -37.389   4.904  1.00108.28           N  
ANISOU  934  N   PRO A 144    15304  14478  11359  -3984   2341    170       N  
ATOM    935  CA  PRO A 144     -26.477 -38.216   4.138  1.00106.26           C  
ANISOU  935  CA  PRO A 144    15279  13846  11248  -4067   2346    249       C  
ATOM    936  C   PRO A 144     -26.158 -37.558   2.806  1.00101.69           C  
ANISOU  936  C   PRO A 144    14589  13210  10840  -4107   2062     28       C  
ATOM    937  O   PRO A 144     -26.899 -36.676   2.378  1.00101.64           O  
ANISOU  937  O   PRO A 144    14315  13441  10864  -4136   1927   -160       O  
ATOM    938  CB  PRO A 144     -27.277 -39.494   3.903  1.00109.55           C  
ANISOU  938  CB  PRO A 144    15740  14084  11800  -4445   2702    328       C  
ATOM    939  CG  PRO A 144     -28.691 -39.028   3.843  1.00110.93           C  
ANISOU  939  CG  PRO A 144    15587  14572  11989  -4635   2737    151       C  
ATOM    940  CD  PRO A 144     -28.794 -37.891   4.819  1.00110.63           C  
ANISOU  940  CD  PRO A 144    15430  14873  11729  -4309   2593    142       C  
ATOM    941  N   ASN A 145     -25.075 -37.978   2.163  1.00 98.26           N  
ANISOU  941  N   ASN A 145    14356  12472  10508  -4082   1992     74       N  
ATOM    942  CA  ASN A 145     -24.714 -37.424   0.864  1.00 94.13           C  
ANISOU  942  CA  ASN A 145    13751  11878  10135  -4105   1756   -103       C  
ATOM    943  C   ASN A 145     -25.754 -37.784  -0.192  1.00 93.58           C  
ANISOU  943  C   ASN A 145    13512  11860  10186  -4453   1822   -258       C  
ATOM    944  O   ASN A 145     -25.926 -37.072  -1.178  1.00 91.70           O  
ANISOU  944  O   ASN A 145    13097  11740  10005  -4451   1626   -424       O  
ATOM    945  CB  ASN A 145     -23.331 -37.912   0.426  1.00 93.13           C  
ANISOU  945  CB  ASN A 145    13885  11409  10093  -4012   1704    -10       C  
ATOM    946  CG  ASN A 145     -22.233 -37.509   1.392  1.00 93.12           C  
ANISOU  946  CG  ASN A 145    14000  11417   9966  -3656   1597    101       C  
ATOM    947  OD1 ASN A 145     -21.814 -38.298   2.236  1.00 95.23           O  
ANISOU  947  OD1 ASN A 145    14461  11598  10122  -3567   1759    316       O  
ATOM    948  ND2 ASN A 145     -21.760 -36.276   1.269  1.00 91.28           N  
ANISOU  948  ND2 ASN A 145    13636  11297   9750  -3442   1340    -50       N  
ATOM    949  N   THR A 146     -26.451 -38.892   0.029  1.00 95.47           N  
ANISOU  949  N   THR A 146    13790  12024  10459  -4745   2116   -208       N  
ATOM    950  CA  THR A 146     -27.460 -39.350  -0.915  1.00 95.65           C  
ANISOU  950  CA  THR A 146    13604  12130  10608  -4996   2142   -420       C  
ATOM    951  C   THR A 146     -28.706 -38.477  -0.873  1.00 95.85           C  
ANISOU  951  C   THR A 146    13274  12591  10553  -5137   2107   -562       C  
ATOM    952  O   THR A 146     -29.525 -38.522  -1.785  1.00 96.86           O  
ANISOU  952  O   THR A 146    13158  12905  10741  -5296   2042   -774       O  
ATOM    953  CB  THR A 146     -27.856 -40.811  -0.657  1.00 97.55           C  
ANISOU  953  CB  THR A 146    13936  12148  10979  -5102   2416   -375       C  
ATOM    954  OG1 THR A 146     -28.869 -41.203  -1.592  1.00 99.01           O  
ANISOU  954  OG1 THR A 146    13886  12461  11272  -5342   2422   -636       O  
ATOM    955  CG2 THR A 146     -28.388 -40.974   0.750  1.00 99.25           C  
ANISOU  955  CG2 THR A 146    14168  12439  11103  -5095   2664   -187       C  
ATOM    956  N   ASN A 147     -28.847 -37.689   0.189  1.00 95.23           N  
ANISOU  956  N   ASN A 147    13139  12708  10337  -4886   2075   -470       N  
ATOM    957  CA  ASN A 147     -29.967 -36.762   0.303  1.00 95.77           C  
ANISOU  957  CA  ASN A 147    12861  13188  10339  -4849   1999   -595       C  
ATOM    958  C   ASN A 147     -29.599 -35.362  -0.156  1.00 93.13           C  
ANISOU  958  C   ASN A 147    12405  12997   9982  -4531   1691   -674       C  
ATOM    959  O   ASN A 147     -30.445 -34.470  -0.201  1.00 93.88           O  
ANISOU  959  O   ASN A 147    12213  13418  10040  -4445   1615   -767       O  
ATOM    960  CB  ASN A 147     -30.496 -36.713   1.735  1.00 97.30           C  
ANISOU  960  CB  ASN A 147    13038  13528  10402  -4768   2190   -472       C  
ATOM    961  CG  ASN A 147     -31.509 -37.797   2.019  1.00100.85           C  
ANISOU  961  CG  ASN A 147    13421  13989  10908  -5129   2528   -455       C  
ATOM    962  OD1 ASN A 147     -31.439 -38.890   1.461  1.00102.13           O  
ANISOU  962  OD1 ASN A 147    13691  13892  11223  -5380   2664   -477       O  
ATOM    963  ND2 ASN A 147     -32.467 -37.496   2.886  1.00102.77           N  
ANISOU  963  ND2 ASN A 147    13479  14512  11059  -5113   2664   -437       N  
ATOM    964  N   ARG A 148     -28.328 -35.173  -0.491  1.00 90.56           N  
ANISOU  964  N   ARG A 148    12297  12412   9700  -4349   1544   -625       N  
ATOM    965  CA  ARG A 148     -27.853 -33.889  -0.982  1.00 87.99           C  
ANISOU  965  CA  ARG A 148    11885  12141   9408  -4058   1302   -689       C  
ATOM    966  C   ARG A 148     -28.040 -33.801  -2.489  1.00 86.73           C  
ANISOU  966  C   ARG A 148    11595  12032   9326  -4148   1183   -793       C  
ATOM    967  O   ARG A 148     -27.960 -34.807  -3.191  1.00 87.46           O  
ANISOU  967  O   ARG A 148    11776  11993   9462  -4403   1241   -823       O  
ATOM    968  CB  ARG A 148     -26.376 -33.697  -0.634  1.00 86.88           C  
ANISOU  968  CB  ARG A 148    12007  11712   9293  -3823   1213   -608       C  
ATOM    969  CG  ARG A 148     -26.065 -33.745   0.854  1.00 88.89           C  
ANISOU  969  CG  ARG A 148    12381  11978   9415  -3680   1297   -517       C  
ATOM    970  CD  ARG A 148     -26.082 -32.358   1.484  1.00 89.51           C  
ANISOU  970  CD  ARG A 148    12307  12247   9456  -3393   1183   -622       C  
ATOM    971  NE  ARG A 148     -25.898 -32.422   2.933  1.00 91.86           N  
ANISOU  971  NE  ARG A 148    12689  12641   9572  -3259   1260   -572       N  
ATOM    972  CZ  ARG A 148     -25.420 -31.429   3.679  1.00 92.55           C  
ANISOU  972  CZ  ARG A 148    12736  12821   9609  -2993   1160   -685       C  
ATOM    973  NH1 ARG A 148     -25.063 -30.283   3.117  1.00 91.37           N  
ANISOU  973  NH1 ARG A 148    12471  12617   9628  -2843   1011   -842       N  
ATOM    974  NH2 ARG A 148     -25.292 -31.586   4.990  1.00 94.37           N  
ANISOU  974  NH2 ARG A 148    13036  13200   9620  -2871   1229   -648       N  
ATOM    975  N   ALA A 149     -28.298 -32.596  -2.985  1.00 85.07           N  
ANISOU  975  N   ALA A 149    11174  12021   9127  -3923   1036   -846       N  
ATOM    976  CA  ALA A 149     -28.368 -32.377  -4.425  1.00 84.43           C  
ANISOU  976  CA  ALA A 149    10975  12027   9077  -3917    912   -906       C  
ATOM    977  C   ALA A 149     -27.016 -31.903  -4.945  1.00 81.88           C  
ANISOU  977  C   ALA A 149    10857  11395   8860  -3687    799   -841       C  
ATOM    978  O   ALA A 149     -26.294 -31.180  -4.256  1.00 80.71           O  
ANISOU  978  O   ALA A 149    10803  11086   8777  -3451    776   -794       O  
ATOM    979  CB  ALA A 149     -29.453 -31.378  -4.767  1.00 85.44           C  
ANISOU  979  CB  ALA A 149    10748  12563   9152  -3766    850   -954       C  
ATOM    980  N   TRP A 150     -26.681 -32.308  -6.165  1.00 81.36           N  
ANISOU  980  N   TRP A 150    10840  11262   8811  -3766    739   -865       N  
ATOM    981  CA  TRP A 150     -25.358 -32.048  -6.717  1.00 78.88           C  
ANISOU  981  CA  TRP A 150    10736  10627   8608  -3589    666   -796       C  
ATOM    982  C   TRP A 150     -25.354 -32.127  -8.240  1.00 78.83           C  
ANISOU  982  C   TRP A 150    10675  10707   8572  -3600    590   -829       C  
ATOM    983  O   TRP A 150     -26.061 -32.949  -8.822  1.00 80.84           O  
ANISOU  983  O   TRP A 150    10836  11157   8722  -3864    606   -942       O  
ATOM    984  CB  TRP A 150     -24.362 -33.043  -6.135  1.00 78.42           C  
ANISOU  984  CB  TRP A 150    10990  10202   8602  -3717    741   -746       C  
ATOM    985  CG  TRP A 150     -23.092 -33.152  -6.892  1.00 77.34           C  
ANISOU  985  CG  TRP A 150    11061   9751   8572  -3628    687   -698       C  
ATOM    986  CD1 TRP A 150     -22.007 -32.339  -6.785  1.00 75.77           C  
ANISOU  986  CD1 TRP A 150    10949   9340   8502  -3358    623   -640       C  
ATOM    987  CD2 TRP A 150     -22.759 -34.145  -7.866  1.00 78.23           C  
ANISOU  987  CD2 TRP A 150    11313   9721   8690  -3822    716   -727       C  
ATOM    988  NE1 TRP A 150     -21.018 -32.759  -7.639  1.00 75.07           N  
ANISOU  988  NE1 TRP A 150    11041   8989   8495  -3360    608   -604       N  
ATOM    989  CE2 TRP A 150     -21.456 -33.868  -8.314  1.00 76.40           C  
ANISOU  989  CE2 TRP A 150    11255   9195   8579  -3633    662   -654       C  
ATOM    990  CE3 TRP A 150     -23.439 -35.240  -8.406  1.00 80.58           C  
ANISOU  990  CE3 TRP A 150    11592  10106   8918  -4150    797   -838       C  
ATOM    991  CZ2 TRP A 150     -20.818 -34.648  -9.277  1.00 76.18           C  
ANISOU  991  CZ2 TRP A 150    11398   8965   8583  -3739    686   -664       C  
ATOM    992  CZ3 TRP A 150     -22.804 -36.011  -9.360  1.00 80.45           C  
ANISOU  992  CZ3 TRP A 150    11735   9894   8938  -4218    816   -870       C  
ATOM    993  CH2 TRP A 150     -21.508 -35.712  -9.786  1.00 78.20           C  
ANISOU  993  CH2 TRP A 150    11626   9335   8751  -3975    756   -767       C  
ATOM    994  N   ASN A 151     -24.547 -31.274  -8.868  1.00 76.64           N  
ANISOU  994  N   ASN A 151    10448  10288   8385  -3316    523   -744       N  
ATOM    995  CA  ASN A 151     -24.474 -31.176 -10.323  1.00 76.79           C  
ANISOU  995  CA  ASN A 151    10417  10412   8347  -3241    459   -736       C  
ATOM    996  C   ASN A 151     -25.844 -30.931 -10.923  1.00 79.77           C  
ANISOU  996  C   ASN A 151    10462  11311   8536  -3243    408   -801       C  
ATOM    997  O   ASN A 151     -26.296 -31.676 -11.788  1.00 82.23           O  
ANISOU  997  O   ASN A 151    10693  11851   8698  -3442    370   -923       O  
ATOM    998  CB  ASN A 151     -23.827 -32.421 -10.932  1.00 76.17           C  
ANISOU  998  CB  ASN A 151    10563  10121   8257  -3490    478   -800       C  
ATOM    999  CG  ASN A 151     -23.257 -32.163 -12.309  1.00 75.74           C  
ANISOU  999  CG  ASN A 151    10547  10050   8179  -3326    423   -756       C  
ATOM   1000  OD1 ASN A 151     -22.880 -31.041 -12.634  1.00 75.02           O  
ANISOU 1000  OD1 ASN A 151    10416   9927   8160  -2990    403   -619       O  
ATOM   1001  ND2 ASN A 151     -23.184 -33.205 -13.125  1.00 76.49           N  
ANISOU 1001  ND2 ASN A 151    10725  10153   8184  -3561    427   -875       N  
ATOM   1002  N   SER A 152     -26.506 -29.887 -10.437  1.00 80.33           N  
ANISOU 1002  N   SER A 152    10322  11585   8614  -3019    414   -740       N  
ATOM   1003  CA  SER A 152     -27.837 -29.541 -10.904  1.00 83.55           C  
ANISOU 1003  CA  SER A 152    10376  12527   8843  -2964    367   -776       C  
ATOM   1004  C   SER A 152     -27.894 -28.083 -11.340  1.00 83.71           C  
ANISOU 1004  C   SER A 152    10253  12654   8899  -2498    367   -594       C  
ATOM   1005  O   SER A 152     -28.972 -27.509 -11.476  1.00 85.81           O  
ANISOU 1005  O   SER A 152    10213  13342   9048  -2346    353   -568       O  
ATOM   1006  CB  SER A 152     -28.876 -29.818  -9.816  1.00 85.82           C  
ANISOU 1006  CB  SER A 152    10496  13020   9091  -3167    422   -877       C  
ATOM   1007  OG  SER A 152     -28.583 -29.106  -8.628  1.00 85.28           O  
ANISOU 1007  OG  SER A 152    10510  12724   9170  -3005    497   -799       O  
ATOM   1008  N   LEU A 153     -26.724 -27.491 -11.562  1.00 82.05           N  
ANISOU 1008  N   LEU A 153    10259  12048   8870  -2266    410   -460       N  
ATOM   1009  CA  LEU A 153     -26.638 -26.121 -12.064  1.00 82.48           C  
ANISOU 1009  CA  LEU A 153    10219  12107   9014  -1816    474   -261       C  
ATOM   1010  C   LEU A 153     -25.638 -25.990 -13.213  1.00 82.48           C  
ANISOU 1010  C   LEU A 153    10384  11899   9054  -1641    487   -128       C  
ATOM   1011  O   LEU A 153     -24.447 -26.254 -13.044  1.00 79.92           O  
ANISOU 1011  O   LEU A 153    10330  11124   8912  -1721    518   -141       O  
ATOM   1012  CB  LEU A 153     -26.276 -25.154 -10.937  1.00 80.48           C  
ANISOU 1012  CB  LEU A 153    10018  11530   9032  -1649    596   -231       C  
ATOM   1013  CG  LEU A 153     -27.433 -24.786 -10.012  1.00 81.17           C  
ANISOU 1013  CG  LEU A 153     9872  11899   9070  -1643    628   -292       C  
ATOM   1014  CD1 LEU A 153     -27.010 -23.740  -8.996  1.00 80.29           C  
ANISOU 1014  CD1 LEU A 153     9812  11463   9229  -1451    763   -296       C  
ATOM   1015  CD2 LEU A 153     -28.604 -24.295 -10.834  1.00 83.81           C  
ANISOU 1015  CD2 LEU A 153     9884  12743   9217  -1413    612   -181       C  
ATOM   1016  N   GLU A 154     -26.132 -25.577 -14.377  1.00 85.79           N  
ANISOU 1016  N   GLU A 154    10629  12679   9289  -1379    468      8       N  
ATOM   1017  CA  GLU A 154     -25.285 -25.407 -15.552  1.00 87.28           C  
ANISOU 1017  CA  GLU A 154    10956  12734   9474  -1167    503    165       C  
ATOM   1018  C   GLU A 154     -25.114 -23.937 -15.931  1.00 90.14           C  
ANISOU 1018  C   GLU A 154    11263  12991   9996   -654    681    459       C  
ATOM   1019  O   GLU A 154     -25.728 -23.055 -15.333  1.00 91.42           O  
ANISOU 1019  O   GLU A 154    11263  13212  10262   -458    771    528       O  
ATOM   1020  CB  GLU A 154     -25.827 -26.210 -16.744  1.00 89.07           C  
ANISOU 1020  CB  GLU A 154    11060  13462   9321  -1257    359     92       C  
ATOM   1021  CG  GLU A 154     -27.211 -25.788 -17.226  1.00 92.09           C  
ANISOU 1021  CG  GLU A 154    11058  14525   9409  -1046    289    141       C  
ATOM   1022  CD  GLU A 154     -27.784 -26.733 -18.269  1.00 94.05           C  
ANISOU 1022  CD  GLU A 154    11147  15326   9263  -1220    115    -39       C  
ATOM   1023  OE1 GLU A 154     -27.139 -27.759 -18.571  1.00 92.71           O  
ANISOU 1023  OE1 GLU A 154    11185  14970   9071  -1534     68   -217       O  
ATOM   1024  OE2 GLU A 154     -28.884 -26.451 -18.785  1.00 97.35           O  
ANISOU 1024  OE2 GLU A 154    11216  16382   9392  -1038     29    -21       O  
ATOM   1025  N   VAL A 155     -24.269 -23.688 -16.928  1.00 91.88           N  
ANISOU 1025  N   VAL A 155    11626  13032  10254   -432    763    639       N  
ATOM   1026  CA  VAL A 155     -23.987 -22.336 -17.394  1.00 94.69           C  
ANISOU 1026  CA  VAL A 155    11964  13216  10799     66    996    954       C  
ATOM   1027  C   VAL A 155     -24.937 -21.930 -18.513  1.00 99.33           C  
ANISOU 1027  C   VAL A 155    12302  14400  11037    446    987   1184       C  
ATOM   1028  O   VAL A 155     -25.129 -22.680 -19.469  1.00100.84           O  
ANISOU 1028  O   VAL A 155    12454  14993  10868    388    832   1146       O  
ATOM   1029  CB  VAL A 155     -22.547 -22.231 -17.936  1.00 94.43           C  
ANISOU 1029  CB  VAL A 155    12208  12673  10999    143   1135   1066       C  
ATOM   1030  CG1 VAL A 155     -22.293 -20.853 -18.521  1.00 96.81           C  
ANISOU 1030  CG1 VAL A 155    12487  12787  11509    665   1430   1419       C  
ATOM   1031  CG2 VAL A 155     -21.543 -22.540 -16.848  1.00 91.43           C  
ANISOU 1031  CG2 VAL A 155    12040  11738  10962   -176   1144    852       C  
ATOM   1032  N   GLU A 156     -25.534 -20.747 -18.390  1.00101.41           N  
ANISOU 1032  N   GLU A 156    12390  14744  11397    848   1159   1413       N  
ATOM   1033  CA  GLU A 156     -26.304 -20.182 -19.491  1.00105.78           C  
ANISOU 1033  CA  GLU A 156    12715  15836  11640   1328   1200   1716       C  
ATOM   1034  C   GLU A 156     -25.366 -19.424 -20.414  1.00107.96           C  
ANISOU 1034  C   GLU A 156    13169  15782  12070   1748   1465   2071       C  
ATOM   1035  O   GLU A 156     -25.303 -19.707 -21.612  1.00110.36           O  
ANISOU 1035  O   GLU A 156    13466  16425  12041   1931   1413   2216       O  
ATOM   1036  CB  GLU A 156     -27.400 -19.245 -18.991  1.00107.00           C  
ANISOU 1036  CB  GLU A 156    12593  16235  11827   1626   1302   1848       C  
ATOM   1037  CG  GLU A 156     -28.154 -18.543 -20.114  1.00110.85           C  
ANISOU 1037  CG  GLU A 156    12835  17279  12002   2214   1378   2227       C  
ATOM   1038  CD  GLU A 156     -29.082 -19.473 -20.869  1.00112.53           C  
ANISOU 1038  CD  GLU A 156    12780  18347  11629   2110   1049   2087       C  
ATOM   1039  OE1 GLU A 156     -28.857 -19.686 -22.078  1.00114.30           O  
ANISOU 1039  OE1 GLU A 156    13014  18874  11540   2315   1001   2229       O  
ATOM   1040  OE2 GLU A 156     -30.043 -19.983 -20.255  1.00112.63           O  
ANISOU 1040  OE2 GLU A 156    12557  18743  11496   1823    850   1818       O  
ATOM   1041  N   ASP A 157     -24.633 -18.466 -19.850  1.00107.88           N  
ANISOU 1041  N   ASP A 157    13310  15111  12568   1892   1768   2190       N  
ATOM   1042  CA  ASP A 157     -23.662 -17.708 -20.639  1.00109.79           C  
ANISOU 1042  CA  ASP A 157    13731  14937  13047   2261   2085   2521       C  
ATOM   1043  C   ASP A 157     -22.714 -16.891 -19.773  1.00109.09           C  
ANISOU 1043  C   ASP A 157    13814  14037  13597   2226   2386   2484       C  
ATOM   1044  O   ASP A 157     -22.718 -17.007 -18.553  1.00106.96           O  
ANISOU 1044  O   ASP A 157    13545  13547  13547   1894   2310   2173       O  
ATOM   1045  CB  ASP A 157     -24.368 -16.782 -21.627  1.00115.54           C  
ANISOU 1045  CB  ASP A 157    14278  16056  13567   2909   2285   2985       C  
ATOM   1046  CG  ASP A 157     -25.117 -15.669 -20.937  1.00118.83           C  
ANISOU 1046  CG  ASP A 157    14519  16404  14227   3199   2507   3122       C  
ATOM   1047  OD1 ASP A 157     -26.277 -15.894 -20.552  1.00120.26           O  
ANISOU 1047  OD1 ASP A 157    14445  17112  14137   3141   2297   3001       O  
ATOM   1048  OD2 ASP A 157     -24.547 -14.571 -20.777  1.00120.53           O  
ANISOU 1048  OD2 ASP A 157    14846  16025  14927   3476   2914   3337       O  
ATOM   1049  N   TYR A 158     -21.908 -16.054 -20.420  1.00111.35           N  
ANISOU 1049  N   TYR A 158    14230  13901  14176   2577   2744   2794       N  
ATOM   1050  CA  TYR A 158     -20.908 -15.252 -19.723  1.00111.17           C  
ANISOU 1050  CA  TYR A 158    14351  13087  14799   2536   3067   2731       C  
ATOM   1051  C   TYR A 158     -21.226 -13.764 -19.797  1.00114.58           C  
ANISOU 1051  C   TYR A 158    14695  13275  15567   3049   3521   3067       C  
ATOM   1052  O   TYR A 158     -21.831 -13.296 -20.761  1.00117.86           O  
ANISOU 1052  O   TYR A 158    15013  14030  15738   3547   3669   3490       O  
ATOM   1053  CB  TYR A 158     -19.518 -15.514 -20.304  1.00110.65           C  
ANISOU 1053  CB  TYR A 158    14525  12587  14929   2450   3176   2762       C  
ATOM   1054  CG  TYR A 158     -19.053 -16.942 -20.140  1.00107.78           C  
ANISOU 1054  CG  TYR A 158    14280  12345  14327   1944   2787   2423       C  
ATOM   1055  CD1 TYR A 158     -18.196 -17.299 -19.108  1.00104.89           C  
ANISOU 1055  CD1 TYR A 158    14027  11539  14290   1519   2710   2060       C  
ATOM   1056  CD2 TYR A 158     -19.476 -17.935 -21.012  1.00108.26           C  
ANISOU 1056  CD2 TYR A 158    14327  12974  13831   1904   2511   2457       C  
ATOM   1057  CE1 TYR A 158     -17.771 -18.605 -18.951  1.00102.37           C  
ANISOU 1057  CE1 TYR A 158    13823  11311  13763   1099   2392   1794       C  
ATOM   1058  CE2 TYR A 158     -19.057 -19.243 -20.862  1.00105.80           C  
ANISOU 1058  CE2 TYR A 158    14136  12722  13343   1445   2206   2148       C  
ATOM   1059  CZ  TYR A 158     -18.206 -19.573 -19.829  1.00103.04           C  
ANISOU 1059  CZ  TYR A 158    13915  11896  13338   1059   2160   1844       C  
ATOM   1060  OH  TYR A 158     -17.786 -20.875 -19.677  1.00101.27           O  
ANISOU 1060  OH  TYR A 158    13818  11712  12947    645   1893   1581       O  
ATOM   1061  N   ASN A 166     -18.054 -12.808 -14.284  1.00 87.93           N  
ANISOU 1061  N   ASN A 166    11516   7637  14257   1520   3736   1216       N  
ATOM   1062  CA  ASN A 166     -19.468 -13.025 -14.006  1.00 88.43           C  
ANISOU 1062  CA  ASN A 166    11437   8261  13903   1588   3534   1263       C  
ATOM   1063  C   ASN A 166     -20.094 -14.029 -14.962  1.00 88.78           C  
ANISOU 1063  C   ASN A 166    11483   8907  13343   1631   3232   1513       C  
ATOM   1064  O   ASN A 166     -19.961 -13.905 -16.179  1.00 90.21           O  
ANISOU 1064  O   ASN A 166    11711   9133  13431   1927   3366   1877       O  
ATOM   1065  CB  ASN A 166     -20.232 -11.700 -14.046  1.00 91.46           C  
ANISOU 1065  CB  ASN A 166    11687   8532  14533   2018   3930   1488       C  
ATOM   1066  CG  ASN A 166     -19.844 -10.774 -12.914  1.00 91.76           C  
ANISOU 1066  CG  ASN A 166    11687   8049  15130   1918   4198   1137       C  
ATOM   1067  OD1 ASN A 166     -20.539 -10.686 -11.903  1.00 91.39           O  
ANISOU 1067  OD1 ASN A 166    11526   8172  15026   1807   4099    884       O  
ATOM   1068  ND2 ASN A 166     -18.721 -10.082 -13.073  1.00 92.64           N  
ANISOU 1068  ND2 ASN A 166    11882   7528  15788   1943   4550   1094       N  
ATOM   1069  N   ILE A 167     -20.776 -15.025 -14.404  1.00 88.23           N  
ANISOU 1069  N   ILE A 167    11353   9306  12865   1333   2842   1300       N  
ATOM   1070  CA  ILE A 167     -21.347 -16.097 -15.209  1.00 89.23           C  
ANISOU 1070  CA  ILE A 167    11462  10002  12439   1280   2537   1429       C  
ATOM   1071  C   ILE A 167     -22.825 -16.353 -14.936  1.00 91.82           C  
ANISOU 1071  C   ILE A 167    11571  10938  12380   1293   2345   1418       C  
ATOM   1072  O   ILE A 167     -23.203 -16.742 -13.830  1.00 90.55           O  
ANISOU 1072  O   ILE A 167    11357  10871  12175    995   2178   1123       O  
ATOM   1073  CB  ILE A 167     -20.586 -17.416 -15.013  1.00 86.21           C  
ANISOU 1073  CB  ILE A 167    11245   9601  11909    825   2235   1170       C  
ATOM   1074  CG1 ILE A 167     -19.123 -17.248 -15.419  1.00 85.58           C  
ANISOU 1074  CG1 ILE A 167    11359   8981  12175    826   2409   1199       C  
ATOM   1075  CG2 ILE A 167     -21.234 -18.522 -15.823  1.00 86.21           C  
ANISOU 1075  CG2 ILE A 167    11216  10173  11369    740   1952   1246       C  
ATOM   1076  CD1 ILE A 167     -18.335 -18.530 -15.416  1.00 82.79           C  
ANISOU 1076  CD1 ILE A 167    11173   8613  11671    452   2145   1013       C  
ATOM   1077  N   TRP A 168     -23.644 -16.131 -15.963  1.00 95.87           N  
ANISOU 1077  N   TRP A 168    11941  11886  12598   1656   2377   1748       N  
ATOM   1078  CA  TRP A 168     -25.062 -16.471 -15.934  1.00 98.70           C  
ANISOU 1078  CA  TRP A 168    12047  12919  12535   1681   2170   1753       C  
ATOM   1079  C   TRP A 168     -25.259 -17.984 -15.889  1.00 98.48           C  
ANISOU 1079  C   TRP A 168    12030  13277  12112   1214   1772   1488       C  
ATOM   1080  O   TRP A 168     -25.083 -18.672 -16.905  1.00 98.42           O  
ANISOU 1080  O   TRP A 168    12067  13512  11816   1195   1638   1564       O  
ATOM   1081  CB  TRP A 168     -25.774 -15.902 -17.167  1.00101.88           C  
ANISOU 1081  CB  TRP A 168    12279  13746  12683   2219   2289   2179       C  
ATOM   1082  CG  TRP A 168     -26.504 -14.613 -16.920  1.00104.05           C  
ANISOU 1082  CG  TRP A 168    12379  13999  13158   2668   2591   2409       C  
ATOM   1083  CD1 TRP A 168     -26.294 -13.737 -15.898  1.00103.56           C  
ANISOU 1083  CD1 TRP A 168    12355  13416  13578   2678   2854   2297       C  
ATOM   1084  CD2 TRP A 168     -27.575 -14.066 -17.704  1.00107.62           C  
ANISOU 1084  CD2 TRP A 168    12578  14992  13322   3186   2670   2780       C  
ATOM   1085  NE1 TRP A 168     -27.161 -12.676 -16.000  1.00107.16           N  
ANISOU 1085  NE1 TRP A 168    12618  14001  14099   3165   3121   2582       N  
ATOM   1086  CE2 TRP A 168     -27.958 -12.855 -17.100  1.00109.76           C  
ANISOU 1086  CE2 TRP A 168    12763  14989  13953   3502   3010   2905       C  
ATOM   1087  CE3 TRP A 168     -28.242 -14.481 -18.860  1.00109.68           C  
ANISOU 1087  CE3 TRP A 168    12661  15970  13043   3427   2486   3004       C  
ATOM   1088  CZ2 TRP A 168     -28.978 -12.055 -17.614  1.00114.27           C  
ANISOU 1088  CZ2 TRP A 168    13087  15959  14373   4074   3186   3291       C  
ATOM   1089  CZ3 TRP A 168     -29.254 -13.689 -19.367  1.00114.24           C  
ANISOU 1089  CZ3 TRP A 168    12971  17000  13435   3996   2629   3371       C  
ATOM   1090  CH2 TRP A 168     -29.613 -12.491 -18.746  1.00116.49           C  
ANISOU 1090  CH2 TRP A 168    13186  16979  14098   4327   2983   3534       C  
ATOM   1091  N   LEU A 169     -25.628 -18.487 -14.710  1.00 99.25           N  
ANISOU 1091  N   LEU A 169    12088  13419  12205    848   1617   1176       N  
ATOM   1092  CA  LEU A 169     -25.890 -19.914 -14.515  1.00100.20           C  
ANISOU 1092  CA  LEU A 169    12215  13851  12005    388   1301    920       C  
ATOM   1093  C   LEU A 169     -27.385 -20.237 -14.562  1.00104.85           C  
ANISOU 1093  C   LEU A 169    12494  15121  12224    375   1144    892       C  
ATOM   1094  O   LEU A 169     -28.221 -19.337 -14.513  1.00107.13           O  
ANISOU 1094  O   LEU A 169    12561  15625  12518    709   1266   1049       O  
ATOM   1095  CB  LEU A 169     -25.317 -20.380 -13.177  1.00 97.88           C  
ANISOU 1095  CB  LEU A 169    12081  13192  11916     -9   1245    613       C  
ATOM   1096  CG  LEU A 169     -23.818 -20.206 -12.947  1.00 96.23           C  
ANISOU 1096  CG  LEU A 169    12141  12357  12065    -69   1355    557       C  
ATOM   1097  CD1 LEU A 169     -23.450 -20.608 -11.533  1.00 94.34           C  
ANISOU 1097  CD1 LEU A 169    11994  11897  11955   -404   1280    256       C  
ATOM   1098  CD2 LEU A 169     -23.043 -21.032 -13.942  1.00 95.38           C  
ANISOU 1098  CD2 LEU A 169    12206  12200  11832   -174   1259    613       C  
ATOM   1099  N   LYS A 170     -27.716 -21.524 -14.646  1.00106.69           N  
ANISOU 1099  N   LYS A 170    12699  15679  12159    -16    895    681       N  
ATOM   1100  CA  LYS A 170     -29.113 -21.956 -14.673  1.00111.48           C  
ANISOU 1100  CA  LYS A 170    12985  16941  12433   -105    741    590       C  
ATOM   1101  C   LYS A 170     -29.279 -23.430 -14.300  1.00112.45           C  
ANISOU 1101  C   LYS A 170    13143  17194  12389   -666    540    269       C  
ATOM   1102  O   LYS A 170     -28.298 -24.137 -14.075  1.00110.19           O  
ANISOU 1102  O   LYS A 170    13145  16502  12221   -951    516    149       O  
ATOM   1103  CB  LYS A 170     -29.728 -21.709 -16.052  1.00114.84           C  
ANISOU 1103  CB  LYS A 170    13176  17926  12530    249    692    803       C  
ATOM   1104  CG  LYS A 170     -29.177 -22.613 -17.144  1.00114.49           C  
ANISOU 1104  CG  LYS A 170    13254  17994  12253    104    551    749       C  
ATOM   1105  CD  LYS A 170     -30.067 -22.598 -18.378  1.00118.68           C  
ANISOU 1105  CD  LYS A 170    13472  19280  12343    379    432    858       C  
ATOM   1106  CE  LYS A 170     -31.465 -23.111 -18.061  1.00121.22           C  
ANISOU 1106  CE  LYS A 170    13414  20240  12402    160    253    626       C  
ATOM   1107  NZ  LYS A 170     -32.351 -23.109 -19.258  1.00125.90           N  
ANISOU 1107  NZ  LYS A 170    13648  21654  12532    430    107    689       N  
ATOM   1108  N   LEU A 171     -30.530 -23.883 -14.246  1.00116.63           N  
ANISOU 1108  N   LEU A 171    13365  18288  12662   -812    420    138       N  
ATOM   1109  CA  LEU A 171     -30.844 -25.279 -13.949  1.00118.36           C  
ANISOU 1109  CA  LEU A 171    13576  18654  12742  -1348    280   -169       C  
ATOM   1110  C   LEU A 171     -30.423 -26.193 -15.096  1.00120.62           C  
ANISOU 1110  C   LEU A 171    13948  19055  12828  -1516    156   -262       C  
ATOM   1111  O   LEU A 171     -30.290 -25.750 -16.235  1.00122.27           O  
ANISOU 1111  O   LEU A 171    14101  19472  12884  -1187    133    -95       O  
ATOM   1112  CB  LEU A 171     -32.340 -25.451 -13.669  1.00121.93           C  
ANISOU 1112  CB  LEU A 171    13629  19703  12998  -1453    213   -298       C  
ATOM   1113  CG  LEU A 171     -32.882 -25.072 -12.288  1.00122.51           C  
ANISOU 1113  CG  LEU A 171    13628  19684  13237  -1498    321   -331       C  
ATOM   1114  CD1 LEU A 171     -32.093 -25.770 -11.193  1.00119.80           C  
ANISOU 1114  CD1 LEU A 171    13618  18803  13097  -1868    377   -474       C  
ATOM   1115  CD2 LEU A 171     -32.895 -23.566 -12.075  1.00123.41           C  
ANISOU 1115  CD2 LEU A 171    13692  19681  13517   -984    475    -72       C  
ATOM   1116  N   LYS A 172     -30.223 -27.472 -14.790  1.00121.37           N  
ANISOU 1116  N   LYS A 172    14181  19013  12921  -2011    102   -522       N  
ATOM   1117  CA  LYS A 172     -29.733 -28.425 -15.781  1.00123.46           C  
ANISOU 1117  CA  LYS A 172    14567  19303  13039  -2216     16   -656       C  
ATOM   1118  C   LYS A 172     -30.837 -29.200 -16.490  1.00128.83           C  
ANISOU 1118  C   LYS A 172    14911  20644  13396  -2451   -126   -920       C  
ATOM   1119  O   LYS A 172     -32.015 -29.097 -16.147  1.00131.25           O  
ANISOU 1119  O   LYS A 172    14875  21394  13601  -2498   -162  -1010       O  
ATOM   1120  CB  LYS A 172     -28.760 -29.418 -15.141  1.00120.64           C  
ANISOU 1120  CB  LYS A 172    14579  18366  12892  -2605     76   -786       C  
ATOM   1121  CG  LYS A 172     -27.402 -28.839 -14.792  1.00117.42           C  
ANISOU 1121  CG  LYS A 172    14513  17338  12763  -2394    179   -580       C  
ATOM   1122  CD  LYS A 172     -26.430 -29.936 -14.380  1.00115.27           C  
ANISOU 1122  CD  LYS A 172    14577  16586  12634  -2744    215   -701       C  
ATOM   1123  CE  LYS A 172     -25.094 -29.362 -13.953  1.00112.61           C  
ANISOU 1123  CE  LYS A 172    14528  15683  12574  -2546    301   -531       C  
ATOM   1124  NZ  LYS A 172     -24.388 -28.694 -15.074  1.00112.85           N  
ANISOU 1124  NZ  LYS A 172    14622  15640  12615  -2212    319   -353       N  
ATOM   1125  N   GLU A 173     -30.428 -29.978 -17.488  1.00130.72           N  
ANISOU 1125  N   GLU A 173    15236  20953  13478  -2604   -199  -1069       N  
ATOM   1126  CA  GLU A 173     -31.322 -30.885 -18.190  1.00135.41           C  
ANISOU 1126  CA  GLU A 173    15534  22130  13784  -2910   -329  -1415       C  
ATOM   1127  C   GLU A 173     -31.733 -32.008 -17.242  1.00135.17           C  
ANISOU 1127  C   GLU A 173    15513  21932  13915  -3490   -259  -1721       C  
ATOM   1128  O   GLU A 173     -32.907 -32.140 -16.893  1.00138.22           O  
ANISOU 1128  O   GLU A 173    15547  22744  14225  -3658   -287  -1890       O  
ATOM   1129  CB  GLU A 173     -30.611 -31.478 -19.409  1.00136.74           C  
ANISOU 1129  CB  GLU A 173    15858  22313  13784  -2952   -390  -1525       C  
ATOM   1130  CG  GLU A 173     -29.666 -30.516 -20.127  1.00136.02           C  
ANISOU 1130  CG  GLU A 173    15965  22048  13670  -2422   -361  -1155       C  
ATOM   1131  CD  GLU A 173     -30.346 -29.727 -21.230  1.00140.21           C  
ANISOU 1131  CD  GLU A 173    16153  23304  13817  -1958   -478  -1016       C  
ATOM   1132  OE1 GLU A 173     -31.580 -29.850 -21.377  1.00144.02           O  
ANISOU 1132  OE1 GLU A 173    16213  24462  14047  -2026   -608  -1209       O  
ATOM   1133  OE2 GLU A 173     -29.645 -28.988 -21.953  1.00140.07           O  
ANISOU 1133  OE2 GLU A 173    16277  23197  13747  -1509   -426   -704       O  
ATOM   1134  N   LYS A 174     -30.752 -32.809 -16.827  1.00132.03           N  
ANISOU 1134  N   LYS A 174    15513  20906  13745  -3775   -144  -1770       N  
ATOM   1135  CA  LYS A 174     -30.990 -33.940 -15.931  1.00131.37           C  
ANISOU 1135  CA  LYS A 174    15506  20569  13840  -4299    -16  -2005       C  
ATOM   1136  C   LYS A 174     -29.818 -34.147 -14.968  1.00125.03           C  
ANISOU 1136  C   LYS A 174    15162  19004  13340  -4339    139  -1822       C  
ATOM   1137  O   LYS A 174     -28.872 -33.359 -14.955  1.00122.19           O  
ANISOU 1137  O   LYS A 174    15022  18338  13067  -3983    132  -1550       O  
ATOM   1138  CB  LYS A 174     -31.249 -35.215 -16.738  1.00136.73           C  
ANISOU 1138  CB  LYS A 174    16110  21434  14407  -4744    -27  -2410       C  
ATOM   1139  CG  LYS A 174     -32.250 -36.170 -16.096  1.00141.38           C  
ANISOU 1139  CG  LYS A 174    16493  22141  15084  -5262     86  -2728       C  
ATOM   1140  CD  LYS A 174     -32.554 -37.362 -16.996  1.00146.30           C  
ANISOU 1140  CD  LYS A 174    17055  22857  15675  -5503    156  -3058       C  
ATOM   1141  CE  LYS A 174     -33.568 -38.298 -16.350  1.00149.95           C  
ANISOU 1141  CE  LYS A 174    17375  23293  16306  -5811    367  -3256       C  
ATOM   1142  NZ  LYS A 174     -33.939 -39.435 -17.236  1.00154.34           N  
ANISOU 1142  NZ  LYS A 174    17840  23952  16848  -6034    452  -3606       N  
ATOM   1143  N   GLN A 175     -29.885 -35.206 -14.164  1.00122.45           N  
ANISOU 1143  N   GLN A 175    14962  18388  13174  -4762    294  -1970       N  
ATOM   1144  CA  GLN A 175     -28.863 -35.471 -13.154  1.00116.74           C  
ANISOU 1144  CA  GLN A 175    14640  17019  12699  -4785    441  -1791       C  
ATOM   1145  C   GLN A 175     -27.722 -36.350 -13.665  1.00112.39           C  
ANISOU 1145  C   GLN A 175    14442  16025  12237  -4925    508  -1831       C  
ATOM   1146  O   GLN A 175     -27.511 -37.460 -13.177  1.00113.37           O  
ANISOU 1146  O   GLN A 175    14765  15801  12509  -5182    690  -1891       O  
ATOM   1147  CB  GLN A 175     -29.483 -36.086 -11.891  1.00117.97           C  
ANISOU 1147  CB  GLN A 175    14776  17070  12977  -5089    616  -1844       C  
ATOM   1148  CG  GLN A 175     -30.388 -37.290 -12.136  1.00122.20           C  
ANISOU 1148  CG  GLN A 175    15153  17774  13505  -5493    735  -2143       C  
ATOM   1149  CD  GLN A 175     -30.671 -38.068 -10.866  1.00123.40           C  
ANISOU 1149  CD  GLN A 175    15439  17618  13831  -5620    985  -2080       C  
ATOM   1150  OE1 GLN A 175     -30.584 -37.529  -9.763  1.00122.09           O  
ANISOU 1150  OE1 GLN A 175    15330  17343  13716  -5536   1027  -1891       O  
ATOM   1151  NE2 GLN A 175     -31.004 -39.346 -11.015  1.00126.47           N  
ANISOU 1151  NE2 GLN A 175    15873  17874  14305  -5821   1164  -2246       N  
ATOM   1152  N   ASP A 176     -26.980 -35.845 -14.642  1.00107.37           N  
ANISOU 1152  N   ASP A 176    13891  15381  11524  -4644    395  -1741       N  
ATOM   1153  CA  ASP A 176     -25.794 -36.540 -15.115  1.00102.08           C  
ANISOU 1153  CA  ASP A 176    13565  14274  10949  -4713    461  -1744       C  
ATOM   1154  C   ASP A 176     -24.651 -36.325 -14.137  1.00 95.36           C  
ANISOU 1154  C   ASP A 176    13040  12865  10329  -4547    546  -1477       C  
ATOM   1155  O   ASP A 176     -24.591 -35.305 -13.456  1.00 94.01           O  
ANISOU 1155  O   ASP A 176    12821  12689  10209  -4265    502  -1281       O  
ATOM   1156  CB  ASP A 176     -25.400 -36.048 -16.506  1.00102.20           C  
ANISOU 1156  CB  ASP A 176    13547  14497  10787  -4450    330  -1727       C  
ATOM   1157  CG  ASP A 176     -25.162 -34.559 -16.548  1.00100.87           C  
ANISOU 1157  CG  ASP A 176    13310  14416  10601  -3947    238  -1425       C  
ATOM   1158  OD1 ASP A 176     -25.746 -33.842 -15.713  1.00100.93           O  
ANISOU 1158  OD1 ASP A 176    13158  14541  10649  -3826    228  -1319       O  
ATOM   1159  OD2 ASP A 176     -24.394 -34.105 -17.419  1.00100.35           O  
ANISOU 1159  OD2 ASP A 176    13351  14285  10494  -3671    204  -1295       O  
ATOM   1160  N   VAL A 177     -23.748 -37.295 -14.064  1.00 91.04           N  
ANISOU 1160  N   VAL A 177    12798  11870   9924  -4660    676  -1468       N  
ATOM   1161  CA  VAL A 177     -22.608 -37.201 -13.164  1.00 84.82           C  
ANISOU 1161  CA  VAL A 177    12278  10622   9329  -4414    740  -1212       C  
ATOM   1162  C   VAL A 177     -21.401 -36.598 -13.871  1.00 79.88           C  
ANISOU 1162  C   VAL A 177    11825   9775   8753  -4201    670  -1096       C  
ATOM   1163  O   VAL A 177     -20.259 -36.842 -13.483  1.00 77.99           O  
ANISOU 1163  O   VAL A 177    11791   9171   8671  -3970    723   -932       O  
ATOM   1164  CB  VAL A 177     -22.230 -38.572 -12.599  1.00 85.12           C  
ANISOU 1164  CB  VAL A 177    12494  10355   9493  -4404    917  -1172       C  
ATOM   1165  CG1 VAL A 177     -23.267 -39.026 -11.590  1.00 87.06           C  
ANISOU 1165  CG1 VAL A 177    12627  10716   9737  -4578   1025  -1219       C  
ATOM   1166  CG2 VAL A 177     -22.088 -39.583 -13.726  1.00 86.88           C  
ANISOU 1166  CG2 VAL A 177    12768  10544   9698  -4511    985  -1329       C  
ATOM   1167  N   PHE A 178     -21.664 -35.810 -14.909  1.00 77.85           N  
ANISOU 1167  N   PHE A 178    11402   9826   8352  -4045    549  -1117       N  
ATOM   1168  CA  PHE A 178     -20.608 -35.118 -15.632  1.00 73.81           C  
ANISOU 1168  CA  PHE A 178    11007   9144   7891  -3723    514   -956       C  
ATOM   1169  C   PHE A 178     -20.474 -33.689 -15.129  1.00 71.19           C  
ANISOU 1169  C   PHE A 178    10573   8821   7656  -3361    466   -749       C  
ATOM   1170  O   PHE A 178     -21.433 -33.106 -14.629  1.00 71.60           O  
ANISOU 1170  O   PHE A 178    10397   9162   7645  -3316    425   -751       O  
ATOM   1171  CB  PHE A 178     -20.904 -35.100 -17.133  1.00 74.74           C  
ANISOU 1171  CB  PHE A 178    11013   9604   7783  -3670    448  -1056       C  
ATOM   1172  CG  PHE A 178     -21.055 -36.465 -17.743  1.00 76.25           C  
ANISOU 1172  CG  PHE A 178    11282   9811   7880  -4040    502  -1329       C  
ATOM   1173  CD1 PHE A 178     -20.009 -37.376 -17.706  1.00 75.08           C  
ANISOU 1173  CD1 PHE A 178    11453   9176   7897  -4179    631  -1340       C  
ATOM   1174  CD2 PHE A 178     -22.234 -36.829 -18.377  1.00 79.18           C  
ANISOU 1174  CD2 PHE A 178    11389  10691   8004  -4243    436  -1597       C  
ATOM   1175  CE1 PHE A 178     -20.144 -38.631 -18.274  1.00 77.03           C  
ANISOU 1175  CE1 PHE A 178    11738   9425   8104  -4401    727  -1557       C  
ATOM   1176  CE2 PHE A 178     -22.372 -38.079 -18.946  1.00 81.32           C  
ANISOU 1176  CE2 PHE A 178    11716  10963   8217  -4615    508  -1909       C  
ATOM   1177  CZ  PHE A 178     -21.326 -38.981 -18.893  1.00 80.26           C  
ANISOU 1177  CZ  PHE A 178    11896  10306   8294  -4651    675  -1860       C  
ATOM   1178  N   CYS A 179     -19.278 -33.129 -15.260  1.00 68.97           N  
ANISOU 1178  N   CYS A 179    10450   8207   7550  -3114    496   -589       N  
ATOM   1179  CA  CYS A 179     -19.051 -31.727 -14.932  1.00 68.15           C  
ANISOU 1179  CA  CYS A 179    10249   8057   7587  -2774    495   -424       C  
ATOM   1180  C   CYS A 179     -19.642 -30.873 -16.047  1.00 70.43           C  
ANISOU 1180  C   CYS A 179    10341   8699   7720  -2515    469   -339       C  
ATOM   1181  O   CYS A 179     -19.976 -31.395 -17.108  1.00 72.55           O  
ANISOU 1181  O   CYS A 179    10577   9225   7764  -2580    432   -411       O  
ATOM   1182  CB  CYS A 179     -17.555 -31.462 -14.790  1.00 65.81           C  
ANISOU 1182  CB  CYS A 179    10161   7290   7555  -2624    559   -315       C  
ATOM   1183  SG  CYS A 179     -16.655 -32.794 -13.955  1.00175.41           S  
ANISOU 1183  SG  CYS A 179    24312  20795  21540  -2891    594   -382       S  
ATOM   1184  N   ASP A 180     -19.781 -29.571 -15.817  1.00 70.99           N  
ANISOU 1184  N   ASP A 180    10275   8798   7902  -2206    504   -192       N  
ATOM   1185  CA  ASP A 180     -20.385 -28.691 -16.819  1.00 73.90           C  
ANISOU 1185  CA  ASP A 180    10450   9511   8119  -1893    514    -51       C  
ATOM   1186  C   ASP A 180     -19.482 -28.492 -18.036  1.00 74.31           C  
ANISOU 1186  C   ASP A 180    10634   9421   8181  -1670    589     99       C  
ATOM   1187  O   ASP A 180     -18.321 -28.111 -17.905  1.00 71.46           O  
ANISOU 1187  O   ASP A 180    10442   8606   8104  -1557    699    200       O  
ATOM   1188  CB  ASP A 180     -20.751 -27.337 -16.213  1.00 75.24           C  
ANISOU 1188  CB  ASP A 180    10455   9683   8449  -1604    589     84       C  
ATOM   1189  CG  ASP A 180     -21.741 -26.567 -17.067  1.00 79.15           C  
ANISOU 1189  CG  ASP A 180    10698  10647   8729  -1293    594    234       C  
ATOM   1190  OD1 ASP A 180     -21.938 -26.929 -18.245  1.00 81.59           O  
ANISOU 1190  OD1 ASP A 180    10970  11265   8767  -1238    541    260       O  
ATOM   1191  OD2 ASP A 180     -22.326 -25.593 -16.558  1.00 80.27           O  
ANISOU 1191  OD2 ASP A 180    10670  10870   8958  -1084    658    323       O  
ATOM   1192  N   SER A 181     -20.043 -28.735 -19.218  1.00 69.43           N  
ANISOU 1192  N   SER A 181     8383   8320   9677  -1636  -2069   1183       N  
ATOM   1193  CA  SER A 181     -19.289 -28.701 -20.470  1.00 69.95           C  
ANISOU 1193  CA  SER A 181     8587   8302   9687  -1597  -2116   1217       C  
ATOM   1194  C   SER A 181     -18.798 -27.302 -20.834  1.00 70.17           C  
ANISOU 1194  C   SER A 181     8553   8244   9866  -1304  -2063   1323       C  
ATOM   1195  O   SER A 181     -17.737 -27.145 -21.441  1.00 68.61           O  
ANISOU 1195  O   SER A 181     8520   7855   9694  -1233  -2027   1324       O  
ATOM   1196  CB  SER A 181     -20.137 -29.268 -21.613  1.00 71.59           C  
ANISOU 1196  CB  SER A 181     8718   8790   9693  -1780  -2241   1240       C  
ATOM   1197  OG  SER A 181     -21.370 -28.581 -21.726  1.00 73.35           O  
ANISOU 1197  OG  SER A 181     8621   9350   9899  -1702  -2302   1338       O  
ATOM   1198  N   LYS A 182     -19.575 -26.289 -20.459  1.00 73.00           N  
ANISOU 1198  N   LYS A 182     8679   8725  10331  -1135  -2029   1412       N  
ATOM   1199  CA  LYS A 182     -19.245 -24.906 -20.789  1.00 74.85           C  
ANISOU 1199  CA  LYS A 182     8868   8841  10731   -851  -1926   1528       C  
ATOM   1200  C   LYS A 182     -18.066 -24.395 -19.962  1.00 73.09           C  
ANISOU 1200  C   LYS A 182     8762   8286  10722   -770  -1775   1396       C  
ATOM   1201  O   LYS A 182     -17.500 -23.345 -20.253  1.00 72.57           O  
ANISOU 1201  O   LYS A 182     8718   8032  10823   -591  -1642   1443       O  
ATOM   1202  CB  LYS A 182     -20.467 -23.998 -20.607  1.00 78.80           C  
ANISOU 1202  CB  LYS A 182     9095   9560  11284   -668  -1909   1663       C  
ATOM   1203  CG  LYS A 182     -21.662 -24.388 -21.465  1.00 83.13           C  
ANISOU 1203  CG  LYS A 182     9458  10524  11604   -719  -2071   1779       C  
ATOM   1204  CD  LYS A 182     -22.677 -23.254 -21.582  1.00 87.41           C  
ANISOU 1204  CD  LYS A 182     9737  11283  12193   -420  -2039   1971       C  
ATOM   1205  CE  LYS A 182     -22.094 -22.050 -22.317  1.00 88.93           C  
ANISOU 1205  CE  LYS A 182    10027  11263  12500    -92  -1901   2164       C  
ATOM   1206  NZ  LYS A 182     -23.084 -20.951 -22.528  1.00 91.89           N  
ANISOU 1206  NZ  LYS A 182    10176  11834  12903    261  -1846   2395       N  
ATOM   1207  N   LEU A 183     -17.699 -25.153 -18.936  1.00 72.34           N  
ANISOU 1207  N   LEU A 183     8739   8135  10612   -903  -1782   1225       N  
ATOM   1208  CA  LEU A 183     -16.586 -24.787 -18.068  1.00 71.46           C  
ANISOU 1208  CA  LEU A 183     8697   7801  10654   -835  -1670   1056       C  
ATOM   1209  C   LEU A 183     -15.300 -25.473 -18.518  1.00 69.53           C  
ANISOU 1209  C   LEU A 183     8667   7402  10348   -904  -1684    973       C  
ATOM   1210  O   LEU A 183     -14.214 -24.899 -18.435  1.00 68.95           O  
ANISOU 1210  O   LEU A 183     8631   7152  10414   -822  -1584    866       O  
ATOM   1211  CB  LEU A 183     -16.901 -25.156 -16.615  1.00 71.20           C  
ANISOU 1211  CB  LEU A 183     8603   7846  10602   -877  -1664    930       C  
ATOM   1212  CG  LEU A 183     -18.131 -24.497 -15.993  1.00 71.70           C  
ANISOU 1212  CG  LEU A 183     8442   8069  10731   -803  -1628    981       C  
ATOM   1213  CD1 LEU A 183     -18.402 -25.040 -14.601  1.00 71.13           C  
ANISOU 1213  CD1 LEU A 183     8341   8092  10593   -863  -1616    865       C  
ATOM   1214  CD2 LEU A 183     -17.947 -23.000 -15.941  1.00 71.95           C  
ANISOU 1214  CD2 LEU A 183     8375   7961  11003   -595  -1480    967       C  
ATOM   1215  N   MET A 184     -15.436 -26.705 -18.998  1.00 68.38           N  
ANISOU 1215  N   MET A 184     8654   7328  10000  -1063  -1792   1003       N  
ATOM   1216  CA  MET A 184     -14.291 -27.483 -19.453  1.00 66.20           C  
ANISOU 1216  CA  MET A 184     8594   6913   9645  -1114  -1801    933       C  
ATOM   1217  C   MET A 184     -13.575 -26.787 -20.606  1.00 65.04           C  
ANISOU 1217  C   MET A 184     8489   6655   9570  -1029  -1747    989       C  
ATOM   1218  O   MET A 184     -14.146 -25.932 -21.279  1.00 66.22           O  
ANISOU 1218  O   MET A 184     8537   6854   9769   -949  -1725   1132       O  
ATOM   1219  CB  MET A 184     -14.736 -28.876 -19.901  1.00 66.94           C  
ANISOU 1219  CB  MET A 184     8835   7080   9519  -1314  -1893    959       C  
ATOM   1220  CG  MET A 184     -15.671 -29.600 -18.942  1.00 67.65           C  
ANISOU 1220  CG  MET A 184     8891   7279   9532  -1440  -1910    943       C  
ATOM   1221  SD  MET A 184     -14.912 -30.042 -17.374  1.00127.45           S  
ANISOU 1221  SD  MET A 184    16563  14747  17115  -1351  -1833    824       S  
ATOM   1222  CE  MET A 184     -15.589 -28.773 -16.310  1.00131.44           C  
ANISOU 1222  CE  MET A 184    16784  15380  17776  -1221  -1792    808       C  
ATOM   1223  N   SER A 185     -12.317 -27.154 -20.818  1.00 62.96           N  
ANISOU 1223  N   SER A 185     8373   6248   9302  -1023  -1710    889       N  
ATOM   1224  CA  SER A 185     -11.552 -26.663 -21.957  1.00 61.84           C  
ANISOU 1224  CA  SER A 185     8296   5994   9205   -969  -1637    938       C  
ATOM   1225  C   SER A 185     -10.358 -27.572 -22.188  1.00 59.80           C  
ANISOU 1225  C   SER A 185     8218   5643   8860  -1005  -1636    823       C  
ATOM   1226  O   SER A 185      -9.957 -28.312 -21.300  1.00 58.88           O  
ANISOU 1226  O   SER A 185     8152   5523   8698  -1012  -1663    698       O  
ATOM   1227  CB  SER A 185     -11.096 -25.226 -21.727  1.00 62.42           C  
ANISOU 1227  CB  SER A 185     8245   5932   9539   -837  -1469    906       C  
ATOM   1228  OG  SER A 185     -10.586 -25.058 -20.420  1.00 62.14           O  
ANISOU 1228  OG  SER A 185     8123   5864   9624   -815  -1425    695       O  
ATOM   1229  N   ALA A 186      -9.802 -27.531 -23.390  1.00 59.32           N  
ANISOU 1229  N   ALA A 186     8259   5520   8758  -1000  -1595    880       N  
ATOM   1230  CA  ALA A 186      -8.665 -28.376 -23.724  1.00 58.24           C  
ANISOU 1230  CA  ALA A 186     8290   5301   8536  -1014  -1580    776       C  
ATOM   1231  C   ALA A 186      -7.913 -27.774 -24.895  1.00 58.27           C  
ANISOU 1231  C   ALA A 186     8334   5218   8586   -967  -1464    829       C  
ATOM   1232  O   ALA A 186      -8.474 -26.986 -25.650  1.00 58.82           O  
ANISOU 1232  O   ALA A 186     8362   5311   8675   -935  -1425    995       O  
ATOM   1233  CB  ALA A 186      -9.131 -29.776 -24.068  1.00 58.39           C  
ANISOU 1233  CB  ALA A 186     8491   5377   8316  -1142  -1693    794       C  
ATOM   1234  N   ALA A 187      -6.647 -28.152 -25.045  1.00 58.01           N  
ANISOU 1234  N   ALA A 187     8384   5100   8558   -939  -1396    703       N  
ATOM   1235  CA  ALA A 187      -5.847 -27.685 -26.176  1.00 58.88           C  
ANISOU 1235  CA  ALA A 187     8546   5127   8700   -908  -1260    744       C  
ATOM   1236  C   ALA A 187      -4.584 -28.514 -26.358  1.00 59.01           C  
ANISOU 1236  C   ALA A 187     8671   5101   8649   -889  -1225    597       C  
ATOM   1237  O   ALA A 187      -4.080 -29.102 -25.406  1.00 57.66           O  
ANISOU 1237  O   ALA A 187     8478   4950   8479   -847  -1267    441       O  
ATOM   1238  CB  ALA A 187      -5.486 -26.221 -26.007  1.00 59.32           C  
ANISOU 1238  CB  ALA A 187     8439   5070   9029   -851  -1072    736       C  
ATOM   1239  N   ILE A 188      -4.076 -28.551 -27.586  1.00 61.05           N  
ANISOU 1239  N   ILE A 188     9044   5321   8831   -889  -1140    658       N  
ATOM   1240  CA  ILE A 188      -2.824 -29.242 -27.875  1.00 62.62           C  
ANISOU 1240  CA  ILE A 188     9332   5484   8976   -848  -1077    522       C  
ATOM   1241  C   ILE A 188      -2.110 -28.620 -29.079  1.00 65.22           C  
ANISOU 1241  C   ILE A 188     9690   5752   9339   -835   -893    582       C  
ATOM   1242  O   ILE A 188      -2.718 -28.388 -30.121  1.00 65.89           O  
ANISOU 1242  O   ILE A 188     9872   5858   9306   -857   -882    769       O  
ATOM   1243  CB  ILE A 188      -3.045 -30.766 -28.074  1.00 47.92           C  
ANISOU 1243  CB  ILE A 188     7698   3650   6860   -879  -1204    503       C  
ATOM   1244  CG1 ILE A 188      -1.715 -31.483 -28.312  1.00 48.46           C  
ANISOU 1244  CG1 ILE A 188     7859   3674   6878   -787  -1120    367       C  
ATOM   1245  CG2 ILE A 188      -4.015 -31.039 -29.209  1.00 48.53           C  
ANISOU 1245  CG2 ILE A 188     7920   3784   6734   -986  -1272    652       C  
ATOM   1246  CD1 ILE A 188      -1.833 -32.989 -28.312  1.00 48.77           C  
ANISOU 1246  CD1 ILE A 188     8144   3678   6706   -788  -1196    328       C  
ATOM   1247  N   LYS A 189      -0.823 -28.329 -28.913  1.00 67.43           N  
ANISOU 1247  N   LYS A 189     9868   5985   9769   -791   -740    421       N  
ATOM   1248  CA  LYS A 189       0.002 -27.778 -29.986  1.00 70.80           C  
ANISOU 1248  CA  LYS A 189    10315   6341  10245   -790   -521    457       C  
ATOM   1249  C   LYS A 189       1.466 -27.864 -29.570  1.00 73.67           C  
ANISOU 1249  C   LYS A 189    10536   6720  10736   -753   -402    203       C  
ATOM   1250  O   LYS A 189       1.777 -27.780 -28.385  1.00 73.67           O  
ANISOU 1250  O   LYS A 189    10347   6781  10863   -730   -448     13       O  
ATOM   1251  CB  LYS A 189      -0.387 -26.324 -30.285  1.00 70.90           C  
ANISOU 1251  CB  LYS A 189    10246   6242  10451   -816   -343    610       C  
ATOM   1252  CG  LYS A 189       0.313 -25.706 -31.502  1.00 72.00           C  
ANISOU 1252  CG  LYS A 189    10452   6283  10622   -812    -74    713       C  
ATOM   1253  CD  LYS A 189      -0.284 -24.346 -31.864  1.00 72.68           C  
ANISOU 1253  CD  LYS A 189    10527   6227  10860   -795    116    941       C  
ATOM   1254  CE  LYS A 189       0.537 -23.632 -32.928  1.00 74.42           C  
ANISOU 1254  CE  LYS A 189    10812   6308  11156   -791    452   1040       C  
ATOM   1255  NZ  LYS A 189       0.763 -24.476 -34.126  1.00 74.75           N  
ANISOU 1255  NZ  LYS A 189    11049   6471  10881   -747    412   1139       N  
ATOM   1256  N   ASP A 190       2.352 -28.048 -30.546  1.00 77.01           N  
ANISOU 1256  N   ASP A 190    11032   7128  11101   -736   -254    191       N  
ATOM   1257  CA  ASP A 190       3.792 -28.106 -30.298  1.00 80.05           C  
ANISOU 1257  CA  ASP A 190    11248   7569  11598   -696   -121    -53       C  
ATOM   1258  C   ASP A 190       4.157 -29.104 -29.195  1.00 81.06           C  
ANISOU 1258  C   ASP A 190    11307   7846  11647   -573   -305   -245       C  
ATOM   1259  O   ASP A 190       4.956 -28.798 -28.306  1.00 81.01           O  
ANISOU 1259  O   ASP A 190    11033   7956  11791   -538   -271   -477       O  
ATOM   1260  CB  ASP A 190       4.343 -26.712 -29.975  1.00 82.09           C  
ANISOU 1260  CB  ASP A 190    11245   7760  12185   -796    114   -174       C  
ATOM   1261  CG  ASP A 190       4.000 -25.685 -31.039  1.00 84.34           C  
ANISOU 1261  CG  ASP A 190    11634   7857  12555   -877    349     58       C  
ATOM   1262  OD1 ASP A 190       3.786 -26.078 -32.205  1.00 85.20           O  
ANISOU 1262  OD1 ASP A 190    11972   7951  12448   -839    365    263       O  
ATOM   1263  OD2 ASP A 190       3.950 -24.482 -30.708  1.00 85.69           O  
ANISOU 1263  OD2 ASP A 190    11665   7894  12999   -968    534     34       O  
ATOM   1264  N   ASN A 191       3.548 -30.287 -29.263  1.00 82.59           N  
ANISOU 1264  N   ASN A 191    11742   8043  11595   -506   -484   -148       N  
ATOM   1265  CA  ASN A 191       3.803 -31.386 -28.327  1.00 84.19           C  
ANISOU 1265  CA  ASN A 191    11966   8341  11681   -349   -628   -261       C  
ATOM   1266  C   ASN A 191       3.539 -31.070 -26.851  1.00 84.74           C  
ANISOU 1266  C   ASN A 191    11829   8514  11854   -312   -742   -359       C  
ATOM   1267  O   ASN A 191       4.255 -31.538 -25.965  1.00 84.83           O  
ANISOU 1267  O   ASN A 191    11717   8681  11831   -140   -791   -516       O  
ATOM   1268  CB  ASN A 191       5.208 -31.963 -28.528  1.00 85.50           C  
ANISOU 1268  CB  ASN A 191    12082   8603  11800   -185   -531   -422       C  
ATOM   1269  CG  ASN A 191       5.420 -32.487 -29.933  1.00 85.49           C  
ANISOU 1269  CG  ASN A 191    12327   8505  11649   -198   -428   -333       C  
ATOM   1270  OD1 ASN A 191       4.474 -32.907 -30.600  1.00 84.54           O  
ANISOU 1270  OD1 ASN A 191    12473   8272  11375   -286   -491   -172       O  
ATOM   1271  ND2 ASN A 191       6.666 -32.463 -30.393  1.00 86.62           N  
ANISOU 1271  ND2 ASN A 191    12362   8724  11826   -116   -265   -462       N  
ATOM   1272  N   ARG A 192       2.505 -30.273 -26.600  1.00 85.33           N  
ANISOU 1272  N   ARG A 192    11861   8526  12033   -447   -780   -261       N  
ATOM   1273  CA  ARG A 192       2.072 -29.980 -25.240  1.00 86.08           C  
ANISOU 1273  CA  ARG A 192    11790   8712  12203   -426   -888   -339       C  
ATOM   1274  C   ARG A 192       0.555 -30.024 -25.159  1.00 82.91           C  
ANISOU 1274  C   ARG A 192    11533   8226  11741   -522  -1006   -137       C  
ATOM   1275  O   ARG A 192      -0.129 -29.218 -25.784  1.00 82.56           O  
ANISOU 1275  O   ARG A 192    11498   8089  11782   -643   -952     -3       O  
ATOM   1276  CB  ARG A 192       2.579 -28.610 -24.790  1.00 90.17           C  
ANISOU 1276  CB  ARG A 192    11990   9274  12996   -503   -755   -522       C  
ATOM   1277  CG  ARG A 192       4.089 -28.510 -24.686  1.00 94.67           C  
ANISOU 1277  CG  ARG A 192    12332   9996  13641   -436   -642   -786       C  
ATOM   1278  CD  ARG A 192       4.529 -27.122 -24.259  1.00 98.38           C  
ANISOU 1278  CD  ARG A 192    12485  10488  14408   -578   -478  -1011       C  
ATOM   1279  NE  ARG A 192       5.971 -26.947 -24.404  1.00102.48           N  
ANISOU 1279  NE  ARG A 192    12766  11155  15017   -573   -329  -1275       N  
ATOM   1280  CZ  ARG A 192       6.627 -25.830 -24.104  1.00105.91           C  
ANISOU 1280  CZ  ARG A 192    12893  11629  15720   -728   -142  -1549       C  
ATOM   1281  NH1 ARG A 192       5.970 -24.780 -23.634  1.00106.57           N  
ANISOU 1281  NH1 ARG A 192    12900  11581  16012   -883    -70  -1585       N  
ATOM   1282  NH2 ARG A 192       7.941 -25.765 -24.273  1.00108.47           N  
ANISOU 1282  NH2 ARG A 192    12978  12124  16110   -738     -8  -1805       N  
ATOM   1283  N   ALA A 193       0.033 -30.974 -24.391  1.00 80.72           N  
ANISOU 1283  N   ALA A 193    11367   7994  11311   -452  -1151   -107       N  
ATOM   1284  CA  ALA A 193      -1.408 -31.122 -24.246  1.00 78.02           C  
ANISOU 1284  CA  ALA A 193    11137   7603  10905   -560  -1258     58       C  
ATOM   1285  C   ALA A 193      -1.857 -30.598 -22.895  1.00 75.40           C  
ANISOU 1285  C   ALA A 193    10613   7366  10668   -536  -1319     -5       C  
ATOM   1286  O   ALA A 193      -1.166 -30.764 -21.897  1.00 75.71           O  
ANISOU 1286  O   ALA A 193    10531   7533  10701   -395  -1338   -159       O  
ATOM   1287  CB  ALA A 193      -1.816 -32.570 -24.413  1.00 78.47           C  
ANISOU 1287  CB  ALA A 193    11483   7600  10731   -551  -1331    140       C  
ATOM   1288  N   VAL A 194      -3.021 -29.960 -22.877  1.00 72.81           N  
ANISOU 1288  N   VAL A 194    10247   7010  10409   -654  -1349    111       N  
ATOM   1289  CA  VAL A 194      -3.572 -29.387 -21.661  1.00 70.63           C  
ANISOU 1289  CA  VAL A 194     9794   6816  10226   -643  -1390     57       C  
ATOM   1290  C   VAL A 194      -5.066 -29.645 -21.573  1.00 67.74           C  
ANISOU 1290  C   VAL A 194     9513   6444   9778   -740  -1485    233       C  
ATOM   1291  O   VAL A 194      -5.812 -29.354 -22.507  1.00 67.94           O  
ANISOU 1291  O   VAL A 194     9588   6422   9803   -841  -1484    383       O  
ATOM   1292  CB  VAL A 194      -3.339 -27.865 -21.601  1.00 71.77           C  
ANISOU 1292  CB  VAL A 194     9703   6932  10635   -680  -1263    -39       C  
ATOM   1293  CG1 VAL A 194      -4.107 -27.255 -20.444  1.00 72.00           C  
ANISOU 1293  CG1 VAL A 194     9575   7029  10753   -682  -1297    -88       C  
ATOM   1294  CG2 VAL A 194      -1.864 -27.552 -21.482  1.00 73.04           C  
ANISOU 1294  CG2 VAL A 194     9712   7140  10899   -623  -1157   -278       C  
ATOM   1295  N   HIS A 195      -5.491 -30.208 -20.449  1.00 65.19           N  
ANISOU 1295  N   HIS A 195     9197   6202   9369   -697  -1559    214       N  
ATOM   1296  CA  HIS A 195      -6.900 -30.274 -20.110  1.00 62.69           C  
ANISOU 1296  CA  HIS A 195     8887   5916   9016   -798  -1624    339       C  
ATOM   1297  C   HIS A 195      -7.150 -29.308 -18.962  1.00 61.24           C  
ANISOU 1297  C   HIS A 195     8469   5829   8972   -744  -1611    247       C  
ATOM   1298  O   HIS A 195      -6.554 -29.430 -17.898  1.00 61.30           O  
ANISOU 1298  O   HIS A 195     8402   5934   8953   -622  -1615    105       O  
ATOM   1299  CB  HIS A 195      -7.301 -31.696 -19.729  1.00 62.09           C  
ANISOU 1299  CB  HIS A 195     9029   5829   8734   -818  -1673    400       C  
ATOM   1300  CG  HIS A 195      -7.240 -32.659 -20.872  1.00 61.75           C  
ANISOU 1300  CG  HIS A 195     9232   5670   8559   -911  -1668    465       C  
ATOM   1301  ND1 HIS A 195      -6.053 -33.047 -21.454  1.00 61.76           N  
ANISOU 1301  ND1 HIS A 195     9345   5599   8523   -814  -1617    400       N  
ATOM   1302  CD2 HIS A 195      -8.221 -33.303 -21.548  1.00 62.18           C  
ANISOU 1302  CD2 HIS A 195     9429   5691   8507  -1104  -1699    557       C  
ATOM   1303  CE1 HIS A 195      -6.305 -33.893 -22.437  1.00 62.31           C  
ANISOU 1303  CE1 HIS A 195     9639   5569   8466   -934  -1611    456       C  
ATOM   1304  NE2 HIS A 195      -7.612 -34.065 -22.515  1.00 62.57           N  
ANISOU 1304  NE2 HIS A 195     9690   5629   8453  -1124  -1663    538       N  
ATOM   1305  N   ALA A 196      -8.025 -28.339 -19.189  1.00 60.48           N  
ANISOU 1305  N   ALA A 196     8251   5722   9007   -812  -1589    325       N  
ATOM   1306  CA  ALA A 196      -8.186 -27.230 -18.260  1.00 60.30           C  
ANISOU 1306  CA  ALA A 196     8007   5747   9158   -763  -1533    214       C  
ATOM   1307  C   ALA A 196      -9.617 -27.006 -17.804  1.00 60.18           C  
ANISOU 1307  C   ALA A 196     7922   5803   9142   -805  -1573    330       C  
ATOM   1308  O   ALA A 196     -10.572 -27.365 -18.485  1.00 60.57           O  
ANISOU 1308  O   ALA A 196     8042   5868   9105   -893  -1630    511       O  
ATOM   1309  CB  ALA A 196      -7.633 -25.958 -18.863  1.00 60.69           C  
ANISOU 1309  CB  ALA A 196     7945   5673   9441   -758  -1390    155       C  
ATOM   1310  N   ASP A 197      -9.735 -26.370 -16.649  1.00 60.25           N  
ANISOU 1310  N   ASP A 197     7766   5885   9242   -744  -1537    197       N  
ATOM   1311  CA  ASP A 197     -11.008 -26.133 -16.012  1.00 60.76           C  
ANISOU 1311  CA  ASP A 197     7737   6041   9308   -760  -1555    273       C  
ATOM   1312  C   ASP A 197     -10.849 -24.847 -15.227  1.00 61.33           C  
ANISOU 1312  C   ASP A 197     7608   6106   9589   -686  -1443     91       C  
ATOM   1313  O   ASP A 197      -9.807 -24.201 -15.299  1.00 62.12           O  
ANISOU 1313  O   ASP A 197     7648   6121   9833   -661  -1349    -87       O  
ATOM   1314  CB  ASP A 197     -11.312 -27.278 -15.056  1.00 61.63           C  
ANISOU 1314  CB  ASP A 197     7928   6283   9205   -762  -1634    277       C  
ATOM   1315  CG  ASP A 197     -12.784 -27.404 -14.744  1.00 63.15           C  
ANISOU 1315  CG  ASP A 197     8071   6572   9351   -837  -1659    415       C  
ATOM   1316  OD1 ASP A 197     -13.555 -26.478 -15.066  1.00 64.41           O  
ANISOU 1316  OD1 ASP A 197     8089   6737   9648   -843  -1627    480       O  
ATOM   1317  OD2 ASP A 197     -13.171 -28.434 -14.168  1.00 63.28           O  
ANISOU 1317  OD2 ASP A 197     8190   6658   9193   -881  -1690    464       O  
ATOM   1318  N   MET A 198     -11.873 -24.477 -14.471  1.00 61.52           N  
ANISOU 1318  N   MET A 198     7518   6219   9636   -667  -1433    112       N  
ATOM   1319  CA  MET A 198     -11.802 -23.299 -13.618  1.00 62.13           C  
ANISOU 1319  CA  MET A 198     7416   6288   9904   -602  -1310    -91       C  
ATOM   1320  C   MET A 198     -11.058 -23.622 -12.331  1.00 61.44           C  
ANISOU 1320  C   MET A 198     7267   6370   9706   -550  -1342   -352       C  
ATOM   1321  O   MET A 198     -10.650 -22.727 -11.595  1.00 62.00           O  
ANISOU 1321  O   MET A 198     7182   6464   9911   -516  -1245   -614       O  
ATOM   1322  CB  MET A 198     -13.206 -22.794 -13.283  1.00 63.22           C  
ANISOU 1322  CB  MET A 198     7450   6480  10092   -574  -1279     29       C  
ATOM   1323  CG  MET A 198     -13.971 -22.210 -14.454  1.00 63.78           C  
ANISOU 1323  CG  MET A 198     7523   6438  10275   -557  -1233    271       C  
ATOM   1324  SD  MET A 198     -13.268 -20.663 -15.042  1.00 84.10           S  
ANISOU 1324  SD  MET A 198    10066   8714  13175   -484   -994    192       S  
ATOM   1325  CE  MET A 198     -13.123 -19.768 -13.503  1.00 89.65           C  
ANISOU 1325  CE  MET A 198    10600   9420  14043   -445   -852   -148       C  
ATOM   1326  N   GLY A 199     -10.887 -24.911 -12.066  1.00 60.66           N  
ANISOU 1326  N   GLY A 199     7297   6400   9352   -534  -1464   -284       N  
ATOM   1327  CA  GLY A 199     -10.226 -25.351 -10.853  1.00 60.83           C  
ANISOU 1327  CA  GLY A 199     7278   6633   9202   -425  -1507   -475       C  
ATOM   1328  C   GLY A 199      -9.123 -26.353 -11.116  1.00 59.76           C  
ANISOU 1328  C   GLY A 199     7277   6531   8897   -362  -1580   -482       C  
ATOM   1329  O   GLY A 199      -8.327 -26.654 -10.227  1.00 60.39           O  
ANISOU 1329  O   GLY A 199     7303   6819   8826   -222  -1618   -654       O  
ATOM   1330  N   TYR A 200      -9.074 -26.879 -12.334  1.00 58.09           N  
ANISOU 1330  N   TYR A 200     7236   6145   8692   -440  -1600   -297       N  
ATOM   1331  CA  TYR A 200      -8.027 -27.825 -12.688  1.00 57.41           C  
ANISOU 1331  CA  TYR A 200     7293   6061   8461   -367  -1646   -297       C  
ATOM   1332  C   TYR A 200      -7.082 -27.217 -13.710  1.00 55.73           C  
ANISOU 1332  C   TYR A 200     7028   5720   8425   -414  -1591   -397       C  
ATOM   1333  O   TYR A 200      -7.440 -26.294 -14.434  1.00 54.75           O  
ANISOU 1333  O   TYR A 200     6848   5442   8514   -522  -1513   -364       O  
ATOM   1334  CB  TYR A 200      -8.613 -29.119 -13.264  1.00 58.24           C  
ANISOU 1334  CB  TYR A 200     7672   6060   8396   -426  -1688    -31       C  
ATOM   1335  CG  TYR A 200      -9.291 -30.052 -12.273  1.00 59.88           C  
ANISOU 1335  CG  TYR A 200     7996   6365   8391   -374  -1702     81       C  
ATOM   1336  CD1 TYR A 200      -9.691 -29.615 -11.020  1.00 61.17           C  
ANISOU 1336  CD1 TYR A 200     8009   6714   8521   -296  -1691     -4       C  
ATOM   1337  CD2 TYR A 200      -9.526 -31.381 -12.601  1.00 60.58           C  
ANISOU 1337  CD2 TYR A 200     8363   6341   8313   -410  -1695    267       C  
ATOM   1338  CE1 TYR A 200     -10.312 -30.473 -10.127  1.00 62.38           C  
ANISOU 1338  CE1 TYR A 200     8285   6950   8468   -244  -1672    123       C  
ATOM   1339  CE2 TYR A 200     -10.143 -32.244 -11.713  1.00 61.84           C  
ANISOU 1339  CE2 TYR A 200     8659   6545   8293   -376  -1654    386       C  
ATOM   1340  CZ  TYR A 200     -10.534 -31.785 -10.479  1.00 62.56           C  
ANISOU 1340  CZ  TYR A 200     8596   6833   8343   -287  -1643    328       C  
ATOM   1341  OH  TYR A 200     -11.148 -32.642  -9.594  1.00 63.70           O  
ANISOU 1341  OH  TYR A 200     8889   7018   8298   -247  -1573    468       O  
ATOM   1342  N   TRP A 201      -5.865 -27.740 -13.757  1.00 55.76           N  
ANISOU 1342  N   TRP A 201     7054   5797   8335   -309  -1613   -507       N  
ATOM   1343  CA  TRP A 201      -4.958 -27.431 -14.854  1.00 55.41           C  
ANISOU 1343  CA  TRP A 201     7004   5627   8424   -361  -1550   -564       C  
ATOM   1344  C   TRP A 201      -4.001 -28.595 -15.072  1.00 55.79           C  
ANISOU 1344  C   TRP A 201     7189   5735   8272   -226  -1602   -549       C  
ATOM   1345  O   TRP A 201      -3.000 -28.733 -14.375  1.00 56.85           O  
ANISOU 1345  O   TRP A 201     7191   6089   8319    -65  -1628   -749       O  
ATOM   1346  CB  TRP A 201      -4.191 -26.132 -14.605  1.00 55.58           C  
ANISOU 1346  CB  TRP A 201     6750   5692   8678   -399  -1441   -869       C  
ATOM   1347  CG  TRP A 201      -3.284 -25.773 -15.736  1.00 54.75           C  
ANISOU 1347  CG  TRP A 201     6637   5440   8724   -474  -1333   -919       C  
ATOM   1348  CD1 TRP A 201      -1.962 -26.078 -15.848  1.00 55.24           C  
ANISOU 1348  CD1 TRP A 201     6622   5625   8743   -405  -1326  -1098       C  
ATOM   1349  CD2 TRP A 201      -3.634 -25.056 -16.926  1.00 53.66           C  
ANISOU 1349  CD2 TRP A 201     6571   5030   8787   -611  -1203   -771       C  
ATOM   1350  NE1 TRP A 201      -1.466 -25.588 -17.028  1.00 54.97           N  
ANISOU 1350  NE1 TRP A 201     6607   5392   8886   -520  -1186  -1083       N  
ATOM   1351  CE2 TRP A 201      -2.473 -24.957 -17.709  1.00 53.97           C  
ANISOU 1351  CE2 TRP A 201     6587   5017   8903   -639  -1105   -871       C  
ATOM   1352  CE3 TRP A 201      -4.815 -24.485 -17.399  1.00 53.00           C  
ANISOU 1352  CE3 TRP A 201     6559   4771   8809   -684  -1154   -554       C  
ATOM   1353  CZ2 TRP A 201      -2.458 -24.310 -18.942  1.00 53.97           C  
ANISOU 1353  CZ2 TRP A 201     6662   4771   9074   -743   -944   -746       C  
ATOM   1354  CZ3 TRP A 201      -4.798 -23.845 -18.623  1.00 53.11           C  
ANISOU 1354  CZ3 TRP A 201     6640   4564   8977   -756  -1012   -421       C  
ATOM   1355  CH2 TRP A 201      -3.630 -23.762 -19.380  1.00 53.64           C  
ANISOU 1355  CH2 TRP A 201     6710   4560   9111   -787   -901   -510       C  
ATOM   1356  N   ILE A 202      -4.323 -29.428 -16.054  1.00 55.34           N  
ANISOU 1356  N   ILE A 202     7389   5502   8134   -280  -1614   -322       N  
ATOM   1357  CA  ILE A 202      -3.611 -30.676 -16.275  1.00 56.15           C  
ANISOU 1357  CA  ILE A 202     7688   5608   8037   -142  -1640   -268       C  
ATOM   1358  C   ILE A 202      -2.768 -30.620 -17.540  1.00 56.85           C  
ANISOU 1358  C   ILE A 202     7818   5579   8204   -184  -1578   -292       C  
ATOM   1359  O   ILE A 202      -3.272 -30.336 -18.619  1.00 56.10           O  
ANISOU 1359  O   ILE A 202     7808   5307   8199   -352  -1540   -172       O  
ATOM   1360  CB  ILE A 202      -4.597 -31.833 -16.374  1.00 56.00           C  
ANISOU 1360  CB  ILE A 202     7967   5461   7850   -185  -1666    -25       C  
ATOM   1361  CG1 ILE A 202      -5.640 -31.711 -15.266  1.00 41.43           C  
ANISOU 1361  CG1 ILE A 202     6067   3709   5966   -201  -1696     23       C  
ATOM   1362  CG2 ILE A 202      -3.870 -33.156 -16.284  1.00 57.40           C  
ANISOU 1362  CG2 ILE A 202     8370   5626   7815     11  -1656     25       C  
ATOM   1363  CD1 ILE A 202      -6.839 -32.588 -15.465  1.00 41.39           C  
ANISOU 1363  CD1 ILE A 202     6300   3563   5862   -342  -1689    240       C  
ATOM   1364  N   GLU A 203      -1.479 -30.902 -17.400  1.00 58.71           N  
ANISOU 1364  N   GLU A 203     7979   5948   8379    -10  -1567   -445       N  
ATOM   1365  CA  GLU A 203      -0.560 -30.810 -18.523  1.00 59.67           C  
ANISOU 1365  CA  GLU A 203     8105   5991   8577    -38  -1487   -496       C  
ATOM   1366  C   GLU A 203       0.188 -32.104 -18.784  1.00 61.24           C  
ANISOU 1366  C   GLU A 203     8503   6197   8569    160  -1494   -445       C  
ATOM   1367  O   GLU A 203       0.703 -32.736 -17.864  1.00 62.70           O  
ANISOU 1367  O   GLU A 203     8664   6571   8587    409  -1544   -497       O  
ATOM   1368  CB  GLU A 203       0.457 -29.697 -18.295  1.00 60.77           C  
ANISOU 1368  CB  GLU A 203     7900   6287   8901    -47  -1414   -787       C  
ATOM   1369  CG  GLU A 203      -0.136 -28.319 -18.200  1.00 61.05           C  
ANISOU 1369  CG  GLU A 203     7764   6245   9189   -246  -1340   -856       C  
ATOM   1370  CD  GLU A 203       0.898 -27.246 -18.435  1.00 63.34           C  
ANISOU 1370  CD  GLU A 203     7786   6568   9711   -336  -1189  -1126       C  
ATOM   1371  OE1 GLU A 203       0.700 -26.108 -17.963  1.00 64.37           O  
ANISOU 1371  OE1 GLU A 203     7719   6689  10049   -457  -1105  -1288       O  
ATOM   1372  OE2 GLU A 203       1.909 -27.543 -19.103  1.00 64.44           O  
ANISOU 1372  OE2 GLU A 203     7916   6731   9836   -298  -1130  -1187       O  
ATOM   1373  N   SER A 204       0.251 -32.474 -20.056  1.00 61.77           N  
ANISOU 1373  N   SER A 204     8769   6067   8635     71  -1433   -339       N  
ATOM   1374  CA  SER A 204       1.073 -33.579 -20.509  1.00 64.35           C  
ANISOU 1374  CA  SER A 204     9284   6364   8804    248  -1399   -316       C  
ATOM   1375  C   SER A 204       1.935 -33.085 -21.664  1.00 66.31           C  
ANISOU 1375  C   SER A 204     9450   6576   9168    178  -1294   -406       C  
ATOM   1376  O   SER A 204       1.647 -32.046 -22.253  1.00 65.66           O  
ANISOU 1376  O   SER A 204     9260   6423   9266    -32  -1240   -413       O  
ATOM   1377  CB  SER A 204       0.199 -34.743 -20.960  1.00 64.16           C  
ANISOU 1377  CB  SER A 204     9649   6102   8626    191  -1399   -102       C  
ATOM   1378  OG  SER A 204      -0.722 -34.330 -21.947  1.00 63.14           O  
ANISOU 1378  OG  SER A 204     9598   5816   8578    -92  -1393     -6       O  
ATOM   1379  N   ALA A 205       2.992 -33.822 -21.981  1.00 69.39           N  
ANISOU 1379  N   ALA A 205     9898   7014   9453    373  -1245   -460       N  
ATOM   1380  CA  ALA A 205       3.904 -33.418 -23.041  1.00 71.92           C  
ANISOU 1380  CA  ALA A 205    10131   7325   9870    323  -1123   -555       C  
ATOM   1381  C   ALA A 205       4.475 -34.624 -23.777  1.00 75.16           C  
ANISOU 1381  C   ALA A 205    10806   7644  10107    485  -1064   -495       C  
ATOM   1382  O   ALA A 205       4.209 -35.770 -23.415  1.00 75.46           O  
ANISOU 1382  O   ALA A 205    11101   7605   9964    646  -1102   -387       O  
ATOM   1383  CB  ALA A 205       5.022 -32.564 -22.473  1.00 73.12           C  
ANISOU 1383  CB  ALA A 205     9871   7756  10156    394  -1086   -825       C  
ATOM   1384  N   LEU A 206       5.267 -34.356 -24.809  1.00 78.03           N  
ANISOU 1384  N   LEU A 206    11120   7995  10532    444   -940   -565       N  
ATOM   1385  CA  LEU A 206       5.901 -35.416 -25.583  1.00 81.06           C  
ANISOU 1385  CA  LEU A 206    11736   8299  10763    602   -858   -537       C  
ATOM   1386  C   LEU A 206       7.413 -35.396 -25.415  1.00 85.81           C  
ANISOU 1386  C   LEU A 206    12069   9158  11378    844   -785   -736       C  
ATOM   1387  O   LEU A 206       8.119 -34.698 -26.142  1.00 86.20           O  
ANISOU 1387  O   LEU A 206    11934   9266  11554    742   -662   -849       O  
ATOM   1388  CB  LEU A 206       5.541 -35.294 -27.067  1.00 79.26           C  
ANISOU 1388  CB  LEU A 206    11711   7864  10540    373   -763   -444       C  
ATOM   1389  CG  LEU A 206       6.119 -36.343 -28.024  1.00 79.14           C  
ANISOU 1389  CG  LEU A 206    11962   7743  10365    495   -656   -434       C  
ATOM   1390  CD1 LEU A 206       5.636 -37.723 -27.657  1.00 79.06           C  
ANISOU 1390  CD1 LEU A 206    12298   7571  10169    631   -699   -343       C  
ATOM   1391  CD2 LEU A 206       5.764 -36.030 -29.467  1.00 78.22           C  
ANISOU 1391  CD2 LEU A 206    11992   7492  10236    260   -570   -363       C  
ATOM   1392  N   ASN A 207       7.899 -36.150 -24.435  1.00 90.31           N  
ANISOU 1392  N   ASN A 207    12603   9903  11805   1177   -851   -772       N  
ATOM   1393  CA  ASN A 207       9.322 -36.425 -24.314  1.00 95.84           C  
ANISOU 1393  CA  ASN A 207    13081  10884  12450   1485   -795   -939       C  
ATOM   1394  C   ASN A 207       9.503 -37.921 -24.493  1.00 94.41           C  
ANISOU 1394  C   ASN A 207    13272  10559  12041   1803   -748   -795       C  
ATOM   1395  O   ASN A 207       9.250 -38.691 -23.568  1.00 95.53           O  
ANISOU 1395  O   ASN A 207    13557  10714  12027   2060   -818   -688       O  
ATOM   1396  CB  ASN A 207       9.854 -35.971 -22.955  1.00102.97           C  
ANISOU 1396  CB  ASN A 207    13571  12201  13352   1669   -908  -1124       C  
ATOM   1397  CG  ASN A 207      11.341 -36.221 -22.796  1.00111.97           C  
ANISOU 1397  CG  ASN A 207    14408  13721  14414   2003   -868  -1324       C  
ATOM   1398  OD1 ASN A 207      12.160 -35.642 -23.509  1.00112.96           O  
ANISOU 1398  OD1 ASN A 207    14292  13948  14678   1883   -747  -1502       O  
ATOM   1399  ND2 ASN A 207      11.699 -37.071 -21.838  1.00119.59           N  
ANISOU 1399  ND2 ASN A 207    15371  14920  15148   2439   -959  -1288       N  
ATOM   1400  N   ASP A 208       9.908 -38.315 -25.700  1.00 91.76           N  
ANISOU 1400  N   ASP A 208    13117  10061  11687   1781   -604   -785       N  
ATOM   1401  CA  ASP A 208       9.950 -39.718 -26.136  1.00 90.07           C  
ANISOU 1401  CA  ASP A 208    13334   9603  11286   2009   -509   -657       C  
ATOM   1402  C   ASP A 208       8.558 -40.335 -26.297  1.00 85.31           C  
ANISOU 1402  C   ASP A 208    13183   8609  10623   1799   -527   -465       C  
ATOM   1403  O   ASP A 208       8.316 -41.093 -27.235  1.00 85.42           O  
ANISOU 1403  O   ASP A 208    13561   8335  10560   1730   -414   -409       O  
ATOM   1404  CB  ASP A 208      10.826 -40.584 -25.221  1.00 93.29           C  
ANISOU 1404  CB  ASP A 208    13699  10221  11526   2538   -508   -659       C  
ATOM   1405  CG  ASP A 208      12.290 -40.206 -25.285  1.00 95.97           C  
ANISOU 1405  CG  ASP A 208    13609  10967  11889   2769   -464   -873       C  
ATOM   1406  OD1 ASP A 208      12.771 -39.858 -26.382  1.00 96.22           O  
ANISOU 1406  OD1 ASP A 208    13576  10968  12013   2603   -341   -973       O  
ATOM   1407  OD2 ASP A 208      12.961 -40.261 -24.233  1.00 98.15           O  
ANISOU 1407  OD2 ASP A 208    13596  11623  12074   3121   -549   -948       O  
ATOM   1408  N   THR A 209       7.652 -40.009 -25.380  1.00 80.81           N  
ANISOU 1408  N   THR A 209    12572   8049  10085   1686   -660   -391       N  
ATOM   1409  CA  THR A 209       6.266 -40.455 -25.467  1.00 76.55           C  
ANISOU 1409  CA  THR A 209    12384   7190   9512   1436   -681   -236       C  
ATOM   1410  C   THR A 209       5.336 -39.484 -24.740  1.00 72.32           C  
ANISOU 1410  C   THR A 209    11634   6754   9090   1198   -833   -212       C  
ATOM   1411  O   THR A 209       5.785 -38.686 -23.918  1.00 72.34           O  
ANISOU 1411  O   THR A 209    11271   7050   9167   1295   -915   -308       O  
ATOM   1412  CB  THR A 209       6.085 -41.862 -24.886  1.00 77.36           C  
ANISOU 1412  CB  THR A 209    12870   7080   9445   1703   -603   -101       C  
ATOM   1413  OG1 THR A 209       4.836 -42.406 -25.330  1.00 76.75           O  
ANISOU 1413  OG1 THR A 209    13164   6651   9347   1389   -564     -5       O  
ATOM   1414  CG2 THR A 209       6.110 -41.820 -23.364  1.00 77.11           C  
ANISOU 1414  CG2 THR A 209    12677   7262   9358   1969   -699    -41       C  
ATOM   1415  N   TRP A 210       4.045 -39.549 -25.055  1.00 69.03           N  
ANISOU 1415  N   TRP A 210    11431   6114   8683    885   -862   -108       N  
ATOM   1416  CA  TRP A 210       3.048 -38.693 -24.414  1.00 65.47           C  
ANISOU 1416  CA  TRP A 210    10805   5736   8333    668   -991    -68       C  
ATOM   1417  C   TRP A 210       2.700 -39.170 -23.015  1.00 65.65           C  
ANISOU 1417  C   TRP A 210    10869   5800   8277    851  -1040     12       C  
ATOM   1418  O   TRP A 210       2.176 -40.270 -22.838  1.00 66.99           O  
ANISOU 1418  O   TRP A 210    11386   5740   8326    888   -973    132       O  
ATOM   1419  CB  TRP A 210       1.769 -38.637 -25.243  1.00 63.34           C  
ANISOU 1419  CB  TRP A 210    10718   5272   8077    295  -1010     13       C  
ATOM   1420  CG  TRP A 210       1.894 -37.784 -26.443  1.00 61.78           C  
ANISOU 1420  CG  TRP A 210    10402   5111   7959    103   -993    -31       C  
ATOM   1421  CD1 TRP A 210       2.230 -38.181 -27.698  1.00 62.32           C  
ANISOU 1421  CD1 TRP A 210    10650   5079   7948     53   -897    -57       C  
ATOM   1422  CD2 TRP A 210       1.691 -36.371 -26.506  1.00 59.81           C  
ANISOU 1422  CD2 TRP A 210     9847   5001   7876    -46  -1043    -44       C  
ATOM   1423  NE1 TRP A 210       2.250 -37.101 -28.543  1.00 61.18           N  
ANISOU 1423  NE1 TRP A 210    10330   5022   7893   -106   -890    -62       N  
ATOM   1424  CE2 TRP A 210       1.922 -35.976 -27.832  1.00 59.68           C  
ANISOU 1424  CE2 TRP A 210     9852   4958   7867   -166   -966    -46       C  
ATOM   1425  CE3 TRP A 210       1.340 -35.402 -25.565  1.00 58.51           C  
ANISOU 1425  CE3 TRP A 210     9410   4968   7854    -79  -1123    -54       C  
ATOM   1426  CZ2 TRP A 210       1.808 -34.650 -28.243  1.00 58.69           C  
ANISOU 1426  CZ2 TRP A 210     9503   4905   7890   -302   -947    -25       C  
ATOM   1427  CZ3 TRP A 210       1.228 -34.090 -25.972  1.00 57.37           C  
ANISOU 1427  CZ3 TRP A 210     9043   4878   7876   -229  -1103    -62       C  
ATOM   1428  CH2 TRP A 210       1.460 -33.725 -27.297  1.00 57.56           C  
ANISOU 1428  CH2 TRP A 210     9113   4847   7910   -331  -1006    -32       C  
ATOM   1429  N   LYS A 211       2.976 -38.328 -22.027  1.00 64.63           N  
ANISOU 1429  N   LYS A 211    10390   5954   8211    952  -1137    -65       N  
ATOM   1430  CA  LYS A 211       2.706 -38.668 -20.639  1.00 64.73           C  
ANISOU 1430  CA  LYS A 211    10403   6073   8119   1156  -1190      5       C  
ATOM   1431  C   LYS A 211       2.385 -37.419 -19.840  1.00 63.08           C  
ANISOU 1431  C   LYS A 211     9822   6112   8033   1043  -1313    -93       C  
ATOM   1432  O   LYS A 211       2.852 -36.332 -20.162  1.00 62.00           O  
ANISOU 1432  O   LYS A 211     9374   6125   8056    929  -1335   -258       O  
ATOM   1433  CB  LYS A 211       3.901 -39.401 -20.026  1.00 67.07           C  
ANISOU 1433  CB  LYS A 211    10691   6546   8246   1631  -1151    -12       C  
ATOM   1434  CG  LYS A 211       5.232 -38.694 -20.231  1.00 67.63           C  
ANISOU 1434  CG  LYS A 211    10375   6939   8380   1771  -1174   -235       C  
ATOM   1435  CD  LYS A 211       6.402 -39.603 -19.877  1.00 70.55           C  
ANISOU 1435  CD  LYS A 211    10773   7478   8555   2267  -1121   -233       C  
ATOM   1436  CE  LYS A 211       7.733 -38.910 -20.135  1.00 71.55           C  
ANISOU 1436  CE  LYS A 211    10472   7964   8750   2375  -1136   -488       C  
ATOM   1437  NZ  LYS A 211       8.897 -39.825 -19.971  1.00 74.56           N  
ANISOU 1437  NZ  LYS A 211    10868   8528   8934   2877  -1076   -485       N  
ATOM   1438  N   ILE A 212       1.577 -37.581 -18.799  1.00 62.96           N  
ANISOU 1438  N   ILE A 212     9855   6119   7948   1066  -1362      5       N  
ATOM   1439  CA  ILE A 212       1.221 -36.470 -17.925  1.00 61.49           C  
ANISOU 1439  CA  ILE A 212     9340   6166   7858    982  -1466    -97       C  
ATOM   1440  C   ILE A 212       2.470 -35.833 -17.323  1.00 61.88           C  
ANISOU 1440  C   ILE A 212     9000   6601   7909   1212  -1517   -334       C  
ATOM   1441  O   ILE A 212       3.445 -36.522 -17.024  1.00 63.97           O  
ANISOU 1441  O   ILE A 212     9268   7032   8006   1560  -1505   -356       O  
ATOM   1442  CB  ILE A 212       0.252 -36.934 -16.811  1.00 61.69           C  
ANISOU 1442  CB  ILE A 212     9504   6179   7757   1032  -1489     56       C  
ATOM   1443  CG1 ILE A 212      -0.280 -35.746 -16.011  1.00 60.83           C  
ANISOU 1443  CG1 ILE A 212     9076   6277   7759    902  -1582    -55       C  
ATOM   1444  CG2 ILE A 212       0.919 -37.934 -15.895  1.00 63.83           C  
ANISOU 1444  CG2 ILE A 212     9896   6582   7776   1467  -1459    133       C  
ATOM   1445  CD1 ILE A 212      -1.291 -36.138 -14.960  1.00 61.30           C  
ANISOU 1445  CD1 ILE A 212     9261   6334   7698    927  -1590     94       C  
ATOM   1446  N   GLU A 213       2.446 -34.514 -17.176  1.00 60.61           N  
ANISOU 1446  N   GLU A 213     8498   6589   7942   1018  -1559   -525       N  
ATOM   1447  CA  GLU A 213       3.580 -33.789 -16.617  1.00 62.20           C  
ANISOU 1447  CA  GLU A 213     8284   7172   8176   1154  -1593   -820       C  
ATOM   1448  C   GLU A 213       3.212 -33.051 -15.340  1.00 62.07           C  
ANISOU 1448  C   GLU A 213     8008   7415   8160   1151  -1681   -961       C  
ATOM   1449  O   GLU A 213       3.839 -33.241 -14.304  1.00 64.30           O  
ANISOU 1449  O   GLU A 213     8103   8072   8256   1441  -1758  -1087       O  
ATOM   1450  CB  GLU A 213       4.156 -32.801 -17.635  1.00 62.28           C  
ANISOU 1450  CB  GLU A 213     8089   7131   8445    911  -1504  -1001       C  
ATOM   1451  CG  GLU A 213       5.086 -33.424 -18.667  1.00 63.42           C  
ANISOU 1451  CG  GLU A 213     8337   7209   8551   1014  -1418   -985       C  
ATOM   1452  CD  GLU A 213       6.402 -33.882 -18.073  1.00 66.05           C  
ANISOU 1452  CD  GLU A 213     8451   7928   8717   1383  -1451  -1155       C  
ATOM   1453  OE1 GLU A 213       6.777 -33.375 -16.995  1.00 67.22           O  
ANISOU 1453  OE1 GLU A 213     8258   8451   8832   1488  -1536  -1374       O  
ATOM   1454  OE2 GLU A 213       7.062 -34.746 -18.687  1.00 67.03           O  
ANISOU 1454  OE2 GLU A 213     8731   8005   8730   1580  -1392  -1083       O  
ATOM   1455  N   LYS A 214       2.199 -32.199 -15.416  1.00 60.00           N  
ANISOU 1455  N   LYS A 214     7728   6980   8090    846  -1668   -944       N  
ATOM   1456  CA  LYS A 214       1.837 -31.386 -14.264  1.00 60.37           C  
ANISOU 1456  CA  LYS A 214     7522   7251   8165    816  -1727  -1110       C  
ATOM   1457  C   LYS A 214       0.341 -31.387 -14.003  1.00 58.66           C  
ANISOU 1457  C   LYS A 214     7503   6824   7961    667  -1739   -892       C  
ATOM   1458  O   LYS A 214      -0.445 -31.779 -14.854  1.00 57.13           O  
ANISOU 1458  O   LYS A 214     7586   6310   7810    512  -1699   -653       O  
ATOM   1459  CB  LYS A 214       2.360 -29.955 -14.423  1.00 60.99           C  
ANISOU 1459  CB  LYS A 214     7234   7416   8523    598  -1660  -1439       C  
ATOM   1460  CG  LYS A 214       3.870 -29.829 -14.240  1.00 63.63           C  
ANISOU 1460  CG  LYS A 214     7244   8110   8823    749  -1663  -1757       C  
ATOM   1461  CD  LYS A 214       4.360 -28.397 -14.430  1.00 64.64           C  
ANISOU 1461  CD  LYS A 214     7023   8273   9266    468  -1544  -2110       C  
ATOM   1462  CE  LYS A 214       4.053 -27.879 -15.826  1.00 63.17           C  
ANISOU 1462  CE  LYS A 214     7001   7644   9355    182  -1375  -1967       C  
ATOM   1463  NZ  LYS A 214       4.562 -26.495 -16.043  1.00 64.17           N  
ANISOU 1463  NZ  LYS A 214     6831   7743   9809    -89  -1196  -2286       N  
ATOM   1464  N   ALA A 215      -0.040 -30.962 -12.806  1.00 59.27           N  
ANISOU 1464  N   ALA A 215     7415   7122   7983    715  -1794   -996       N  
ATOM   1465  CA  ALA A 215      -1.444 -30.891 -12.432  1.00 46.16           C  
ANISOU 1465  CA  ALA A 215     5888   5315   6335    584  -1796   -819       C  
ATOM   1466  C   ALA A 215      -1.617 -29.825 -11.365  1.00 55.68           C  
ANISOU 1466  C   ALA A 215     6787   6764   7605    553  -1818  -1069       C  
ATOM   1467  O   ALA A 215      -0.841 -29.759 -10.420  1.00 57.32           O  
ANISOU 1467  O   ALA A 215     6773   7343   7663    756  -1879  -1296       O  
ATOM   1468  CB  ALA A 215      -1.928 -32.231 -11.929  1.00 46.68           C  
ANISOU 1468  CB  ALA A 215     6260   5356   6120    778  -1817   -546       C  
ATOM   1469  N   SER A 216      -2.628 -28.981 -11.528  1.00 54.89           N  
ANISOU 1469  N   SER A 216     6661   6476   7717    311  -1766  -1042       N  
ATOM   1470  CA  SER A 216      -2.886 -27.913 -10.575  1.00 56.26           C  
ANISOU 1470  CA  SER A 216     6569   6825   7983    260  -1754  -1288       C  
ATOM   1471  C   SER A 216      -4.327 -27.995 -10.114  1.00 55.75           C  
ANISOU 1471  C   SER A 216     6634   6668   7881    204  -1754  -1078       C  
ATOM   1472  O   SER A 216      -5.228 -28.200 -10.927  1.00 54.88           O  
ANISOU 1472  O   SER A 216     6720   6275   7856     56  -1722   -818       O  
ATOM   1473  CB  SER A 216      -2.619 -26.555 -11.213  1.00 56.43           C  
ANISOU 1473  CB  SER A 216     6392   6693   8356     27  -1632  -1509       C  
ATOM   1474  OG  SER A 216      -1.267 -26.433 -11.603  1.00 57.69           O  
ANISOU 1474  OG  SER A 216     6398   6958   8565     48  -1606  -1736       O  
ATOM   1475  N   PHE A 217      -4.541 -27.835  -8.812  1.00 56.76           N  
ANISOU 1475  N   PHE A 217     6629   7070   7865    321  -1789  -1206       N  
ATOM   1476  CA  PHE A 217      -5.867 -28.008  -8.237  1.00 56.63           C  
ANISOU 1476  CA  PHE A 217     6723   7016   7778    294  -1778  -1012       C  
ATOM   1477  C   PHE A 217      -6.209 -26.911  -7.232  1.00 57.90           C  
ANISOU 1477  C   PHE A 217     6626   7362   8013    266  -1746  -1275       C  
ATOM   1478  O   PHE A 217      -5.439 -26.636  -6.319  1.00 59.45           O  
ANISOU 1478  O   PHE A 217     6610   7894   8085    404  -1787  -1572       O  
ATOM   1479  CB  PHE A 217      -5.963 -29.371  -7.548  1.00 58.27           C  
ANISOU 1479  CB  PHE A 217     7147   7362   7630    525  -1826   -792       C  
ATOM   1480  CG  PHE A 217      -5.963 -30.540  -8.493  1.00 58.30           C  
ANISOU 1480  CG  PHE A 217     7472   7107   7572    519  -1813   -497       C  
ATOM   1481  CD1 PHE A 217      -7.156 -31.122  -8.887  1.00 57.89           C  
ANISOU 1481  CD1 PHE A 217     7661   6803   7533    360  -1760   -212       C  
ATOM   1482  CD2 PHE A 217      -4.772 -31.074  -8.967  1.00 59.25           C  
ANISOU 1482  CD2 PHE A 217     7640   7255   7617    668  -1842   -533       C  
ATOM   1483  CE1 PHE A 217      -7.168 -32.203  -9.748  1.00 57.73           C  
ANISOU 1483  CE1 PHE A 217     7937   6540   7458    322  -1729     10       C  
ATOM   1484  CE2 PHE A 217      -4.775 -32.157  -9.831  1.00 58.87           C  
ANISOU 1484  CE2 PHE A 217     7905   6949   7514    664  -1807   -285       C  
ATOM   1485  CZ  PHE A 217      -5.974 -32.721 -10.222  1.00 58.23           C  
ANISOU 1485  CZ  PHE A 217     8077   6596   7451    479  -1747    -24       C  
ATOM   1486  N   ILE A 218      -7.368 -26.285  -7.414  1.00 57.63           N  
ANISOU 1486  N   ILE A 218     6598   7129   8169     98  -1671  -1181       N  
ATOM   1487  CA  ILE A 218      -7.906 -25.343  -6.437  1.00 59.77           C  
ANISOU 1487  CA  ILE A 218     6672   7538   8501     83  -1616  -1388       C  
ATOM   1488  C   ILE A 218      -9.018 -26.077  -5.704  1.00 61.01           C  
ANISOU 1488  C   ILE A 218     6965   7782   8434    156  -1632  -1140       C  
ATOM   1489  O   ILE A 218      -9.390 -25.742  -4.573  1.00 62.55           O  
ANISOU 1489  O   ILE A 218     7039   8205   8524    233  -1613  -1276       O  
ATOM   1490  CB  ILE A 218      -8.491 -24.093  -7.122  1.00 58.88           C  
ANISOU 1490  CB  ILE A 218     6475   7134   8762   -117  -1484  -1432       C  
ATOM   1491  CG1 ILE A 218      -7.440 -23.421  -8.001  1.00 58.75           C  
ANISOU 1491  CG1 ILE A 218     6374   6959   8988   -218  -1416  -1621       C  
ATOM   1492  CG2 ILE A 218      -9.024 -23.105  -6.095  1.00 60.37           C  
ANISOU 1492  CG2 ILE A 218     6472   7440   9026   -119  -1398  -1670       C  
ATOM   1493  CD1 ILE A 218      -6.185 -23.038  -7.248  1.00 60.77           C  
ANISOU 1493  CD1 ILE A 218     6390   7500   9200   -166  -1424  -2058       C  
ATOM   1494  N   GLU A 219      -9.526 -27.105  -6.374  1.00 60.41           N  
ANISOU 1494  N   GLU A 219     7145   7525   8284    118  -1651   -793       N  
ATOM   1495  CA  GLU A 219     -10.652 -27.876  -5.891  1.00 61.03           C  
ANISOU 1495  CA  GLU A 219     7378   7618   8193    121  -1625   -531       C  
ATOM   1496  C   GLU A 219     -10.451 -29.324  -6.284  1.00 61.07           C  
ANISOU 1496  C   GLU A 219     7679   7525   8001    172  -1646   -267       C  
ATOM   1497  O   GLU A 219      -9.646 -29.625  -7.161  1.00 60.41           O  
ANISOU 1497  O   GLU A 219     7679   7313   7960    169  -1684   -258       O  
ATOM   1498  CB  GLU A 219     -11.924 -27.376  -6.562  1.00 60.52           C  
ANISOU 1498  CB  GLU A 219     7295   7342   8360    -94  -1566   -387       C  
ATOM   1499  CG  GLU A 219     -11.951 -27.629  -8.068  1.00 59.39           C  
ANISOU 1499  CG  GLU A 219     7281   6922   8362   -250  -1587   -216       C  
ATOM   1500  CD  GLU A 219     -13.088 -26.921  -8.766  1.00 59.13           C  
ANISOU 1500  CD  GLU A 219     7165   6753   8547   -411  -1545   -110       C  
ATOM   1501  OE1 GLU A 219     -13.318 -27.206  -9.960  1.00 57.98           O  
ANISOU 1501  OE1 GLU A 219     7121   6440   8467   -534  -1570     55       O  
ATOM   1502  OE2 GLU A 219     -13.742 -26.073  -8.123  1.00 60.25           O  
ANISOU 1502  OE2 GLU A 219     7134   6980   8780   -394  -1486   -195       O  
ATOM   1503  N   VAL A 220     -11.183 -30.219  -5.632  1.00 62.28           N  
ANISOU 1503  N   VAL A 220     8002   7718   7943    216  -1591    -54       N  
ATOM   1504  CA  VAL A 220     -11.306 -31.591  -6.106  1.00 62.28           C  
ANISOU 1504  CA  VAL A 220     8327   7524   7813    193  -1546    225       C  
ATOM   1505  C   VAL A 220     -12.784 -31.947  -6.140  1.00 62.69           C  
ANISOU 1505  C   VAL A 220     8469   7452   7897    -30  -1448    431       C  
ATOM   1506  O   VAL A 220     -13.480 -31.838  -5.131  1.00 63.72           O  
ANISOU 1506  O   VAL A 220     8536   7743   7930      8  -1382    451       O  
ATOM   1507  CB  VAL A 220     -10.544 -32.587  -5.231  1.00 63.91           C  
ANISOU 1507  CB  VAL A 220     8712   7884   7687    505  -1523    302       C  
ATOM   1508  CG1 VAL A 220     -10.711 -33.988  -5.780  1.00 50.26           C  
ANISOU 1508  CG1 VAL A 220     7359   5872   5865    465  -1423    589       C  
ATOM   1509  CG2 VAL A 220      -9.076 -32.224  -5.183  1.00 50.08           C  
ANISOU 1509  CG2 VAL A 220     6810   6332   5887    732  -1635     67       C  
ATOM   1510  N   LYS A 221     -13.260 -32.362  -7.309  1.00 61.99           N  
ANISOU 1510  N   LYS A 221     8506   7112   7936   -268  -1436    561       N  
ATOM   1511  CA  LYS A 221     -14.683 -32.607  -7.509  1.00 62.76           C  
ANISOU 1511  CA  LYS A 221     8619   7133   8093   -528  -1359    706       C  
ATOM   1512  C   LYS A 221     -14.967 -34.052  -7.886  1.00 63.94           C  
ANISOU 1512  C   LYS A 221     9097   7066   8129   -664  -1249    906       C  
ATOM   1513  O   LYS A 221     -14.088 -34.762  -8.369  1.00 63.86           O  
ANISOU 1513  O   LYS A 221     9308   6901   8053   -586  -1250    939       O  
ATOM   1514  CB  LYS A 221     -15.214 -31.678  -8.589  1.00 61.34           C  
ANISOU 1514  CB  LYS A 221     8236   6902   8168   -724  -1437    650       C  
ATOM   1515  CG  LYS A 221     -14.276 -31.566  -9.761  1.00 60.05           C  
ANISOU 1515  CG  LYS A 221     8125   6591   8100   -726  -1523    597       C  
ATOM   1516  CD  LYS A 221     -14.733 -30.497 -10.717  1.00 59.29           C  
ANISOU 1516  CD  LYS A 221     7824   6474   8232   -848  -1581    561       C  
ATOM   1517  CE  LYS A 221     -13.896 -30.521 -11.971  1.00 58.82           C  
ANISOU 1517  CE  LYS A 221     7852   6257   8238   -872  -1639    546       C  
ATOM   1518  NZ  LYS A 221     -14.498 -29.662 -13.019  1.00 58.91           N  
ANISOU 1518  NZ  LYS A 221     7714   6245   8424   -985  -1675    582       N  
ATOM   1519  N   ASN A 222     -16.206 -34.476  -7.670  1.00 65.41           N  
ANISOU 1519  N   ASN A 222     9310   7235   8306   -880  -1132   1022       N  
ATOM   1520  CA  ASN A 222     -16.569 -35.871  -7.843  1.00 67.42           C  
ANISOU 1520  CA  ASN A 222     9889   7267   8462  -1045   -964   1187       C  
ATOM   1521  C   ASN A 222     -17.276 -36.140  -9.164  1.00 67.85           C  
ANISOU 1521  C   ASN A 222     9943   7175   8660  -1412   -983   1180       C  
ATOM   1522  O   ASN A 222     -17.762 -37.246  -9.394  1.00 70.02           O  
ANISOU 1522  O   ASN A 222    10453   7259   8890  -1639   -825   1267       O  
ATOM   1523  CB  ASN A 222     -17.451 -36.331  -6.682  1.00 69.51           C  
ANISOU 1523  CB  ASN A 222    10208   7601   8600  -1074   -770   1312       C  
ATOM   1524  CG  ASN A 222     -17.233 -37.783  -6.324  1.00 71.91           C  
ANISOU 1524  CG  ASN A 222    10936   7663   8723  -1037   -539   1501       C  
ATOM   1525  OD1 ASN A 222     -17.500 -38.202  -5.201  1.00 74.03           O  
ANISOU 1525  OD1 ASN A 222    11322   7983   8824   -916   -361   1634       O  
ATOM   1526  ND2 ASN A 222     -16.733 -38.558  -7.275  1.00 71.96           N  
ANISOU 1526  ND2 ASN A 222    11193   7392   8756  -1121   -517   1523       N  
ATOM   1527  N   CYS A 223     -17.334 -35.132 -10.030  1.00 66.03           N  
ANISOU 1527  N   CYS A 223     9454   7041   8594  -1469  -1160   1069       N  
ATOM   1528  CA  CYS A 223     -18.003 -35.290 -11.316  1.00 66.32           C  
ANISOU 1528  CA  CYS A 223     9448   7026   8726  -1780  -1209   1053       C  
ATOM   1529  C   CYS A 223     -17.090 -35.960 -12.330  1.00 66.24           C  
ANISOU 1529  C   CYS A 223     9691   6788   8688  -1795  -1234   1036       C  
ATOM   1530  O   CYS A 223     -15.924 -36.224 -12.047  1.00 65.48           O  
ANISOU 1530  O   CYS A 223     9778   6583   8518  -1546  -1220   1042       O  
ATOM   1531  CB  CYS A 223     -18.499 -33.945 -11.848  1.00 65.11           C  
ANISOU 1531  CB  CYS A 223     8930   7080   8728  -1789  -1365    985       C  
ATOM   1532  SG  CYS A 223     -17.239 -32.665 -12.016  1.00 74.76           S  
ANISOU 1532  SG  CYS A 223    10028   8319  10058  -1472  -1500    884       S  
ATOM   1533  N   HIS A 224     -17.632 -36.246 -13.507  1.00 67.35           N  
ANISOU 1533  N   HIS A 224     9827   6892   8870  -2079  -1272   1002       N  
ATOM   1534  CA  HIS A 224     -16.859 -36.900 -14.552  1.00 67.73           C  
ANISOU 1534  CA  HIS A 224    10116   6733   8885  -2122  -1284    967       C  
ATOM   1535  C   HIS A 224     -16.503 -35.929 -15.663  1.00 66.25           C  
ANISOU 1535  C   HIS A 224     9737   6651   8782  -2072  -1472    902       C  
ATOM   1536  O   HIS A 224     -17.316 -35.093 -16.058  1.00 66.18           O  
ANISOU 1536  O   HIS A 224     9442   6856   8847  -2159  -1574    892       O  
ATOM   1537  CB  HIS A 224     -17.624 -38.091 -15.121  1.00 70.05           C  
ANISOU 1537  CB  HIS A 224    10597   6887   9131  -2497  -1156    944       C  
ATOM   1538  CG  HIS A 224     -17.869 -39.173 -14.121  1.00 72.64           C  
ANISOU 1538  CG  HIS A 224    11194   7022   9383  -2555   -904   1029       C  
ATOM   1539  ND1 HIS A 224     -18.857 -39.093 -13.164  1.00 74.24           N  
ANISOU 1539  ND1 HIS A 224    11261   7358   9591  -2650   -804   1083       N  
ATOM   1540  CD2 HIS A 224     -17.245 -40.357 -13.920  1.00 74.42           C  
ANISOU 1540  CD2 HIS A 224    11833   6919   9523  -2506   -702   1089       C  
ATOM   1541  CE1 HIS A 224     -18.836 -40.185 -12.421  1.00 76.74           C  
ANISOU 1541  CE1 HIS A 224    11904   7428   9823  -2671   -542   1182       C  
ATOM   1542  NE2 HIS A 224     -17.867 -40.968 -12.859  1.00 76.98           N  
ANISOU 1542  NE2 HIS A 224    12282   7167   9800  -2572   -471   1195       N  
ATOM   1543  N   TRP A 225     -15.278 -36.048 -16.160  1.00 64.98           N  
ANISOU 1543  N   TRP A 225     9741   6344   8605  -1909  -1498    874       N  
ATOM   1544  CA  TRP A 225     -14.814 -35.194 -17.235  1.00 63.00           C  
ANISOU 1544  CA  TRP A 225     9356   6156   8427  -1852  -1633    829       C  
ATOM   1545  C   TRP A 225     -15.406 -35.671 -18.547  1.00 63.71           C  
ANISOU 1545  C   TRP A 225     9491   6253   8463  -2132  -1671    798       C  
ATOM   1546  O   TRP A 225     -15.110 -36.775 -18.994  1.00 64.77           O  
ANISOU 1546  O   TRP A 225     9903   6197   8508  -2253  -1591    759       O  
ATOM   1547  CB  TRP A 225     -13.292 -35.226 -17.317  1.00 61.86           C  
ANISOU 1547  CB  TRP A 225     9358   5872   8274  -1601  -1626    792       C  
ATOM   1548  CG  TRP A 225     -12.734 -34.172 -18.209  1.00 60.36           C  
ANISOU 1548  CG  TRP A 225     9009   5742   8184  -1514  -1723    753       C  
ATOM   1549  CD1 TRP A 225     -12.609 -34.231 -19.561  1.00 60.53           C  
ANISOU 1549  CD1 TRP A 225     9085   5730   8182  -1617  -1765    744       C  
ATOM   1550  CD2 TRP A 225     -12.232 -32.894 -17.811  1.00 58.84           C  
ANISOU 1550  CD2 TRP A 225     8588   5641   8128  -1315  -1756    712       C  
ATOM   1551  NE1 TRP A 225     -12.056 -33.066 -20.033  1.00 59.37           N  
ANISOU 1551  NE1 TRP A 225     8772   5636   8149  -1478  -1810    736       N  
ATOM   1552  CE2 TRP A 225     -11.815 -32.229 -18.976  1.00 58.37           C  
ANISOU 1552  CE2 TRP A 225     8473   5566   8140  -1308  -1795    706       C  
ATOM   1553  CE3 TRP A 225     -12.093 -32.251 -16.582  1.00 58.40           C  
ANISOU 1553  CE3 TRP A 225     8376   5677   8136  -1154  -1739    664       C  
ATOM   1554  CZ2 TRP A 225     -11.267 -30.947 -18.947  1.00 57.49           C  
ANISOU 1554  CZ2 TRP A 225     8171   5482   8191  -1161  -1785    660       C  
ATOM   1555  CZ3 TRP A 225     -11.551 -30.982 -16.555  1.00 57.64           C  
ANISOU 1555  CZ3 TRP A 225     8074   5628   8198  -1023  -1750    580       C  
ATOM   1556  CH2 TRP A 225     -11.144 -30.344 -17.728  1.00 57.24           C  
ANISOU 1556  CH2 TRP A 225     7988   5515   8246  -1036  -1758    582       C  
ATOM   1557  N   PRO A 226     -16.244 -34.833 -19.168  1.00 63.55           N  
ANISOU 1557  N   PRO A 226     9195   6468   8485  -2218  -1786    809       N  
ATOM   1558  CA  PRO A 226     -16.916 -35.169 -20.425  1.00 64.75           C  
ANISOU 1558  CA  PRO A 226     9320   6737   8547  -2470  -1855    764       C  
ATOM   1559  C   PRO A 226     -15.937 -35.522 -21.537  1.00 64.13           C  
ANISOU 1559  C   PRO A 226     9453   6516   8398  -2445  -1871    715       C  
ATOM   1560  O   PRO A 226     -14.909 -34.868 -21.681  1.00 62.33           O  
ANISOU 1560  O   PRO A 226     9236   6215   8232  -2197  -1889    747       O  
ATOM   1561  CB  PRO A 226     -17.670 -33.880 -20.774  1.00 64.91           C  
ANISOU 1561  CB  PRO A 226     8980   7059   8622  -2393  -1985    832       C  
ATOM   1562  CG  PRO A 226     -16.996 -32.807 -19.986  1.00 62.98           C  
ANISOU 1562  CG  PRO A 226     8649   6753   8529  -2083  -1965    893       C  
ATOM   1563  CD  PRO A 226     -16.566 -33.468 -18.721  1.00 62.62           C  
ANISOU 1563  CD  PRO A 226     8771   6534   8490  -2044  -1850    863       C  
ATOM   1564  N   LYS A 227     -16.266 -36.551 -22.311  1.00 65.67           N  
ANISOU 1564  N   LYS A 227     9807   6677   8469  -2719  -1845    613       N  
ATOM   1565  CA  LYS A 227     -15.393 -37.013 -23.383  1.00 65.10           C  
ANISOU 1565  CA  LYS A 227     9958   6468   8309  -2717  -1840    544       C  
ATOM   1566  C   LYS A 227     -15.450 -36.111 -24.611  1.00 64.78           C  
ANISOU 1566  C   LYS A 227     9727   6674   8211  -2658  -1991    571       C  
ATOM   1567  O   LYS A 227     -14.615 -36.219 -25.503  1.00 64.83           O  
ANISOU 1567  O   LYS A 227     9883   6599   8152  -2591  -1991    541       O  
ATOM   1568  CB  LYS A 227     -15.717 -38.460 -23.761  1.00 66.83           C  
ANISOU 1568  CB  LYS A 227    10417   6565   8411  -3005  -1708    391       C  
ATOM   1569  CG  LYS A 227     -15.369 -39.467 -22.682  1.00 66.71           C  
ANISOU 1569  CG  LYS A 227    10649   6270   8429  -2927  -1470    395       C  
ATOM   1570  CD  LYS A 227     -15.546 -40.889 -23.179  1.00 69.16           C  
ANISOU 1570  CD  LYS A 227    11192   6436   8649  -3129  -1270    238       C  
ATOM   1571  CE  LYS A 227     -15.054 -41.900 -22.162  1.00 69.73           C  
ANISOU 1571  CE  LYS A 227    11553   6186   8755  -2998  -1016    285       C  
ATOM   1572  NZ  LYS A 227     -15.267 -43.295 -22.637  1.00 73.03           N  
ANISOU 1572  NZ  LYS A 227    12201   6424   9125  -3198   -789    133       N  
ATOM   1573  N   SER A 228     -16.436 -35.223 -24.658  1.00 64.78           N  
ANISOU 1573  N   SER A 228     9405   6985   8225  -2657  -2104    645       N  
ATOM   1574  CA  SER A 228     -16.500 -34.245 -25.732  1.00 64.89           C  
ANISOU 1574  CA  SER A 228     9241   7237   8178  -2522  -2225    730       C  
ATOM   1575  C   SER A 228     -15.307 -33.301 -25.630  1.00 61.74           C  
ANISOU 1575  C   SER A 228     8881   6658   7920  -2196  -2176    842       C  
ATOM   1576  O   SER A 228     -14.679 -32.968 -26.631  1.00 61.00           O  
ANISOU 1576  O   SER A 228     8846   6565   7766  -2092  -2186    878       O  
ATOM   1577  CB  SER A 228     -17.817 -33.469 -25.684  1.00 66.77           C  
ANISOU 1577  CB  SER A 228     9120   7845   8404  -2527  -2336    813       C  
ATOM   1578  OG  SER A 228     -18.101 -33.006 -24.377  1.00 65.96           O  
ANISOU 1578  OG  SER A 228     8894   7689   8478  -2431  -2282    876       O  
ATOM   1579  N   HIS A 229     -14.992 -32.899 -24.403  1.00 59.93           N  
ANISOU 1579  N   HIS A 229     8614   6286   7870  -2052  -2106    874       N  
ATOM   1580  CA  HIS A 229     -13.875 -32.004 -24.140  1.00 58.13           C  
ANISOU 1580  CA  HIS A 229     8387   5900   7800  -1786  -2040    921       C  
ATOM   1581  C   HIS A 229     -12.636 -32.787 -23.721  1.00 56.04           C  
ANISOU 1581  C   HIS A 229     8369   5375   7547  -1738  -1949    821       C  
ATOM   1582  O   HIS A 229     -11.841 -32.311 -22.913  1.00 54.37           O  
ANISOU 1582  O   HIS A 229     8126   5062   7471  -1557  -1890    801       O  
ATOM   1583  CB  HIS A 229     -14.230 -31.016 -23.020  1.00 58.07           C  
ANISOU 1583  CB  HIS A 229     8161   5932   7972  -1646  -2018    974       C  
ATOM   1584  CG  HIS A 229     -15.415 -30.149 -23.315  1.00 59.69           C  
ANISOU 1584  CG  HIS A 229     8108   6386   8184  -1623  -2085   1093       C  
ATOM   1585  ND1 HIS A 229     -16.664 -30.659 -23.602  1.00 61.55           N  
ANISOU 1585  ND1 HIS A 229     8238   6874   8275  -1814  -2180   1097       N  
ATOM   1586  CD2 HIS A 229     -15.545 -28.801 -23.335  1.00 59.97           C  
ANISOU 1586  CD2 HIS A 229     7964   6463   8358  -1416  -2053   1207       C  
ATOM   1587  CE1 HIS A 229     -17.508 -29.663 -23.801  1.00 62.81           C  
ANISOU 1587  CE1 HIS A 229     8143   7261   8463  -1693  -2227   1223       C  
ATOM   1588  NE2 HIS A 229     -16.856 -28.526 -23.643  1.00 61.98           N  
ANISOU 1588  NE2 HIS A 229     8011   7006   8533  -1439  -2140   1307       N  
ATOM   1589  N   THR A 230     -12.469 -33.986 -24.268  1.00 56.44           N  
ANISOU 1589  N   THR A 230     8657   5338   7450  -1889  -1932    743       N  
ATOM   1590  CA  THR A 230     -11.353 -34.841 -23.881  1.00 55.87           C  
ANISOU 1590  CA  THR A 230     8837   5023   7368  -1807  -1831    668       C  
ATOM   1591  C   THR A 230     -10.496 -35.209 -25.084  1.00 56.34           C  
ANISOU 1591  C   THR A 230     9077   4996   7335  -1796  -1803    618       C  
ATOM   1592  O   THR A 230     -11.014 -35.583 -26.133  1.00 58.10           O  
ANISOU 1592  O   THR A 230     9356   5302   7417  -1977  -1845    587       O  
ATOM   1593  CB  THR A 230     -11.852 -36.115 -23.198  1.00 57.39           C  
ANISOU 1593  CB  THR A 230     9220   5100   7486  -1968  -1762    622       C  
ATOM   1594  OG1 THR A 230     -12.796 -35.767 -22.181  1.00 57.71           O  
ANISOU 1594  OG1 THR A 230     9077   5258   7593  -2008  -1781    673       O  
ATOM   1595  CG2 THR A 230     -10.701 -36.877 -22.570  1.00 57.25           C  
ANISOU 1595  CG2 THR A 230     9447   4844   7460  -1785  -1643    594       C  
ATOM   1596  N   LEU A 231      -9.182 -35.102 -24.919  1.00 55.12           N  
ANISOU 1596  N   LEU A 231     8990   4709   7243  -1582  -1732    590       N  
ATOM   1597  CA  LEU A 231      -8.231 -35.357 -25.998  1.00 54.96           C  
ANISOU 1597  CA  LEU A 231     9121   4610   7150  -1533  -1683    543       C  
ATOM   1598  C   LEU A 231      -7.662 -36.761 -25.914  1.00 55.21           C  
ANISOU 1598  C   LEU A 231     9463   4433   7081  -1532  -1585    455       C  
ATOM   1599  O   LEU A 231      -7.138 -37.146 -24.874  1.00 54.61           O  
ANISOU 1599  O   LEU A 231     9450   4252   7048  -1374  -1524    448       O  
ATOM   1600  CB  LEU A 231      -7.077 -34.360 -25.915  1.00 54.12           C  
ANISOU 1600  CB  LEU A 231     8874   4499   7188  -1304  -1635    548       C  
ATOM   1601  CG  LEU A 231      -7.199 -33.012 -26.611  1.00 53.57           C  
ANISOU 1601  CG  LEU A 231     8604   4544   7205  -1278  -1646    635       C  
ATOM   1602  CD1 LEU A 231      -6.171 -32.061 -26.057  1.00 52.34           C  
ANISOU 1602  CD1 LEU A 231     8288   4346   7251  -1098  -1560    595       C  
ATOM   1603  CD2 LEU A 231      -6.988 -33.202 -28.087  1.00 54.93           C  
ANISOU 1603  CD2 LEU A 231     8904   4737   7229  -1331  -1627    654       C  
ATOM   1604  N   TRP A 232      -7.758 -37.512 -27.009  1.00 56.80           N  
ANISOU 1604  N   TRP A 232     9862   4584   7133  -1686  -1560    386       N  
ATOM   1605  CA  TRP A 232      -7.173 -38.849 -27.087  1.00 58.42           C  
ANISOU 1605  CA  TRP A 232    10380   4571   7247  -1662  -1417    292       C  
ATOM   1606  C   TRP A 232      -7.847 -39.788 -26.082  1.00 59.08           C  
ANISOU 1606  C   TRP A 232    10544   4584   7318  -1720  -1318    287       C  
ATOM   1607  O   TRP A 232      -7.228 -40.227 -25.110  1.00 58.65           O  
ANISOU 1607  O   TRP A 232    10581   4403   7299  -1502  -1219    323       O  
ATOM   1608  CB  TRP A 232      -5.658 -38.768 -26.853  1.00 58.22           C  
ANISOU 1608  CB  TRP A 232    10409   4431   7280  -1351  -1345    290       C  
ATOM   1609  CG  TRP A 232      -4.904 -39.964 -27.288  1.00 60.27           C  
ANISOU 1609  CG  TRP A 232    10959   4511   7432  -1267  -1189    203       C  
ATOM   1610  CD1 TRP A 232      -5.412 -41.079 -27.874  1.00 62.66           C  
ANISOU 1610  CD1 TRP A 232    11478   4723   7608  -1451  -1087    114       C  
ATOM   1611  CD2 TRP A 232      -3.490 -40.174 -27.174  1.00 60.50           C  
ANISOU 1611  CD2 TRP A 232    11092   4419   7476   -972  -1105    183       C  
ATOM   1612  NE1 TRP A 232      -4.403 -41.975 -28.133  1.00 64.17           N  
ANISOU 1612  NE1 TRP A 232    11912   4728   7743  -1275   -927     53       N  
ATOM   1613  CE2 TRP A 232      -3.213 -41.442 -27.713  1.00 62.83           C  
ANISOU 1613  CE2 TRP A 232    11678   4546   7649   -966   -942    103       C  
ATOM   1614  CE3 TRP A 232      -2.434 -39.413 -26.668  1.00 59.15           C  
ANISOU 1614  CE3 TRP A 232    10699   4368   7406   -693  -1122    197       C  
ATOM   1615  CZ2 TRP A 232      -1.921 -41.968 -27.761  1.00 63.57           C  
ANISOU 1615  CZ2 TRP A 232    11939   4498   7717   -676   -822     71       C  
ATOM   1616  CZ3 TRP A 232      -1.153 -39.936 -26.721  1.00 60.26           C  
ANISOU 1616  CZ3 TRP A 232    10945   4440   7511   -419  -1011    145       C  
ATOM   1617  CH2 TRP A 232      -0.908 -41.201 -27.260  1.00 62.31           C  
ANISOU 1617  CH2 TRP A 232    11565   4466   7645   -395   -870     99       C  
ATOM   1618  N   SER A 233      -9.121 -40.087 -26.327  1.00 60.35           N  
ANISOU 1618  N   SER A 233    10678   4831   7422  -2017  -1343    245       N  
ATOM   1619  CA  SER A 233      -9.938 -40.856 -25.386  1.00 62.14           C  
ANISOU 1619  CA  SER A 233    10951   4999   7660  -2123  -1234    247       C  
ATOM   1620  C   SER A 233     -10.129 -42.318 -25.802  1.00 65.69           C  
ANISOU 1620  C   SER A 233    11667   5274   8020  -2282  -1033    116       C  
ATOM   1621  O   SER A 233     -10.799 -43.091 -25.114  1.00 67.33           O  
ANISOU 1621  O   SER A 233    11949   5388   8246  -2394   -891    107       O  
ATOM   1622  CB  SER A 233     -11.302 -40.186 -25.210  1.00 62.08           C  
ANISOU 1622  CB  SER A 233    10689   5217   7681  -2359  -1373    275       C  
ATOM   1623  OG  SER A 233     -12.185 -41.000 -24.457  1.00 64.09           O  
ANISOU 1623  OG  SER A 233    10993   5418   7941  -2521  -1242    252       O  
ATOM   1624  N   ASN A 234      -9.530 -42.689 -26.926  1.00 67.22           N  
ANISOU 1624  N   ASN A 234    12010   5406   8124  -2294  -1001     10       N  
ATOM   1625  CA  ASN A 234      -9.664 -44.035 -27.457  1.00 71.32           C  
ANISOU 1625  CA  ASN A 234    12780   5751   8566  -2453   -802   -144       C  
ATOM   1626  C   ASN A 234      -8.734 -45.030 -26.780  1.00 73.51           C  
ANISOU 1626  C   ASN A 234    13326   5726   8878  -2185   -567    -96       C  
ATOM   1627  O   ASN A 234      -7.531 -44.802 -26.688  1.00 72.74           O  
ANISOU 1627  O   ASN A 234    13284   5564   8788  -1870   -570    -25       O  
ATOM   1628  CB  ASN A 234      -9.377 -44.020 -28.952  1.00 72.55           C  
ANISOU 1628  CB  ASN A 234    13003   5970   8591  -2569   -861   -288       C  
ATOM   1629  CG  ASN A 234      -8.063 -43.344 -29.275  1.00 71.04           C  
ANISOU 1629  CG  ASN A 234    12834   5755   8403  -2271   -927   -209       C  
ATOM   1630  OD1 ASN A 234      -7.987 -42.119 -29.332  1.00 69.20           O  
ANISOU 1630  OD1 ASN A 234    12394   5693   8205  -2209  -1117   -109       O  
ATOM   1631  ND2 ASN A 234      -7.016 -44.138 -29.476  1.00 71.98           N  
ANISOU 1631  ND2 ASN A 234    13199   5652   8497  -2082   -754   -254       N  
ATOM   1632  N   GLY A 235      -9.297 -46.141 -26.320  1.00 76.82           N  
ANISOU 1632  N   GLY A 235    13908   5965   9316  -2309   -356   -135       N  
ATOM   1633  CA  GLY A 235      -8.511 -47.206 -25.726  1.00 79.34           C  
ANISOU 1633  CA  GLY A 235    14518   5980   9649  -2057   -107    -73       C  
ATOM   1634  C   GLY A 235      -7.758 -46.758 -24.495  1.00 78.08           C  
ANISOU 1634  C   GLY A 235    14327   5808   9531  -1672   -136    138       C  
ATOM   1635  O   GLY A 235      -6.556 -46.986 -24.371  1.00 62.04           O  
ANISOU 1635  O   GLY A 235    12435   3666   7471  -1331    -72    200       O  
ATOM   1636  N   VAL A 236      -8.473 -46.115 -23.582  1.00 77.33           N  
ANISOU 1636  N   VAL A 236    14044   5848   9492  -1722   -234    238       N  
ATOM   1637  CA  VAL A 236      -7.866 -45.630 -22.351  1.00 76.32           C  
ANISOU 1637  CA  VAL A 236    13875   5742   9383  -1380   -279    420       C  
ATOM   1638  C   VAL A 236      -8.148 -46.561 -21.170  1.00 79.63           C  
ANISOU 1638  C   VAL A 236    14496   5965   9795  -1284    -51    548       C  
ATOM   1639  O   VAL A 236      -9.295 -46.741 -20.762  1.00 80.57           O  
ANISOU 1639  O   VAL A 236    14578   6082   9952  -1544     10    551       O  
ATOM   1640  CB  VAL A 236      -8.321 -44.202 -22.017  1.00 72.65           C  
ANISOU 1640  CB  VAL A 236    13080   5547   8975  -1440   -538    464       C  
ATOM   1641  CG1 VAL A 236      -7.786 -43.779 -20.665  1.00 71.37           C  
ANISOU 1641  CG1 VAL A 236    12896   5402   8819  -1113   -575    626       C  
ATOM   1642  CG2 VAL A 236      -7.856 -43.243 -23.092  1.00 70.34           C  
ANISOU 1642  CG2 VAL A 236    12610   5425   8692  -1457   -736    383       C  
ATOM   1643  N   LEU A 237      -7.084 -47.150 -20.635  1.00 81.58           N  
ANISOU 1643  N   LEU A 237    14955   6061   9980   -893     83    661       N  
ATOM   1644  CA  LEU A 237      -7.179 -48.024 -19.476  1.00 84.70           C  
ANISOU 1644  CA  LEU A 237    15567   6279  10335   -713    312    825       C  
ATOM   1645  C   LEU A 237      -7.407 -47.175 -18.233  1.00 83.43           C  
ANISOU 1645  C   LEU A 237    15246   6294  10160   -571    182    981       C  
ATOM   1646  O   LEU A 237      -6.543 -46.391 -17.845  1.00 81.59           O  
ANISOU 1646  O   LEU A 237    14897   6223   9879   -253      9   1043       O  
ATOM   1647  CB  LEU A 237      -5.894 -48.844 -19.323  1.00 86.93           C  
ANISOU 1647  CB  LEU A 237    16105   6403  10522   -274    477    913       C  
ATOM   1648  CG  LEU A 237      -5.717 -50.147 -20.112  1.00 90.60           C  
ANISOU 1648  CG  LEU A 237    16864   6582  10977   -341    740    822       C  
ATOM   1649  CD1 LEU A 237      -5.998 -49.968 -21.589  1.00 89.79           C  
ANISOU 1649  CD1 LEU A 237    16679   6510  10928   -704    648    582       C  
ATOM   1650  CD2 LEU A 237      -4.314 -50.698 -19.914  1.00 92.34           C  
ANISOU 1650  CD2 LEU A 237    17277   6716  11090    167    854    927       C  
ATOM   1651  N   GLU A 238      -8.572 -47.333 -17.613  1.00 84.66           N  
ANISOU 1651  N   GLU A 238    15392   6422  10352   -811    269   1029       N  
ATOM   1652  CA  GLU A 238      -8.897 -46.583 -16.406  1.00 83.20           C  
ANISOU 1652  CA  GLU A 238    15081   6393  10140   -699    170   1178       C  
ATOM   1653  C   GLU A 238      -8.017 -47.018 -15.239  1.00 84.24           C  
ANISOU 1653  C   GLU A 238    15398   6487  10122   -188    288   1393       C  
ATOM   1654  O   GLU A 238      -7.887 -46.307 -14.249  1.00 83.09           O  
ANISOU 1654  O   GLU A 238    15149   6525   9897     42    165   1515       O  
ATOM   1655  CB  GLU A 238     -10.382 -46.723 -16.059  1.00 84.98           C  
ANISOU 1655  CB  GLU A 238    15258   6597  10435  -1090    266   1175       C  
ATOM   1656  CG  GLU A 238     -11.313 -46.185 -17.141  1.00 84.42           C  
ANISOU 1656  CG  GLU A 238    14940   6663  10474  -1554    113    965       C  
ATOM   1657  CD  GLU A 238     -12.746 -46.028 -16.671  1.00 85.86           C  
ANISOU 1657  CD  GLU A 238    14986   6921  10715  -1900    147    964       C  
ATOM   1658  OE1 GLU A 238     -12.996 -46.175 -15.456  1.00 87.22           O  
ANISOU 1658  OE1 GLU A 238    15248   7043  10850  -1783    271   1138       O  
ATOM   1659  OE2 GLU A 238     -13.623 -45.753 -17.520  1.00 85.74           O  
ANISOU 1659  OE2 GLU A 238    14768   7042  10766  -2274     52    793       O  
ATOM   1660  N   SER A 239      -7.402 -48.186 -15.374  1.00 86.79           N  
ANISOU 1660  N   SER A 239    15992   6599  10387     10    523   1433       N  
ATOM   1661  CA  SER A 239      -6.494 -48.694 -14.357  1.00 88.50           C  
ANISOU 1661  CA  SER A 239    16376   6820  10430    546    645   1639       C  
ATOM   1662  C   SER A 239      -5.113 -48.061 -14.485  1.00 85.93           C  
ANISOU 1662  C   SER A 239    15921   6715  10015    963    434   1621       C  
ATOM   1663  O   SER A 239      -4.193 -48.423 -13.760  1.00 87.93           O  
ANISOU 1663  O   SER A 239    16255   7057  10098   1460    497   1761       O  
ATOM   1664  CB  SER A 239      -6.374 -50.215 -14.460  1.00 93.24           C  
ANISOU 1664  CB  SER A 239    17326   7098  11001    611    998   1692       C  
ATOM   1665  OG  SER A 239      -5.679 -50.599 -15.634  1.00 93.59           O  
ANISOU 1665  OG  SER A 239    17449   7028  11084    602   1015   1543       O  
ATOM   1666  N   GLU A 240      -4.971 -47.113 -15.404  1.00 82.00           N  
ANISOU 1666  N   GLU A 240    15204   6331   9622    771    188   1444       N  
ATOM   1667  CA  GLU A 240      -3.679 -46.479 -15.626  1.00 80.18           C  
ANISOU 1667  CA  GLU A 240    14836   6297   9333   1124     -5   1395       C  
ATOM   1668  C   GLU A 240      -3.738 -44.964 -15.529  1.00 76.29           C  
ANISOU 1668  C   GLU A 240    14027   6062   8896   1062   -332   1315       C  
ATOM   1669  O   GLU A 240      -2.712 -44.314 -15.338  1.00 75.33           O  
ANISOU 1669  O   GLU A 240    13698   6206   8718   1397   -506   1266       O  
ATOM   1670  CB  GLU A 240      -3.111 -46.876 -16.984  1.00 80.34           C  
ANISOU 1670  CB  GLU A 240    14934   6171   9419   1029     44   1244       C  
ATOM   1671  CG  GLU A 240      -2.780 -48.343 -17.121  1.00 84.26           C  
ANISOU 1671  CG  GLU A 240    15753   6412   9850   1173    354   1304       C  
ATOM   1672  CD  GLU A 240      -1.634 -48.571 -18.078  1.00 84.63           C  
ANISOU 1672  CD  GLU A 240    15851   6428   9878   1362    363   1204       C  
ATOM   1673  OE1 GLU A 240      -0.828 -47.636 -18.259  1.00 82.43           O  
ANISOU 1673  OE1 GLU A 240    15353   6375   9591   1549    139   1141       O  
ATOM   1674  OE2 GLU A 240      -1.537 -49.679 -18.645  1.00 87.18           O  
ANISOU 1674  OE2 GLU A 240    16433   6495  10196   1325    602   1179       O  
ATOM   1675  N   MET A 241      -4.932 -44.400 -15.676  1.00 74.38           N  
ANISOU 1675  N   MET A 241    13672   5808   8781    621   -411   1265       N  
ATOM   1676  CA  MET A 241      -5.079 -42.951 -15.616  1.00 70.98           C  
ANISOU 1676  CA  MET A 241    12801   5721   8449    507   -689   1139       C  
ATOM   1677  C   MET A 241      -4.872 -42.430 -14.202  1.00 70.45           C  
ANISOU 1677  C   MET A 241    12509   5988   8272    821   -770   1199       C  
ATOM   1678  O   MET A 241      -5.618 -42.765 -13.289  1.00 71.47           O  
ANISOU 1678  O   MET A 241    12751   6081   8323    817   -667   1343       O  
ATOM   1679  CB  MET A 241      -6.426 -42.496 -16.182  1.00 69.41           C  
ANISOU 1679  CB  MET A 241    12495   5474   8403    -17   -744   1069       C  
ATOM   1680  CG  MET A 241      -7.603 -43.337 -15.760  1.00 71.29           C  
ANISOU 1680  CG  MET A 241    12998   5471   8619   -257   -545   1189       C  
ATOM   1681  SD  MET A 241      -9.080 -42.947 -16.712  1.00 71.41           S  
ANISOU 1681  SD  MET A 241    12805   5532   8794   -861   -606   1041       S  
ATOM   1682  CE  MET A 241      -9.362 -41.253 -16.225  1.00 55.47           C  
ANISOU 1682  CE  MET A 241    10313   3900   6864   -852   -891   1006       C  
ATOM   1683  N   ILE A 242      -3.838 -41.613 -14.046  1.00 69.03           N  
ANISOU 1683  N   ILE A 242    12001   6148   8079   1080   -943   1067       N  
ATOM   1684  CA  ILE A 242      -3.444 -41.075 -12.750  1.00 69.27           C  
ANISOU 1684  CA  ILE A 242    11773   6569   7978   1404  -1043   1056       C  
ATOM   1685  C   ILE A 242      -4.574 -40.372 -12.008  1.00 68.06           C  
ANISOU 1685  C   ILE A 242    11437   6546   7876   1179  -1100   1056       C  
ATOM   1686  O   ILE A 242      -4.929 -40.760 -10.902  1.00 69.66           O  
ANISOU 1686  O   ILE A 242    11741   6815   7913   1352  -1018   1204       O  
ATOM   1687  CB  ILE A 242      -2.269 -40.109 -12.903  1.00 67.94           C  
ANISOU 1687  CB  ILE A 242    11205   6757   7851   1574  -1227    822       C  
ATOM   1688  CG1 ILE A 242      -1.012 -40.884 -13.282  1.00 69.63           C  
ANISOU 1688  CG1 ILE A 242    11566   6945   7945   1932  -1162    841       C  
ATOM   1689  CG2 ILE A 242      -2.036 -39.339 -11.619  1.00 68.32           C  
ANISOU 1689  CG2 ILE A 242    10913   7254   7793   1796  -1354    726       C  
ATOM   1690  CD1 ILE A 242       0.233 -40.072 -13.148  1.00 69.69           C  
ANISOU 1690  CD1 ILE A 242    11158   7379   7942   2167  -1319    610       C  
ATOM   1691  N   ILE A 243      -5.128 -39.332 -12.615  1.00 65.62           N  
ANISOU 1691  N   ILE A 243    10865   6281   7787    822  -1224    904       N  
ATOM   1692  CA  ILE A 243      -6.241 -38.621 -12.015  1.00 64.87           C  
ANISOU 1692  CA  ILE A 243    10586   6299   7763    606  -1269    896       C  
ATOM   1693  C   ILE A 243      -7.497 -39.459 -12.178  1.00 65.34           C  
ANISOU 1693  C   ILE A 243    10941   6055   7830    318  -1110   1067       C  
ATOM   1694  O   ILE A 243      -7.926 -39.721 -13.297  1.00 64.87           O  
ANISOU 1694  O   ILE A 243    10999   5761   7886     15  -1080   1053       O  
ATOM   1695  CB  ILE A 243      -6.442 -37.260 -12.683  1.00 63.45           C  
ANISOU 1695  CB  ILE A 243    10056   6232   7820    350  -1420    705       C  
ATOM   1696  CG1 ILE A 243      -5.088 -36.587 -12.913  1.00 63.41           C  
ANISOU 1696  CG1 ILE A 243     9814   6424   7854    550  -1521    510       C  
ATOM   1697  CG2 ILE A 243      -7.354 -36.378 -11.842  1.00 62.96           C  
ANISOU 1697  CG2 ILE A 243     9749   6358   7814    244  -1471    669       C  
ATOM   1698  CD1 ILE A 243      -5.182 -35.236 -13.565  1.00 61.40           C  
ANISOU 1698  CD1 ILE A 243     9253   6232   7845    321  -1613    337       C  
ATOM   1699  N   PRO A 244      -8.082 -39.893 -11.053  1.00 66.63           N  
ANISOU 1699  N   PRO A 244    11216   6244   7857    405   -996   1216       N  
ATOM   1700  CA  PRO A 244      -9.250 -40.781 -11.026  1.00 68.12           C  
ANISOU 1700  CA  PRO A 244    11693   6147   8044    134   -791   1376       C  
ATOM   1701  C   PRO A 244     -10.448 -40.249 -11.808  1.00 66.81           C  
ANISOU 1701  C   PRO A 244    11361   5941   8084   -353   -852   1283       C  
ATOM   1702  O   PRO A 244     -10.761 -39.063 -11.725  1.00 65.11           O  
ANISOU 1702  O   PRO A 244    10785   5979   7976   -428  -1020   1169       O  
ATOM   1703  CB  PRO A 244      -9.593 -40.848  -9.539  1.00 69.55           C  
ANISOU 1703  CB  PRO A 244    11874   6501   8053    344   -708   1510       C  
ATOM   1704  CG  PRO A 244      -8.306 -40.593  -8.849  1.00 69.93           C  
ANISOU 1704  CG  PRO A 244    11807   6842   7922    838   -812   1477       C  
ATOM   1705  CD  PRO A 244      -7.592 -39.590  -9.697  1.00 67.41           C  
ANISOU 1705  CD  PRO A 244    11170   6675   7769    786  -1038   1228       C  
ATOM   1706  N   LYS A 245     -11.104 -41.137 -12.551  1.00 67.91           N  
ANISOU 1706  N   LYS A 245    11762   5774   8269   -668   -703   1323       N  
ATOM   1707  CA  LYS A 245     -12.294 -40.802 -13.326  1.00 67.26           C  
ANISOU 1707  CA  LYS A 245    11524   5695   8338  -1128   -753   1233       C  
ATOM   1708  C   LYS A 245     -13.381 -40.195 -12.452  1.00 67.60           C  
ANISOU 1708  C   LYS A 245    11321   5954   8409  -1243   -766   1262       C  
ATOM   1709  O   LYS A 245     -13.945 -39.151 -12.782  1.00 66.27           O  
ANISOU 1709  O   LYS A 245    10811   6005   8363  -1394   -934   1164       O  
ATOM   1710  CB  LYS A 245     -12.828 -42.052 -14.029  1.00 69.38           C  
ANISOU 1710  CB  LYS A 245    12139   5612   8609  -1448   -542   1246       C  
ATOM   1711  CG  LYS A 245     -14.259 -41.938 -14.539  1.00 69.81           C  
ANISOU 1711  CG  LYS A 245    12036   5721   8769  -1938   -548   1158       C  
ATOM   1712  CD  LYS A 245     -14.819 -43.311 -14.899  1.00 73.32           C  
ANISOU 1712  CD  LYS A 245    12741   5909   9207  -2203   -262   1118       C  
ATOM   1713  CE  LYS A 245     -16.263 -43.228 -15.370  1.00 74.54           C  
ANISOU 1713  CE  LYS A 245    12654   6220   9448  -2666   -267    982       C  
ATOM   1714  NZ  LYS A 245     -16.812 -44.565 -15.721  1.00 78.35           N  
ANISOU 1714  NZ  LYS A 245    13313   6512   9946  -2907     18    883       N  
ATOM   1715  N   ASN A 246     -13.662 -40.841 -11.326  1.00 69.94           N  
ANISOU 1715  N   ASN A 246    11801   6190   8585  -1142   -570   1413       N  
ATOM   1716  CA  ASN A 246     -14.678 -40.350 -10.406  1.00 70.95           C  
ANISOU 1716  CA  ASN A 246    11717   6523   8717  -1232   -548   1450       C  
ATOM   1717  C   ASN A 246     -14.216 -39.066  -9.715  1.00 69.59           C  
ANISOU 1717  C   ASN A 246    11198   6706   8536   -939   -753   1375       C  
ATOM   1718  O   ASN A 246     -14.967 -38.455  -8.956  1.00 69.76           O  
ANISOU 1718  O   ASN A 246    10998   6938   8568   -973   -762   1373       O  
ATOM   1719  CB  ASN A 246     -15.040 -41.430  -9.380  1.00 74.70           C  
ANISOU 1719  CB  ASN A 246    12516   6822   9043  -1184   -244   1651       C  
ATOM   1720  CG  ASN A 246     -16.464 -41.297  -8.861  1.00 76.67           C  
ANISOU 1720  CG  ASN A 246    12615   7172   9344  -1491   -138   1674       C  
ATOM   1721  OD1 ASN A 246     -17.299 -40.618  -9.459  1.00 75.90           O  
ANISOU 1721  OD1 ASN A 246    12208   7231   9401  -1796   -273   1538       O  
ATOM   1722  ND2 ASN A 246     -16.748 -41.956  -7.745  1.00 79.69           N  
ANISOU 1722  ND2 ASN A 246    13214   7480   9584  -1388    119   1860       N  
ATOM   1723  N   LEU A 247     -12.977 -38.666  -9.988  1.00 68.22           N  
ANISOU 1723  N   LEU A 247    10973   6598   8350   -668   -897   1290       N  
ATOM   1724  CA  LEU A 247     -12.447 -37.396  -9.506  1.00 66.40           C  
ANISOU 1724  CA  LEU A 247    10399   6683   8148   -448  -1082   1151       C  
ATOM   1725  C   LEU A 247     -12.168 -36.443 -10.661  1.00 64.43           C  
ANISOU 1725  C   LEU A 247     9918   6461   8101   -572  -1259    987       C  
ATOM   1726  O   LEU A 247     -11.137 -35.776 -10.678  1.00 63.25           O  
ANISOU 1726  O   LEU A 247     9620   6437   7975   -362  -1370    858       O  
ATOM   1727  CB  LEU A 247     -11.163 -37.611  -8.705  1.00 66.34           C  
ANISOU 1727  CB  LEU A 247    10463   6802   7942     -5  -1090   1157       C  
ATOM   1728  CG  LEU A 247     -11.262 -38.370  -7.382  1.00 67.89           C  
ANISOU 1728  CG  LEU A 247    10858   7055   7881    242   -926   1338       C  
ATOM   1729  CD1 LEU A 247      -9.966 -38.248  -6.594  1.00 67.80           C  
ANISOU 1729  CD1 LEU A 247    10785   7320   7656    720  -1007   1290       C  
ATOM   1730  CD2 LEU A 247     -12.438 -37.863  -6.570  1.00 67.95           C  
ANISOU 1730  CD2 LEU A 247    10693   7222   7904     94   -886   1352       C  
ATOM   1731  N   ALA A 248     -13.088 -36.392 -11.622  1.00 64.57           N  
ANISOU 1731  N   ALA A 248     9902   6379   8252   -911  -1271    990       N  
ATOM   1732  CA  ALA A 248     -12.969 -35.515 -12.787  1.00 62.85           C  
ANISOU 1732  CA  ALA A 248     9491   6187   8202  -1023  -1414    882       C  
ATOM   1733  C   ALA A 248     -11.681 -35.736 -13.570  1.00 61.52           C  
ANISOU 1733  C   ALA A 248     9451   5902   8023   -888  -1451    827       C  
ATOM   1734  O   ALA A 248     -11.183 -34.833 -14.233  1.00 59.29           O  
ANISOU 1734  O   ALA A 248     8990   5675   7862   -863  -1553    727       O  
ATOM   1735  CB  ALA A 248     -13.101 -34.061 -12.376  1.00 62.16           C  
ANISOU 1735  CB  ALA A 248     9050   6324   8243   -942  -1513    780       C  
ATOM   1736  N   GLY A 249     -11.147 -36.947 -13.491  1.00 63.06           N  
ANISOU 1736  N   GLY A 249     9966   5919   8076   -792  -1341    901       N  
ATOM   1737  CA  GLY A 249      -9.957 -37.289 -14.240  1.00 62.85           C  
ANISOU 1737  CA  GLY A 249    10078   5778   8026   -654  -1354    856       C  
ATOM   1738  C   GLY A 249     -10.291 -37.512 -15.695  1.00 62.42           C  
ANISOU 1738  C   GLY A 249    10109   5562   8044   -938  -1367    832       C  
ATOM   1739  O   GLY A 249     -11.233 -38.232 -16.013  1.00 63.58           O  
ANISOU 1739  O   GLY A 249    10410   5577   8169  -1208  -1284    881       O  
ATOM   1740  N   PRO A 250      -9.527 -36.878 -16.588  1.00 61.17           N  
ANISOU 1740  N   PRO A 250     9839   5439   7966   -892  -1460    738       N  
ATOM   1741  CA  PRO A 250      -9.739 -37.027 -18.028  1.00 61.30           C  
ANISOU 1741  CA  PRO A 250     9928   5350   8015  -1122  -1482    711       C  
ATOM   1742  C   PRO A 250      -9.434 -38.443 -18.479  1.00 62.93           C  
ANISOU 1742  C   PRO A 250    10513   5296   8102  -1159  -1350    732       C  
ATOM   1743  O   PRO A 250      -8.332 -38.931 -18.244  1.00 64.05           O  
ANISOU 1743  O   PRO A 250    10810   5351   8175   -892  -1286    735       O  
ATOM   1744  CB  PRO A 250      -8.713 -36.063 -18.630  1.00 59.80           C  
ANISOU 1744  CB  PRO A 250     9560   5244   7916   -976  -1564    624       C  
ATOM   1745  CG  PRO A 250      -8.446 -35.075 -17.552  1.00 59.08           C  
ANISOU 1745  CG  PRO A 250     9203   5340   7903   -792  -1610    576       C  
ATOM   1746  CD  PRO A 250      -8.497 -35.872 -16.289  1.00 60.22           C  
ANISOU 1746  CD  PRO A 250     9479   5488   7913   -648  -1542    634       C  
ATOM   1747  N   VAL A 251     -10.403 -39.093 -19.113  1.00 63.53           N  
ANISOU 1747  N   VAL A 251    10725   5262   8152  -1483  -1298    728       N  
ATOM   1748  CA  VAL A 251     -10.192 -40.432 -19.640  1.00 65.13           C  
ANISOU 1748  CA  VAL A 251    11260   5228   8260  -1546  -1123    697       C  
ATOM   1749  C   VAL A 251      -9.292 -40.323 -20.860  1.00 64.96           C  
ANISOU 1749  C   VAL A 251    11250   5207   8225  -1479  -1165    604       C  
ATOM   1750  O   VAL A 251      -9.760 -40.398 -21.994  1.00 66.34           O  
ANISOU 1750  O   VAL A 251    11387   5443   8375  -1706  -1184    514       O  
ATOM   1751  CB  VAL A 251     -11.525 -41.105 -20.027  1.00 66.32           C  
ANISOU 1751  CB  VAL A 251    11424   5387   8388  -1914  -1022    637       C  
ATOM   1752  CG1 VAL A 251     -11.307 -42.574 -20.357  1.00 69.03           C  
ANISOU 1752  CG1 VAL A 251    12080   5491   8657  -1943   -776    581       C  
ATOM   1753  CG2 VAL A 251     -12.545 -40.960 -18.903  1.00 66.06           C  
ANISOU 1753  CG2 VAL A 251    11308   5403   8389  -2028  -1000    725       C  
ATOM   1754  N   SER A 252      -7.997 -40.141 -20.624  1.00 63.76           N  
ANISOU 1754  N   SER A 252    11155   4998   8074  -1163  -1185    623       N  
ATOM   1755  CA  SER A 252      -7.061 -39.875 -21.710  1.00 62.52           C  
ANISOU 1755  CA  SER A 252    10983   4850   7922  -1087  -1226    541       C  
ATOM   1756  C   SER A 252      -5.727 -40.581 -21.522  1.00 62.60           C  
ANISOU 1756  C   SER A 252    11219   4703   7864   -761  -1121    545       C  
ATOM   1757  O   SER A 252      -5.312 -40.852 -20.398  1.00 63.05           O  
ANISOU 1757  O   SER A 252    11311   4768   7876   -489  -1070    618       O  
ATOM   1758  CB  SER A 252      -6.821 -38.372 -21.833  1.00 60.99           C  
ANISOU 1758  CB  SER A 252    10431   4895   7849  -1030  -1386    520       C  
ATOM   1759  OG  SER A 252      -5.779 -38.100 -22.749  1.00 61.21           O  
ANISOU 1759  OG  SER A 252    10445   4927   7887   -924  -1388    453       O  
ATOM   1760  N   GLN A 253      -5.054 -40.863 -22.632  1.00 62.26           N  
ANISOU 1760  N   GLN A 253    11265   4605   7787   -749  -1073    462       N  
ATOM   1761  CA  GLN A 253      -3.719 -41.439 -22.592  1.00 62.60           C  
ANISOU 1761  CA  GLN A 253    11494   4522   7769   -415   -981    456       C  
ATOM   1762  C   GLN A 253      -2.702 -40.343 -22.331  1.00 60.71           C  
ANISOU 1762  C   GLN A 253    10907   4559   7602   -166  -1093    409       C  
ATOM   1763  O   GLN A 253      -1.499 -40.584 -22.322  1.00 49.19           O  
ANISOU 1763  O   GLN A 253     9464   3126   6100    132  -1041    372       O  
ATOM   1764  CB  GLN A 253      -3.396 -42.152 -23.902  1.00 51.25           C  
ANISOU 1764  CB  GLN A 253    10228   2976   6267   -502   -862    359       C  
ATOM   1765  CG  GLN A 253      -4.418 -43.199 -24.313  1.00 57.89           C  
ANISOU 1765  CG  GLN A 253    11241   3709   7048   -786   -716    321       C  
ATOM   1766  CD  GLN A 253      -3.896 -44.125 -25.396  1.00 59.85           C  
ANISOU 1766  CD  GLN A 253    11726   3799   7214   -794   -565    215       C  
ATOM   1767  OE1 GLN A 253      -2.700 -44.154 -25.677  1.00 59.95           O  
ANISOU 1767  OE1 GLN A 253    11811   3762   7204   -530   -535    200       O  
ATOM   1768  NE2 GLN A 253      -4.793 -44.891 -26.006  1.00 61.60           N  
ANISOU 1768  NE2 GLN A 253    12069   3944   7392  -1099   -465    123       N  
ATOM   1769  N   HIS A 254      -3.204 -39.129 -22.144  1.00 58.60           N  
ANISOU 1769  N   HIS A 254    10316   4499   7450   -299  -1228    394       N  
ATOM   1770  CA  HIS A 254      -2.392 -38.026 -21.673  1.00 57.61           C  
ANISOU 1770  CA  HIS A 254     9846   4622   7424   -114  -1306    320       C  
ATOM   1771  C   HIS A 254      -2.334 -38.091 -20.155  1.00 58.49           C  
ANISOU 1771  C   HIS A 254     9872   4863   7488    110  -1328    351       C  
ATOM   1772  O   HIS A 254      -1.352 -37.679 -19.539  1.00 59.21           O  
ANISOU 1772  O   HIS A 254     9750   5167   7582    369  -1359    262       O  
ATOM   1773  CB  HIS A 254      -3.001 -36.695 -22.090  1.00 56.12           C  
ANISOU 1773  CB  HIS A 254     9383   4552   7389   -343  -1399    296       C  
ATOM   1774  CG  HIS A 254      -2.887 -36.403 -23.553  1.00 56.22           C  
ANISOU 1774  CG  HIS A 254     9424   4512   7427   -496  -1380    276       C  
ATOM   1775  ND1 HIS A 254      -1.675 -36.313 -24.205  1.00 56.55           N  
ANISOU 1775  ND1 HIS A 254     9444   4565   7479   -363  -1314    194       N  
ATOM   1776  CD2 HIS A 254      -3.838 -36.144 -24.484  1.00 56.01           C  
ANISOU 1776  CD2 HIS A 254     9424   4463   7395   -754  -1417    330       C  
ATOM   1777  CE1 HIS A 254      -1.886 -36.029 -25.478  1.00 56.60           C  
ANISOU 1777  CE1 HIS A 254     9493   4531   7482   -535  -1298    212       C  
ATOM   1778  NE2 HIS A 254      -3.189 -35.919 -25.673  1.00 56.25           N  
ANISOU 1778  NE2 HIS A 254     9475   4482   7417   -760  -1370    296       N  
ATOM   1779  N   ASN A 255      -3.400 -38.618 -19.556  1.00 58.39           N  
ANISOU 1779  N   ASN A 255    10015   4752   7420      2  -1304    465       N  
ATOM   1780  CA  ASN A 255      -3.466 -38.824 -18.117  1.00 58.49           C  
ANISOU 1780  CA  ASN A 255    10006   4874   7345    219  -1298    531       C  
ATOM   1781  C   ASN A 255      -2.705 -40.087 -17.739  1.00 60.46           C  
ANISOU 1781  C   ASN A 255    10554   5004   7415    550  -1166    618       C  
ATOM   1782  O   ASN A 255      -3.009 -40.743 -16.744  1.00 62.34           O  
ANISOU 1782  O   ASN A 255    10955   5204   7528    704  -1087    752       O  
ATOM   1783  CB  ASN A 255      -4.926 -38.929 -17.676  1.00 58.93           C  
ANISOU 1783  CB  ASN A 255    10125   4854   7410    -35  -1286    633       C  
ATOM   1784  CG  ASN A 255      -5.102 -38.762 -16.181  1.00 60.42           C  
ANISOU 1784  CG  ASN A 255    10202   5226   7527    156  -1301    686       C  
ATOM   1785  OD1 ASN A 255      -4.171 -38.389 -15.469  1.00 60.90           O  
ANISOU 1785  OD1 ASN A 255    10081   5524   7534    462  -1356    616       O  
ATOM   1786  ND2 ASN A 255      -6.307 -39.034 -15.696  1.00 61.27           N  
ANISOU 1786  ND2 ASN A 255    10400   5258   7620    -31  -1250    791       N  
ATOM   1787  N   TYR A 256      -1.708 -40.420 -18.550  1.00 60.25           N  
ANISOU 1787  N   TYR A 256    10609   4915   7370    683  -1120    557       N  
ATOM   1788  CA  TYR A 256      -0.907 -41.609 -18.336  1.00 62.02           C  
ANISOU 1788  CA  TYR A 256    11124   5011   7430   1040   -975    644       C  
ATOM   1789  C   TYR A 256       0.479 -41.245 -17.850  1.00 62.01           C  
ANISOU 1789  C   TYR A 256    10853   5347   7361   1456  -1046    553       C  
ATOM   1790  O   TYR A 256       1.006 -40.180 -18.170  1.00 59.89           O  
ANISOU 1790  O   TYR A 256    10223   5321   7211   1392  -1166    374       O  
ATOM   1791  CB  TYR A 256      -0.784 -42.419 -19.626  1.00 62.99           C  
ANISOU 1791  CB  TYR A 256    11566   4808   7559    911   -841    629       C  
ATOM   1792  CG  TYR A 256      -1.953 -43.332 -19.902  1.00 64.55           C  
ANISOU 1792  CG  TYR A 256    12143   4636   7747    606   -694    718       C  
ATOM   1793  CD1 TYR A 256      -3.100 -43.280 -19.127  1.00 64.79           C  
ANISOU 1793  CD1 TYR A 256    12176   4652   7790    419   -697    809       C  
ATOM   1794  CD2 TYR A 256      -1.901 -44.260 -20.932  1.00 66.22           C  
ANISOU 1794  CD2 TYR A 256    12607   4614   7940    480   -522    666       C  
ATOM   1795  CE1 TYR A 256      -4.165 -44.114 -19.378  1.00 66.38           C  
ANISOU 1795  CE1 TYR A 256    12548   4673   8002     97   -525    822       C  
ATOM   1796  CE2 TYR A 256      -2.963 -45.100 -21.189  1.00 67.85           C  
ANISOU 1796  CE2 TYR A 256    12961   4666   8152    156   -359    662       C  
ATOM   1797  CZ  TYR A 256      -4.092 -45.021 -20.409  1.00 68.06           C  
ANISOU 1797  CZ  TYR A 256    12938   4716   8205    -36   -361    735       C  
ATOM   1798  OH  TYR A 256      -5.152 -45.852 -20.657  1.00 70.07           O  
ANISOU 1798  OH  TYR A 256    13321   4825   8478   -361   -194    704       O  
ATOM   1799  N   ARG A 257       1.059 -42.150 -17.073  1.00 64.64           N  
ANISOU 1799  N   ARG A 257    11363   5700   7497   1887   -952    676       N  
ATOM   1800  CA  ARG A 257       2.451 -42.056 -16.680  1.00 66.17           C  
ANISOU 1800  CA  ARG A 257    11325   6240   7575   2342  -1004    593       C  
ATOM   1801  C   ARG A 257       2.977 -43.465 -16.471  1.00 70.02           C  
ANISOU 1801  C   ARG A 257    12206   6542   7854   2780   -812    788       C  
ATOM   1802  O   ARG A 257       2.418 -44.224 -15.679  1.00 71.40           O  
ANISOU 1802  O   ARG A 257    12676   6559   7895   2923   -693   1007       O  
ATOM   1803  CB  ARG A 257       2.592 -41.244 -15.401  1.00 65.56           C  
ANISOU 1803  CB  ARG A 257    10863   6622   7427   2512  -1165    518       C  
ATOM   1804  CG  ARG A 257       4.013 -40.873 -15.074  1.00 66.71           C  
ANISOU 1804  CG  ARG A 257    10635   7232   7478   2892  -1263    338       C  
ATOM   1805  CD  ARG A 257       4.642 -40.088 -16.190  1.00 65.02           C  
ANISOU 1805  CD  ARG A 257    10162   7065   7476   2659  -1303     99       C  
ATOM   1806  NE  ARG A 257       5.976 -39.631 -15.829  1.00 66.51           N  
ANISOU 1806  NE  ARG A 257     9925   7745   7599   2965  -1393   -124       N  
ATOM   1807  CZ  ARG A 257       6.319 -38.352 -15.735  1.00 65.15           C  
ANISOU 1807  CZ  ARG A 257     9282   7891   7583   2771  -1507   -412       C  
ATOM   1808  NH1 ARG A 257       5.425 -37.408 -15.988  1.00 61.61           N  
ANISOU 1808  NH1 ARG A 257     8759   7288   7363   2316  -1538   -473       N  
ATOM   1809  NH2 ARG A 257       7.557 -38.021 -15.397  1.00 67.61           N  
ANISOU 1809  NH2 ARG A 257     9189   8674   7824   3034  -1573   -649       N  
ATOM   1810  N   PRO A 258       4.043 -43.826 -17.203  1.00 74.83           N  
ANISOU 1810  N   PRO A 258    12348   8972   7112   3229   -259   -863       N  
ATOM   1811  CA  PRO A 258       4.681 -45.140 -17.094  1.00 78.15           C  
ANISOU 1811  CA  PRO A 258    12968   9301   7425   3681   -265   -997       C  
ATOM   1812  C   PRO A 258       5.001 -45.482 -15.648  1.00 78.80           C  
ANISOU 1812  C   PRO A 258    13180   9199   7561   3829   -373   -920       C  
ATOM   1813  O   PRO A 258       5.426 -44.614 -14.894  1.00 77.50           O  
ANISOU 1813  O   PRO A 258    12768   9226   7452   3707   -434   -784       O  
ATOM   1814  CB  PRO A 258       5.975 -44.954 -17.885  1.00 80.46           C  
ANISOU 1814  CB  PRO A 258    12869  10123   7580   3926   -212  -1028       C  
ATOM   1815  CG  PRO A 258       5.635 -43.937 -18.902  1.00 68.79           C  
ANISOU 1815  CG  PRO A 258    11126   8912   6098   3589   -142   -968       C  
ATOM   1816  CD  PRO A 258       4.681 -42.992 -18.238  1.00 75.31           C  
ANISOU 1816  CD  PRO A 258    11990   9516   7109   3157   -198   -817       C  
ATOM   1817  N   GLY A 259       4.789 -46.734 -15.267  1.00 81.29           N  
ANISOU 1817  N   GLY A 259    13885   9142   7858   4077   -407  -1003       N  
ATOM   1818  CA  GLY A 259       5.024 -47.151 -13.900  1.00 83.12           C  
ANISOU 1818  CA  GLY A 259    14267   9187   8127   4217   -516   -906       C  
ATOM   1819  C   GLY A 259       4.132 -46.446 -12.895  1.00 81.11           C  
ANISOU 1819  C   GLY A 259    14076   8759   7982   3827   -569   -767       C  
ATOM   1820  O   GLY A 259       4.563 -46.137 -11.786  1.00 81.23           O  
ANISOU 1820  O   GLY A 259    13993   8858   8012   3841   -654   -652       O  
ATOM   1821  N   TYR A 260       2.887 -46.188 -13.282  1.00 79.62           N  
ANISOU 1821  N   TYR A 260    14039   8355   7857   3486   -521   -787       N  
ATOM   1822  CA  TYR A 260       1.915 -45.615 -12.360  1.00 77.89           C  
ANISOU 1822  CA  TYR A 260    13907   7955   7734   3138   -561   -681       C  
ATOM   1823  C   TYR A 260       0.507 -46.104 -12.651  1.00 76.82           C  
ANISOU 1823  C   TYR A 260    14117   7441   7631   2915   -523   -723       C  
ATOM   1824  O   TYR A 260       0.214 -46.561 -13.751  1.00 77.19           O  
ANISOU 1824  O   TYR A 260    14267   7420   7642   2939   -458   -838       O  
ATOM   1825  CB  TYR A 260       1.947 -44.086 -12.413  1.00 76.58           C  
ANISOU 1825  CB  TYR A 260    13363   8089   7646   2840   -549   -612       C  
ATOM   1826  CG  TYR A 260       3.175 -43.483 -11.783  1.00 78.20           C  
ANISOU 1826  CG  TYR A 260    13243   8634   7836   2962   -616   -541       C  
ATOM   1827  CD1 TYR A 260       3.256 -43.302 -10.414  1.00 78.31           C  
ANISOU 1827  CD1 TYR A 260    13277   8610   7867   2929   -709   -463       C  
ATOM   1828  CD2 TYR A 260       4.256 -43.100 -12.555  1.00 79.81           C  
ANISOU 1828  CD2 TYR A 260    13104   9229   7990   3097   -588   -551       C  
ATOM   1829  CE1 TYR A 260       4.383 -42.762  -9.833  1.00 79.43           C  
ANISOU 1829  CE1 TYR A 260    13117   9079   7984   3025   -782   -406       C  
ATOM   1830  CE2 TYR A 260       5.384 -42.553 -11.985  1.00 80.99           C  
ANISOU 1830  CE2 TYR A 260    12940   9712   8119   3184   -657   -479       C  
ATOM   1831  CZ  TYR A 260       5.442 -42.386 -10.625  1.00 80.61           C  
ANISOU 1831  CZ  TYR A 260    12928   9603   8097   3145   -758   -412       C  
ATOM   1832  OH  TYR A 260       6.564 -41.844 -10.056  1.00 81.68           O  
ANISOU 1832  OH  TYR A 260    12746  10086   8202   3215   -837   -348       O  
ATOM   1833  N   HIS A 261      -0.361 -46.005 -11.653  1.00 75.60           N  
ANISOU 1833  N   HIS A 261    14125   7070   7529   2690   -566   -634       N  
ATOM   1834  CA  HIS A 261      -1.776 -46.282 -11.844  1.00 74.19           C  
ANISOU 1834  CA  HIS A 261    14216   6588   7383   2413   -533   -647       C  
ATOM   1835  C   HIS A 261      -2.602 -45.166 -11.228  1.00 71.45           C  
ANISOU 1835  C   HIS A 261    13731   6296   7121   2055   -531   -563       C  
ATOM   1836  O   HIS A 261      -2.065 -44.132 -10.843  1.00 70.76           O  
ANISOU 1836  O   HIS A 261    13340   6467   7077   2014   -552   -521       O  
ATOM   1837  CB  HIS A 261      -2.154 -47.633 -11.242  1.00 75.93           C  
ANISOU 1837  CB  HIS A 261    14858   6426   7565   2522   -588   -625       C  
ATOM   1838  CG  HIS A 261      -1.613 -48.798 -12.006  1.00 78.63           C  
ANISOU 1838  CG  HIS A 261    15303   6714   7858   2788   -585   -716       C  
ATOM   1839  ND1 HIS A 261      -2.340 -49.454 -12.977  1.00 79.25           N  
ANISOU 1839  ND1 HIS A 261    15484   6689   7939   2640   -539   -790       N  
ATOM   1840  CD2 HIS A 261      -0.410 -49.418 -11.954  1.00 81.10           C  
ANISOU 1840  CD2 HIS A 261    15621   7074   8120   3204   -625   -755       C  
ATOM   1841  CE1 HIS A 261      -1.612 -50.431 -13.486  1.00 82.03           C  
ANISOU 1841  CE1 HIS A 261    15916   7002   8249   2946   -552   -887       C  
ATOM   1842  NE2 HIS A 261      -0.437 -50.430 -12.883  1.00 83.34           N  
ANISOU 1842  NE2 HIS A 261    16018   7265   8384   3296   -600   -866       N  
ATOM   1843  N   THR A 262      -3.909 -45.374 -11.141  1.00 70.07           N  
ANISOU 1843  N   THR A 262    13776   5880   6968   1798   -510   -547       N  
ATOM   1844  CA  THR A 262      -4.801 -44.343 -10.636  1.00 53.20           C  
ANISOU 1844  CA  THR A 262    11510   3794   4910   1477   -497   -490       C  
ATOM   1845  C   THR A 262      -4.502 -44.041  -9.176  1.00 71.06           C  
ANISOU 1845  C   THR A 262    13722   6117   7161   1499   -567   -414       C  
ATOM   1846  O   THR A 262      -4.404 -44.946  -8.361  1.00 54.76           O  
ANISOU 1846  O   THR A 262    11888   3902   5017   1622   -620   -358       O  
ATOM   1847  CB  THR A 262      -6.270 -44.745 -10.798  1.00 52.56           C  
ANISOU 1847  CB  THR A 262    11606   3530   4834   1196   -458   -465       C  
ATOM   1848  OG1 THR A 262      -6.529 -45.043 -12.173  1.00 52.75           O  
ANISOU 1848  OG1 THR A 262    11628   3561   4855   1158   -401   -532       O  
ATOM   1849  CG2 THR A 262      -7.174 -43.618 -10.377  1.00 50.42           C  
ANISOU 1849  CG2 THR A 262    11182   3330   4646    908   -436   -429       C  
ATOM   1850  N   GLN A 263      -4.345 -42.761  -8.859  1.00 69.88           N  
ANISOU 1850  N   GLN A 263    13271   6190   7090   1375   -574   -411       N  
ATOM   1851  CA  GLN A 263      -4.074 -42.340  -7.490  1.00 70.14           C  
ANISOU 1851  CA  GLN A 263    13227   6321   7102   1372   -641   -371       C  
ATOM   1852  C   GLN A 263      -5.369 -42.176  -6.713  1.00 70.06           C  
ANISOU 1852  C   GLN A 263    13336   6191   7092   1118   -625   -348       C  
ATOM   1853  O   GLN A 263      -5.690 -41.078  -6.267  1.00 68.74           O  
ANISOU 1853  O   GLN A 263    12975   6144   6998    951   -626   -382       O  
ATOM   1854  CB  GLN A 263      -3.297 -41.025  -7.480  1.00 68.74           C  
ANISOU 1854  CB  GLN A 263    12679   6424   7015   1344   -669   -402       C  
ATOM   1855  CG  GLN A 263      -2.111 -41.005  -8.431  1.00 69.09           C  
ANISOU 1855  CG  GLN A 263    12538   6651   7061   1540   -667   -415       C  
ATOM   1856  CD  GLN A 263      -1.070 -42.049  -8.092  1.00 70.61           C  
ANISOU 1856  CD  GLN A 263    12829   6875   7126   1875   -717   -390       C  
ATOM   1857  OE1 GLN A 263      -1.185 -43.204  -8.487  1.00 71.53           O  
ANISOU 1857  OE1 GLN A 263    13202   6803   7174   2035   -695   -397       O  
ATOM   1858  NE2 GLN A 263      -0.044 -41.645  -7.356  1.00 71.27           N  
ANISOU 1858  NE2 GLN A 263    12707   7190   7180   1987   -795   -366       N  
ATOM   1859  N   ILE A 264      -6.102 -43.276  -6.556  1.00 71.74           N  
ANISOU 1859  N   ILE A 264    13865   6169   7223   1091   -614   -295       N  
ATOM   1860  CA  ILE A 264      -7.374 -43.259  -5.846  1.00 71.91           C  
ANISOU 1860  CA  ILE A 264    14003   6104   7215    845   -592   -254       C  
ATOM   1861  C   ILE A 264      -7.166 -42.795  -4.412  1.00 72.43           C  
ANISOU 1861  C   ILE A 264    13972   6333   7216    839   -646   -230       C  
ATOM   1862  O   ILE A 264      -7.948 -42.007  -3.886  1.00 71.07           O  
ANISOU 1862  O   ILE A 264    13690   6247   7065    640   -618   -266       O  
ATOM   1863  CB  ILE A 264      -8.046 -44.646  -5.847  1.00 73.86           C  
ANISOU 1863  CB  ILE A 264    14607   6086   7371    814   -592   -170       C  
ATOM   1864  CG1 ILE A 264      -8.079 -45.231  -7.260  1.00 74.05           C  
ANISOU 1864  CG1 ILE A 264    14604   6095   7438    831   -544   -208       C  
ATOM   1865  CG2 ILE A 264      -9.451 -44.559  -5.274  1.00 73.65           C  
ANISOU 1865  CG2 ILE A 264    14620   6057   7309    514   -551   -117       C  
ATOM   1866  CD1 ILE A 264      -8.879 -46.513  -7.383  1.00 75.38           C  
ANISOU 1866  CD1 ILE A 264    14967   6134   7542    722   -538   -144       C  
ATOM   1867  N   THR A 265      -6.095 -43.282  -3.795  1.00 74.51           N  
ANISOU 1867  N   THR A 265    14264   6655   7391   1073   -724   -179       N  
ATOM   1868  CA  THR A 265      -5.751 -42.899  -2.433  1.00 75.31           C  
ANISOU 1868  CA  THR A 265    14265   6949   7401   1087   -789   -157       C  
ATOM   1869  C   THR A 265      -4.553 -41.954  -2.439  1.00 75.54           C  
ANISOU 1869  C   THR A 265    13983   7228   7490   1209   -839   -240       C  
ATOM   1870  O   THR A 265      -3.496 -42.262  -1.890  1.00 76.91           O  
ANISOU 1870  O   THR A 265    14121   7525   7578   1417   -920   -192       O  
ATOM   1871  CB  THR A 265      -5.437 -44.128  -1.567  1.00 77.22           C  
ANISOU 1871  CB  THR A 265    14755   7108   7479   1243   -863     -4       C  
ATOM   1872  OG1 THR A 265      -6.345 -45.185  -1.892  1.00 77.47           O  
ANISOU 1872  OG1 THR A 265    15104   6848   7484   1157   -830     86       O  
ATOM   1873  CG2 THR A 265      -5.581 -43.794  -0.101  1.00 78.12           C  
ANISOU 1873  CG2 THR A 265    14806   7419   7456   1160   -910     34       C  
ATOM   1874  N   GLY A 266      -4.726 -40.805  -3.080  1.00 74.62           N  
ANISOU 1874  N   GLY A 266    13639   7187   7527   1069   -797   -348       N  
ATOM   1875  CA  GLY A 266      -3.720 -39.762  -3.059  1.00 75.37           C  
ANISOU 1875  CA  GLY A 266    13428   7511   7700   1111   -850   -422       C  
ATOM   1876  C   GLY A 266      -4.124 -38.669  -2.093  1.00 75.90           C  
ANISOU 1876  C   GLY A 266    13344   7701   7794    931   -876   -520       C  
ATOM   1877  O   GLY A 266      -5.202 -38.725  -1.509  1.00 76.10           O  
ANISOU 1877  O   GLY A 266    13487   7659   7769    790   -837   -533       O  
ATOM   1878  N   PRO A 267      -3.258 -37.666  -1.915  1.00 76.46           N  
ANISOU 1878  N   PRO A 267    13148   7965   7939    931   -944   -599       N  
ATOM   1879  CA  PRO A 267      -3.536 -36.543  -1.017  1.00 76.65           C  
ANISOU 1879  CA  PRO A 267    13021   8098   8005    771   -983   -735       C  
ATOM   1880  C   PRO A 267      -4.499 -35.547  -1.644  1.00 75.20           C  
ANISOU 1880  C   PRO A 267    12753   7790   8028    565   -921   -825       C  
ATOM   1881  O   PRO A 267      -4.154 -34.382  -1.821  1.00 75.20           O  
ANISOU 1881  O   PRO A 267    12534   7844   8196    477   -967   -917       O  
ATOM   1882  CB  PRO A 267      -2.164 -35.894  -0.851  1.00 77.91           C  
ANISOU 1882  CB  PRO A 267    12930   8476   8195    839  -1090   -774       C  
ATOM   1883  CG  PRO A 267      -1.461 -36.202  -2.113  1.00 77.62           C  
ANISOU 1883  CG  PRO A 267    12835   8427   8229    954  -1068   -679       C  
ATOM   1884  CD  PRO A 267      -1.918 -37.571  -2.516  1.00 77.41           C  
ANISOU 1884  CD  PRO A 267    13090   8228   8095   1085   -995   -569       C  
ATOM   1885  N   TRP A 268      -5.700 -36.006  -1.972  1.00 74.11           N  
ANISOU 1885  N   TRP A 268    12790   7485   7885    486   -827   -788       N  
ATOM   1886  CA  TRP A 268      -6.706 -35.142  -2.564  1.00 72.42           C  
ANISOU 1886  CA  TRP A 268    12499   7161   7856    310   -767   -854       C  
ATOM   1887  C   TRP A 268      -7.499 -34.475  -1.457  1.00 72.69           C  
ANISOU 1887  C   TRP A 268    12499   7247   7874    200   -767   -995       C  
ATOM   1888  O   TRP A 268      -8.353 -33.630  -1.713  1.00 72.20           O  
ANISOU 1888  O   TRP A 268    12352   7111   7969     75   -729  -1079       O  
ATOM   1889  CB  TRP A 268      -7.637 -35.962  -3.452  1.00 71.33           C  
ANISOU 1889  CB  TRP A 268    12545   6854   7702    269   -671   -750       C  
ATOM   1890  CG  TRP A 268      -6.911 -36.895  -4.348  1.00 71.38           C  
ANISOU 1890  CG  TRP A 268    12645   6816   7660    412   -666   -638       C  
ATOM   1891  CD1 TRP A 268      -6.761 -38.235  -4.181  1.00 72.39           C  
ANISOU 1891  CD1 TRP A 268    13011   6879   7616    540   -662   -548       C  
ATOM   1892  CD2 TRP A 268      -6.217 -36.558  -5.552  1.00 71.09           C  
ANISOU 1892  CD2 TRP A 268    12463   6804   7745    452   -669   -610       C  
ATOM   1893  NE1 TRP A 268      -6.020 -38.759  -5.212  1.00 72.86           N  
ANISOU 1893  NE1 TRP A 268    13087   6912   7686    681   -658   -496       N  
ATOM   1894  CE2 TRP A 268      -5.673 -37.747  -6.068  1.00 71.89           C  
ANISOU 1894  CE2 TRP A 268    12717   6871   7725    626   -656   -531       C  
ATOM   1895  CE3 TRP A 268      -6.006 -35.366  -6.245  1.00 70.61           C  
ANISOU 1895  CE3 TRP A 268    12154   6793   7881    355   -684   -636       C  
ATOM   1896  CZ2 TRP A 268      -4.929 -37.778  -7.247  1.00 71.77           C  
ANISOU 1896  CZ2 TRP A 268    12600   6914   7757    715   -645   -498       C  
ATOM   1897  CZ3 TRP A 268      -5.268 -35.399  -7.415  1.00 70.56           C  
ANISOU 1897  CZ3 TRP A 268    12044   6847   7919    416   -678   -566       C  
ATOM   1898  CH2 TRP A 268      -4.740 -36.595  -7.904  1.00 70.96           C  
ANISOU 1898  CH2 TRP A 268    12234   6905   7821    599   -652   -509       C  
ATOM   1899  N   HIS A 269      -7.197 -34.864  -0.221  1.00 73.78           N  
ANISOU 1899  N   HIS A 269    12693   7530   7811    262   -812  -1022       N  
ATOM   1900  CA  HIS A 269      -7.862 -34.326   0.960  1.00 74.40           C  
ANISOU 1900  CA  HIS A 269    12735   7719   7813    179   -811  -1173       C  
ATOM   1901  C   HIS A 269      -7.368 -32.919   1.269  1.00 75.19           C  
ANISOU 1901  C   HIS A 269    12602   7891   8075    135   -892  -1376       C  
ATOM   1902  O   HIS A 269      -7.810 -32.288   2.229  1.00 76.17           O  
ANISOU 1902  O   HIS A 269    12667   8113   8160     79   -903  -1558       O  
ATOM   1903  CB  HIS A 269      -7.604 -35.234   2.159  1.00 75.51           C  
ANISOU 1903  CB  HIS A 269    13003   8027   7661    256   -843  -1112       C  
ATOM   1904  CG  HIS A 269      -6.158 -35.346   2.531  1.00 76.10           C  
ANISOU 1904  CG  HIS A 269    13005   8248   7662    394   -958  -1089       C  
ATOM   1905  ND1 HIS A 269      -5.340 -36.346   2.050  1.00 76.04           N  
ANISOU 1905  ND1 HIS A 269    13097   8201   7594    552   -984   -907       N  
ATOM   1906  CD2 HIS A 269      -5.386 -34.589   3.349  1.00 77.07           C  
ANISOU 1906  CD2 HIS A 269    12957   8571   7756    403  -1058  -1232       C  
ATOM   1907  CE1 HIS A 269      -4.126 -36.197   2.551  1.00 77.20           C  
ANISOU 1907  CE1 HIS A 269    13119   8536   7676    659  -1091   -922       C  
ATOM   1908  NE2 HIS A 269      -4.128 -35.139   3.342  1.00 77.81           N  
ANISOU 1908  NE2 HIS A 269    13032   8765   7767    556  -1141  -1114       N  
ATOM   1909  N   LEU A 270      -6.443 -32.446   0.443  1.00 75.02           N  
ANISOU 1909  N   LEU A 270    12449   7826   8230    155   -951  -1347       N  
ATOM   1910  CA  LEU A 270      -5.886 -31.113   0.576  1.00 75.92           C  
ANISOU 1910  CA  LEU A 270    12347   7966   8533     84  -1046  -1510       C  
ATOM   1911  C   LEU A 270      -6.827 -30.088  -0.036  1.00 75.53           C  
ANISOU 1911  C   LEU A 270    12222   7725   8751    -40  -1007  -1597       C  
ATOM   1912  O   LEU A 270      -6.891 -28.946   0.415  1.00 76.81           O  
ANISOU 1912  O   LEU A 270    12260   7864   9060   -113  -1070  -1793       O  
ATOM   1913  CB  LEU A 270      -4.522 -31.040  -0.109  1.00 76.12           C  
ANISOU 1913  CB  LEU A 270    12243   8045   8633    133  -1127  -1407       C  
ATOM   1914  CG  LEU A 270      -3.290 -31.558   0.636  1.00 77.92           C  
ANISOU 1914  CG  LEU A 270    12440   8508   8657    254  -1218  -1377       C  
ATOM   1915  CD1 LEU A 270      -3.395 -33.032   0.964  1.00 78.09           C  
ANISOU 1915  CD1 LEU A 270    12677   8579   8415    407  -1165  -1231       C  
ATOM   1916  CD2 LEU A 270      -2.032 -31.294  -0.172  1.00 78.29           C  
ANISOU 1916  CD2 LEU A 270    12306   8627   8811    280  -1289  -1285       C  
ATOM   1917  N   GLY A 271      -7.556 -30.501  -1.067  1.00 74.22           N  
ANISOU 1917  N   GLY A 271    12135   7416   8649    -59   -912  -1455       N  
ATOM   1918  CA  GLY A 271      -8.423 -29.593  -1.794  1.00 73.78           C  
ANISOU 1918  CA  GLY A 271    11998   7186   8851   -162   -879  -1490       C  
ATOM   1919  C   GLY A 271      -7.645 -28.784  -2.811  1.00 73.86           C  
ANISOU 1919  C   GLY A 271    11840   7113   9111   -216   -952  -1419       C  
ATOM   1920  O   GLY A 271      -8.033 -28.699  -3.973  1.00 72.98           O  
ANISOU 1920  O   GLY A 271    11706   6888   9136   -264   -908  -1285       O  
ATOM   1921  N   LYS A 272      -6.543 -28.188  -2.370  1.00 75.46           N  
ANISOU 1921  N   LYS A 272    11915   7396   9360   -225  -1070  -1498       N  
ATOM   1922  CA  LYS A 272      -5.693 -27.395  -3.247  1.00 76.38           C  
ANISOU 1922  CA  LYS A 272    11852   7468   9700   -305  -1154  -1414       C  
ATOM   1923  C   LYS A 272      -4.264 -27.935  -3.220  1.00 76.81           C  
ANISOU 1923  C   LYS A 272    11847   7733   9606   -233  -1215  -1323       C  
ATOM   1924  O   LYS A 272      -3.607 -27.911  -2.178  1.00 78.63           O  
ANISOU 1924  O   LYS A 272    12049   8108   9717   -201  -1293  -1441       O  
ATOM   1925  CB  LYS A 272      -5.727 -25.920  -2.828  1.00 78.84           C  
ANISOU 1925  CB  LYS A 272    12029   7654  10274   -426  -1263  -1599       C  
ATOM   1926  CG  LYS A 272      -4.775 -25.014  -3.602  1.00 80.50           C  
ANISOU 1926  CG  LYS A 272    12045   7817  10724   -550  -1378  -1502       C  
ATOM   1927  CD  LYS A 272      -4.975 -23.539  -3.242  1.00 82.81           C  
ANISOU 1927  CD  LYS A 272    12242   7904  11318   -680  -1494  -1686       C  
ATOM   1928  CE  LYS A 272      -4.004 -22.647  -4.008  1.00 84.33           C  
ANISOU 1928  CE  LYS A 272    12244   8042  11755   -841  -1622  -1553       C  
ATOM   1929  NZ  LYS A 272      -4.250 -21.197  -3.782  1.00 86.50           N  
ANISOU 1929  NZ  LYS A 272    12450   8045  12370   -979  -1748  -1711       N  
ATOM   1930  N   LEU A 273      -3.792 -28.426  -4.366  1.00 74.89           N  
ANISOU 1930  N   LEU A 273    11569   7531   9355   -199  -1178  -1118       N  
ATOM   1931  CA  LEU A 273      -2.465 -29.036  -4.464  1.00 73.85           C  
ANISOU 1931  CA  LEU A 273    11367   7622   9070    -92  -1218  -1020       C  
ATOM   1932  C   LEU A 273      -1.846 -28.882  -5.851  1.00 72.38           C  
ANISOU 1932  C   LEU A 273    11026   7490   8986   -128  -1213   -833       C  
ATOM   1933  O   LEU A 273      -2.483 -28.388  -6.779  1.00 71.60           O  
ANISOU 1933  O   LEU A 273    10894   7250   9063   -239  -1175   -758       O  
ATOM   1934  CB  LEU A 273      -2.524 -30.519  -4.106  1.00 73.07           C  
ANISOU 1934  CB  LEU A 273    11476   7604   8684    105  -1143   -976       C  
ATOM   1935  CG  LEU A 273      -3.257 -31.437  -5.084  1.00 71.51           C  
ANISOU 1935  CG  LEU A 273    11442   7295   8433    164  -1017   -851       C  
ATOM   1936  CD1 LEU A 273      -2.679 -32.840  -5.031  1.00 71.98           C  
ANISOU 1936  CD1 LEU A 273    11642   7459   8249    380   -986   -767       C  
ATOM   1937  CD2 LEU A 273      -4.738 -31.472  -4.771  1.00 70.43           C  
ANISOU 1937  CD2 LEU A 273    11469   6979   8312     90   -942   -920       C  
ATOM   1938  N   GLU A 274      -0.600 -29.323  -5.981  1.00 72.14           N  
ANISOU 1938  N   GLU A 274    10887   7696   8827    -26  -1250   -752       N  
ATOM   1939  CA  GLU A 274       0.139 -29.197  -7.226  1.00 71.52           C  
ANISOU 1939  CA  GLU A 274    10622   7749   8801    -51  -1245   -579       C  
ATOM   1940  C   GLU A 274       0.946 -30.462  -7.490  1.00 71.33           C  
ANISOU 1940  C   GLU A 274    10630   7947   8527    194  -1194   -497       C  
ATOM   1941  O   GLU A 274       2.022 -30.655  -6.925  1.00 72.57           O  
ANISOU 1941  O   GLU A 274    10681   8326   8568    293  -1265   -506       O  
ATOM   1942  CB  GLU A 274       1.073 -27.987  -7.165  1.00 72.95           C  
ANISOU 1942  CB  GLU A 274    10528   8038   9152   -230  -1383   -565       C  
ATOM   1943  CG  GLU A 274       1.710 -27.614  -8.495  1.00 73.22           C  
ANISOU 1943  CG  GLU A 274    10336   8213   9273   -322  -1383   -360       C  
ATOM   1944  CD  GLU A 274       0.735 -26.946  -9.441  1.00 71.83           C  
ANISOU 1944  CD  GLU A 274    10166   7813   9315   -489  -1344   -272       C  
ATOM   1945  OE1 GLU A 274      -0.200 -26.274  -8.963  1.00 71.15           O  
ANISOU 1945  OE1 GLU A 274    10173   7455   9406   -596  -1372   -382       O  
ATOM   1946  OE2 GLU A 274       0.904 -27.091 -10.666  1.00 71.61           O  
ANISOU 1946  OE2 GLU A 274    10036   7899   9272   -503  -1287    -92       O  
ATOM   1947  N   MET A 275       0.415 -31.324  -8.348  1.00 70.04           N  
ANISOU 1947  N   MET A 275    10612   7719   8280    297  -1076   -428       N  
ATOM   1948  CA  MET A 275       1.095 -32.558  -8.712  1.00 70.36           C  
ANISOU 1948  CA  MET A 275    10708   7923   8102    553  -1022   -372       C  
ATOM   1949  C   MET A 275       2.156 -32.296  -9.768  1.00 70.98           C  
ANISOU 1949  C   MET A 275    10510   8275   8184    561  -1027   -249       C  
ATOM   1950  O   MET A 275       1.917 -31.576 -10.736  1.00 70.78           O  
ANISOU 1950  O   MET A 275    10351   8244   8298    384  -1009   -161       O  
ATOM   1951  CB  MET A 275       0.094 -33.583  -9.242  1.00 69.38           C  
ANISOU 1951  CB  MET A 275    10860   7610   7891    643   -902   -370       C  
ATOM   1952  CG  MET A 275       0.736 -34.840  -9.787  1.00 70.58           C  
ANISOU 1952  CG  MET A 275    11088   7883   7846    915   -846   -333       C  
ATOM   1953  SD  MET A 275      -0.390 -35.857 -10.754  1.00 98.42           S  
ANISOU 1953  SD  MET A 275    14900  11191  11306    957   -718   -334       S  
ATOM   1954  CE  MET A 275      -1.707 -36.117  -9.576  1.00 48.92           C  
ANISOU 1954  CE  MET A 275     8926   4617   5043    866   -717   -409       C  
ATOM   1955  N   ASP A 276       3.332 -32.878  -9.572  1.00 71.97           N  
ANISOU 1955  N   ASP A 276    10535   8662   8146    771  -1055   -230       N  
ATOM   1956  CA  ASP A 276       4.390 -32.808 -10.572  1.00 72.80           C  
ANISOU 1956  CA  ASP A 276    10367   9091   8203    823  -1043   -116       C  
ATOM   1957  C   ASP A 276       5.260 -34.053 -10.503  1.00 73.59           C  
ANISOU 1957  C   ASP A 276    10500   9394   8066   1181  -1014   -127       C  
ATOM   1958  O   ASP A 276       5.011 -34.944  -9.694  1.00 73.18           O  
ANISOU 1958  O   ASP A 276    10699   9198   7909   1369  -1012   -203       O  
ATOM   1959  CB  ASP A 276       5.235 -31.544 -10.397  1.00 73.69           C  
ANISOU 1959  CB  ASP A 276    10144   9407   8447    600  -1164    -52       C  
ATOM   1960  CG  ASP A 276       5.813 -31.416  -9.004  1.00 74.22           C  
ANISOU 1960  CG  ASP A 276    10184   9542   8476    631  -1283   -141       C  
ATOM   1961  OD1 ASP A 276       5.097 -31.724  -8.030  1.00 73.45           O  
ANISOU 1961  OD1 ASP A 276    10335   9215   8358    670  -1291   -261       O  
ATOM   1962  OD2 ASP A 276       6.984 -31.003  -8.883  1.00 75.54           O  
ANISOU 1962  OD2 ASP A 276    10065  10019   8618    603  -1371    -85       O  
ATOM   1963  N   PHE A 277       6.274 -34.118 -11.355  1.00 75.16           N  
ANISOU 1963  N   PHE A 277    10440   9936   8180   1281   -992    -43       N  
ATOM   1964  CA  PHE A 277       7.125 -35.296 -11.400  1.00 77.06           C  
ANISOU 1964  CA  PHE A 277    10693  10383   8204   1660   -958    -63       C  
ATOM   1965  C   PHE A 277       8.582 -34.968 -11.131  1.00 78.98           C  
ANISOU 1965  C   PHE A 277    10577  11057   8376   1731  -1043      3       C  
ATOM   1966  O   PHE A 277       9.380 -34.801 -12.049  1.00 80.20           O  
ANISOU 1966  O   PHE A 277    10442  11560   8470   1760  -1010     87       O  
ATOM   1967  CB  PHE A 277       6.948 -36.029 -12.723  1.00 78.15           C  
ANISOU 1967  CB  PHE A 277    10892  10559   8244   1816   -825    -65       C  
ATOM   1968  CG  PHE A 277       5.632 -36.729 -12.835  1.00 77.08           C  
ANISOU 1968  CG  PHE A 277    11151  10014   8122   1829   -751   -150       C  
ATOM   1969  CD1 PHE A 277       4.514 -36.056 -13.289  1.00 75.28           C  
ANISOU 1969  CD1 PHE A 277    10990   9571   8041   1529   -719   -129       C  
ATOM   1970  CD2 PHE A 277       5.506 -38.054 -12.458  1.00 78.14           C  
ANISOU 1970  CD2 PHE A 277    11588   9973   8127   2134   -724   -240       C  
ATOM   1971  CE1 PHE A 277       3.297 -36.695 -13.385  1.00 73.98           C  
ANISOU 1971  CE1 PHE A 277    11166   9065   7879   1522   -655   -200       C  
ATOM   1972  CE2 PHE A 277       4.292 -38.696 -12.547  1.00 76.87           C  
ANISOU 1972  CE2 PHE A 277    11788   9439   7979   2109   -666   -306       C  
ATOM   1973  CZ  PHE A 277       3.185 -38.016 -13.015  1.00 74.70           C  
ANISOU 1973  CZ  PHE A 277    11556   8991   7835   1796   -628   -289       C  
ATOM   1974  N   ASP A 278       8.907 -34.881  -9.847  1.00 79.51           N  
ANISOU 1974  N   ASP A 278    10654  11124   8432   1748  -1155    -32       N  
ATOM   1975  CA  ASP A 278      10.247 -34.562  -9.392  1.00 82.14           C  
ANISOU 1975  CA  ASP A 278    10654  11864   8693   1794  -1259     24       C  
ATOM   1976  C   ASP A 278      10.378 -35.103  -7.975  1.00 83.19           C  
ANISOU 1976  C   ASP A 278    10944  11930   8733   1961  -1348    -42       C  
ATOM   1977  O   ASP A 278       9.409 -35.609  -7.411  1.00 81.63           O  
ANISOU 1977  O   ASP A 278    11096  11378   8542   1999  -1325   -117       O  
ATOM   1978  CB  ASP A 278      10.459 -33.047  -9.413  1.00 81.93           C  
ANISOU 1978  CB  ASP A 278    10342  11944   8846   1380  -1354     88       C  
ATOM   1979  CG  ASP A 278      11.901 -32.654  -9.174  1.00 84.47           C  
ANISOU 1979  CG  ASP A 278    10265  12740   9089   1378  -1459    169       C  
ATOM   1980  OD1 ASP A 278      12.790 -33.508  -9.361  1.00 86.20           O  
ANISOU 1980  OD1 ASP A 278    10363  13278   9111   1711  -1426    202       O  
ATOM   1981  OD2 ASP A 278      12.145 -31.489  -8.805  1.00 85.01           O  
ANISOU 1981  OD2 ASP A 278    10137  12864   9298   1044  -1579    197       O  
ATOM   1982  N   PHE A 279      11.572 -35.010  -7.403  1.00 85.86           N  
ANISOU 1982  N   PHE A 279    11014  12638   8971   2053  -1452      1       N  
ATOM   1983  CA  PHE A 279      11.778 -35.440  -6.030  1.00 86.68           C  
ANISOU 1983  CA  PHE A 279    11226  12739   8970   2192  -1554    -39       C  
ATOM   1984  C   PHE A 279      11.300 -34.366  -5.070  1.00 85.99           C  
ANISOU 1984  C   PHE A 279    11150  12513   9010   1829  -1662   -113       C  
ATOM   1985  O   PHE A 279      11.486 -33.177  -5.320  1.00 85.94           O  
ANISOU 1985  O   PHE A 279    10908  12595   9149   1505  -1718   -104       O  
ATOM   1986  CB  PHE A 279      13.257 -35.718  -5.766  1.00 89.49           C  
ANISOU 1986  CB  PHE A 279    11261  13581   9158   2427  -1635     38       C  
ATOM   1987  CG  PHE A 279      13.838 -36.798  -6.627  1.00 90.65           C  
ANISOU 1987  CG  PHE A 279    11373  13904   9166   2840  -1536     86       C  
ATOM   1988  CD1 PHE A 279      13.522 -38.126  -6.400  1.00 90.67           C  
ANISOU 1988  CD1 PHE A 279    11706  13679   9067   3216  -1489     55       C  
ATOM   1989  CD2 PHE A 279      14.721 -36.485  -7.648  1.00 92.09           C  
ANISOU 1989  CD2 PHE A 279    11187  14488   9316   2855  -1496    159       C  
ATOM   1990  CE1 PHE A 279      14.064 -39.124  -7.187  1.00 92.40           C  
ANISOU 1990  CE1 PHE A 279    11907  14032   9170   3621  -1404     66       C  
ATOM   1991  CE2 PHE A 279      15.266 -37.476  -8.437  1.00 93.75           C  
ANISOU 1991  CE2 PHE A 279    11353  14886   9383   3262  -1398    170       C  
ATOM   1992  CZ  PHE A 279      14.938 -38.798  -8.206  1.00 93.93           C  
ANISOU 1992  CZ  PHE A 279    11724  14645   9319   3657  -1354    109       C  
ATOM   1993  N   CYS A 280      10.683 -34.785  -3.972  1.00 85.99           N  
ANISOU 1993  N   CYS A 280    11425  12294   8954   1882  -1696   -188       N  
ATOM   1994  CA  CYS A 280      10.366 -33.856  -2.901  1.00 86.41           C  
ANISOU 1994  CA  CYS A 280    11472  12283   9077   1593  -1809   -290       C  
ATOM   1995  C   CYS A 280      11.679 -33.295  -2.386  1.00 89.60           C  
ANISOU 1995  C   CYS A 280    11512  13118   9414   1536  -1959   -262       C  
ATOM   1996  O   CYS A 280      12.711 -33.961  -2.460  1.00 91.75           O  
ANISOU 1996  O   CYS A 280    11618  13717   9524   1809  -1980   -162       O  
ATOM   1997  CB  CYS A 280       9.617 -34.555  -1.770  1.00 86.13           C  
ANISOU 1997  CB  CYS A 280    11762  12036   8928   1703  -1817   -354       C  
ATOM   1998  SG  CYS A 280       7.946 -35.093  -2.176  1.00 96.78           S  
ANISOU 1998  SG  CYS A 280    13534  12881  10357   1689  -1661   -396       S  
ATOM   1999  N   ASP A 281      11.645 -32.069  -1.879  1.00 90.08           N  
ANISOU 1999  N   ASP A 281    11444  13181   9602   1184  -2069   -357       N  
ATOM   2000  CA  ASP A 281      12.854 -31.421  -1.392  1.00 93.16           C  
ANISOU 2000  CA  ASP A 281    11481  13971   9943   1063  -2229   -342       C  
ATOM   2001  C   ASP A 281      13.485 -32.208  -0.248  1.00 96.09           C  
ANISOU 2001  C   ASP A 281    11849  14604  10057   1319  -2318   -334       C  
ATOM   2002  O   ASP A 281      12.829 -32.508   0.748  1.00 95.76           O  
ANISOU 2002  O   ASP A 281    12056  14395   9935   1353  -2338   -428       O  
ATOM   2003  CB  ASP A 281      12.546 -29.990  -0.953  1.00 92.53           C  
ANISOU 2003  CB  ASP A 281    11334  13760  10063    630  -2342   -485       C  
ATOM   2004  CG  ASP A 281      12.057 -29.128  -2.096  1.00 90.76           C  
ANISOU 2004  CG  ASP A 281    11070  13306  10109    369  -2282   -452       C  
ATOM   2005  OD1 ASP A 281      12.533 -29.329  -3.232  1.00 90.87           O  
ANISOU 2005  OD1 ASP A 281    10920  13478  10129    441  -2208   -288       O  
ATOM   2006  OD2 ASP A 281      11.197 -28.254  -1.865  1.00 89.42           O  
ANISOU 2006  OD2 ASP A 281    11027  12810  10139    105  -2309   -588       O  
ATOM   2007  N   GLY A 282      14.756 -32.559  -0.410  1.00 99.36           N  
ANISOU 2007  N   GLY A 282    11968  15456  10329   1506  -2370   -207       N  
ATOM   2008  CA  GLY A 282      15.491 -33.255   0.629  1.00102.85           C  
ANISOU 2008  CA  GLY A 282    12352  16201  10526   1756  -2474   -167       C  
ATOM   2009  C   GLY A 282      15.197 -34.739   0.731  1.00104.07           C  
ANISOU 2009  C   GLY A 282    12793  16223  10527   2199  -2384    -87       C  
ATOM   2010  O   GLY A 282      15.529 -35.369   1.733  1.00105.81           O  
ANISOU 2010  O   GLY A 282    13053  16596  10553   2402  -2471    -48       O  
ATOM   2011  N   THR A 283      14.579 -35.302  -0.302  1.00103.83           N  
ANISOU 2011  N   THR A 283    12963  15906  10581   2342  -2220    -56       N  
ATOM   2012  CA  THR A 283      14.272 -36.729  -0.307  1.00105.49           C  
ANISOU 2012  CA  THR A 283    13472  15935  10675   2750  -2139     13       C  
ATOM   2013  C   THR A 283      14.906 -37.446  -1.491  1.00108.53           C  
ANISOU 2013  C   THR A 283    13748  16455  11034   3076  -2041    105       C  
ATOM   2014  O   THR A 283      15.190 -36.839  -2.521  1.00107.90           O  
ANISOU 2014  O   THR A 283    13440  16505  11053   2939  -1984    109       O  
ATOM   2015  CB  THR A 283      12.763 -36.984  -0.334  1.00102.38           C  
ANISOU 2015  CB  THR A 283    13507  15014  10378   2658  -2032    -64       C  
ATOM   2016  OG1 THR A 283      12.203 -36.414  -1.523  1.00100.29           O  
ANISOU 2016  OG1 THR A 283    13241  14556  10308   2458  -1916   -110       O  
ATOM   2017  CG2 THR A 283      12.101 -36.364   0.879  1.00101.65           C  
ANISOU 2017  CG2 THR A 283    13527  14815  10282   2381  -2116   -171       C  
ATOM   2018  N   THR A 284      15.125 -38.746  -1.331  1.00112.46           N  
ANISOU 2018  N   THR A 284    14411  16924  11393   3511  -2024    182       N  
ATOM   2019  CA  THR A 284      15.702 -39.566  -2.386  1.00116.28           C  
ANISOU 2019  CA  THR A 284    14828  17516  11836   3887  -1929    235       C  
ATOM   2020  C   THR A 284      14.830 -40.797  -2.621  1.00118.70           C  
ANISOU 2020  C   THR A 284    15596  17357  12149   4160  -1830    223       C  
ATOM   2021  O   THR A 284      14.475 -41.500  -1.676  1.00119.75           O  
ANISOU 2021  O   THR A 284    16002  17288  12210   4293  -1890    268       O  
ATOM   2022  CB  THR A 284      17.126 -40.018  -2.024  1.00119.67           C  
ANISOU 2022  CB  THR A 284    14944  18439  12087   4236  -2031    344       C  
ATOM   2023  OG1 THR A 284      17.088 -40.802  -0.825  1.00120.90           O  
ANISOU 2023  OG1 THR A 284    15309  18507  12119   4454  -2133    412       O  
ATOM   2024  CG2 THR A 284      18.029 -38.815  -1.802  1.00120.74           C  
ANISOU 2024  CG2 THR A 284    14606  19060  12208   3939  -2141    363       C  
ATOM   2025  N   VAL A 285      14.477 -41.050  -3.878  1.00119.74           N  
ANISOU 2025  N   VAL A 285    15812  17325  12359   4222  -1685    169       N  
ATOM   2026  CA  VAL A 285      13.678 -42.223  -4.225  1.00119.51           C  
ANISOU 2026  CA  VAL A 285    16217  16850  12343   4465  -1594    140       C  
ATOM   2027  C   VAL A 285      14.448 -43.118  -5.190  1.00121.34           C  
ANISOU 2027  C   VAL A 285    16373  17227  12504   4917  -1522    132       C  
ATOM   2028  O   VAL A 285      15.020 -42.638  -6.168  1.00123.03           O  
ANISOU 2028  O   VAL A 285    16271  17757  12718   4897  -1455    102       O  
ATOM   2029  CB  VAL A 285      12.331 -41.828  -4.867  1.00116.29           C  
ANISOU 2029  CB  VAL A 285    16052  16045  12087   4129  -1479     45       C  
ATOM   2030  CG1 VAL A 285      11.454 -43.054  -5.076  1.00115.72           C  
ANISOU 2030  CG1 VAL A 285    16448  15500  12022   4335  -1408     18       C  
ATOM   2031  CG2 VAL A 285      11.613 -40.807  -4.006  1.00114.39           C  
ANISOU 2031  CG2 VAL A 285    15834  15703  11926   3690  -1541     25       C  
ATOM   2032  N   VAL A 286      14.471 -44.417  -4.909  1.00119.49           N  
ANISOU 2032  N   VAL A 286    16424  16769  12206   5327  -1541    161       N  
ATOM   2033  CA  VAL A 286      15.118 -45.371  -5.801  1.00119.61           C  
ANISOU 2033  CA  VAL A 286    16423  16858  12165   5804  -1473    116       C  
ATOM   2034  C   VAL A 286      14.134 -46.457  -6.212  1.00117.68           C  
ANISOU 2034  C   VAL A 286    16688  16042  11984   5956  -1398     38       C  
ATOM   2035  O   VAL A 286      13.089 -46.620  -5.591  1.00116.27           O  
ANISOU 2035  O   VAL A 286    16865  15445  11867   5747  -1423     65       O  
ATOM   2036  CB  VAL A 286      16.349 -46.018  -5.144  1.00123.36           C  
ANISOU 2036  CB  VAL A 286    16718  17647  12505   6261  -1588    224       C  
ATOM   2037  CG1 VAL A 286      17.430 -44.978  -4.902  1.00124.24           C  
ANISOU 2037  CG1 VAL A 286    16280  18386  12538   6121  -1659    292       C  
ATOM   2038  CG2 VAL A 286      15.957 -46.699  -3.844  1.00124.04           C  
ANISOU 2038  CG2 VAL A 286    17138  17420  12571   6348  -1713    344       C  
ATOM   2039  N   VAL A 287      14.462 -47.193  -7.265  1.00118.09           N  
ANISOU 2039  N   VAL A 287    16769  16090  12012   6310  -1306    -70       N  
ATOM   2040  CA  VAL A 287      13.607 -48.287  -7.702  1.00117.27           C  
ANISOU 2040  CA  VAL A 287    17152  15438  11966   6472  -1247   -166       C  
ATOM   2041  C   VAL A 287      14.193 -49.610  -7.234  1.00121.55           C  
ANISOU 2041  C   VAL A 287    17890  15832  12461   7025  -1334   -119       C  
ATOM   2042  O   VAL A 287      15.368 -49.892  -7.470  1.00124.93           O  
ANISOU 2042  O   VAL A 287    18038  16629  12800   7439  -1347   -127       O  
ATOM   2043  CB  VAL A 287      13.455 -48.310  -9.230  1.00116.05           C  
ANISOU 2043  CB  VAL A 287    16961  15314  11819   6499  -1090   -354       C  
ATOM   2044  CG1 VAL A 287      12.369 -49.291  -9.637  1.00115.35           C  
ANISOU 2044  CG1 VAL A 287    17401  14622  11804   6544  -1040   -467       C  
ATOM   2045  CG2 VAL A 287      13.131 -46.921  -9.746  1.00112.77           C  
ANISOU 2045  CG2 VAL A 287    16259  15147  11441   5996  -1019   -360       C  
ATOM   2046  N   THR A 288      13.380 -50.416  -6.560  1.00121.92           N  
ANISOU 2046  N   THR A 288    18407  15348  12569   7034  -1399    -54       N  
ATOM   2047  CA  THR A 288      13.830 -51.726  -6.102  1.00126.49           C  
ANISOU 2047  CA  THR A 288    19220  15704  13134   7505  -1486     11       C  
ATOM   2048  C   THR A 288      12.675 -52.691  -5.888  1.00126.40           C  
ANISOU 2048  C   THR A 288    19753  15043  13230   7320  -1478      8       C  
ATOM   2049  O   THR A 288      11.562 -52.285  -5.557  1.00123.12           O  
ANISOU 2049  O   THR A 288    19553  14364  12863   6944  -1483     56       O  
ATOM   2050  CB  THR A 288      14.642 -51.632  -4.797  1.00128.66           C  
ANISOU 2050  CB  THR A 288    19283  16276  13327   7598  -1634    228       C  
ATOM   2051  OG1 THR A 288      14.915 -52.952  -4.310  1.00101.82           O  
ANISOU 2051  OG1 THR A 288    16120  12611   9956   7836  -1676    288       O  
ATOM   2052  CG2 THR A 288      13.868 -50.866  -3.743  1.00125.80           C  
ANISOU 2052  CG2 THR A 288    18990  15850  12957   7165  -1718    375       C  
ATOM   2053  N   GLU A 289      12.957 -53.974  -6.086  1.00130.21           N  
ANISOU 2053  N   GLU A 289    20434  15290  13749   7576  -1472    -45       N  
ATOM   2054  CA  GLU A 289      12.000 -55.033  -5.804  1.00131.05           C  
ANISOU 2054  CA  GLU A 289    21018  14814  13961   7416  -1494    -16       C  
ATOM   2055  C   GLU A 289      11.788 -55.128  -4.298  1.00131.77           C  
ANISOU 2055  C   GLU A 289    21211  14808  14046   7278  -1624    247       C  
ATOM   2056  O   GLU A 289      10.698 -55.462  -3.831  1.00130.52           O  
ANISOU 2056  O   GLU A 289    21384  14255  13951   6967  -1644    327       O  
ATOM   2057  CB  GLU A 289      12.524 -56.365  -6.346  1.00135.10           C  
ANISOU 2057  CB  GLU A 289    21671  15143  14520   7766  -1487   -125       C  
ATOM   2058  CG  GLU A 289      11.737 -57.591  -5.904  1.00136.72           C  
ANISOU 2058  CG  GLU A 289    22330  14772  14846   7649  -1548    -51       C  
ATOM   2059  CD  GLU A 289      12.578 -58.855  -5.910  1.00142.22           C  
ANISOU 2059  CD  GLU A 289    23096  15350  15590   8071  -1607    -59       C  
ATOM   2060  OE1 GLU A 289      12.023 -59.946  -5.655  1.00144.68           O  
ANISOU 2060  OE1 GLU A 289    23766  15183  16022   8014  -1664     -7       O  
ATOM   2061  OE2 GLU A 289      13.797 -58.757  -6.164  1.00144.45           O  
ANISOU 2061  OE2 GLU A 289    23063  16028  15795   8456  -1598   -112       O  
ATOM   2062  N   ASP A 290      12.839 -54.814  -3.545  1.00134.08           N  
ANISOU 2062  N   ASP A 290    21189  15509  14247   7493  -1711    386       N  
ATOM   2063  CA  ASP A 290      12.805 -54.894  -2.088  1.00135.57           C  
ANISOU 2063  CA  ASP A 290    21418  15695  14398   7395  -1843    644       C  
ATOM   2064  C   ASP A 290      11.768 -53.963  -1.463  1.00132.74           C  
ANISOU 2064  C   ASP A 290    21131  15297  14007   6942  -1862    729       C  
ATOM   2065  O   ASP A 290      11.379 -54.143  -0.310  1.00133.29           O  
ANISOU 2065  O   ASP A 290    21333  15266  14046   6777  -1953    927       O  
ATOM   2066  CB  ASP A 290      14.187 -54.591  -1.503  1.00137.40           C  
ANISOU 2066  CB  ASP A 290    21231  16461  14514   7687  -1930    756       C  
ATOM   2067  CG  ASP A 290      15.219 -55.634  -1.873  1.00141.94           C  
ANISOU 2067  CG  ASP A 290    21754  17061  15115   8149  -1930    715       C  
ATOM   2068  OD1 ASP A 290      15.054 -56.286  -2.923  1.00142.85           O  
ANISOU 2068  OD1 ASP A 290    22049  16917  15313   8279  -1839    524       O  
ATOM   2069  OD2 ASP A 290      16.196 -55.800  -1.114  1.00144.83           O  
ANISOU 2069  OD2 ASP A 290    21894  17721  15413   8379  -2026    868       O  
ATOM   2070  N   CYS A 291      11.324 -52.967  -2.220  1.00129.89           N  
ANISOU 2070  N   CYS A 291    20674  15031  13648   6745  -1779    585       N  
ATOM   2071  CA  CYS A 291      10.319 -52.044  -1.716  1.00126.73           C  
ANISOU 2071  CA  CYS A 291    20342  14586  13222   6323  -1794    643       C  
ATOM   2072  C   CYS A 291       8.978 -52.753  -1.583  1.00126.04           C  
ANISOU 2072  C   CYS A 291    20703  13962  13223   6028  -1754    663       C  
ATOM   2073  O   CYS A 291       8.760 -53.795  -2.197  1.00128.00           O  
ANISOU 2073  O   CYS A 291    21189  13877  13568   6116  -1700    580       O  
ATOM   2074  CB  CYS A 291      10.188 -50.838  -2.639  1.00123.85           C  
ANISOU 2074  CB  CYS A 291    19716  14462  12879   6102  -1686    464       C  
ATOM   2075  SG  CYS A 291       9.436 -49.421  -1.839  1.00144.82           S  
ANISOU 2075  SG  CYS A 291    22201  17312  15511   5495  -1682    488       S  
ATOM   2076  N   GLY A 292       8.082 -52.190  -0.777  1.00123.21           N  
ANISOU 2076  N   GLY A 292    20441  13553  12820   5666  -1787    768       N  
ATOM   2077  CA  GLY A 292       6.780 -52.793  -0.552  1.00122.18           C  
ANISOU 2077  CA  GLY A 292    20683  12984  12754   5347  -1751    811       C  
ATOM   2078  C   GLY A 292       5.823 -52.573  -1.706  1.00118.83           C  
ANISOU 2078  C   GLY A 292    20399  12319  12431   5111  -1617    617       C  
ATOM   2079  O   GLY A 292       6.235 -52.182  -2.795  1.00118.25           O  
ANISOU 2079  O   GLY A 292    20173  12364  12394   5250  -1545    443       O  
ATOM   2080  N   ASN A 293       4.541 -52.827  -1.465  1.00116.94           N  
ANISOU 2080  N   ASN A 293    20427  11776  12228   4743  -1583    655       N  
ATOM   2081  CA  ASN A 293       3.514 -52.642  -2.486  1.00113.55           C  
ANISOU 2081  CA  ASN A 293    20120  11137  11887   4464  -1461    487       C  
ATOM   2082  C   ASN A 293       2.905 -51.241  -2.417  1.00109.28           C  
ANISOU 2082  C   ASN A 293    19454  10753  11315   4173  -1424    461       C  
ATOM   2083  O   ASN A 293       3.128 -50.512  -1.452  1.00108.91           O  
ANISOU 2083  O   ASN A 293    19209  10992  11180   4082  -1480    553       O  
ATOM   2084  CB  ASN A 293       2.424 -53.708  -2.335  1.00113.80           C  
ANISOU 2084  CB  ASN A 293    20474  10788  11977   4209  -1447    541       C  
ATOM   2085  CG  ASN A 293       1.558 -53.843  -3.578  1.00111.33           C  
ANISOU 2085  CG  ASN A 293    20269  10280  11752   3992  -1333    354       C  
ATOM   2086  OD1 ASN A 293       1.846 -53.253  -4.620  1.00109.38           O  
ANISOU 2086  OD1 ASN A 293    19870  10163  11528   4067  -1258    180       O  
ATOM   2087  ND2 ASN A 293       0.495 -54.630  -3.474  1.00111.58           N  
ANISOU 2087  ND2 ASN A 293    20542  10026  11826   3716  -1327    402       N  
ATOM   2088  N   ARG A 294       2.144 -50.869  -3.443  1.00106.16           N  
ANISOU 2088  N   ARG A 294    19089  10243  11002   3953  -1309    301       N  
ATOM   2089  CA  ARG A 294       1.491 -49.563  -3.496  1.00101.64           C  
ANISOU 2089  CA  ARG A 294    18292   9876  10450   3567  -1230    226       C  
ATOM   2090  C   ARG A 294       0.377 -49.427  -2.461  1.00 99.10           C  
ANISOU 2090  C   ARG A 294    18116   9456  10081   3223  -1248    347       C  
ATOM   2091  O   ARG A 294      -0.462 -50.316  -2.321  1.00 99.98           O  
ANISOU 2091  O   ARG A 294    18566   9231  10193   3125  -1256    431       O  
ATOM   2092  CB  ARG A 294       0.927 -49.308  -4.897  1.00100.30           C  
ANISOU 2092  CB  ARG A 294    18123   9608  10379   3427  -1107     46       C  
ATOM   2093  CG  ARG A 294       0.182 -50.493  -5.487  1.00101.89           C  
ANISOU 2093  CG  ARG A 294    18657   9437  10619   3381  -1074     13       C  
ATOM   2094  CD  ARG A 294      -0.351 -50.201  -6.882  1.00100.22           C  
ANISOU 2094  CD  ARG A 294    18394   9211  10475   3219   -957   -164       C  
ATOM   2095  NE  ARG A 294      -1.693 -49.626  -6.858  1.00 97.33           N  
ANISOU 2095  NE  ARG A 294    18048   8790  10141   2778   -897   -156       N  
ATOM   2096  CZ  ARG A 294      -1.953 -48.327  -6.954  1.00 94.34           C  
ANISOU 2096  CZ  ARG A 294    17486   8561   9799   2604   -853   -195       C  
ATOM   2097  NH1 ARG A 294      -3.206 -47.897  -6.923  1.00 92.14           N  
ANISOU 2097  NH1 ARG A 294    17224   8232   9551   2224   -799   -188       N  
ATOM   2098  NH2 ARG A 294      -0.962 -47.456  -7.082  1.00 93.84           N  
ANISOU 2098  NH2 ARG A 294    17061   8853   9742   2719   -850   -238       N  
ATOM   2099  N   GLY A 295       0.378 -48.308  -1.742  1.00 95.97           N  
ANISOU 2099  N   GLY A 295    17440   9383   9643   3023  -1252    342       N  
ATOM   2100  CA  GLY A 295      -0.657 -48.018  -0.765  1.00 93.90           C  
ANISOU 2100  CA  GLY A 295    17254   9110   9315   2700  -1253    420       C  
ATOM   2101  C   GLY A 295      -0.974 -46.536  -0.732  1.00 90.58           C  
ANISOU 2101  C   GLY A 295    16516   8963   8935   2420  -1191    281       C  
ATOM   2102  O   GLY A 295      -0.563 -45.803  -1.623  1.00 89.25           O  
ANISOU 2102  O   GLY A 295    16118   8924   8871   2432  -1141    144       O  
ATOM   2103  N   PRO A 296      -1.705 -46.087   0.299  1.00 89.38           N  
ANISOU 2103  N   PRO A 296    16351   8907   8702   2171  -1198    318       N  
ATOM   2104  CA  PRO A 296      -2.076 -44.676   0.454  1.00 86.93           C  
ANISOU 2104  CA  PRO A 296    15765   8826   8440   1915  -1150    170       C  
ATOM   2105  C   PRO A 296      -0.854 -43.776   0.396  1.00 86.81           C  
ANISOU 2105  C   PRO A 296    15403   9120   8460   2036  -1199     75       C  
ATOM   2106  O   PRO A 296       0.185 -44.139   0.939  1.00 89.53           O  
ANISOU 2106  O   PRO A 296    15690   9621   8705   2269  -1296    157       O  
ATOM   2107  CB  PRO A 296      -2.675 -44.632   1.861  1.00 87.79           C  
ANISOU 2107  CB  PRO A 296    15924   9044   8387   1754  -1187    248       C  
ATOM   2108  CG  PRO A 296      -3.180 -46.006   2.100  1.00 89.62           C  
ANISOU 2108  CG  PRO A 296    16517   9005   8531   1793  -1208    447       C  
ATOM   2109  CD  PRO A 296      -2.207 -46.916   1.409  1.00 91.35           C  
ANISOU 2109  CD  PRO A 296    16848   9059   8800   2128  -1257    508       C  
ATOM   2110  N   SER A 297      -0.976 -42.627  -0.258  1.00 84.10           N  
ANISOU 2110  N   SER A 297    14830   8867   8260   1873  -1142    -78       N  
ATOM   2111  CA  SER A 297       0.136 -41.697  -0.381  1.00 83.84           C  
ANISOU 2111  CA  SER A 297    14458   9119   8278   1933  -1192   -159       C  
ATOM   2112  C   SER A 297       0.641 -41.293   0.991  1.00 85.16           C  
ANISOU 2112  C   SER A 297    14488   9557   8311   1925  -1299   -155       C  
ATOM   2113  O   SER A 297      -0.133 -41.186   1.938  1.00 85.37           O  
ANISOU 2113  O   SER A 297    14602   9587   8248   1766  -1303   -161       O  
ATOM   2114  CB  SER A 297      -0.293 -40.448  -1.144  1.00 81.70           C  
ANISOU 2114  CB  SER A 297    13988   8863   8191   1694  -1126   -300       C  
ATOM   2115  OG  SER A 297      -0.862 -40.783  -2.393  1.00 80.56           O  
ANISOU 2115  OG  SER A 297    13963   8497   8148   1672  -1028   -302       O  
ATOM   2116  N   LEU A 298       1.943 -41.071   1.095  1.00 86.24           N  
ANISOU 2116  N   LEU A 298    14394   9955   8417   2094  -1385   -148       N  
ATOM   2117  CA  LEU A 298       2.536 -40.667   2.357  1.00 87.65           C  
ANISOU 2117  CA  LEU A 298    14416  10433   8456   2087  -1501   -153       C  
ATOM   2118  C   LEU A 298       3.239 -39.334   2.184  1.00 86.91           C  
ANISOU 2118  C   LEU A 298    13965  10588   8467   1961  -1546   -297       C  
ATOM   2119  O   LEU A 298       3.551 -38.933   1.066  1.00 85.65           O  
ANISOU 2119  O   LEU A 298    13670  10408   8465   1955  -1501   -334       O  
ATOM   2120  CB  LEU A 298       3.526 -41.726   2.837  1.00 90.67           C  
ANISOU 2120  CB  LEU A 298    14846  10933   8674   2412  -1598     20       C  
ATOM   2121  CG  LEU A 298       2.938 -43.113   3.092  1.00 91.62           C  
ANISOU 2121  CG  LEU A 298    15336  10779   8696   2546  -1585    195       C  
ATOM   2122  CD1 LEU A 298       4.036 -44.148   3.213  1.00 94.39           C  
ANISOU 2122  CD1 LEU A 298    15722  11192   8950   2926  -1677    362       C  
ATOM   2123  CD2 LEU A 298       2.089 -43.098   4.344  1.00 91.88           C  
ANISOU 2123  CD2 LEU A 298    15492  10842   8578   2351  -1608    233       C  
ATOM   2124  N   ARG A 299       3.483 -38.649   3.295  1.00 87.95           N  
ANISOU 2124  N   ARG A 299    13948  10964   8505   1847  -1640   -374       N  
ATOM   2125  CA  ARG A 299       4.197 -37.380   3.263  1.00 88.00           C  
ANISOU 2125  CA  ARG A 299    13626  11201   8610   1704  -1710   -513       C  
ATOM   2126  C   ARG A 299       5.624 -37.539   3.773  1.00 89.88           C  
ANISOU 2126  C   ARG A 299    13650  11796   8705   1885  -1846   -439       C  
ATOM   2127  O   ARG A 299       5.918 -38.438   4.558  1.00 91.55           O  
ANISOU 2127  O   ARG A 299    13963  12111   8712   2079  -1905   -310       O  
ATOM   2128  CB  ARG A 299       3.452 -36.325   4.085  1.00 87.85           C  
ANISOU 2128  CB  ARG A 299    13567  11201   8612   1418  -1729   -708       C  
ATOM   2129  CG  ARG A 299       2.958 -36.830   5.426  1.00 89.40           C  
ANISOU 2129  CG  ARG A 299    13922  11478   8566   1426  -1760   -690       C  
ATOM   2130  CD  ARG A 299       2.189 -35.758   6.176  1.00 89.52           C  
ANISOU 2130  CD  ARG A 299    13887  11530   8597   1163  -1763   -922       C  
ATOM   2131  NE  ARG A 299       3.035 -34.630   6.552  1.00 91.13           N  
ANISOU 2131  NE  ARG A 299    13807  11977   8843   1048  -1886  -1093       N  
ATOM   2132  CZ  ARG A 299       2.678 -33.683   7.414  1.00 92.03           C  
ANISOU 2132  CZ  ARG A 299    13844  12191   8933    854  -1933  -1328       C  
ATOM   2133  NH1 ARG A 299       1.490 -33.727   7.999  1.00 91.70           N  
ANISOU 2133  NH1 ARG A 299    13965  12065   8810    771  -1856  -1415       N  
ATOM   2134  NH2 ARG A 299       3.514 -32.694   7.696  1.00 93.46           N  
ANISOU 2134  NH2 ARG A 299    13777  12568   9164    741  -2060  -1484       N  
ATOM   2135  N   THR A 300       6.506 -36.662   3.308  1.00 89.78           N  
ANISOU 2135  N   THR A 300    13330  11979   8801   1813  -1900   -502       N  
ATOM   2136  CA  THR A 300       7.900 -36.669   3.724  1.00 92.04           C  
ANISOU 2136  CA  THR A 300    13357  12653   8963   1950  -2033   -440       C  
ATOM   2137  C   THR A 300       8.020 -36.332   5.201  1.00 93.84           C  
ANISOU 2137  C   THR A 300    13529  13118   9009   1849  -2160   -515       C  
ATOM   2138  O   THR A 300       8.786 -36.956   5.932  1.00 96.55           O  
ANISOU 2138  O   THR A 300    13819  13724   9141   2047  -2260   -397       O  
ATOM   2139  CB  THR A 300       8.707 -35.637   2.939  1.00 92.12           C  
ANISOU 2139  CB  THR A 300    13032  12833   9137   1811  -2067   -499       C  
ATOM   2140  OG1 THR A 300       8.225 -34.324   3.250  1.00 91.39           O  
ANISOU 2140  OG1 THR A 300    12856  12686   9180   1457  -2103   -694       O  
ATOM   2141  CG2 THR A 300       8.560 -35.874   1.455  1.00 90.55           C  
ANISOU 2141  CG2 THR A 300    12862  12445   9098   1883  -1937   -434       C  
ATOM   2142  N   THR A 301       7.260 -35.331   5.631  1.00 92.40           N  
ANISOU 2142  N   THR A 301    13351  12852   8903   1549  -2160   -718       N  
ATOM   2143  CA  THR A 301       7.288 -34.888   7.017  1.00 93.37           C  
ANISOU 2143  CA  THR A 301    13417  13209   8850   1424  -2274   -844       C  
ATOM   2144  C   THR A 301       6.381 -35.747   7.888  1.00 92.32           C  
ANISOU 2144  C   THR A 301    13570  12997   8512   1498  -2229   -781       C  
ATOM   2145  O   THR A 301       5.206 -35.936   7.584  1.00 90.33           O  
ANISOU 2145  O   THR A 301    13547  12434   8338   1436  -2101   -800       O  
ATOM   2146  CB  THR A 301       6.860 -33.420   7.149  1.00 93.36           C  
ANISOU 2146  CB  THR A 301    13302  13151   9021   1085  -2299  -1123       C  
ATOM   2147  OG1 THR A 301       5.529 -33.263   6.646  1.00 91.11           O  
ANISOU 2147  OG1 THR A 301    13228  12490   8900    980  -2154  -1197       O  
ATOM   2148  CG2 THR A 301       7.796 -32.523   6.363  1.00 93.96           C  
ANISOU 2148  CG2 THR A 301    13086  13318   9297    968  -2366  -1158       C  
ATOM   2149  N   THR A 302       6.944 -36.266   8.973  1.00 93.59           N  
ANISOU 2149  N   THR A 302    13699  13462   8398   1620  -2342   -688       N  
ATOM   2150  CA  THR A 302       6.185 -37.033   9.950  1.00 93.24           C  
ANISOU 2150  CA  THR A 302    13892  13415   8120   1662  -2324   -602       C  
ATOM   2151  C   THR A 302       5.235 -36.083  10.667  1.00 93.36           C  
ANISOU 2151  C   THR A 302    13920  13439   8115   1373  -2301   -870       C  
ATOM   2152  O   THR A 302       5.428 -34.869  10.629  1.00 92.93           O  
ANISOU 2152  O   THR A 302    13669  13450   8192   1173  -2347  -1118       O  
ATOM   2153  CB  THR A 302       7.132 -37.678  10.981  1.00 94.94           C  
ANISOU 2153  CB  THR A 302    14022  14015   8036   1847  -2475   -432       C  
ATOM   2154  OG1 THR A 302       8.234 -38.288  10.300  1.00 95.44           O  
ANISOU 2154  OG1 THR A 302    13983  14136   8144   2122  -2519   -239       O  
ATOM   2155  CG2 THR A 302       6.420 -38.732  11.809  1.00 95.28           C  
ANISOU 2155  CG2 THR A 302    14336  14024   7843   1936  -2455   -243       C  
ATOM   2156  N   ALA A 303       4.207 -36.629  11.310  1.00 94.63           N  
ANISOU 2156  N   ALA A 303    14308  13534   8115   1350  -2234   -823       N  
ATOM   2157  CA  ALA A 303       3.328 -35.831  12.153  1.00 96.12           C  
ANISOU 2157  CA  ALA A 303    14493  13808   8221   1116  -2212  -1078       C  
ATOM   2158  C   ALA A 303       4.146 -35.143  13.241  1.00100.25           C  
ANISOU 2158  C   ALA A 303    14779  14763   8549   1038  -2376  -1245       C  
ATOM   2159  O   ALA A 303       3.843 -34.023  13.647  1.00100.56           O  
ANISOU 2159  O   ALA A 303    14711  14872   8627    828  -2395  -1563       O  
ATOM   2160  CB  ALA A 303       2.253 -36.704  12.769  1.00 96.30           C  
ANISOU 2160  CB  ALA A 303    14769  13788   8035   1126  -2127   -940       C  
ATOM   2161  N   SER A 304       5.191 -35.826  13.700  1.00103.99           N  
ANISOU 2161  N   SER A 304    15173  15524   8816   1216  -2500  -1033       N  
ATOM   2162  CA  SER A 304       6.090 -35.286  14.710  1.00108.80           C  
ANISOU 2162  CA  SER A 304    15540  16588   9212   1154  -2673  -1155       C  
ATOM   2163  C   SER A 304       7.063 -34.279  14.114  1.00109.75           C  
ANISOU 2163  C   SER A 304    15387  16758   9555   1062  -2763  -1323       C  
ATOM   2164  O   SER A 304       7.697 -33.521  14.842  1.00 85.57           O  
ANISOU 2164  O   SER A 304    12108  14024   6381    927  -2907  -1512       O  
ATOM   2165  CB  SER A 304       6.874 -36.412  15.373  1.00112.14           C  
ANISOU 2165  CB  SER A 304    15959  17311   9337   1393  -2782   -833       C  
ATOM   2166  OG  SER A 304       7.614 -37.146  14.414  1.00112.38           O  
ANISOU 2166  OG  SER A 304    15991  17196   9513   1644  -2781   -577       O  
ATOM   2167  N   GLY A 305       7.185 -34.278  12.790  1.00108.55           N  
ANISOU 2167  N   GLY A 305    15242  16297   9707   1118  -2685  -1247       N  
ATOM   2168  CA  GLY A 305       8.062 -33.339  12.116  1.00110.23           C  
ANISOU 2168  CA  GLY A 305    15193  16546  10143   1007  -2760  -1365       C  
ATOM   2169  C   GLY A 305       9.334 -33.972  11.585  1.00111.82           C  
ANISOU 2169  C   GLY A 305    15233  16925  10327   1238  -2829  -1107       C  
ATOM   2170  O   GLY A 305      10.169 -33.297  10.980  1.00111.94           O  
ANISOU 2170  O   GLY A 305    15004  17024  10505   1156  -2892  -1156       O  
ATOM   2171  N   LYS A 306       9.481 -35.274  11.809  1.00114.72           N  
ANISOU 2171  N   LYS A 306    15733  17355  10500   1528  -2818   -826       N  
ATOM   2172  CA  LYS A 306      10.671 -35.995  11.370  1.00116.38           C  
ANISOU 2172  CA  LYS A 306    15799  17746  10674   1810  -2881   -577       C  
ATOM   2173  C   LYS A 306      10.675 -36.150   9.854  1.00113.63           C  
ANISOU 2173  C   LYS A 306    15480  17084  10609   1908  -2755   -506       C  
ATOM   2174  O   LYS A 306       9.645 -36.446   9.251  1.00111.97           O  
ANISOU 2174  O   LYS A 306    15530  16477  10536   1904  -2604   -501       O  
ATOM   2175  CB  LYS A 306      10.731 -37.371  12.035  1.00118.40           C  
ANISOU 2175  CB  LYS A 306    16227  18094  10666   2111  -2909   -293       C  
ATOM   2176  CG  LYS A 306      12.043 -38.117  11.840  1.00121.26           C  
ANISOU 2176  CG  LYS A 306    16415  18714  10945   2441  -3006    -46       C  
ATOM   2177  CD  LYS A 306      11.861 -39.614  12.060  1.00122.79           C  
ANISOU 2177  CD  LYS A 306    16876  18781  10999   2782  -2987    262       C  
ATOM   2178  CE  LYS A 306      10.993 -39.903  13.278  1.00124.02           C  
ANISOU 2178  CE  LYS A 306    17245  18962  10917   2675  -3006    294       C  
ATOM   2179  NZ  LYS A 306      10.664 -41.349  13.409  1.00125.30           N  
ANISOU 2179  NZ  LYS A 306    17711  18914  10982   2959  -2983    614       N  
ATOM   2180  N   LEU A 307      11.835 -35.950   9.239  1.00112.05           N  
ANISOU 2180  N   LEU A 307    14998  17098  10480   1987  -2817   -448       N  
ATOM   2181  CA  LEU A 307      11.947 -36.061   7.791  1.00108.37           C  
ANISOU 2181  CA  LEU A 307    14516  16412  10249   2079  -2701   -383       C  
ATOM   2182  C   LEU A 307      12.525 -37.404   7.371  1.00108.90           C  
ANISOU 2182  C   LEU A 307    14640  16508  10228   2507  -2676   -121       C  
ATOM   2183  O   LEU A 307      13.495 -37.879   7.954  1.00112.67           O  
ANISOU 2183  O   LEU A 307    14960  17337  10511   2719  -2799     15       O  
ATOM   2184  CB  LEU A 307      12.811 -34.931   7.233  1.00109.10           C  
ANISOU 2184  CB  LEU A 307    14245  16715  10491   1874  -2770   -485       C  
ATOM   2185  CG  LEU A 307      13.181 -35.020   5.750  1.00109.26           C  
ANISOU 2185  CG  LEU A 307    14165  16644  10707   1976  -2669   -390       C  
ATOM   2186  CD1 LEU A 307      11.937 -35.038   4.875  1.00106.53           C  
ANISOU 2186  CD1 LEU A 307    14101  15807  10568   1901  -2492   -441       C  
ATOM   2187  CD2 LEU A 307      14.099 -33.875   5.354  1.00110.88           C  
ANISOU 2187  CD2 LEU A 307    13982  17120  11026   1734  -2761   -458       C  
ATOM   2188  N   ILE A 308      11.916 -38.014   6.361  1.00105.61           N  
ANISOU 2188  N   ILE A 308    14451  15719   9957   2639  -2523    -61       N  
ATOM   2189  CA  ILE A 308      12.470 -39.213   5.752  1.00105.38           C  
ANISOU 2189  CA  ILE A 308    14478  15669   9892   3051  -2488    141       C  
ATOM   2190  C   ILE A 308      13.092 -38.839   4.417  1.00103.14           C  
ANISOU 2190  C   ILE A 308    13961  15448   9780   3080  -2424    116       C  
ATOM   2191  O   ILE A 308      12.503 -38.094   3.639  1.00100.13           O  
ANISOU 2191  O   ILE A 308    13587  14863   9595   2828  -2329    -10       O  
ATOM   2192  CB  ILE A 308      11.401 -40.277   5.514  1.00104.50           C  
ANISOU 2192  CB  ILE A 308    14797  15102   9807   3197  -2369    224       C  
ATOM   2193  CG1 ILE A 308      10.601 -40.521   6.789  1.00105.35           C  
ANISOU 2193  CG1 ILE A 308    15135  15142   9752   3090  -2414    248       C  
ATOM   2194  CG2 ILE A 308      12.036 -41.569   5.032  1.00106.35           C  
ANISOU 2194  CG2 ILE A 308    15110  15303   9997   3653  -2362    416       C  
ATOM   2195  CD1 ILE A 308       9.625 -41.650   6.658  1.00104.84           C  
ANISOU 2195  CD1 ILE A 308    15485  14660   9690   3222  -2321    372       C  
ATOM   2196  N   THR A 309      14.284 -39.360   4.160  1.00104.74           N  
ANISOU 2196  N   THR A 309    13943  15957   9896   3397  -2476    247       N  
ATOM   2197  CA  THR A 309      15.026 -39.010   2.960  1.00104.11           C  
ANISOU 2197  CA  THR A 309    13580  16047   9929   3437  -2423    240       C  
ATOM   2198  C   THR A 309      15.108 -40.194   2.006  1.00104.18           C  
ANISOU 2198  C   THR A 309    13745  15885   9956   3850  -2309    338       C  
ATOM   2199  O   THR A 309      15.309 -40.025   0.805  1.00103.28           O  
ANISOU 2199  O   THR A 309    13507  15783   9952   3872  -2209    306       O  
ATOM   2200  CB  THR A 309      16.449 -38.547   3.315  1.00106.61           C  
ANISOU 2200  CB  THR A 309    13440  16939  10128   3461  -2571    291       C  
ATOM   2201  OG1 THR A 309      17.119 -39.582   4.044  1.00109.53           O  
ANISOU 2201  OG1 THR A 309    13811  17519  10287   3854  -2666    453       O  
ATOM   2202  CG2 THR A 309      16.401 -37.293   4.171  1.00106.28           C  
ANISOU 2202  CG2 THR A 309    13239  17058  10087   3022  -2693    156       C  
ATOM   2203  N   GLU A 310      14.945 -41.396   2.546  1.00105.81           N  
ANISOU 2203  N   GLU A 310    14227  15928  10048   4173  -2331    456       N  
ATOM   2204  CA  GLU A 310      15.112 -42.603   1.749  1.00107.21           C  
ANISOU 2204  CA  GLU A 310    14567  15930  10236   4607  -2250    536       C  
ATOM   2205  C   GLU A 310      13.779 -43.232   1.380  1.00104.88           C  
ANISOU 2205  C   GLU A 310    14744  15059  10046   4579  -2128    500       C  
ATOM   2206  O   GLU A 310      13.032 -43.686   2.246  1.00104.62           O  
ANISOU 2206  O   GLU A 310    15014  14778   9958   4536  -2165    560       O  
ATOM   2207  CB  GLU A 310      15.992 -43.610   2.486  1.00111.50           C  
ANISOU 2207  CB  GLU A 310    15083  16678  10602   5046  -2374    716       C  
ATOM   2208  CG  GLU A 310      17.397 -43.096   2.751  1.00114.76           C  
ANISOU 2208  CG  GLU A 310    14999  17708  10898   5118  -2494    765       C  
ATOM   2209  CD  GLU A 310      18.166 -43.950   3.740  1.00119.07           C  
ANISOU 2209  CD  GLU A 310    15507  18484  11249   5492  -2647    958       C  
ATOM   2210  OE1 GLU A 310      17.541 -44.515   4.662  1.00119.46           O  
ANISOU 2210  OE1 GLU A 310    15872  18291  11227   5511  -2705   1052       O  
ATOM   2211  OE2 GLU A 310      19.403 -44.053   3.599  1.00122.16           O  
ANISOU 2211  OE2 GLU A 310    15538  19324  11552   5766  -2712   1032       O  
ATOM   2212  N   TRP A 311      13.494 -43.258   0.083  1.00103.46           N  
ANISOU 2212  N   TRP A 311    14609  14698  10002   4590  -1987    411       N  
ATOM   2213  CA  TRP A 311      12.255 -43.829  -0.428  1.00101.50           C  
ANISOU 2213  CA  TRP A 311    14782  13927   9857   4547  -1868    364       C  
ATOM   2214  C   TRP A 311      12.533 -44.839  -1.542  1.00102.09           C  
ANISOU 2214  C   TRP A 311    14968  13861   9962   4936  -1779    355       C  
ATOM   2215  O   TRP A 311      13.632 -44.893  -2.093  1.00104.19           O  
ANISOU 2215  O   TRP A 311    14939  14463  10185   5197  -1781    357       O  
ATOM   2216  CB  TRP A 311      11.328 -42.723  -0.941  1.00 98.62           C  
ANISOU 2216  CB  TRP A 311    14403  13426   9641   4087  -1775    224       C  
ATOM   2217  CG  TRP A 311      10.837 -41.794   0.129  1.00 97.73           C  
ANISOU 2217  CG  TRP A 311    14255  13360   9520   3713  -1848    188       C  
ATOM   2218  CD1 TRP A 311      11.538 -40.789   0.728  1.00 98.54           C  
ANISOU 2218  CD1 TRP A 311    14016  13844   9582   3534  -1953    161       C  
ATOM   2219  CD2 TRP A 311       9.531 -41.777   0.715  1.00 95.97           C  
ANISOU 2219  CD2 TRP A 311    14342  12802   9319   3473  -1820    155       C  
ATOM   2220  NE1 TRP A 311      10.751 -40.154   1.657  1.00 97.39           N  
ANISOU 2220  NE1 TRP A 311    13962  13606   9433   3215  -1993     90       N  
ATOM   2221  CE2 TRP A 311       9.513 -40.741   1.667  1.00 95.82           C  
ANISOU 2221  CE2 TRP A 311    14150  12989   9266   3180  -1907     90       C  
ATOM   2222  CE3 TRP A 311       8.376 -42.539   0.528  1.00 94.86           C  
ANISOU 2222  CE3 TRP A 311    14599  12226   9217   3470  -1733    170       C  
ATOM   2223  CZ2 TRP A 311       8.383 -40.450   2.431  1.00 94.54           C  
ANISOU 2223  CZ2 TRP A 311    14191  12632   9099   2915  -1897     29       C  
ATOM   2224  CZ3 TRP A 311       7.257 -42.248   1.286  1.00 93.50           C  
ANISOU 2224  CZ3 TRP A 311    14613  11874   9038   3185  -1726    137       C  
ATOM   2225  CH2 TRP A 311       7.268 -41.215   2.225  1.00 93.32           C  
ANISOU 2225  CH2 TRP A 311    14402  12084   8972   2925  -1801     63       C  
ATOM   2226  N   CYS A 312      11.522 -45.634  -1.869  1.00100.29           N  
ANISOU 2226  N   CYS A 312    15160  13147   9799   4967  -1704    333       N  
ATOM   2227  CA  CYS A 312      11.645 -46.658  -2.889  1.00100.58           C  
ANISOU 2227  CA  CYS A 312    15369  12980   9868   5324  -1625    289       C  
ATOM   2228  C   CYS A 312      10.319 -46.869  -3.601  1.00 97.50           C  
ANISOU 2228  C   CYS A 312    15331  12122   9594   5112  -1505    190       C  
ATOM   2229  O   CYS A 312       9.255 -46.518  -3.084  1.00 95.22           O  
ANISOU 2229  O   CYS A 312    15225  11608   9345   4760  -1501    200       O  
ATOM   2230  CB  CYS A 312      12.089 -47.974  -2.260  1.00103.88           C  
ANISOU 2230  CB  CYS A 312    16005  13260  10206   5773  -1724    425       C  
ATOM   2231  SG  CYS A 312      11.015 -48.538  -0.919  1.00134.55           S  
ANISOU 2231  SG  CYS A 312    20326  16735  14062   5608  -1815    584       S  
ATOM   2232  N   CYS A 313      10.393 -47.451  -4.791  1.00 97.52           N  
ANISOU 2232  N   CYS A 313    15413  12004   9635   5335  -1409     85       N  
ATOM   2233  CA  CYS A 313       9.211 -47.917  -5.499  1.00 95.29           C  
ANISOU 2233  CA  CYS A 313    15501  11262   9442   5205  -1311     -8       C  
ATOM   2234  C   CYS A 313       9.578 -49.221  -6.178  1.00 97.79           C  
ANISOU 2234  C   CYS A 313    16035  11374   9747   5669  -1291    -69       C  
ATOM   2235  O   CYS A 313      10.750 -49.470  -6.460  1.00100.81           O  
ANISOU 2235  O   CYS A 313    16184  12056  10065   6052  -1307    -86       O  
ATOM   2236  CB  CYS A 313       8.760 -46.900  -6.536  1.00 92.34           C  
ANISOU 2236  CB  CYS A 313    14942  10999   9142   4869  -1189   -135       C  
ATOM   2237  SG  CYS A 313       9.905 -46.703  -7.900  1.00 87.12           S  
ANISOU 2237  SG  CYS A 313    13900  10763   8438   5123  -1104   -245       S  
ATOM   2238  N   ARG A 314       8.582 -50.054  -6.440  1.00 96.87           N  
ANISOU 2238  N   ARG A 314    16360  10752   9694   5639  -1260   -112       N  
ATOM   2239  CA  ARG A 314       8.848 -51.382  -6.968  1.00 99.62           C  
ANISOU 2239  CA  ARG A 314    16985  10816  10049   6079  -1264   -183       C  
ATOM   2240  C   ARG A 314       8.902 -51.369  -8.492  1.00 99.23           C  
ANISOU 2240  C   ARG A 314    16860  10832  10011   6154  -1127   -412       C  
ATOM   2241  O   ARG A 314       9.569 -52.202  -9.104  1.00101.92           O  
ANISOU 2241  O   ARG A 314    17222  11180  10324   6544  -1107   -524       O  
ATOM   2242  CB  ARG A 314       7.792 -52.369  -6.468  1.00 99.77           C  
ANISOU 2242  CB  ARG A 314    17476  10299  10132   5904  -1297   -118       C  
ATOM   2243  CG  ARG A 314       8.330 -53.761  -6.192  1.00104.00           C  
ANISOU 2243  CG  ARG A 314    18167  10671  10678   6190  -1354    -82       C  
ATOM   2244  CD  ARG A 314       7.495 -54.474  -5.141  1.00104.60           C  
ANISOU 2244  CD  ARG A 314    18568  10378  10797   5952  -1430     92       C  
ATOM   2245  NE  ARG A 314       6.164 -54.829  -5.623  1.00103.08           N  
ANISOU 2245  NE  ARG A 314    18674   9808  10682   5586  -1365     18       N  
ATOM   2246  CZ  ARG A 314       5.257 -55.483  -4.901  1.00103.45           C  
ANISOU 2246  CZ  ARG A 314    19002   9531  10772   5327  -1412    150       C  
ATOM   2247  NH1 ARG A 314       4.072 -55.770  -5.420  1.00102.09           N  
ANISOU 2247  NH1 ARG A 314    19049   9080  10663   4991  -1352     79       N  
ATOM   2248  NH2 ARG A 314       5.535 -55.851  -3.659  1.00105.30           N  
ANISOU 2248  NH2 ARG A 314    19277   9754  10979   5398  -1522    367       N  
ATOM   2249  N   SER A 315       8.209 -50.408  -9.095  1.00 96.07           N  
ANISOU 2249  N   SER A 315    16332  10527   9642   5731  -1028   -483       N  
ATOM   2250  CA  SER A 315       8.110 -50.342 -10.548  1.00 95.87           C  
ANISOU 2250  CA  SER A 315    16242  10575   9609   5736   -897   -683       C  
ATOM   2251  C   SER A 315       7.861 -48.932 -11.087  1.00 93.20           C  
ANISOU 2251  C   SER A 315    15554  10575   9283   5315   -812   -691       C  
ATOM   2252  O   SER A 315       7.699 -48.755 -12.293  1.00 92.61           O  
ANISOU 2252  O   SER A 315    15401  10598   9190   5258   -704   -828       O  
ATOM   2253  CB  SER A 315       7.013 -51.286 -11.045  1.00 95.40           C  
ANISOU 2253  CB  SER A 315    16672   9969   9608   5688   -865   -797       C  
ATOM   2254  OG  SER A 315       7.280 -52.625 -10.667  1.00 98.43           O  
ANISOU 2254  OG  SER A 315    17293  10104  10000   5925   -939   -773       O  
ATOM   2255  N   CYS A 316       7.839 -47.937 -10.200  1.00 91.71           N  
ANISOU 2255  N   CYS A 316    15159  10562   9123   5026   -868   -547       N  
ATOM   2256  CA  CYS A 316       7.589 -46.552 -10.608  1.00 89.36           C  
ANISOU 2256  CA  CYS A 316    14547  10535   8870   4618   -811   -538       C  
ATOM   2257  C   CYS A 316       8.647 -46.054 -11.592  1.00 90.88           C  
ANISOU 2257  C   CYS A 316    14313  11226   8991   4750   -748   -588       C  
ATOM   2258  O   CYS A 316       9.690 -46.682 -11.769  1.00 93.99           O  
ANISOU 2258  O   CYS A 316    14598  11827   9289   5170   -756   -624       O  
ATOM   2259  CB  CYS A 316       7.545 -45.622  -9.394  1.00 87.71           C  
ANISOU 2259  CB  CYS A 316    14190  10434   8704   4343   -902   -400       C  
ATOM   2260  SG  CYS A 316       9.170 -45.065  -8.838  1.00195.20           S  
ANISOU 2260  SG  CYS A 316    27327  24608  22233   4536   -992   -310       S  
ATOM   2261  N   THR A 317       8.371 -44.920 -12.229  1.00 88.84           N  
ANISOU 2261  N   THR A 317    13805  11171   8780   4393   -688   -578       N  
ATOM   2262  CA  THR A 317       9.288 -44.367 -13.219  1.00 90.21           C  
ANISOU 2262  CA  THR A 317    13558  11841   8879   4449   -624   -594       C  
ATOM   2263  C   THR A 317       9.846 -43.008 -12.816  1.00 89.37           C  
ANISOU 2263  C   THR A 317    13031  12110   8816   4169   -682   -455       C  
ATOM   2264  O   THR A 317       9.198 -41.979 -13.001  1.00 69.86           O  
ANISOU 2264  O   THR A 317    10478   9612   6455   3755   -670   -406       O  
ATOM   2265  CB  THR A 317       8.632 -44.255 -14.603  1.00 89.39           C  
ANISOU 2265  CB  THR A 317    13482  11716   8767   4296   -499   -692       C  
ATOM   2266  OG1 THR A 317       7.361 -43.602 -14.482  1.00 69.01           O  
ANISOU 2266  OG1 THR A 317    11055   8844   6321   3853   -496   -648       O  
ATOM   2267  CG2 THR A 317       8.434 -45.634 -15.206  1.00 74.37           C  
ANISOU 2267  CG2 THR A 317    11915   9559   6783   4644   -440   -869       C  
ATOM   2268  N   LEU A 318      11.058 -43.028 -12.269  1.00 92.08           N  
ANISOU 2268  N   LEU A 318    13111  12796   9079   4404   -754   -394       N  
ATOM   2269  CA  LEU A 318      11.787 -41.820 -11.903  1.00 92.65           C  
ANISOU 2269  CA  LEU A 318    12756  13272   9174   4169   -825   -271       C  
ATOM   2270  C   LEU A 318      11.863 -40.878 -13.102  1.00 92.05           C  
ANISOU 2270  C   LEU A 318    12365  13493   9116   3903   -743   -242       C  
ATOM   2271  O   LEU A 318      12.065 -41.331 -14.224  1.00 93.72           O  
ANISOU 2271  O   LEU A 318    12523  13862   9226   4090   -634   -313       O  
ATOM   2272  CB  LEU A 318      13.194 -42.205 -11.434  1.00 96.44           C  
ANISOU 2272  CB  LEU A 318    12973  14150   9520   4541   -895   -226       C  
ATOM   2273  CG  LEU A 318      14.057 -41.233 -10.630  1.00 97.48           C  
ANISOU 2273  CG  LEU A 318    12720  14666   9653   4365  -1016    -98       C  
ATOM   2274  CD1 LEU A 318      15.019 -42.006  -9.743  1.00100.50           C  
ANISOU 2274  CD1 LEU A 318    13052  15221   9912   4777  -1112    -61       C  
ATOM   2275  CD2 LEU A 318      14.831 -40.300 -11.543  1.00 98.56           C  
ANISOU 2275  CD2 LEU A 318    12371  15318   9758   4196   -977    -34       C  
ATOM   2276  N   PRO A 319      11.694 -39.564 -12.877  1.00 90.40           N  
ANISOU 2276  N   PRO A 319    11953  13362   9035   3466   -799   -139       N  
ATOM   2277  CA  PRO A 319      11.408 -38.878 -11.610  1.00 88.53           C  
ANISOU 2277  CA  PRO A 319    11759  12958   8919   3206   -924    -88       C  
ATOM   2278  C   PRO A 319      10.026 -39.201 -11.056  1.00 85.60           C  
ANISOU 2278  C   PRO A 319    11843  12035   8648   3092   -920   -156       C  
ATOM   2279  O   PRO A 319       9.087 -39.415 -11.822  1.00 84.01           O  
ANISOU 2279  O   PRO A 319    11852  11579   8488   3012   -825   -209       O  
ATOM   2280  CB  PRO A 319      11.496 -37.395 -11.989  1.00 88.09           C  
ANISOU 2280  CB  PRO A 319    11372  13110   8989   2769   -953     13       C  
ATOM   2281  CG  PRO A 319      12.371 -37.369 -13.182  1.00 90.30           C  
ANISOU 2281  CG  PRO A 319    11311  13846   9151   2877   -876     66       C  
ATOM   2282  CD  PRO A 319      12.002 -38.602 -13.946  1.00 90.66           C  
ANISOU 2282  CD  PRO A 319    11621  13746   9080   3216   -748    -56       C  
ATOM   2283  N   PRO A 320       9.908 -39.229  -9.723  1.00 84.29           N  
ANISOU 2283  N   PRO A 320    11806  11721   8500   3073  -1024   -149       N  
ATOM   2284  CA  PRO A 320       8.732 -39.750  -9.026  1.00 82.52           C  
ANISOU 2284  CA  PRO A 320    12007  11028   8319   3031  -1026   -199       C  
ATOM   2285  C   PRO A 320       7.542 -38.799  -9.020  1.00 79.45           C  
ANISOU 2285  C   PRO A 320    11702  10388   8098   2606  -1010   -217       C  
ATOM   2286  O   PRO A 320       7.703 -37.588  -9.168  1.00 79.11           O  
ANISOU 2286  O   PRO A 320    11389  10507   8164   2321  -1043   -182       O  
ATOM   2287  CB  PRO A 320       9.245 -39.937  -7.601  1.00 83.64           C  
ANISOU 2287  CB  PRO A 320    12153  11236   8390   3144  -1154   -161       C  
ATOM   2288  CG  PRO A 320      10.254 -38.858  -7.443  1.00 84.63           C  
ANISOU 2288  CG  PRO A 320    11843  11784   8528   2997  -1235   -109       C  
ATOM   2289  CD  PRO A 320      10.924 -38.724  -8.782  1.00 85.72           C  
ANISOU 2289  CD  PRO A 320    11706  12222   8643   3068  -1154    -85       C  
ATOM   2290  N   LEU A 321       6.353 -39.364  -8.840  1.00 77.96           N  
ANISOU 2290  N   LEU A 321    11886   9800   7936   2570   -966   -265       N  
ATOM   2291  CA  LEU A 321       5.133 -38.581  -8.740  1.00 75.65           C  
ANISOU 2291  CA  LEU A 321    11694   9258   7791   2210   -948   -289       C  
ATOM   2292  C   LEU A 321       5.081 -37.945  -7.366  1.00 75.82           C  
ANISOU 2292  C   LEU A 321    11683   9277   7847   2057  -1055   -296       C  
ATOM   2293  O   LEU A 321       5.029 -38.643  -6.357  1.00 76.52           O  
ANISOU 2293  O   LEU A 321    11963   9277   7835   2198  -1102   -297       O  
ATOM   2294  CB  LEU A 321       3.913 -39.483  -8.936  1.00 75.16           C  
ANISOU 2294  CB  LEU A 321    12028   8812   7717   2230   -869   -333       C  
ATOM   2295  CG  LEU A 321       2.591 -38.905  -9.453  1.00 73.66           C  
ANISOU 2295  CG  LEU A 321    11932   8394   7661   1915   -803   -356       C  
ATOM   2296  CD1 LEU A 321       1.599 -40.025  -9.698  1.00 73.39           C  
ANISOU 2296  CD1 LEU A 321    12275   8036   7573   1981   -734   -392       C  
ATOM   2297  CD2 LEU A 321       2.000 -37.887  -8.500  1.00 72.91           C  
ANISOU 2297  CD2 LEU A 321    11795   8225   7683   1636   -863   -367       C  
ATOM   2298  N   ARG A 322       5.088 -36.618  -7.325  1.00 75.55           N  
ANISOU 2298  N   ARG A 322    11414   9338   7953   1764  -1100   -301       N  
ATOM   2299  CA  ARG A 322       4.978 -35.922  -6.054  1.00 75.83           C  
ANISOU 2299  CA  ARG A 322    11420   9366   8027   1598  -1203   -351       C  
ATOM   2300  C   ARG A 322       3.839 -34.912  -6.043  1.00 74.10           C  
ANISOU 2300  C   ARG A 322    11243   8915   7996   1268  -1188   -415       C  
ATOM   2301  O   ARG A 322       3.405 -34.425  -7.090  1.00 72.80           O  
ANISOU 2301  O   ARG A 322    11021   8676   7964   1123  -1126   -387       O  
ATOM   2302  CB  ARG A 322       6.301 -35.253  -5.671  1.00 77.35           C  
ANISOU 2302  CB  ARG A 322    11267   9923   8201   1585  -1320   -325       C  
ATOM   2303  CG  ARG A 322       6.671 -34.039  -6.496  1.00 76.86           C  
ANISOU 2303  CG  ARG A 322    10893  10007   8302   1336  -1338   -287       C  
ATOM   2304  CD  ARG A 322       7.832 -33.294  -5.856  1.00 78.54           C  
ANISOU 2304  CD  ARG A 322    10792  10544   8506   1253  -1479   -277       C  
ATOM   2305  NE  ARG A 322       8.141 -32.044  -6.541  1.00 78.74           N  
ANISOU 2305  NE  ARG A 322    10530  10675   8712    958  -1519   -225       N  
ATOM   2306  CZ  ARG A 322       9.097 -31.200  -6.167  1.00 80.79           C  
ANISOU 2306  CZ  ARG A 322    10491  11197   9007    801  -1649   -205       C  
ATOM   2307  NH1 ARG A 322       9.847 -31.466  -5.109  1.00 82.31           N  
ANISOU 2307  NH1 ARG A 322    10618  11604   9053    919  -1750   -245       N  
ATOM   2308  NH2 ARG A 322       9.302 -30.088  -6.855  1.00 81.63           N  
ANISOU 2308  NH2 ARG A 322    10362  11357   9296    510  -1688   -133       N  
ATOM   2309  N   TYR A 323       3.355 -34.618  -4.843  1.00 74.81           N  
ANISOU 2309  N   TYR A 323    11428   8910   8085   1167  -1247   -501       N  
ATOM   2310  CA  TYR A 323       2.303 -33.635  -4.653  1.00 74.49           C  
ANISOU 2310  CA  TYR A 323    11418   8666   8218    890  -1242   -591       C  
ATOM   2311  C   TYR A 323       2.819 -32.535  -3.743  1.00 78.73           C  
ANISOU 2311  C   TYR A 323    11753   9338   8823    730  -1373   -685       C  
ATOM   2312  O   TYR A 323       3.373 -32.814  -2.683  1.00 79.60           O  
ANISOU 2312  O   TYR A 323    11856   9606   8781    826  -1452   -723       O  
ATOM   2313  CB  TYR A 323       1.083 -34.283  -4.006  1.00 72.37           C  
ANISOU 2313  CB  TYR A 323    11463   8162   7874    905  -1182   -644       C  
ATOM   2314  CG  TYR A 323       0.624 -35.555  -4.673  1.00 71.01           C  
ANISOU 2314  CG  TYR A 323    11534   7845   7603   1071  -1078   -562       C  
ATOM   2315  CD1 TYR A 323      -0.390 -35.538  -5.615  1.00 69.30           C  
ANISOU 2315  CD1 TYR A 323    11419   7425   7488    960   -979   -551       C  
ATOM   2316  CD2 TYR A 323       1.190 -36.777  -4.343  1.00 72.17           C  
ANISOU 2316  CD2 TYR A 323    11815   8047   7558   1338  -1088   -500       C  
ATOM   2317  CE1 TYR A 323      -0.820 -36.701  -6.219  1.00 68.81           C  
ANISOU 2317  CE1 TYR A 323    11590   7223   7333   1089   -895   -498       C  
ATOM   2318  CE2 TYR A 323       0.768 -37.942  -4.944  1.00 71.74           C  
ANISOU 2318  CE2 TYR A 323    12009   7818   7432   1485  -1007   -445       C  
ATOM   2319  CZ  TYR A 323      -0.237 -37.899  -5.880  1.00 69.71           C  
ANISOU 2319  CZ  TYR A 323    11853   7362   7272   1348   -911   -454       C  
ATOM   2320  OH  TYR A 323      -0.662 -39.055  -6.482  1.00 68.94           O  
ANISOU 2320  OH  TYR A 323    12009   7084   7100   1472   -840   -420       O  
ATOM   2321  N   ARG A 324       2.644 -31.285  -4.156  1.00 81.75           N  
ANISOU 2321  N   ARG A 324    11975   9654   9434    483  -1406   -720       N  
ATOM   2322  CA  ARG A 324       3.025 -30.156  -3.315  1.00 85.95           C  
ANISOU 2322  CA  ARG A 324    12340  10254  10063    298  -1541   -842       C  
ATOM   2323  C   ARG A 324       1.778 -29.440  -2.814  1.00 86.79           C  
ANISOU 2323  C   ARG A 324    12576  10087  10314    130  -1532  -1002       C  
ATOM   2324  O   ARG A 324       0.988 -28.933  -3.606  1.00 86.27           O  
ANISOU 2324  O   ARG A 324    12530   9807  10443      8  -1475   -980       O  
ATOM   2325  CB  ARG A 324       3.933 -29.182  -4.075  1.00 87.43           C  
ANISOU 2325  CB  ARG A 324    12223  10577  10420    132  -1620   -761       C  
ATOM   2326  CG  ARG A 324       5.261 -29.782  -4.517  1.00 88.65           C  
ANISOU 2326  CG  ARG A 324    12190  11074  10420    296  -1635   -615       C  
ATOM   2327  CD  ARG A 324       6.205 -28.726  -5.074  1.00 89.79           C  
ANISOU 2327  CD  ARG A 324    12000  11403  10714     85  -1732   -532       C  
ATOM   2328  NE  ARG A 324       5.590 -27.953  -6.148  1.00 88.70           N  
ANISOU 2328  NE  ARG A 324    11824  11064  10815   -122  -1691   -455       N  
ATOM   2329  CZ  ARG A 324       6.205 -26.987  -6.823  1.00 90.08           C  
ANISOU 2329  CZ  ARG A 324    11731  11341  11155   -348  -1765   -339       C  
ATOM   2330  NH1 ARG A 324       5.562 -26.337  -7.782  1.00 89.42           N  
ANISOU 2330  NH1 ARG A 324    11634  11059  11283   -525  -1730   -245       N  
ATOM   2331  NH2 ARG A 324       7.461 -26.670  -6.541  1.00 92.34           N  
ANISOU 2331  NH2 ARG A 324    11753  11941  11391   -408  -1882   -299       N  
ATOM   2332  N   GLY A 325       1.603 -29.405  -1.497  1.00 88.61           N  
ANISOU 2332  N   GLY A 325    12881  10350  10435    135  -1586  -1163       N  
ATOM   2333  CA  GLY A 325       0.430 -28.782  -0.913  1.00 89.49           C  
ANISOU 2333  CA  GLY A 325    13105  10249  10648     11  -1570  -1344       C  
ATOM   2334  C   GLY A 325       0.694 -28.013   0.367  1.00 92.68           C  
ANISOU 2334  C   GLY A 325    13434  10747  11032    -85  -1696  -1567       C  
ATOM   2335  O   GLY A 325       1.779 -27.472   0.572  1.00 95.25           O  
ANISOU 2335  O   GLY A 325    13563  11243  11384   -159  -1826  -1591       O  
ATOM   2336  N   GLU A 326      -0.317 -27.974   1.228  1.00 93.23           N  
ANISOU 2336  N   GLU A 326    13652  10729  11042    -92  -1658  -1738       N  
ATOM   2337  CA  GLU A 326      -0.271 -27.217   2.473  1.00 95.41           C  
ANISOU 2337  CA  GLU A 326    13878  11087  11285   -182  -1762  -2001       C  
ATOM   2338  C   GLU A 326       0.725 -27.807   3.466  1.00 96.79           C  
ANISOU 2338  C   GLU A 326    14008  11599  11168    -86  -1850  -2000       C  
ATOM   2339  O   GLU A 326       1.707 -27.163   3.841  1.00 98.92           O  
ANISOU 2339  O   GLU A 326    14096  12029  11460   -178  -1994  -2085       O  
ATOM   2340  CB  GLU A 326      -1.661 -27.201   3.108  1.00 95.33           C  
ANISOU 2340  CB  GLU A 326    14035  10955  11232   -176  -1671  -2168       C  
ATOM   2341  CG  GLU A 326      -1.865 -26.117   4.144  1.00 97.78           C  
ANISOU 2341  CG  GLU A 326    14285  11272  11595   -289  -1764  -2496       C  
ATOM   2342  CD  GLU A 326      -2.117 -24.764   3.517  1.00 98.50           C  
ANISOU 2342  CD  GLU A 326    14280  11074  12071   -449  -1818  -2614       C  
ATOM   2343  OE1 GLU A 326      -2.485 -24.722   2.323  1.00 96.81           O  
ANISOU 2343  OE1 GLU A 326    14073  10649  12061   -467  -1750  -2436       O  
ATOM   2344  OE2 GLU A 326      -1.951 -23.745   4.220  1.00101.00           O  
ANISOU 2344  OE2 GLU A 326    14519  11370  12486   -557  -1936  -2885       O  
ATOM   2345  N   ASP A 327       0.460 -29.041   3.885  1.00 95.58           N  
ANISOU 2345  N   ASP A 327    14020  11553  10742     90  -1771  -1890       N  
ATOM   2346  CA  ASP A 327       1.284 -29.711   4.884  1.00 95.93           C  
ANISOU 2346  CA  ASP A 327    14043  11918  10487    207  -1851  -1858       C  
ATOM   2347  C   ASP A 327       2.662 -30.123   4.370  1.00 96.04           C  
ANISOU 2347  C   ASP A 327    13906  12121  10464    311  -1922  -1663       C  
ATOM   2348  O   ASP A 327       3.449 -30.714   5.109  1.00 98.19           O  
ANISOU 2348  O   ASP A 327    14138  12673  10495    434  -1998  -1603       O  
ATOM   2349  CB  ASP A 327       0.549 -30.927   5.455  1.00 94.81           C  
ANISOU 2349  CB  ASP A 327    14137  11807  10081    356  -1754  -1760       C  
ATOM   2350  CG  ASP A 327      -0.099 -31.779   4.381  1.00 91.94           C  
ANISOU 2350  CG  ASP A 327    13946  11204   9781    449  -1611  -1556       C  
ATOM   2351  OD1 ASP A 327       0.397 -31.781   3.237  1.00 90.65           O  
ANISOU 2351  OD1 ASP A 327    13710  10955   9778    477  -1598  -1433       O  
ATOM   2352  OD2 ASP A 327      -1.107 -32.454   4.684  1.00 91.11           O  
ANISOU 2352  OD2 ASP A 327    14044  11018   9555    480  -1514  -1519       O  
ATOM   2353  N   GLY A 328       2.950 -29.813   3.110  1.00 93.54           N  
ANISOU 2353  N   GLY A 328    13490  11679  10373    270  -1897  -1556       N  
ATOM   2354  CA  GLY A 328       4.245 -30.118   2.535  1.00 93.24           C  
ANISOU 2354  CA  GLY A 328    13270  11851  10304    365  -1952  -1382       C  
ATOM   2355  C   GLY A 328       4.145 -31.087   1.377  1.00 90.85           C  
ANISOU 2355  C   GLY A 328    13066  11447  10004    545  -1824  -1164       C  
ATOM   2356  O   GLY A 328       3.095 -31.206   0.753  1.00 89.38           O  
ANISOU 2356  O   GLY A 328    13046  10989   9926    518  -1705  -1150       O  
ATOM   2357  N   CYS A 329       5.239 -31.790   1.099  1.00 90.53           N  
ANISOU 2357  N   CYS A 329    12919  11640   9837    737  -1852  -1005       N  
ATOM   2358  CA  CYS A 329       5.297 -32.703  -0.038  1.00 87.68           C  
ANISOU 2358  CA  CYS A 329    12631  11213   9471    931  -1741   -827       C  
ATOM   2359  C   CYS A 329       4.747 -34.088   0.305  1.00 85.56           C  
ANISOU 2359  C   CYS A 329    12663  10838   9010   1169  -1663   -750       C  
ATOM   2360  O   CYS A 329       4.829 -34.532   1.448  1.00 86.57           O  
ANISOU 2360  O   CYS A 329    12870  11076   8948   1252  -1723   -762       O  
ATOM   2361  CB  CYS A 329       6.736 -32.818  -0.548  1.00 89.18           C  
ANISOU 2361  CB  CYS A 329    12551  11718   9614   1053  -1800   -704       C  
ATOM   2362  SG  CYS A 329       6.892 -33.360  -2.268  1.00173.56           S  
ANISOU 2362  SG  CYS A 329    23214  22360  20373   1194  -1669   -546       S  
ATOM   2363  N   TRP A 330       4.170 -34.751  -0.693  1.00 82.79           N  
ANISOU 2363  N   TRP A 330    12479  10271   8707   1258  -1537   -665       N  
ATOM   2364  CA  TRP A 330       3.725 -36.139  -0.574  1.00 81.01           C  
ANISOU 2364  CA  TRP A 330    12547   9906   8326   1480  -1470   -570       C  
ATOM   2365  C   TRP A 330       4.232 -36.920  -1.781  1.00 80.53           C  
ANISOU 2365  C   TRP A 330    12493   9836   8270   1699  -1404   -456       C  
ATOM   2366  O   TRP A 330       4.550 -36.334  -2.816  1.00 79.89           O  
ANISOU 2366  O   TRP A 330    12223   9810   8321   1626  -1374   -454       O  
ATOM   2367  CB  TRP A 330       2.197 -36.223  -0.540  1.00 77.68           C  
ANISOU 2367  CB  TRP A 330    12384   9174   7955   1336  -1373   -621       C  
ATOM   2368  CG  TRP A 330       1.550 -35.563   0.636  1.00 76.06           C  
ANISOU 2368  CG  TRP A 330    12196   8981   7723   1151  -1414   -753       C  
ATOM   2369  CD1 TRP A 330       1.598 -34.242   0.961  1.00 75.42           C  
ANISOU 2369  CD1 TRP A 330    11915   8974   7767    939  -1476   -910       C  
ATOM   2370  CD2 TRP A 330       0.723 -36.191   1.625  1.00 75.41           C  
ANISOU 2370  CD2 TRP A 330    12343   8834   7475   1158  -1394   -750       C  
ATOM   2371  NE1 TRP A 330       0.868 -34.009   2.100  1.00 75.55           N  
ANISOU 2371  NE1 TRP A 330    12019   8991   7695    838  -1491  -1034       N  
ATOM   2372  CE2 TRP A 330       0.320 -35.190   2.526  1.00 75.55           C  
ANISOU 2372  CE2 TRP A 330    12270   8931   7505    963  -1436   -926       C  
ATOM   2373  CE3 TRP A 330       0.293 -37.503   1.839  1.00 75.23           C  
ANISOU 2373  CE3 TRP A 330    12595   8696   7295   1302  -1349   -609       C  
ATOM   2374  CZ2 TRP A 330      -0.494 -35.460   3.624  1.00 75.92           C  
ANISOU 2374  CZ2 TRP A 330    12466   8996   7383    915  -1423   -968       C  
ATOM   2375  CZ3 TRP A 330      -0.515 -37.767   2.928  1.00 75.63           C  
ANISOU 2375  CZ3 TRP A 330    12799   8745   7191   1228  -1345   -619       C  
ATOM   2376  CH2 TRP A 330      -0.900 -36.752   3.806  1.00 75.95           C  
ANISOU 2376  CH2 TRP A 330    12721   8918   7220   1040  -1375   -797       C  
ATOM   2377  N   TYR A 331       4.296 -38.241  -1.658  1.00 80.87           N  
ANISOU 2377  N   TYR A 331    12756   9807   8166   1967  -1384   -361       N  
ATOM   2378  CA  TYR A 331       4.699 -39.076  -2.784  1.00 80.40           C  
ANISOU 2378  CA  TYR A 331    12740   9708   8100   2206  -1316   -290       C  
ATOM   2379  C   TYR A 331       3.556 -39.947  -3.285  1.00 78.49           C  
ANISOU 2379  C   TYR A 331    12847   9103   7872   2222  -1211   -278       C  
ATOM   2380  O   TYR A 331       2.597 -40.210  -2.560  1.00 78.21           O  
ANISOU 2380  O   TYR A 331    13044   8872   7801   2116  -1204   -278       O  
ATOM   2381  CB  TYR A 331       5.918 -39.925  -2.426  1.00 82.74           C  
ANISOU 2381  CB  TYR A 331    12978  10222   8238   2555  -1392   -197       C  
ATOM   2382  CG  TYR A 331       7.221 -39.229  -2.729  1.00 83.86           C  
ANISOU 2382  CG  TYR A 331    12721  10755   8389   2592  -1452   -193       C  
ATOM   2383  CD1 TYR A 331       7.376 -38.494  -3.891  1.00 82.77           C  
ANISOU 2383  CD1 TYR A 331    12371  10696   8382   2458  -1391   -223       C  
ATOM   2384  CD2 TYR A 331       8.288 -39.291  -1.850  1.00 86.19           C  
ANISOU 2384  CD2 TYR A 331    12834  11362   8551   2740  -1576   -140       C  
ATOM   2385  CE1 TYR A 331       8.560 -37.849  -4.177  1.00 84.24           C  
ANISOU 2385  CE1 TYR A 331    12177  11260   8569   2459  -1448   -196       C  
ATOM   2386  CE2 TYR A 331       9.479 -38.645  -2.126  1.00 87.57           C  
ANISOU 2386  CE2 TYR A 331    12623  11923   8727   2747  -1635   -126       C  
ATOM   2387  CZ  TYR A 331       9.608 -37.926  -3.293  1.00 86.59           C  
ANISOU 2387  CZ  TYR A 331    12295  11868   8738   2598  -1569   -152       C  
ATOM   2388  OH  TYR A 331      10.788 -37.279  -3.578  1.00 88.32           O  
ANISOU 2388  OH  TYR A 331    12115  12493   8952   2575  -1630   -115       O  
ATOM   2389  N   GLY A 332       3.663 -40.381  -4.536  1.00 77.29           N  
ANISOU 2389  N   GLY A 332    12720   8887   7761   2341  -1130   -273       N  
ATOM   2390  CA  GLY A 332       2.648 -41.221  -5.143  1.00 76.24           C  
ANISOU 2390  CA  GLY A 332    12907   8420   7639   2348  -1037   -277       C  
ATOM   2391  C   GLY A 332       2.436 -42.522  -4.397  1.00 77.97           C  
ANISOU 2391  C   GLY A 332    13457   8435   7734   2543  -1071   -203       C  
ATOM   2392  O   GLY A 332       3.265 -42.922  -3.581  1.00 80.05           O  
ANISOU 2392  O   GLY A 332    13689   8839   7889   2753  -1163   -134       O  
ATOM   2393  N   MET A 333       1.321 -43.182  -4.690  1.00 77.66           N  
ANISOU 2393  N   MET A 333    13730   8066   7710   2461  -1006   -203       N  
ATOM   2394  CA  MET A 333       0.942 -44.418  -4.017  1.00 79.30           C  
ANISOU 2394  CA  MET A 333    14287   8023   7819   2585  -1042   -109       C  
ATOM   2395  C   MET A 333       1.993 -45.505  -4.200  1.00 81.88           C  
ANISOU 2395  C   MET A 333    14694   8342   8075   2994  -1091    -58       C  
ATOM   2396  O   MET A 333       2.133 -46.399  -3.366  1.00 83.85           O  
ANISOU 2396  O   MET A 333    15148   8476   8234   3162  -1169     58       O  
ATOM   2397  CB  MET A 333      -0.399 -44.913  -4.556  1.00 78.28           C  
ANISOU 2397  CB  MET A 333    14456   7551   7738   2403   -961   -126       C  
ATOM   2398  CG  MET A 333      -1.528 -43.918  -4.423  1.00 75.75           C  
ANISOU 2398  CG  MET A 333    14064   7230   7489   2027   -906   -174       C  
ATOM   2399  SD  MET A 333      -3.086 -44.614  -4.982  1.00100.20           S  
ANISOU 2399  SD  MET A 333    17499   9961  10612   1817   -823   -169       S  
ATOM   2400  CE  MET A 333      -3.210 -46.028  -3.896  1.00107.41           C  
ANISOU 2400  CE  MET A 333    18776  10649  11385   1946   -903    -11       C  
ATOM   2401  N   GLU A 334       2.731 -45.412  -5.301  1.00 81.89           N  
ANISOU 2401  N   GLU A 334    14521   8480   8114   3161  -1047   -139       N  
ATOM   2402  CA  GLU A 334       3.741 -46.401  -5.646  1.00 84.03           C  
ANISOU 2402  CA  GLU A 334    14838   8765   8325   3584  -1077   -128       C  
ATOM   2403  C   GLU A 334       4.984 -46.245  -4.783  1.00 85.36           C  
ANISOU 2403  C   GLU A 334    14762   9264   8406   3805  -1184    -44       C  
ATOM   2404  O   GLU A 334       5.810 -47.153  -4.697  1.00 88.03           O  
ANISOU 2404  O   GLU A 334    15159   9609   8680   4188  -1238      5       O  
ATOM   2405  CB  GLU A 334       4.130 -46.252  -7.116  1.00 83.84           C  
ANISOU 2405  CB  GLU A 334    14656   8859   8340   3678   -983   -256       C  
ATOM   2406  CG  GLU A 334       3.050 -45.621  -7.975  1.00 81.03           C  
ANISOU 2406  CG  GLU A 334    14313   8397   8076   3327   -880   -338       C  
ATOM   2407  CD  GLU A 334       1.832 -46.501  -8.132  1.00 80.76           C  
ANISOU 2407  CD  GLU A 334    14699   7926   8060   3229   -847   -354       C  
ATOM   2408  OE1 GLU A 334       0.723 -45.956  -8.298  1.00 78.10           O  
ANISOU 2408  OE1 GLU A 334    14404   7484   7789   2883   -794   -370       O  
ATOM   2409  OE2 GLU A 334       1.985 -47.739  -8.103  1.00 83.40           O  
ANISOU 2409  OE2 GLU A 334    15319   8020   8350   3497   -879   -348       O  
ATOM   2410  N   ILE A 335       5.111 -45.089  -4.142  1.00 83.60           N  
ANISOU 2410  N   ILE A 335    14265   9313   8186   3567  -1220    -34       N  
ATOM   2411  CA  ILE A 335       6.311 -44.778  -3.380  1.00 84.81           C  
ANISOU 2411  CA  ILE A 335    14134   9838   8252   3724  -1327     30       C  
ATOM   2412  C   ILE A 335       6.125 -45.066  -1.898  1.00 84.86           C  
ANISOU 2412  C   ILE A 335    14279   9810   8154   3703  -1434    151       C  
ATOM   2413  O   ILE A 335       5.212 -44.541  -1.266  1.00 83.20           O  
ANISOU 2413  O   ILE A 335    14141   9518   7953   3386  -1430    140       O  
ATOM   2414  CB  ILE A 335       6.704 -43.307  -3.541  1.00 83.63           C  
ANISOU 2414  CB  ILE A 335    13579  10037   8162   3470  -1326    -38       C  
ATOM   2415  CG1 ILE A 335       6.460 -42.838  -4.978  1.00 82.14           C  
ANISOU 2415  CG1 ILE A 335    13289   9832   8088   3351  -1206   -135       C  
ATOM   2416  CG2 ILE A 335       8.151 -43.098  -3.116  1.00 86.02           C  
ANISOU 2416  CG2 ILE A 335    13546  10766   8371   3678  -1427     16       C  
ATOM   2417  CD1 ILE A 335       7.287 -43.568  -6.016  1.00 84.21           C  
ANISOU 2417  CD1 ILE A 335    13494  10195   8308   3703  -1159   -155       C  
ATOM   2418  N   ARG A 336       6.998 -45.899  -1.346  1.00 86.88           N  
ANISOU 2418  N   ARG A 336    14559  10152   8301   4052  -1532    269       N  
ATOM   2419  CA  ARG A 336       6.963 -46.192   0.078  1.00 87.73           C  
ANISOU 2419  CA  ARG A 336    14764  10290   8280   4056  -1648    415       C  
ATOM   2420  C   ARG A 336       8.334 -45.881   0.661  1.00 88.99           C  
ANISOU 2420  C   ARG A 336    14576  10906   8331   4251  -1765    473       C  
ATOM   2421  O   ARG A 336       9.300 -45.780  -0.082  1.00 89.79           O  
ANISOU 2421  O   ARG A 336    14430  11230   8455   4462  -1753    428       O  
ATOM   2422  CB  ARG A 336       6.582 -47.657   0.310  1.00 90.32           C  
ANISOU 2422  CB  ARG A 336    15513  10233   8574   4285  -1680    558       C  
ATOM   2423  CG  ARG A 336       5.308 -48.114  -0.403  1.00 89.13           C  
ANISOU 2423  CG  ARG A 336    15712   9625   8529   4115  -1572    502       C  
ATOM   2424  CD  ARG A 336       4.036 -47.562   0.235  1.00 87.26           C  
ANISOU 2424  CD  ARG A 336    15578   9294   8282   3681  -1539    504       C  
ATOM   2425  NE  ARG A 336       3.840 -46.145  -0.053  1.00 84.94           N  
ANISOU 2425  NE  ARG A 336    14985   9232   8056   3380  -1472    341       N  
ATOM   2426  CZ  ARG A 336       2.744 -45.459   0.251  1.00 83.20           C  
ANISOU 2426  CZ  ARG A 336    14795   8957   7861   3013  -1421    284       C  
ATOM   2427  NH1 ARG A 336       2.662 -44.172  -0.053  1.00 81.45           N  
ANISOU 2427  NH1 ARG A 336    14299   8920   7726   2779  -1375    137       N  
ATOM   2428  NH2 ARG A 336       1.728 -46.055   0.852  1.00 83.38           N  
ANISOU 2428  NH2 ARG A 336    15116   8741   7826   2880  -1418    381       N  
ATOM   2429  N   PRO A 337       8.423 -45.691   1.985  1.00 89.32           N  
ANISOU 2429  N   PRO A 337    14572  11129   8238   4167  -1878    570       N  
ATOM   2430  CA  PRO A 337       9.750 -45.456   2.562  1.00 91.20           C  
ANISOU 2430  CA  PRO A 337    14474  11823   8355   4357  -2003    634       C  
ATOM   2431  C   PRO A 337      10.602 -46.722   2.513  1.00 94.24           C  
ANISOU 2431  C   PRO A 337    14944  12186   8677   4859  -2071    793       C  
ATOM   2432  O   PRO A 337      10.072 -47.830   2.596  1.00 95.13           O  
ANISOU 2432  O   PRO A 337    15433  11915   8795   5019  -2071    903       O  
ATOM   2433  CB  PRO A 337       9.443 -45.088   4.016  1.00 91.81           C  
ANISOU 2433  CB  PRO A 337    14550  12052   8282   4135  -2105    697       C  
ATOM   2434  CG  PRO A 337       8.017 -44.671   4.021  1.00 88.96           C  
ANISOU 2434  CG  PRO A 337    14402  11402   7996   3759  -2005    596       C  
ATOM   2435  CD  PRO A 337       7.352 -45.502   2.977  1.00 88.12           C  
ANISOU 2435  CD  PRO A 337    14606  10854   8022   3859  -1891    600       C  
ATOM   2436  N   LEU A 338      11.913 -46.549   2.387  1.00 95.83           N  
ANISOU 2436  N   LEU A 338    14793  12795   8825   5104  -2133    807       N  
ATOM   2437  CA  LEU A 338      12.826 -47.673   2.216  1.00 99.14           C  
ANISOU 2437  CA  LEU A 338    15237  13233   9200   5630  -2191    932       C  
ATOM   2438  C   LEU A 338      12.944 -48.531   3.475  1.00102.25           C  
ANISOU 2438  C   LEU A 338    15812  13588   9451   5826  -2342   1172       C  
ATOM   2439  O   LEU A 338      12.706 -49.740   3.441  1.00103.91           O  
ANISOU 2439  O   LEU A 338    16372  13421   9689   6109  -2360   1294       O  
ATOM   2440  CB  LEU A 338      14.206 -47.164   1.788  1.00100.43           C  
ANISOU 2440  CB  LEU A 338    14917  13918   9323   5817  -2218    890       C  
ATOM   2441  CG  LEU A 338      15.272 -48.190   1.403  1.00104.14           C  
ANISOU 2441  CG  LEU A 338    15325  14487   9756   6398  -2255    975       C  
ATOM   2442  CD1 LEU A 338      14.700 -49.231   0.460  1.00104.41           C  
ANISOU 2442  CD1 LEU A 338    15749  14007   9916   6639  -2149    914       C  
ATOM   2443  CD2 LEU A 338      16.463 -47.492   0.766  1.00104.72           C  
ANISOU 2443  CD2 LEU A 338    14884  15106   9801   6488  -2239    897       C  
ATOM   2444  N   LYS A 339      13.310 -47.893   4.582  1.00103.25           N  
ANISOU 2444  N   LYS A 339    15703  14104   9424   5664  -2459   1242       N  
ATOM   2445  CA  LYS A 339      13.573 -48.604   5.829  1.00106.55           C  
ANISOU 2445  CA  LYS A 339    16218  14599   9669   5847  -2620   1492       C  
ATOM   2446  C   LYS A 339      12.564 -48.242   6.913  1.00106.34           C  
ANISOU 2446  C   LYS A 339    16355  14512   9537   5441  -2649   1532       C  
ATOM   2447  O   LYS A 339      12.242 -49.063   7.769  1.00108.20           O  
ANISOU 2447  O   LYS A 339    16839  14596   9674   5511  -2727   1748       O  
ATOM   2448  CB  LYS A 339      14.990 -48.298   6.319  1.00108.38           C  
ANISOU 2448  CB  LYS A 339    16003  15418   9759   6044  -2752   1563       C  
ATOM   2449  CG  LYS A 339      16.068 -48.506   5.268  1.00109.20           C  
ANISOU 2449  CG  LYS A 339    15848  15686   9958   6392  -2696   1494       C  
ATOM   2450  CD  LYS A 339      17.304 -47.677   5.572  1.00110.35           C  
ANISOU 2450  CD  LYS A 339    15458  16491   9981   6390  -2792   1485       C  
ATOM   2451  CE  LYS A 339      18.288 -47.725   4.415  1.00111.59           C  
ANISOU 2451  CE  LYS A 339    15323  16860  10218   6682  -2715   1397       C  
ATOM   2452  NZ  LYS A 339      19.444 -46.807   4.624  1.00113.10           N  
ANISOU 2452  NZ  LYS A 339    14966  17711  10297   6606  -2798   1383       N  
ATOM   2453  N   GLU A 340      12.070 -47.009   6.872  1.00104.44           N  
ANISOU 2453  N   GLU A 340    15959  14396   9328   5006  -2578   1321       N  
ATOM   2454  CA  GLU A 340      11.114 -46.538   7.868  1.00104.48           C  
ANISOU 2454  CA  GLU A 340    16076  14396   9227   4620  -2591   1307       C  
ATOM   2455  C   GLU A 340       9.801 -47.308   7.794  1.00104.32           C  
ANISOU 2455  C   GLU A 340    16516  13854   9266   4531  -2506   1381       C  
ATOM   2456  O   GLU A 340       9.383 -47.735   6.720  1.00102.69           O  
ANISOU 2456  O   GLU A 340    16511  13266   9242   4604  -2393   1323       O  
ATOM   2457  CB  GLU A 340      10.850 -45.044   7.684  1.00101.72           C  
ANISOU 2457  CB  GLU A 340    15474  14229   8944   4206  -2526   1032       C  
ATOM   2458  CG  GLU A 340      10.021 -44.425   8.791  1.00100.94           C  
ANISOU 2458  CG  GLU A 340    15422  14220   8713   3837  -2551    973       C  
ATOM   2459  CD  GLU A 340      10.783 -44.314  10.087  1.00 89.37           C  
ANISOU 2459  CD  GLU A 340    13748  13223   6986   3874  -2726   1077       C  
ATOM   2460  OE1 GLU A 340      12.029 -44.284  10.040  1.00 93.26           O  
ANISOU 2460  OE1 GLU A 340    13954  14046   7433   4096  -2826   1128       O  
ATOM   2461  OE2 GLU A 340      10.138 -44.257  11.153  1.00 93.88           O  
ANISOU 2461  OE2 GLU A 340    14427  13863   7381   3680  -2764   1110       O  
ATOM   2462  N   LYS A 341       9.163 -47.490   8.945  1.00106.35           N  
ANISOU 2462  N   LYS A 341    16929  14127   9351   4361  -2565   1513       N  
ATOM   2463  CA  LYS A 341       7.879 -48.172   9.012  1.00106.79           C  
ANISOU 2463  CA  LYS A 341    17397  13745   9434   4220  -2495   1609       C  
ATOM   2464  C   LYS A 341       6.775 -47.227   8.568  1.00103.88           C  
ANISOU 2464  C   LYS A 341    17038  13252   9177   3809  -2343   1354       C  
ATOM   2465  O   LYS A 341       6.795 -46.047   8.907  1.00102.21           O  
ANISOU 2465  O   LYS A 341    16560  13351   8923   3558  -2337   1164       O  
ATOM   2466  CB  LYS A 341       7.617 -48.656  10.436  1.00109.35           C  
ANISOU 2466  CB  LYS A 341    17843  14201   9504   4167  -2613   1861       C  
ATOM   2467  CG  LYS A 341       6.372 -49.514  10.589  1.00109.42           C  
ANISOU 2467  CG  LYS A 341    18278  13781   9517   4035  -2564   2027       C  
ATOM   2468  CD  LYS A 341       6.267 -50.063  12.002  1.00112.63           C  
ANISOU 2468  CD  LYS A 341    18709  14366   9719   3952  -2656   2294       C  
ATOM   2469  CE  LYS A 341       5.069 -50.985  12.152  1.00113.34           C  
ANISOU 2469  CE  LYS A 341    19149  14046   9868   3759  -2586   2469       C  
ATOM   2470  NZ  LYS A 341       4.971 -51.550  13.529  1.00116.97           N  
ANISOU 2470  NZ  LYS A 341    19610  14706  10127   3663  -2678   2764       N  
ATOM   2471  N   GLU A 342       5.814 -47.749   7.813  1.00103.92           N  
ANISOU 2471  N   GLU A 342    17354  12799   9332   3745  -2228   1347       N  
ATOM   2472  CA  GLU A 342       4.761 -46.917   7.237  1.00101.97           C  
ANISOU 2472  CA  GLU A 342    17116  12412   9214   3392  -2080   1117       C  
ATOM   2473  C   GLU A 342       3.854 -46.301   8.301  1.00102.19           C  
ANISOU 2473  C   GLU A 342    17134  12604   9089   3037  -2071   1081       C  
ATOM   2474  O   GLU A 342       3.303 -45.216   8.105  1.00 99.81           O  
ANISOU 2474  O   GLU A 342    16692  12370   8861   2757  -1984    847       O  
ATOM   2475  CB  GLU A 342       3.927 -47.714   6.227  1.00101.49           C  
ANISOU 2475  CB  GLU A 342    17396  11844   9323   3404  -1974   1137       C  
ATOM   2476  CG  GLU A 342       4.706 -48.204   5.008  1.00102.32           C  
ANISOU 2476  CG  GLU A 342    17502  11786   9588   3734  -1953   1097       C  
ATOM   2477  CD  GLU A 342       3.809 -48.782   3.925  1.00101.24           C  
ANISOU 2477  CD  GLU A 342    17670  11179   9618   3684  -1838   1046       C  
ATOM   2478  OE1 GLU A 342       4.271 -49.668   3.175  1.00102.77           O  
ANISOU 2478  OE1 GLU A 342    18010  11141   9897   3997  -1845   1079       O  
ATOM   2479  OE2 GLU A 342       2.644 -48.345   3.818  1.00 98.95           O  
ANISOU 2479  OE2 GLU A 342    17465  10762   9368   3338  -1742    959       O  
ATOM   2480  N   GLU A 343       3.705 -46.995   9.426  1.00105.03           N  
ANISOU 2480  N   GLU A 343    17638  13036   9232   3059  -2162   1317       N  
ATOM   2481  CA  GLU A 343       2.838 -46.530  10.503  1.00105.23           C  
ANISOU 2481  CA  GLU A 343    17657  13259   9067   2743  -2151   1299       C  
ATOM   2482  C   GLU A 343       3.340 -45.228  11.109  1.00104.76           C  
ANISOU 2482  C   GLU A 343    17227  13666   8909   2610  -2193   1072       C  
ATOM   2483  O   GLU A 343       2.566 -44.449  11.659  1.00104.09           O  
ANISOU 2483  O   GLU A 343    17077  13730   8742   2319  -2142    910       O  
ATOM   2484  CB  GLU A 343       2.728 -47.588  11.599  1.00108.83           C  
ANISOU 2484  CB  GLU A 343    18318  13750   9282   2814  -2258   1639       C  
ATOM   2485  CG  GLU A 343       1.990 -48.842  11.185  1.00109.77           C  
ANISOU 2485  CG  GLU A 343    18843  13381   9484   2854  -2224   1871       C  
ATOM   2486  CD  GLU A 343       1.569 -49.675  12.374  1.00113.08           C  
ANISOU 2486  CD  GLU A 343    19450  13855   9659   2788  -2310   2201       C  
ATOM   2487  OE1 GLU A 343       1.694 -49.183  13.516  1.00114.29           O  
ANISOU 2487  OE1 GLU A 343    19420  14457   9548   2680  -2375   2222       O  
ATOM   2488  OE2 GLU A 343       1.110 -50.817  12.168  1.00114.80           O  
ANISOU 2488  OE2 GLU A 343    19908  13690  10020   2783  -2279   2401       O  
ATOM   2489  N   ASN A 344       4.643 -45.004  11.006  1.00105.66           N  
ANISOU 2489  N   ASN A 344    17097  14018   9032   2826  -2292   1051       N  
ATOM   2490  CA  ASN A 344       5.256 -43.806  11.552  1.00105.58           C  
ANISOU 2490  CA  ASN A 344    16732  14446   8937   2700  -2358    840       C  
ATOM   2491  C   ASN A 344       4.859 -42.559  10.772  1.00101.74           C  
ANISOU 2491  C   ASN A 344    16096  13885   8674   2457  -2248    511       C  
ATOM   2492  O   ASN A 344       5.031 -41.444  11.250  1.00101.48           O  
ANISOU 2492  O   ASN A 344    15820  14138   8599   2267  -2285    290       O  
ATOM   2493  CB  ASN A 344       6.775 -43.956  11.558  1.00109.15           C  
ANISOU 2493  CB  ASN A 344    16951  15173   9349   2994  -2496    930       C  
ATOM   2494  CG  ASN A 344       7.222 -45.282  12.132  1.00113.95           C  
ANISOU 2494  CG  ASN A 344    17721  15787   9788   3299  -2610   1284       C  
ATOM   2495  OD1 ASN A 344       6.412 -46.178  12.359  1.00115.15           O  
ANISOU 2495  OD1 ASN A 344    18195  15665   9893   3298  -2581   1480       O  
ATOM   2496  ND2 ASN A 344       8.519 -45.413  12.373  1.00117.19           N  
ANISOU 2496  ND2 ASN A 344    17905  16512  10111   3558  -2748   1383       N  
ATOM   2497  N   LEU A 345       4.320 -42.755   9.574  1.00 98.59           N  
ANISOU 2497  N   LEU A 345    15852  13094   8515   2460  -2120    479       N  
ATOM   2498  CA  LEU A 345       3.987 -41.639   8.694  1.00 94.71           C  
ANISOU 2498  CA  LEU A 345    15223  12505   8257   2257  -2021    211       C  
ATOM   2499  C   LEU A 345       2.506 -41.296   8.685  1.00 92.66           C  
ANISOU 2499  C   LEU A 345    15124  12032   8051   1977  -1894     94       C  
ATOM   2500  O   LEU A 345       1.694 -41.956   9.335  1.00 93.69           O  
ANISOU 2500  O   LEU A 345    15472  12095   8029   1924  -1872    222       O  
ATOM   2501  CB  LEU A 345       4.440 -41.938   7.268  1.00 91.71           C  
ANISOU 2501  CB  LEU A 345    14849  11895   8103   2438  -1963    233       C  
ATOM   2502  CG  LEU A 345       5.938 -41.827   7.036  1.00 91.30           C  
ANISOU 2502  CG  LEU A 345    14522  12117   8051   2665  -2064    259       C  
ATOM   2503  CD1 LEU A 345       6.252 -42.039   5.573  1.00 89.24           C  
ANISOU 2503  CD1 LEU A 345    14253  11655   7999   2816  -1981    250       C  
ATOM   2504  CD2 LEU A 345       6.409 -40.466   7.498  1.00 90.50           C  
ANISOU 2504  CD2 LEU A 345    14086  12360   7941   2449  -2134     57       C  
ATOM   2505  N   VAL A 346       2.166 -40.252   7.938  1.00 90.28           N  
ANISOU 2505  N   VAL A 346    14697  11639   7967   1798  -1816   -136       N  
ATOM   2506  CA  VAL A 346       0.778 -39.866   7.753  1.00 88.73           C  
ANISOU 2506  CA  VAL A 346    14622  11234   7858   1558  -1689   -256       C  
ATOM   2507  C   VAL A 346       0.362 -40.198   6.329  1.00 86.70           C  
ANISOU 2507  C   VAL A 346    14499  10612   7832   1590  -1577   -221       C  
ATOM   2508  O   VAL A 346       1.120 -39.971   5.389  1.00 86.56           O  
ANISOU 2508  O   VAL A 346    14351  10565   7973   1691  -1583   -249       O  
ATOM   2509  CB  VAL A 346       0.580 -38.367   7.997  1.00 88.92           C  
ANISOU 2509  CB  VAL A 346    14413  11405   7968   1325  -1690   -553       C  
ATOM   2510  CG1 VAL A 346      -0.899 -38.037   8.091  1.00 87.96           C  
ANISOU 2510  CG1 VAL A 346    14410  11132   7880   1110  -1570   -668       C  
ATOM   2511  CG2 VAL A 346       1.293 -37.946   9.265  1.00 91.78           C  
ANISOU 2511  CG2 VAL A 346    14595  12166   8113   1314  -1825   -626       C  
ATOM   2512  N   ASN A 347      -0.836 -40.749   6.175  1.00 85.25           N  
ANISOU 2512  N   ASN A 347    14563  10181   7649   1492  -1478   -157       N  
ATOM   2513  CA  ASN A 347      -1.358 -41.082   4.856  1.00 82.82           C  
ANISOU 2513  CA  ASN A 347    14394   9536   7537   1491  -1373   -136       C  
ATOM   2514  C   ASN A 347      -2.745 -40.498   4.624  1.00 80.43           C  
ANISOU 2514  C   ASN A 347    14133   9098   7329   1225  -1256   -261       C  
ATOM   2515  O   ASN A 347      -3.223 -39.674   5.401  1.00 79.66           O  
ANISOU 2515  O   ASN A 347    13921   9169   7178   1057  -1253   -404       O  
ATOM   2516  CB  ASN A 347      -1.396 -42.596   4.656  1.00 84.04           C  
ANISOU 2516  CB  ASN A 347    14850   9460   7620   1670  -1376    103       C  
ATOM   2517  CG  ASN A 347      -2.193 -43.301   5.730  1.00 85.51           C  
ANISOU 2517  CG  ASN A 347    15249   9643   7599   1579  -1387    255       C  
ATOM   2518  OD1 ASN A 347      -1.663 -43.640   6.788  1.00 87.98           O  
ANISOU 2518  OD1 ASN A 347    15551  10166   7711   1672  -1488    375       O  
ATOM   2519  ND2 ASN A 347      -3.473 -43.527   5.466  1.00 84.30           N  
ANISOU 2519  ND2 ASN A 347    15275   9276   7478   1383  -1286    269       N  
ATOM   2520  N   SER A 348      -3.389 -40.934   3.547  1.00 79.51           N  
ANISOU 2520  N   SER A 348    14174   8690   7347   1197  -1164   -218       N  
ATOM   2521  CA  SER A 348      -4.735 -40.479   3.225  1.00 78.19           C  
ANISOU 2521  CA  SER A 348    14044   8394   7270    959  -1054   -309       C  
ATOM   2522  C   SER A 348      -5.756 -41.144   4.141  1.00 80.29           C  
ANISOU 2522  C   SER A 348    14506   8659   7340    840  -1025   -200       C  
ATOM   2523  O   SER A 348      -6.031 -42.337   4.020  1.00 81.11           O  
ANISOU 2523  O   SER A 348    14869   8577   7373    882  -1019     -7       O  
ATOM   2524  CB  SER A 348      -5.064 -40.783   1.766  1.00 75.81           C  
ANISOU 2524  CB  SER A 348    13840   7816   7150    960   -975   -286       C  
ATOM   2525  OG  SER A 348      -4.041 -40.315   0.909  1.00 74.97           O  
ANISOU 2525  OG  SER A 348    13554   7745   7188   1084  -1002   -346       O  
ATOM   2526  N   LEU A 349      -6.320 -40.359   5.051  1.00 81.58           N  
ANISOU 2526  N   LEU A 349    14543   9035   7418    685  -1010   -329       N  
ATOM   2527  CA  LEU A 349      -7.232 -40.885   6.057  1.00 84.01           C  
ANISOU 2527  CA  LEU A 349    14984   9438   7499    561   -982   -229       C  
ATOM   2528  C   LEU A 349      -8.684 -40.798   5.596  1.00 83.05           C  
ANISOU 2528  C   LEU A 349    14930   9180   7446    351   -856   -259       C  
ATOM   2529  O   LEU A 349      -9.555 -40.325   6.327  1.00 83.63           O  
ANISOU 2529  O   LEU A 349    14927   9436   7412    198   -803   -349       O  
ATOM   2530  CB  LEU A 349      -7.041 -40.135   7.375  1.00 86.41           C  
ANISOU 2530  CB  LEU A 349    15100  10108   7623    523  -1033   -366       C  
ATOM   2531  CG  LEU A 349      -5.578 -39.945   7.788  1.00 88.83           C  
ANISOU 2531  CG  LEU A 349    15271  10600   7882    703  -1166   -385       C  
ATOM   2532  CD1 LEU A 349      -5.460 -39.167   9.089  1.00 90.98           C  
ANISOU 2532  CD1 LEU A 349    15358  11246   7963    638  -1219   -553       C  
ATOM   2533  CD2 LEU A 349      -4.867 -41.284   7.900  1.00 91.07           C  
ANISOU 2533  CD2 LEU A 349    15745  10815   8041    894  -1245    -95       C  
TER    2534      LEU A 349                                                      
ATOM   2535  N   ASP B   1       3.706 -18.813 -22.014  1.00 97.51           N  
ANISOU 2535  N   ASP B   1    13021  12316  11711  -5028   1561  -1152       N  
ATOM   2536  CA  ASP B   1       2.972 -18.330 -23.176  1.00 96.97           C  
ANISOU 2536  CA  ASP B   1    12987  12009  11847  -4939   1528   -987       C  
ATOM   2537  C   ASP B   1       1.850 -17.385 -22.759  1.00 96.97           C  
ANISOU 2537  C   ASP B   1    13180  11640  12025  -4944   1610  -1022       C  
ATOM   2538  O   ASP B   1       0.711 -17.805 -22.573  1.00 96.08           O  
ANISOU 2538  O   ASP B   1    13050  11403  12053  -4788   1681  -1009       O  
ATOM   2539  CB  ASP B   1       2.407 -19.507 -23.968  1.00 95.25           C  
ANISOU 2539  CB  ASP B   1    12590  11864  11738  -4705   1482   -845       C  
ATOM   2540  CG  ASP B   1       1.670 -19.068 -25.214  1.00 96.23           C  
ANISOU 2540  CG  ASP B   1    12739  11775  12050  -4633   1439   -686       C  
ATOM   2541  OD1 ASP B   1       2.322 -18.920 -26.268  1.00 97.13           O  
ANISOU 2541  OD1 ASP B   1    12809  11996  12101  -4703   1361   -606       O  
ATOM   2542  OD2 ASP B   1       0.439 -18.876 -25.142  1.00 96.39           O  
ANISOU 2542  OD2 ASP B   1    12825  11534  12266  -4528   1490   -657       O  
ATOM   2543  N   SER B   2       2.180 -16.105 -22.613  1.00 98.17           N  
ANISOU 2543  N   SER B   2    13507  11609  12185  -5134   1598  -1090       N  
ATOM   2544  CA  SER B   2       1.204 -15.111 -22.184  1.00 98.50           C  
ANISOU 2544  CA  SER B   2    13743  11266  12416  -5154   1646  -1177       C  
ATOM   2545  C   SER B   2       0.846 -14.156 -23.312  1.00 98.47           C  
ANISOU 2545  C   SER B   2    13875  10929  12611  -5179   1527  -1023       C  
ATOM   2546  O   SER B   2       1.643 -13.930 -24.220  1.00 98.84           O  
ANISOU 2546  O   SER B   2    13912  11057  12585  -5285   1436   -879       O  
ATOM   2547  CB  SER B   2       1.730 -14.327 -20.982  1.00101.45           C  
ANISOU 2547  CB  SER B   2    14243  11611  12691  -5352   1701  -1417       C  
ATOM   2548  OG  SER B   2       2.024 -15.191 -19.899  1.00100.51           O  
ANISOU 2548  OG  SER B   2    14030  11794  12364  -5361   1810  -1563       O  
ATOM   2549  N   GLY B   3      -0.358 -13.597 -23.250  1.00 98.35           N  
ANISOU 2549  N   GLY B   3    13995  10535  12838  -5098   1529  -1072       N  
ATOM   2550  CA  GLY B   3      -0.815 -12.683 -24.280  1.00 99.43           C  
ANISOU 2550  CA  GLY B   3    14305  10290  13186  -5114   1381   -930       C  
ATOM   2551  C   GLY B   3      -2.247 -12.230 -24.089  1.00 99.66           C  
ANISOU 2551  C   GLY B   3    14466   9894  13506  -4974   1370  -1058       C  
ATOM   2552  O   GLY B   3      -2.912 -12.615 -23.123  1.00 79.66           O  
ANISOU 2552  O   GLY B   3    11871   7392  11003  -4878   1521  -1284       O  
ATOM   2553  N   CYS B   4      -2.721 -11.404 -25.016  1.00100.99           N  
ANISOU 2553  N   CYS B   4    14827   9660  13887  -4968   1194   -938       N  
ATOM   2554  CA  CYS B   4      -4.087 -10.900 -24.964  1.00102.08           C  
ANISOU 2554  CA  CYS B   4    15114   9332  14341  -4801   1125  -1097       C  
ATOM   2555  C   CYS B   4      -4.799 -11.108 -26.299  1.00101.22           C  
ANISOU 2555  C   CYS B   4    15035   9046  14380  -4673    998   -887       C  
ATOM   2556  O   CYS B   4      -4.225 -10.881 -27.364  1.00101.97           O  
ANISOU 2556  O   CYS B   4    15203   9144  14397  -4789    881   -609       O  
ATOM   2557  CB  CYS B   4      -4.105  -9.418 -24.579  1.00106.51           C  
ANISOU 2557  CB  CYS B   4    15965   9412  15090  -4884    958  -1253       C  
ATOM   2558  SG  CYS B   4      -3.331  -9.036 -22.987  1.00102.24           S  
ANISOU 2558  SG  CYS B   4    15413   9033  14402  -5043   1087  -1561       S  
ATOM   2559  N   VAL B   5      -6.049 -11.557 -26.232  1.00100.09           N  
ANISOU 2559  N   VAL B   5    14827   8768  14436  -4445   1047  -1049       N  
ATOM   2560  CA  VAL B   5      -6.846 -11.804 -27.432  1.00100.11           C  
ANISOU 2560  CA  VAL B   5    14856   8579  14601  -4298    926   -908       C  
ATOM   2561  C   VAL B   5      -8.211 -11.127 -27.284  1.00103.64           C  
ANISOU 2561  C   VAL B   5    15483   8479  15417  -4063    810  -1202       C  
ATOM   2562  O   VAL B   5      -8.695 -10.953 -26.169  1.00104.16           O  
ANISOU 2562  O   VAL B   5    15506   8486  15584  -3969    932  -1561       O  
ATOM   2563  CB  VAL B   5      -7.026 -13.317 -27.683  1.00 78.11           C  
ANISOU 2563  CB  VAL B   5    11728   6237  11712  -4197   1104   -840       C  
ATOM   2564  CG1 VAL B   5      -7.652 -13.568 -29.038  1.00 78.03           C  
ANISOU 2564  CG1 VAL B   5    11745   6068  11834  -4090    968   -678       C  
ATOM   2565  CG2 VAL B   5      -5.692 -14.035 -27.594  1.00 75.67           C  
ANISOU 2565  CG2 VAL B   5    11220   6468  11063  -4345   1196   -660       C  
ATOM   2566  N   VAL B   6      -8.820 -10.732 -28.401  1.00107.10           N  
ANISOU 2566  N   VAL B   6    16121   8524  16049  -3943    571  -1087       N  
ATOM   2567  CA  VAL B   6     -10.124 -10.069 -28.366  1.00111.63           C  
ANISOU 2567  CA  VAL B   6    16871   8542  17000  -3633    396  -1405       C  
ATOM   2568  C   VAL B   6     -11.163 -10.774 -29.235  1.00111.67           C  
ANISOU 2568  C   VAL B   6    16772   8469  17190  -3368    380  -1438       C  
ATOM   2569  O   VAL B   6     -10.903 -11.090 -30.395  1.00110.64           O  
ANISOU 2569  O   VAL B   6    16711   8379  16949  -3451    281  -1100       O  
ATOM   2570  CB  VAL B   6     -10.022  -8.579 -28.779  1.00127.59           C  
ANISOU 2570  CB  VAL B   6    19309   9975  19193  -3641     29  -1327       C  
ATOM   2571  CG1 VAL B   6      -9.146  -8.419 -30.006  1.00128.02           C  
ANISOU 2571  CG1 VAL B   6    19521  10090  19032  -3885    -64   -826       C  
ATOM   2572  CG2 VAL B   6     -11.404  -7.982 -29.019  1.00130.98           C  
ANISOU 2572  CG2 VAL B   6    19921   9812  20034  -3228   -241  -1634       C  
ATOM   2573  N   SER B   7     -12.337 -11.024 -28.662  1.00113.39           N  
ANISOU 2573  N   SER B   7    16759   8620  17702  -3030    497  -1881       N  
ATOM   2574  CA  SER B   7     -13.441 -11.615 -29.408  1.00114.34           C  
ANISOU 2574  CA  SER B   7    16649   8746  18049  -2641    423  -1966       C  
ATOM   2575  C   SER B   7     -14.491 -10.570 -29.755  1.00120.85           C  
ANISOU 2575  C   SER B   7    17686   9004  19229  -2221     36  -2215       C  
ATOM   2576  O   SER B   7     -15.136 -10.012 -28.871  1.00123.49           O  
ANISOU 2576  O   SER B   7    17964   9155  19800  -2006     34  -2666       O  
ATOM   2577  CB  SER B   7     -14.090 -12.742 -28.613  1.00111.82           C  
ANISOU 2577  CB  SER B   7    15806   8882  17799  -2491    784  -2265       C  
ATOM   2578  OG  SER B   7     -15.237 -13.218 -29.291  1.00112.17           O  
ANISOU 2578  OG  SER B   7    15597   8926  18096  -2088    685  -2403       O  
ATOM   2579  N   TRP B   8     -14.660 -10.319 -31.048  1.00124.05           N  
ANISOU 2579  N   TRP B   8    18329   9146  19657  -2091   -308  -1938       N  
ATOM   2580  CA  TRP B   8     -15.601  -9.313 -31.524  1.00130.78           C  
ANISOU 2580  CA  TRP B   8    19447   9411  20834  -1671   -763  -2121       C  
ATOM   2581  C   TRP B   8     -17.047  -9.696 -31.231  1.00130.76           C  
ANISOU 2581  C   TRP B   8    19004   9484  21195  -1133   -745  -2657       C  
ATOM   2582  O   TRP B   8     -17.806  -8.906 -30.668  1.00134.58           O  
ANISOU 2582  O   TRP B   8    19507   9745  21881   -814   -886  -3057       O  
ATOM   2583  CB  TRP B   8     -15.416  -9.095 -33.026  1.00134.21           C  
ANISOU 2583  CB  TRP B   8    20238   9618  21139  -1674  -1126  -1650       C  
ATOM   2584  CG  TRP B   8     -14.204  -8.292 -33.363  1.00137.64           C  
ANISOU 2584  CG  TRP B   8    21190   9833  21273  -2152  -1233  -1185       C  
ATOM   2585  CD1 TRP B   8     -12.903  -8.648 -33.165  1.00135.17           C  
ANISOU 2585  CD1 TRP B   8    20865   9890  20601  -2699   -927   -884       C  
ATOM   2586  CD2 TRP B   8     -14.178  -6.995 -33.966  1.00144.10           C  
ANISOU 2586  CD2 TRP B   8    22482  10197  22072  -2091  -1591   -970       C  
ATOM   2587  NE1 TRP B   8     -12.069  -7.650 -33.603  1.00138.97           N  
ANISOU 2587  NE1 TRP B   8    21713  10211  20878  -2967  -1056   -525       N  
ATOM   2588  CE2 TRP B   8     -12.828  -6.624 -34.101  1.00144.68           C  
ANISOU 2588  CE2 TRP B   8    22777  10392  21801  -2631  -1466   -548       C  
ATOM   2589  CE3 TRP B   8     -15.168  -6.110 -34.404  1.00149.87           C  
ANISOU 2589  CE3 TRP B   8    23434  10461  23047  -1617  -2016  -1103       C  
ATOM   2590  CZ2 TRP B   8     -12.440  -5.403 -34.655  1.00150.60           C  
ANISOU 2590  CZ2 TRP B   8    23983  10777  22462  -2747  -1744   -241       C  
ATOM   2591  CZ3 TRP B   8     -14.783  -4.900 -34.955  1.00155.54           C  
ANISOU 2591  CZ3 TRP B   8    24648  10785  23664  -1730  -2321   -775       C  
ATOM   2592  CH2 TRP B   8     -13.431  -4.558 -35.075  1.00155.88           C  
ANISOU 2592  CH2 TRP B   8    24925  10927  23376  -2307  -2177   -341       C  
ATOM   2593  N   LYS B   9     -17.417 -10.912 -31.622  1.00126.42           N  
ANISOU 2593  N   LYS B   9    18032   9385  20616  -1033   -546  -2632       N  
ATOM   2594  CA  LYS B   9     -18.774 -11.405 -31.437  1.00126.07           C  
ANISOU 2594  CA  LYS B   9    17518   9474  20911   -571   -495  -3128       C  
ATOM   2595  C   LYS B   9     -19.132 -11.458 -29.957  1.00125.62           C  
ANISOU 2595  C   LYS B   9    17145   9614  20969   -578   -144  -3621       C  
ATOM   2596  O   LYS B   9     -20.195 -10.995 -29.550  1.00129.29           O  
ANISOU 2596  O   LYS B   9    17444  10044  21637   -187   -242  -4064       O  
ATOM   2597  CB  LYS B   9     -18.925 -12.787 -32.077  1.00121.98           C  
ANISOU 2597  CB  LYS B   9    16605   9429  20312   -561   -304  -2969       C  
ATOM   2598  CG  LYS B   9     -18.470 -12.847 -33.530  1.00121.59           C  
ANISOU 2598  CG  LYS B   9    16829   9298  20071   -597   -603  -2478       C  
ATOM   2599  CD  LYS B   9     -18.673 -14.233 -34.123  1.00117.88           C  
ANISOU 2599  CD  LYS B   9    15921   9306  19562   -550   -427  -2401       C  
ATOM   2600  CE  LYS B   9     -18.205 -14.294 -35.569  1.00117.43           C  
ANISOU 2600  CE  LYS B   9    16114   9230  19273   -585   -716  -1946       C  
ATOM   2601  NZ  LYS B   9     -18.486 -15.619 -36.189  1.00114.04           N  
ANISOU 2601  NZ  LYS B   9    15235   9245  18851   -481   -592  -1940       N  
ATOM   2602  N   ASN B  10     -18.232 -12.011 -29.152  1.00121.63           N  
ANISOU 2602  N   ASN B  10    16557   9487  20168  -1015    260  -3458       N  
ATOM   2603  CA  ASN B  10     -18.439 -12.076 -27.712  1.00121.60           C  
ANISOU 2603  CA  ASN B  10    16298   9720  20182  -1082    613  -3869       C  
ATOM   2604  C   ASN B  10     -18.327 -10.690 -27.093  1.00125.03           C  
ANISOU 2604  C   ASN B  10    17064   9789  20652  -1033    397  -4077       C  
ATOM   2605  O   ASN B  10     -18.755 -10.472 -25.958  1.00126.98           O  
ANISOU 2605  O   ASN B  10    17107  10201  20938   -956    583  -4504       O  
ATOM   2606  CB  ASN B  10     -17.425 -13.023 -27.069  1.00118.11           C  
ANISOU 2606  CB  ASN B  10    15740   9770  19365  -1553   1040  -3581       C  
ATOM   2607  CG  ASN B  10     -17.748 -13.338 -25.624  1.00119.36           C  
ANISOU 2607  CG  ASN B  10    15589  10270  19492  -1620   1443  -3973       C  
ATOM   2608  OD1 ASN B  10     -18.890 -13.210 -25.187  1.00122.47           O  
ANISOU 2608  OD1 ASN B  10    15703  10680  20151  -1316   1498  -4477       O  
ATOM   2609  ND2 ASN B  10     -16.737 -13.759 -24.873  1.00117.40           N  
ANISOU 2609  ND2 ASN B  10    15382  10327  18899  -2024   1723  -3758       N  
ATOM   2610  N   LYS B  11     -17.753  -9.763 -27.856  1.00125.86           N  
ANISOU 2610  N   LYS B  11    17682   9431  20706  -1086     -1  -3749       N  
ATOM   2611  CA  LYS B  11     -17.533  -8.395 -27.402  1.00128.89           C  
ANISOU 2611  CA  LYS B  11    18456   9430  21085  -1071   -257  -3851       C  
ATOM   2612  C   LYS B  11     -16.717  -8.386 -26.121  1.00126.33           C  
ANISOU 2612  C   LYS B  11    18091   9355  20553  -1438     73  -3946       C  
ATOM   2613  O   LYS B  11     -16.957  -7.580 -25.225  1.00129.68           O  
ANISOU 2613  O   LYS B  11    18549   9682  21040  -1321     28  -4312       O  
ATOM   2614  CB  LYS B  11     -18.863  -7.676 -27.186  1.00133.84           C  
ANISOU 2614  CB  LYS B  11    18965   9893  21997   -525   -492  -4350       C  
ATOM   2615  CG  LYS B  11     -19.662  -7.440 -28.450  1.00136.12           C  
ANISOU 2615  CG  LYS B  11    19357   9896  22466   -123   -897  -4259       C  
ATOM   2616  CD  LYS B  11     -20.939  -6.684 -28.130  1.00141.68           C  
ANISOU 2616  CD  LYS B  11    19898  10500  23432    399  -1118  -4774       C  
ATOM   2617  CE  LYS B  11     -21.599  -6.157 -29.389  1.00145.65           C  
ANISOU 2617  CE  LYS B  11    20611  10640  24088    785  -1607  -4643       C  
ATOM   2618  NZ  LYS B  11     -22.804  -5.346 -29.073  1.00151.99           N  
ANISOU 2618  NZ  LYS B  11    21245  11351  25154   1281  -1858  -5145       N  
ATOM   2619  N   GLU B  12     -15.754  -9.296 -26.042  1.00120.58           N  
ANISOU 2619  N   GLU B  12    17279   8985  19553  -1866    397  -3619       N  
ATOM   2620  CA  GLU B  12     -14.951  -9.452 -24.840  1.00118.08           C  
ANISOU 2620  CA  GLU B  12    16891   8997  18977  -2209    729  -3677       C  
ATOM   2621  C   GLU B  12     -13.516  -9.820 -25.194  1.00113.67           C  
ANISOU 2621  C   GLU B  12    16522   8617  18052  -2685    802  -3127       C  
ATOM   2622  O   GLU B  12     -13.274 -10.581 -26.129  1.00111.11           O  
ANISOU 2622  O   GLU B  12    16152   8428  17637  -2776    818  -2768       O  
ATOM   2623  CB  GLU B  12     -15.563 -10.521 -23.928  1.00116.07           C  
ANISOU 2623  CB  GLU B  12    16127   9252  18720  -2163   1189  -4015       C  
ATOM   2624  CG  GLU B  12     -14.779 -10.778 -22.648  1.00114.80           C  
ANISOU 2624  CG  GLU B  12    15903   9464  18253  -2512   1544  -4081       C  
ATOM   2625  CD  GLU B  12     -15.433 -11.811 -21.752  1.00113.55           C  
ANISOU 2625  CD  GLU B  12    15289   9828  18026  -2479   1978  -4352       C  
ATOM   2626  OE1 GLU B  12     -16.635 -12.093 -21.937  1.00114.67           O  
ANISOU 2626  OE1 GLU B  12    15135  10008  18427  -2156   2008  -4636       O  
ATOM   2627  OE2 GLU B  12     -14.740 -12.340 -20.859  1.00111.90           O  
ANISOU 2627  OE2 GLU B  12    15021  10010  17486  -2782   2276  -4269       O  
ATOM   2628  N   LEU B  13     -12.568  -9.268 -24.445  1.00113.11           N  
ANISOU 2628  N   LEU B  13    16623   8586  17766  -2962    825  -3088       N  
ATOM   2629  CA  LEU B  13     -11.163  -9.608 -24.611  1.00109.32           C  
ANISOU 2629  CA  LEU B  13    16226   8395  16915  -3376    893  -2627       C  
ATOM   2630  C   LEU B  13     -10.598 -10.143 -23.300  1.00106.88           C  
ANISOU 2630  C   LEU B  13    15697   8566  16346  -3575   1252  -2772       C  
ATOM   2631  O   LEU B  13     -11.176  -9.929 -22.236  1.00109.14           O  
ANISOU 2631  O   LEU B  13    15867   8869  16730  -3455   1405  -3227       O  
ATOM   2632  CB  LEU B  13     -10.360  -8.397 -25.080  1.00112.81           C  
ANISOU 2632  CB  LEU B  13    17075   8449  17340  -3546    530  -2379       C  
ATOM   2633  CG  LEU B  13     -10.202  -7.212 -24.129  1.00117.59           C  
ANISOU 2633  CG  LEU B  13    17865   8773  18040  -3554    397  -2686       C  
ATOM   2634  CD1 LEU B  13      -8.931  -6.455 -24.462  1.00119.53           C  
ANISOU 2634  CD1 LEU B  13    18340   8904  18171  -3876    201  -2335       C  
ATOM   2635  CD2 LEU B  13     -11.401  -6.284 -24.209  1.00122.36           C  
ANISOU 2635  CD2 LEU B  13    18656   8810  19025  -3162     91  -3052       C  
ATOM   2636  N   LYS B  14      -9.467 -10.837 -23.381  1.00102.37           N  
ANISOU 2636  N   LYS B  14    15057   8404  15433  -3855   1368  -2409       N  
ATOM   2637  CA  LYS B  14      -8.887 -11.490 -22.213  1.00 99.55           C  
ANISOU 2637  CA  LYS B  14    14511   8516  14796  -4029   1680  -2503       C  
ATOM   2638  C   LYS B  14      -7.365 -11.582 -22.324  1.00 97.27           C  
ANISOU 2638  C   LYS B  14    14278   8508  14171  -4302   1624  -2149       C  
ATOM   2639  O   LYS B  14      -6.820 -11.750 -23.416  1.00 95.61           O  
ANISOU 2639  O   LYS B  14    14096   8341  13891  -4355   1466  -1780       O  
ATOM   2640  CB  LYS B  14      -9.508 -12.882 -22.034  1.00 95.99           C  
ANISOU 2640  CB  LYS B  14    13726   8427  14319  -3950   1985  -2541       C  
ATOM   2641  CG  LYS B  14      -8.931 -13.726 -20.902  1.00 94.19           C  
ANISOU 2641  CG  LYS B  14    13332   8683  13775  -4137   2286  -2572       C  
ATOM   2642  CD  LYS B  14      -9.026 -13.026 -19.553  1.00 97.36           C  
ANISOU 2642  CD  LYS B  14    13797   9047  14147  -4210   2426  -3009       C  
ATOM   2643  CE  LYS B  14      -8.705 -13.979 -18.406  1.00 96.27           C  
ANISOU 2643  CE  LYS B  14    13500   9380  13698  -4399   2755  -3078       C  
ATOM   2644  NZ  LYS B  14      -7.470 -14.775 -18.648  1.00 93.31           N  
ANISOU 2644  NZ  LYS B  14    13107   9351  12994  -4541   2700  -2643       N  
ATOM   2645  N   CYS B  15      -6.691 -11.451 -21.186  1.00 97.75           N  
ANISOU 2645  N   CYS B  15    14333   8776  14031  -4462   1758  -2312       N  
ATOM   2646  CA  CYS B  15      -5.241 -11.563 -21.117  1.00 96.50           C  
ANISOU 2646  CA  CYS B  15    14179   8920  13566  -4688   1728  -2076       C  
ATOM   2647  C   CYS B  15      -4.838 -12.685 -20.178  1.00 93.72           C  
ANISOU 2647  C   CYS B  15    13620   9069  12921  -4760   1995  -2129       C  
ATOM   2648  O   CYS B  15      -5.616 -13.087 -19.313  1.00 93.62           O  
ANISOU 2648  O   CYS B  15    13511   9132  12928  -4711   2227  -2400       O  
ATOM   2649  CB  CYS B  15      -4.640 -10.256 -20.606  1.00100.37           C  
ANISOU 2649  CB  CYS B  15    14891   9162  14083  -4832   1584  -2233       C  
ATOM   2650  SG  CYS B  15      -4.890  -8.856 -21.699  1.00 91.56           S  
ANISOU 2650  SG  CYS B  15    14078   7412  13298  -4792   1203  -2111       S  
ATOM   2651  N   GLY B  16      -3.619 -13.187 -20.341  1.00 91.81           N  
ANISOU 2651  N   GLY B  16    13308   9166  12408  -4879   1957  -1893       N  
ATOM   2652  CA  GLY B  16      -3.089 -14.158 -19.402  1.00 89.87           C  
ANISOU 2652  CA  GLY B  16    12922   9350  11873  -4951   2139  -1947       C  
ATOM   2653  C   GLY B  16      -2.221 -15.217 -20.042  1.00 86.17           C  
ANISOU 2653  C   GLY B  16    12292   9235  11213  -4918   2064  -1651       C  
ATOM   2654  O   GLY B  16      -1.750 -15.048 -21.165  1.00 85.71           O  
ANISOU 2654  O   GLY B  16    12229   9142  11194  -4900   1887  -1428       O  
ATOM   2655  N   SER B  17      -2.011 -16.311 -19.315  1.00 83.79           N  
ANISOU 2655  N   SER B  17    11864   9266  10705  -4917   2190  -1671       N  
ATOM   2656  CA  SER B  17      -1.216 -17.433 -19.802  1.00 80.58           C  
ANISOU 2656  CA  SER B  17    11294   9177  10143  -4849   2091  -1453       C  
ATOM   2657  C   SER B  17      -2.105 -18.478 -20.463  1.00 79.06           C  
ANISOU 2657  C   SER B  17    10938   9002  10101  -4620   2101  -1292       C  
ATOM   2658  O   SER B  17      -3.326 -18.342 -20.472  1.00 79.04           O  
ANISOU 2658  O   SER B  17    10938   8792  10300  -4535   2213  -1360       O  
ATOM   2659  CB  SER B  17      -0.444 -18.071 -18.649  1.00 79.59           C  
ANISOU 2659  CB  SER B  17    11150   9364   9727  -4977   2163  -1559       C  
ATOM   2660  OG  SER B  17       0.139 -19.299 -19.042  1.00 76.63           O  
ANISOU 2660  OG  SER B  17    10612   9252   9252  -4880   2056  -1386       O  
ATOM   2661  N   GLY B  18      -1.489 -19.516 -21.020  1.00 78.13           N  
ANISOU 2661  N   GLY B  18    10661   9122   9904  -4525   1982  -1116       N  
ATOM   2662  CA  GLY B  18      -2.244 -20.604 -21.616  1.00 77.35           C  
ANISOU 2662  CA  GLY B  18    10388   9049   9954  -4310   1969   -974       C  
ATOM   2663  C   GLY B  18      -1.723 -21.099 -22.954  1.00 76.88           C  
ANISOU 2663  C   GLY B  18    10182   9087   9941  -4200   1777   -791       C  
ATOM   2664  O   GLY B  18      -0.514 -21.172 -23.164  1.00 77.13           O  
ANISOU 2664  O   GLY B  18    10185   9310   9809  -4282   1669   -775       O  
ATOM   2665  N   ILE B  19      -2.636 -21.455 -23.857  1.00 76.34           N  
ANISOU 2665  N   ILE B  19    10008   8907  10091  -4033   1748   -690       N  
ATOM   2666  CA  ILE B  19      -2.257 -21.954 -25.181  1.00 75.69           C  
ANISOU 2666  CA  ILE B  19     9778   8926  10056  -3940   1589   -543       C  
ATOM   2667  C   ILE B  19      -3.111 -21.351 -26.304  1.00 77.16           C  
ANISOU 2667  C   ILE B  19     9990   8880  10445  -3892   1549   -473       C  
ATOM   2668  O   ILE B  19      -4.337 -21.343 -26.225  1.00 77.07           O  
ANISOU 2668  O   ILE B  19     9978   8677  10629  -3803   1631   -517       O  
ATOM   2669  CB  ILE B  19      -2.303 -23.495 -25.243  1.00 73.45           C  
ANISOU 2669  CB  ILE B  19     9277   8821   9810  -3782   1547   -479       C  
ATOM   2670  CG1 ILE B  19      -1.158 -24.089 -24.423  1.00 74.05           C  
ANISOU 2670  CG1 ILE B  19     9338   9131   9666  -3868   1517   -530       C  
ATOM   2671  CG2 ILE B  19      -2.211 -23.981 -26.671  1.00 56.50           C  
ANISOU 2671  CG2 ILE B  19     6964   6742   7761  -3677   1411   -374       C  
ATOM   2672  CD1 ILE B  19      -0.994 -25.579 -24.584  1.00 73.20           C  
ANISOU 2672  CD1 ILE B  19     9033   9170   9607  -3747   1429   -467       C  
ATOM   2673  N   PHE B  20      -2.454 -20.840 -27.344  1.00 78.91           N  
ANISOU 2673  N   PHE B  20    10246   9126  10612  -3977   1435   -381       N  
ATOM   2674  CA  PHE B  20      -3.155 -20.229 -28.472  1.00 80.55           C  
ANISOU 2674  CA  PHE B  20    10522   9105  10978  -3979   1376   -293       C  
ATOM   2675  C   PHE B  20      -3.008 -21.048 -29.751  1.00 80.17           C  
ANISOU 2675  C   PHE B  20    10281   9240  10939  -3899   1282   -182       C  
ATOM   2676  O   PHE B  20      -1.896 -21.371 -30.172  1.00 79.72           O  
ANISOU 2676  O   PHE B  20    10138   9454  10696  -3962   1228   -156       O  
ATOM   2677  CB  PHE B  20      -2.652 -18.806 -28.717  1.00 82.64           C  
ANISOU 2677  CB  PHE B  20    11041   9189  11170  -4194   1328   -259       C  
ATOM   2678  CG  PHE B  20      -3.493 -18.023 -29.691  1.00 83.94           C  
ANISOU 2678  CG  PHE B  20    11369   9013  11512  -4221   1252   -168       C  
ATOM   2679  CD1 PHE B  20      -4.862 -17.913 -29.509  1.00 83.98           C  
ANISOU 2679  CD1 PHE B  20    11424   8707  11778  -4098   1282   -258       C  
ATOM   2680  CD2 PHE B  20      -2.916 -17.378 -30.773  1.00 85.80           C  
ANISOU 2680  CD2 PHE B  20    11733   9225  11642  -4387   1154    -13       C  
ATOM   2681  CE1 PHE B  20      -5.643 -17.187 -30.391  1.00 85.77           C  
ANISOU 2681  CE1 PHE B  20    11842   8560  12188  -4110   1177   -203       C  
ATOM   2682  CE2 PHE B  20      -3.693 -16.648 -31.662  1.00 87.66           C  
ANISOU 2682  CE2 PHE B  20    12181   9103  12022  -4426   1059     92       C  
ATOM   2683  CZ  PHE B  20      -5.058 -16.555 -31.469  1.00 87.68           C  
ANISOU 2683  CZ  PHE B  20    12250   8750  12314  -4274   1049     -5       C  
ATOM   2684  N   ILE B  21      -4.140 -21.378 -30.363  1.00 80.31           N  
ANISOU 2684  N   ILE B  21    10224   9116  11173  -3776   1273   -158       N  
ATOM   2685  CA  ILE B  21      -4.144 -22.071 -31.642  1.00 79.78           C  
ANISOU 2685  CA  ILE B  21     9980   9198  11133  -3720   1188    -79       C  
ATOM   2686  C   ILE B  21      -4.466 -21.060 -32.737  1.00 82.54           C  
ANISOU 2686  C   ILE B  21    10524   9327  11510  -3863   1127     17       C  
ATOM   2687  O   ILE B  21      -5.459 -20.344 -32.644  1.00 84.15           O  
ANISOU 2687  O   ILE B  21    10907   9164  11901  -3863   1133    -10       O  
ATOM   2688  CB  ILE B  21      -5.180 -23.208 -31.656  1.00 77.45           C  
ANISOU 2688  CB  ILE B  21     9459   8908  11062  -3506   1206   -132       C  
ATOM   2689  CG1 ILE B  21      -5.064 -24.063 -30.391  1.00 75.90           C  
ANISOU 2689  CG1 ILE B  21     9167   8830  10843  -3400   1274   -197       C  
ATOM   2690  CG2 ILE B  21      -5.021 -24.064 -32.902  1.00 76.32           C  
ANISOU 2690  CG2 ILE B  21     9089   8976  10933  -3447   1109    -89       C  
ATOM   2691  CD1 ILE B  21      -3.715 -24.725 -30.211  1.00 74.81           C  
ANISOU 2691  CD1 ILE B  21     8935   8985  10506  -3419   1211   -182       C  
ATOM   2692  N   THR B  22      -3.624 -20.996 -33.766  1.00 83.74           N  
ANISOU 2692  N   THR B  22    10668   9690  11458  -4000   1065    115       N  
ATOM   2693  CA  THR B  22      -3.798 -20.016 -34.837  1.00 87.00           C  
ANISOU 2693  CA  THR B  22    11331   9913  11813  -4193    995    258       C  
ATOM   2694  C   THR B  22      -4.315 -20.650 -36.123  1.00 86.84           C  
ANISOU 2694  C   THR B  22    11173   9996  11826  -4172    931    308       C  
ATOM   2695  O   THR B  22      -3.801 -21.674 -36.571  1.00 85.61           O  
ANISOU 2695  O   THR B  22    10725  10233  11571  -4114    927    259       O  
ATOM   2696  CB  THR B  22      -2.483 -19.273 -35.153  1.00 89.65           C  
ANISOU 2696  CB  THR B  22    11823  10422  11820  -4453    980    352       C  
ATOM   2697  OG1 THR B  22      -1.525 -20.191 -35.694  1.00 89.00           O  
ANISOU 2697  OG1 THR B  22    11478  10820  11518  -4468    982    310       O  
ATOM   2698  CG2 THR B  22      -1.913 -18.639 -33.905  1.00 90.25           C  
ANISOU 2698  CG2 THR B  22    12014  10414  11864  -4501   1034    274       C  
ATOM   2699  N   ASP B  23      -5.332 -20.033 -36.714  1.00 88.69           N  
ANISOU 2699  N   ASP B  23    11637   9858  12205  -4220    856    382       N  
ATOM   2700  CA  ASP B  23      -5.850 -20.488 -37.996  1.00 88.86           C  
ANISOU 2700  CA  ASP B  23    11582   9955  12224  -4259    760    440       C  
ATOM   2701  C   ASP B  23      -4.858 -20.138 -39.092  1.00 90.85           C  
ANISOU 2701  C   ASP B  23    11946  10509  12063  -4536    689    649       C  
ATOM   2702  O   ASP B  23      -4.829 -19.008 -39.573  1.00 93.86           O  
ANISOU 2702  O   ASP B  23    12746  10627  12291  -4748    587    869       O  
ATOM   2703  CB  ASP B  23      -7.211 -19.852 -38.278  1.00 91.22           C  
ANISOU 2703  CB  ASP B  23    12136   9739  12785  -4061    614    443       C  
ATOM   2704  CG  ASP B  23      -7.776 -20.247 -39.629  1.00 92.25           C  
ANISOU 2704  CG  ASP B  23    12150  10006  12897  -3796    415    494       C  
ATOM   2705  OD1 ASP B  23      -7.319 -21.251 -40.210  1.00 90.51           O  
ANISOU 2705  OD1 ASP B  23    11579  10265  12547  -3810    441    459       O  
ATOM   2706  OD2 ASP B  23      -8.691 -19.549 -40.106  1.00 95.20           O  
ANISOU 2706  OD2 ASP B  23    12776  10005  13390  -3548    206    542       O  
ATOM   2707  N   ASN B  24      -4.047 -21.119 -39.476  1.00 89.25           N  
ANISOU 2707  N   ASN B  24    11382  10848  11681  -4520    730    566       N  
ATOM   2708  CA  ASN B  24      -3.024 -20.929 -40.498  1.00 90.90           C  
ANISOU 2708  CA  ASN B  24    11622  11452  11464  -4788    698    695       C  
ATOM   2709  C   ASN B  24      -3.607 -21.019 -41.901  1.00 91.31           C  
ANISOU 2709  C   ASN B  24    11691  11608  11394  -4938    563    852       C  
ATOM   2710  O   ASN B  24      -2.911 -20.793 -42.888  1.00 94.10           O  
ANISOU 2710  O   ASN B  24    12100  12302  11351  -5203    532    999       O  
ATOM   2711  CB  ASN B  24      -1.915 -21.971 -40.344  1.00 88.67           C  
ANISOU 2711  CB  ASN B  24    10947  11698  11045  -4688    763    485       C  
ATOM   2712  CG  ASN B  24      -1.537 -22.212 -38.896  1.00 85.71           C  
ANISOU 2712  CG  ASN B  24    10507  11221  10837  -4490    843    329       C  
ATOM   2713  OD1 ASN B  24      -0.693 -21.512 -38.336  1.00 86.70           O  
ANISOU 2713  OD1 ASN B  24    10806  11330  10806  -4627    887    345       O  
ATOM   2714  ND2 ASN B  24      -2.159 -23.210 -38.283  1.00 82.15           N  
ANISOU 2714  ND2 ASN B  24     9808  10712  10695  -4187    850    186       N  
ATOM   2715  N   VAL B  25      -4.890 -21.355 -41.974  1.00 88.97           N  
ANISOU 2715  N   VAL B  25    11326  11042  11435  -4565    453    774       N  
ATOM   2716  CA  VAL B  25      -5.575 -21.520 -43.248  1.00 69.97           C  
ANISOU 2716  CA  VAL B  25     8890   8723   8973  -4292    245    829       C  
ATOM   2717  C   VAL B  25      -6.058 -20.189 -43.806  1.00 74.03           C  
ANISOU 2717  C   VAL B  25     9973   8794   9363  -4329     52   1127       C  
ATOM   2718  O   VAL B  25      -5.804 -19.867 -44.963  1.00 77.04           O  
ANISOU 2718  O   VAL B  25    10522   9372   9376  -4472    -74   1347       O  
ATOM   2719  CB  VAL B  25      -6.765 -22.488 -43.117  1.00 70.80           C  
ANISOU 2719  CB  VAL B  25     8638   8737   9524  -3740    177    556       C  
ATOM   2720  CG1 VAL B  25      -7.584 -22.516 -44.397  1.00 72.73           C  
ANISOU 2720  CG1 VAL B  25     8890   9007   9735  -3420    -74    592       C  
ATOM   2721  CG2 VAL B  25      -6.274 -23.878 -42.771  1.00 67.38           C  
ANISOU 2721  CG2 VAL B  25     7667   8740   9194  -3703    307    297       C  
ATOM   2722  N   HIS B  26      -6.754 -19.417 -42.982  1.00 74.52           N  
ANISOU 2722  N   HIS B  26    10339   8256   9721  -4196     14   1126       N  
ATOM   2723  CA  HIS B  26      -7.259 -18.125 -43.423  1.00110.66           C  
ANISOU 2723  CA  HIS B  26    15483  12321  14243  -4186   -223   1384       C  
ATOM   2724  C   HIS B  26      -6.263 -17.015 -43.131  1.00114.00           C  
ANISOU 2724  C   HIS B  26    16352  12572  14390  -4745   -152   1651       C  
ATOM   2725  O   HIS B  26      -6.641 -15.895 -42.794  1.00117.14           O  
ANISOU 2725  O   HIS B  26    17217  12381  14911  -4755   -288   1771       O  
ATOM   2726  CB  HIS B  26      -8.602 -17.821 -42.775  1.00 78.57           C  
ANISOU 2726  CB  HIS B  26    11499   7687  10668  -3708   -350   1188       C  
ATOM   2727  CG  HIS B  26      -9.600 -18.923 -42.929  1.00 75.96           C  
ANISOU 2727  CG  HIS B  26    10695   7511  10657  -3195   -384    884       C  
ATOM   2728  ND1 HIS B  26      -9.579 -20.057 -42.146  1.00 76.74           N  
ANISOU 2728  ND1 HIS B  26    10297   7877  10985  -3110   -146    600       N  
ATOM   2729  CD2 HIS B  26     -10.640 -19.072 -43.781  1.00 77.24           C  
ANISOU 2729  CD2 HIS B  26    10806   7590  10950  -2753   -641    817       C  
ATOM   2730  CE1 HIS B  26     -10.568 -20.854 -42.503  1.00 75.65           C  
ANISOU 2730  CE1 HIS B  26     9819   7800  11125  -2666   -236    374       C  
ATOM   2731  NE2 HIS B  26     -11.228 -20.281 -43.493  1.00 78.84           N  
ANISOU 2731  NE2 HIS B  26    10464   8012  11480  -2431   -534    478       N  
ATOM   2732  N   THR B  27      -4.984 -17.347 -43.263  1.00113.57           N  
ANISOU 2732  N   THR B  27    16126  13041  13983  -5207     51   1709       N  
ATOM   2733  CA  THR B  27      -3.917 -16.366 -43.170  1.00116.43           C  
ANISOU 2733  CA  THR B  27    16820  13380  14039  -5689    129   1918       C  
ATOM   2734  C   THR B  27      -3.676 -15.745 -44.538  1.00121.98           C  
ANISOU 2734  C   THR B  27    17897  14156  14296  -5999    -29   2309       C  
ATOM   2735  O   THR B  27      -3.405 -16.454 -45.509  1.00121.60           O  
ANISOU 2735  O   THR B  27    17604  14654  13945  -6098    -13   2354       O  
ATOM   2736  CB  THR B  27      -2.617 -17.006 -42.673  1.00113.10           C  
ANISOU 2736  CB  THR B  27    15939  13572  13464  -5737    382   1659       C  
ATOM   2737  OG1 THR B  27      -2.386 -18.230 -43.382  1.00110.64           O  
ANISOU 2737  OG1 THR B  27    15178  13862  12997  -5731    429   1547       O  
ATOM   2738  CG2 THR B  27      -2.709 -17.303 -41.189  1.00109.23           C  
ANISOU 2738  CG2 THR B  27    15229  12930  13344  -5451    510   1358       C  
ATOM   2739  N   TRP B  28      -3.785 -14.421 -44.607  1.00127.72           N  
ANISOU 2739  N   TRP B  28    19187  14358  14983  -6090   -193   2561       N  
ATOM   2740  CA  TRP B  28      -3.570 -13.683 -45.848  1.00134.57           C  
ANISOU 2740  CA  TRP B  28    20493  15222  15417  -6370   -366   2968       C  
ATOM   2741  C   TRP B  28      -2.155 -13.890 -46.378  1.00137.28           C  
ANISOU 2741  C   TRP B  28    20571  16306  15282  -6742   -144   2947       C  
ATOM   2742  O   TRP B  28      -1.931 -13.947 -47.588  1.00140.06           O  
ANISOU 2742  O   TRP B  28    21013  17004  15199  -6971   -203   3186       O  
ATOM   2743  CB  TRP B  28      -3.835 -12.192 -45.626  1.00139.27           C  
ANISOU 2743  CB  TRP B  28    21697  15096  16123  -6370   -579   3174       C  
ATOM   2744  CG  TRP B  28      -5.235 -11.772 -45.951  1.00141.12           C  
ANISOU 2744  CG  TRP B  28    22405  14615  16601  -6050   -975   3367       C  
ATOM   2745  CD1 TRP B  28      -5.624 -10.939 -46.958  1.00146.81           C  
ANISOU 2745  CD1 TRP B  28    23707  14974  17100  -6072  -1320   3768       C  
ATOM   2746  CD2 TRP B  28      -6.434 -12.174 -45.277  1.00137.88           C  
ANISOU 2746  CD2 TRP B  28    21833  13831  16724  -5487  -1095   3060       C  
ATOM   2747  NE1 TRP B  28      -6.989 -10.792 -46.949  1.00147.09           N  
ANISOU 2747  NE1 TRP B  28    23953  14417  17519  -5507  -1683   3709       N  
ATOM   2748  CE2 TRP B  28      -7.510 -11.541 -45.928  1.00141.64           C  
ANISOU 2748  CE2 TRP B  28    22731  13777  17307  -5082  -1524   3210       C  
ATOM   2749  CE3 TRP B  28      -6.700 -13.007 -44.187  1.00132.58           C  
ANISOU 2749  CE3 TRP B  28    20627  13301  16447  -5191   -873   2606       C  
ATOM   2750  CZ2 TRP B  28      -8.833 -11.714 -45.523  1.00140.12           C  
ANISOU 2750  CZ2 TRP B  28    22389  13225  17623  -4391  -1722   2870       C  
ATOM   2751  CZ3 TRP B  28      -8.015 -13.177 -43.787  1.00131.14           C  
ANISOU 2751  CZ3 TRP B  28    20321  12765  16742  -4551  -1041   2308       C  
ATOM   2752  CH2 TRP B  28      -9.064 -12.533 -44.453  1.00134.86           C  
ANISOU 2752  CH2 TRP B  28    21168  12741  17330  -4156  -1454   2416       C  
ATOM   2753  N   THR B  29      -1.207 -14.007 -45.457  1.00136.78           N  
ANISOU 2753  N   THR B  29    20187  16485  15299  -6778     89   2642       N  
ATOM   2754  CA  THR B  29       0.187 -14.219 -45.812  1.00139.23           C  
ANISOU 2754  CA  THR B  29    20226  17449  15225  -7085    270   2536       C  
ATOM   2755  C   THR B  29       0.615 -15.651 -45.526  1.00134.59           C  
ANISOU 2755  C   THR B  29    18989  17469  14679  -6913    440   2154       C  
ATOM   2756  O   THR B  29       0.249 -16.227 -44.502  1.00130.08           O  
ANISOU 2756  O   THR B  29    18172  16763  14490  -6585    496   1903       O  
ATOM   2757  CB  THR B  29       1.109 -13.254 -45.048  1.00142.15           C  
ANISOU 2757  CB  THR B  29    20741  17653  15616  -7269    357   2476       C  
ATOM   2758  OG1 THR B  29       0.594 -13.047 -43.727  1.00139.37           O  
ANISOU 2758  OG1 THR B  29    20405  16823  15726  -6968    362   2312       O  
ATOM   2759  CG2 THR B  29       1.180 -11.916 -45.761  1.00149.10           C  
ANISOU 2759  CG2 THR B  29    22192  18191  16268  -7597    212   2860       C  
ATOM   2760  N   GLU B  30       1.388 -16.221 -46.442  1.00136.07           N  
ANISOU 2760  N   GLU B  30    18906  18325  14470  -7124    505   2098       N  
ATOM   2761  CA  GLU B  30       1.925 -17.561 -46.262  1.00132.22           C  
ANISOU 2761  CA  GLU B  30    17809  18432  13998  -6953    625   1709       C  
ATOM   2762  C   GLU B  30       3.095 -17.497 -45.285  1.00130.22           C  
ANISOU 2762  C   GLU B  30    17398  18292  13788  -6966    751   1429       C  
ATOM   2763  O   GLU B  30       4.255 -17.447 -45.692  1.00132.93           O  
ANISOU 2763  O   GLU B  30    17626  19089  13794  -7243    819   1328       O  
ATOM   2764  CB  GLU B  30       2.373 -18.144 -47.604  1.00135.85           C  
ANISOU 2764  CB  GLU B  30    18022  19591  14004  -7168    629   1704       C  
ATOM   2765  CG  GLU B  30       1.256 -18.283 -48.637  1.00138.01           C  
ANISOU 2765  CG  GLU B  30    18424  19848  14166  -7162    496   1995       C  
ATOM   2766  CD  GLU B  30       0.874 -16.961 -49.283  1.00144.53           C  
ANISOU 2766  CD  GLU B  30    19922  20229  14763  -7427    354   2486       C  
ATOM   2767  OE1 GLU B  30       1.490 -15.927 -48.946  1.00148.07           O  
ANISOU 2767  OE1 GLU B  30    20693  20398  15170  -7638    376   2575       O  
ATOM   2768  OE2 GLU B  30      -0.045 -16.955 -50.128  1.00146.33           O  
ANISOU 2768  OE2 GLU B  30    20372  20377  14851  -7402    196   2790       O  
ATOM   2769  N   GLN B  31       2.775 -17.499 -43.994  1.00125.30           N  
ANISOU 2769  N   GLN B  31    16771  17271  13569  -6677    776   1300       N  
ATOM   2770  CA  GLN B  31       3.762 -17.264 -42.946  1.00123.35           C  
ANISOU 2770  CA  GLN B  31    16459  17035  13373  -6689    870   1094       C  
ATOM   2771  C   GLN B  31       4.814 -18.361 -42.874  1.00119.19           C  
ANISOU 2771  C   GLN B  31    15470  17113  12703  -6625    940    750       C  
ATOM   2772  O   GLN B  31       5.959 -18.110 -42.496  1.00121.02           O  
ANISOU 2772  O   GLN B  31    15658  17543  12783  -6797   1007    603       O  
ATOM   2773  CB  GLN B  31       3.070 -17.153 -41.586  1.00120.89           C  
ANISOU 2773  CB  GLN B  31    16210  16213  13507  -6366    873   1027       C  
ATOM   2774  CG  GLN B  31       1.691 -16.509 -41.625  1.00122.00           C  
ANISOU 2774  CG  GLN B  31    16700  15760  13895  -6271    771   1274       C  
ATOM   2775  CD  GLN B  31       1.740 -14.995 -41.682  1.00127.45           C  
ANISOU 2775  CD  GLN B  31    17884  16019  14520  -6540    710   1527       C  
ATOM   2776  OE1 GLN B  31       0.712 -14.338 -41.848  1.00129.00           O  
ANISOU 2776  OE1 GLN B  31    18437  15702  14875  -6493    579   1746       O  
ATOM   2777  NE2 GLN B  31       2.934 -14.433 -41.537  1.00130.60           N  
ANISOU 2777  NE2 GLN B  31    18319  16598  14707  -6820    783   1486       N  
ATOM   2778  N   TYR B  32       4.423 -19.574 -43.242  1.00119.36           N  
ANISOU 2778  N   TYR B  32    16464  11557  17329  -1722   -322  -1346       N  
ATOM   2779  CA  TYR B  32       5.264 -20.738 -43.002  1.00113.48           C  
ANISOU 2779  CA  TYR B  32    15286  11486  16345  -1962   -461  -1225       C  
ATOM   2780  C   TYR B  32       6.022 -21.229 -44.231  1.00110.26           C  
ANISOU 2780  C   TYR B  32    14503  11641  15751  -1799   -826   -937       C  
ATOM   2781  O   TYR B  32       5.526 -21.147 -45.353  1.00110.37           O  
ANISOU 2781  O   TYR B  32    14391  11574  15969  -1323  -1005   -912       O  
ATOM   2782  CB  TYR B  32       4.427 -21.875 -42.425  1.00110.35           C  
ANISOU 2782  CB  TYR B  32    14479  11114  16334  -1670   -348  -1514       C  
ATOM   2783  CG  TYR B  32       3.789 -21.559 -41.092  1.00111.74           C  
ANISOU 2783  CG  TYR B  32    14986  10837  16633  -1938     58  -1827       C  
ATOM   2784  CD1 TYR B  32       4.334 -22.041 -39.912  1.00110.87           C  
ANISOU 2784  CD1 TYR B  32    14958  10929  16240  -2505    182  -1838       C  
ATOM   2785  CD2 TYR B  32       2.635 -20.790 -41.014  1.00114.42           C  
ANISOU 2785  CD2 TYR B  32    15549  10551  17374  -1621    322  -2115       C  
ATOM   2786  CE1 TYR B  32       3.751 -21.765 -38.693  1.00112.55           C  
ANISOU 2786  CE1 TYR B  32    15514  10732  16517  -2822    582  -2147       C  
ATOM   2787  CE2 TYR B  32       2.044 -20.512 -39.798  1.00116.29           C  
ANISOU 2787  CE2 TYR B  32    16083  10378  17726  -1876    761  -2450       C  
ATOM   2788  CZ  TYR B  32       2.607 -21.001 -38.643  1.00115.16           C  
ANISOU 2788  CZ  TYR B  32    16063  10445  17247  -2511    902  -2475       C  
ATOM   2789  OH  TYR B  32       2.023 -20.724 -37.431  1.00117.43           O  
ANISOU 2789  OH  TYR B  32    16693  10327  17600  -2838   1366  -2829       O  
ATOM   2790  N   LYS B  33       7.230 -21.738 -44.001  1.00107.83           N  
ANISOU 2790  N   LYS B  33    14007  11917  15048  -2210   -930   -722       N  
ATOM   2791  CA  LYS B  33       8.032 -22.344 -45.063  1.00104.99           C  
ANISOU 2791  CA  LYS B  33    13224  12153  14513  -2071  -1207   -493       C  
ATOM   2792  C   LYS B  33       8.776 -23.577 -44.559  1.00101.31           C  
ANISOU 2792  C   LYS B  33    12288  12256  13950  -2165  -1273   -418       C  
ATOM   2793  O   LYS B  33       9.280 -23.592 -43.436  1.00101.64           O  
ANISOU 2793  O   LYS B  33    12439  12396  13782  -2637  -1187   -367       O  
ATOM   2794  CB  LYS B  33       9.023 -21.336 -45.652  1.00107.90           C  
ANISOU 2794  CB  LYS B  33    13897  12700  14401  -2510  -1302   -214       C  
ATOM   2795  CG  LYS B  33       8.407 -20.353 -46.631  1.00110.36           C  
ANISOU 2795  CG  LYS B  33    14586  12550  14795  -2272  -1366   -204       C  
ATOM   2796  CD  LYS B  33       9.471 -19.571 -47.381  1.00113.08           C  
ANISOU 2796  CD  LYS B  33    15184  13172  14608  -2725  -1494     86       C  
ATOM   2797  CE  LYS B  33      10.242 -18.646 -46.459  1.00 91.04           C  
ANISOU 2797  CE  LYS B  33    12898  10329  11363  -3503  -1332    192       C  
ATOM   2798  NZ  LYS B  33      11.357 -17.970 -47.176  1.00 93.71           N  
ANISOU 2798  NZ  LYS B  33    13437  11041  11129  -4031  -1450    470       N  
ATOM   2799  N   PHE B  34       8.837 -24.609 -45.397  1.00 97.91           N  
ANISOU 2799  N   PHE B  34    11366  12175  13661  -1716  -1432   -403       N  
ATOM   2800  CA  PHE B  34       9.527 -25.848 -45.050  1.00 95.21           C  
ANISOU 2800  CA  PHE B  34    10574  12326  13275  -1682  -1508   -323       C  
ATOM   2801  C   PHE B  34      10.983 -25.818 -45.506  1.00 96.53           C  
ANISOU 2801  C   PHE B  34    10499  13140  13039  -1952  -1645    -18       C  
ATOM   2802  O   PHE B  34      11.271 -25.512 -46.663  1.00 97.25           O  
ANISOU 2802  O   PHE B  34    10525  13413  13011  -1852  -1721     60       O  
ATOM   2803  CB  PHE B  34       8.824 -27.047 -45.685  1.00 91.67           C  
ANISOU 2803  CB  PHE B  34     9759  11882  13191  -1056  -1560   -500       C  
ATOM   2804  CG  PHE B  34       7.677 -27.583 -44.877  1.00 89.58           C  
ANISOU 2804  CG  PHE B  34     9552  11207  13276   -881  -1426   -783       C  
ATOM   2805  CD1 PHE B  34       6.733 -26.731 -44.331  1.00 90.17           C  
ANISOU 2805  CD1 PHE B  34     9993  10752  13515   -985  -1249   -977       C  
ATOM   2806  CD2 PHE B  34       7.530 -28.946 -44.687  1.00 87.53           C  
ANISOU 2806  CD2 PHE B  34     8997  11080  13182   -612  -1452   -872       C  
ATOM   2807  CE1 PHE B  34       5.670 -27.231 -43.603  1.00 89.28           C  
ANISOU 2807  CE1 PHE B  34     9892  10313  13718   -856  -1085  -1272       C  
ATOM   2808  CE2 PHE B  34       6.474 -29.451 -43.956  1.00 86.57           C  
ANISOU 2808  CE2 PHE B  34     8949  10607  13336   -524  -1315  -1144       C  
ATOM   2809  CZ  PHE B  34       5.543 -28.592 -43.415  1.00 87.43           C  
ANISOU 2809  CZ  PHE B  34     9365  10253  13600   -660  -1124  -1354       C  
ATOM   2810  N   GLN B  35      11.895 -26.134 -44.590  1.00 97.42           N  
ANISOU 2810  N   GLN B  35    10463  13625  12928  -2318  -1682    158       N  
ATOM   2811  CA  GLN B  35      13.319 -26.192 -44.908  1.00 99.39           C  
ANISOU 2811  CA  GLN B  35    10362  14580  12821  -2571  -1810    449       C  
ATOM   2812  C   GLN B  35      13.986 -27.374 -44.214  1.00100.35           C  
ANISOU 2812  C   GLN B  35    10023  15126  12981  -2480  -1922    583       C  
ATOM   2813  O   GLN B  35      13.747 -27.626 -43.034  1.00100.41           O  
ANISOU 2813  O   GLN B  35    10179  14943  13029  -2668  -1919    572       O  
ATOM   2814  CB  GLN B  35      14.008 -24.877 -44.537  1.00101.44           C  
ANISOU 2814  CB  GLN B  35    10993  14936  12613  -3327  -1786    632       C  
ATOM   2815  CG  GLN B  35      13.638 -23.719 -45.447  1.00101.44           C  
ANISOU 2815  CG  GLN B  35    11431  14607  12504  -3408  -1723    579       C  
ATOM   2816  CD  GLN B  35      13.844 -22.375 -44.795  1.00103.60           C  
ANISOU 2816  CD  GLN B  35    12323  14637  12403  -4131  -1626    658       C  
ATOM   2817  OE1 GLN B  35      14.437 -22.273 -43.723  1.00104.77           O  
ANISOU 2817  OE1 GLN B  35    12528  14986  12292  -4672  -1616    779       O  
ATOM   2818  NE2 GLN B  35      13.348 -21.328 -45.440  1.00104.69           N  
ANISOU 2818  NE2 GLN B  35    12972  14314  12492  -4164  -1563    600       N  
ATOM   2819  N   PRO B  36      14.831 -28.107 -44.950  1.00101.87           N  
ANISOU 2819  N   PRO B  36     9668  15881  13156  -2186  -2015    709       N  
ATOM   2820  CA  PRO B  36      15.440 -29.332 -44.427  1.00102.56           C  
ANISOU 2820  CA  PRO B  36     9286  16330  13350  -1943  -2139    846       C  
ATOM   2821  C   PRO B  36      16.533 -29.038 -43.413  1.00105.33           C  
ANISOU 2821  C   PRO B  36     9510  17152  13360  -2531  -2288   1172       C  
ATOM   2822  O   PRO B  36      16.875 -27.878 -43.198  1.00106.99           O  
ANISOU 2822  O   PRO B  36     9995  17448  13209  -3171  -2268   1275       O  
ATOM   2823  CB  PRO B  36      16.057 -29.960 -45.675  1.00103.90           C  
ANISOU 2823  CB  PRO B  36     8942  16955  13580  -1479  -2133    859       C  
ATOM   2824  CG  PRO B  36      16.395 -28.800 -46.531  1.00105.26           C  
ANISOU 2824  CG  PRO B  36     9244  17308  13441  -1839  -2070    891       C  
ATOM   2825  CD  PRO B  36      15.292 -27.802 -46.315  1.00103.10           C  
ANISOU 2825  CD  PRO B  36     9638  16359  13178  -2082  -1996    732       C  
ATOM   2826  N   GLU B  37      17.062 -30.085 -42.790  1.00105.93           N  
ANISOU 2826  N   GLU B  37     9202  17516  13532  -2333  -2454   1347       N  
ATOM   2827  CA  GLU B  37      18.209 -29.941 -41.905  1.00109.32           C  
ANISOU 2827  CA  GLU B  37     9381  18513  13641  -2844  -2668   1715       C  
ATOM   2828  C   GLU B  37      19.485 -29.970 -42.730  1.00111.86           C  
ANISOU 2828  C   GLU B  37     9045  19643  13812  -2774  -2732   1921       C  
ATOM   2829  O   GLU B  37      20.299 -29.050 -42.678  1.00114.57           O  
ANISOU 2829  O   GLU B  37     9325  20459  13747  -3404  -2773   2113       O  
ATOM   2830  CB  GLU B  37      18.247 -31.071 -40.874  1.00110.45           C  
ANISOU 2830  CB  GLU B  37     9391  18618  13955  -2640  -2872   1860       C  
ATOM   2831  CG  GLU B  37      17.216 -30.956 -39.765  1.00108.83           C  
ANISOU 2831  CG  GLU B  37     9827  17755  13769  -2952  -2823   1712       C  
ATOM   2832  CD  GLU B  37      17.517 -31.876 -38.597  1.00111.46           C  
ANISOU 2832  CD  GLU B  37    10078  18167  14104  -2997  -3088   1959       C  
ATOM   2833  OE1 GLU B  37      18.254 -32.865 -38.792  1.00113.91           O  
ANISOU 2833  OE1 GLU B  37     9842  18877  14563  -2515  -3295   2182       O  
ATOM   2834  OE2 GLU B  37      17.024 -31.605 -37.482  1.00111.54           O  
ANISOU 2834  OE2 GLU B  37    10593  17827  13961  -3518  -3086   1934       O  
ATOM   2835  N   SER B  38      19.645 -31.046 -43.490  1.00111.28           N  
ANISOU 2835  N   SER B  38     8496  19726  14059  -2027  -2708   1858       N  
ATOM   2836  CA  SER B  38      20.818 -31.234 -44.326  1.00114.67           C  
ANISOU 2836  CA  SER B  38     8382  20770  14415  -1809  -2641   1950       C  
ATOM   2837  C   SER B  38      20.404 -31.788 -45.680  1.00113.30           C  
ANISOU 2837  C   SER B  38     8044  20489  14516  -1167  -2438   1668       C  
ATOM   2838  O   SER B  38      20.235 -32.997 -45.834  1.00112.71           O  
ANISOU 2838  O   SER B  38     7810  20218  14798   -484  -2405   1566       O  
ATOM   2839  CB  SER B  38      21.806 -32.181 -43.648  1.00118.33           C  
ANISOU 2839  CB  SER B  38     8486  21497  14977  -1515  -2776   2180       C  
ATOM   2840  OG  SER B  38      22.935 -32.418 -44.469  1.00122.41           O  
ANISOU 2840  OG  SER B  38     8527  22504  15479  -1248  -2645   2203       O  
ATOM   2841  N   PRO B  39      20.229 -30.895 -46.663  1.00113.69           N  
ANISOU 2841  N   PRO B  39     8222  20611  14363  -1423  -2294   1535       N  
ATOM   2842  CA  PRO B  39      19.854 -31.227 -48.040  1.00112.99           C  
ANISOU 2842  CA  PRO B  39     8103  20400  14428   -948  -2078   1259       C  
ATOM   2843  C   PRO B  39      20.730 -32.333 -48.617  1.00116.77           C  
ANISOU 2843  C   PRO B  39     8021  21258  15090   -367  -1958   1242       C  
ATOM   2844  O   PRO B  39      20.253 -33.147 -49.406  1.00 96.25           O  
ANISOU 2844  O   PRO B  39     5386  18431  12753    204  -1809   1004       O  
ATOM   2845  CB  PRO B  39      20.102 -29.916 -48.784  1.00114.15           C  
ANISOU 2845  CB  PRO B  39     8463  20747  14161  -1534  -1989   1257       C  
ATOM   2846  CG  PRO B  39      19.864 -28.867 -47.762  1.00113.44           C  
ANISOU 2846  CG  PRO B  39     8866  20408  13828  -2203  -2111   1393       C  
ATOM   2847  CD  PRO B  39      20.361 -29.440 -46.466  1.00114.76           C  
ANISOU 2847  CD  PRO B  39     8741  20800  14061  -2246  -2304   1628       C  
ATOM   2848  N   SER B  40      21.997 -32.358 -48.217  1.00102.36           N  
ANISOU 2848  N   SER B  40     5875  19893  13126   -515  -1987   1461       N  
ATOM   2849  CA  SER B  40      22.912 -33.398 -48.663  1.00110.20           C  
ANISOU 2849  CA  SER B  40     6407  21131  14331     42  -1851   1434       C  
ATOM   2850  C   SER B  40      22.431 -34.779 -48.222  1.00109.45           C  
ANISOU 2850  C   SER B  40     6351  20536  14700    731  -1909   1363       C  
ATOM   2851  O   SER B  40      22.505 -35.743 -48.985  1.00111.08           O  
ANISOU 2851  O   SER B  40     6398  20632  15174   1318  -1716   1177       O  
ATOM   2852  CB  SER B  40      24.326 -33.128 -48.145  1.00116.12           C  
ANISOU 2852  CB  SER B  40     6782  22478  14861   -268  -1929   1713       C  
ATOM   2853  OG  SER B  40      24.333 -32.957 -46.739  1.00116.03           O  
ANISOU 2853  OG  SER B  40     6932  22377  14779   -581  -2214   1973       O  
ATOM   2854  N   LYS B  41      21.929 -34.865 -46.994  1.00107.14           N  
ANISOU 2854  N   LYS B  41     6308  19936  14465    608  -2161   1507       N  
ATOM   2855  CA  LYS B  41      21.412 -36.123 -46.471  1.00102.90           C  
ANISOU 2855  CA  LYS B  41     5869  18922  14305   1170  -2251   1465       C  
ATOM   2856  C   LYS B  41      20.172 -36.540 -47.246  1.00118.60           C  
ANISOU 2856  C   LYS B  41     8151  20410  16501   1535  -2077   1134       C  
ATOM   2857  O   LYS B  41      19.961 -37.725 -47.507  1.00119.07           O  
ANISOU 2857  O   LYS B  41     8225  20148  16870   2124  -1986    996       O  
ATOM   2858  CB  LYS B  41      21.085 -35.999 -44.982  1.00101.83           C  
ANISOU 2858  CB  LYS B  41     5962  18628  14101    833  -2563   1701       C  
ATOM   2859  CG  LYS B  41      22.293 -35.733 -44.101  1.00106.97           C  
ANISOU 2859  CG  LYS B  41     6353  19754  14536    481  -2773   2054       C  
ATOM   2860  CD  LYS B  41      21.901 -35.645 -42.634  1.00107.39           C  
ANISOU 2860  CD  LYS B  41     6694  19628  14480     86  -3079   2292       C  
ATOM   2861  CE  LYS B  41      23.117 -35.434 -41.746  1.00113.08           C  
ANISOU 2861  CE  LYS B  41     7172  20835  14960   -277  -3305   2664       C  
ATOM   2862  NZ  LYS B  41      23.898 -34.241 -42.163  1.00113.84           N  
ANISOU 2862  NZ  LYS B  41     7125  21452  14677   -837  -3182   2724       N  
ATOM   2863  N   LEU B  42      19.357 -35.553 -47.607  1.00114.58           N  
ANISOU 2863  N   LEU B  42     7894  19831  15808   1161  -2038   1013       N  
ATOM   2864  CA  LEU B  42      18.168 -35.791 -48.413  1.00110.46           C  
ANISOU 2864  CA  LEU B  42     7633  18906  15432   1451  -1893    691       C  
ATOM   2865  C   LEU B  42      18.578 -36.415 -49.739  1.00112.78           C  
ANISOU 2865  C   LEU B  42     7738  19309  15806   1879  -1615    493       C  
ATOM   2866  O   LEU B  42      18.037 -37.440 -50.148  1.00112.07           O  
ANISOU 2866  O   LEU B  42     7786  18836  15960   2372  -1484    280       O  
ATOM   2867  CB  LEU B  42      17.404 -34.483 -48.658  1.00106.66           C  
ANISOU 2867  CB  LEU B  42     7606  18192  14729    916  -1877    587       C  
ATOM   2868  CG  LEU B  42      16.408 -33.967 -47.612  1.00102.41           C  
ANISOU 2868  CG  LEU B  42     7601  17102  14209    570  -1996    572       C  
ATOM   2869  CD1 LEU B  42      17.071 -33.708 -46.268  1.00104.17           C  
ANISOU 2869  CD1 LEU B  42     7741  17553  14286    161  -2197    885       C  
ATOM   2870  CD2 LEU B  42      15.720 -32.705 -48.115  1.00 99.68           C  
ANISOU 2870  CD2 LEU B  42     7675  16505  13692    180  -1934    448       C  
ATOM   2871  N   ALA B  43      19.555 -35.795 -50.393  1.00115.57           N  
ANISOU 2871  N   ALA B  43     7790  20207  15914   1635  -1507    562       N  
ATOM   2872  CA  ALA B  43      20.065 -36.292 -51.664  1.00118.24           C  
ANISOU 2872  CA  ALA B  43     7891  20765  16269   1957  -1210    375       C  
ATOM   2873  C   ALA B  43      20.600 -37.714 -51.530  1.00120.90           C  
ANISOU 2873  C   ALA B  43     8053  20934  16950   2561  -1105    363       C  
ATOM   2874  O   ALA B  43      20.387 -38.556 -52.405  1.00121.47           O  
ANISOU 2874  O   ALA B  43     8166  20814  17174   2995   -852    119       O  
ATOM   2875  CB  ALA B  43      21.142 -35.368 -52.192  1.00122.10           C  
ANISOU 2875  CB  ALA B  43     8039  21947  16405   1518  -1124    482       C  
ATOM   2876  N   SER B  44      21.297 -37.968 -50.428  1.00122.96           N  
ANISOU 2876  N   SER B  44     8135  21271  17313   2565  -1311    631       N  
ATOM   2877  CA  SER B  44      21.834 -39.292 -50.144  1.00126.54           C  
ANISOU 2877  CA  SER B  44     8416  21549  18116   3133  -1288    671       C  
ATOM   2878  C   SER B  44      20.703 -40.311 -50.064  1.00122.55           C  
ANISOU 2878  C   SER B  44     8335  20348  17880   3550  -1258    497       C  
ATOM   2879  O   SER B  44      20.790 -41.411 -50.621  1.00125.05           O  
ANISOU 2879  O   SER B  44     8651  20429  18436   4063  -1035    347       O  
ATOM   2880  CB  SER B  44      22.615 -39.264 -48.830  1.00129.38           C  
ANISOU 2880  CB  SER B  44     8560  22110  18490   2995  -1616   1016       C  
ATOM   2881  OG  SER B  44      23.538 -38.189 -48.815  1.00114.85           O  
ANISOU 2881  OG  SER B  44     6403  20912  16323   2484  -1656   1187       O  
ATOM   2882  N   ALA B  45      19.636 -39.925 -49.373  1.00117.01           N  
ANISOU 2882  N   ALA B  45     8006  19333  17118   3300  -1459    509       N  
ATOM   2883  CA  ALA B  45      18.460 -40.772 -49.230  1.00114.82           C  
ANISOU 2883  CA  ALA B  45     8156  18437  17033   3601  -1439    337       C  
ATOM   2884  C   ALA B  45      17.805 -41.035 -50.582  1.00113.04           C  
ANISOU 2884  C   ALA B  45     8132  18025  16793   3798  -1116    -19       C  
ATOM   2885  O   ALA B  45      17.299 -42.129 -50.834  1.00114.45           O  
ANISOU 2885  O   ALA B  45     8569  17775  17143   4192   -967   -193       O  
ATOM   2886  CB  ALA B  45      17.470 -40.138 -48.271  1.00109.81           C  
ANISOU 2886  CB  ALA B  45     7814  17607  16301   3237  -1692    380       C  
ATOM   2887  N   ILE B  46      17.818 -40.026 -51.447  1.00111.86           N  
ANISOU 2887  N   ILE B  46     7888  18219  16396   3491  -1023   -127       N  
ATOM   2888  CA  ILE B  46      17.275 -40.168 -52.794  1.00111.58           C  
ANISOU 2888  CA  ILE B  46     7999  18113  16284   3624   -760   -465       C  
ATOM   2889  C   ILE B  46      18.086 -41.177 -53.605  1.00116.52           C  
ANISOU 2889  C   ILE B  46     8424  18830  17017   4062   -434   -576       C  
ATOM   2890  O   ILE B  46      17.520 -42.046 -54.271  1.00116.95           O  
ANISOU 2890  O   ILE B  46     8742  18544  17149   4376   -219   -849       O  
ATOM   2891  CB  ILE B  46      17.239 -38.817 -53.540  1.00111.26           C  
ANISOU 2891  CB  ILE B  46     7848  18504  15920   3182   -772   -519       C  
ATOM   2892  CG1 ILE B  46      16.339 -37.818 -52.810  1.00107.04           C  
ANISOU 2892  CG1 ILE B  46     7587  17774  15310   2764  -1060   -446       C  
ATOM   2893  CG2 ILE B  46      16.752 -39.006 -54.966  1.00112.10           C  
ANISOU 2893  CG2 ILE B  46     8056  18615  15922   3320   -534   -873       C  
ATOM   2894  CD1 ILE B  46      16.297 -36.448 -53.457  1.00106.13           C  
ANISOU 2894  CD1 ILE B  46     7592  17858  14873   2225  -1083   -422       C  
ATOM   2895  N   GLN B  47      19.410 -41.057 -53.545  1.00121.19           N  
ANISOU 2895  N   GLN B  47     8552  19883  17610   4064   -388   -387       N  
ATOM   2896  CA  GLN B  47      20.292 -41.976 -54.258  1.00126.99           C  
ANISOU 2896  CA  GLN B  47     9027  20730  18492   4496    -57   -498       C  
ATOM   2897  C   GLN B  47      20.093 -43.410 -53.775  1.00129.08           C  
ANISOU 2897  C   GLN B  47     9516  20415  19114   5021    -22   -504       C  
ATOM   2898  O   GLN B  47      19.952 -44.336 -54.579  1.00131.10           O  
ANISOU 2898  O   GLN B  47     9929  20419  19466   5395    306   -764       O  
ATOM   2899  CB  GLN B  47      21.759 -41.569 -54.086  1.00132.31           C  
ANISOU 2899  CB  GLN B  47     9118  22012  19141   4390    -67   -275       C  
ATOM   2900  CG  GLN B  47      22.119 -40.193 -54.638  1.00131.83           C  
ANISOU 2900  CG  GLN B  47     8825  22590  18672   3835    -51   -263       C  
ATOM   2901  CD  GLN B  47      23.623 -39.967 -54.707  1.00138.41           C  
ANISOU 2901  CD  GLN B  47     9065  24064  19460   3763     40   -118       C  
ATOM   2902  OE1 GLN B  47      24.406 -40.917 -54.671  1.00143.90           O  
ANISOU 2902  OE1 GLN B  47     9472  24743  20459   4223    179   -109       O  
ATOM   2903  NE2 GLN B  47      24.031 -38.707 -54.805  1.00138.34           N  
ANISOU 2903  NE2 GLN B  47     8871  24621  19070   3173    -37     -6       N  
ATOM   2904  N   LYS B  48      20.079 -43.582 -52.456  1.00129.13           N  
ANISOU 2904  N   LYS B  48     9563  20220  19282   5019   -357   -225       N  
ATOM   2905  CA  LYS B  48      19.888 -44.899 -51.859  1.00131.79           C  
ANISOU 2905  CA  LYS B  48    10131  20018  19927   5479   -383   -184       C  
ATOM   2906  C   LYS B  48      18.542 -45.502 -52.259  1.00128.52           C  
ANISOU 2906  C   LYS B  48    10316  19042  19476   5592   -230   -475       C  
ATOM   2907  O   LYS B  48      18.454 -46.685 -52.599  1.00131.55           O  
ANISOU 2907  O   LYS B  48    10923  19034  20026   6021      4   -631       O  
ATOM   2908  CB  LYS B  48      19.997 -44.814 -50.334  1.00131.82           C  
ANISOU 2908  CB  LYS B  48    10100  19965  20021   5364   -828    167       C  
ATOM   2909  CG  LYS B  48      19.793 -46.145 -49.623  1.00134.68           C  
ANISOU 2909  CG  LYS B  48    10725  19784  20664   5821   -915    251       C  
ATOM   2910  CD  LYS B  48      19.906 -46.005 -48.111  1.00134.95           C  
ANISOU 2910  CD  LYS B  48    10727  19823  20726   5675  -1398    606       C  
ATOM   2911  CE  LYS B  48      19.730 -47.348 -47.420  1.00138.30           C  
ANISOU 2911  CE  LYS B  48    11442  19706  21397   6147  -1510    718       C  
ATOM   2912  NZ  LYS B  48      20.759 -48.333 -47.852  1.00146.18           N  
ANISOU 2912  NZ  LYS B  48    12169  20664  22710   6702  -1348    721       N  
ATOM   2913  N   ALA B  49      17.497 -44.680 -52.229  1.00122.85           N  
ANISOU 2913  N   ALA B  49     9861  18280  18534   5193   -363   -573       N  
ATOM   2914  CA  ALA B  49      16.153 -45.144 -52.558  1.00119.98           C  
ANISOU 2914  CA  ALA B  49    10042  17428  18118   5226   -279   -882       C  
ATOM   2915  C   ALA B  49      16.018 -45.527 -54.029  1.00122.73           C  
ANISOU 2915  C   ALA B  49    10495  17766  18371   5389     98  -1249       C  
ATOM   2916  O   ALA B  49      15.375 -46.522 -54.362  1.00123.25           O  
ANISOU 2916  O   ALA B  49    10971  17378  18479   5625    274  -1499       O  
ATOM   2917  CB  ALA B  49      15.124 -44.094 -52.183  1.00113.60           C  
ANISOU 2917  CB  ALA B  49     9408  16604  17151   4761   -533   -922       C  
ATOM   2918  N   HIS B  50      16.613 -44.726 -54.907  1.00125.25           N  
ANISOU 2918  N   HIS B  50    10468  18602  18520   5228    225  -1303       N  
ATOM   2919  CA  HIS B  50      16.602 -45.021 -56.335  1.00128.81           C  
ANISOU 2919  CA  HIS B  50    10968  19140  18832   5357    599  -1665       C  
ATOM   2920  C   HIS B  50      17.339 -46.329 -56.582  1.00136.31           C  
ANISOU 2920  C   HIS B  50    11908  19881  20002   5865    941  -1726       C  
ATOM   2921  O   HIS B  50      16.875 -47.176 -57.346  1.00137.74           O  
ANISOU 2921  O   HIS B  50    12449  19731  20154   6075   1240  -2056       O  
ATOM   2922  CB  HIS B  50      17.251 -43.881 -57.125  1.00130.13           C  
ANISOU 2922  CB  HIS B  50    10712  19984  18746   5064    667  -1682       C  
ATOM   2923  CG  HIS B  50      17.300 -44.115 -58.604  1.00133.38           C  
ANISOU 2923  CG  HIS B  50    11142  20577  18961   5149   1071  -2077       C  
ATOM   2924  ND1 HIS B  50      18.172 -43.442 -59.432  1.00136.89           N  
ANISOU 2924  ND1 HIS B  50    11166  21665  19180   4978   1278  -2131       N  
ATOM   2925  CD2 HIS B  50      16.582 -44.940 -59.404  1.00134.50           C  
ANISOU 2925  CD2 HIS B  50    11691  20363  19051   5330   1326  -2462       C  
ATOM   2926  CE1 HIS B  50      17.994 -43.847 -60.677  1.00139.37           C  
ANISOU 2926  CE1 HIS B  50    11624  22018  19312   5057   1661  -2542       C  
ATOM   2927  NE2 HIS B  50      17.036 -44.756 -60.687  1.00137.99           N  
ANISOU 2927  NE2 HIS B  50    11961  21231  19238   5272   1692  -2752       N  
ATOM   2928  N   GLU B  51      18.484 -46.487 -55.920  1.00141.54           N  
ANISOU 2928  N   GLU B  51    12161  20721  20895   6051    888  -1419       N  
ATOM   2929  CA  GLU B  51      19.267 -47.717 -56.004  1.00149.55           C  
ANISOU 2929  CA  GLU B  51    13099  21508  22214   6579   1165  -1438       C  
ATOM   2930  C   GLU B  51      18.431 -48.913 -55.558  1.00149.52           C  
ANISOU 2930  C   GLU B  51    13678  20767  22364   6858   1167  -1519       C  
ATOM   2931  O   GLU B  51      18.533 -50.002 -56.123  1.00154.21           O  
ANISOU 2931  O   GLU B  51    14497  21009  23088   7235   1524  -1746       O  
ATOM   2932  CB  GLU B  51      20.532 -47.600 -55.148  1.00154.59           C  
ANISOU 2932  CB  GLU B  51    13168  22461  23109   6696    962  -1065       C  
ATOM   2933  CG  GLU B  51      21.506 -48.767 -55.276  1.00163.91           C  
ANISOU 2933  CG  GLU B  51    14131  23483  24666   7274   1223  -1089       C  
ATOM   2934  CD  GLU B  51      21.200 -49.907 -54.322  1.00166.37           C  
ANISOU 2934  CD  GLU B  51    14783  23153  25279   7643   1045   -957       C  
ATOM   2935  OE1 GLU B  51      21.208 -49.679 -53.094  1.00165.03           O  
ANISOU 2935  OE1 GLU B  51    14546  22978  25178   7534    588   -614       O  
ATOM   2936  OE2 GLU B  51      20.950 -51.032 -54.803  1.00170.05           O  
ANISOU 2936  OE2 GLU B  51    15616  23115  25883   8020   1365  -1208       O  
ATOM   2937  N   GLU B  52      17.600 -48.694 -54.543  1.00144.70           N  
ANISOU 2937  N   GLU B  52    13336  19925  21719   6643    789  -1354       N  
ATOM   2938  CA  GLU B  52      16.695 -49.726 -54.053  1.00143.56           C  
ANISOU 2938  CA  GLU B  52    13784  19114  21647   6817    760  -1444       C  
ATOM   2939  C   GLU B  52      15.695 -50.107 -55.140  1.00140.56           C  
ANISOU 2939  C   GLU B  52    13911  18445  21052   6756   1056  -1904       C  
ATOM   2940  O   GLU B  52      15.186 -51.227 -55.168  1.00142.53           O  
ANISOU 2940  O   GLU B  52    14670  18132  21353   6972   1216  -2089       O  
ATOM   2941  CB  GLU B  52      15.967 -49.235 -52.798  1.00139.40           C  
ANISOU 2941  CB  GLU B  52    13409  18487  21068   6520    313  -1226       C  
ATOM   2942  CG  GLU B  52      15.116 -50.286 -52.104  1.00139.84           C  
ANISOU 2942  CG  GLU B  52    14060  17888  21187   6677    239  -1293       C  
ATOM   2943  CD  GLU B  52      14.619 -49.824 -50.750  1.00136.43           C  
ANISOU 2943  CD  GLU B  52    13701  17406  20731   6424   -198  -1066       C  
ATOM   2944  OE1 GLU B  52      15.112 -48.789 -50.255  1.00134.90           O  
ANISOU 2944  OE1 GLU B  52    13066  17677  20513   6179   -439   -797       O  
ATOM   2945  OE2 GLU B  52      13.736 -50.498 -50.180  1.00135.57           O  
ANISOU 2945  OE2 GLU B  52    14116  16782  20613   6440   -292  -1184       O  
ATOM   2946  N   GLY B  53      15.422 -49.167 -56.038  1.00115.07           N  
ANISOU 2946  N   GLY B  53    13368  14382  15972   1938  -3066   3762       N  
ATOM   2947  CA  GLY B  53      14.518 -49.420 -57.142  1.00113.25           C  
ANISOU 2947  CA  GLY B  53    13365  13605  16060   1707  -3221   3673       C  
ATOM   2948  C   GLY B  53      13.277 -48.552 -57.109  1.00109.38           C  
ANISOU 2948  C   GLY B  53    12792  13035  15731   1257  -3165   3773       C  
ATOM   2949  O   GLY B  53      12.260 -48.891 -57.714  1.00110.22           O  
ANISOU 2949  O   GLY B  53    13040  12669  16169   1066  -3316   3763       O  
ATOM   2950  N   ILE B  54      13.354 -47.427 -56.406  1.00105.46           N  
ANISOU 2950  N   ILE B  54    12050  13017  15002   1110  -2968   3825       N  
ATOM   2951  CA  ILE B  54      12.218 -46.515 -56.335  1.00101.72           C  
ANISOU 2951  CA  ILE B  54    11505  12525  14620    736  -2910   3909       C  
ATOM   2952  C   ILE B  54      12.177 -45.608 -57.566  1.00 97.80           C  
ANISOU 2952  C   ILE B  54    11090  12075  13994    600  -2904   3559       C  
ATOM   2953  O   ILE B  54      13.210 -45.328 -58.173  1.00 97.83           O  
ANISOU 2953  O   ILE B  54    11110  12303  13757    743  -2826   3285       O  
ATOM   2954  CB  ILE B  54      12.220 -45.694 -55.028  1.00101.18           C  
ANISOU 2954  CB  ILE B  54    11178  12911  14356    668  -2716   4115       C  
ATOM   2955  CG1 ILE B  54      10.787 -45.440 -54.556  1.00101.45           C  
ANISOU 2955  CG1 ILE B  54    11172  12766  14609    385  -2702   4401       C  
ATOM   2956  CG2 ILE B  54      12.986 -44.396 -55.198  1.00 78.74           C  
ANISOU 2956  CG2 ILE B  54     8179  10557  11183    597  -2554   3805       C  
ATOM   2957  CD1 ILE B  54      10.689 -44.967 -53.126  1.00101.82           C  
ANISOU 2957  CD1 ILE B  54    11002  13196  14489    416  -2540   4685       C  
ATOM   2958  N   CYS B  55      10.977 -45.170 -57.939  1.00 94.62           N  
ANISOU 2958  N   CYS B  55    10745  11469  13738    358  -2967   3571       N  
ATOM   2959  CA  CYS B  55      10.793 -44.366 -59.145  1.00 91.78           C  
ANISOU 2959  CA  CYS B  55    10543  11106  13223    315  -2967   3273       C  
ATOM   2960  C   CYS B  55      10.575 -42.896 -58.819  1.00 88.72           C  
ANISOU 2960  C   CYS B  55    10071  11044  12593    118  -2737   3287       C  
ATOM   2961  O   CYS B  55      11.017 -42.016 -59.556  1.00 87.99           O  
ANISOU 2961  O   CYS B  55    10102  11089  12240    133  -2573   3070       O  
ATOM   2962  CB  CYS B  55       9.611 -44.886 -59.964  1.00 92.37           C  
ANISOU 2962  CB  CYS B  55    10767  10746  13585    275  -3246   3179       C  
ATOM   2963  SG  CYS B  55       8.007 -44.713 -59.148  1.00143.21           S  
ANISOU 2963  SG  CYS B  55    17017  17076  20322    -40  -3299   3442       S  
ATOM   2964  N   GLY B  56       9.877 -42.634 -57.719  1.00 87.82           N  
ANISOU 2964  N   GLY B  56     9774  11030  12564    -51  -2700   3553       N  
ATOM   2965  CA  GLY B  56       9.612 -41.269 -57.306  1.00 85.92           C  
ANISOU 2965  CA  GLY B  56     9464  11079  12103   -215  -2508   3564       C  
ATOM   2966  C   GLY B  56       9.053 -41.168 -55.903  1.00 86.36           C  
ANISOU 2966  C   GLY B  56     9280  11312  12222   -315  -2471   3878       C  
ATOM   2967  O   GLY B  56       8.902 -42.175 -55.215  1.00 87.78           O  
ANISOU 2967  O   GLY B  56     9357  11385  12610   -252  -2549   4130       O  
ATOM   2968  N   ILE B  57       8.762 -39.946 -55.465  1.00 85.67           N  
ANISOU 2968  N   ILE B  57     9133  11482  11934   -437  -2326   3876       N  
ATOM   2969  CA  ILE B  57       8.131 -39.737 -54.163  1.00 86.25           C  
ANISOU 2969  CA  ILE B  57     8989  11766  12016   -489  -2293   4162       C  
ATOM   2970  C   ILE B  57       6.918 -38.818 -54.283  1.00 85.08           C  
ANISOU 2970  C   ILE B  57     8891  11619  11816   -625  -2300   4176       C  
ATOM   2971  O   ILE B  57       6.743 -38.130 -55.285  1.00 83.99           O  
ANISOU 2971  O   ILE B  57     8978  11377  11557   -651  -2291   3944       O  
ATOM   2972  CB  ILE B  57       9.118 -39.172 -53.104  1.00 74.52           C  
ANISOU 2972  CB  ILE B  57     7300  10728  10287   -414  -2129   4134       C  
ATOM   2973  CG1 ILE B  57       9.178 -37.644 -53.155  1.00 72.89           C  
ANISOU 2973  CG1 ILE B  57     7125  10729   9840   -553  -1967   3911       C  
ATOM   2974  CG2 ILE B  57      10.504 -39.768 -53.273  1.00 75.75           C  
ANISOU 2974  CG2 ILE B  57     7414  10968  10402   -249  -2109   3962       C  
ATOM   2975  CD1 ILE B  57      10.236 -37.050 -52.243  1.00 73.10           C  
ANISOU 2975  CD1 ILE B  57     6916  11184   9676   -508  -1830   3748       C  
ATOM   2976  N   ARG B  58       6.071 -38.825 -53.262  1.00 85.80           N  
ANISOU 2976  N   ARG B  58     8790  11842  11967   -661  -2303   4461       N  
ATOM   2977  CA  ARG B  58       4.921 -37.937 -53.240  1.00 85.18           C  
ANISOU 2977  CA  ARG B  58     8717  11844  11805   -744  -2315   4474       C  
ATOM   2978  C   ARG B  58       4.889 -37.147 -51.939  1.00 85.09           C  
ANISOU 2978  C   ARG B  58     8527  12237  11568   -709  -2181   4627       C  
ATOM   2979  O   ARG B  58       4.995 -37.714 -50.851  1.00 85.56           O  
ANISOU 2979  O   ARG B  58     8376  12461  11673   -624  -2140   4904       O  
ATOM   2980  CB  ARG B  58       3.616 -38.722 -53.414  1.00 86.72           C  
ANISOU 2980  CB  ARG B  58     8811  11804  12334   -827  -2477   4629       C  
ATOM   2981  CG  ARG B  58       3.637 -39.722 -54.558  1.00 87.94           C  
ANISOU 2981  CG  ARG B  58     9094  11546  12774   -838  -2659   4458       C  
ATOM   2982  CD  ARG B  58       2.299 -39.790 -55.275  1.00 88.95           C  
ANISOU 2982  CD  ARG B  58     9192  11506  13100   -912  -2860   4322       C  
ATOM   2983  NE  ARG B  58       2.054 -38.603 -56.087  1.00 87.33           N  
ANISOU 2983  NE  ARG B  58     9212  11421  12548   -800  -2890   4036       N  
ATOM   2984  CZ  ARG B  58       2.160 -38.564 -57.412  1.00 87.37           C  
ANISOU 2984  CZ  ARG B  58     9485  11239  12472   -660  -3026   3706       C  
ATOM   2985  NH1 ARG B  58       1.920 -37.435 -58.062  1.00 86.23           N  
ANISOU 2985  NH1 ARG B  58     9600  11203  11959   -499  -2999   3507       N  
ATOM   2986  NH2 ARG B  58       2.497 -39.653 -58.088  1.00 88.83           N  
ANISOU 2986  NH2 ARG B  58     9713  11122  12916   -633  -3183   3580       N  
ATOM   2987  N   SER B  59       4.747 -35.832 -52.063  1.00 84.39           N  
ANISOU 2987  N   SER B  59     8557  12295  11211   -730  -2107   4442       N  
ATOM   2988  CA  SER B  59       4.595 -34.963 -50.905  1.00 84.36           C  
ANISOU 2988  CA  SER B  59     8409  12664  10979   -676  -2016   4523       C  
ATOM   2989  C   SER B  59       3.412 -35.416 -50.061  1.00 85.73           C  
ANISOU 2989  C   SER B  59     8380  12930  11263   -643  -2023   4810       C  
ATOM   2990  O   SER B  59       2.514 -36.097 -50.552  1.00 86.53           O  
ANISOU 2990  O   SER B  59     8452  12807  11619   -721  -2128   4925       O  
ATOM   2991  CB  SER B  59       4.368 -33.519 -51.351  1.00 82.85           C  
ANISOU 2991  CB  SER B  59     8460  12491  10529   -707  -1940   4272       C  
ATOM   2992  OG  SER B  59       5.314 -33.122 -52.323  1.00 82.10           O  
ANISOU 2992  OG  SER B  59     8621  12196  10376   -777  -1822   3973       O  
ATOM   2993  N   VAL B  60       3.419 -35.038 -48.788  1.00 86.69           N  
ANISOU 2993  N   VAL B  60     8362  13369  11209   -532  -1870   4847       N  
ATOM   2994  CA  VAL B  60       2.301 -35.321 -47.901  1.00 88.90           C  
ANISOU 2994  CA  VAL B  60     8474  13759  11544   -494  -1767   5063       C  
ATOM   2995  C   VAL B  60       1.437 -34.082 -47.809  1.00 88.19           C  
ANISOU 2995  C   VAL B  60     8448  13832  11228   -468  -1745   4906       C  
ATOM   2996  O   VAL B  60       0.209 -34.160 -47.843  1.00 89.48           O  
ANISOU 2996  O   VAL B  60     8524  13994  11482   -505  -1759   5017       O  
ATOM   2997  CB  VAL B  60       2.782 -35.669 -46.486  1.00 91.21           C  
ANISOU 2997  CB  VAL B  60     8611  14326  11717   -293  -1600   5206       C  
ATOM   2998  CG1 VAL B  60       1.608 -36.055 -45.602  1.00 93.25           C  
ANISOU 2998  CG1 VAL B  60     8683  14700  12046   -249  -1461   5519       C  
ATOM   2999  CG2 VAL B  60       3.792 -36.787 -46.539  1.00 92.73           C  
ANISOU 2999  CG2 VAL B  60     8792  14391  12051   -229  -1622   5317       C  
ATOM   3000  N   THR B  61       2.098 -32.935 -47.695  1.00 86.61           N  
ANISOU 3000  N   THR B  61     8378  13788  10742   -398  -1730   4661       N  
ATOM   3001  CA  THR B  61       1.409 -31.662 -47.540  1.00 85.80           C  
ANISOU 3001  CA  THR B  61     8389  13822  10388   -322  -1712   4500       C  
ATOM   3002  C   THR B  61       1.860 -30.628 -48.579  1.00 83.35           C  
ANISOU 3002  C   THR B  61     8377  13382   9910   -375  -1799   4299       C  
ATOM   3003  O   THR B  61       2.818 -30.852 -49.315  1.00 83.07           O  
ANISOU 3003  O   THR B  61     8423  13206   9935   -484  -1855   4294       O  
ATOM   3004  CB  THR B  61       1.571 -31.112 -46.104  1.00 87.38           C  
ANISOU 3004  CB  THR B  61     8464  14376  10359   -134  -1596   4456       C  
ATOM   3005  OG1 THR B  61       1.035 -29.786 -46.027  1.00 87.33           O  
ANISOU 3005  OG1 THR B  61     8611  14470  10099    -43  -1609   4267       O  
ATOM   3006  CG2 THR B  61       3.035 -31.088 -45.697  1.00 87.75           C  
ANISOU 3006  CG2 THR B  61     8437  14581  10324    -89  -1611   4356       C  
ATOM   3007  N   ARG B  62       1.149 -29.505 -48.628  1.00 81.71           N  
ANISOU 3007  N   ARG B  62     8355  13223   9468   -277  -1795   4172       N  
ATOM   3008  CA  ARG B  62       1.401 -28.426 -49.584  1.00 79.70           C  
ANISOU 3008  CA  ARG B  62     8485  12817   8982   -288  -1827   4057       C  
ATOM   3009  C   ARG B  62       2.806 -27.835 -49.460  1.00 78.28           C  
ANISOU 3009  C   ARG B  62     8402  12570   8770   -424  -1651   3793       C  
ATOM   3010  O   ARG B  62       3.607 -27.903 -50.394  1.00 78.06           O  
ANISOU 3010  O   ARG B  62     8580  12230   8848   -580  -1524   3624       O  
ATOM   3011  CB  ARG B  62       0.353 -27.326 -49.375  1.00 80.07           C  
ANISOU 3011  CB  ARG B  62     8722  12938   8764    -88  -1810   3931       C  
ATOM   3012  CG  ARG B  62       0.528 -26.062 -50.204  1.00 80.05           C  
ANISOU 3012  CG  ARG B  62     9235  12697   8481    -43  -1729   3756       C  
ATOM   3013  CD  ARG B  62      -0.147 -24.874 -49.520  1.00 80.79           C  
ANISOU 3013  CD  ARG B  62     9459  12991   8246    184  -1740   3698       C  
ATOM   3014  NE  ARG B  62      -0.279 -23.718 -50.403  1.00 81.70           N  
ANISOU 3014  NE  ARG B  62    10172  12758   8112    296  -1602   3492       N  
ATOM   3015  CZ  ARG B  62      -0.460 -22.467 -49.989  1.00 82.84           C  
ANISOU 3015  CZ  ARG B  62    10598  12897   7979    450  -1525   3346       C  
ATOM   3016  NH1 ARG B  62      -0.519 -22.190 -48.695  1.00 83.15           N  
ANISOU 3016  NH1 ARG B  62    10342  13305   7945    516  -1604   3346       N  
ATOM   3017  NH2 ARG B  62      -0.572 -21.488 -50.874  1.00 84.06           N  
ANISOU 3017  NH2 ARG B  62    11369  12662   7909    578  -1357   3200       N  
ATOM   3018  N   LEU B  63       3.094 -27.264 -48.295  1.00 77.73           N  
ANISOU 3018  N   LEU B  63     8155  12812   8566   -355  -1636   3717       N  
ATOM   3019  CA  LEU B  63       4.368 -26.600 -48.040  1.00 77.47           C  
ANISOU 3019  CA  LEU B  63     8133  12764   8537   -497  -1481   3362       C  
ATOM   3020  C   LEU B  63       5.570 -27.531 -48.216  1.00 76.57           C  
ANISOU 3020  C   LEU B  63     7799  12631   8662   -648  -1439   3294       C  
ATOM   3021  O   LEU B  63       6.691 -27.075 -48.443  1.00 77.38           O  
ANISOU 3021  O   LEU B  63     7932  12627   8841   -839  -1269   2953       O  
ATOM   3022  CB  LEU B  63       4.371 -25.996 -46.638  1.00 78.54           C  
ANISOU 3022  CB  LEU B  63     8032  13323   8486   -324  -1554   3268       C  
ATOM   3023  CG  LEU B  63       3.204 -25.093 -46.252  1.00 78.82           C  
ANISOU 3023  CG  LEU B  63     8234  13472   8244   -104  -1622   3330       C  
ATOM   3024  CD1 LEU B  63       3.374 -24.593 -44.833  1.00 69.03           C  
ANISOU 3024  CD1 LEU B  63     6730  12684   6814    106  -1712   3197       C  
ATOM   3025  CD2 LEU B  63       3.092 -23.932 -47.211  1.00 79.30           C  
ANISOU 3025  CD2 LEU B  63     8827  13086   8217   -205  -1455   3095       C  
ATOM   3026  N   GLU B  64       5.331 -28.833 -48.103  1.00 75.36           N  
ANISOU 3026  N   GLU B  64     7418  12575   8639   -562  -1577   3608       N  
ATOM   3027  CA  GLU B  64       6.363 -29.824 -48.369  1.00 75.20           C  
ANISOU 3027  CA  GLU B  64     7242  12509   8821   -640  -1562   3576       C  
ATOM   3028  C   GLU B  64       6.710 -29.777 -49.848  1.00 74.36           C  
ANISOU 3028  C   GLU B  64     7464  11958   8832   -837  -1430   3424       C  
ATOM   3029  O   GLU B  64       7.876 -29.644 -50.222  1.00 74.97           O  
ANISOU 3029  O   GLU B  64     7540  11961   8986   -986  -1273   3147       O  
ATOM   3030  CB  GLU B  64       5.868 -31.219 -47.977  1.00 75.16           C  
ANISOU 3030  CB  GLU B  64     7012  12605   8938   -487  -1714   3986       C  
ATOM   3031  CG  GLU B  64       6.835 -32.356 -48.282  1.00 75.61           C  
ANISOU 3031  CG  GLU B  64     6961  12578   9187   -503  -1723   3989       C  
ATOM   3032  CD  GLU B  64       6.335 -33.693 -47.772  1.00 76.72           C  
ANISOU 3032  CD  GLU B  64     6930  12761   9459   -340  -1828   4419       C  
ATOM   3033  OE1 GLU B  64       5.440 -33.702 -46.901  1.00 77.18           O  
ANISOU 3033  OE1 GLU B  64     6953  12911   9462   -232  -1740   4540       O  
ATOM   3034  OE2 GLU B  64       6.836 -34.735 -48.241  1.00 77.49           O  
ANISOU 3034  OE2 GLU B  64     7033  12665   9745   -345  -1855   4476       O  
ATOM   3035  N   ASN B  65       5.681 -29.881 -50.683  1.00 73.50           N  
ANISOU 3035  N   ASN B  65     7614  11594   8720   -805  -1490   3588       N  
ATOM   3036  CA  ASN B  65       5.836 -29.749 -52.123  1.00 73.63           C  
ANISOU 3036  CA  ASN B  65     8006  11210   8760   -887  -1376   3459       C  
ATOM   3037  C   ASN B  65       6.507 -28.427 -52.484  1.00 75.16           C  
ANISOU 3037  C   ASN B  65     8499  11235   8824  -1020  -1075   3156       C  
ATOM   3038  O   ASN B  65       7.351 -28.373 -53.380  1.00 75.99           O  
ANISOU 3038  O   ASN B  65     8787  11095   8989  -1145   -861   2992       O  
ATOM   3039  CB  ASN B  65       4.472 -29.869 -52.805  1.00 73.05           C  
ANISOU 3039  CB  ASN B  65     8141  10983   8631   -744  -1533   3617       C  
ATOM   3040  CG  ASN B  65       4.530 -29.573 -54.288  1.00 73.42           C  
ANISOU 3040  CG  ASN B  65     8641  10658   8595   -709  -1423   3467       C  
ATOM   3041  OD1 ASN B  65       4.140 -28.493 -54.734  1.00 73.48           O  
ANISOU 3041  OD1 ASN B  65     9032  10527   8360   -617  -1295   3373       O  
ATOM   3042  ND2 ASN B  65       5.013 -30.535 -55.064  1.00 73.90           N  
ANISOU 3042  ND2 ASN B  65     8697  10556   8826   -728  -1466   3449       N  
ATOM   3043  N   LEU B  66       6.137 -27.367 -51.766  1.00 75.85           N  
ANISOU 3043  N   LEU B  66     8635  11439   8744   -993  -1034   3085       N  
ATOM   3044  CA  LEU B  66       6.767 -26.064 -51.950  1.00 77.48           C  
ANISOU 3044  CA  LEU B  66     9121  11439   8880  -1156   -720   2784       C  
ATOM   3045  C   LEU B  66       8.261 -26.128 -51.656  1.00 79.27           C  
ANISOU 3045  C   LEU B  66     9051  11757   9311  -1409   -548   2489       C  
ATOM   3046  O   LEU B  66       9.062 -25.562 -52.390  1.00 80.87           O  
ANISOU 3046  O   LEU B  66     9474  11662   9591  -1630   -211   2263       O  
ATOM   3047  CB  LEU B  66       6.105 -25.001 -51.074  1.00 77.61           C  
ANISOU 3047  CB  LEU B  66     9201  11590   8698  -1053   -760   2733       C  
ATOM   3048  CG  LEU B  66       4.659 -24.641 -51.405  1.00 76.64           C  
ANISOU 3048  CG  LEU B  66     9408  11388   8322   -782   -883   2941       C  
ATOM   3049  CD1 LEU B  66       4.249 -23.355 -50.704  1.00 77.75           C  
ANISOU 3049  CD1 LEU B  66     9722  11576   8243   -686   -839   2807       C  
ATOM   3050  CD2 LEU B  66       4.470 -24.520 -52.905  1.00 76.63           C  
ANISOU 3050  CD2 LEU B  66     9919  10953   8245   -731   -725   2964       C  
ATOM   3051  N   MET B  67       8.628 -26.825 -50.585  1.00 79.83           N  
ANISOU 3051  N   MET B  67     8616  12258   9456  -1346   -760   2488       N  
ATOM   3052  CA  MET B  67      10.034 -27.004 -50.241  1.00 82.09           C  
ANISOU 3052  CA  MET B  67     8539  12739   9912  -1508   -664   2165       C  
ATOM   3053  C   MET B  67      10.772 -27.740 -51.349  1.00 82.25           C  
ANISOU 3053  C   MET B  67     8618  12547  10087  -1619   -525   2156       C  
ATOM   3054  O   MET B  67      11.852 -27.321 -51.770  1.00 84.42           O  
ANISOU 3054  O   MET B  67     8862  12720  10493  -1868   -235   1831       O  
ATOM   3055  CB  MET B  67      10.180 -27.773 -48.931  1.00 82.25           C  
ANISOU 3055  CB  MET B  67     8056  13293   9902  -1277   -956   2223       C  
ATOM   3056  CG  MET B  67      11.619 -28.091 -48.577  1.00 72.39           C  
ANISOU 3056  CG  MET B  67     6389  12330   8785  -1345   -920   1861       C  
ATOM   3057  SD  MET B  67      11.792 -28.981 -47.025  1.00102.72           S  
ANISOU 3057  SD  MET B  67     9713  16827  12490   -929  -1259   1942       S  
ATOM   3058  CE  MET B  67      11.013 -30.536 -47.445  1.00100.68           C  
ANISOU 3058  CE  MET B  67     9587  16414  12253   -713  -1414   2561       C  
ATOM   3059  N   TRP B  68      10.180 -28.837 -51.812  1.00 80.66           N  
ANISOU 3059  N   TRP B  68     8481  12281   9885  -1437   -723   2494       N  
ATOM   3060  CA  TRP B  68      10.751 -29.601 -52.910  1.00 81.32           C  
ANISOU 3060  CA  TRP B  68     8660  12157  10079  -1468   -641   2499       C  
ATOM   3061  C   TRP B  68      11.003 -28.704 -54.114  1.00 85.01           C  
ANISOU 3061  C   TRP B  68     9572  12217  10512  -1640   -268   2350       C  
ATOM   3062  O   TRP B  68      12.073 -28.748 -54.709  1.00 86.94           O  
ANISOU 3062  O   TRP B  68     9785  12389  10860  -1790    -14   2147       O  
ATOM   3063  CB  TRP B  68       9.835 -30.761 -53.304  1.00 77.59           C  
ANISOU 3063  CB  TRP B  68     8270  11586   9626  -1252   -924   2852       C  
ATOM   3064  CG  TRP B  68       9.719 -31.829 -52.262  1.00 75.62           C  
ANISOU 3064  CG  TRP B  68     7635  11648   9449  -1086  -1202   3056       C  
ATOM   3065  CD1 TRP B  68       8.582 -32.244 -51.641  1.00 74.34           C  
ANISOU 3065  CD1 TRP B  68     7405  11567   9273   -940  -1420   3376       C  
ATOM   3066  CD2 TRP B  68      10.784 -32.616 -51.718  1.00 75.91           C  
ANISOU 3066  CD2 TRP B  68     7321  11955   9565  -1013  -1252   2968       C  
ATOM   3067  NE1 TRP B  68       8.870 -33.244 -50.745  1.00 74.48           N  
ANISOU 3067  NE1 TRP B  68     7099  11841   9360   -785  -1562   3539       N  
ATOM   3068  CE2 TRP B  68      10.216 -33.489 -50.774  1.00 75.38           C  
ANISOU 3068  CE2 TRP B  68     7052  12083   9506   -792  -1485   3287       C  
ATOM   3069  CE3 TRP B  68      12.162 -32.666 -51.938  1.00 77.26           C  
ANISOU 3069  CE3 TRP B  68     7323  12242   9791  -1088  -1105   2645       C  
ATOM   3070  CZ2 TRP B  68      10.980 -34.400 -50.049  1.00 76.57           C  
ANISOU 3070  CZ2 TRP B  68     6905  12516   9673   -588  -1582   3314       C  
ATOM   3071  CZ3 TRP B  68      12.917 -33.570 -51.218  1.00 78.26           C  
ANISOU 3071  CZ3 TRP B  68     7094  12704   9936   -888  -1246   2621       C  
ATOM   3072  CH2 TRP B  68      12.326 -34.425 -50.286  1.00 77.89           C  
ANISOU 3072  CH2 TRP B  68     6919  12823   9854   -613  -1486   2963       C  
ATOM   3073  N   LYS B  69      10.020 -27.877 -54.457  1.00 87.07           N  
ANISOU 3073  N   LYS B  69    10255  12225  10603  -1582   -208   2460       N  
ATOM   3074  CA  LYS B  69      10.167 -26.947 -55.575  1.00 90.97           C  
ANISOU 3074  CA  LYS B  69    11271  12293  11000  -1668    191   2374       C  
ATOM   3075  C   LYS B  69      11.195 -25.851 -55.299  1.00 95.98           C  
ANISOU 3075  C   LYS B  69    11866  12847  11753  -2011    609   2039       C  
ATOM   3076  O   LYS B  69      11.742 -25.262 -56.228  1.00 98.33           O  
ANISOU 3076  O   LYS B  69    12506  12793  12063  -2161   1053   1945       O  
ATOM   3077  CB  LYS B  69       8.822 -26.311 -55.933  1.00 90.05           C  
ANISOU 3077  CB  LYS B  69    11636  11958  10621  -1436    128   2562       C  
ATOM   3078  CG  LYS B  69       7.874 -27.224 -56.694  1.00 88.23           C  
ANISOU 3078  CG  LYS B  69    11551  11683  10290  -1124   -175   2796       C  
ATOM   3079  CD  LYS B  69       6.572 -26.506 -57.021  1.00 88.05           C  
ANISOU 3079  CD  LYS B  69    11959  11519   9977   -853   -247   2906       C  
ATOM   3080  CE  LYS B  69       5.672 -27.349 -57.915  1.00 87.48           C  
ANISOU 3080  CE  LYS B  69    12013  11405   9819   -536   -546   3031       C  
ATOM   3081  NZ  LYS B  69       5.283 -28.645 -57.293  1.00 85.76           N  
ANISOU 3081  NZ  LYS B  69    11270  11469   9848   -550   -958   3148       N  
ATOM   3082  N   GLN B  70      11.449 -25.582 -54.022  1.00 98.55           N  
ANISOU 3082  N   GLN B  70    11772  13499  12174  -2123    482   1844       N  
ATOM   3083  CA  GLN B  70      12.360 -24.512 -53.624  1.00103.96           C  
ANISOU 3083  CA  GLN B  70    12346  14129  13025  -2471    823   1436       C  
ATOM   3084  C   GLN B  70      13.802 -24.992 -53.466  1.00106.81           C  
ANISOU 3084  C   GLN B  70    12172  14758  13652  -2702    933   1099       C  
ATOM   3085  O   GLN B  70      14.720 -24.183 -53.350  1.00110.07           O  
ANISOU 3085  O   GLN B  70    12440  15101  14281  -3058   1279    695       O  
ATOM   3086  CB  GLN B  70      11.880 -23.852 -52.324  1.00105.17           C  
ANISOU 3086  CB  GLN B  70    12323  14518  13117  -2427    606   1310       C  
ATOM   3087  CG  GLN B  70      10.690 -22.901 -52.488  1.00105.74           C  
ANISOU 3087  CG  GLN B  70    12962  14268  12948  -2281    646   1493       C  
ATOM   3088  CD  GLN B  70      10.056 -22.512 -51.157  1.00106.01           C  
ANISOU 3088  CD  GLN B  70    12782  14638  12860  -2118    329   1438       C  
ATOM   3089  OE1 GLN B  70      10.610 -22.777 -50.089  1.00107.10           O  
ANISOU 3089  OE1 GLN B  70    12374  15220  13100  -2138    132   1208       O  
ATOM   3090  NE2 GLN B  70       8.884 -21.888 -51.220  1.00105.11           N  
ANISOU 3090  NE2 GLN B  70    13100  14353  12486  -1892    269   1638       N  
ATOM   3091  N   ILE B  71      14.001 -26.307 -53.466  1.00106.07           N  
ANISOU 3091  N   ILE B  71    11780  14965  13559  -2497    646   1238       N  
ATOM   3092  CA  ILE B  71      15.335 -26.857 -53.240  1.00109.07           C  
ANISOU 3092  CA  ILE B  71    11620  15687  14135  -2616    684    910       C  
ATOM   3093  C   ILE B  71      15.760 -27.874 -54.307  1.00108.50           C  
ANISOU 3093  C   ILE B  71    11615  15537  14072  -2513    738   1061       C  
ATOM   3094  O   ILE B  71      16.887 -28.369 -54.290  1.00110.57           O  
ANISOU 3094  O   ILE B  71    11465  16075  14470  -2574    794    796       O  
ATOM   3095  CB  ILE B  71      15.448 -27.473 -51.824  1.00109.32           C  
ANISOU 3095  CB  ILE B  71    11090  16310  14137  -2388    242    814       C  
ATOM   3096  CG1 ILE B  71      16.905 -27.490 -51.350  1.00113.70           C  
ANISOU 3096  CG1 ILE B  71    11043  17270  14886  -2547    326    272       C  
ATOM   3097  CG2 ILE B  71      14.826 -28.860 -51.783  1.00106.21           C  
ANISOU 3097  CG2 ILE B  71    10698  16050  13606  -1997   -143   1252       C  
ATOM   3098  CD1 ILE B  71      17.083 -27.982 -49.931  1.00114.43           C  
ANISOU 3098  CD1 ILE B  71    10611  17984  14883  -2237    -94    124       C  
ATOM   3099  N   THR B  72      14.859 -28.170 -55.239  1.00105.84           N  
ANISOU 3099  N   THR B  72    11784  14853  13576  -2321    701   1443       N  
ATOM   3100  CA  THR B  72      15.151 -29.106 -56.329  1.00105.35           C  
ANISOU 3100  CA  THR B  72    11853  14684  13493  -2170    723   1574       C  
ATOM   3101  C   THR B  72      16.404 -28.770 -57.150  1.00109.00           C  
ANISOU 3101  C   THR B  72    12286  15052  14076  -2417   1226   1302       C  
ATOM   3102  O   THR B  72      17.259 -29.637 -57.340  1.00109.76           O  
ANISOU 3102  O   THR B  72    12069  15392  14242  -2345   1181   1187       O  
ATOM   3103  CB  THR B  72      13.946 -29.285 -57.278  1.00102.72           C  
ANISOU 3103  CB  THR B  72    12093  13980  12957  -1912    618   1937       C  
ATOM   3104  OG1 THR B  72      12.793 -29.663 -56.518  1.00100.12           O  
ANISOU 3104  OG1 THR B  72    11712  13767  12561  -1717    177   2172       O  
ATOM   3105  CG2 THR B  72      14.238 -30.353 -58.323  1.00102.47           C  
ANISOU 3105  CG2 THR B  72    12156  13878  12899  -1699    560   2023       C  
ATOM   3106  N   PRO B  73      16.523 -27.521 -57.643  1.00112.12           N  
ANISOU 3106  N   PRO B  73    13019  15087  14496  -2694   1737   1209       N  
ATOM   3107  CA  PRO B  73      17.724 -27.247 -58.434  1.00116.04           C  
ANISOU 3107  CA  PRO B  73    13463  15489  15137  -2952   2284    981       C  
ATOM   3108  C   PRO B  73      18.989 -27.409 -57.603  1.00118.32           C  
ANISOU 3108  C   PRO B  73    12988  16261  15707  -3208   2296    513       C  
ATOM   3109  O   PRO B  73      19.982 -27.914 -58.117  1.00120.84           O  
ANISOU 3109  O   PRO B  73    13050  16752  16112  -3240   2483    352       O  
ATOM   3110  CB  PRO B  73      17.541 -25.785 -58.853  1.00119.44           C  
ANISOU 3110  CB  PRO B  73    14392  15409  15580  -3232   2848    977       C  
ATOM   3111  CG  PRO B  73      16.617 -25.212 -57.846  1.00117.44           C  
ANISOU 3111  CG  PRO B  73    14188  15155  15279  -3219   2548   1004       C  
ATOM   3112  CD  PRO B  73      15.679 -26.320 -57.507  1.00112.46           C  
ANISOU 3112  CD  PRO B  73    13494  14787  14449  -2786   1891   1293       C  
ATOM   3113  N   GLU B  74      18.943 -27.005 -56.337  1.00116.96           N  
ANISOU 3113  N   GLU B  74    12444  16350  15645  -3332   2074    271       N  
ATOM   3114  CA  GLU B  74      20.085 -27.181 -55.447  1.00118.52           C  
ANISOU 3114  CA  GLU B  74    11874  17093  16067  -3483   1994   -237       C  
ATOM   3115  C   GLU B  74      20.358 -28.666 -55.250  1.00117.32           C  
ANISOU 3115  C   GLU B  74    11385  17401  15791  -3065   1538   -153       C  
ATOM   3116  O   GLU B  74      21.508 -29.100 -55.246  1.00120.87           O  
ANISOU 3116  O   GLU B  74    11339  18226  16361  -3097   1605   -496       O  
ATOM   3117  CB  GLU B  74      19.839 -26.503 -54.096  1.00116.76           C  
ANISOU 3117  CB  GLU B  74    11368  17086  15911  -3575   1763   -504       C  
ATOM   3118  CG  GLU B  74      21.018 -26.606 -53.128  1.00118.58           C  
ANISOU 3118  CG  GLU B  74    10772  17937  16346  -3675   1643  -1121       C  
ATOM   3119  CD  GLU B  74      20.760 -25.920 -51.794  1.00117.81           C  
ANISOU 3119  CD  GLU B  74    10406  18081  16276  -3696   1383  -1425       C  
ATOM   3120  OE1 GLU B  74      21.723 -25.763 -51.012  1.00121.14           O  
ANISOU 3120  OE1 GLU B  74    10156  18989  16883  -3805   1315  -2037       O  
ATOM   3121  OE2 GLU B  74      19.601 -25.540 -51.524  1.00114.39           O  
ANISOU 3121  OE2 GLU B  74    10409  17391  15663  -3567   1228  -1089       O  
ATOM   3122  N   LEU B  75      19.289 -29.438 -55.095  1.00112.78           N  
ANISOU 3122  N   LEU B  75    11083  16780  14988  -2672   1092    295       N  
ATOM   3123  CA  LEU B  75      19.406 -30.879 -54.922  1.00111.49           C  
ANISOU 3123  CA  LEU B  75    10712  16932  14717  -2259    674    444       C  
ATOM   3124  C   LEU B  75      20.044 -31.529 -56.139  1.00113.18           C  
ANISOU 3124  C   LEU B  75    11033  17043  14927  -2187    869    467       C  
ATOM   3125  O   LEU B  75      21.052 -32.222 -56.018  1.00115.49           O  
ANISOU 3125  O   LEU B  75    10893  17731  15256  -2062    805    219       O  
ATOM   3126  CB  LEU B  75      18.039 -31.499 -54.646  1.00 80.52           C  
ANISOU 3126  CB  LEU B  75     7115  12857  10620  -1936    252    939       C  
ATOM   3127  CG  LEU B  75      17.607 -31.471 -53.183  1.00 79.67           C  
ANISOU 3127  CG  LEU B  75     6727  13087  10456  -1796    -86    949       C  
ATOM   3128  CD1 LEU B  75      16.211 -32.033 -53.020  1.00 76.74           C  
ANISOU 3128  CD1 LEU B  75     6680  12523   9956  -1538   -406   1462       C  
ATOM   3129  CD2 LEU B  75      18.597 -32.259 -52.351  1.00 81.75           C  
ANISOU 3129  CD2 LEU B  75     6426  13921  10713  -1555   -306    692       C  
ATOM   3130  N   ASN B  76      19.457 -31.294 -57.308  1.00113.08           N  
ANISOU 3130  N   ASN B  76    11602  16534  14831  -2205   1097    747       N  
ATOM   3131  CA  ASN B  76      20.005 -31.814 -58.555  1.00115.40           C  
ANISOU 3131  CA  ASN B  76    12062  16710  15072  -2094   1314    777       C  
ATOM   3132  C   ASN B  76      21.435 -31.342 -58.786  1.00121.22           C  
ANISOU 3132  C   ASN B  76    12400  17669  15987  -2403   1805    344       C  
ATOM   3133  O   ASN B  76      22.222 -32.014 -59.451  1.00122.89           O  
ANISOU 3133  O   ASN B  76    12484  18039  16172  -2257   1901    256       O  
ATOM   3134  CB  ASN B  76      19.119 -31.422 -59.738  1.00114.42           C  
ANISOU 3134  CB  ASN B  76    12655  16038  14782  -2027   1518   1106       C  
ATOM   3135  CG  ASN B  76      18.158 -32.524 -60.138  1.00111.06           C  
ANISOU 3135  CG  ASN B  76    12534  15474  14190  -1591   1037   1443       C  
ATOM   3136  OD1 ASN B  76      18.486 -33.707 -60.060  1.00110.63           O  
ANISOU 3136  OD1 ASN B  76    12252  15638  14146  -1336    718   1435       O  
ATOM   3137  ND2 ASN B  76      16.966 -32.139 -60.575  1.00109.08           N  
ANISOU 3137  ND2 ASN B  76    12798  14854  13795  -1494    983   1708       N  
ATOM   3138  N   HIS B  77      21.769 -30.185 -58.226  1.00124.69           N  
ANISOU 3138  N   HIS B  77    12622  18126  16629  -2836   2118     44       N  
ATOM   3139  CA  HIS B  77      23.127 -29.668 -58.302  1.00130.88           C  
ANISOU 3139  CA  HIS B  77    12915  19141  17671  -3217   2597   -449       C  
ATOM   3140  C   HIS B  77      24.045 -30.502 -57.415  1.00131.99           C  
ANISOU 3140  C   HIS B  77    12291  19988  17871  -3040   2229   -841       C  
ATOM   3141  O   HIS B  77      25.138 -30.886 -57.825  1.00135.52           O  
ANISOU 3141  O   HIS B  77    12359  20744  18389  -3045   2426  -1122       O  
ATOM   3142  CB  HIS B  77      23.159 -28.200 -57.872  1.00134.57           C  
ANISOU 3142  CB  HIS B  77    13357  19382  18392  -3747   2998   -708       C  
ATOM   3143  CG  HIS B  77      24.450 -27.509 -58.176  1.00141.32           C  
ANISOU 3143  CG  HIS B  77    13799  20309  19588  -4248   3636  -1190       C  
ATOM   3144  ND1 HIS B  77      24.981 -27.445 -59.447  1.00144.81           N  
ANISOU 3144  ND1 HIS B  77    14473  20505  20042  -4354   4221  -1086       N  
ATOM   3145  CD2 HIS B  77      25.313 -26.842 -57.375  1.00146.29           C  
ANISOU 3145  CD2 HIS B  77    13770  21235  20578  -4679   3799  -1806       C  
ATOM   3146  CE1 HIS B  77      26.118 -26.774 -59.414  1.00151.57           C  
ANISOU 3146  CE1 HIS B  77    14820  21489  21280  -4871   4761  -1588       C  
ATOM   3147  NE2 HIS B  77      26.342 -26.396 -58.169  1.00152.72           N  
ANISOU 3147  NE2 HIS B  77    14400  21961  21665  -5093   4500  -2064       N  
ATOM   3148  N   ILE B  78      23.585 -30.779 -56.198  1.00126.63           N  
ANISOU 3148  N   ILE B  78    11401  19588  17124  -2831   1704   -851       N  
ATOM   3149  CA  ILE B  78      24.334 -31.591 -55.245  1.00126.58           C  
ANISOU 3149  CA  ILE B  78    10741  20268  17086  -2532   1301  -1182       C  
ATOM   3150  C   ILE B  78      24.643 -32.978 -55.806  1.00125.40           C  
ANISOU 3150  C   ILE B  78    10623  20276  16746  -2062   1076   -995       C  
ATOM   3151  O   ILE B  78      25.753 -33.487 -55.655  1.00128.99           O  
ANISOU 3151  O   ILE B  78    10542  21253  17215  -1913   1039  -1381       O  
ATOM   3152  CB  ILE B  78      23.563 -31.736 -53.919  1.00123.85           C  
ANISOU 3152  CB  ILE B  78    10333  20117  16607  -2268    783  -1068       C  
ATOM   3153  CG1 ILE B  78      23.481 -30.386 -53.205  1.00124.89           C  
ANISOU 3153  CG1 ILE B  78    10299  20227  16926  -2682    953  -1403       C  
ATOM   3154  CG2 ILE B  78      24.224 -32.762 -53.018  1.00125.57           C  
ANISOU 3154  CG2 ILE B  78    10018  21009  16683  -1788    343  -1289       C  
ATOM   3155  CD1 ILE B  78      22.694 -30.422 -51.917  1.00122.30           C  
ANISOU 3155  CD1 ILE B  78     9932  20106  16431  -2398    482  -1289       C  
ATOM   3156  N   LEU B  79      23.649 -33.573 -56.457  1.00120.45           N  
ANISOU 3156  N   LEU B  79    10616  19202  15945  -1813    913   -442       N  
ATOM   3157  CA  LEU B  79      23.783 -34.894 -57.060  1.00119.31           C  
ANISOU 3157  CA  LEU B  79    10607  19088  15636  -1361    676   -239       C  
ATOM   3158  C   LEU B  79      24.978 -34.985 -57.999  1.00123.03           C  
ANISOU 3158  C   LEU B  79    10861  19737  16148  -1417   1055   -538       C  
ATOM   3159  O   LEU B  79      25.879 -35.801 -57.796  1.00125.06           O  
ANISOU 3159  O   LEU B  79    10698  20475  16343  -1116    884   -790       O  
ATOM   3160  CB  LEU B  79      22.507 -35.252 -57.826  1.00115.22           C  
ANISOU 3160  CB  LEU B  79    10802  17978  14998  -1207    539    307       C  
ATOM   3161  CG  LEU B  79      21.449 -36.088 -57.104  1.00111.47           C  
ANISOU 3161  CG  LEU B  79    10510  17410  14435   -878      2    682       C  
ATOM   3162  CD1 LEU B  79      20.953 -35.385 -55.858  1.00110.32           C  
ANISOU 3162  CD1 LEU B  79    10188  17400  14330  -1035   -105    669       C  
ATOM   3163  CD2 LEU B  79      20.293 -36.406 -58.038  1.00108.48           C  
ANISOU 3163  CD2 LEU B  79    10755  16469  13994   -773    -95   1102       C  
ATOM   3164  N   SER B  80      24.971 -34.143 -59.027  1.00124.53           N  
ANISOU 3164  N   SER B  80    11359  19545  16413  -1762   1591   -492       N  
ATOM   3165  CA  SER B  80      26.038 -34.115 -60.019  1.00128.76           C  
ANISOU 3165  CA  SER B  80    11739  20200  16983  -1846   2064   -717       C  
ATOM   3166  C   SER B  80      27.398 -33.891 -59.361  1.00133.44           C  
ANISOU 3166  C   SER B  80    11483  21439  17781  -2053   2223  -1344       C  
ATOM   3167  O   SER B  80      28.349 -34.629 -59.618  1.00136.21           O  
ANISOU 3167  O   SER B  80    11464  22224  18067  -1797   2201  -1584       O  
ATOM   3168  CB  SER B  80      25.762 -33.022 -61.053  1.00130.30           C  
ANISOU 3168  CB  SER B  80    12423  19852  17231  -2221   2704   -547       C  
ATOM   3169  OG  SER B  80      26.737 -33.025 -62.078  1.00134.84           O  
ANISOU 3169  OG  SER B  80    12902  20519  17810  -2266   3217   -692       O  
ATOM   3170  N   GLU B  81      27.473 -32.880 -58.500  1.00134.31           N  
ANISOU 3170  N   GLU B  81    11267  21632  18133  -2487   2352  -1650       N  
ATOM   3171  CA  GLU B  81      28.712 -32.543 -57.806  1.00139.11           C  
ANISOU 3171  CA  GLU B  81    11005  22867  18985  -2726   2482  -2347       C  
ATOM   3172  C   GLU B  81      29.207 -33.679 -56.916  1.00138.38           C  
ANISOU 3172  C   GLU B  81    10403  23474  18702  -2160   1867  -2586       C  
ATOM   3173  O   GLU B  81      30.411 -33.836 -56.711  1.00143.34           O  
ANISOU 3173  O   GLU B  81    10318  24728  19416  -2137   1932  -3152       O  
ATOM   3174  CB  GLU B  81      28.531 -31.278 -56.966  1.00140.84           C  
ANISOU 3174  CB  GLU B  81    11027  22993  19491  -3245   2633  -2640       C  
ATOM   3175  CG  GLU B  81      28.273 -30.019 -57.772  1.00143.46           C  
ANISOU 3175  CG  GLU B  81    11792  22659  20058  -3844   3340  -2512       C  
ATOM   3176  CD  GLU B  81      28.143 -28.791 -56.895  1.00147.73           C  
ANISOU 3176  CD  GLU B  81    12130  23094  20905  -4342   3465  -2858       C  
ATOM   3177  OE1 GLU B  81      27.900 -28.952 -55.680  1.00147.04           O  
ANISOU 3177  OE1 GLU B  81    11742  23371  20756  -4132   2911  -3045       O  
ATOM   3178  OE2 GLU B  81      28.292 -27.667 -57.418  1.00152.24           O  
ANISOU 3178  OE2 GLU B  81    12868  23205  21771  -4916   4133  -2942       O  
ATOM   3179  N   ASN B  82      28.276 -34.462 -56.382  1.00159.95           N  
ANISOU 3179  N   ASN B  82    10296  25981  24497   2083   -385   4890       N  
ATOM   3180  CA  ASN B  82      28.645 -35.586 -55.533  1.00158.51           C  
ANISOU 3180  CA  ASN B  82    10237  25869  24121   2449   -824   4522       C  
ATOM   3181  C   ASN B  82      28.582 -36.915 -56.277  1.00156.23           C  
ANISOU 3181  C   ASN B  82    10208  25919  23235   2913   -610   4561       C  
ATOM   3182  O   ASN B  82      28.218 -37.944 -55.708  1.00153.56           O  
ANISOU 3182  O   ASN B  82    10277  25593  22475   3216   -917   4338       O  
ATOM   3183  CB  ASN B  82      27.797 -35.619 -54.260  1.00155.07           C  
ANISOU 3183  CB  ASN B  82    10210  25152  23557   2367  -1339   4278       C  
ATOM   3184  CG  ASN B  82      28.064 -34.430 -53.352  1.00157.94           C  
ANISOU 3184  CG  ASN B  82    10304  25184  24522   1978  -1652   4114       C  
ATOM   3185  OD1 ASN B  82      29.050 -33.712 -53.524  1.00163.30           O  
ANISOU 3185  OD1 ASN B  82    10463  25843  25739   1823  -1558   4112       O  
ATOM   3186  ND2 ASN B  82      27.191 -34.221 -52.375  1.00154.79           N  
ANISOU 3186  ND2 ASN B  82    10271  24523  24019   1827  -2026   3952       N  
ATOM   3187  N   GLU B  83      28.932 -36.867 -57.560  1.00157.19           N  
ANISOU 3187  N   GLU B  83    10123  26298  23304   2970    -85   4839       N  
ATOM   3188  CA  GLU B  83      29.161 -38.058 -58.377  1.00156.44           C  
ANISOU 3188  CA  GLU B  83    10164  26550  22726   3420    144   4840       C  
ATOM   3189  C   GLU B  83      27.972 -39.005 -58.494  1.00150.44           C  
ANISOU 3189  C   GLU B  83    10059  25846  21255   3680    131   4808       C  
ATOM   3190  O   GLU B  83      27.965 -40.081 -57.893  1.00149.08           O  
ANISOU 3190  O   GLU B  83    10181  25678  20785   4006   -202   4517       O  
ATOM   3191  CB  GLU B  83      30.373 -38.832 -57.858  1.00159.53           C  
ANISOU 3191  CB  GLU B  83    10286  27037  23293   3726   -165   4503       C  
ATOM   3192  CG  GLU B  83      31.595 -37.975 -57.599  1.00164.68           C  
ANISOU 3192  CG  GLU B  83    10272  27618  24682   3500   -223   4436       C  
ATOM   3193  CD  GLU B  83      32.681 -38.740 -56.876  1.00167.82           C  
ANISOU 3193  CD  GLU B  83    10442  28058  25266   3813   -644   4030       C  
ATOM   3194  OE1 GLU B  83      32.528 -39.969 -56.709  1.00165.85           O  
ANISOU 3194  OE1 GLU B  83    10566  27904  24546   4217   -840   3847       O  
ATOM   3195  OE2 GLU B  83      33.682 -38.116 -56.471  1.00172.57           O  
ANISOU 3195  OE2 GLU B  83    10505  28579  26484   3664   -793   3874       O  
ATOM   3196  N   VAL B  84      26.981 -38.602 -59.283  1.00147.21           N  
ANISOU 3196  N   VAL B  84     9893  25460  20581   3545    487   5093       N  
ATOM   3197  CA  VAL B  84      25.856 -39.467 -59.618  1.00142.43           C  
ANISOU 3197  CA  VAL B  84     9875  24934  19310   3803    555   5061       C  
ATOM   3198  C   VAL B  84      25.094 -38.863 -60.795  1.00141.25           C  
ANISOU 3198  C   VAL B  84     9829  24873  18965   3670   1036   5413       C  
ATOM   3199  O   VAL B  84      25.099 -37.646 -60.987  1.00142.87           O  
ANISOU 3199  O   VAL B  84     9779  24951  19554   3291   1197   5669       O  
ATOM   3200  CB  VAL B  84      24.919 -39.690 -58.411  1.00122.03           C  
ANISOU 3200  CB  VAL B  84     7723  22064  16578   3745    101   4829       C  
ATOM   3201  CG1 VAL B  84      24.111 -38.447 -58.128  1.00120.74           C  
ANISOU 3201  CG1 VAL B  84     7553  21644  16680   3275    100   4999       C  
ATOM   3202  CG2 VAL B  84      24.010 -40.886 -58.649  1.00118.18           C  
ANISOU 3202  CG2 VAL B  84     7842  21650  15412   4107    109   4689       C  
ATOM   3203  N   LYS B  85      24.457 -39.717 -61.589  1.00138.83           N  
ANISOU 3203  N   LYS B  85     9922  24764  18064   3998   1245   5406       N  
ATOM   3204  CA  LYS B  85      23.773 -39.275 -62.800  1.00137.56           C  
ANISOU 3204  CA  LYS B  85     9903  24719  17644   3961   1679   5709       C  
ATOM   3205  C   LYS B  85      22.253 -39.425 -62.700  1.00130.66           C  
ANISOU 3205  C   LYS B  85     9559  23704  16380   3957   1623   5638       C  
ATOM   3206  O   LYS B  85      21.642 -40.162 -63.473  1.00128.84           O  
ANISOU 3206  O   LYS B  85     9695  23632  15624   4265   1796   5588       O  
ATOM   3207  CB  LYS B  85      24.309 -40.040 -64.017  1.00140.92           C  
ANISOU 3207  CB  LYS B  85    10329  25512  17702   4353   2005   5761       C  
ATOM   3208  CG  LYS B  85      24.390 -41.555 -63.824  1.00140.02           C  
ANISOU 3208  CG  LYS B  85    10509  25520  17173   4806   1805   5394       C  
ATOM   3209  CD  LYS B  85      24.926 -42.257 -65.064  1.00128.65           C  
ANISOU 3209  CD  LYS B  85     9056  24438  15387   5174   2113   5432       C  
ATOM   3210  CE  LYS B  85      24.560 -43.737 -65.067  1.00126.51           C  
ANISOU 3210  CE  LYS B  85     9243  24231  14594   5610   1948   5073       C  
ATOM   3211  NZ  LYS B  85      24.995 -44.440 -63.830  1.00126.04           N  
ANISOU 3211  NZ  LYS B  85     9200  24001  14686   5703   1503   4733       N  
ATOM   3212  N   LEU B  86      21.645 -38.719 -61.752  1.00127.03           N  
ANISOU 3212  N   LEU B  86     9135  22937  16194   3609   1366   5607       N  
ATOM   3213  CA  LEU B  86      20.196 -38.789 -61.577  1.00121.18           C  
ANISOU 3213  CA  LEU B  86     8858  22043  15142   3574   1295   5520       C  
ATOM   3214  C   LEU B  86      19.507 -37.445 -61.815  1.00119.45           C  
ANISOU 3214  C   LEU B  86     8568  21648  15172   3155   1447   5786       C  
ATOM   3215  O   LEU B  86      19.916 -36.417 -61.273  1.00120.72           O  
ANISOU 3215  O   LEU B  86     8400  21603  15865   2765   1330   5896       O  
ATOM   3216  CB  LEU B  86      19.839 -39.335 -60.193  1.00118.05           C  
ANISOU 3216  CB  LEU B  86     8784  21364  14708   3550    799   5154       C  
ATOM   3217  CG  LEU B  86      18.352 -39.535 -59.897  1.00112.55           C  
ANISOU 3217  CG  LEU B  86     8800  20326  13637   3419    690   4909       C  
ATOM   3218  CD1 LEU B  86      17.687 -40.334 -61.004  1.00111.04           C  
ANISOU 3218  CD1 LEU B  86     8941  20341  12909   3783    985   4886       C  
ATOM   3219  CD2 LEU B  86      18.161 -40.225 -58.554  1.00110.36           C  
ANISOU 3219  CD2 LEU B  86     8964  19718  13251   3391    232   4513       C  
ATOM   3220  N   THR B  87      18.456 -37.467 -62.629  1.00116.41           N  
ANISOU 3220  N   THR B  87     8515  21313  14401   3246   1684   5855       N  
ATOM   3221  CA  THR B  87      17.699 -36.264 -62.948  1.00114.68           C  
ANISOU 3221  CA  THR B  87     8306  20916  14353   2893   1822   6087       C  
ATOM   3222  C   THR B  87      16.438 -36.184 -62.103  1.00110.32           C  
ANISOU 3222  C   THR B  87     8231  19978  13708   2655   1524   5783       C  
ATOM   3223  O   THR B  87      15.495 -36.943 -62.314  1.00107.49           O  
ANISOU 3223  O   THR B  87     8408  19570  12863   2850   1519   5530       O  
ATOM   3224  CB  THR B  87      17.296 -36.238 -64.430  1.00114.25           C  
ANISOU 3224  CB  THR B  87     8457  21051  13904   3107   2216   6294       C  
ATOM   3225  OG1 THR B  87      18.465 -36.370 -65.248  1.00119.13           O  
ANISOU 3225  OG1 THR B  87     8815  21920  14530   3297   2445   6497       O  
ATOM   3226  CG2 THR B  87      16.591 -34.937 -64.766  1.00113.01           C  
ANISOU 3226  CG2 THR B  87     8323  20667  13947   2756   2317   6539       C  
ATOM   3227  N   ILE B  88      16.420 -35.267 -61.143  1.00110.67           N  
ANISOU 3227  N   ILE B  88     8145  19690  14213   2209   1257   5755       N  
ATOM   3228  CA  ILE B  88      15.245 -35.094 -60.300  1.00107.24           C  
ANISOU 3228  CA  ILE B  88     8215  18834  13698   1927    964   5428       C  
ATOM   3229  C   ILE B  88      14.280 -34.094 -60.922  1.00106.80           C  
ANISOU 3229  C   ILE B  88     8242  18651  13686   1689   1146   5605       C  
ATOM   3230  O   ILE B  88      14.660 -32.967 -61.239  1.00109.77           O  
ANISOU 3230  O   ILE B  88     8178  19036  14494   1453   1280   5958       O  
ATOM   3231  CB  ILE B  88      15.618 -34.640 -58.880  1.00107.68           C  
ANISOU 3231  CB  ILE B  88     8143  18585  14183   1592    540   5244       C  
ATOM   3232  CG1 ILE B  88      16.554 -35.656 -58.229  1.00109.22           C  
ANISOU 3232  CG1 ILE B  88     8297  18890  14311   1859    319   5048       C  
ATOM   3233  CG2 ILE B  88      14.371 -34.461 -58.033  1.00103.58           C  
ANISOU 3233  CG2 ILE B  88     8152  17658  13547   1311    272   4904       C  
ATOM   3234  CD1 ILE B  88      17.007 -35.260 -56.846  1.00109.88           C  
ANISOU 3234  CD1 ILE B  88     8252  18710  14787   1595   -121   4853       C  
ATOM   3235  N   MET B  89      13.033 -34.514 -61.098  1.00103.46           N  
ANISOU 3235  N   MET B  89     8380  18096  12836   1757   1145   5351       N  
ATOM   3236  CA  MET B  89      12.017 -33.650 -61.683  1.00102.56           C  
ANISOU 3236  CA  MET B  89     8402  17849  12717   1573   1280   5456       C  
ATOM   3237  C   MET B  89      10.795 -33.571 -60.767  1.00 98.19           C  
ANISOU 3237  C   MET B  89     8333  16872  12101   1294    978   5033       C  
ATOM   3238  O   MET B  89      10.314 -34.587 -60.269  1.00 95.38           O  
ANISOU 3238  O   MET B  89     8414  16422  11406   1428    834   4652       O  
ATOM   3239  CB  MET B  89      11.618 -34.164 -63.069  1.00103.06           C  
ANISOU 3239  CB  MET B  89     8637  18218  12305   1983   1635   5573       C  
ATOM   3240  CG  MET B  89      11.257 -33.071 -64.066  1.00104.62           C  
ANISOU 3240  CG  MET B  89     8684  18465  12601   1893   1902   5945       C  
ATOM   3241  SD  MET B  89      10.898 -33.719 -65.714  1.00202.66           S  
ANISOU 3241  SD  MET B  89    21295  31296  24409   2451   2306   6078       S  
ATOM   3242  CE  MET B  89      10.652 -32.205 -66.644  1.00113.07           C  
ANISOU 3242  CE  MET B  89     9856  19780  13325   2261   2413   6433       C  
ATOM   3243  N   THR B  90      10.305 -32.358 -60.538  1.00 97.88           N  
ANISOU 3243  N   THR B  90     8207  16574  12409    903    890   5101       N  
ATOM   3244  CA  THR B  90       9.140 -32.156 -59.684  1.00 94.40           C  
ANISOU 3244  CA  THR B  90     8179  15744  11946    616    619   4702       C  
ATOM   3245  C   THR B  90       8.015 -31.461 -60.436  1.00 93.51           C  
ANISOU 3245  C   THR B  90     8240  15521  11767    527    749   4735       C  
ATOM   3246  O   THR B  90       8.208 -30.387 -61.006  1.00 95.12           O  
ANISOU 3246  O   THR B  90     8118  15745  12280    387    874   5097       O  
ATOM   3247  CB  THR B  90       9.479 -31.312 -58.444  1.00 78.30           C  
ANISOU 3247  CB  THR B  90     5912  13425  10412    197    283   4630       C  
ATOM   3248  OG1 THR B  90       9.556 -29.927 -58.812  1.00 84.66           O  
ANISOU 3248  OG1 THR B  90     6340  14148  11680    -81    340   4949       O  
ATOM   3249  CG2 THR B  90      10.797 -31.752 -57.842  1.00 81.00           C  
ANISOU 3249  CG2 THR B  90     5947  13909  10922    294    158   4683       C  
ATOM   3250  N   GLY B  91       6.841 -32.083 -60.431  1.00 92.03           N  
ANISOU 3250  N   GLY B  91     8569  15205  11194    612    715   4350       N  
ATOM   3251  CA  GLY B  91       5.654 -31.487 -61.015  1.00 91.59           C  
ANISOU 3251  CA  GLY B  91     8725  15005  11069    532    774   4278       C  
ATOM   3252  C   GLY B  91       4.818 -30.822 -59.941  1.00 90.16           C  
ANISOU 3252  C   GLY B  91     8710  14412  11134     99    471   3946       C  
ATOM   3253  O   GLY B  91       5.211 -30.781 -58.776  1.00 89.52           O  
ANISOU 3253  O   GLY B  91     8566  14179  11270   -129    227   3807       O  
ATOM   3254  N   ASP B  92       3.661 -30.300 -60.328  1.00 89.82           N  
ANISOU 3254  N   ASP B  92     8880  14198  11049      6    473   3800       N  
ATOM   3255  CA  ASP B  92       2.800 -29.606 -59.382  1.00 89.17           C  
ANISOU 3255  CA  ASP B  92     8939  13736  11204   -398    198   3468       C  
ATOM   3256  C   ASP B  92       1.932 -30.583 -58.593  1.00 87.99           C  
ANISOU 3256  C   ASP B  92     9271  13416  10747   -404     80   2919       C  
ATOM   3257  O   ASP B  92       2.106 -31.799 -58.684  1.00 87.32           O  
ANISOU 3257  O   ASP B  92     9390  13480  10309   -115    184   2815       O  
ATOM   3258  CB  ASP B  92       1.923 -28.592 -60.116  1.00 88.57           C  
ANISOU 3258  CB  ASP B  92     8873  13534  11245   -496    232   3527       C  
ATOM   3259  CG  ASP B  92       2.731 -27.617 -60.941  1.00 92.23           C  
ANISOU 3259  CG  ASP B  92     8895  14142  12006   -493    384   4109       C  
ATOM   3260  OD1 ASP B  92       2.255 -27.210 -62.020  1.00 93.14           O  
ANISOU 3260  OD1 ASP B  92     9055  14320  12015   -343    548   4288       O  
ATOM   3261  OD2 ASP B  92       3.845 -27.258 -60.511  1.00 94.65           O  
ANISOU 3261  OD2 ASP B  92     8808  14494  12660   -633    342   4388       O  
ATOM   3262  N   ILE B  93       1.005 -30.041 -57.810  1.00 88.35           N  
ANISOU 3262  N   ILE B  93     9487  13140  10943   -738   -129   2570       N  
ATOM   3263  CA  ILE B  93       0.047 -30.854 -57.072  1.00 87.81           C  
ANISOU 3263  CA  ILE B  93     9876  12877  10609   -789   -205   2046       C  
ATOM   3264  C   ILE B  93      -1.376 -30.351 -57.300  1.00 86.97           C  
ANISOU 3264  C   ILE B  93     9988  12546  10512   -933   -234   1717       C  
ATOM   3265  O   ILE B  93      -1.637 -29.150 -57.234  1.00 87.00           O  
ANISOU 3265  O   ILE B  93     9806  12398  10852  -1194   -368   1765       O  
ATOM   3266  CB  ILE B  93       0.345 -30.865 -55.562  1.00 88.89           C  
ANISOU 3266  CB  ILE B  93    10049  12839  10886  -1065   -456   1851       C  
ATOM   3267  CG1 ILE B  93       0.575 -29.442 -55.051  1.00 90.80           C  
ANISOU 3267  CG1 ILE B  93     9949  12929  11623  -1425   -685   1962       C  
ATOM   3268  CG2 ILE B  93       1.557 -31.724 -55.269  1.00 90.92           C  
ANISOU 3268  CG2 ILE B  93    10224  13298  11023   -852   -440   2041       C  
ATOM   3269  CD1 ILE B  93       0.785 -29.354 -53.560  1.00 91.11           C  
ANISOU 3269  CD1 ILE B  93    10028  12796  11795  -1683   -965   1725       C  
ATOM   3270  N   LYS B  94      -2.289 -31.277 -57.581  1.00 86.09           N  
ANISOU 3270  N   LYS B  94    10254  12400  10056   -755   -120   1367       N  
ATOM   3271  CA  LYS B  94      -3.697 -30.945 -57.788  1.00 84.58           C  
ANISOU 3271  CA  LYS B  94    10283  11993   9862   -862   -149    979       C  
ATOM   3272  C   LYS B  94      -4.579 -32.021 -57.160  1.00 81.98           C  
ANISOU 3272  C   LYS B  94    10376  11493   9279   -878   -122    460       C  
ATOM   3273  O   LYS B  94      -4.337 -33.211 -57.347  1.00 82.50           O  
ANISOU 3273  O   LYS B  94    10617  11679   9050   -605     20    435       O  
ATOM   3274  CB  LYS B  94      -4.008 -30.817 -59.283  1.00 85.83           C  
ANISOU 3274  CB  LYS B  94    10408  12318   9887   -541     15   1134       C  
ATOM   3275  CG  LYS B  94      -3.207 -29.743 -60.013  1.00 88.86           C  
ANISOU 3275  CG  LYS B  94    10399  12861  10505   -516     42   1686       C  
ATOM   3276  CD  LYS B  94      -3.508 -29.740 -61.502  1.00 90.68           C  
ANISOU 3276  CD  LYS B  94    10656  13284  10513   -140    226   1847       C  
ATOM   3277  CE  LYS B  94      -2.741 -28.641 -62.222  1.00 94.62           C  
ANISOU 3277  CE  LYS B  94    10788  13922  11243   -130    288   2432       C  
ATOM   3278  NZ  LYS B  94      -3.175 -28.492 -63.641  1.00 96.56           N  
ANISOU 3278  NZ  LYS B  94    11106  14328  11255    226    445   2575       N  
ATOM   3279  N   GLY B  95      -5.593 -31.602 -56.409  1.00 79.43           N  
ANISOU 3279  N   GLY B  95    10208  10884   9088  -1200   -251     45       N  
ATOM   3280  CA  GLY B  95      -6.493 -32.540 -55.758  1.00 76.81           C  
ANISOU 3280  CA  GLY B  95    10265  10360   8558  -1265   -196   -449       C  
ATOM   3281  C   GLY B  95      -5.865 -33.269 -54.585  1.00 76.65           C  
ANISOU 3281  C   GLY B  95    10386  10310   8425  -1352   -224   -450       C  
ATOM   3282  O   GLY B  95      -5.093 -32.689 -53.826  1.00 77.98           O  
ANISOU 3282  O   GLY B  95    10367  10490   8770  -1535   -390   -251       O  
ATOM   3283  N   ILE B  96      -6.206 -34.547 -54.440  1.00 75.27           N  
ANISOU 3283  N   ILE B  96    10550  10084   7967  -1209    -75   -684       N  
ATOM   3284  CA  ILE B  96      -5.682 -35.379 -53.360  1.00 75.10           C  
ANISOU 3284  CA  ILE B  96    10736  10013   7785  -1249    -86   -692       C  
ATOM   3285  C   ILE B  96      -4.217 -35.731 -53.589  1.00 76.01           C  
ANISOU 3285  C   ILE B  96    10655  10397   7828   -982   -102   -229       C  
ATOM   3286  O   ILE B  96      -3.826 -36.108 -54.695  1.00 76.74           O  
ANISOU 3286  O   ILE B  96    10633  10707   7816   -645     23    -16       O  
ATOM   3287  CB  ILE B  96      -6.486 -36.687 -53.221  1.00 74.62           C  
ANISOU 3287  CB  ILE B  96    11101   9789   7464  -1160    100  -1054       C  
ATOM   3288  CG1 ILE B  96      -7.963 -36.381 -52.973  1.00 73.42           C  
ANISOU 3288  CG1 ILE B  96    11121   9366   7410  -1433    137  -1551       C  
ATOM   3289  CG2 ILE B  96      -5.925 -37.552 -52.104  1.00 75.44           C  
ANISOU 3289  CG2 ILE B  96    11457   9825   7381  -1185     88  -1023       C  
ATOM   3290  CD1 ILE B  96      -8.823 -37.613 -52.820  1.00 73.20           C  
ANISOU 3290  CD1 ILE B  96    11185   9160   7469  -1190    286  -1684       C  
ATOM   3291  N   MET B  97      -3.414 -35.602 -52.538  1.00 75.93           N  
ANISOU 3291  N   MET B  97    10599  10381   7870  -1119   -265    -97       N  
ATOM   3292  CA  MET B  97      -2.008 -35.972 -52.599  1.00 76.77           C  
ANISOU 3292  CA  MET B  97    10516  10722   7930   -879   -307    290       C  
ATOM   3293  C   MET B  97      -1.865 -37.452 -52.274  1.00 76.05           C  
ANISOU 3293  C   MET B  97    10793  10603   7501   -655   -211    194       C  
ATOM   3294  O   MET B  97      -1.684 -37.825 -51.116  1.00 76.53           O  
ANISOU 3294  O   MET B  97    11080  10533   7466   -767   -318    100       O  
ATOM   3295  CB  MET B  97      -1.194 -35.121 -51.627  1.00 78.13           C  
ANISOU 3295  CB  MET B  97    10446  10892   8349  -1106   -567    445       C  
ATOM   3296  CG  MET B  97      -1.454 -33.625 -51.773  1.00 77.81           C  
ANISOU 3296  CG  MET B  97    10075  10802   8687  -1382   -691    486       C  
ATOM   3297  SD  MET B  97      -0.394 -32.602 -50.736  1.00118.97           S  
ANISOU 3297  SD  MET B  97    14930  16017  14258  -1614  -1022    667       S  
ATOM   3298  CE  MET B  97      -1.160 -31.000 -50.952  1.00 79.02           C  
ANISOU 3298  CE  MET B  97     9611  10802   9613  -1954  -1136    583       C  
ATOM   3299  N   GLN B  98      -1.956 -38.286 -53.307  1.00 74.80           N  
ANISOU 3299  N   GLN B  98    10702  10562   7158   -323    -19    215       N  
ATOM   3300  CA  GLN B  98      -1.933 -39.737 -53.149  1.00 73.80           C  
ANISOU 3300  CA  GLN B  98    10929  10376   6734    -88     83     97       C  
ATOM   3301  C   GLN B  98      -0.701 -40.224 -52.410  1.00 75.63           C  
ANISOU 3301  C   GLN B  98    11157  10697   6882     29    -55    329       C  
ATOM   3302  O   GLN B  98       0.417 -39.809 -52.701  1.00 77.21           O  
ANISOU 3302  O   GLN B  98    10984  11151   7202    157   -145    668       O  
ATOM   3303  CB  GLN B  98      -2.025 -40.430 -54.507  1.00 73.00           C  
ANISOU 3303  CB  GLN B  98    10801  10445   6489    302    270    121       C  
ATOM   3304  CG  GLN B  98      -3.420 -40.419 -55.105  1.00 70.35           C  
ANISOU 3304  CG  GLN B  98    10625   9949   6153    252    406   -240       C  
ATOM   3305  CD  GLN B  98      -4.399 -41.219 -54.284  1.00 68.73           C  
ANISOU 3305  CD  GLN B  98    10869   9395   5849     79    472   -653       C  
ATOM   3306  OE1 GLN B  98      -4.052 -42.261 -53.730  1.00 69.48           O  
ANISOU 3306  OE1 GLN B  98    11223   9406   5770    184    493   -658       O  
ATOM   3307  NE2 GLN B  98      -5.629 -40.735 -54.193  1.00 67.07           N  
ANISOU 3307  NE2 GLN B  98    10755   8971   5760   -187    513   -999       N  
ATOM   3308  N   ALA B  99      -0.923 -41.105 -51.445  1.00 75.57           N  
ANISOU 3308  N   ALA B  99    11568  10469   6675    -13    -68    141       N  
ATOM   3309  CA  ALA B  99       0.156 -41.644 -50.647  1.00 77.24           C  
ANISOU 3309  CA  ALA B  99    11851  10726   6772    116   -226    317       C  
ATOM   3310  C   ALA B  99       1.024 -42.546 -51.500  1.00 78.14           C  
ANISOU 3310  C   ALA B  99    11861  11071   6757    563   -165    526       C  
ATOM   3311  O   ALA B  99       0.582 -43.059 -52.523  1.00 77.13           O  
ANISOU 3311  O   ALA B  99    11762  10995   6548    773     23    453       O  
ATOM   3312  CB  ALA B  99      -0.403 -42.415 -49.475  1.00 77.76           C  
ANISOU 3312  CB  ALA B  99    12448  10480   6619    -18   -222     71       C  
ATOM   3313  N   GLY B 100       2.264 -42.730 -51.070  1.00 79.91           N  
ANISOU 3313  N   GLY B 100    11953  11439   6969    723   -343    760       N  
ATOM   3314  CA  GLY B 100       3.162 -43.674 -51.699  1.00 81.90           C  
ANISOU 3314  CA  GLY B 100    12131  11901   7086   1157   -316    932       C  
ATOM   3315  C   GLY B 100       3.404 -44.832 -50.755  1.00 83.45           C  
ANISOU 3315  C   GLY B 100    12768  11904   7033   1283   -416    846       C  
ATOM   3316  O   GLY B 100       3.566 -44.636 -49.551  1.00 84.44           O  
ANISOU 3316  O   GLY B 100    13063  11879   7139   1095   -602    818       O  
ATOM   3317  N   LYS B 101       3.425 -46.042 -51.299  1.00 84.14           N  
ANISOU 3317  N   LYS B 101    13056  11990   6924   1619   -303    800       N  
ATOM   3318  CA  LYS B 101       3.563 -47.238 -50.479  1.00 85.11           C  
ANISOU 3318  CA  LYS B 101    13648  11885   6806   1757   -379    720       C  
ATOM   3319  C   LYS B 101       4.960 -47.374 -49.887  1.00 88.31           C  
ANISOU 3319  C   LYS B 101    13920  12441   7191   1958   -652    943       C  
ATOM   3320  O   LYS B 101       5.136 -48.006 -48.845  1.00 89.51           O  
ANISOU 3320  O   LYS B 101    14462  12383   7164   1981   -796    904       O  
ATOM   3321  CB  LYS B 101       3.207 -48.484 -51.286  1.00 84.37           C  
ANISOU 3321  CB  LYS B 101    13773  11730   6554   2075   -202    595       C  
ATOM   3322  CG  LYS B 101       1.776 -48.500 -51.800  1.00 81.21           C  
ANISOU 3322  CG  LYS B 101    13544  11134   6178   1902     46    311       C  
ATOM   3323  CD  LYS B 101       0.772 -48.464 -50.663  1.00 79.66           C  
ANISOU 3323  CD  LYS B 101    13785  10540   5941   1505     89     91       C  
ATOM   3324  CE  LYS B 101      -0.642 -48.672 -51.180  1.00 77.58           C  
ANISOU 3324  CE  LYS B 101    13649  10051   5778   1353    334   -233       C  
ATOM   3325  NZ  LYS B 101      -1.619 -48.847 -50.074  1.00 77.11           N  
ANISOU 3325  NZ  LYS B 101    13884   9588   5825    965    407   -438       N  
ATOM   3326  N   ARG B 102       5.950 -46.781 -50.546  1.00 90.03           N  
ANISOU 3326  N   ARG B 102    13590  13021   7597   2110   -719   1175       N  
ATOM   3327  CA  ARG B 102       7.320 -46.834 -50.047  1.00 93.76           C  
ANISOU 3327  CA  ARG B 102    13855  13659   8112   2304   -989   1361       C  
ATOM   3328  C   ARG B 102       7.683 -45.575 -49.277  1.00 93.61           C  
ANISOU 3328  C   ARG B 102    13560  13672   8335   1996  -1197   1438       C  
ATOM   3329  O   ARG B 102       6.841 -44.698 -49.076  1.00 91.81           O  
ANISOU 3329  O   ARG B 102    13341  13321   8221   1628  -1135   1344       O  
ATOM   3330  CB  ARG B 102       8.319 -47.070 -51.179  1.00 96.65           C  
ANISOU 3330  CB  ARG B 102    13765  14405   8551   2692   -939   1557       C  
ATOM   3331  CG  ARG B 102       8.294 -48.483 -51.734  1.00 98.31           C  
ANISOU 3331  CG  ARG B 102    14246  14596   8511   3091   -842   1471       C  
ATOM   3332  CD  ARG B 102       9.623 -48.860 -52.363  1.00102.06           C  
ANISOU 3332  CD  ARG B 102    14322  15431   9025   3517   -916   1653       C  
ATOM   3333  NE  ARG B 102       9.601 -50.220 -52.893  1.00103.85           N  
ANISOU 3333  NE  ARG B 102    14802  15634   9021   3918   -848   1544       N  
ATOM   3334  CZ  ARG B 102      10.652 -50.834 -53.424  1.00107.42           C  
ANISOU 3334  CZ  ARG B 102    15006  16361   9448   4348   -912   1636       C  
ATOM   3335  NH1 ARG B 102      11.819 -50.212 -53.494  1.00109.89           N  
ANISOU 3335  NH1 ARG B 102    14796  16996   9962   4422  -1025   1845       N  
ATOM   3336  NH2 ARG B 102      10.537 -52.073 -53.882  1.00108.54           N  
ANISOU 3336  NH2 ARG B 102    15403  16448   9391   4705   -865   1501       N  
ATOM   3337  N   SER B 103       8.937 -45.492 -48.845  1.00 95.77           N  
ANISOU 3337  N   SER B 103    13575  14106   8709   2159  -1463   1582       N  
ATOM   3338  CA  SER B 103       9.370 -44.396 -47.988  1.00 96.12           C  
ANISOU 3338  CA  SER B 103    13371  14153   8996   1904  -1720   1617       C  
ATOM   3339  C   SER B 103      10.875 -44.157 -48.053  1.00 98.19           C  
ANISOU 3339  C   SER B 103    13108  14700   9500   2128  -1945   1809       C  
ATOM   3340  O   SER B 103      11.611 -44.924 -48.670  1.00 99.91           O  
ANISOU 3340  O   SER B 103    13195  15110   9654   2498  -1911   1909       O  
ATOM   3341  CB  SER B 103       8.956 -44.673 -46.543  1.00 97.08           C  
ANISOU 3341  CB  SER B 103    14044  13957   8884   1762  -1919   1425       C  
ATOM   3342  OG  SER B 103       9.429 -45.937 -46.116  1.00 99.59           O  
ANISOU 3342  OG  SER B 103    14740  14195   8903   2103  -2038   1410       O  
ATOM   3343  N   LEU B 104      11.323 -43.084 -47.407  1.00 97.83           N  
ANISOU 3343  N   LEU B 104    12744  14674   9754   1904  -2181   1834       N  
ATOM   3344  CA  LEU B 104      12.740 -42.747 -47.355  1.00 99.94           C  
ANISOU 3344  CA  LEU B 104    12470  15180  10323   2072  -2420   1979       C  
ATOM   3345  C   LEU B 104      13.357 -43.186 -46.033  1.00101.56           C  
ANISOU 3345  C   LEU B 104    12939  15257  10390   2215  -2829   1844       C  
ATOM   3346  O   LEU B 104      12.657 -43.341 -45.035  1.00100.46           O  
ANISOU 3346  O   LEU B 104    13329  14846   9996   2073  -2941   1663       O  
ATOM   3347  CB  LEU B 104      12.933 -41.243 -47.537  1.00 99.51           C  
ANISOU 3347  CB  LEU B 104    11827  15223  10760   1751  -2443   2092       C  
ATOM   3348  CG  LEU B 104      12.246 -40.627 -48.753  1.00 96.42           C  
ANISOU 3348  CG  LEU B 104    11201  14925  10507   1575  -2066   2235       C  
ATOM   3349  CD1 LEU B 104      12.505 -39.133 -48.819  1.00 96.69           C  
ANISOU 3349  CD1 LEU B 104    10671  15011  11055   1255  -2126   2362       C  
ATOM   3350  CD2 LEU B 104      12.725 -41.308 -50.018  1.00 97.08           C  
ANISOU 3350  CD2 LEU B 104    11076  15297  10513   1926  -1798   2425       C  
ATOM   3351  N   ARG B 105      14.671 -43.380 -46.035  1.00104.49           N  
ANISOU 3351  N   ARG B 105    12939  15834  10927   2509  -3048   1927       N  
ATOM   3352  CA  ARG B 105      15.395 -43.798 -44.840  1.00107.16           C  
ANISOU 3352  CA  ARG B 105    13484  16082  11151   2709  -3480   1797       C  
ATOM   3353  C   ARG B 105      16.810 -43.229 -44.857  1.00110.50           C  
ANISOU 3353  C   ARG B 105    13207  16753  12026   2839  -3746   1871       C  
ATOM   3354  O   ARG B 105      17.483 -43.263 -45.885  1.00111.67           O  
ANISOU 3354  O   ARG B 105    12855  17176  12399   3001  -3572   2043       O  
ATOM   3355  CB  ARG B 105      15.424 -45.327 -44.730  1.00107.85           C  
ANISOU 3355  CB  ARG B 105    14125  16078  10776   3096  -3490   1747       C  
ATOM   3356  CG  ARG B 105      15.732 -46.047 -46.038  1.00107.89           C  
ANISOU 3356  CG  ARG B 105    13915  16311  10766   3389  -3211   1885       C  
ATOM   3357  CD  ARG B 105      15.552 -47.561 -45.919  1.00108.22           C  
ANISOU 3357  CD  ARG B 105    14567  16196  10355   3733  -3209   1808       C  
ATOM   3358  NE  ARG B 105      16.634 -48.199 -45.171  1.00111.85           N  
ANISOU 3358  NE  ARG B 105    15099  16663  10737   4096  -3614   1755       N  
ATOM   3359  CZ  ARG B 105      16.735 -49.509 -44.961  1.00112.79           C  
ANISOU 3359  CZ  ARG B 105    15706  16643  10506   4449  -3702   1700       C  
ATOM   3360  NH1 ARG B 105      15.818 -50.337 -45.441  1.00110.40           N  
ANISOU 3360  NH1 ARG B 105    15848  16177   9921   4475  -3404   1684       N  
ATOM   3361  NH2 ARG B 105      17.755 -49.994 -44.268  1.00116.52           N  
ANISOU 3361  NH2 ARG B 105    16199  17100  10972   4731  -4064   1633       N  
ATOM   3362  N   PRO B 106      17.260 -42.689 -43.714  1.00112.57           N  
ANISOU 3362  N   PRO B 106    13415  16923  12433   2773  -4165   1727       N  
ATOM   3363  CA  PRO B 106      18.595 -42.089 -43.597  1.00116.35           C  
ANISOU 3363  CA  PRO B 106    13208  17599  13400   2876  -4466   1743       C  
ATOM   3364  C   PRO B 106      19.707 -43.135 -43.584  1.00119.88           C  
ANISOU 3364  C   PRO B 106    13618  18189  13741   3374  -4673   1725       C  
ATOM   3365  O   PRO B 106      19.563 -44.159 -42.915  1.00104.17           O  
ANISOU 3365  O   PRO B 106    12256  16039  11286   3627  -4844   1604       O  
ATOM   3366  CB  PRO B 106      18.533 -41.369 -42.248  1.00117.38           C  
ANISOU 3366  CB  PRO B 106    13458  17535  13607   2691  -4885   1522       C  
ATOM   3367  CG  PRO B 106      17.514 -42.121 -41.469  1.00115.36           C  
ANISOU 3367  CG  PRO B 106    14083  17009  12741   2698  -4886   1383       C  
ATOM   3368  CD  PRO B 106      16.486 -42.563 -42.466  1.00111.40           C  
ANISOU 3368  CD  PRO B 106    13839  16481  12008   2588  -4369   1520       C  
ATOM   3369  N   GLN B 131      18.319 -42.449 -66.494  1.00124.08           N  
ANISOU 3369  N   GLN B 131    10722  23356  13066   5283   2314   5239       N  
ATOM   3370  CA  GLN B 131      17.201 -42.590 -65.568  1.00119.22           C  
ANISOU 3370  CA  GLN B 131    10433  22445  12421   5176   2077   4986       C  
ATOM   3371  C   GLN B 131      16.937 -41.289 -64.814  1.00118.68           C  
ANISOU 3371  C   GLN B 131    10123  22155  12814   4698   2005   5191       C  
ATOM   3372  O   GLN B 131      17.867 -40.644 -64.330  1.00121.50           O  
ANISOU 3372  O   GLN B 131    10050  22498  13617   4454   1947   5371       O  
ATOM   3373  CB  GLN B 131      17.453 -43.738 -64.583  1.00117.42           C  
ANISOU 3373  CB  GLN B 131    10378  22099  12137   5368   1743   4623       C  
ATOM   3374  CG  GLN B 131      17.437 -45.126 -65.216  1.00117.29           C  
ANISOU 3374  CG  GLN B 131    10703  22208  11653   5818   1766   4336       C  
ATOM   3375  CD  GLN B 131      17.464 -46.242 -64.187  1.00115.24           C  
ANISOU 3375  CD  GLN B 131    10734  21722  11332   5972   1408   3966       C  
ATOM   3376  OE1 GLN B 131      17.728 -46.009 -63.008  1.00114.34           O  
ANISOU 3376  OE1 GLN B 131    10539  21398  11509   5774   1117   3948       O  
ATOM   3377  NE2 GLN B 131      17.185 -47.463 -64.630  1.00114.80           N  
ANISOU 3377  NE2 GLN B 131    11054  21674  10891   6316   1397   3665       N  
ATOM   3378  N   THR B 132      15.667 -40.907 -64.717  1.00115.29           N  
ANISOU 3378  N   THR B 132     9994  21516  12296   4541   1984   5122       N  
ATOM   3379  CA  THR B 132      15.292 -39.681 -64.021  1.00114.17           C  
ANISOU 3379  CA  THR B 132     9795  21031  12552   3992   1858   5227       C  
ATOM   3380  C   THR B 132      14.446 -39.964 -62.779  1.00110.26           C  
ANISOU 3380  C   THR B 132     9807  20052  12036   3732   1467   4819       C  
ATOM   3381  O   THR B 132      13.996 -41.090 -62.569  1.00108.14           O  
ANISOU 3381  O   THR B 132     9979  19691  11419   3966   1337   4478       O  
ATOM   3382  CB  THR B 132      14.539 -38.712 -64.951  1.00113.93           C  
ANISOU 3382  CB  THR B 132     9763  21037  12489   3868   2145   5488       C  
ATOM   3383  OG1 THR B 132      14.208 -37.516 -64.234  1.00112.72           O  
ANISOU 3383  OG1 THR B 132     9538  20532  12760   3335   1992   5572       O  
ATOM   3384  CG2 THR B 132      13.265 -39.352 -65.469  1.00110.61           C  
ANISOU 3384  CG2 THR B 132     9909  20546  11573   4090   2172   5198       C  
ATOM   3385  N   PHE B 133      14.234 -38.935 -61.963  1.00109.31           N  
ANISOU 3385  N   PHE B 133     9616  19621  12297   3250   1289   4857       N  
ATOM   3386  CA  PHE B 133      13.480 -39.073 -60.721  1.00105.80           C  
ANISOU 3386  CA  PHE B 133     9613  18731  11854   2973    934   4495       C  
ATOM   3387  C   PHE B 133      12.328 -38.080 -60.689  1.00102.39           C  
ANISOU 3387  C   PHE B 133     9365  18020  11519   2593    943   4480       C  
ATOM   3388  O   PHE B 133      12.517 -36.893 -60.950  1.00103.80           O  
ANISOU 3388  O   PHE B 133     9176  18218  12047   2340   1044   4781       O  
ATOM   3389  CB  PHE B 133      14.399 -38.842 -59.520  1.00108.06           C  
ANISOU 3389  CB  PHE B 133     9647  18889  12520   2770    618   4468       C  
ATOM   3390  CG  PHE B 133      13.872 -39.409 -58.231  1.00105.81           C  
ANISOU 3390  CG  PHE B 133     9861  18235  12106   2649    254   4073       C  
ATOM   3391  CD1 PHE B 133      13.581 -40.760 -58.125  1.00104.79           C  
ANISOU 3391  CD1 PHE B 133    10193  18074  11548   2966    196   3797       C  
ATOM   3392  CD2 PHE B 133      13.694 -38.600 -57.119  1.00104.80           C  
ANISOU 3392  CD2 PHE B 133     9739  17791  12288   2231    -26   3982       C  
ATOM   3393  CE1 PHE B 133      13.106 -41.291 -56.942  1.00102.72           C  
ANISOU 3393  CE1 PHE B 133    10409  17465  11156   2854   -104   3472       C  
ATOM   3394  CE2 PHE B 133      13.222 -39.128 -55.931  1.00102.71           C  
ANISOU 3394  CE2 PHE B 133     9951  17210  11864   2139   -334   3635       C  
ATOM   3395  CZ  PHE B 133      12.926 -40.474 -55.844  1.00101.67           C  
ANISOU 3395  CZ  PHE B 133    10294  17044  11292   2445   -358   3398       C  
ATOM   3396  N   LEU B 134      11.137 -38.568 -60.361  1.00 98.24           N  
ANISOU 3396  N   LEU B 134     9399  17221  10707   2551    836   4123       N  
ATOM   3397  CA  LEU B 134       9.933 -37.742 -60.404  1.00 95.06           C  
ANISOU 3397  CA  LEU B 134     9205  16561  10352   2239    847   4047       C  
ATOM   3398  C   LEU B 134       9.373 -37.462 -59.008  1.00 91.74           C  
ANISOU 3398  C   LEU B 134     9048  15717  10093   1836    519   3752       C  
ATOM   3399  O   LEU B 134       9.240 -38.370 -58.195  1.00 90.48           O  
ANISOU 3399  O   LEU B 134     9237  15398   9742   1894    336   3455       O  
ATOM   3400  CB  LEU B 134       8.856 -38.402 -61.278  1.00 93.16           C  
ANISOU 3400  CB  LEU B 134     9371  16351   9676   2504   1022   3847       C  
ATOM   3401  CG  LEU B 134       8.991 -38.420 -62.808  1.00 95.17           C  
ANISOU 3401  CG  LEU B 134     9445  16993   9720   2874   1364   4107       C  
ATOM   3402  CD1 LEU B 134      10.069 -39.377 -63.297  1.00 98.19           C  
ANISOU 3402  CD1 LEU B 134     9633  17756   9919   3327   1486   4217       C  
ATOM   3403  CD2 LEU B 134       7.657 -38.769 -63.443  1.00 92.68           C  
ANISOU 3403  CD2 LEU B 134     9565  16587   9064   3017   1443   3829       C  
ATOM   3404  N   ILE B 135       9.049 -36.202 -58.733  1.00 90.28           N  
ANISOU 3404  N   ILE B 135     8702  15347  10252   1439    448   3840       N  
ATOM   3405  CA  ILE B 135       8.409 -35.840 -57.473  1.00 86.83           C  
ANISOU 3405  CA  ILE B 135     8515  14525   9952   1059    152   3542       C  
ATOM   3406  C   ILE B 135       7.033 -35.249 -57.744  1.00 83.30           C  
ANISOU 3406  C   ILE B 135     8324  13861   9464    844    207   3385       C  
ATOM   3407  O   ILE B 135       6.903 -34.323 -58.544  1.00 84.06           O  
ANISOU 3407  O   ILE B 135     8173  14029   9738    768    355   3636       O  
ATOM   3408  CB  ILE B 135       9.227 -34.804 -56.691  1.00 88.76           C  
ANISOU 3408  CB  ILE B 135     8328  14690  10706    744    -67   3702       C  
ATOM   3409  CG1 ILE B 135      10.709 -35.172 -56.690  1.00 92.70           C  
ANISOU 3409  CG1 ILE B 135     8425  15459  11337    971    -79   3924       C  
ATOM   3410  CG2 ILE B 135       8.695 -34.670 -55.274  1.00 86.37           C  
ANISOU 3410  CG2 ILE B 135     8321  14033  10463    436   -402   3346       C  
ATOM   3411  CD1 ILE B 135      11.005 -36.482 -56.025  1.00 92.51           C  
ANISOU 3411  CD1 ILE B 135     8716  15437  10998   1227   -236   3670       C  
ATOM   3412  N   ASP B 136       6.016 -35.783 -57.073  1.00 77.14           N  
ANISOU 3412  N   ASP B 136     8642  13022   7645   2452    776   -631       N  
ATOM   3413  CA  ASP B 136       4.642 -35.328 -57.259  1.00 76.44           C  
ANISOU 3413  CA  ASP B 136     8534  12868   7641   2316    593   -526       C  
ATOM   3414  C   ASP B 136       4.227 -35.375 -58.723  1.00 80.69           C  
ANISOU 3414  C   ASP B 136     9101  13836   7720   2450    466   -508       C  
ATOM   3415  O   ASP B 136       4.406 -36.389 -59.396  1.00 83.14           O  
ANISOU 3415  O   ASP B 136     9571  14338   7680   2597    387   -845       O  
ATOM   3416  CB  ASP B 136       4.460 -33.911 -56.710  1.00 74.12           C  
ANISOU 3416  CB  ASP B 136     8058  12416   7689   2165    702   -123       C  
ATOM   3417  CG  ASP B 136       4.326 -33.882 -55.207  1.00 70.20           C  
ANISOU 3417  CG  ASP B 136     7565  11477   7629   1984    741   -213       C  
ATOM   3418  OD1 ASP B 136       3.639 -34.764 -54.656  1.00 69.15           O  
ANISOU 3418  OD1 ASP B 136     7548  11135   7593   1908    608   -494       O  
ATOM   3419  OD2 ASP B 136       4.903 -32.971 -54.579  1.00 68.68           O  
ANISOU 3419  OD2 ASP B 136     7272  11155   7669   1894    905     -1       O  
ATOM   3420  N   GLY B 137       3.683 -34.266 -59.209  1.00 82.36           N  
ANISOU 3420  N   GLY B 137     9175  14191   7928   2414    435   -118       N  
ATOM   3421  CA  GLY B 137       3.223 -34.184 -60.579  1.00 87.27           C  
ANISOU 3421  CA  GLY B 137     9819  15259   8081   2533    277    -25       C  
ATOM   3422  C   GLY B 137       2.031 -35.081 -60.834  1.00 89.19           C  
ANISOU 3422  C   GLY B 137    10154  15494   8242   2490    -74   -390       C  
ATOM   3423  O   GLY B 137       1.434 -35.614 -59.899  1.00 71.16           O  
ANISOU 3423  O   GLY B 137     7883  12821   6334   2333   -171   -635       O  
ATOM   3424  N   PRO B 138       1.684 -35.260 -62.114  1.00 94.08           N  
ANISOU 3424  N   PRO B 138    10835  16567   8343   2603   -269   -424       N  
ATOM   3425  CA  PRO B 138       0.530 -36.073 -62.496  1.00 96.48           C  
ANISOU 3425  CA  PRO B 138    11202  16923   8534   2529   -656   -780       C  
ATOM   3426  C   PRO B 138       0.776 -37.546 -62.229  1.00 96.15           C  
ANISOU 3426  C   PRO B 138    11398  16672   8461   2506   -702  -1386       C  
ATOM   3427  O   PRO B 138       1.924 -37.961 -62.079  1.00 95.61           O  
ANISOU 3427  O   PRO B 138    11460  16565   8301   2645   -449  -1530       O  
ATOM   3428  CB  PRO B 138       0.432 -35.838 -64.003  1.00 85.74           C  
ANISOU 3428  CB  PRO B 138     9886  16182   6511   2688   -813   -650       C  
ATOM   3429  CG  PRO B 138       1.821 -35.531 -64.421  1.00 86.56           C  
ANISOU 3429  CG  PRO B 138    10057  16555   6275   2870   -441   -467       C  
ATOM   3430  CD  PRO B 138       2.405 -34.741 -63.289  1.00 98.18           C  
ANISOU 3430  CD  PRO B 138    11373  17619   8311   2785   -133   -139       C  
ATOM   3431  N   GLU B 139      -0.298 -38.322 -62.164  1.00 97.03           N  
ANISOU 3431  N   GLU B 139    11549  16633   8685   2330  -1030  -1726       N  
ATOM   3432  CA  GLU B 139      -0.176 -39.766 -62.052  1.00 97.73           C  
ANISOU 3432  CA  GLU B 139    11911  16483   8740   2289  -1128  -2308       C  
ATOM   3433  C   GLU B 139       0.381 -40.312 -63.356  1.00102.39           C  
ANISOU 3433  C   GLU B 139    12730  17516   8658   2528  -1179  -2618       C  
ATOM   3434  O   GLU B 139      -0.056 -39.925 -64.437  1.00105.76           O  
ANISOU 3434  O   GLU B 139    13114  18438   8631   2581  -1373  -2527       O  
ATOM   3435  CB  GLU B 139      -1.534 -40.396 -61.758  1.00 98.68           C  
ANISOU 3435  CB  GLU B 139    11990  16359   9147   1980  -1481  -2564       C  
ATOM   3436  CG  GLU B 139      -2.201 -39.847 -60.514  1.00 94.71           C  
ANISOU 3436  CG  GLU B 139    11230  15493   9261   1749  -1405  -2277       C  
ATOM   3437  CD  GLU B 139      -1.385 -40.100 -59.267  1.00 90.67           C  
ANISOU 3437  CD  GLU B 139    10834  14518   9099   1732  -1091  -2273       C  
ATOM   3438  OE1 GLU B 139      -0.752 -41.173 -59.186  1.00 91.35           O  
ANISOU 3438  OE1 GLU B 139    11209  14391   9109   1786  -1068  -2627       O  
ATOM   3439  OE2 GLU B 139      -1.374 -39.228 -58.372  1.00 87.12           O  
ANISOU 3439  OE2 GLU B 139    10196  13914   8992   1680   -885  -1926       O  
ATOM   3440  N   THR B 140       1.358 -41.203 -63.256  1.00102.90           N  
ANISOU 3440  N   THR B 140    13038  17422   8638   2699  -1002  -2982       N  
ATOM   3441  CA  THR B 140       1.959 -41.778 -64.449  1.00108.35           C  
ANISOU 3441  CA  THR B 140    13957  18528   8683   2971   -992  -3350       C  
ATOM   3442  C   THR B 140       2.075 -43.289 -64.330  1.00111.10           C  
ANISOU 3442  C   THR B 140    14643  18477   9093   3005  -1110  -4030       C  
ATOM   3443  O   THR B 140       1.950 -43.845 -63.240  1.00107.80           O  
ANISOU 3443  O   THR B 140    14282  17452   9225   2849  -1126  -4124       O  
ATOM   3444  CB  THR B 140       3.346 -41.184 -64.724  1.00107.45           C  
ANISOU 3444  CB  THR B 140    13768  18763   8296   3279   -553  -3078       C  
ATOM   3445  OG1 THR B 140       3.892 -41.775 -65.911  1.00112.87           O  
ANISOU 3445  OG1 THR B 140    14669  19908   8310   3561   -506  -3474       O  
ATOM   3446  CG2 THR B 140       4.275 -41.449 -63.553  1.00103.16           C  
ANISOU 3446  CG2 THR B 140    13202  17755   8240   3345   -271  -3070       C  
ATOM   3447  N   ALA B 141       2.312 -43.947 -65.457  1.00117.97           N  
ANISOU 3447  N   ALA B 141    15761  19681   9381   3213  -1190  -4502       N  
ATOM   3448  CA  ALA B 141       2.432 -45.396 -65.474  1.00122.17           C  
ANISOU 3448  CA  ALA B 141    16628  19714  10075   3218  -1292  -5094       C  
ATOM   3449  C   ALA B 141       3.885 -45.825 -65.308  1.00122.88           C  
ANISOU 3449  C   ALA B 141    16791  19628  10268   3552   -889  -5129       C  
ATOM   3450  O   ALA B 141       4.165 -46.953 -64.906  1.00124.39           O  
ANISOU 3450  O   ALA B 141    17225  19262  10775   3596   -909  -5492       O  
ATOM   3451  CB  ALA B 141       1.853 -45.958 -66.756  1.00129.62           C  
ANISOU 3451  CB  ALA B 141    17760  20883  10605   3129  -1573  -5452       C  
ATOM   3452  N   GLU B 142       4.805 -44.920 -65.625  1.00122.22           N  
ANISOU 3452  N   GLU B 142    16475  20020   9943   3771   -539  -4722       N  
ATOM   3453  CA  GLU B 142       6.228 -45.202 -65.483  1.00122.96           C  
ANISOU 3453  CA  GLU B 142    16531  20040  10149   4072   -165  -4701       C  
ATOM   3454  C   GLU B 142       6.609 -45.265 -64.012  1.00117.59           C  
ANISOU 3454  C   GLU B 142    15775  18858  10047   4076    -69  -4563       C  
ATOM   3455  O   GLU B 142       7.500 -46.021 -63.621  1.00118.77           O  
ANISOU 3455  O   GLU B 142    15997  18675  10456   4279     68  -4717       O  
ATOM   3456  CB  GLU B 142       7.064 -44.140 -66.199  1.00123.83           C  
ANISOU 3456  CB  GLU B 142    16364  20805   9879   4224    172  -4258       C  
ATOM   3457  CG  GLU B 142       6.814 -42.719 -65.731  1.00118.42           C  
ANISOU 3457  CG  GLU B 142    15379  20385   9229   4081    252  -3658       C  
ATOM   3458  CD  GLU B 142       7.395 -41.677 -66.664  1.00120.69           C  
ANISOU 3458  CD  GLU B 142    15451  21320   9086   4152    517  -3204       C  
ATOM   3459  OE1 GLU B 142       8.522 -41.881 -67.155  1.00124.28           O  
ANISOU 3459  OE1 GLU B 142    15849  21956   9414   4350    808  -3231       O  
ATOM   3460  OE2 GLU B 142       6.722 -40.653 -66.905  1.00119.42           O  
ANISOU 3460  OE2 GLU B 142    15172  21481   8722   4007    432  -2798       O  
ATOM   3461  N   CYS B 143       5.919 -44.468 -63.203  1.00112.13           N  
ANISOU 3461  N   CYS B 143    14935  18129   9542   3863   -151  -4271       N  
ATOM   3462  CA  CYS B 143       6.191 -44.385 -61.778  1.00106.64           C  
ANISOU 3462  CA  CYS B 143    14149  16973   9395   3799    -62  -4063       C  
ATOM   3463  C   CYS B 143       4.884 -44.400 -61.001  1.00103.42           C  
ANISOU 3463  C   CYS B 143    13769  16118   9410   3356   -358  -3962       C  
ATOM   3464  O   CYS B 143       4.358 -43.351 -60.640  1.00 99.79           O  
ANISOU 3464  O   CYS B 143    13055  15757   9104   3114   -350  -3508       O  
ATOM   3465  CB  CYS B 143       6.966 -43.108 -61.463  1.00103.09           C  
ANISOU 3465  CB  CYS B 143    13330  16846   8994   3830    258  -3481       C  
ATOM   3466  SG  CYS B 143       7.340 -42.885 -59.721  1.00117.10           S  
ANISOU 3466  SG  CYS B 143    14964  18081  11448   3676    342  -3154       S  
ATOM   3467  N   PRO B 144       4.353 -45.600 -60.740  1.00105.43           N  
ANISOU 3467  N   PRO B 144    14326  15860   9872   3247   -606  -4391       N  
ATOM   3468  CA  PRO B 144       3.079 -45.737 -60.030  1.00104.12           C  
ANISOU 3468  CA  PRO B 144    14168  15289  10105   2793   -868  -4324       C  
ATOM   3469  C   PRO B 144       3.222 -45.318 -58.575  1.00 99.74           C  
ANISOU 3469  C   PRO B 144    13464  14384  10049   2635   -714  -3902       C  
ATOM   3470  O   PRO B 144       4.340 -45.281 -58.067  1.00 98.34           O  
ANISOU 3470  O   PRO B 144    13269  14145   9952   2882   -484  -3782       O  
ATOM   3471  CB  PRO B 144       2.800 -47.238 -60.114  1.00108.05           C  
ANISOU 3471  CB  PRO B 144    15067  15283  10704   2757  -1110  -4899       C  
ATOM   3472  CG  PRO B 144       4.148 -47.857 -60.203  1.00109.92           C  
ANISOU 3472  CG  PRO B 144    15489  15428  10845   3231   -900  -5137       C  
ATOM   3473  CD  PRO B 144       4.971 -46.907 -61.024  1.00109.86           C  
ANISOU 3473  CD  PRO B 144    15233  16148  10360   3549   -627  -4950       C  
ATOM   3474  N   ASN B 145       2.109 -45.013 -57.916  1.00 98.59           N  
ANISOU 3474  N   ASN B 145    13194  14049  10215   2234   -841  -3698       N  
ATOM   3475  CA  ASN B 145       2.145 -44.591 -56.519  1.00 95.23           C  
ANISOU 3475  CA  ASN B 145    12647  13332  10206   2061   -688  -3329       C  
ATOM   3476  C   ASN B 145       2.563 -45.715 -55.574  1.00 96.23           C  
ANISOU 3476  C   ASN B 145    13067  12874  10621   2064   -696  -3472       C  
ATOM   3477  O   ASN B 145       2.997 -45.465 -54.453  1.00 92.53           O  
ANISOU 3477  O   ASN B 145    12552  12216  10390   2036   -546  -3190       O  
ATOM   3478  CB  ASN B 145       0.794 -44.009 -56.099  1.00 94.34           C  
ANISOU 3478  CB  ASN B 145    12310  13204  10330   1659   -789  -3114       C  
ATOM   3479  CG  ASN B 145       0.370 -42.842 -56.962  1.00 94.90           C  
ANISOU 3479  CG  ASN B 145    12084  13809  10166   1694   -805  -2903       C  
ATOM   3480  OD1 ASN B 145       1.185 -42.000 -57.332  1.00 94.07           O  
ANISOU 3480  OD1 ASN B 145    11859  14035   9848   1941   -617  -2678       O  
ATOM   3481  ND2 ASN B 145      -0.913 -42.790 -57.296  1.00 97.00           N  
ANISOU 3481  ND2 ASN B 145    12213  14160  10482   1439  -1044  -2948       N  
ATOM   3482  N   THR B 146       2.432 -46.952 -56.040  1.00101.97           N  
ANISOU 3482  N   THR B 146    14119  13306  11319   2100   -893  -3912       N  
ATOM   3483  CA  THR B 146       2.833 -48.118 -55.265  1.00104.96           C  
ANISOU 3483  CA  THR B 146    14833  13066  11980   2141   -934  -4050       C  
ATOM   3484  C   THR B 146       4.350 -48.145 -55.081  1.00106.47           C  
ANISOU 3484  C   THR B 146    15045  13306  12101   2626   -730  -3996       C  
ATOM   3485  O   THR B 146       4.862 -48.698 -54.106  1.00106.27           O  
ANISOU 3485  O   THR B 146    15178  12855  12343   2694   -711  -3888       O  
ATOM   3486  CB  THR B 146       2.367 -49.420 -55.944  1.00109.80           C  
ANISOU 3486  CB  THR B 146    15815  13313  12591   2088  -1206  -4583       C  
ATOM   3487  OG1 THR B 146       1.023 -49.260 -56.413  1.00110.52           O  
ANISOU 3487  OG1 THR B 146    15792  13542  12659   1670  -1421  -4673       O  
ATOM   3488  CG2 THR B 146       2.425 -50.591 -54.974  1.00111.47           C  
ANISOU 3488  CG2 THR B 146    16386  12756  13211   1986  -1290  -4625       C  
ATOM   3489  N   ASN B 147       5.063 -47.538 -56.024  1.00108.92           N  
ANISOU 3489  N   ASN B 147    15172  14168  12044   2956   -581  -4044       N  
ATOM   3490  CA  ASN B 147       6.517 -47.452 -55.954  1.00111.06           C  
ANISOU 3490  CA  ASN B 147    15354  14606  12239   3411   -360  -3984       C  
ATOM   3491  C   ASN B 147       6.949 -46.018 -55.673  1.00108.00           C  
ANISOU 3491  C   ASN B 147    14553  14689  11794   3372   -129  -3510       C  
ATOM   3492  O   ASN B 147       7.987 -45.570 -56.153  1.00108.92           O  
ANISOU 3492  O   ASN B 147    14466  15225  11696   3689     80  -3456       O  
ATOM   3493  CB  ASN B 147       7.144 -47.951 -57.264  1.00116.57           C  
ANISOU 3493  CB  ASN B 147    16156  15583  12553   3841   -311  -4433       C  
ATOM   3494  CG  ASN B 147       8.598 -48.374 -57.102  1.00119.25           C  
ANISOU 3494  CG  ASN B 147    16462  15905  12944   4324   -128  -4469       C  
ATOM   3495  OD1 ASN B 147       9.515 -47.639 -57.464  1.00119.09           O  
ANISOU 3495  OD1 ASN B 147    16106  16402  12740   4506    120  -4242       O  
ATOM   3496  ND2 ASN B 147       8.811 -49.570 -56.568  1.00122.19           N  
ANISOU 3496  ND2 ASN B 147    17138  15659  13631   4436   -262  -4644       N  
ATOM   3497  N   ARG B 148       6.140 -45.299 -54.900  1.00105.28           N  
ANISOU 3497  N   ARG B 148    14078  14267  11656   2972   -156  -3180       N  
ATOM   3498  CA  ARG B 148       6.468 -43.929 -54.518  1.00102.71           C  
ANISOU 3498  CA  ARG B 148    13405  14275  11346   2895     40  -2754       C  
ATOM   3499  C   ARG B 148       6.744 -43.823 -53.024  1.00101.98           C  
ANISOU 3499  C   ARG B 148    13298  13871  11579   2758     75  -2494       C  
ATOM   3500  O   ARG B 148       6.239 -44.617 -52.231  1.00102.61           O  
ANISOU 3500  O   ARG B 148    13617  13492  11879   2589    -61  -2549       O  
ATOM   3501  CB  ARG B 148       5.349 -42.959 -54.912  1.00100.71           C  
ANISOU 3501  CB  ARG B 148    12976  14258  11033   2600      8  -2581       C  
ATOM   3502  CG  ARG B 148       5.169 -42.768 -56.413  1.00103.61           C  
ANISOU 3502  CG  ARG B 148    13302  15074  10992   2739    -24  -2727       C  
ATOM   3503  CD  ARG B 148       5.700 -41.429 -56.899  1.00102.76           C  
ANISOU 3503  CD  ARG B 148    12889  15462  10693   2824    192  -2370       C  
ATOM   3504  NE  ARG B 148       5.247 -41.128 -58.255  1.00105.94           N  
ANISOU 3504  NE  ARG B 148    13261  16303  10687   2879    125  -2415       N  
ATOM   3505  CZ  ARG B 148       5.429 -39.962 -58.867  1.00106.11           C  
ANISOU 3505  CZ  ARG B 148    13056  16757  10503   2907    265  -2062       C  
ATOM   3506  NH1 ARG B 148       6.054 -38.972 -58.247  1.00103.44           N  
ANISOU 3506  NH1 ARG B 148    12495  16432  10374   2859    483  -1674       N  
ATOM   3507  NH2 ARG B 148       4.977 -39.781 -60.100  1.00109.26           N  
ANISOU 3507  NH2 ARG B 148    13467  17567  10481   2963    167  -2089       N  
ATOM   3508  N   ALA B 149       7.555 -42.841 -52.646  1.00101.35           N  
ANISOU 3508  N   ALA B 149    12946  14050  11513   2808    252  -2206       N  
ATOM   3509  CA  ALA B 149       7.837 -42.590 -51.237  1.00 98.15           C  
ANISOU 3509  CA  ALA B 149    12510  13431  11351   2660    270  -1968       C  
ATOM   3510  C   ALA B 149       6.946 -41.475 -50.710  1.00 91.56           C  
ANISOU 3510  C   ALA B 149    11531  12627  10631   2289    328  -1729       C  
ATOM   3511  O   ALA B 149       6.632 -40.529 -51.430  1.00 90.58           O  
ANISOU 3511  O   ALA B 149    11208  12794  10414   2239    412  -1630       O  
ATOM   3512  CB  ALA B 149       9.297 -42.243 -51.034  1.00 99.25           C  
ANISOU 3512  CB  ALA B 149    12430  13811  11471   2916    390  -1842       C  
ATOM   3513  N   TRP B 150       6.555 -41.587 -49.447  1.00 85.57           N  
ANISOU 3513  N   TRP B 150    10881  11568  10065   2052    292  -1627       N  
ATOM   3514  CA  TRP B 150       5.580 -40.675 -48.875  1.00 79.51           C  
ANISOU 3514  CA  TRP B 150    10005  10785   9420   1721    364  -1471       C  
ATOM   3515  C   TRP B 150       5.548 -40.805 -47.361  1.00 77.10           C  
ANISOU 3515  C   TRP B 150     9822  10228   9244   1524    372  -1358       C  
ATOM   3516  O   TRP B 150       5.708 -41.902 -46.828  1.00 78.51           O  
ANISOU 3516  O   TRP B 150    10254  10132   9443   1550    260  -1406       O  
ATOM   3517  CB  TRP B 150       4.213 -40.982 -49.469  1.00 79.27           C  
ANISOU 3517  CB  TRP B 150    10023  10686   9410   1553    277  -1599       C  
ATOM   3518  CG  TRP B 150       3.077 -40.313 -48.807  1.00 77.70           C  
ANISOU 3518  CG  TRP B 150     9711  10429   9381   1238    347  -1481       C  
ATOM   3519  CD1 TRP B 150       2.585 -39.076 -49.081  1.00 76.92           C  
ANISOU 3519  CD1 TRP B 150     9353  10539   9333   1182    446  -1348       C  
ATOM   3520  CD2 TRP B 150       2.260 -40.853 -47.767  1.00 78.09           C  
ANISOU 3520  CD2 TRP B 150     9895  10193   9582    954    344  -1480       C  
ATOM   3521  NE1 TRP B 150       1.513 -38.806 -48.266  1.00 76.70           N  
ANISOU 3521  NE1 TRP B 150     9266  10382   9494    916    512  -1306       N  
ATOM   3522  CE2 TRP B 150       1.294 -39.885 -47.449  1.00 77.27           C  
ANISOU 3522  CE2 TRP B 150     9567  10182   9609    752    469  -1381       C  
ATOM   3523  CE3 TRP B 150       2.254 -42.064 -47.070  1.00 79.69           C  
ANISOU 3523  CE3 TRP B 150    10389  10062   9827    853    260  -1528       C  
ATOM   3524  CZ2 TRP B 150       0.330 -40.088 -46.463  1.00 77.33           C  
ANISOU 3524  CZ2 TRP B 150     9598  10025   9761    451    548  -1355       C  
ATOM   3525  CZ3 TRP B 150       1.298 -42.265 -46.091  1.00 79.88           C  
ANISOU 3525  CZ3 TRP B 150    10466   9903   9982    514    326  -1453       C  
ATOM   3526  CH2 TRP B 150       0.350 -41.284 -45.797  1.00 78.62           C  
ANISOU 3526  CH2 TRP B 150    10044   9905   9923    314    486  -1380       C  
ATOM   3527  N   ASN B 151       5.343 -39.679 -46.682  1.00 73.82           N  
ANISOU 3527  N   ASN B 151     9249   9897   8902   1336    502  -1208       N  
ATOM   3528  CA  ASN B 151       5.360 -39.618 -45.221  1.00 72.26           C  
ANISOU 3528  CA  ASN B 151     9159   9548   8749   1144    534  -1113       C  
ATOM   3529  C   ASN B 151       6.678 -40.121 -44.655  1.00 71.76           C  
ANISOU 3529  C   ASN B 151     9188   9469   8608   1325    431  -1062       C  
ATOM   3530  O   ASN B 151       6.712 -41.075 -43.882  1.00 72.73           O  
ANISOU 3530  O   ASN B 151     9565   9361   8709   1299    325  -1032       O  
ATOM   3531  CB  ASN B 151       4.172 -40.376 -44.616  1.00 73.40           C  
ANISOU 3531  CB  ASN B 151     9504   9431   8953    888    523  -1141       C  
ATOM   3532  CG  ASN B 151       3.949 -40.041 -43.154  1.00 73.05           C  
ANISOU 3532  CG  ASN B 151     9535   9324   8895    646    630  -1032       C  
ATOM   3533  OD1 ASN B 151       4.333 -38.969 -42.684  1.00 72.01           O  
ANISOU 3533  OD1 ASN B 151     9266   9346   8749    620    730   -990       O  
ATOM   3534  ND2 ASN B 151       3.320 -40.956 -42.427  1.00 74.27           N  
ANISOU 3534  ND2 ASN B 151     9924   9251   9043    447    614   -991       N  
ATOM   3535  N   SER B 152       7.761 -39.467 -45.055  1.00 70.91           N  
ANISOU 3535  N   SER B 152     8854   9618   8471   1504    456  -1022       N  
ATOM   3536  CA  SER B 152       9.093 -39.850 -44.616  1.00 72.15           C  
ANISOU 3536  CA  SER B 152     8995   9840   8581   1709    343   -972       C  
ATOM   3537  C   SER B 152       9.806 -38.677 -43.972  1.00 71.11           C  
ANISOU 3537  C   SER B 152     8636   9915   8467   1584    391   -865       C  
ATOM   3538  O   SER B 152      10.961 -38.789 -43.571  1.00 72.45           O  
ANISOU 3538  O   SER B 152     8704  10213   8612   1717    282   -810       O  
ATOM   3539  CB  SER B 152       9.915 -40.360 -45.796  1.00 74.10           C  
ANISOU 3539  CB  SER B 152     9128  10243   8784   2078    320  -1063       C  
ATOM   3540  OG  SER B 152       9.342 -41.527 -46.349  1.00 75.76           O  
ANISOU 3540  OG  SER B 152     9591  10218   8977   2201    240  -1223       O  
ATOM   3541  N   LEU B 153       9.115 -37.548 -43.879  1.00 69.66           N  
ANISOU 3541  N   LEU B 153     8363   9752   8352   1332    538   -849       N  
ATOM   3542  CA  LEU B 153       9.716 -36.355 -43.303  1.00 69.86           C  
ANISOU 3542  CA  LEU B 153     8203   9910   8431   1173    582   -793       C  
ATOM   3543  C   LEU B 153       8.979 -35.864 -42.067  1.00 69.62           C  
ANISOU 3543  C   LEU B 153     8329   9729   8393    880    630   -834       C  
ATOM   3544  O   LEU B 153       7.748 -35.869 -42.019  1.00 68.15           O  
ANISOU 3544  O   LEU B 153     8260   9394   8240    762    742   -882       O  
ATOM   3545  CB  LEU B 153       9.812 -35.237 -44.341  1.00 69.73           C  
ANISOU 3545  CB  LEU B 153     7918  10047   8531   1166    733   -734       C  
ATOM   3546  CG  LEU B 153      10.915 -35.396 -45.386  1.00 71.15           C  
ANISOU 3546  CG  LEU B 153     7861  10500   8674   1413    734   -668       C  
ATOM   3547  CD1 LEU B 153      11.095 -34.111 -46.178  1.00 71.47           C  
ANISOU 3547  CD1 LEU B 153     7644  10690   8820   1319    897   -532       C  
ATOM   3548  CD2 LEU B 153      12.215 -35.808 -44.720  1.00 72.90           C  
ANISOU 3548  CD2 LEU B 153     7980  10855   8863   1511    587   -655       C  
ATOM   3549  N   GLU B 154       9.751 -35.449 -41.069  1.00 71.63           N  
ANISOU 3549  N   GLU B 154     8563  10061   8590    765    543   -833       N  
ATOM   3550  CA  GLU B 154       9.201 -34.864 -39.856  1.00 73.29           C  
ANISOU 3550  CA  GLU B 154     8923  10186   8736    492    603   -920       C  
ATOM   3551  C   GLU B 154       9.983 -33.611 -39.472  1.00 76.30           C  
ANISOU 3551  C   GLU B 154     9126  10673   9194    331    589   -980       C  
ATOM   3552  O   GLU B 154      11.130 -33.434 -39.878  1.00 77.72           O  
ANISOU 3552  O   GLU B 154     9069  11023   9436    409    479   -911       O  
ATOM   3553  CB  GLU B 154       9.201 -35.879 -38.707  1.00 74.17           C  
ANISOU 3553  CB  GLU B 154     9324  10260   8599    458    460   -885       C  
ATOM   3554  CG  GLU B 154      10.577 -36.392 -38.299  1.00 75.71           C  
ANISOU 3554  CG  GLU B 154     9477  10615   8672    600    182   -791       C  
ATOM   3555  CD  GLU B 154      10.510 -37.381 -37.147  1.00 77.41           C  
ANISOU 3555  CD  GLU B 154    10020  10773   8622    575     21   -692       C  
ATOM   3556  OE1 GLU B 154       9.389 -37.698 -36.695  1.00 77.02           O  
ANISOU 3556  OE1 GLU B 154    10226  10562   8475    417    162   -691       O  
ATOM   3557  OE2 GLU B 154      11.577 -37.842 -36.692  1.00 79.68           O  
ANISOU 3557  OE2 GLU B 154    10288  11190   8796    712   -247   -587       O  
ATOM   3558  N   VAL B 155       9.349 -32.741 -38.694  1.00 78.28           N  
ANISOU 3558  N   VAL B 155     9474  10815   9453     98    714  -1128       N  
ATOM   3559  CA  VAL B 155       9.964 -31.491 -38.264  1.00 81.30           C  
ANISOU 3559  CA  VAL B 155     9740  11216   9936   -102    699  -1246       C  
ATOM   3560  C   VAL B 155      10.742 -31.702 -36.972  1.00 85.73           C  
ANISOU 3560  C   VAL B 155    10418  11930  10227   -235    473  -1329       C  
ATOM   3561  O   VAL B 155      10.282 -32.404 -36.074  1.00 86.84           O  
ANISOU 3561  O   VAL B 155    10827  12082  10084   -261    443  -1353       O  
ATOM   3562  CB  VAL B 155       8.894 -30.398 -38.063  1.00 81.29           C  
ANISOU 3562  CB  VAL B 155     9806  10985  10096   -252    946  -1422       C  
ATOM   3563  CG1 VAL B 155       9.477 -29.170 -37.389  1.00 83.74           C  
ANISOU 3563  CG1 VAL B 155    10086  11237  10493   -493    913  -1616       C  
ATOM   3564  CG2 VAL B 155       8.269 -30.028 -39.394  1.00 79.70           C  
ANISOU 3564  CG2 VAL B 155     9441  10662  10179   -112   1110  -1296       C  
ATOM   3565  N   GLU B 156      11.932 -31.116 -36.889  1.00 88.81           N  
ANISOU 3565  N   GLU B 156    10591  12463  10691   -333    299  -1346       N  
ATOM   3566  CA  GLU B 156      12.681 -31.130 -35.643  1.00 93.36           C  
ANISOU 3566  CA  GLU B 156    11246  13219  11008   -495     38  -1453       C  
ATOM   3567  C   GLU B 156      12.412 -29.833 -34.894  1.00 97.66           C  
ANISOU 3567  C   GLU B 156    11886  13634  11586   -815    120  -1758       C  
ATOM   3568  O   GLU B 156      11.874 -29.846 -33.788  1.00 99.44           O  
ANISOU 3568  O   GLU B 156    12410  13858  11516   -940    139  -1947       O  
ATOM   3569  CB  GLU B 156      14.182 -31.294 -35.900  1.00 94.15           C  
ANISOU 3569  CB  GLU B 156    11006  13593  11171   -433   -244  -1322       C  
ATOM   3570  CG  GLU B 156      15.022 -31.522 -34.639  1.00 96.94           C  
ANISOU 3570  CG  GLU B 156    11408  14201  11222   -549   -602  -1385       C  
ATOM   3571  CD  GLU B 156      14.994 -32.965 -34.153  1.00 96.48           C  
ANISOU 3571  CD  GLU B 156    11570  14244  10842   -294   -780  -1196       C  
ATOM   3572  OE1 GLU B 156      14.092 -33.323 -33.368  1.00 96.18           O  
ANISOU 3572  OE1 GLU B 156    11923  14105  10516   -355   -705  -1237       O  
ATOM   3573  OE2 GLU B 156      15.885 -33.743 -34.552  1.00 97.01           O  
ANISOU 3573  OE2 GLU B 156    11416  14486  10957    -26   -984   -995       O  
ATOM   3574  N   ASP B 157      12.772 -28.712 -35.513  1.00100.55           N  
ANISOU 3574  N   ASP B 157    12018  13876  12311   -948    187  -1808       N  
ATOM   3575  CA  ASP B 157      12.650 -27.413 -34.861  1.00105.85           C  
ANISOU 3575  CA  ASP B 157    12779  14350  13088  -1255    238  -2130       C  
ATOM   3576  C   ASP B 157      12.040 -26.340 -35.751  1.00106.72           C  
ANISOU 3576  C   ASP B 157    12812  14095  13642  -1276    519  -2137       C  
ATOM   3577  O   ASP B 157      11.948 -26.496 -36.966  1.00104.00           O  
ANISOU 3577  O   ASP B 157    12279  13720  13518  -1093    632  -1856       O  
ATOM   3578  CB  ASP B 157      14.011 -26.945 -34.349  1.00111.02           C  
ANISOU 3578  CB  ASP B 157    13245  15197  13740  -1518    -86  -2229       C  
ATOM   3579  CG  ASP B 157      14.474 -27.729 -33.143  1.00114.56           C  
ANISOU 3579  CG  ASP B 157    13847  15977  13703  -1546   -397  -2301       C  
ATOM   3580  OD1 ASP B 157      13.627 -28.036 -32.278  1.00115.27           O  
ANISOU 3580  OD1 ASP B 157    14303  16048  13446  -1537   -311  -2452       O  
ATOM   3581  OD2 ASP B 157      15.681 -28.038 -33.062  1.00117.21           O  
ANISOU 3581  OD2 ASP B 157    13919  16618  13997  -1570   -725  -2185       O  
ATOM   3582  N   TYR B 158      11.638 -25.240 -35.126  1.00111.30           N  
ANISOU 3582  N   TYR B 158    13556  14396  14337  -1487    618  -2466       N  
ATOM   3583  CA  TYR B 158      10.957 -24.157 -35.820  1.00113.29           C  
ANISOU 3583  CA  TYR B 158    13788  14226  15030  -1481    875  -2487       C  
ATOM   3584  C   TYR B 158      11.884 -22.972 -36.035  1.00115.20           C  
ANISOU 3584  C   TYR B 158    13866  14262  15645  -1778    773  -2530       C  
ATOM   3585  O   TYR B 158      12.636 -22.593 -35.140  1.00118.86           O  
ANISOU 3585  O   TYR B 158    14368  14781  16014  -2073    559  -2802       O  
ATOM   3586  CB  TYR B 158       9.744 -23.697 -35.009  1.00117.58           C  
ANISOU 3586  CB  TYR B 158    14635  14522  15518  -1464   1107  -2851       C  
ATOM   3587  CG  TYR B 158       8.627 -24.712 -34.915  1.00117.31           C  
ANISOU 3587  CG  TYR B 158    14723  14635  15215  -1209   1283  -2780       C  
ATOM   3588  CD1 TYR B 158       7.396 -24.468 -35.503  1.00117.07           C  
ANISOU 3588  CD1 TYR B 158    14677  14374  15431   -999   1569  -2736       C  
ATOM   3589  CD2 TYR B 158       8.800 -25.908 -34.233  1.00117.61           C  
ANISOU 3589  CD2 TYR B 158    14878  15034  14775  -1191   1148  -2735       C  
ATOM   3590  CE1 TYR B 158       6.370 -25.390 -35.423  1.00116.12           C  
ANISOU 3590  CE1 TYR B 158    14619  14401  15099   -820   1724  -2674       C  
ATOM   3591  CE2 TYR B 158       7.780 -26.836 -34.147  1.00116.70           C  
ANISOU 3591  CE2 TYR B 158    14876  15017  14450  -1018   1315  -2646       C  
ATOM   3592  CZ  TYR B 158       6.568 -26.572 -34.744  1.00116.16           C  
ANISOU 3592  CZ  TYR B 158    14755  14737  14645   -854   1607  -2629       C  
ATOM   3593  OH  TYR B 158       5.550 -27.494 -34.658  1.00115.82           O  
ANISOU 3593  OH  TYR B 158    14778  14807  14423   -734   1767  -2544       O  
ATOM   3594  N   GLY B 159      11.830 -22.388 -37.226  1.00113.22           N  
ANISOU 3594  N   GLY B 159    13434  13779  15807  -1727    913  -2246       N  
ATOM   3595  CA  GLY B 159      12.508 -21.129 -37.473  1.00115.81           C  
ANISOU 3595  CA  GLY B 159    13645  13793  16563  -2039    878  -2254       C  
ATOM   3596  C   GLY B 159      11.605 -20.007 -37.003  1.00117.70           C  
ANISOU 3596  C   GLY B 159    14170  13477  17072  -2094   1052  -2596       C  
ATOM   3597  O   GLY B 159      10.491 -20.260 -36.550  1.00116.41           O  
ANISOU 3597  O   GLY B 159    14232  13255  16742  -1866   1217  -2801       O  
ATOM   3598  N   PHE B 160      12.075 -18.771 -37.112  1.00121.05           N  
ANISOU 3598  N   PHE B 160    14575  13480  17938  -2394   1028  -2661       N  
ATOM   3599  CA  PHE B 160      11.318 -17.630 -36.611  1.00124.09           C  
ANISOU 3599  CA  PHE B 160    15254  13263  18634  -2441   1175  -3043       C  
ATOM   3600  C   PHE B 160      11.237 -16.518 -37.653  1.00126.16           C  
ANISOU 3600  C   PHE B 160    15448  12969  19517  -2478   1304  -2734       C  
ATOM   3601  O   PHE B 160      11.523 -16.738 -38.829  1.00123.89           O  
ANISOU 3601  O   PHE B 160    14907  12826  19340  -2399   1335  -2189       O  
ATOM   3602  CB  PHE B 160      11.950 -17.103 -35.320  1.00128.90           C  
ANISOU 3602  CB  PHE B 160    16039  13790  19146  -2836    968  -3603       C  
ATOM   3603  CG  PHE B 160      11.973 -18.107 -34.197  1.00127.41           C  
ANISOU 3603  CG  PHE B 160    15975  14131  18304  -2802    831  -3900       C  
ATOM   3604  CD1 PHE B 160      13.129 -18.313 -33.460  1.00129.84           C  
ANISOU 3604  CD1 PHE B 160    16206  14784  18343  -3145    480  -4072       C  
ATOM   3605  CD2 PHE B 160      10.837 -18.829 -33.866  1.00124.23           C  
ANISOU 3605  CD2 PHE B 160    15753  13889  17558  -2446   1041  -3982       C  
ATOM   3606  CE1 PHE B 160      13.155 -19.230 -32.424  1.00129.13           C  
ANISOU 3606  CE1 PHE B 160    16256  15181  17625  -3101    329  -4286       C  
ATOM   3607  CE2 PHE B 160      10.858 -19.747 -32.830  1.00123.50           C  
ANISOU 3607  CE2 PHE B 160    15804  14268  16852  -2440    928  -4191       C  
ATOM   3608  CZ  PHE B 160      12.017 -19.946 -32.109  1.00125.98           C  
ANISOU 3608  CZ  PHE B 160    16081  14911  16874  -2753    565  -4330       C  
ATOM   3609  N   GLY B 161      10.847 -15.324 -37.215  1.00130.97           N  
ANISOU 3609  N   GLY B 161    16308  12935  20520  -2586   1384  -3081       N  
ATOM   3610  CA  GLY B 161      10.733 -14.187 -38.111  1.00134.42           C  
ANISOU 3610  CA  GLY B 161    16741  12740  21591  -2622   1493  -2781       C  
ATOM   3611  C   GLY B 161       9.361 -13.547 -38.060  1.00136.15           C  
ANISOU 3611  C   GLY B 161    17214  12412  22105  -2247   1738  -2967       C  
ATOM   3612  O   GLY B 161       8.486 -13.997 -37.322  1.00134.79           O  
ANISOU 3612  O   GLY B 161    17188  12394  21632  -1975   1856  -3348       O  
ATOM   3613  N   THR B 164       8.432 -13.926 -42.158  1.00118.18           N  
ANISOU 3613  N   THR B 164    14380  10322  20200  -1483   1977   -995       N  
ATOM   3614  CA  THR B 164       8.171 -15.324 -42.478  1.00112.10           C  
ANISOU 3614  CA  THR B 164    13434  10280  18879  -1223   1969   -857       C  
ATOM   3615  C   THR B 164       8.682 -16.250 -41.382  1.00109.94           C  
ANISOU 3615  C   THR B 164    13167  10473  18131  -1388   1861  -1304       C  
ATOM   3616  O   THR B 164       9.611 -15.910 -40.652  1.00112.89           O  
ANISOU 3616  O   THR B 164    13579  10776  18538  -1776   1737  -1573       O  
ATOM   3617  CB  THR B 164       8.818 -15.723 -43.814  1.00110.10           C  
ANISOU 3617  CB  THR B 164    12921  10412  18499  -1243   1936   -211       C  
ATOM   3618  OG1 THR B 164      10.226 -15.460 -43.762  1.00112.29           O  
ANISOU 3618  OG1 THR B 164    13072  10757  18838  -1708   1840   -130       O  
ATOM   3619  CG2 THR B 164       8.204 -14.929 -44.954  1.00112.51           C  
ANISOU 3619  CG2 THR B 164    13237  10341  19169  -1032   2026    303       C  
ATOM   3620  N   THR B 165       8.069 -17.422 -41.271  1.00105.63           N  
ANISOU 3620  N   THR B 165    12585  10399  17151  -1107   1887  -1364       N  
ATOM   3621  CA  THR B 165       8.487 -18.400 -40.276  1.00103.75           C  
ANISOU 3621  CA  THR B 165    12376  10610  16433  -1220   1776  -1702       C  
ATOM   3622  C   THR B 165       8.802 -19.748 -40.918  1.00 98.58           C  
ANISOU 3622  C   THR B 165    11520  10566  15370  -1081   1699  -1386       C  
ATOM   3623  O   THR B 165       7.934 -20.388 -41.507  1.00 95.58           O  
ANISOU 3623  O   THR B 165    11104  10348  14864   -764   1782  -1212       O  
ATOM   3624  CB  THR B 165       7.434 -18.567 -39.174  1.00104.75           C  
ANISOU 3624  CB  THR B 165    12729  10674  16398  -1061   1897  -2192       C  
ATOM   3625  OG1 THR B 165       7.337 -17.350 -38.424  1.00110.00           O  
ANISOU 3625  OG1 THR B 165    13606  10795  17394  -1213   1956  -2598       O  
ATOM   3626  CG2 THR B 165       7.825 -19.692 -38.237  1.00103.16           C  
ANISOU 3626  CG2 THR B 165    12574  10979  15641  -1158   1777  -2429       C  
ATOM   3627  N   ASN B 166      10.056 -20.166 -40.804  1.00 97.90           N  
ANISOU 3627  N   ASN B 166    11290  10808  15099  -1315   1526  -1333       N  
ATOM   3628  CA  ASN B 166      10.508 -21.403 -41.421  1.00 93.73           C  
ANISOU 3628  CA  ASN B 166    10568  10822  14225  -1166   1452  -1062       C  
ATOM   3629  C   ASN B 166      10.483 -22.546 -40.413  1.00 91.30           C  
ANISOU 3629  C   ASN B 166    10367  10848  13474  -1109   1337  -1347       C  
ATOM   3630  O   ASN B 166      10.287 -22.315 -39.223  1.00 92.61           O  
ANISOU 3630  O   ASN B 166    10737  10890  13562  -1242   1306  -1736       O  
ATOM   3631  CB  ASN B 166      11.914 -21.211 -41.993  1.00 94.91           C  
ANISOU 3631  CB  ASN B 166    10432  11167  14464  -1403   1355   -787       C  
ATOM   3632  CG  ASN B 166      12.008 -20.004 -42.914  1.00 97.38           C  
ANISOU 3632  CG  ASN B 166    10665  11117  15218  -1533   1477   -458       C  
ATOM   3633  OD1 ASN B 166      11.828 -20.119 -44.124  1.00 96.34           O  
ANISOU 3633  OD1 ASN B 166    10415  11102  15087  -1345   1586    -42       O  
ATOM   3634  ND2 ASN B 166      12.285 -18.839 -42.341  1.00101.28           N  
ANISOU 3634  ND2 ASN B 166    11249  11155  16077  -1866   1450   -641       N  
ATOM   3635  N   ILE B 167      10.657 -23.777 -40.891  1.00 88.44           N  
ANISOU 3635  N   ILE B 167     9896  10895  12811   -903   1280  -1155       N  
ATOM   3636  CA  ILE B 167      10.725 -24.936 -40.000  1.00 87.25           C  
ANISOU 3636  CA  ILE B 167     9858  11035  12256   -844   1148  -1340       C  
ATOM   3637  C   ILE B 167      11.683 -26.012 -40.487  1.00 86.46           C  
ANISOU 3637  C   ILE B 167     9556  11355  11941   -725    997  -1121       C  
ATOM   3638  O   ILE B 167      11.739 -26.316 -41.679  1.00 84.83           O  
ANISOU 3638  O   ILE B 167     9186  11273  11772   -539   1070   -842       O  
ATOM   3639  CB  ILE B 167       9.349 -25.582 -39.767  1.00 84.81           C  
ANISOU 3639  CB  ILE B 167     9761  10682  11782   -625   1279  -1441       C  
ATOM   3640  CG1 ILE B 167       8.513 -25.545 -41.039  1.00 83.08           C  
ANISOU 3640  CG1 ILE B 167     9449  10379  11737   -390   1431  -1184       C  
ATOM   3641  CG2 ILE B 167       8.609 -24.882 -38.653  1.00 86.96           C  
ANISOU 3641  CG2 ILE B 167    10263  10687  12091   -748   1388  -1805       C  
ATOM   3642  CD1 ILE B 167       7.053 -25.835 -40.796  1.00 81.90           C  
ANISOU 3642  CD1 ILE B 167     9442  10128  11550   -235   1577  -1310       C  
ATOM   3643  N   TRP B 168      12.425 -26.586 -39.545  1.00 88.40           N  
ANISOU 3643  N   TRP B 168     9817  11827  11943   -809    782  -1261       N  
ATOM   3644  CA  TRP B 168      13.367 -27.656 -39.840  1.00 88.83           C  
ANISOU 3644  CA  TRP B 168     9679  12264  11810   -646    616  -1092       C  
ATOM   3645  C   TRP B 168      12.646 -28.924 -40.250  1.00 87.12           C  
ANISOU 3645  C   TRP B 168     9600  12122  11377   -312    665  -1001       C  
ATOM   3646  O   TRP B 168      11.512 -29.159 -39.848  1.00 85.61           O  
ANISOU 3646  O   TRP B 168     9677  11759  11092   -272    758  -1115       O  
ATOM   3647  CB  TRP B 168      14.227 -27.962 -38.619  1.00 90.94           C  
ANISOU 3647  CB  TRP B 168     9953  12734  11863   -791    329  -1255       C  
ATOM   3648  CG  TRP B 168      15.340 -27.003 -38.414  1.00 94.37           C  
ANISOU 3648  CG  TRP B 168    10124  13230  12503  -1112    192  -1302       C  
ATOM   3649  CD1 TRP B 168      15.367 -25.689 -38.769  1.00 96.17           C  
ANISOU 3649  CD1 TRP B 168    10264  13189  13086  -1380    320  -1318       C  
ATOM   3650  CD2 TRP B 168      16.609 -27.288 -37.818  1.00 97.13           C  
ANISOU 3650  CD2 TRP B 168    10239  13922  12744  -1217   -122  -1324       C  
ATOM   3651  NE1 TRP B 168      16.573 -25.134 -38.421  1.00100.18           N  
ANISOU 3651  NE1 TRP B 168    10501  13839  13724  -1697    113  -1366       N  
ATOM   3652  CE2 TRP B 168      17.353 -26.097 -37.836  1.00100.87           C  
ANISOU 3652  CE2 TRP B 168    10467  14336  13524  -1598   -169  -1377       C  
ATOM   3653  CE3 TRP B 168      17.185 -28.436 -37.268  1.00 97.43           C  
ANISOU 3653  CE3 TRP B 168    10243  14296  12479  -1022   -389  -1285       C  
ATOM   3654  CZ2 TRP B 168      18.646 -26.021 -37.326  1.00105.00           C  
ANISOU 3654  CZ2 TRP B 168    10669  15177  14052  -1813   -480  -1417       C  
ATOM   3655  CZ3 TRP B 168      18.464 -28.359 -36.764  1.00101.50           C  
ANISOU 3655  CZ3 TRP B 168    10445  15130  12990  -1180   -706  -1305       C  
ATOM   3656  CH2 TRP B 168      19.182 -27.162 -36.794  1.00105.28           C  
ANISOU 3656  CH2 TRP B 168    10639  15595  13770  -1584   -754  -1382       C  
ATOM   3657  N   LEU B 169      13.311 -29.739 -41.060  1.00 88.01           N  
ANISOU 3657  N   LEU B 169     9517  12493  11428    -79    613   -813       N  
ATOM   3658  CA  LEU B 169      12.802 -31.066 -41.379  1.00 87.13           C  
ANISOU 3658  CA  LEU B 169     9556  12433  11115    226    605   -770       C  
ATOM   3659  C   LEU B 169      13.920 -32.101 -41.408  1.00 89.92           C  
ANISOU 3659  C   LEU B 169     9759  13074  11334    446    411   -695       C  
ATOM   3660  O   LEU B 169      14.982 -31.861 -41.980  1.00 92.04           O  
ANISOU 3660  O   LEU B 169     9684  13583  11703    482    398   -587       O  
ATOM   3661  CB  LEU B 169      12.045 -31.065 -42.707  1.00 84.37           C  
ANISOU 3661  CB  LEU B 169     9184  12025  10849    394    803   -648       C  
ATOM   3662  CG  LEU B 169      10.598 -30.573 -42.655  1.00 82.07           C  
ANISOU 3662  CG  LEU B 169     9093  11447  10642    317    958   -720       C  
ATOM   3663  CD1 LEU B 169      10.506 -29.079 -42.908  1.00 82.57           C  
ANISOU 3663  CD1 LEU B 169     9045  11341  10986    129   1090   -672       C  
ATOM   3664  CD2 LEU B 169       9.749 -31.348 -43.645  1.00 80.13           C  
ANISOU 3664  CD2 LEU B 169     8908  11213  10324    551   1021   -652       C  
ATOM   3665  N   LYS B 170      13.674 -33.244 -40.775  1.00 91.03           N  
ANISOU 3665  N   LYS B 170    10145  13180  11263    596    271   -736       N  
ATOM   3666  CA  LYS B 170      14.613 -34.358 -40.800  1.00 94.38           C  
ANISOU 3666  CA  LYS B 170    10472  13803  11585    886     74   -660       C  
ATOM   3667  C   LYS B 170      13.879 -35.634 -41.186  1.00 94.96           C  
ANISOU 3667  C   LYS B 170    10819  13709  11552   1160     93   -651       C  
ATOM   3668  O   LYS B 170      12.651 -35.649 -41.267  1.00 93.09           O  
ANISOU 3668  O   LYS B 170    10827  13242  11301   1068    231   -702       O  
ATOM   3669  CB  LYS B 170      15.273 -34.539 -39.437  1.00 97.29           C  
ANISOU 3669  CB  LYS B 170    10890  14270  11806    788   -214   -684       C  
ATOM   3670  CG  LYS B 170      14.321 -35.032 -38.367  1.00 97.36           C  
ANISOU 3670  CG  LYS B 170    11345  14063  11585    691   -265   -738       C  
ATOM   3671  CD  LYS B 170      15.068 -35.469 -37.122  1.00100.58           C  
ANISOU 3671  CD  LYS B 170    11825  14625  11765    676   -595   -699       C  
ATOM   3672  CE  LYS B 170      14.114 -35.991 -36.063  1.00100.12           C  
ANISOU 3672  CE  LYS B 170    12233  14388  11421    562   -609   -702       C  
ATOM   3673  NZ  LYS B 170      14.824 -36.298 -34.794  1.00103.24           N  
ANISOU 3673  NZ  LYS B 170    12727  14975  11526    518   -948   -639       N  
ATOM   3674  N   LEU B 171      14.630 -36.706 -41.415  1.00 98.03           N  
ANISOU 3674  N   LEU B 171    11149  14200  11896   1497    -53   -599       N  
ATOM   3675  CA  LEU B 171      14.042 -37.979 -41.824  1.00 98.74           C  
ANISOU 3675  CA  LEU B 171    11515  14077  11925   1762    -61   -618       C  
ATOM   3676  C   LEU B 171      13.434 -38.740 -40.649  1.00 99.27           C  
ANISOU 3676  C   LEU B 171    11987  13881  11849   1674   -213   -585       C  
ATOM   3677  O   LEU B 171      13.902 -38.634 -39.516  1.00100.38           O  
ANISOU 3677  O   LEU B 171    12163  14097  11879   1564   -396   -520       O  
ATOM   3678  CB  LEU B 171      15.077 -38.853 -42.541  1.00101.42           C  
ANISOU 3678  CB  LEU B 171    11661  14575  12298   2202   -141   -607       C  
ATOM   3679  CG  LEU B 171      15.516 -38.429 -43.945  1.00101.17           C  
ANISOU 3679  CG  LEU B 171    11288  14812  12339   2356     74   -640       C  
ATOM   3680  CD1 LEU B 171      16.630 -37.391 -43.892  1.00102.36           C  
ANISOU 3680  CD1 LEU B 171    10973  15332  12587   2228     96   -547       C  
ATOM   3681  CD2 LEU B 171      15.937 -39.636 -44.776  1.00103.11           C  
ANISOU 3681  CD2 LEU B 171    11539  15077  12563   2837     63   -729       C  
ATOM   3682  N   LYS B 172      12.384 -39.505 -40.929  1.00 99.32           N  
ANISOU 3682  N   LYS B 172    12295  13599  11842   1698   -142   -617       N  
ATOM   3683  CA  LYS B 172      11.740 -40.322 -39.909  1.00101.36           C  
ANISOU 3683  CA  LYS B 172    12948  13591  11972   1589   -246   -538       C  
ATOM   3684  C   LYS B 172      12.446 -41.662 -39.771  1.00104.19           C  
ANISOU 3684  C   LYS B 172    13455  13814  12319   1936   -490   -432       C  
ATOM   3685  O   LYS B 172      12.943 -42.212 -40.752  1.00105.39           O  
ANISOU 3685  O   LYS B 172    13492  13961  12590   2282   -507   -505       O  
ATOM   3686  CB  LYS B 172      10.268 -40.547 -40.253  1.00101.19           C  
ANISOU 3686  CB  LYS B 172    13147  13312  11989   1408    -62   -607       C  
ATOM   3687  CG  LYS B 172       9.424 -39.288 -40.197  1.00100.06           C  
ANISOU 3687  CG  LYS B 172    12891  13253  11876   1093    167   -689       C  
ATOM   3688  CD  LYS B 172       7.992 -39.554 -40.624  1.00 99.85           C  
ANISOU 3688  CD  LYS B 172    12995  13023  11919    953    324   -752       C  
ATOM   3689  CE  LYS B 172       7.341 -40.620 -39.768  1.00102.07           C  
ANISOU 3689  CE  LYS B 172    13627  13051  12103    817    274   -658       C  
ATOM   3690  NZ  LYS B 172       5.916 -40.819 -40.146  1.00101.67           N  
ANISOU 3690  NZ  LYS B 172    13632  12842  12154    619    431   -722       N  
ATOM   3691  N   GLU B 173      12.491 -42.181 -38.548  1.00105.40           N  
ANISOU 3691  N   GLU B 173    13876  13858  12315   1863   -676   -259       N  
ATOM   3692  CA  GLU B 173      13.110 -43.474 -38.293  1.00108.15           C  
ANISOU 3692  CA  GLU B 173    14413  14008  12670   2205   -941   -101       C  
ATOM   3693  C   GLU B 173      12.055 -44.571 -38.323  1.00107.12           C  
ANISOU 3693  C   GLU B 173    14726  13399  12577   2146   -906    -48       C  
ATOM   3694  O   GLU B 173      12.372 -45.758 -38.248  1.00110.93           O  
ANISOU 3694  O   GLU B 173    15444  13576  13127   2427  -1102     75       O  
ATOM   3695  CB  GLU B 173      13.830 -43.464 -36.945  1.00111.67           C  
ANISOU 3695  CB  GLU B 173    14911  14616  12902   2175  -1216    120       C  
ATOM   3696  CG  GLU B 173      14.880 -42.373 -36.816  1.00112.23           C  
ANISOU 3696  CG  GLU B 173    14531  15160  12953   2160  -1294     54       C  
ATOM   3697  CD  GLU B 173      15.548 -42.363 -35.457  1.00116.22           C  
ANISOU 3697  CD  GLU B 173    15092  15863  13202   2101  -1618    246       C  
ATOM   3698  OE1 GLU B 173      15.948 -41.270 -35.003  1.00116.31           O  
ANISOU 3698  OE1 GLU B 173    14863  16215  13113   1855  -1651    155       O  
ATOM   3699  OE2 GLU B 173      15.677 -43.444 -34.844  1.00119.82           O  
ANISOU 3699  OE2 GLU B 173    15848  16122  13555   2292  -1859    492       O  
ATOM   3700  N   LYS B 174      10.798 -44.159 -38.440  1.00102.52           N  
ANISOU 3700  N   LYS B 174    14235  12735  11983   1778   -660   -139       N  
ATOM   3701  CA  LYS B 174       9.683 -45.092 -38.475  1.00101.67           C  
ANISOU 3701  CA  LYS B 174    14489  12207  11936   1621   -603   -100       C  
ATOM   3702  C   LYS B 174       8.769 -44.765 -39.649  1.00 96.91           C  
ANISOU 3702  C   LYS B 174    13749  11583  11490   1511   -382   -355       C  
ATOM   3703  O   LYS B 174       8.688 -43.615 -40.075  1.00 93.98           O  
ANISOU 3703  O   LYS B 174    13068  11522  11118   1428   -220   -489       O  
ATOM   3704  CB  LYS B 174       8.907 -45.027 -37.160  1.00103.45           C  
ANISOU 3704  CB  LYS B 174    14976  12390  11941   1211   -537    109       C  
ATOM   3705  CG  LYS B 174       7.822 -46.079 -37.020  1.00106.26           C  
ANISOU 3705  CG  LYS B 174    15703  12309  12362    992   -486    228       C  
ATOM   3706  CD  LYS B 174       8.389 -47.473 -37.207  1.00110.36           C  
ANISOU 3706  CD  LYS B 174    16508  12399  13027   1319   -753    362       C  
ATOM   3707  CE  LYS B 174       7.286 -48.513 -37.227  1.00112.55           C  
ANISOU 3707  CE  LYS B 174    17147  12174  13442   1054   -703    451       C  
ATOM   3708  NZ  LYS B 174       7.821 -49.880 -37.460  1.00116.66           N  
ANISOU 3708  NZ  LYS B 174    17987  12175  14163   1388   -969    551       N  
ATOM   3709  N   GLN B 175       8.093 -45.778 -40.179  1.00 96.24           N  
ANISOU 3709  N   GLN B 175    13903  11118  11545   1508   -402   -414       N  
ATOM   3710  CA  GLN B 175       7.162 -45.578 -41.283  1.00 92.62           C  
ANISOU 3710  CA  GLN B 175    13330  10651  11210   1390   -251   -655       C  
ATOM   3711  C   GLN B 175       5.722 -45.710 -40.809  1.00 91.02           C  
ANISOU 3711  C   GLN B 175    13281  10271  11032    925   -118   -593       C  
ATOM   3712  O   GLN B 175       5.400 -46.596 -40.019  1.00 94.36           O  
ANISOU 3712  O   GLN B 175    14030  10371  11450    759   -181   -398       O  
ATOM   3713  CB  GLN B 175       7.436 -46.586 -42.400  1.00 94.55           C  
ANISOU 3713  CB  GLN B 175    13686  10639  11599   1715   -381   -858       C  
ATOM   3714  CG  GLN B 175       6.493 -46.470 -43.593  1.00 93.40           C  
ANISOU 3714  CG  GLN B 175    13445  10513  11529   1597   -286  -1127       C  
ATOM   3715  CD  GLN B 175       6.643 -47.622 -44.566  1.00 96.54           C  
ANISOU 3715  CD  GLN B 175    14051  10594  12036   1868   -433  -1376       C  
ATOM   3716  OE1 GLN B 175       7.472 -48.509 -44.368  1.00 99.93           O  
ANISOU 3716  OE1 GLN B 175    14691  10752  12527   2185   -588  -1349       O  
ATOM   3717  NE2 GLN B 175       5.836 -47.618 -45.622  1.00 96.16           N  
ANISOU 3717  NE2 GLN B 175    13949  10575  12013   1761   -404  -1636       N  
ATOM   3718  N   ASP B 176       4.860 -44.824 -41.296  1.00 86.47           N  
ANISOU 3718  N   ASP B 176    12447   9915  10491    722     72   -732       N  
ATOM   3719  CA  ASP B 176       3.441 -44.869 -40.966  1.00 85.07           C  
ANISOU 3719  CA  ASP B 176    12305   9643  10375    299    225   -704       C  
ATOM   3720  C   ASP B 176       2.647 -43.990 -41.917  1.00 81.49           C  
ANISOU 3720  C   ASP B 176    11510   9431  10020    229    356   -902       C  
ATOM   3721  O   ASP B 176       3.217 -43.254 -42.718  1.00 79.59           O  
ANISOU 3721  O   ASP B 176    11043   9435   9764    479    349  -1015       O  
ATOM   3722  CB  ASP B 176       3.211 -44.409 -39.527  1.00 85.04           C  
ANISOU 3722  CB  ASP B 176    12360   9754  10198     33    380   -493       C  
ATOM   3723  CG  ASP B 176       3.802 -43.045 -39.257  1.00 82.32           C  
ANISOU 3723  CG  ASP B 176    11759   9791   9728    129    476   -538       C  
ATOM   3724  OD1 ASP B 176       4.707 -42.637 -40.010  1.00 80.75           O  
ANISOU 3724  OD1 ASP B 176    11385   9733   9562    431    379   -640       O  
ATOM   3725  OD2 ASP B 176       3.371 -42.382 -38.294  1.00 82.36           O  
ANISOU 3725  OD2 ASP B 176    11742   9952   9601   -107    659   -485       O  
ATOM   3726  N   VAL B 177       1.328 -44.066 -41.821  1.00 81.09           N  
ANISOU 3726  N   VAL B 177    11407   9327  10076   -115    475   -913       N  
ATOM   3727  CA  VAL B 177       0.464 -43.228 -42.636  1.00 78.60           C  
ANISOU 3727  CA  VAL B 177    10742   9252   9870   -178    574  -1062       C  
ATOM   3728  C   VAL B 177      -0.137 -42.113 -41.792  1.00 76.45           C  
ANISOU 3728  C   VAL B 177    10254   9212   9582   -366    842   -990       C  
ATOM   3729  O   VAL B 177      -1.139 -41.507 -42.168  1.00 75.90           O  
ANISOU 3729  O   VAL B 177     9895   9295   9648   -480    958  -1065       O  
ATOM   3730  CB  VAL B 177      -0.654 -44.045 -43.307  1.00 81.44           C  
ANISOU 3730  CB  VAL B 177    11099   9439  10406   -404    487  -1179       C  
ATOM   3731  CG1 VAL B 177      -0.068 -45.014 -44.323  1.00 83.05           C  
ANISOU 3731  CG1 VAL B 177    11509   9425  10619   -172    223  -1352       C  
ATOM   3732  CG2 VAL B 177      -1.458 -44.794 -42.265  1.00 84.40           C  
ANISOU 3732  CG2 VAL B 177    11643   9578  10845   -813    586  -1020       C  
ATOM   3733  N   PHE B 178       0.481 -41.850 -40.645  1.00 75.47           N  
ANISOU 3733  N   PHE B 178    10270   9121   9285   -378    927   -860       N  
ATOM   3734  CA  PHE B 178       0.061 -40.747 -39.792  1.00 74.28           C  
ANISOU 3734  CA  PHE B 178     9960   9187   9078   -516   1189   -856       C  
ATOM   3735  C   PHE B 178       0.691 -39.441 -40.263  1.00 72.40           C  
ANISOU 3735  C   PHE B 178     9488   9154   8866   -274   1205   -956       C  
ATOM   3736  O   PHE B 178       1.866 -39.405 -40.631  1.00 71.44           O  
ANISOU 3736  O   PHE B 178     9412   9052   8680    -36   1039   -946       O  
ATOM   3737  CB  PHE B 178       0.462 -41.000 -38.335  1.00 74.34           C  
ANISOU 3737  CB  PHE B 178    10247   9175   8826   -654   1254   -699       C  
ATOM   3738  CG  PHE B 178      -0.174 -42.220 -37.725  1.00 76.37           C  
ANISOU 3738  CG  PHE B 178    10762   9217   9039   -941   1278   -522       C  
ATOM   3739  CD1 PHE B 178      -1.551 -42.307 -37.588  1.00 77.51           C  
ANISOU 3739  CD1 PHE B 178    10757   9386   9305  -1261   1508   -527       C  
ATOM   3740  CD2 PHE B 178       0.610 -43.264 -37.254  1.00 77.68           C  
ANISOU 3740  CD2 PHE B 178    11302   9154   9061   -895   1074   -320       C  
ATOM   3741  CE1 PHE B 178      -2.135 -43.421 -37.017  1.00 80.75           C  
ANISOU 3741  CE1 PHE B 178    11394   9592   9694  -1584   1551   -325       C  
ATOM   3742  CE2 PHE B 178       0.033 -44.380 -36.680  1.00 81.03           C  
ANISOU 3742  CE2 PHE B 178    11998   9326   9464  -1184   1096   -102       C  
ATOM   3743  CZ  PHE B 178      -1.341 -44.458 -36.562  1.00 82.61           C  
ANISOU 3743  CZ  PHE B 178    12054   9550   9784  -1557   1346   -100       C  
ATOM   3744  N   CYS B 179      -0.095 -38.369 -40.258  1.00 72.38           N  
ANISOU 3744  N   CYS B 179     9221   9293   8985   -333   1413  -1041       N  
ATOM   3745  CA  CYS B 179       0.440 -37.048 -40.546  1.00 70.94           C  
ANISOU 3745  CA  CYS B 179     8856   9236   8862   -152   1453  -1105       C  
ATOM   3746  C   CYS B 179       1.338 -36.655 -39.381  1.00 71.50           C  
ANISOU 3746  C   CYS B 179     9098   9341   8727   -188   1488  -1103       C  
ATOM   3747  O   CYS B 179       1.128 -37.111 -38.258  1.00 73.21           O  
ANISOU 3747  O   CYS B 179     9514   9547   8754   -376   1572  -1068       O  
ATOM   3748  CB  CYS B 179      -0.686 -36.024 -40.697  1.00 71.37           C  
ANISOU 3748  CB  CYS B 179     8616   9368   9133   -185   1667  -1191       C  
ATOM   3749  SG  CYS B 179      -2.168 -36.609 -41.554  1.00 79.52           S  
ANISOU 3749  SG  CYS B 179     9416  10419  10378   -275   1655  -1199       S  
ATOM   3750  N   ASP B 180       2.336 -35.819 -39.655  1.00 70.79           N  
ANISOU 3750  N   ASP B 180     8926   9313   8657    -34   1413  -1127       N  
ATOM   3751  CA  ASP B 180       3.277 -35.350 -38.638  1.00 71.69           C  
ANISOU 3751  CA  ASP B 180     9160   9487   8591    -83   1389  -1158       C  
ATOM   3752  C   ASP B 180       2.544 -34.724 -37.460  1.00 73.33           C  
ANISOU 3752  C   ASP B 180     9426   9723   8711   -285   1636  -1295       C  
ATOM   3753  O   ASP B 180       1.785 -33.775 -37.628  1.00 73.34           O  
ANISOU 3753  O   ASP B 180     9246   9705   8914   -286   1837  -1422       O  
ATOM   3754  CB  ASP B 180       4.240 -34.330 -39.249  1.00 71.07           C  
ANISOU 3754  CB  ASP B 180     8897   9462   8643     52   1315  -1181       C  
ATOM   3755  CG  ASP B 180       5.441 -34.053 -38.367  1.00 72.29           C  
ANISOU 3755  CG  ASP B 180     9142   9702   8622     -1   1189  -1206       C  
ATOM   3756  OD1 ASP B 180       5.438 -34.449 -37.183  1.00 74.27           O  
ANISOU 3756  OD1 ASP B 180     9614   9989   8617   -139   1177  -1229       O  
ATOM   3757  OD2 ASP B 180       6.394 -33.425 -38.863  1.00 71.77           O  
ANISOU 3757  OD2 ASP B 180     8913   9696   8662     76   1096  -1189       O  
ATOM   3758  N   SER B 181       2.789 -35.258 -36.268  1.00 68.27           N  
ANISOU 3758  N   SER B 181     9722   6366   9852  -2116  -1132  -1046       N  
ATOM   3759  CA  SER B 181       2.107 -34.807 -35.060  1.00 67.22           C  
ANISOU 3759  CA  SER B 181     9570   6254   9718  -2082  -1142   -969       C  
ATOM   3760  C   SER B 181       2.442 -33.360 -34.727  1.00 67.47           C  
ANISOU 3760  C   SER B 181     9576   6246   9814  -2122  -1024   -992       C  
ATOM   3761  O   SER B 181       1.657 -32.670 -34.081  1.00 67.50           O  
ANISOU 3761  O   SER B 181     9598   6240   9811  -2106  -1017   -902       O  
ATOM   3762  CB  SER B 181       2.486 -35.696 -33.877  1.00 66.62           C  
ANISOU 3762  CB  SER B 181     9436   6237   9641  -2034  -1196  -1018       C  
ATOM   3763  OG  SER B 181       3.853 -35.536 -33.541  1.00 66.99           O  
ANISOU 3763  OG  SER B 181     9415   6294   9746  -2065  -1124  -1165       O  
ATOM   3764  N   LYS B 182       3.606 -32.904 -35.178  1.00 68.15           N  
ANISOU 3764  N   LYS B 182     9618   6300   9977  -2173   -928  -1115       N  
ATOM   3765  CA  LYS B 182       4.107 -31.591 -34.789  1.00 68.64           C  
ANISOU 3765  CA  LYS B 182     9634   6319  10128  -2209   -817  -1159       C  
ATOM   3766  C   LYS B 182       3.500 -30.440 -35.599  1.00 68.85           C  
ANISOU 3766  C   LYS B 182     9730   6271  10159  -2237   -769  -1058       C  
ATOM   3767  O   LYS B 182       3.887 -29.286 -35.425  1.00 69.70           O  
ANISOU 3767  O   LYS B 182     9802   6328  10352  -2263   -684  -1078       O  
ATOM   3768  CB  LYS B 182       5.640 -31.557 -34.863  1.00 70.28           C  
ANISOU 3768  CB  LYS B 182     9750   6512  10443  -2256   -732  -1339       C  
ATOM   3769  CG  LYS B 182       6.332 -32.586 -33.973  1.00 70.91           C  
ANISOU 3769  CG  LYS B 182     9793   6673  10476  -2249   -770  -1432       C  
ATOM   3770  CD  LYS B 182       7.836 -32.349 -33.878  1.00 72.19           C  
ANISOU 3770  CD  LYS B 182     9911   6865  10654  -2299   -675  -1555       C  
ATOM   3771  CE  LYS B 182       8.154 -31.018 -33.207  1.00 72.18           C  
ANISOU 3771  CE  LYS B 182     9890   6854  10680  -2324   -584  -1558       C  
ATOM   3772  NZ  LYS B 182       9.617 -30.768 -33.036  1.00 72.78           N  
ANISOU 3772  NZ  LYS B 182    10077   6961  10614  -2451   -543  -1598       N  
ATOM   3773  N   LEU B 183       2.547 -30.752 -36.472  1.00 68.00           N  
ANISOU 3773  N   LEU B 183     9730   6154   9953  -2233   -831   -944       N  
ATOM   3774  CA  LEU B 183       1.915 -29.728 -37.299  1.00 67.68           C  
ANISOU 3774  CA  LEU B 183     9792   6048   9876  -2268   -792   -838       C  
ATOM   3775  C   LEU B 183       0.435 -29.602 -36.976  1.00 65.25           C  
ANISOU 3775  C   LEU B 183     9544   5759   9491  -2233   -858   -685       C  
ATOM   3776  O   LEU B 183      -0.213 -28.621 -37.338  1.00 64.87           O  
ANISOU 3776  O   LEU B 183     9567   5663   9416  -2253   -821   -589       O  
ATOM   3777  CB  LEU B 183       2.096 -30.054 -38.780  1.00 69.44           C  
ANISOU 3777  CB  LEU B 183    10124   6221  10037  -2308   -802   -839       C  
ATOM   3778  CG  LEU B 183       3.525 -30.338 -39.237  1.00 71.10           C  
ANISOU 3778  CG  LEU B 183    10284   6399  10330  -2342   -745   -987       C  
ATOM   3779  CD1 LEU B 183       3.589 -30.543 -40.745  1.00 72.47           C  
ANISOU 3779  CD1 LEU B 183    10618   6508  10410  -2388   -739   -970       C  
ATOM   3780  CD2 LEU B 183       4.449 -29.216 -38.811  1.00 71.65           C  
ANISOU 3780  CD2 LEU B 183    10263   6421  10539  -2369   -643  -1051       C  
ATOM   3781  N   MET B 184      -0.091 -30.606 -36.286  1.00 63.49           N  
ANISOU 3781  N   MET B 184     9290   5597   9238  -2181   -955   -662       N  
ATOM   3782  CA  MET B 184      -1.505 -30.646 -35.944  1.00 61.92           C  
ANISOU 3782  CA  MET B 184     9128   5406   8991  -2144  -1029   -522       C  
ATOM   3783  C   MET B 184      -1.770 -29.911 -34.637  1.00 60.73           C  
ANISOU 3783  C   MET B 184     8929   5260   8886  -2123   -973   -497       C  
ATOM   3784  O   MET B 184      -0.899 -29.838 -33.773  1.00 61.12           O  
ANISOU 3784  O   MET B 184     8909   5327   8985  -2118   -925   -594       O  
ATOM   3785  CB  MET B 184      -1.972 -32.094 -35.805  1.00 60.96           C  
ANISOU 3785  CB  MET B 184     8999   5334   8829  -2098  -1160   -501       C  
ATOM   3786  CG  MET B 184      -1.120 -33.101 -36.553  1.00 60.95           C  
ANISOU 3786  CG  MET B 184     8999   5351   8809  -2106  -1198   -597       C  
ATOM   3787  SD  MET B 184      -1.196 -32.897 -38.337  1.00107.58           S  
ANISOU 3787  SD  MET B 184    15034  11191  14649  -2158  -1212   -570       S  
ATOM   3788  CE  MET B 184      -2.855 -33.471 -38.660  1.00 91.12           C  
ANISOU 3788  CE  MET B 184    13019   9106  12497  -2120  -1372   -413       C  
ATOM   3789  N   SER B 185      -2.975 -29.369 -34.497  1.00 59.39           N  
ANISOU 3789  N   SER B 185     8800   5066   8700  -2109   -984   -370       N  
ATOM   3790  CA  SER B 185      -3.397 -28.769 -33.237  1.00 58.39           C  
ANISOU 3790  CA  SER B 185     8642   4934   8609  -2084   -937   -334       C  
ATOM   3791  C   SER B 185      -4.890 -28.991 -33.018  1.00 58.11           C  
ANISOU 3791  C   SER B 185     8634   4890   8556  -2049  -1002   -199       C  
ATOM   3792  O   SER B 185      -5.591 -29.434 -33.922  1.00 46.72           O  
ANISOU 3792  O   SER B 185     7230   3441   7081  -2050  -1085   -131       O  
ATOM   3793  CB  SER B 185      -3.055 -27.282 -33.198  1.00 58.41           C  
ANISOU 3793  CB  SER B 185     8649   4888   8654  -2116   -813   -343       C  
ATOM   3794  OG  SER B 185      -3.493 -26.630 -34.372  1.00 59.09           O  
ANISOU 3794  OG  SER B 185     8807   4931   8714  -2148   -795   -271       O  
ATOM   3795  N   ALA B 186      -5.366 -28.694 -31.814  1.00 58.10           N  
ANISOU 3795  N   ALA B 186     8613   4879   8585  -2020   -968   -163       N  
ATOM   3796  CA  ALA B 186      -6.771 -28.891 -31.475  1.00 58.35           C  
ANISOU 3796  CA  ALA B 186     8653   4892   8626  -1989  -1009    -43       C  
ATOM   3797  C   ALA B 186      -7.116 -28.126 -30.212  1.00 45.88           C  
ANISOU 3797  C   ALA B 186     7068   3279   7086  -1969   -919    -14       C  
ATOM   3798  O   ALA B 186      -6.266 -27.952 -29.348  1.00 45.75           O  
ANISOU 3798  O   ALA B 186     7040   3268   7076  -1966   -874    -95       O  
ATOM   3799  CB  ALA B 186      -7.067 -30.366 -31.284  1.00 45.81           C  
ANISOU 3799  CB  ALA B 186     7046   3338   7023  -1957  -1124    -38       C  
ATOM   3800  N   ALA B 187      -8.364 -27.680 -30.101  1.00 54.00           N  
ANISOU 3800  N   ALA B 187     8106   4266   8144  -1954   -897     99       N  
ATOM   3801  CA  ALA B 187      -8.807 -27.003 -28.882  1.00 55.08           C  
ANISOU 3801  CA  ALA B 187     8247   4361   8321  -1930   -802    134       C  
ATOM   3802  C   ALA B 187     -10.323 -26.929 -28.746  1.00 56.29           C  
ANISOU 3802  C   ALA B 187     8397   4470   8521  -1905   -791    259       C  
ATOM   3803  O   ALA B 187     -11.039 -26.925 -29.738  1.00 56.60           O  
ANISOU 3803  O   ALA B 187     8432   4502   8570  -1912   -843    327       O  
ATOM   3804  CB  ALA B 187      -8.213 -25.609 -28.804  1.00 55.71           C  
ANISOU 3804  CB  ALA B 187     8342   4412   8415  -1952   -691    102       C  
ATOM   3805  N   ILE B 188     -10.803 -26.862 -27.508  1.00 57.52           N  
ANISOU 3805  N   ILE B 188     8556   4587   8712  -1875   -723    289       N  
ATOM   3806  CA  ILE B 188     -12.225 -26.662 -27.245  1.00 59.30           C  
ANISOU 3806  CA  ILE B 188     8772   4758   9001  -1850   -674    401       C  
ATOM   3807  C   ILE B 188     -12.431 -25.564 -26.209  1.00 61.05           C  
ANISOU 3807  C   ILE B 188     9021   4917   9258  -1831   -522    425       C  
ATOM   3808  O   ILE B 188     -11.809 -25.578 -25.147  1.00 60.53           O  
ANISOU 3808  O   ILE B 188     8982   4839   9177  -1819   -484    370       O  
ATOM   3809  CB  ILE B 188     -12.912 -27.949 -26.749  1.00 59.31           C  
ANISOU 3809  CB  ILE B 188     8751   4755   9028  -1825   -733    434       C  
ATOM   3810  CG1 ILE B 188     -12.819 -29.033 -27.810  1.00 59.56           C  
ANISOU 3810  CG1 ILE B 188     8753   4842   9035  -1839   -890    421       C  
ATOM   3811  CG2 ILE B 188     -14.367 -27.687 -26.410  1.00 47.08           C  
ANISOU 3811  CG2 ILE B 188     7186   3139   7562  -1802   -658    544       C  
ATOM   3812  CD1 ILE B 188     -13.755 -30.183 -27.593  1.00 60.38           C  
ANISOU 3812  CD1 ILE B 188     8821   4932   9188  -1818   -955    476       C  
ATOM   3813  N   LYS B 189     -13.299 -24.610 -26.529  1.00 63.82           N  
ANISOU 3813  N   LYS B 189     9370   5222   9655  -1825   -445    507       N  
ATOM   3814  CA  LYS B 189     -13.691 -23.579 -25.579  1.00 66.73           C  
ANISOU 3814  CA  LYS B 189     9765   5521  10070  -1798   -290    545       C  
ATOM   3815  C   LYS B 189     -15.020 -22.985 -26.022  1.00 69.58           C  
ANISOU 3815  C   LYS B 189    10117   5832  10488  -1785   -233    654       C  
ATOM   3816  O   LYS B 189     -15.282 -22.871 -27.220  1.00 69.73           O  
ANISOU 3816  O   LYS B 189    10120   5871  10503  -1804   -312    686       O  
ATOM   3817  CB  LYS B 189     -12.619 -22.490 -25.477  1.00 67.04           C  
ANISOU 3817  CB  LYS B 189     9824   5561  10088  -1814   -237    480       C  
ATOM   3818  CG  LYS B 189     -12.776 -21.558 -24.273  1.00 67.87           C  
ANISOU 3818  CG  LYS B 189     9951   5594  10241  -1781   -102    503       C  
ATOM   3819  CD  LYS B 189     -11.595 -20.597 -24.151  1.00 68.14           C  
ANISOU 3819  CD  LYS B 189     9995   5634  10261  -1800    -90    428       C  
ATOM   3820  CE  LYS B 189     -11.844 -19.526 -23.096  1.00 69.18           C  
ANISOU 3820  CE  LYS B 189    10141   5689  10453  -1764     19    470       C  
ATOM   3821  NZ  LYS B 189     -12.091 -20.103 -21.750  1.00 69.74           N  
ANISOU 3821  NZ  LYS B 189    10244   5719  10537  -1725     33    479       N  
ATOM   3822  N   ASP B 190     -15.855 -22.634 -25.047  1.00 72.53           N  
ANISOU 3822  N   ASP B 190    10511   6133  10914  -1750    -99    712       N  
ATOM   3823  CA  ASP B 190     -17.160 -22.030 -25.302  1.00 75.44           C  
ANISOU 3823  CA  ASP B 190    10886   6444  11334  -1735    -30    812       C  
ATOM   3824  C   ASP B 190     -18.040 -22.913 -26.184  1.00 77.20           C  
ANISOU 3824  C   ASP B 190    11055   6687  11589  -1745   -174    868       C  
ATOM   3825  O   ASP B 190     -18.772 -22.416 -27.039  1.00 77.87           O  
ANISOU 3825  O   ASP B 190    11122   6755  11712  -1747   -217    936       O  
ATOM   3826  CB  ASP B 190     -16.995 -20.634 -25.913  1.00 76.36           C  
ANISOU 3826  CB  ASP B 190    11021   6543  11448  -1742     25    828       C  
ATOM   3827  CG  ASP B 190     -16.097 -19.735 -25.079  1.00 76.82           C  
ANISOU 3827  CG  ASP B 190    11098   6580  11511  -1729    142    776       C  
ATOM   3828  OD1 ASP B 190     -16.103 -19.871 -23.837  1.00 77.05           O  
ANISOU 3828  OD1 ASP B 190    11139   6567  11570  -1697    227    769       O  
ATOM   3829  OD2 ASP B 190     -15.385 -18.891 -25.663  1.00 77.00           O  
ANISOU 3829  OD2 ASP B 190    11116   6619  11523  -1747    135    749       O  
ATOM   3830  N   ASN B 191     -17.965 -24.222 -25.952  1.00 78.18           N  
ANISOU 3830  N   ASN B 191    11149   6842  11714  -1747   -260    843       N  
ATOM   3831  CA  ASN B 191     -18.658 -25.219 -26.770  1.00 79.38           C  
ANISOU 3831  CA  ASN B 191    11229   7017  11915  -1754   -421    886       C  
ATOM   3832  C   ASN B 191     -18.419 -25.035 -28.268  1.00 79.42           C  
ANISOU 3832  C   ASN B 191    11210   7065  11903  -1777   -571    889       C  
ATOM   3833  O   ASN B 191     -19.352 -25.081 -29.068  1.00 80.33           O  
ANISOU 3833  O   ASN B 191    11275   7158  12089  -1774   -670    964       O  
ATOM   3834  CB  ASN B 191     -20.161 -25.274 -26.450  1.00 80.70           C  
ANISOU 3834  CB  ASN B 191    11362   7114  12187  -1732   -381    986       C  
ATOM   3835  CG  ASN B 191     -20.458 -25.946 -25.112  1.00 80.47           C  
ANISOU 3835  CG  ASN B 191    11365   7042  12169  -1716   -272    984       C  
ATOM   3836  OD1 ASN B 191     -19.738 -26.844 -24.676  1.00 79.55           O  
ANISOU 3836  OD1 ASN B 191    11262   6957  12008  -1719   -298    921       O  
ATOM   3837  ND2 ASN B 191     -21.530 -25.514 -24.462  1.00 81.09           N  
ANISOU 3837  ND2 ASN B 191    11468   7042  12301  -1700   -154   1057       N  
ATOM   3838  N   ARG B 192     -17.160 -24.806 -28.627  1.00 78.66           N  
ANISOU 3838  N   ARG B 192    11152   7018  11716  -1801   -588    807       N  
ATOM   3839  CA  ARG B 192     -16.748 -24.725 -30.023  1.00 78.49           C  
ANISOU 3839  CA  ARG B 192    11139   7031  11653  -1829   -718    797       C  
ATOM   3840  C   ARG B 192     -15.391 -25.394 -30.199  1.00 75.51           C  
ANISOU 3840  C   ARG B 192    10782   6723  11185  -1855   -778    689       C  
ATOM   3841  O   ARG B 192     -14.363 -24.840 -29.822  1.00 74.68           O  
ANISOU 3841  O   ARG B 192    10712   6634  11030  -1867   -693    617       O  
ATOM   3842  CB  ARG B 192     -16.694 -23.272 -30.501  1.00 81.13           C  
ANISOU 3842  CB  ARG B 192    11519   7330  11976  -1836   -639    824       C  
ATOM   3843  CG  ARG B 192     -18.055 -22.600 -30.607  1.00 84.38           C  
ANISOU 3843  CG  ARG B 192    11912   7672  12477  -1810   -612    935       C  
ATOM   3844  CD  ARG B 192     -17.937 -21.146 -31.034  1.00 86.93           C  
ANISOU 3844  CD  ARG B 192    12291   7956  12781  -1813   -526    960       C  
ATOM   3845  NE  ARG B 192     -19.218 -20.451 -30.935  1.00 89.54           N  
ANISOU 3845  NE  ARG B 192    12608   8215  13199  -1781   -482   1063       N  
ATOM   3846  CZ  ARG B 192     -19.412 -19.177 -31.259  1.00 91.17           C  
ANISOU 3846  CZ  ARG B 192    12862   8372  13407  -1773   -408   1106       C  
ATOM   3847  NH1 ARG B 192     -18.409 -18.441 -31.712  1.00 91.12           N  
ANISOU 3847  NH1 ARG B 192    12918   8378  13327  -1796   -363   1059       N  
ATOM   3848  NH2 ARG B 192     -20.617 -18.639 -31.131  1.00 92.53           N  
ANISOU 3848  NH2 ARG B 192    13016   8476  13663  -1741   -381   1199       N  
ATOM   3849  N   ALA B 193     -15.401 -26.594 -30.765  1.00 73.89           N  
ANISOU 3849  N   ALA B 193    10550   6555  10969  -1861   -930    678       N  
ATOM   3850  CA  ALA B 193     -14.179 -27.362 -30.967  1.00 71.97           C  
ANISOU 3850  CA  ALA B 193    10326   6376  10644  -1881   -994    577       C  
ATOM   3851  C   ALA B 193     -13.526 -26.986 -32.284  1.00 71.01           C  
ANISOU 3851  C   ALA B 193    10253   6270  10458  -1915  -1055    549       C  
ATOM   3852  O   ALA B 193     -14.199 -26.574 -33.216  1.00 72.03           O  
ANISOU 3852  O   ALA B 193    10401   6364  10604  -1921  -1115    620       O  
ATOM   3853  CB  ALA B 193     -14.486 -28.845 -30.950  1.00 71.97           C  
ANISOU 3853  CB  ALA B 193    10283   6401  10659  -1868  -1119    577       C  
ATOM   3854  N   VAL B 194     -12.210 -27.137 -32.356  1.00 69.35           N  
ANISOU 3854  N   VAL B 194    10069   6103  10176  -1938  -1040    446       N  
ATOM   3855  CA  VAL B 194     -11.475 -26.906 -33.591  1.00 68.48           C  
ANISOU 3855  CA  VAL B 194    10016   6002  10001  -1976  -1082    408       C  
ATOM   3856  C   VAL B 194     -10.329 -27.895 -33.708  1.00 67.53           C  
ANISOU 3856  C   VAL B 194     9895   5939   9826  -1989  -1131    300       C  
ATOM   3857  O   VAL B 194      -9.539 -28.051 -32.776  1.00 67.21           O  
ANISOU 3857  O   VAL B 194     9825   5928   9785  -1983  -1067    221       O  
ATOM   3858  CB  VAL B 194     -10.889 -25.478 -33.662  1.00 68.37           C  
ANISOU 3858  CB  VAL B 194    10043   5958   9975  -2000   -946    388       C  
ATOM   3859  CG1 VAL B 194      -9.775 -25.413 -34.690  1.00 68.40           C  
ANISOU 3859  CG1 VAL B 194    10104   5974   9910  -2045   -958    314       C  
ATOM   3860  CG2 VAL B 194     -11.963 -24.465 -33.990  1.00 69.03           C  
ANISOU 3860  CG2 VAL B 194    10150   5980  10097  -1991   -918    499       C  
ATOM   3861  N   HIS B 195     -10.254 -28.568 -34.852  1.00 66.81           N  
ANISOU 3861  N   HIS B 195     9840   5856   9690  -2004  -1251    296       N  
ATOM   3862  CA  HIS B 195      -9.074 -29.348 -35.195  1.00 65.52           C  
ANISOU 3862  CA  HIS B 195     9687   5737   9471  -2021  -1280    189       C  
ATOM   3863  C   HIS B 195      -8.318 -28.648 -36.319  1.00 66.12           C  
ANISOU 3863  C   HIS B 195     9844   5787   9492  -2068  -1242    152       C  
ATOM   3864  O   HIS B 195      -8.830 -28.510 -37.428  1.00 66.63           O  
ANISOU 3864  O   HIS B 195     9986   5810   9521  -2084  -1317    213       O  
ATOM   3865  CB  HIS B 195      -9.461 -30.769 -35.603  1.00 63.92           C  
ANISOU 3865  CB  HIS B 195     9474   5558   9254  -2000  -1435    201       C  
ATOM   3866  CG  HIS B 195     -10.056 -31.571 -34.490  1.00 62.12           C  
ANISOU 3866  CG  HIS B 195     9173   5351   9080  -1958  -1462    226       C  
ATOM   3867  ND1 HIS B 195     -11.351 -31.388 -34.050  1.00 61.67           N  
ANISOU 3867  ND1 HIS B 195     9080   5258   9094  -1936  -1473    328       N  
ATOM   3868  CD2 HIS B 195      -9.533 -32.556 -33.722  1.00 60.92           C  
ANISOU 3868  CD2 HIS B 195     8982   5243   8923  -1936  -1473    162       C  
ATOM   3869  CE1 HIS B 195     -11.599 -32.229 -33.061  1.00 60.89           C  
ANISOU 3869  CE1 HIS B 195     8930   5176   9031  -1906  -1480    327       C  
ATOM   3870  NE2 HIS B 195     -10.513 -32.948 -32.842  1.00 60.44           N  
ANISOU 3870  NE2 HIS B 195     8876   5167   8923  -1904  -1487    229       N  
ATOM   3871  N   ALA B 196      -7.102 -28.200 -36.027  1.00 66.35           N  
ANISOU 3871  N   ALA B 196     9860   5829   9520  -2092  -1128     51       N  
ATOM   3872  CA  ALA B 196      -6.338 -27.397 -36.974  1.00 67.41           C  
ANISOU 3872  CA  ALA B 196    10066   5925   9620  -2142  -1057     14       C  
ATOM   3873  C   ALA B 196      -5.083 -28.080 -37.501  1.00 67.54           C  
ANISOU 3873  C   ALA B 196    10090   5963   9608  -2170  -1057   -106       C  
ATOM   3874  O   ALA B 196      -4.579 -29.036 -36.916  1.00 66.90           O  
ANISOU 3874  O   ALA B 196     9938   5936   9545  -2147  -1088   -181       O  
ATOM   3875  CB  ALA B 196      -5.985 -26.055 -36.364  1.00 67.74           C  
ANISOU 3875  CB  ALA B 196    10088   5941   9710  -2156   -906      3       C  
ATOM   3876  N   ASP B 197      -4.581 -27.549 -38.609  1.00 58.04           N  
ANISOU 3876  N   ASP B 197     8117   6617   7317  -1444   -773   -273       N  
ATOM   3877  CA  ASP B 197      -3.395 -28.056 -39.274  1.00 59.20           C  
ANISOU 3877  CA  ASP B 197     8158   6964   7371  -1409   -739   -239       C  
ATOM   3878  C   ASP B 197      -2.808 -26.879 -40.037  1.00 59.82           C  
ANISOU 3878  C   ASP B 197     8221   7082   7426  -1603   -725   -224       C  
ATOM   3879  O   ASP B 197      -3.107 -25.727 -39.724  1.00 60.18           O  
ANISOU 3879  O   ASP B 197     8338   7014   7512  -1762   -750   -250       O  
ATOM   3880  CB  ASP B 197      -3.785 -29.176 -40.237  1.00 59.25           C  
ANISOU 3880  CB  ASP B 197     8242   6899   7371  -1249   -717   -208       C  
ATOM   3881  CG  ASP B 197      -2.592 -29.961 -40.750  1.00 60.76           C  
ANISOU 3881  CG  ASP B 197     8337   7300   7451  -1129   -660   -181       C  
ATOM   3882  OD1 ASP B 197      -1.537 -29.349 -41.020  1.00 62.44           O  
ANISOU 3882  OD1 ASP B 197     8412   7712   7599  -1223   -628   -164       O  
ATOM   3883  OD2 ASP B 197      -2.713 -31.192 -40.904  1.00 60.16           O  
ANISOU 3883  OD2 ASP B 197     8327   7188   7342   -940   -642   -174       O  
ATOM   3884  N   MET B 198      -1.980 -27.160 -41.036  1.00 60.63           N  
ANISOU 3884  N   MET B 198     8252   7333   7451  -1589   -674   -180       N  
ATOM   3885  CA  MET B 198      -1.425 -26.111 -41.875  1.00 62.05           C  
ANISOU 3885  CA  MET B 198     8426   7556   7593  -1790   -645   -145       C  
ATOM   3886  C   MET B 198      -2.282 -25.931 -43.117  1.00 61.54           C  
ANISOU 3886  C   MET B 198     8540   7282   7560  -1779   -643   -110       C  
ATOM   3887  O   MET B 198      -2.243 -24.886 -43.760  1.00 62.20           O  
ANISOU 3887  O   MET B 198     8703   7295   7636  -1950   -637    -73       O  
ATOM   3888  CB  MET B 198       0.015 -26.431 -42.278  1.00 64.02           C  
ANISOU 3888  CB  MET B 198     8467   8136   7720  -1796   -575   -106       C  
ATOM   3889  CG  MET B 198       0.988 -26.619 -41.118  1.00 65.38           C  
ANISOU 3889  CG  MET B 198     8418   8584   7840  -1802   -593   -124       C  
ATOM   3890  SD  MET B 198       1.123 -25.189 -40.024  1.00 45.99           S  
ANISOU 3890  SD  MET B 198     5966   6105   5405  -2124   -670   -173       S  
ATOM   3891  CE  MET B 198       1.276 -23.881 -41.228  1.00 47.13           C  
ANISOU 3891  CE  MET B 198     6218   6153   5538  -2413   -629   -125       C  
ATOM   3892  N   GLY B 199      -3.055 -26.959 -43.447  1.00 60.46           N  
ANISOU 3892  N   GLY B 199     8481   7045   7446  -1589   -655   -115       N  
ATOM   3893  CA  GLY B 199      -3.953 -26.906 -44.585  1.00 59.69           C  
ANISOU 3893  CA  GLY B 199     8545   6769   7365  -1573   -679    -84       C  
ATOM   3894  C   GLY B 199      -5.382 -27.225 -44.195  1.00 57.88           C  
ANISOU 3894  C   GLY B 199     8413   6336   7241  -1490   -754   -107       C  
ATOM   3895  O   GLY B 199      -6.303 -27.056 -44.991  1.00 57.31           O  
ANISOU 3895  O   GLY B 199     8457   6123   7197  -1489   -803    -78       O  
ATOM   3896  N   TYR B 200      -5.567 -27.691 -42.964  1.00 56.82           N  
ANISOU 3896  N   TYR B 200     8220   6213   7157  -1426   -765   -149       N  
ATOM   3897  CA  TYR B 200      -6.898 -28.018 -42.468  1.00 55.03           C  
ANISOU 3897  CA  TYR B 200     8052   5833   7024  -1365   -819   -164       C  
ATOM   3898  C   TYR B 200      -7.361 -27.002 -41.432  1.00 55.01           C  
ANISOU 3898  C   TYR B 200     8040   5760   7101  -1427   -834   -190       C  
ATOM   3899  O   TYR B 200      -6.554 -26.384 -40.746  1.00 55.13           O  
ANISOU 3899  O   TYR B 200     8003   5854   7088  -1507   -811   -218       O  
ATOM   3900  CB  TYR B 200      -6.926 -29.417 -41.844  1.00 54.12           C  
ANISOU 3900  CB  TYR B 200     7918   5755   6891  -1237   -808   -184       C  
ATOM   3901  CG  TYR B 200      -6.901 -30.574 -42.825  1.00 54.34           C  
ANISOU 3901  CG  TYR B 200     8032   5765   6849  -1147   -802   -174       C  
ATOM   3902  CD1 TYR B 200      -6.395 -30.424 -44.107  1.00 55.37           C  
ANISOU 3902  CD1 TYR B 200     8205   5933   6899  -1161   -780   -156       C  
ATOM   3903  CD2 TYR B 200      -7.397 -31.820 -42.465  1.00 54.16           C  
ANISOU 3903  CD2 TYR B 200     8080   5673   6826  -1057   -813   -184       C  
ATOM   3904  CE1 TYR B 200      -6.374 -31.483 -44.999  1.00 55.77           C  
ANISOU 3904  CE1 TYR B 200     8372   5955   6864  -1070   -769   -165       C  
ATOM   3905  CE2 TYR B 200      -7.383 -32.881 -43.352  1.00 54.61           C  
ANISOU 3905  CE2 TYR B 200     8270   5675   6804   -984   -809   -190       C  
ATOM   3906  CZ  TYR B 200      -6.870 -32.706 -44.617  1.00 55.10           C  
ANISOU 3906  CZ  TYR B 200     8378   5776   6780   -982   -787   -188       C  
ATOM   3907  OH  TYR B 200      -6.852 -33.754 -45.504  1.00 55.33           O  
ANISOU 3907  OH  TYR B 200     8573   5740   6709   -901   -778   -211       O  
ATOM   3908  N   TRP B 201      -8.671 -26.829 -41.334  1.00 55.40           N  
ANISOU 3908  N   TRP B 201     8140   5672   7238  -1390   -875   -184       N  
ATOM   3909  CA  TRP B 201      -9.256 -26.075 -40.235  1.00 56.50           C  
ANISOU 3909  CA  TRP B 201     8279   5745   7444  -1392   -870   -220       C  
ATOM   3910  C   TRP B 201     -10.698 -26.525 -40.041  1.00 56.31           C  
ANISOU 3910  C   TRP B 201     8243   5653   7500  -1302   -897   -204       C  
ATOM   3911  O   TRP B 201     -11.576 -26.163 -40.817  1.00 57.19           O  
ANISOU 3911  O   TRP B 201     8385   5685   7658  -1280   -943   -160       O  
ATOM   3912  CB  TRP B 201      -9.198 -24.575 -40.505  1.00 58.16           C  
ANISOU 3912  CB  TRP B 201     8582   5847   7669  -1474   -874   -217       C  
ATOM   3913  CG  TRP B 201      -9.868 -23.767 -39.440  1.00 59.52           C  
ANISOU 3913  CG  TRP B 201     8798   5921   7898  -1442   -859   -266       C  
ATOM   3914  CD1 TRP B 201     -11.155 -23.315 -39.442  1.00 60.00           C  
ANISOU 3914  CD1 TRP B 201     8899   5860   8038  -1334   -873   -249       C  
ATOM   3915  CD2 TRP B 201      -9.286 -23.319 -38.210  1.00 60.53           C  
ANISOU 3915  CD2 TRP B 201     8935   6077   7988  -1504   -824   -345       C  
ATOM   3916  NE1 TRP B 201     -11.407 -22.609 -38.293  1.00 60.94           N  
ANISOU 3916  NE1 TRP B 201     9066   5917   8172  -1304   -830   -317       N  
ATOM   3917  CE2 TRP B 201     -10.277 -22.599 -37.518  1.00 61.20           C  
ANISOU 3917  CE2 TRP B 201     9096   6029   8127  -1421   -805   -383       C  
ATOM   3918  CE3 TRP B 201      -8.022 -23.454 -37.630  1.00 60.87           C  
ANISOU 3918  CE3 TRP B 201     8920   6264   7943  -1616   -813   -386       C  
ATOM   3919  CZ2 TRP B 201     -10.041 -22.015 -36.273  1.00 62.12           C  
ANISOU 3919  CZ2 TRP B 201     9274   6126   8204  -1457   -769   -475       C  
ATOM   3920  CZ3 TRP B 201      -7.792 -22.877 -36.394  1.00 61.58           C  
ANISOU 3920  CZ3 TRP B 201     9048   6353   7995  -1673   -799   -469       C  
ATOM   3921  CH2 TRP B 201      -8.793 -22.165 -35.731  1.00 62.25           C  
ANISOU 3921  CH2 TRP B 201     9249   6277   8126  -1599   -775   -520       C  
ATOM   3922  N   ILE B 202     -10.939 -27.311 -38.998  1.00 55.22           N  
ANISOU 3922  N   ILE B 202     8047   5566   7367  -1258   -870   -228       N  
ATOM   3923  CA  ILE B 202     -12.217 -27.999 -38.856  1.00 54.57           C  
ANISOU 3923  CA  ILE B 202     7927   5462   7343  -1211   -886   -200       C  
ATOM   3924  C   ILE B 202     -12.980 -27.587 -37.599  1.00 53.84           C  
ANISOU 3924  C   ILE B 202     7787   5372   7299  -1166   -838   -226       C  
ATOM   3925  O   ILE B 202     -12.605 -27.953 -36.485  1.00 53.43           O  
ANISOU 3925  O   ILE B 202     7719   5378   7204  -1160   -789   -260       O  
ATOM   3926  CB  ILE B 202     -12.007 -29.519 -38.887  1.00 55.01           C  
ANISOU 3926  CB  ILE B 202     7992   5560   7350  -1207   -889   -184       C  
ATOM   3927  CG1 ILE B 202     -11.130 -29.888 -40.085  1.00 55.18           C  
ANISOU 3927  CG1 ILE B 202     8078   5586   7300  -1218   -912   -174       C  
ATOM   3928  CG2 ILE B 202     -13.336 -30.245 -38.956  1.00 55.43           C  
ANISOU 3928  CG2 ILE B 202     8020   5586   7454  -1222   -920   -145       C  
ATOM   3929  CD1 ILE B 202     -10.600 -31.296 -40.059  1.00 55.52           C  
ANISOU 3929  CD1 ILE B 202     8175   5652   7269  -1174   -895   -174       C  
ATOM   3930  N   GLU B 203     -14.061 -26.833 -37.794  1.00 54.07           N  
ANISOU 3930  N   GLU B 203     7792   5349   7401  -1115   -850   -206       N  
ATOM   3931  CA  GLU B 203     -14.835 -26.292 -36.681  1.00 54.89           C  
ANISOU 3931  CA  GLU B 203     7853   5460   7541  -1036   -784   -236       C  
ATOM   3932  C   GLU B 203     -16.073 -27.110 -36.349  1.00 55.90           C  
ANISOU 3932  C   GLU B 203     7852   5673   7714  -1010   -769   -189       C  
ATOM   3933  O   GLU B 203     -16.853 -27.473 -37.233  1.00 56.59           O  
ANISOU 3933  O   GLU B 203     7872   5783   7847  -1024   -835   -123       O  
ATOM   3934  CB  GLU B 203     -15.273 -24.854 -36.964  1.00 55.48           C  
ANISOU 3934  CB  GLU B 203     7987   5430   7663   -952   -785   -243       C  
ATOM   3935  CG  GLU B 203     -14.150 -23.858 -37.115  1.00 55.52           C  
ANISOU 3935  CG  GLU B 203     8146   5329   7619  -1013   -786   -292       C  
ATOM   3936  CD  GLU B 203     -14.658 -22.480 -37.483  1.00 57.21           C  
ANISOU 3936  CD  GLU B 203     8473   5391   7874   -923   -789   -284       C  
ATOM   3937  OE1 GLU B 203     -13.937 -21.744 -38.191  1.00 57.79           O  
ANISOU 3937  OE1 GLU B 203     8683   5357   7918   -999   -821   -275       O  
ATOM   3938  OE2 GLU B 203     -15.779 -22.131 -37.061  1.00 58.33           O  
ANISOU 3938  OE2 GLU B 203     8572   5523   8069   -766   -753   -280       O  
ATOM   3939  N   SER B 204     -16.252 -27.358 -35.057  1.00 56.49           N  
ANISOU 3939  N   SER B 204     7891   5810   7764   -988   -682   -219       N  
ATOM   3940  CA  SER B 204     -17.428 -28.020 -34.529  1.00 58.41           C  
ANISOU 3940  CA  SER B 204     8002   6156   8037   -981   -638   -170       C  
ATOM   3941  C   SER B 204     -18.004 -27.155 -33.421  1.00 60.35           C  
ANISOU 3941  C   SER B 204     8209   6437   8283   -859   -528   -216       C  
ATOM   3942  O   SER B 204     -17.322 -26.279 -32.902  1.00 60.40           O  
ANISOU 3942  O   SER B 204     8334   6371   8244   -810   -491   -298       O  
ATOM   3943  CB  SER B 204     -17.044 -29.378 -33.965  1.00 58.69           C  
ANISOU 3943  CB  SER B 204     8060   6234   8006  -1080   -618   -150       C  
ATOM   3944  OG  SER B 204     -16.254 -30.089 -34.894  1.00 58.60           O  
ANISOU 3944  OG  SER B 204     8136   6163   7968  -1152   -701   -134       O  
ATOM   3945  N   ALA B 205     -19.255 -27.403 -33.054  1.00 62.73           N  
ANISOU 3945  N   ALA B 205     8351   6861   8624   -818   -471   -165       N  
ATOM   3946  CA  ALA B 205     -19.911 -26.603 -32.028  1.00 65.23           C  
ANISOU 3946  CA  ALA B 205     8620   7233   8930   -666   -343   -207       C  
ATOM   3947  C   ALA B 205     -21.045 -27.356 -31.345  1.00 67.81           C  
ANISOU 3947  C   ALA B 205     8751   7753   9259   -684   -252   -140       C  
ATOM   3948  O   ALA B 205     -21.319 -28.510 -31.666  1.00 67.09           O  
ANISOU 3948  O   ALA B 205     8579   7732   9180   -845   -299    -58       O  
ATOM   3949  CB  ALA B 205     -20.423 -25.306 -32.624  1.00 66.17           C  
ANISOU 3949  CB  ALA B 205     8738   7285   9117   -488   -357   -218       C  
ATOM   3950  N   LEU B 206     -21.702 -26.683 -30.405  1.00 71.34           N  
ANISOU 3950  N   LEU B 206     9139   8281   9684   -526   -113   -176       N  
ATOM   3951  CA  LEU B 206     -22.840 -27.253 -29.695  1.00 74.89           C  
ANISOU 3951  CA  LEU B 206     9376   8954  10126   -531      4   -107       C  
ATOM   3952  C   LEU B 206     -24.102 -26.435 -29.937  1.00 80.28           C  
ANISOU 3952  C   LEU B 206     9847   9770  10886   -322     58    -72       C  
ATOM   3953  O   LEU B 206     -24.497 -25.619 -29.106  1.00 82.23           O  
ANISOU 3953  O   LEU B 206    10090  10060  11093   -112    204   -132       O  
ATOM   3954  CB  LEU B 206     -22.551 -27.351 -28.192  1.00 73.81           C  
ANISOU 3954  CB  LEU B 206     9330   8855   9858   -515    156   -168       C  
ATOM   3955  CG  LEU B 206     -23.648 -27.900 -27.269  1.00 74.38           C  
ANISOU 3955  CG  LEU B 206     9203   9170   9889   -526    316    -98       C  
ATOM   3956  CD1 LEU B 206     -24.097 -29.272 -27.708  1.00 73.67           C  
ANISOU 3956  CD1 LEU B 206     8971   9184   9836   -774    255     39       C  
ATOM   3957  CD2 LEU B 206     -23.179 -27.942 -25.829  1.00 74.03           C  
ANISOU 3957  CD2 LEU B 206     9305   9137   9685   -509    451   -166       C  
ATOM   3958  N   ASN B 207     -24.723 -26.635 -31.092  1.00 83.58           N  
ANISOU 3958  N   ASN B 207    10097  10257  11401   -362    -64     22       N  
ATOM   3959  CA  ASN B 207     -26.053 -26.101 -31.316  1.00 89.30           C  
ANISOU 3959  CA  ASN B 207    10548  11188  12194   -176    -26     91       C  
ATOM   3960  C   ASN B 207     -27.012 -27.259 -31.144  1.00 88.92           C  
ANISOU 3960  C   ASN B 207    10211  11421  12154   -376     -1    209       C  
ATOM   3961  O   ASN B 207     -26.978 -28.209 -31.924  1.00 88.63           O  
ANISOU 3961  O   ASN B 207    10141  11391  12143   -630   -142    277       O  
ATOM   3962  CB  ASN B 207     -26.179 -25.499 -32.711  1.00 94.63           C  
ANISOU 3962  CB  ASN B 207    11209  11790  12955    -88   -193    133       C  
ATOM   3963  CG  ASN B 207     -27.450 -24.692 -32.880  1.00103.06           C  
ANISOU 3963  CG  ASN B 207    12021  13055  14083    195   -152    199       C  
ATOM   3964  OD1 ASN B 207     -28.092 -24.318 -31.900  1.00105.42           O  
ANISOU 3964  OD1 ASN B 207    12201  13500  14355    384     28    181       O  
ATOM   3965  ND2 ASN B 207     -27.816 -24.415 -34.126  1.00108.62           N  
ANISOU 3965  ND2 ASN B 207    12638  13778  14854    244   -316    279       N  
ATOM   3966  N   ASP B 208     -27.840 -27.193 -30.104  1.00 88.67           N  
ANISOU 3966  N   ASP B 208     9991  11614  12085   -277    187    228       N  
ATOM   3967  CA  ASP B 208     -28.667 -28.322 -29.683  1.00 87.84           C  
ANISOU 3967  CA  ASP B 208     9634  11781  11961   -510    251    339       C  
ATOM   3968  C   ASP B 208     -27.779 -29.501 -29.299  1.00 84.24           C  
ANISOU 3968  C   ASP B 208     9407  11174  11427   -814    228    333       C  
ATOM   3969  O   ASP B 208     -27.724 -29.895 -28.136  1.00 84.59           O  
ANISOU 3969  O   ASP B 208     9495  11274  11373   -864    384    328       O  
ATOM   3970  CB  ASP B 208     -29.669 -28.723 -30.769  1.00 88.86           C  
ANISOU 3970  CB  ASP B 208     9449  12131  12183   -635    109    470       C  
ATOM   3971  CG  ASP B 208     -30.630 -29.801 -30.306  1.00 90.74           C  
ANISOU 3971  CG  ASP B 208     9402  12679  12396   -903    184    592       C  
ATOM   3972  OD1 ASP B 208     -30.886 -30.750 -31.078  1.00 90.58           O  
ANISOU 3972  OD1 ASP B 208     9304  12710  12404  -1218     30    677       O  
ATOM   3973  OD2 ASP B 208     -31.142 -29.694 -29.173  1.00 92.60           O  
ANISOU 3973  OD2 ASP B 208     9503  13109  12573   -813    401    603       O  
ATOM   3974  N   THR B 209     -27.083 -30.057 -30.284  1.00 81.01           N  
ANISOU 3974  N   THR B 209     9157  10574  11048   -994     39    337       N  
ATOM   3975  CA  THR B 209     -26.123 -31.121 -30.038  1.00 78.17           C  
ANISOU 3975  CA  THR B 209     9053  10035  10615  -1222      5    326       C  
ATOM   3976  C   THR B 209     -24.773 -30.795 -30.663  1.00 74.26           C  
ANISOU 3976  C   THR B 209     8846   9251  10118  -1164   -118    231       C  
ATOM   3977  O   THR B 209     -24.657 -29.887 -31.483  1.00 73.65           O  
ANISOU 3977  O   THR B 209     8774   9106  10105  -1016   -203    193       O  
ATOM   3978  CB  THR B 209     -26.615 -32.457 -30.599  1.00 79.35           C  
ANISOU 3978  CB  THR B 209     9127  10246  10776  -1553    -90    438       C  
ATOM   3979  OG1 THR B 209     -26.892 -32.313 -31.998  1.00 79.37           O  
ANISOU 3979  OG1 THR B 209     9048  10245  10865  -1587   -273    460       O  
ATOM   3980  CG2 THR B 209     -27.874 -32.902 -29.878  1.00 82.65           C  
ANISOU 3980  CG2 THR B 209     9258  10968  11176  -1676     45    546       C  
ATOM   3981  N   TRP B 210     -23.752 -31.538 -30.259  1.00 71.91           N  
ANISOU 3981  N   TRP B 210     8785   8799   9738  -1277   -124    206       N  
ATOM   3982  CA  TRP B 210     -22.426 -31.387 -30.834  1.00 69.13           C  
ANISOU 3982  CA  TRP B 210     8674   8220   9372  -1246   -233    131       C  
ATOM   3983  C   TRP B 210     -22.391 -31.943 -32.245  1.00 69.30           C  
ANISOU 3983  C   TRP B 210     8717   8165   9449  -1381   -400    171       C  
ATOM   3984  O   TRP B 210     -22.800 -33.081 -32.481  1.00 70.14           O  
ANISOU 3984  O   TRP B 210     8810   8294   9544  -1590   -440    245       O  
ATOM   3985  CB  TRP B 210     -21.394 -32.127 -29.991  1.00 67.31           C  
ANISOU 3985  CB  TRP B 210     8656   7892   9027  -1308   -194    111       C  
ATOM   3986  CG  TRP B 210     -20.956 -31.387 -28.784  1.00 66.64           C  
ANISOU 3986  CG  TRP B 210     8635   7827   8859  -1160    -77     33       C  
ATOM   3987  CD1 TRP B 210     -21.444 -31.520 -27.521  1.00 67.93           C  
ANISOU 3987  CD1 TRP B 210     8752   8119   8939  -1147     74     52       C  
ATOM   3988  CD2 TRP B 210     -19.923 -30.399 -28.716  1.00 65.14           C  
ANISOU 3988  CD2 TRP B 210     8583   7527   8641  -1026   -103    -81       C  
ATOM   3989  NE1 TRP B 210     -20.782 -30.670 -26.670  1.00 67.64           N  
ANISOU 3989  NE1 TRP B 210     8831   8054   8816  -1002    137    -55       N  
ATOM   3990  CE2 TRP B 210     -19.842 -29.971 -27.381  1.00 65.85           C  
ANISOU 3990  CE2 TRP B 210     8717   7678   8624   -941     24   -138       C  
ATOM   3991  CE3 TRP B 210     -19.061 -29.832 -29.658  1.00 63.52           C  
ANISOU 3991  CE3 TRP B 210     8472   7185   8476   -993   -219   -137       C  
ATOM   3992  CZ2 TRP B 210     -18.930 -29.002 -26.963  1.00 65.15           C  
ANISOU 3992  CZ2 TRP B 210     8774   7510   8471   -842     22   -259       C  
ATOM   3993  CZ3 TRP B 210     -18.158 -28.871 -29.242  1.00 62.85           C  
ANISOU 3993  CZ3 TRP B 210     8513   7031   8336   -905   -210   -243       C  
ATOM   3994  CH2 TRP B 210     -18.098 -28.467 -27.909  1.00 63.73           C  
ANISOU 3994  CH2 TRP B 210     8676   7196   8343   -840    -99   -307       C  
ATOM   3995  N   LYS B 211     -21.893 -31.142 -33.180  1.00 68.69           N  
ANISOU 3995  N   LYS B 211     8698   7986   9415  -1276   -495    120       N  
ATOM   3996  CA  LYS B 211     -21.709 -31.599 -34.553  1.00 68.24           C  
ANISOU 3996  CA  LYS B 211     8700   7846   9381  -1386   -651    143       C  
ATOM   3997  C   LYS B 211     -20.706 -30.727 -35.290  1.00 66.29           C  
ANISOU 3997  C   LYS B 211     8593   7455   9138  -1265   -717     75       C  
ATOM   3998  O   LYS B 211     -20.357 -29.644 -34.830  1.00 65.91           O  
ANISOU 3998  O   LYS B 211     8572   7376   9093  -1108   -655     17       O  
ATOM   3999  CB  LYS B 211     -23.042 -31.629 -35.301  1.00 70.37           C  
ANISOU 3999  CB  LYS B 211     8742   8274   9721  -1454   -727    223       C  
ATOM   4000  CG  LYS B 211     -23.901 -30.401 -35.077  1.00 72.09           C  
ANISOU 4000  CG  LYS B 211     8745   8641  10004  -1244   -671    235       C  
ATOM   4001  CD  LYS B 211     -25.280 -30.589 -35.680  1.00 74.66           C  
ANISOU 4001  CD  LYS B 211     8789   9193  10387  -1319   -746    336       C  
ATOM   4002  CE  LYS B 211     -26.215 -29.480 -35.239  1.00 77.02           C  
ANISOU 4002  CE  LYS B 211     8845   9678  10740  -1067   -654    360       C  
ATOM   4003  NZ  LYS B 211     -26.320 -29.421 -33.758  1.00 78.03           N  
ANISOU 4003  NZ  LYS B 211     8939   9878  10831   -993   -449    330       N  
ATOM   4004  N   ILE B 212     -20.241 -31.211 -36.434  1.00 65.13           N  
ANISOU 4004  N   ILE B 212     8554   7215   8976  -1355   -835     81       N  
ATOM   4005  CA  ILE B 212     -19.277 -30.468 -37.232  1.00 63.39           C  
ANISOU 4005  CA  ILE B 212     8462   6879   8745  -1273   -891     33       C  
ATOM   4006  C   ILE B 212     -19.972 -29.298 -37.921  1.00 63.31           C  
ANISOU 4006  C   ILE B 212     8350   6903   8803  -1161   -942     58       C  
ATOM   4007  O   ILE B 212     -21.098 -29.430 -38.399  1.00 64.69           O  
ANISOU 4007  O   ILE B 212     8367   7191   9021  -1190  -1006    126       O  
ATOM   4008  CB  ILE B 212     -18.582 -31.387 -38.254  1.00 63.04           C  
ANISOU 4008  CB  ILE B 212     8571   6740   8642  -1385   -982     32       C  
ATOM   4009  CG1 ILE B 212     -17.482 -30.637 -39.004  1.00 62.18           C  
ANISOU 4009  CG1 ILE B 212     8581   6541   8505  -1310  -1012    -11       C  
ATOM   4010  CG2 ILE B 212     -19.585 -31.985 -39.215  1.00 64.36           C  
ANISOU 4010  CG2 ILE B 212     8673   6956   8825  -1515  -1094     90       C  
ATOM   4011  CD1 ILE B 212     -16.749 -31.494 -40.012  1.00 61.86           C  
ANISOU 4011  CD1 ILE B 212     8692   6426   8388  -1383  -1076    -20       C  
ATOM   4012  N   GLU B 213     -19.308 -28.148 -37.950  1.00 61.95           N  
ANISOU 4012  N   GLU B 213     8271   6637   8631  -1036   -919     11       N  
ATOM   4013  CA  GLU B 213     -19.921 -26.930 -38.468  1.00 62.43           C  
ANISOU 4013  CA  GLU B 213     8284   6690   8747   -889   -953     40       C  
ATOM   4014  C   GLU B 213     -19.246 -26.422 -39.734  1.00 61.31           C  
ANISOU 4014  C   GLU B 213     8285   6430   8579   -897  -1049     51       C  
ATOM   4015  O   GLU B 213     -19.921 -26.063 -40.692  1.00 61.96           O  
ANISOU 4015  O   GLU B 213     8317   6538   8686   -850  -1146    120       O  
ATOM   4016  CB  GLU B 213     -19.912 -25.832 -37.403  1.00 63.24           C  
ANISOU 4016  CB  GLU B 213     8413   6752   8862   -725   -832    -18       C  
ATOM   4017  CG  GLU B 213     -20.861 -26.076 -36.244  1.00 64.34           C  
ANISOU 4017  CG  GLU B 213     8384   7040   9022   -665   -723    -14       C  
ATOM   4018  CD  GLU B 213     -22.311 -25.990 -36.655  1.00 66.13           C  
ANISOU 4018  CD  GLU B 213     8374   7433   9318   -579   -758     78       C  
ATOM   4019  OE1 GLU B 213     -23.155 -26.615 -35.984  1.00 67.27           O  
ANISOU 4019  OE1 GLU B 213     8326   7760   9474   -614   -693    114       O  
ATOM   4020  OE2 GLU B 213     -22.607 -25.293 -37.646  1.00 66.63           O  
ANISOU 4020  OE2 GLU B 213     8435   7466   9417   -480   -852    126       O  
ATOM   4021  N   LYS B 214     -17.917 -26.375 -39.727  1.00 59.81           N  
ANISOU 4021  N   LYS B 214     8262   6135   8330   -955  -1023     -7       N  
ATOM   4022  CA  LYS B 214     -17.166 -25.944 -40.907  1.00 59.00           C  
ANISOU 4022  CA  LYS B 214     8294   5938   8183   -988  -1092      8       C  
ATOM   4023  C   LYS B 214     -15.929 -26.801 -41.158  1.00 57.62           C  
ANISOU 4023  C   LYS B 214     8214   5754   7927  -1110  -1085    -29       C  
ATOM   4024  O   LYS B 214     -15.446 -27.496 -40.263  1.00 56.96           O  
ANISOU 4024  O   LYS B 214     8120   5704   7819  -1143  -1021    -75       O  
ATOM   4025  CB  LYS B 214     -16.747 -24.476 -40.793  1.00 58.92           C  
ANISOU 4025  CB  LYS B 214     8405   5801   8179   -903  -1053    -13       C  
ATOM   4026  CG  LYS B 214     -17.875 -23.480 -40.934  1.00 60.51           C  
ANISOU 4026  CG  LYS B 214     8571   5975   8446   -730  -1074     41       C  
ATOM   4027  CD  LYS B 214     -17.368 -22.053 -40.778  1.00 61.56           C  
ANISOU 4027  CD  LYS B 214     8897   5923   8569   -657  -1028     11       C  
ATOM   4028  CE  LYS B 214     -18.510 -21.046 -40.830  1.00 63.88           C  
ANISOU 4028  CE  LYS B 214     9184   6165   8922   -425  -1035     65       C  
ATOM   4029  NZ  LYS B 214     -18.048 -19.650 -40.586  1.00 65.07           N  
ANISOU 4029  NZ  LYS B 214     9586   6085   9055   -351   -980     26       N  
ATOM   4030  N   ALA B 215     -15.428 -26.741 -42.390  1.00 57.25           N  
ANISOU 4030  N   ALA B 215     8259   5670   7824  -1155  -1147     -1       N  
ATOM   4031  CA  ALA B 215     -14.160 -27.370 -42.743  1.00 55.61           C  
ANISOU 4031  CA  ALA B 215     8139   5466   7525  -1229  -1123    -34       C  
ATOM   4032  C   ALA B 215     -13.478 -26.586 -43.855  1.00 55.51           C  
ANISOU 4032  C   ALA B 215     8234   5405   7454  -1255  -1146     -5       C  
ATOM   4033  O   ALA B 215     -14.059 -26.360 -44.911  1.00 55.91           O  
ANISOU 4033  O   ALA B 215     8319   5434   7491  -1250  -1229     55       O  
ATOM   4034  CB  ALA B 215     -14.371 -28.799 -43.162  1.00 55.28           C  
ANISOU 4034  CB  ALA B 215     8105   5460   7439  -1282  -1165    -32       C  
ATOM   4035  N   SER B 216     -12.238 -26.179 -43.605  1.00 55.32           N  
ANISOU 4035  N   SER B 216     8254   5383   7381  -1297  -1075    -39       N  
ATOM   4036  CA  SER B 216     -11.481 -25.379 -44.553  1.00 55.88           C  
ANISOU 4036  CA  SER B 216     8423   5423   7387  -1357  -1073     -4       C  
ATOM   4037  C   SER B 216     -10.225 -26.115 -44.985  1.00 55.51           C  
ANISOU 4037  C   SER B 216     8380   5480   7231  -1410  -1022    -24       C  
ATOM   4038  O   SER B 216      -9.474 -26.620 -44.150  1.00 54.87           O  
ANISOU 4038  O   SER B 216     8231   5484   7134  -1408   -962    -75       O  
ATOM   4039  CB  SER B 216     -11.104 -24.043 -43.924  1.00 56.66           C  
ANISOU 4039  CB  SER B 216     8573   5442   7514  -1392  -1029    -18       C  
ATOM   4040  OG  SER B 216     -12.242 -23.400 -43.384  1.00 57.43           O  
ANISOU 4040  OG  SER B 216     8674   5443   7704  -1293  -1052    -12       O  
ATOM   4041  N   PHE B 217     -10.006 -26.166 -46.294  1.00 56.21           N  
ANISOU 4041  N   PHE B 217     8548   5576   7233  -1438  -1045     22       N  
ATOM   4042  CA  PHE B 217      -8.848 -26.846 -46.853  1.00 56.46           C  
ANISOU 4042  CA  PHE B 217     8586   5723   7143  -1456   -979      6       C  
ATOM   4043  C   PHE B 217      -8.092 -25.951 -47.831  1.00 57.13           C  
ANISOU 4043  C   PHE B 217     8739   5831   7138  -1548   -944     64       C  
ATOM   4044  O   PHE B 217      -8.699 -25.196 -48.595  1.00 58.12           O  
ANISOU 4044  O   PHE B 217     8966   5858   7260  -1576  -1004    131       O  
ATOM   4045  CB  PHE B 217      -9.281 -28.117 -47.585  1.00 57.15           C  
ANISOU 4045  CB  PHE B 217     8733   5813   7168  -1396  -1021     -8       C  
ATOM   4046  CG  PHE B 217     -10.077 -29.068 -46.742  1.00 57.28           C  
ANISOU 4046  CG  PHE B 217     8710   5794   7258  -1344  -1057    -49       C  
ATOM   4047  CD1 PHE B 217      -9.440 -30.008 -45.953  1.00 57.16           C  
ANISOU 4047  CD1 PHE B 217     8661   5833   7225  -1285   -991   -100       C  
ATOM   4048  CD2 PHE B 217     -11.465 -29.040 -46.758  1.00 57.49           C  
ANISOU 4048  CD2 PHE B 217     8731   5750   7363  -1355  -1157    -24       C  
ATOM   4049  CE1 PHE B 217     -10.169 -30.891 -45.183  1.00 57.07           C  
ANISOU 4049  CE1 PHE B 217     8642   5772   7268  -1258  -1018   -122       C  
ATOM   4050  CE2 PHE B 217     -12.201 -29.922 -45.989  1.00 57.25           C  
ANISOU 4050  CE2 PHE B 217     8656   5706   7392  -1344  -1179    -50       C  
ATOM   4051  CZ  PHE B 217     -11.553 -30.846 -45.201  1.00 56.99           C  
ANISOU 4051  CZ  PHE B 217     8623   5695   7336  -1306  -1107    -98       C  
ATOM   4052  N   ILE B 218      -6.767 -26.031 -47.794  1.00 56.64           N  
ANISOU 4052  N   ILE B 218     8612   5915   6994  -1595   -846     50       N  
ATOM   4053  CA  ILE B 218      -5.935 -25.456 -48.839  1.00 57.05           C  
ANISOU 4053  CA  ILE B 218     8711   6039   6927  -1696   -787    111       C  
ATOM   4054  C   ILE B 218      -5.271 -26.635 -49.521  1.00 56.73           C  
ANISOU 4054  C   ILE B 218     8650   6149   6756  -1603   -720     86       C  
ATOM   4055  O   ILE B 218      -4.623 -26.499 -50.558  1.00 57.37           O  
ANISOU 4055  O   ILE B 218     8771   6324   6704  -1645   -654    129       O  
ATOM   4056  CB  ILE B 218      -4.841 -24.542 -48.276  1.00 58.13           C  
ANISOU 4056  CB  ILE B 218     8761   6270   7055  -1850   -713    121       C  
ATOM   4057  CG1 ILE B 218      -5.350 -23.749 -47.078  1.00 57.22           C  
ANISOU 4057  CG1 ILE B 218     8653   6018   7071  -1896   -763     90       C  
ATOM   4058  CG2 ILE B 218      -4.317 -23.602 -49.355  1.00 60.35           C  
ANISOU 4058  CG2 ILE B 218     9135   6561   7234  -2008   -670    212       C  
ATOM   4059  CD1 ILE B 218      -4.258 -22.974 -46.376  1.00 57.92           C  
ANISOU 4059  CD1 ILE B 218     8664   6205   7139  -2076   -708     77       C  
ATOM   4060  N   GLU B 219      -5.456 -27.803 -48.915  1.00 55.78           N  
ANISOU 4060  N   GLU B 219     8489   6042   6665  -1466   -728     17       N  
ATOM   4061  CA  GLU B 219      -4.854 -29.034 -49.397  1.00 55.99           C  
ANISOU 4061  CA  GLU B 219     8531   6173   6569  -1332   -658    -22       C  
ATOM   4062  C   GLU B 219      -5.690 -30.240 -48.995  1.00 54.86           C  
ANISOU 4062  C   GLU B 219     8466   5910   6470  -1212   -722    -82       C  
ATOM   4063  O   GLU B 219      -6.373 -30.217 -47.973  1.00 53.33           O  
ANISOU 4063  O   GLU B 219     8226   5632   6404  -1223   -782    -96       O  
ATOM   4064  CB  GLU B 219      -3.453 -29.186 -48.812  1.00 56.37           C  
ANISOU 4064  CB  GLU B 219     8398   6450   6569  -1290   -542    -34       C  
ATOM   4065  CG  GLU B 219      -3.441 -29.415 -47.310  1.00 55.18           C  
ANISOU 4065  CG  GLU B 219     8127   6313   6527  -1248   -567    -71       C  
ATOM   4066  CD  GLU B 219      -2.062 -29.717 -46.792  1.00 55.97           C  
ANISOU 4066  CD  GLU B 219     8033   6675   6557  -1178   -472    -74       C  
ATOM   4067  OE1 GLU B 219      -1.126 -29.749 -47.615  1.00 57.20           O  
ANISOU 4067  OE1 GLU B 219     8131   7015   6588  -1157   -374    -48       O  
ATOM   4068  OE2 GLU B 219      -1.918 -29.920 -45.569  1.00 55.51           O  
ANISOU 4068  OE2 GLU B 219     7871   6662   6558  -1138   -495    -97       O  
ATOM   4069  N   VAL B 220      -5.629 -31.293 -49.807  1.00 56.10           N  
ANISOU 4069  N   VAL B 220     8758   6052   6504  -1109   -700   -119       N  
ATOM   4070  CA  VAL B 220      -6.250 -32.570 -49.461  1.00 56.56           C  
ANISOU 4070  CA  VAL B 220     8929   5986   6576  -1014   -745   -178       C  
ATOM   4071  C   VAL B 220      -5.196 -33.676 -49.433  1.00 58.05           C  
ANISOU 4071  C   VAL B 220     9153   6258   6646   -818   -628   -226       C  
ATOM   4072  O   VAL B 220      -4.677 -34.070 -50.476  1.00 59.27           O  
ANISOU 4072  O   VAL B 220     9418   6457   6643   -737   -558   -248       O  
ATOM   4073  CB  VAL B 220      -7.371 -32.954 -50.444  1.00 57.33           C  
ANISOU 4073  CB  VAL B 220     9226   5931   6626  -1077   -855   -193       C  
ATOM   4074  CG1 VAL B 220      -8.024 -34.256 -50.014  1.00 57.62           C  
ANISOU 4074  CG1 VAL B 220     9392   5825   6676  -1034   -905   -251       C  
ATOM   4075  CG2 VAL B 220      -8.409 -31.851 -50.528  1.00 56.65           C  
ANISOU 4075  CG2 VAL B 220     9086   5792   6646  -1223   -973   -129       C  
ATOM   4076  N   LYS B 221      -4.884 -34.165 -48.234  1.00 58.26           N  
ANISOU 4076  N   LYS B 221     9092   6309   6735   -721   -603   -237       N  
ATOM   4077  CA  LYS B 221      -3.858 -35.191 -48.057  1.00 59.58           C  
ANISOU 4077  CA  LYS B 221     9276   6564   6796   -487   -495   -266       C  
ATOM   4078  C   LYS B 221      -4.474 -36.544 -47.734  1.00 60.48           C  
ANISOU 4078  C   LYS B 221     9618   6461   6901   -383   -532   -312       C  
ATOM   4079  O   LYS B 221      -5.659 -36.635 -47.420  1.00 58.94           O  
ANISOU 4079  O   LYS B 221     9504   6088   6801   -524   -640   -315       O  
ATOM   4080  CB  LYS B 221      -2.869 -34.781 -46.967  1.00 59.29           C  
ANISOU 4080  CB  LYS B 221     8976   6749   6803   -434   -439   -229       C  
ATOM   4081  CG  LYS B 221      -3.506 -33.998 -45.841  1.00 57.86           C  
ANISOU 4081  CG  LYS B 221     8676   6526   6782   -598   -529   -205       C  
ATOM   4082  CD  LYS B 221      -2.474 -33.513 -44.845  1.00 58.38           C  
ANISOU 4082  CD  LYS B 221     8493   6828   6860   -581   -488   -178       C  
ATOM   4083  CE  LYS B 221      -3.094 -32.539 -43.859  1.00 57.24           C  
ANISOU 4083  CE  LYS B 221     8263   6634   6850   -766   -568   -169       C  
ATOM   4084  NZ  LYS B 221      -2.102 -32.096 -42.848  1.00 57.81           N  
ANISOU 4084  NZ  LYS B 221     8116   6935   6913   -777   -548   -155       N  
ATOM   4085  N   ASN B 222      -3.660 -37.591 -47.815  1.00 63.09           N  
ANISOU 4085  N   ASN B 222    10053   6810   7109   -135   -436   -343       N  
ATOM   4086  CA  ASN B 222      -4.146 -38.955 -47.675  1.00 64.60           C  
ANISOU 4086  CA  ASN B 222    10537   6751   7255    -29   -457   -390       C  
ATOM   4087  C   ASN B 222      -3.561 -39.649 -46.443  1.00 65.77           C  
ANISOU 4087  C   ASN B 222    10645   6926   7419    178   -412   -360       C  
ATOM   4088  O   ASN B 222      -3.723 -40.858 -46.269  1.00 68.01           O  
ANISOU 4088  O   ASN B 222    11197   7002   7643    316   -404   -386       O  
ATOM   4089  CB  ASN B 222      -3.837 -39.753 -48.951  1.00 66.16           C  
ANISOU 4089  CB  ASN B 222    11011   6864   7261    116   -386   -463       C  
ATOM   4090  CG  ASN B 222      -4.696 -40.998 -49.095  1.00 66.39           C  
ANISOU 4090  CG  ASN B 222    11426   6560   7240    106   -449   -528       C  
ATOM   4091  OD1 ASN B 222      -5.645 -41.024 -49.879  1.00 66.05           O  
ANISOU 4091  OD1 ASN B 222    11559   6365   7173    -97   -546   -570       O  
ATOM   4092  ND2 ASN B 222      -4.357 -42.043 -48.349  1.00 67.00           N  
ANISOU 4092  ND2 ASN B 222    11647   6521   7289    315   -402   -530       N  
ATOM   4093  N   CYS B 223      -2.886 -38.882 -45.590  1.00 64.38           N  
ANISOU 4093  N   CYS B 223    10155   6996   7311    190   -391   -302       N  
ATOM   4094  CA  CYS B 223      -2.348 -39.423 -44.345  1.00 64.68           C  
ANISOU 4094  CA  CYS B 223    10123   7096   7357    373   -372   -259       C  
ATOM   4095  C   CYS B 223      -3.468 -39.657 -43.340  1.00 63.68           C  
ANISOU 4095  C   CYS B 223    10090   6762   7345    224   -470   -240       C  
ATOM   4096  O   CYS B 223      -4.638 -39.468 -43.661  1.00 62.74           O  
ANISOU 4096  O   CYS B 223    10075   6466   7297     -4   -547   -262       O  
ATOM   4097  CB  CYS B 223      -1.259 -38.510 -43.761  1.00 46.61           C  
ANISOU 4097  CB  CYS B 223     7462   5165   5082    400   -336   -208       C  
ATOM   4098  SG  CYS B 223      -1.688 -36.754 -43.523  1.00 77.51           S  
ANISOU 4098  SG  CYS B 223    11120   9194   9138     35   -412   -191       S  
ATOM   4099  N   HIS B 224      -3.113 -40.087 -42.134  1.00 64.43           N  
ANISOU 4099  N   HIS B 224    10137   6899   7443    358   -466   -190       N  
ATOM   4100  CA  HIS B 224      -4.106 -40.277 -41.081  1.00 63.64           C  
ANISOU 4100  CA  HIS B 224    10105   6639   7435    216   -539   -159       C  
ATOM   4101  C   HIS B 224      -3.915 -39.297 -39.935  1.00 62.39           C  
ANISOU 4101  C   HIS B 224     9654   6694   7356    126   -569   -118       C  
ATOM   4102  O   HIS B 224      -2.799 -39.089 -39.459  1.00 62.87           O  
ANISOU 4102  O   HIS B 224     9523   7002   7364    276   -538    -88       O  
ATOM   4103  CB  HIS B 224      -4.074 -41.710 -40.551  1.00 65.40           C  
ANISOU 4103  CB  HIS B 224    10606   6664   7579    417   -517   -128       C  
ATOM   4104  CG  HIS B 224      -4.660 -42.710 -41.495  1.00 66.74           C  
ANISOU 4104  CG  HIS B 224    11148   6526   7684    413   -514   -180       C  
ATOM   4105  ND1 HIS B 224      -4.485 -44.068 -41.345  1.00 68.66           N  
ANISOU 4105  ND1 HIS B 224    11724   6541   7821    624   -477   -168       N  
ATOM   4106  CD2 HIS B 224      -5.424 -42.548 -42.603  1.00 66.54           C  
ANISOU 4106  CD2 HIS B 224    11237   6374   7670    214   -553   -247       C  
ATOM   4107  CE1 HIS B 224      -5.110 -44.699 -42.322  1.00 69.78           C  
ANISOU 4107  CE1 HIS B 224    12185   6417   7910    535   -490   -238       C  
ATOM   4108  NE2 HIS B 224      -5.688 -43.800 -43.099  1.00 68.35           N  
ANISOU 4108  NE2 HIS B 224    11863   6310   7796    283   -542   -286       N  
ATOM   4109  N   TRP B 225      -5.016 -38.695 -39.501  1.00 60.91           N  
ANISOU 4109  N   TRP B 225     9433   6426   7284   -118   -631   -120       N  
ATOM   4110  CA  TRP B 225      -4.982 -37.758 -38.391  1.00 59.61           C  
ANISOU 4110  CA  TRP B 225     9046   6421   7183   -214   -657   -100       C  
ATOM   4111  C   TRP B 225      -4.804 -38.539 -37.094  1.00 59.37           C  
ANISOU 4111  C   TRP B 225     9066   6389   7103    -85   -655    -44       C  
ATOM   4112  O   TRP B 225      -5.673 -39.324 -36.714  1.00 59.52           O  
ANISOU 4112  O   TRP B 225     9278   6201   7134   -121   -664    -17       O  
ATOM   4113  CB  TRP B 225      -6.267 -36.926 -38.354  1.00 58.64           C  
ANISOU 4113  CB  TRP B 225     8894   6203   7185   -467   -706   -121       C  
ATOM   4114  CG  TRP B 225      -6.179 -35.727 -37.465  1.00 58.27           C  
ANISOU 4114  CG  TRP B 225     8642   6308   7192   -568   -721   -127       C  
ATOM   4115  CD1 TRP B 225      -6.074 -35.727 -36.111  1.00 58.88           C  
ANISOU 4115  CD1 TRP B 225     8661   6459   7251   -546   -722   -106       C  
ATOM   4116  CD2 TRP B 225      -6.192 -34.350 -37.867  1.00 57.61           C  
ANISOU 4116  CD2 TRP B 225     8424   6297   7168   -711   -736   -162       C  
ATOM   4117  NE1 TRP B 225      -6.018 -34.438 -35.641  1.00 58.39           N  
ANISOU 4117  NE1 TRP B 225     8443   6511   7230   -670   -738   -140       N  
ATOM   4118  CE2 TRP B 225      -6.090 -33.574 -36.701  1.00 57.43           C  
ANISOU 4118  CE2 TRP B 225     8283   6376   7162   -772   -745   -173       C  
ATOM   4119  CE3 TRP B 225      -6.282 -33.700 -39.100  1.00 57.57           C  
ANISOU 4119  CE3 TRP B 225     8417   6268   7189   -792   -744   -181       C  
ATOM   4120  CZ2 TRP B 225      -6.074 -32.181 -36.729  1.00 56.88           C  
ANISOU 4120  CZ2 TRP B 225     8117   6355   7140   -913   -759   -210       C  
ATOM   4121  CZ3 TRP B 225      -6.265 -32.320 -39.127  1.00 57.12           C  
ANISOU 4121  CZ3 TRP B 225     8253   6266   7182   -927   -757   -199       C  
ATOM   4122  CH2 TRP B 225      -6.162 -31.575 -37.951  1.00 56.86           C  
ANISOU 4122  CH2 TRP B 225     8128   6306   7171   -987   -764   -217       C  
ATOM   4123  N   PRO B 226      -3.663 -38.335 -36.417  1.00 58.92           N  
ANISOU 4123  N   PRO B 226     8832   6577   6977     54   -647    -15       N  
ATOM   4124  CA  PRO B 226      -3.317 -39.097 -35.211  1.00 59.53           C  
ANISOU 4124  CA  PRO B 226     8954   6690   6976    219   -653     54       C  
ATOM   4125  C   PRO B 226      -4.314 -38.889 -34.075  1.00 58.37           C  
ANISOU 4125  C   PRO B 226     8837   6458   6882     50   -685     72       C  
ATOM   4126  O   PRO B 226      -5.032 -37.891 -34.063  1.00 57.07           O  
ANISOU 4126  O   PRO B 226     8579   6292   6814   -173   -701     24       O  
ATOM   4127  CB  PRO B 226      -1.944 -38.539 -34.824  1.00 60.33           C  
ANISOU 4127  CB  PRO B 226     8776   7143   7002    331   -664     70       C  
ATOM   4128  CG  PRO B 226      -1.878 -37.200 -35.468  1.00 59.40           C  
ANISOU 4128  CG  PRO B 226     8467   7145   6957    111   -670      3       C  
ATOM   4129  CD  PRO B 226      -2.637 -37.332 -36.748  1.00 58.69           C  
ANISOU 4129  CD  PRO B 226     8542   6826   6930     37   -640    -39       C  
ATOM   4130  N   LYS B 227      -4.350 -39.831 -33.137  1.00 58.73           N  
ANISOU 4130  N   LYS B 227     9026   6435   6852    173   -683    148       N  
ATOM   4131  CA  LYS B 227      -5.333 -39.816 -32.058  1.00 57.14           C  
ANISOU 4131  CA  LYS B 227     8885   6150   6677     24   -689    180       C  
ATOM   4132  C   LYS B 227      -4.889 -38.949 -30.886  1.00 56.82           C  
ANISOU 4132  C   LYS B 227     8636   6359   6594     -7   -721    178       C  
ATOM   4133  O   LYS B 227      -5.702 -38.555 -30.057  1.00 56.39           O  
ANISOU 4133  O   LYS B 227     8579   6283   6565   -158   -716    174       O  
ATOM   4134  CB  LYS B 227      -5.576 -41.239 -31.564  1.00 57.88           C  
ANISOU 4134  CB  LYS B 227     9262   6041   6687    150   -668    276       C  
ATOM   4135  CG  LYS B 227      -5.959 -42.222 -32.645  1.00 57.83           C  
ANISOU 4135  CG  LYS B 227     9526   5755   6691    176   -643    271       C  
ATOM   4136  CD  LYS B 227      -7.447 -42.469 -32.625  1.00 56.85           C  
ANISOU 4136  CD  LYS B 227     9550   5406   6644    -94   -637    277       C  
ATOM   4137  CE  LYS B 227      -7.830 -43.608 -33.538  1.00 57.67           C  
ANISOU 4137  CE  LYS B 227     9978   5209   6725    -97   -627    278       C  
ATOM   4138  NZ  LYS B 227      -9.288 -43.845 -33.445  1.00 57.49           N  
ANISOU 4138  NZ  LYS B 227    10061   5012   6770   -403   -632    296       N  
ATOM   4139  N   SER B 228      -3.593 -38.667 -30.820  1.00 57.22           N  
ANISOU 4139  N   SER B 228     8511   6664   6567    134   -754    179       N  
ATOM   4140  CA  SER B 228      -3.038 -37.904 -29.712  1.00 56.80           C  
ANISOU 4140  CA  SER B 228     8270   6869   6442     93   -805    173       C  
ATOM   4141  C   SER B 228      -3.499 -36.464 -29.787  1.00 54.16           C  
ANISOU 4141  C   SER B 228     7804   6573   6203   -173   -814     68       C  
ATOM   4142  O   SER B 228      -3.591 -35.773 -28.778  1.00 53.96           O  
ANISOU 4142  O   SER B 228     7715   6650   6138   -281   -841     38       O  
ATOM   4143  CB  SER B 228      -1.513 -37.975 -29.728  1.00 58.79           C  
ANISOU 4143  CB  SER B 228     8334   7420   6583    290   -849    206       C  
ATOM   4144  OG  SER B 228      -0.994 -37.625 -30.994  1.00 58.78           O  
ANISOU 4144  OG  SER B 228     8219   7481   6634    291   -823    159       O  
ATOM   4145  N   HIS B 229      -3.804 -36.029 -31.001  1.00 52.64           N  
ANISOU 4145  N   HIS B 229     7600   6279   6121   -267   -788     13       N  
ATOM   4146  CA  HIS B 229      -4.218 -34.662 -31.242  1.00 51.08           C  
ANISOU 4146  CA  HIS B 229     7310   6083   6014   -489   -793    -75       C  
ATOM   4147  C   HIS B 229      -5.678 -34.633 -31.649  1.00 48.89           C  
ANISOU 4147  C   HIS B 229     7162   5555   5858   -598   -755    -93       C  
ATOM   4148  O   HIS B 229      -6.087 -33.784 -32.432  1.00 47.05           O  
ANISOU 4148  O   HIS B 229     6896   5261   5718   -720   -753   -145       O  
ATOM   4149  CB  HIS B 229      -3.368 -34.042 -32.353  1.00 51.64           C  
ANISOU 4149  CB  HIS B 229     7248   6269   6103   -522   -800   -109       C  
ATOM   4150  CG  HIS B 229      -1.901 -33.997 -32.044  1.00 53.53           C  
ANISOU 4150  CG  HIS B 229     7300   6815   6224   -438   -838    -86       C  
ATOM   4151  ND1 HIS B 229      -1.154 -35.131 -31.798  1.00 54.99           N  
ANISOU 4151  ND1 HIS B 229     7476   7113   6304   -184   -841     -6       N  
ATOM   4152  CD2 HIS B 229      -1.041 -32.954 -31.958  1.00 54.33           C  
ANISOU 4152  CD2 HIS B 229     7208   7146   6288   -578   -877   -126       C  
ATOM   4153  CE1 HIS B 229       0.100 -34.787 -31.566  1.00 56.48           C  
ANISOU 4153  CE1 HIS B 229     7436   7626   6399   -156   -884      7       C  
ATOM   4154  NE2 HIS B 229       0.195 -33.472 -31.659  1.00 56.11           N  
ANISOU 4154  NE2 HIS B 229     7270   7659   6390   -418   -909    -67       N  
ATOM   4155  N   THR B 230      -6.459 -35.566 -31.114  1.00 49.26           N  
ANISOU 4155  N   THR B 230     7350   5470   5895   -559   -729    -37       N  
ATOM   4156  CA  THR B 230      -7.864 -35.690 -31.489  1.00 48.59           C  
ANISOU 4156  CA  THR B 230     7358   5189   5916   -673   -697    -37       C  
ATOM   4157  C   THR B 230      -8.771 -35.570 -30.264  1.00 48.31           C  
ANISOU 4157  C   THR B 230     7339   5146   5873   -747   -659    -23       C  
ATOM   4158  O   THR B 230      -8.407 -36.003 -29.174  1.00 49.41           O  
ANISOU 4158  O   THR B 230     7512   5360   5902   -677   -653     21       O  
ATOM   4159  CB  THR B 230      -8.129 -37.027 -32.208  1.00 49.10           C  
ANISOU 4159  CB  THR B 230     7602   5077   5975   -609   -689     21       C  
ATOM   4160  OG1 THR B 230      -7.062 -37.301 -33.124  1.00 49.27           O  
ANISOU 4160  OG1 THR B 230     7626   5138   5954   -476   -704     12       O  
ATOM   4161  CG2 THR B 230      -9.441 -36.982 -32.972  1.00 48.70           C  
ANISOU 4161  CG2 THR B 230     7598   4869   6037   -767   -686      8       C  
ATOM   4162  N   LEU B 231      -9.946 -34.973 -30.451  1.00 47.67           N  
ANISOU 4162  N   LEU B 231     7223   4993   5895   -873   -631    -53       N  
ATOM   4163  CA  LEU B 231     -10.919 -34.816 -29.375  1.00 48.91           C  
ANISOU 4163  CA  LEU B 231     7374   5163   6045   -935   -569    -42       C  
ATOM   4164  C   LEU B 231     -12.065 -35.797 -29.555  1.00 50.69           C  
ANISOU 4164  C   LEU B 231     7681   5266   6315  -1010   -534     35       C  
ATOM   4165  O   LEU B 231     -12.553 -35.971 -30.663  1.00 51.11           O  
ANISOU 4165  O   LEU B 231     7741   5222   6455  -1072   -563     37       O  
ATOM   4166  CB  LEU B 231     -11.478 -33.397 -29.378  1.00 39.17           C  
ANISOU 4166  CB  LEU B 231     6032   3962   4890   -999   -549   -128       C  
ATOM   4167  CG  LEU B 231     -10.497 -32.276 -29.063  1.00 39.11           C  
ANISOU 4167  CG  LEU B 231     5973   4055   4831   -987   -580   -216       C  
ATOM   4168  CD1 LEU B 231     -10.860 -31.030 -29.833  1.00 38.59           C  
ANISOU 4168  CD1 LEU B 231     5859   3932   4872  -1041   -587   -287       C  
ATOM   4169  CD2 LEU B 231     -10.505 -32.000 -27.588  1.00 40.02           C  
ANISOU 4169  CD2 LEU B 231     6104   4266   4834   -979   -538   -243       C  
ATOM   4170  N   TRP B 232     -12.486 -36.434 -28.466  1.00 52.49           N  
ANISOU 4170  N   TRP B 232     7974   5504   6465  -1028   -475    103       N  
ATOM   4171  CA  TRP B 232     -13.647 -37.321 -28.483  1.00 53.91           C  
ANISOU 4171  CA  TRP B 232     8222   5588   6675  -1153   -430    187       C  
ATOM   4172  C   TRP B 232     -13.455 -38.496 -29.439  1.00 54.85           C  
ANISOU 4172  C   TRP B 232     8514   5531   6796  -1167   -483    236       C  
ATOM   4173  O   TRP B 232     -14.324 -38.783 -30.264  1.00 55.99           O  
ANISOU 4173  O   TRP B 232     8665   5586   7021  -1305   -501    247       O  
ATOM   4174  CB  TRP B 232     -14.903 -36.532 -28.859  1.00 53.33           C  
ANISOU 4174  CB  TRP B 232     7981   5555   6726  -1269   -399    153       C  
ATOM   4175  CG  TRP B 232     -16.149 -37.063 -28.255  1.00 54.17           C  
ANISOU 4175  CG  TRP B 232     8066   5686   6831  -1406   -315    235       C  
ATOM   4176  CD1 TRP B 232     -16.295 -38.232 -27.579  1.00 55.32           C  
ANISOU 4176  CD1 TRP B 232     8363   5774   6881  -1475   -271    340       C  
ATOM   4177  CD2 TRP B 232     -17.436 -36.437 -28.258  1.00 54.06           C  
ANISOU 4177  CD2 TRP B 232     7858   5777   6904  -1492   -257    232       C  
ATOM   4178  NE1 TRP B 232     -17.593 -38.377 -27.165  1.00 56.49           N  
ANISOU 4178  NE1 TRP B 232     8414   5996   7053  -1635   -184    403       N  
ATOM   4179  CE2 TRP B 232     -18.314 -37.286 -27.570  1.00 55.64           C  
ANISOU 4179  CE2 TRP B 232     8074   6008   7059  -1635   -173    337       C  
ATOM   4180  CE3 TRP B 232     -17.929 -35.240 -28.782  1.00 53.09           C  
ANISOU 4180  CE3 TRP B 232     7554   5730   6889  -1449   -265    160       C  
ATOM   4181  CZ2 TRP B 232     -19.657 -36.978 -27.392  1.00 56.72           C  
ANISOU 4181  CZ2 TRP B 232     8006   6290   7254  -1738    -92    370       C  
ATOM   4182  CZ3 TRP B 232     -19.257 -34.937 -28.601  1.00 54.09           C  
ANISOU 4182  CZ3 TRP B 232     7495   5982   7075  -1513   -192    193       C  
ATOM   4183  CH2 TRP B 232     -20.107 -35.800 -27.915  1.00 55.99           C  
ANISOU 4183  CH2 TRP B 232     7712   6293   7270  -1657   -104    295       C  
ATOM   4184  N   SER B 233     -12.320 -39.178 -29.314  1.00 54.51           N  
ANISOU 4184  N   SER B 233     8615   5445   6651  -1015   -511    265       N  
ATOM   4185  CA  SER B 233     -11.968 -40.261 -30.227  1.00 54.02           C  
ANISOU 4185  CA  SER B 233     8757   5199   6569   -971   -552    295       C  
ATOM   4186  C   SER B 233     -12.535 -41.608 -29.791  1.00 54.84           C  
ANISOU 4186  C   SER B 233     9109   5122   6605  -1052   -517    405       C  
ATOM   4187  O   SER B 233     -12.076 -42.653 -30.238  1.00 55.50           O  
ANISOU 4187  O   SER B 233     9439   5023   6627   -970   -539    441       O  
ATOM   4188  CB  SER B 233     -10.449 -40.354 -30.380  1.00 54.11           C  
ANISOU 4188  CB  SER B 233     8797   5263   6498   -727   -589    277       C  
ATOM   4189  OG  SER B 233      -9.800 -40.345 -29.123  1.00 54.88           O  
ANISOU 4189  OG  SER B 233     8874   5492   6483   -606   -575    323       O  
ATOM   4190  N   ASN B 234     -13.540 -41.570 -28.924  1.00 55.20           N  
ANISOU 4190  N   ASN B 234     9105   5215   6654  -1215   -453    460       N  
ATOM   4191  CA  ASN B 234     -14.131 -42.787 -28.385  1.00 56.95           C  
ANISOU 4191  CA  ASN B 234     9560   5279   6800  -1339   -407    582       C  
ATOM   4192  C   ASN B 234     -15.454 -43.162 -29.047  1.00 57.60           C  
ANISOU 4192  C   ASN B 234     9655   5263   6968  -1633   -407    601       C  
ATOM   4193  O   ASN B 234     -16.399 -42.372 -29.060  1.00 57.42           O  
ANISOU 4193  O   ASN B 234     9377   5399   7040  -1778   -382    574       O  
ATOM   4194  CB  ASN B 234     -14.318 -42.660 -26.871  1.00 56.97           C  
ANISOU 4194  CB  ASN B 234     9521   5416   6708  -1340   -323    657       C  
ATOM   4195  CG  ASN B 234     -14.977 -41.354 -26.472  1.00 55.15           C  
ANISOU 4195  CG  ASN B 234     8981   5421   6551  -1409   -272    587       C  
ATOM   4196  OD1 ASN B 234     -14.299 -40.374 -26.182  1.00 53.55           O  
ANISOU 4196  OD1 ASN B 234     8636   5371   6339  -1261   -288    505       O  
ATOM   4197  ND2 ASN B 234     -16.303 -41.337 -26.448  1.00 55.47           N  
ANISOU 4197  ND2 ASN B 234     8921   5498   6657  -1633   -210    621       N  
ATOM   4198  N   GLY B 235     -15.513 -44.375 -29.589  1.00 58.36           N  
ANISOU 4198  N   GLY B 235    10053   5101   7020  -1716   -438    649       N  
ATOM   4199  CA  GLY B 235     -16.718 -44.855 -30.234  1.00 59.57           C  
ANISOU 4199  CA  GLY B 235    10248   5157   7231  -2037   -459    669       C  
ATOM   4200  C   GLY B 235     -16.997 -44.102 -31.510  1.00 58.57           C  
ANISOU 4200  C   GLY B 235     9925   5103   7224  -2084   -543    556       C  
ATOM   4201  O   GLY B 235     -18.093 -43.586 -31.717  1.00 59.10           O  
ANISOU 4201  O   GLY B 235     9753   5317   7384  -2290   -550    553       O  
ATOM   4202  N   VAL B 236     -15.994 -44.039 -32.372  1.00 57.48           N  
ANISOU 4202  N   VAL B 236     9882   4881   7075  -1879   -604    473       N  
ATOM   4203  CA  VAL B 236     -16.127 -43.275 -33.595  1.00 47.64           C  
ANISOU 4203  CA  VAL B 236     8471   3707   5921  -1898   -683    372       C  
ATOM   4204  C   VAL B 236     -16.311 -44.176 -34.814  1.00 57.08           C  
ANISOU 4204  C   VAL B 236     9932   4673   7083  -2028   -764    339       C  
ATOM   4205  O   VAL B 236     -15.383 -44.856 -35.251  1.00 57.39           O  
ANISOU 4205  O   VAL B 236    10249   4522   7033  -1858   -774    309       O  
ATOM   4206  CB  VAL B 236     -14.946 -42.318 -33.788  1.00 51.97           C  
ANISOU 4206  CB  VAL B 236     8884   4380   6481  -1612   -688    293       C  
ATOM   4207  CG1 VAL B 236     -15.137 -41.507 -35.037  1.00 44.50           C  
ANISOU 4207  CG1 VAL B 236     7788   3501   5619  -1647   -762    207       C  
ATOM   4208  CG2 VAL B 236     -14.820 -41.399 -32.586  1.00 50.90           C  
ANISOU 4208  CG2 VAL B 236     8517   4459   6363  -1523   -621    308       C  
ATOM   4209  N   LEU B 237     -17.531 -44.174 -35.345  1.00 58.08           N  
ANISOU 4209  N   LEU B 237     9966   4831   7269  -2325   -823    344       N  
ATOM   4210  CA  LEU B 237     -17.879 -44.941 -36.535  1.00 59.38           C  
ANISOU 4210  CA  LEU B 237    10297   4876   7388  -2447   -901    295       C  
ATOM   4211  C   LEU B 237     -17.294 -44.273 -37.772  1.00 58.13           C  
ANISOU 4211  C   LEU B 237    10092   4749   7246  -2299   -973    188       C  
ATOM   4212  O   LEU B 237     -17.708 -43.177 -38.142  1.00 56.76           O  
ANISOU 4212  O   LEU B 237     9641   4756   7170  -2343  -1024    165       O  
ATOM   4213  CB  LEU B 237     -19.402 -45.039 -36.694  1.00 60.20           C  
ANISOU 4213  CB  LEU B 237    10205   5128   7542  -2768   -939    335       C  
ATOM   4214  CG  LEU B 237     -20.289 -45.669 -35.615  1.00 61.60           C  
ANISOU 4214  CG  LEU B 237    10371   5331   7706  -2999   -869    450       C  
ATOM   4215  CD1 LEU B 237     -20.476 -44.749 -34.421  1.00 60.26           C  
ANISOU 4215  CD1 LEU B 237     9959   5325   7613  -3010   -789    524       C  
ATOM   4216  CD2 LEU B 237     -21.644 -46.049 -36.192  1.00 63.64           C  
ANISOU 4216  CD2 LEU B 237    10500   5705   7976  -3310   -934    467       C  
ATOM   4217  N   GLU B 238     -16.347 -44.944 -38.420  1.00 68.74           N  
ANISOU 4217  N   GLU B 238    12144   6127   7848  -3463    237     22       N  
ATOM   4218  CA  GLU B 238     -15.727 -44.418 -39.630  1.00 68.25           C  
ANISOU 4218  CA  GLU B 238    11928   6028   7975  -3362    303      7       C  
ATOM   4219  C   GLU B 238     -16.744 -44.216 -40.747  1.00 68.31           C  
ANISOU 4219  C   GLU B 238    11823   6297   7833  -3574    379     75       C  
ATOM   4220  O   GLU B 238     -16.479 -43.520 -41.720  1.00 67.23           O  
ANISOU 4220  O   GLU B 238    11506   6193   7845  -3522    434     82       O  
ATOM   4221  CB  GLU B 238     -14.615 -45.349 -40.098  1.00 69.54           C  
ANISOU 4221  CB  GLU B 238    12275   5960   8189  -3221    312    -69       C  
ATOM   4222  CG  GLU B 238     -13.575 -45.639 -39.034  1.00 70.18           C  
ANISOU 4222  CG  GLU B 238    12457   5798   8410  -2984    230   -146       C  
ATOM   4223  CD  GLU B 238     -12.350 -46.321 -39.600  1.00 71.32           C  
ANISOU 4223  CD  GLU B 238    12702   5738   8660  -2806    237   -232       C  
ATOM   4224  OE1 GLU B 238     -12.280 -46.487 -40.836  1.00 71.62           O  
ANISOU 4224  OE1 GLU B 238    12727   5809   8676  -2868    310   -231       O  
ATOM   4225  OE2 GLU B 238     -11.459 -46.689 -38.808  1.00 71.74           O  
ANISOU 4225  OE2 GLU B 238    12833   5609   8814  -2600    166   -303       O  
ATOM   4226  N   SER B 239     -17.906 -44.838 -40.602  1.00 69.60           N  
ANISOU 4226  N   SER B 239    12093   6655   7697  -3807    379    118       N  
ATOM   4227  CA  SER B 239     -18.994 -44.648 -41.543  1.00 69.76           C  
ANISOU 4227  CA  SER B 239    11994   6956   7556  -3998    436    174       C  
ATOM   4228  C   SER B 239     -19.757 -43.374 -41.207  1.00 69.00           C  
ANISOU 4228  C   SER B 239    11608   7089   7519  -4036    420    228       C  
ATOM   4229  O   SER B 239     -20.539 -42.881 -42.013  1.00 69.07           O  
ANISOU 4229  O   SER B 239    11441   7334   7467  -4134    460    271       O  
ATOM   4230  CB  SER B 239     -19.934 -45.853 -41.516  1.00 71.16           C  
ANISOU 4230  CB  SER B 239    12400   7258   7379  -4225    433    182       C  
ATOM   4231  OG  SER B 239     -20.324 -46.174 -40.194  1.00 71.52           O  
ANISOU 4231  OG  SER B 239    12564   7315   7296  -4292    365    184       O  
ATOM   4232  N   GLU B 240     -19.513 -42.842 -40.015  1.00 68.48           N  
ANISOU 4232  N   GLU B 240    11491   6953   7576  -3947    356    222       N  
ATOM   4233  CA  GLU B 240     -20.201 -41.643 -39.553  1.00 68.19           C  
ANISOU 4233  CA  GLU B 240    11183   7129   7596  -3979    327    269       C  
ATOM   4234  C   GLU B 240     -19.304 -40.420 -39.640  1.00 66.41           C  
ANISOU 4234  C   GLU B 240    10740   6778   7714  -3766    319    259       C  
ATOM   4235  O   GLU B 240     -19.792 -39.292 -39.706  1.00 65.82           O  
ANISOU 4235  O   GLU B 240    10399   6892   7717  -3778    309    302       O  
ATOM   4236  CB  GLU B 240     -20.672 -41.824 -38.111  1.00 69.67           C  
ANISOU 4236  CB  GLU B 240    11444   7359   7667  -4050    252    269       C  
ATOM   4237  CG  GLU B 240     -21.878 -42.716 -37.951  1.00 71.96           C  
ANISOU 4237  CG  GLU B 240    11871   7873   7597  -4302    254    290       C  
ATOM   4238  CD  GLU B 240     -23.162 -42.035 -38.362  1.00 72.51           C  
ANISOU 4238  CD  GLU B 240    11693   8321   7538  -4456    272    339       C  
ATOM   4239  OE1 GLU B 240     -23.228 -40.789 -38.281  1.00 71.11           O  
ANISOU 4239  OE1 GLU B 240    11231   8249   7537  -4379    255    365       O  
ATOM   4240  OE2 GLU B 240     -24.106 -42.750 -38.762  1.00 74.08           O  
ANISOU 4240  OE2 GLU B 240    11979   8712   7457  -4645    294    343       O  
ATOM   4241  N   MET B 241     -17.994 -40.654 -39.612  1.00 65.53           N  
ANISOU 4241  N   MET B 241    10742   6355   7800  -3564    315    195       N  
ATOM   4242  CA  MET B 241     -17.008 -39.593 -39.785  1.00 63.10           C  
ANISOU 4242  CA  MET B 241    10255   5901   7820  -3346    311    169       C  
ATOM   4243  C   MET B 241     -17.177 -39.001 -41.158  1.00 61.96           C  
ANISOU 4243  C   MET B 241     9929   5893   7720  -3383    384    207       C  
ATOM   4244  O   MET B 241     -16.851 -39.646 -42.137  1.00 55.44           O  
ANISOU 4244  O   MET B 241     9205   5010   6851  -3392    444    188       O  
ATOM   4245  CB  MET B 241     -15.595 -40.157 -39.716  1.00 62.95           C  
ANISOU 4245  CB  MET B 241    10402   5552   7964  -3124    304     79       C  
ATOM   4246  CG  MET B 241     -15.159 -40.645 -38.368  1.00 63.31           C  
ANISOU 4246  CG  MET B 241    10612   5419   8023  -3011    222     26       C  
ATOM   4247  SD  MET B 241     -13.698 -41.692 -38.496  1.00 56.16           S  
ANISOU 4247  SD  MET B 241     9924   4199   7214  -2784    217    -81       S  
ATOM   4248  CE  MET B 241     -12.742 -40.786 -39.702  1.00 55.14           C  
ANISOU 4248  CE  MET B 241     9581   4002   7367  -2622    281   -113       C  
ATOM   4249  N   ILE B 242     -17.670 -37.773 -41.231  1.00 60.74           N  
ANISOU 4249  N   ILE B 242     9506   5921   7653  -3400    370    259       N  
ATOM   4250  CA  ILE B 242     -17.841 -37.097 -42.512  1.00 60.14           C  
ANISOU 4250  CA  ILE B 242     9242   5983   7628  -3418    428    298       C  
ATOM   4251  C   ILE B 242     -16.553 -37.067 -43.327  1.00 59.85           C  
ANISOU 4251  C   ILE B 242     9231   5708   7801  -3253    477    246       C  
ATOM   4252  O   ILE B 242     -16.495 -37.601 -44.429  1.00 60.33           O  
ANISOU 4252  O   ILE B 242     9355   5782   7785  -3301    543    245       O  
ATOM   4253  CB  ILE B 242     -18.321 -35.666 -42.317  1.00 58.52           C  
ANISOU 4253  CB  ILE B 242     8736   5965   7535  -3407    383    349       C  
ATOM   4254  CG1 ILE B 242     -19.732 -35.664 -41.744  1.00 58.72           C  
ANISOU 4254  CG1 ILE B 242     8690   6298   7324  -3587    342    399       C  
ATOM   4255  CG2 ILE B 242     -18.305 -34.923 -43.632  1.00 57.86           C  
ANISOU 4255  CG2 ILE B 242     8472   5978   7535  -3388    433    383       C  
ATOM   4256  CD1 ILE B 242     -20.358 -34.319 -41.779  1.00 57.84           C  
ANISOU 4256  CD1 ILE B 242     8240   6451   7284  -3509    288    441       C  
ATOM   4257  N   ILE B 243     -15.526 -36.435 -42.777  1.00 59.11           N  
ANISOU 4257  N   ILE B 243     9085   5404   7971  -3054    442    196       N  
ATOM   4258  CA  ILE B 243     -14.234 -36.402 -43.435  1.00 58.89           C  
ANISOU 4258  CA  ILE B 243     9076   5153   8148  -2880    483    129       C  
ATOM   4259  C   ILE B 243     -13.557 -37.754 -43.268  1.00 60.20           C  
ANISOU 4259  C   ILE B 243     9513   5115   8245  -2823    488     54       C  
ATOM   4260  O   ILE B 243     -13.211 -38.142 -42.152  1.00 60.19           O  
ANISOU 4260  O   ILE B 243     9634   4968   8266  -2725    425      6       O  
ATOM   4261  CB  ILE B 243     -13.337 -35.294 -42.866  1.00 57.44           C  
ANISOU 4261  CB  ILE B 243     8708   4851   8263  -2611    432     87       C  
ATOM   4262  CG1 ILE B 243     -14.073 -33.956 -42.887  1.00 56.61           C  
ANISOU 4262  CG1 ILE B 243     8284   5013   8210  -2578    388    164       C  
ATOM   4263  CG2 ILE B 243     -12.057 -35.193 -43.664  1.00 57.01           C  
ANISOU 4263  CG2 ILE B 243     8661   4591   8409  -2471    489     16       C  
ATOM   4264  CD1 ILE B 243     -13.271 -32.807 -42.328  1.00 55.39           C  
ANISOU 4264  CD1 ILE B 243     7912   4795   8340  -2274    321    132       C  
ATOM   4265  N   PRO B 244     -13.372 -38.474 -44.385  1.00 61.36           N  
ANISOU 4265  N   PRO B 244     9751   5258   8305  -2880    554     42       N  
ATOM   4266  CA  PRO B 244     -12.823 -39.832 -44.433  1.00 62.99           C  
ANISOU 4266  CA  PRO B 244    10216   5304   8414  -2855    561    -26       C  
ATOM   4267  C   PRO B 244     -11.538 -39.992 -43.638  1.00 63.53           C  
ANISOU 4267  C   PRO B 244    10357   5104   8677  -2604    506   -129       C  
ATOM   4268  O   PRO B 244     -10.724 -39.074 -43.585  1.00 62.30           O  
ANISOU 4268  O   PRO B 244    10042   4856   8773  -2422    494   -167       O  
ATOM   4269  CB  PRO B 244     -12.539 -40.031 -45.920  1.00 62.82           C  
ANISOU 4269  CB  PRO B 244    10179   5308   8382  -2898    643    -31       C  
ATOM   4270  CG  PRO B 244     -13.542 -39.190 -46.593  1.00 62.19           C  
ANISOU 4270  CG  PRO B 244     9899   5485   8246  -3041    677     64       C  
ATOM   4271  CD  PRO B 244     -13.679 -37.968 -45.734  1.00 61.11           C  
ANISOU 4271  CD  PRO B 244     9569   5385   8266  -2967    623     93       C  
ATOM   4272  N   LYS B 245     -11.374 -41.159 -43.026  1.00 65.32           N  
ANISOU 4272  N   LYS B 245    10818   5220   8780  -2587    466   -174       N  
ATOM   4273  CA  LYS B 245     -10.199 -41.447 -42.219  1.00 66.05           C  
ANISOU 4273  CA  LYS B 245    10981   5082   9032  -2334    399   -276       C  
ATOM   4274  C   LYS B 245      -8.923 -41.358 -43.048  1.00 66.10           C  
ANISOU 4274  C   LYS B 245    10925   4957   9233  -2157    428   -362       C  
ATOM   4275  O   LYS B 245      -7.924 -40.789 -42.606  1.00 65.09           O  
ANISOU 4275  O   LYS B 245    10684   4706   9340  -1917    381   -432       O  
ATOM   4276  CB  LYS B 245     -10.327 -42.833 -41.586  1.00 67.57           C  
ANISOU 4276  CB  LYS B 245    11448   5206   9020  -2374    355   -301       C  
ATOM   4277  CG  LYS B 245      -9.069 -43.312 -40.894  1.00 67.63           C  
ANISOU 4277  CG  LYS B 245    11527   4995   9173  -2107    285   -411       C  
ATOM   4278  CD  LYS B 245      -9.235 -44.717 -40.362  1.00 69.03           C  
ANISOU 4278  CD  LYS B 245    11984   5114   9129  -2164    242   -427       C  
ATOM   4279  CE  LYS B 245      -7.960 -45.198 -39.696  1.00 69.14           C  
ANISOU 4279  CE  LYS B 245    12041   4936   9292  -1890    168   -539       C  
ATOM   4280  NZ  LYS B 245      -8.131 -46.541 -39.080  1.00 70.69           N  
ANISOU 4280  NZ  LYS B 245    12514   5076   9271  -1942    116   -547       N  
ATOM   4281  N   ASN B 246      -8.970 -41.908 -44.257  1.00 67.33           N  
ANISOU 4281  N   ASN B 246    11148   5154   9281  -2278    501   -358       N  
ATOM   4282  CA  ASN B 246      -7.813 -41.902 -45.141  1.00 68.02           C  
ANISOU 4282  CA  ASN B 246    11190   5135   9521  -2143    533   -442       C  
ATOM   4283  C   ASN B 246      -7.545 -40.543 -45.776  1.00 67.11           C  
ANISOU 4283  C   ASN B 246    10818   5078   9601  -2100    575   -423       C  
ATOM   4284  O   ASN B 246      -6.616 -40.397 -46.559  1.00 67.20           O  
ANISOU 4284  O   ASN B 246    10772   5026   9734  -2005    606   -489       O  
ATOM   4285  CB  ASN B 246      -7.965 -42.965 -46.228  1.00 69.63           C  
ANISOU 4285  CB  ASN B 246    11559   5362   9537  -2293    599   -446       C  
ATOM   4286  CG  ASN B 246      -7.715 -44.362 -45.711  1.00 71.53           C  
ANISOU 4286  CG  ASN B 246    12059   5480   9640  -2260    548   -504       C  
ATOM   4287  OD1 ASN B 246      -7.711 -44.597 -44.506  1.00 71.79           O  
ANISOU 4287  OD1 ASN B 246    12161   5448   9668  -2175    468   -517       O  
ATOM   4288  ND2 ASN B 246      -7.505 -45.302 -46.625  1.00 72.93           N  
ANISOU 4288  ND2 ASN B 246    12383   5627   9702  -2327    592   -537       N  
ATOM   4289  N   LEU B 247      -8.368 -39.556 -45.441  1.00 66.35           N  
ANISOU 4289  N   LEU B 247    10572   5113   9524  -2175    573   -335       N  
ATOM   4290  CA  LEU B 247      -8.154 -38.195 -45.904  1.00 65.64           C  
ANISOU 4290  CA  LEU B 247    10236   5082   9621  -2126    600   -310       C  
ATOM   4291  C   LEU B 247      -7.747 -37.301 -44.740  1.00 64.98           C  
ANISOU 4291  C   LEU B 247    10031   4921   9737  -1927    523   -335       C  
ATOM   4292  O   LEU B 247      -8.146 -36.140 -44.674  1.00 64.39           O  
ANISOU 4292  O   LEU B 247     9765   4942   9758  -1941    530   -277       O  
ATOM   4293  CB  LEU B 247      -9.419 -37.640 -46.555  1.00 65.17           C  
ANISOU 4293  CB  LEU B 247    10063   5260   9439  -2358    653   -187       C  
ATOM   4294  CG  LEU B 247      -9.860 -38.247 -47.880  1.00 65.78           C  
ANISOU 4294  CG  LEU B 247    10198   5455   9338  -2541    731   -150       C  
ATOM   4295  CD1 LEU B 247     -10.867 -37.334 -48.552  1.00 65.14           C  
ANISOU 4295  CD1 LEU B 247     9925   5617   9210  -2691    764    -39       C  
ATOM   4296  CD2 LEU B 247      -8.669 -38.487 -48.779  1.00 53.87           C  
ANISOU 4296  CD2 LEU B 247     8711   3819   7937  -2439    775   -238       C  
ATOM   4297  N   ALA B 248      -6.958 -37.858 -43.825  1.00 65.06           N  
ANISOU 4297  N   ALA B 248    10146   4769   9807  -1732    444   -423       N  
ATOM   4298  CA  ALA B 248      -6.541 -37.166 -42.606  1.00 63.68           C  
ANISOU 4298  CA  ALA B 248     9877   4523   9796  -1518    352   -452       C  
ATOM   4299  C   ALA B 248      -7.718 -36.624 -41.802  1.00 62.54           C  
ANISOU 4299  C   ALA B 248     9680   4482   9600  -1635    340   -362       C  
ATOM   4300  O   ALA B 248      -7.570 -35.672 -41.044  1.00 60.45           O  
ANISOU 4300  O   ALA B 248     9269   4206   9495  -1490    294   -363       O  
ATOM   4301  CB  ALA B 248      -5.559 -36.056 -42.929  1.00 62.71           C  
ANISOU 4301  CB  ALA B 248     9561   4388   9879  -1325    353   -494       C  
ATOM   4302  N   GLY B 249      -8.883 -37.240 -41.968  1.00 63.86           N  
ANISOU 4302  N   GLY B 249     9964   4773   9526  -1894    375   -287       N  
ATOM   4303  CA  GLY B 249     -10.066 -36.831 -41.239  1.00 63.50           C  
ANISOU 4303  CA  GLY B 249     9884   4865   9378  -2039    350   -203       C  
ATOM   4304  C   GLY B 249     -10.014 -37.251 -39.786  1.00 63.09           C  
ANISOU 4304  C   GLY B 249     9949   4715   9307  -1936    257   -237       C  
ATOM   4305  O   GLY B 249      -9.769 -38.422 -39.486  1.00 64.50           O  
ANISOU 4305  O   GLY B 249    10329   4807   9370  -1918    232   -281       O  
ATOM   4306  N   PRO B 250     -10.242 -36.294 -38.876  1.00 60.57           N  
ANISOU 4306  N   PRO B 250     9469   4447   9099  -1839    197   -214       N  
ATOM   4307  CA  PRO B 250     -10.224 -36.546 -37.435  1.00 50.58           C  
ANISOU 4307  CA  PRO B 250     8288   3101   7827  -1733    102   -241       C  
ATOM   4308  C   PRO B 250     -11.202 -37.647 -37.052  1.00 59.01           C  
ANISOU 4308  C   PRO B 250     9605   4226   8590  -1990     91   -200       C  
ATOM   4309  O   PRO B 250     -12.397 -37.555 -37.351  1.00 59.41           O  
ANISOU 4309  O   PRO B 250     9596   4526   8452  -2224    115   -110       O  
ATOM   4310  CB  PRO B 250     -10.692 -35.213 -36.849  1.00 49.48           C  
ANISOU 4310  CB  PRO B 250     7827   3173   7800  -1619     41   -183       C  
ATOM   4311  CG  PRO B 250     -10.343 -34.217 -37.860  1.00 48.75           C  
ANISOU 4311  CG  PRO B 250     7498   3148   7876  -1546     90   -168       C  
ATOM   4312  CD  PRO B 250     -10.533 -34.884 -39.179  1.00 49.51           C  
ANISOU 4312  CD  PRO B 250     7727   3254   7831  -1770    191   -152       C  
ATOM   4313  N   VAL B 251     -10.690 -38.684 -36.404  1.00 59.13           N  
ANISOU 4313  N   VAL B 251     9804   4109   8552  -1885     47   -262       N  
ATOM   4314  CA  VAL B 251     -11.545 -39.748 -35.908  1.00 59.66           C  
ANISOU 4314  CA  VAL B 251    10090   4246   8330  -2088     27   -227       C  
ATOM   4315  C   VAL B 251     -12.232 -39.253 -34.638  1.00 57.97           C  
ANISOU 4315  C   VAL B 251     9844   4099   8083  -2126    -53   -190       C  
ATOM   4316  O   VAL B 251     -11.703 -39.359 -33.534  1.00 57.38           O  
ANISOU 4316  O   VAL B 251     9812   3898   8091  -1938   -129   -241       O  
ATOM   4317  CB  VAL B 251     -10.749 -41.059 -35.712  1.00 60.87           C  
ANISOU 4317  CB  VAL B 251    10460   4239   8430  -1973      6   -304       C  
ATOM   4318  CG1 VAL B 251      -9.452 -40.790 -34.977  1.00 60.65           C  
ANISOU 4318  CG1 VAL B 251    10342   4036   8667  -1629    -54   -400       C  
ATOM   4319  CG2 VAL B 251     -11.588 -42.121 -35.019  1.00 61.63           C  
ANISOU 4319  CG2 VAL B 251    10797   4389   8229  -2164    -29   -268       C  
ATOM   4320  N   SER B 252     -13.413 -38.674 -34.815  1.00 57.29           N  
ANISOU 4320  N   SER B 252     9629   4263   7877  -2346    -38   -100       N  
ATOM   4321  CA  SER B 252     -14.079 -37.997 -33.713  1.00 56.75           C  
ANISOU 4321  CA  SER B 252     9378   4384   7798  -2305   -115    -63       C  
ATOM   4322  C   SER B 252     -15.573 -37.820 -33.918  1.00 56.94           C  
ANISOU 4322  C   SER B 252     9286   4762   7585  -2577    -94     29       C  
ATOM   4323  O   SER B 252     -16.060 -37.788 -35.043  1.00 57.06           O  
ANISOU 4323  O   SER B 252     9252   4916   7513  -2745    -19     74       O  
ATOM   4324  CB  SER B 252     -13.455 -36.623 -33.500  1.00 55.51           C  
ANISOU 4324  CB  SER B 252     8896   4245   7950  -1997   -153    -81       C  
ATOM   4325  OG  SER B 252     -14.151 -35.910 -32.493  1.00 55.43           O  
ANISOU 4325  OG  SER B 252     8691   4439   7929  -1956   -229    -45       O  
ATOM   4326  N   GLN B 253     -16.290 -37.682 -32.809  1.00 56.82           N  
ANISOU 4326  N   GLN B 253     9219   4902   7468  -2616   -164     50       N  
ATOM   4327  CA  GLN B 253     -17.705 -37.366 -32.854  1.00 57.06           C  
ANISOU 4327  CA  GLN B 253     9091   5299   7289  -2840   -158    123       C  
ATOM   4328  C   GLN B 253     -17.875 -35.864 -33.032  1.00 55.37           C  
ANISOU 4328  C   GLN B 253     8477   5294   7265  -2663   -183    148       C  
ATOM   4329  O   GLN B 253     -18.984 -35.339 -32.967  1.00 55.34           O  
ANISOU 4329  O   GLN B 253     8277   5611   7137  -2780   -199    196       O  
ATOM   4330  CB  GLN B 253     -18.401 -37.832 -31.578  1.00 58.07           C  
ANISOU 4330  CB  GLN B 253     9322   5520   7222  -2958   -224    126       C  
ATOM   4331  CG  GLN B 253     -18.066 -39.253 -31.179  1.00 59.57           C  
ANISOU 4331  CG  GLN B 253     9927   5453   7255  -3083   -228     93       C  
ATOM   4332  CD  GLN B 253     -19.001 -39.789 -30.120  1.00 60.89           C  
ANISOU 4332  CD  GLN B 253    10209   5767   7158  -3291   -277    112       C  
ATOM   4333  OE1 GLN B 253     -20.055 -39.212 -29.858  1.00 61.08           O  
ANISOU 4333  OE1 GLN B 253    10009   6126   7073  -3398   -289    153       O  
ATOM   4334  NE2 GLN B 253     -18.623 -40.900 -29.506  1.00 61.86           N  
ANISOU 4334  NE2 GLN B 253    10687   5643   7172  -3352   -309     78       N  
ATOM   4335  N   HIS B 254     -16.758 -35.176 -33.235  1.00 53.95           N  
ANISOU 4335  N   HIS B 254     8184   4930   7384  -2379   -191    110       N  
ATOM   4336  CA  HIS B 254     -16.782 -33.796 -33.683  1.00 53.04           C  
ANISOU 4336  CA  HIS B 254     7726   4970   7456  -2221   -204    136       C  
ATOM   4337  C   HIS B 254     -16.790 -33.799 -35.207  1.00 53.68           C  
ANISOU 4337  C   HIS B 254     7799   5076   7521  -2340   -111    166       C  
ATOM   4338  O   HIS B 254     -17.034 -32.777 -35.839  1.00 53.37           O  
ANISOU 4338  O   HIS B 254     7507   5200   7573  -2288   -109    203       O  
ATOM   4339  CB  HIS B 254     -15.559 -33.034 -33.172  1.00 52.00           C  
ANISOU 4339  CB  HIS B 254     7479   4630   7648  -1870   -258     81       C  
ATOM   4340  CG  HIS B 254     -15.563 -32.788 -31.693  1.00 51.48           C  
ANISOU 4340  CG  HIS B 254     7364   4565   7631  -1722   -357     56       C  
ATOM   4341  ND1 HIS B 254     -16.222 -31.723 -31.116  1.00 50.54           N  
ANISOU 4341  ND1 HIS B 254     6961   4694   7550  -1638   -430     85       N  
ATOM   4342  CD2 HIS B 254     -14.965 -33.456 -30.677  1.00 51.70           C  
ANISOU 4342  CD2 HIS B 254     7593   4374   7679  -1634   -400      0       C  
ATOM   4343  CE1 HIS B 254     -16.044 -31.756 -29.807  1.00 50.51           C  
ANISOU 4343  CE1 HIS B 254     6979   4628   7583  -1514   -507     51       C  
ATOM   4344  NE2 HIS B 254     -15.284 -32.797 -29.515  1.00 51.20           N  
ANISOU 4344  NE2 HIS B 254     7362   4432   7662  -1511   -491      1       N  
ATOM   4345  N   ASN B 255     -16.517 -34.965 -35.786  1.00 54.75           N  
ANISOU 4345  N   ASN B 255     8222   5042   7537  -2498    -38    149       N  
ATOM   4346  CA  ASN B 255     -16.547 -35.156 -37.232  1.00 51.22           C  
ANISOU 4346  CA  ASN B 255     7808   4609   7044  -2642     57    175       C  
ATOM   4347  C   ASN B 255     -17.854 -35.837 -37.636  1.00 59.76           C  
ANISOU 4347  C   ASN B 255     8986   5920   7799  -2989    102    235       C  
ATOM   4348  O   ASN B 255     -17.911 -36.565 -38.624  1.00 52.99           O  
ANISOU 4348  O   ASN B 255     8294   5018   6821  -3175    184    247       O  
ATOM   4349  CB  ASN B 255     -15.339 -35.996 -37.667  1.00 51.50           C  
ANISOU 4349  CB  ASN B 255     8097   4306   7166  -2580    109    107       C  
ATOM   4350  CG  ASN B 255     -15.083 -35.945 -39.163  1.00 51.52           C  
ANISOU 4350  CG  ASN B 255     8082   4294   7201  -2651    204    119       C  
ATOM   4351  OD1 ASN B 255     -15.830 -35.329 -39.919  1.00 53.09           O  
ANISOU 4351  OD1 ASN B 255     8099   4728   7347  -2762    233    185       O  
ATOM   4352  ND2 ASN B 255     -14.011 -36.594 -39.594  1.00 51.77           N  
ANISOU 4352  ND2 ASN B 255     8305   4049   7318  -2583    248     50       N  
ATOM   4353  N   TYR B 256     -18.903 -35.592 -36.856  1.00 60.00           N  
ANISOU 4353  N   TYR B 256     8906   6206   7686  -3077     46    268       N  
ATOM   4354  CA  TYR B 256     -20.210 -36.193 -37.104  1.00 61.31           C  
ANISOU 4354  CA  TYR B 256     9142   6624   7530  -3411     80    319       C  
ATOM   4355  C   TYR B 256     -21.235 -35.163 -37.551  1.00 61.22           C  
ANISOU 4355  C   TYR B 256     8815   6969   7478  -3462     70    372       C  
ATOM   4356  O   TYR B 256     -21.081 -33.969 -37.296  1.00 60.39           O  
ANISOU 4356  O   TYR B 256     8436   6939   7570  -3234      7    370       O  
ATOM   4357  CB  TYR B 256     -20.738 -36.878 -35.845  1.00 62.06           C  
ANISOU 4357  CB  TYR B 256     9385   6762   7434  -3523     27    307       C  
ATOM   4358  CG  TYR B 256     -20.173 -38.251 -35.596  1.00 63.33           C  
ANISOU 4358  CG  TYR B 256     9937   6631   7495  -3614     48    271       C  
ATOM   4359  CD1 TYR B 256     -19.077 -38.713 -36.306  1.00 63.42           C  
ANISOU 4359  CD1 TYR B 256    10123   6337   7636  -3525     97    234       C  
ATOM   4360  CD2 TYR B 256     -20.749 -39.093 -34.659  1.00 64.68           C  
ANISOU 4360  CD2 TYR B 256    10309   6837   7432  -3795     14    270       C  
ATOM   4361  CE1 TYR B 256     -18.562 -39.967 -36.080  1.00 64.49           C  
ANISOU 4361  CE1 TYR B 256    10591   6234   7678  -3543    101    190       C  
ATOM   4362  CE2 TYR B 256     -20.243 -40.353 -34.429  1.00 65.81           C  
ANISOU 4362  CE2 TYR B 256    10811   6719   7474  -3845     19    235       C  
ATOM   4363  CZ  TYR B 256     -19.150 -40.782 -35.141  1.00 65.79           C  
ANISOU 4363  CZ  TYR B 256    10938   6448   7609  -3677     58    191       C  
ATOM   4364  OH  TYR B 256     -18.641 -42.034 -34.917  1.00 66.99           O  
ANISOU 4364  OH  TYR B 256    11396   6397   7660  -3643     51    147       O  
ATOM   4365  N   ARG B 257     -22.288 -35.640 -38.206  1.00 61.91           N  
ANISOU 4365  N   ARG B 257     8947   7275   7302  -3760    125    416       N  
ATOM   4366  CA  ARG B 257     -23.418 -34.795 -38.561  1.00 61.95           C  
ANISOU 4366  CA  ARG B 257     8672   7647   7218  -3839    108    458       C  
ATOM   4367  C   ARG B 257     -24.658 -35.659 -38.684  1.00 63.63           C  
ANISOU 4367  C   ARG B 257     9002   8097   7077  -4191    149    485       C  
ATOM   4368  O   ARG B 257     -24.648 -36.662 -39.397  1.00 64.39           O  
ANISOU 4368  O   ARG B 257     9321   8113   7033  -4261    218    477       O  
ATOM   4369  CB  ARG B 257     -23.164 -34.072 -39.878  1.00 61.38           C  
ANISOU 4369  CB  ARG B 257     8453   7583   7287  -3774    150    487       C  
ATOM   4370  CG  ARG B 257     -24.125 -32.939 -40.174  1.00 61.22           C  
ANISOU 4370  CG  ARG B 257     8110   7904   7245  -3765    104    520       C  
ATOM   4371  CD  ARG B 257     -23.903 -31.766 -39.250  1.00 60.37           C  
ANISOU 4371  CD  ARG B 257     7752   7841   7345  -3472     -8    497       C  
ATOM   4372  NE  ARG B 257     -24.743 -30.634 -39.623  1.00 60.59           N  
ANISOU 4372  NE  ARG B 257     7478   8174   7369  -3438    -63    523       N  
ATOM   4373  CZ  ARG B 257     -24.536 -29.385 -39.222  1.00 60.06           C  
ANISOU 4373  CZ  ARG B 257     7159   8152   7508  -3171   -160    513       C  
ATOM   4374  NH1 ARG B 257     -23.512 -29.101 -38.436  1.00 59.36           N  
ANISOU 4374  NH1 ARG B 257     7077   7829   7650  -2920   -206    479       N  
ATOM   4375  NH2 ARG B 257     -25.352 -28.419 -39.614  1.00 60.20           N  
ANISOU 4375  NH2 ARG B 257     6925   8449   7500  -3152   -217    534       N  
ATOM   4376  N   PRO B 258     -25.729 -35.277 -37.977  1.00 66.52           N  
ANISOU 4376  N   PRO B 258     8699   8154   8420  -2362  -1179    604       N  
ATOM   4377  CA  PRO B 258     -27.005 -35.998 -38.002  1.00 70.20           C  
ANISOU 4377  CA  PRO B 258     8938   8772   8964  -2666  -1173    672       C  
ATOM   4378  C   PRO B 258     -27.512 -36.229 -39.422  1.00 71.29           C  
ANISOU 4378  C   PRO B 258     8873   8992   9222  -2658  -1357    539       C  
ATOM   4379  O   PRO B 258     -27.829 -35.275 -40.127  1.00 70.86           O  
ANISOU 4379  O   PRO B 258     8603   9167   9155  -2421  -1328    473       O  
ATOM   4380  CB  PRO B 258     -27.947 -35.050 -37.258  1.00 71.15           C  
ANISOU 4380  CB  PRO B 258     8795   9233   9006  -2632   -886    724       C  
ATOM   4381  CG  PRO B 258     -27.059 -34.313 -36.319  1.00 69.16           C  
ANISOU 4381  CG  PRO B 258     8751   8923   8605  -2457   -739    725       C  
ATOM   4382  CD  PRO B 258     -25.755 -34.139 -37.040  1.00 65.93           C  
ANISOU 4382  CD  PRO B 258     8578   8250   8224  -2211   -922    622       C  
ATOM   4383  N   GLY B 259     -27.576 -37.491 -39.832  1.00 73.28           N  
ANISOU 4383  N   GLY B 259     9190   9059   9595  -2919  -1551    501       N  
ATOM   4384  CA  GLY B 259     -28.109 -37.834 -41.136  1.00 75.27           C  
ANISOU 4384  CA  GLY B 259     9239   9426   9934  -2967  -1737    333       C  
ATOM   4385  C   GLY B 259     -27.087 -37.796 -42.253  1.00 73.79           C  
ANISOU 4385  C   GLY B 259     9206   9109   9723  -2741  -1928    140       C  
ATOM   4386  O   GLY B 259     -27.449 -37.725 -43.427  1.00 74.61           O  
ANISOU 4386  O   GLY B 259     9119   9418   9809  -2693  -2063    -10       O  
ATOM   4387  N   TYR B 260     -25.809 -37.844 -41.890  1.00 72.18           N  
ANISOU 4387  N   TYR B 260     9326   8599   9498  -2606  -1939    143       N  
ATOM   4388  CA  TYR B 260     -24.740 -37.838 -42.884  1.00 70.78           C  
ANISOU 4388  CA  TYR B 260     9300   8293   9302  -2395  -2092    -47       C  
ATOM   4389  C   TYR B 260     -23.689 -38.898 -42.597  1.00 71.09           C  
ANISOU 4389  C   TYR B 260     9656   7887   9469  -2481  -2213   -101       C  
ATOM   4390  O   TYR B 260     -23.527 -39.332 -41.462  1.00 71.71           O  
ANISOU 4390  O   TYR B 260     9889   7752   9605  -2617  -2157     77       O  
ATOM   4391  CB  TYR B 260     -24.087 -36.459 -42.971  1.00 67.65           C  
ANISOU 4391  CB  TYR B 260     8922   8017   8766  -2028  -1972     -9       C  
ATOM   4392  CG  TYR B 260     -25.006 -35.411 -43.538  1.00 67.69           C  
ANISOU 4392  CG  TYR B 260     8604   8420   8696  -1885  -1895     35       C  
ATOM   4393  CD1 TYR B 260     -25.032 -35.148 -44.896  1.00 67.60           C  
ANISOU 4393  CD1 TYR B 260     8456   8618   8613  -1748  -2024    -72       C  
ATOM   4394  CD2 TYR B 260     -25.856 -34.696 -42.716  1.00 68.46           C  
ANISOU 4394  CD2 TYR B 260     8518   8700   8794  -1881  -1692    191       C  
ATOM   4395  CE1 TYR B 260     -25.877 -34.199 -45.420  1.00 68.62           C  
ANISOU 4395  CE1 TYR B 260     8276   9111   8687  -1602  -1977     22       C  
ATOM   4396  CE2 TYR B 260     -26.704 -33.744 -43.229  1.00 69.48           C  
ANISOU 4396  CE2 TYR B 260     8327   9162   8908  -1724  -1628    246       C  
ATOM   4397  CZ  TYR B 260     -26.711 -33.498 -44.581  1.00 69.73           C  
ANISOU 4397  CZ  TYR B 260     8229   9379   8884  -1580  -1783    185       C  
ATOM   4398  OH  TYR B 260     -27.560 -32.545 -45.089  1.00 71.41           O  
ANISOU 4398  OH  TYR B 260     8110   9926   9095  -1407  -1741    293       O  
ATOM   4399  N   HIS B 261     -22.976 -39.310 -43.637  1.00 71.18           N  
ANISOU 4399  N   HIS B 261     9748   7777   9522  -2393  -2378   -342       N  
ATOM   4400  CA  HIS B 261     -21.977 -40.355 -43.501  1.00 71.76           C  
ANISOU 4400  CA  HIS B 261    10086   7406   9774  -2445  -2505   -433       C  
ATOM   4401  C   HIS B 261     -20.663 -39.908 -44.116  1.00 70.04           C  
ANISOU 4401  C   HIS B 261    10005   7121   9485  -2132  -2540   -589       C  
ATOM   4402  O   HIS B 261     -20.541 -38.780 -44.585  1.00 68.19           O  
ANISOU 4402  O   HIS B 261     9675   7174   9062  -1898  -2456   -591       O  
ATOM   4403  CB  HIS B 261     -22.466 -41.640 -44.168  1.00 74.44           C  
ANISOU 4403  CB  HIS B 261    10368   7592  10323  -2721  -2678   -649       C  
ATOM   4404  CG  HIS B 261     -23.777 -42.124 -43.641  1.00 76.61           C  
ANISOU 4404  CG  HIS B 261    10478   7932  10696  -3063  -2643   -504       C  
ATOM   4405  ND1 HIS B 261     -23.875 -43.117 -42.691  1.00 78.81           N  
ANISOU 4405  ND1 HIS B 261    10889   7853  11204  -3332  -2652   -325       N  
ATOM   4406  CD2 HIS B 261     -25.045 -41.739 -43.917  1.00 77.69           C  
ANISOU 4406  CD2 HIS B 261    10311   8465  10744  -3182  -2595   -488       C  
ATOM   4407  CE1 HIS B 261     -25.148 -43.328 -42.409  1.00 81.40           C  
ANISOU 4407  CE1 HIS B 261    11001   8353  11572  -3621  -2593   -215       C  
ATOM   4408  NE2 HIS B 261     -25.879 -42.505 -43.140  1.00 80.74           N  
ANISOU 4408  NE2 HIS B 261    10642   8731  11304  -3532  -2561   -327       N  
ATOM   4409  N   THR B 262     -19.681 -40.798 -44.110  1.00 70.97           N  
ANISOU 4409  N   THR B 262    10333   6848   9785  -2130  -2658   -707       N  
ATOM   4410  CA  THR B 262     -18.368 -40.477 -44.641  1.00 69.89           C  
ANISOU 4410  CA  THR B 262    10314   6630   9609  -1847  -2683   -868       C  
ATOM   4411  C   THR B 262     -18.438 -40.082 -46.106  1.00 71.31           C  
ANISOU 4411  C   THR B 262    10334   7130   9631  -1729  -2712  -1133       C  
ATOM   4412  O   THR B 262     -18.749 -40.906 -46.960  1.00 74.47           O  
ANISOU 4412  O   THR B 262    10663   7531  10102  -1863  -2830  -1398       O  
ATOM   4413  CB  THR B 262     -17.407 -41.652 -44.466  1.00 70.93           C  
ANISOU 4413  CB  THR B 262    10581   6394   9974  -1792  -2699   -937       C  
ATOM   4414  OG1 THR B 262     -17.369 -42.024 -43.083  1.00 71.69           O  
ANISOU 4414  OG1 THR B 262    10807   6257  10175  -1891  -2680   -632       O  
ATOM   4415  CG2 THR B 262     -16.018 -41.264 -44.906  1.00 68.55           C  
ANISOU 4415  CG2 THR B 262    10339   6085   9622  -1474  -2651  -1059       C  
ATOM   4416  N   GLN B 263     -18.155 -38.815 -46.388  1.00 69.80           N  
ANISOU 4416  N   GLN B 263    10078   7222   9221  -1484  -2595  -1054       N  
ATOM   4417  CA  GLN B 263     -18.196 -38.306 -47.754  1.00 71.17           C  
ANISOU 4417  CA  GLN B 263    10095   7752   9193  -1356  -2611  -1223       C  
ATOM   4418  C   GLN B 263     -16.969 -38.737 -48.550  1.00 71.57           C  
ANISOU 4418  C   GLN B 263    10258   7671   9262  -1226  -2677  -1513       C  
ATOM   4419  O   GLN B 263     -16.129 -37.908 -48.891  1.00 69.35           O  
ANISOU 4419  O   GLN B 263     9996   7498   8855   -990  -2589  -1492       O  
ATOM   4420  CB  GLN B 263     -18.287 -36.779 -47.753  1.00 69.99           C  
ANISOU 4420  CB  GLN B 263     9837   7905   8853  -1136  -2452   -989       C  
ATOM   4421  CG  GLN B 263     -19.391 -36.214 -46.870  1.00 70.53           C  
ANISOU 4421  CG  GLN B 263     9782   8091   8925  -1214  -2346   -721       C  
ATOM   4422  CD  GLN B 263     -20.772 -36.461 -47.428  1.00 73.47           C  
ANISOU 4422  CD  GLN B 263     9904   8767   9244  -1390  -2420   -742       C  
ATOM   4423  OE1 GLN B 263     -21.147 -35.897 -48.454  1.00 73.97           O  
ANISOU 4423  OE1 GLN B 263     9776   9192   9138  -1290  -2447   -757       O  
ATOM   4424  NE2 GLN B 263     -21.541 -37.309 -46.754  1.00 75.59           N  
ANISOU 4424  NE2 GLN B 263    10158   8908   9654  -1664  -2458   -723       N  
ATOM   4425  N   ILE B 264     -16.880 -40.029 -48.856  1.00 74.62           N  
ANISOU 4425  N   ILE B 264    10685   7840   9826  -1372  -2781  -1777       N  
ATOM   4426  CA  ILE B 264     -15.749 -40.562 -49.611  1.00 75.74           C  
ANISOU 4426  CA  ILE B 264    10856   7920  10003  -1217  -2710  -2033       C  
ATOM   4427  C   ILE B 264     -15.779 -40.082 -51.059  1.00 76.15           C  
ANISOU 4427  C   ILE B 264    10771   8407   9755  -1146  -2748  -2273       C  
ATOM   4428  O   ILE B 264     -14.734 -39.921 -51.691  1.00 75.98           O  
ANISOU 4428  O   ILE B 264    10774   8443   9653   -965  -2675  -2419       O  
ATOM   4429  CB  ILE B 264     -15.715 -42.105 -49.593  1.00 79.14           C  
ANISOU 4429  CB  ILE B 264    11299   8066  10705  -1359  -2692  -2207       C  
ATOM   4430  CG1 ILE B 264     -16.064 -42.645 -48.205  1.00 79.63           C  
ANISOU 4430  CG1 ILE B 264    11459   7780  11018  -1492  -2697  -1927       C  
ATOM   4431  CG2 ILE B 264     -14.351 -42.619 -50.034  1.00 79.68           C  
ANISOU 4431  CG2 ILE B 264    11424   7984  10868  -1176  -2602  -2400       C  
ATOM   4432  CD1 ILE B 264     -16.023 -44.162 -48.104  1.00 83.19           C  
ANISOU 4432  CD1 ILE B 264    11933   7905  11770  -1624  -2691  -2050       C  
ATOM   4433  N   THR B 265     -16.979 -39.853 -51.579  1.00 77.01           N  
ANISOU 4433  N   THR B 265    10714   8864   9682  -1293  -2866  -2295       N  
ATOM   4434  CA  THR B 265     -17.121 -39.387 -52.949  1.00 78.26           C  
ANISOU 4434  CA  THR B 265    10710   9533   9493  -1228  -2919  -2469       C  
ATOM   4435  C   THR B 265     -17.531 -37.919 -52.992  1.00 75.51           C  
ANISOU 4435  C   THR B 265    10226   9569   8893  -1063  -2806  -2071       C  
ATOM   4436  O   THR B 265     -18.348 -37.515 -53.821  1.00 77.76           O  
ANISOU 4436  O   THR B 265    10298  10331   8918  -1086  -2857  -2034       O  
ATOM   4437  CB  THR B 265     -18.133 -40.230 -53.737  1.00 83.17           C  
ANISOU 4437  CB  THR B 265    11150  10403  10047  -1475  -3006  -2717       C  
ATOM   4438  OG1 THR B 265     -18.207 -41.543 -53.171  1.00 85.52           O  
ANISOU 4438  OG1 THR B 265    11531  10268  10695  -1671  -2960  -2834       O  
ATOM   4439  CG2 THR B 265     -17.710 -40.339 -55.193  1.00 86.04           C  
ANISOU 4439  CG2 THR B 265    11432  11150  10108  -1422  -2988  -3009       C  
ATOM   4440  N   GLY B 266     -16.960 -37.128 -52.090  1.00 71.04           N  
ANISOU 4440  N   GLY B 266     9775   8790   8427   -896  -2660  -1778       N  
ATOM   4441  CA  GLY B 266     -17.121 -35.687 -52.132  1.00 68.55           C  
ANISOU 4441  CA  GLY B 266     9351   8749   7945   -704  -2527  -1429       C  
ATOM   4442  C   GLY B 266     -16.163 -35.108 -53.149  1.00 68.27           C  
ANISOU 4442  C   GLY B 266     9305   8943   7690   -503  -2461  -1479       C  
ATOM   4443  O   GLY B 266     -15.348 -35.832 -53.712  1.00 69.95           O  
ANISOU 4443  O   GLY B 266     9599   9097   7882   -508  -2503  -1804       O  
ATOM   4444  N   PRO B 267     -16.254 -33.798 -53.398  1.00 67.20           N  
ANISOU 4444  N   PRO B 267     9058   9064   7411   -325  -2345  -1155       N  
ATOM   4445  CA  PRO B 267     -15.404 -33.158 -54.405  1.00 67.95           C  
ANISOU 4445  CA  PRO B 267     9122   9418   7280   -150  -2262  -1131       C  
ATOM   4446  C   PRO B 267     -13.983 -32.919 -53.916  1.00 65.90           C  
ANISOU 4446  C   PRO B 267     9041   8814   7184    -13  -2123  -1155       C  
ATOM   4447  O   PRO B 267     -13.490 -31.797 -53.986  1.00 64.90           O  
ANISOU 4447  O   PRO B 267     8887   8740   7031    156  -1973   -898       O  
ATOM   4448  CB  PRO B 267     -16.100 -31.819 -54.638  1.00 68.03           C  
ANISOU 4448  CB  PRO B 267     8946   9731   7173    -17  -2187   -701       C  
ATOM   4449  CG  PRO B 267     -16.795 -31.537 -53.368  1.00 66.18           C  
ANISOU 4449  CG  PRO B 267     8720   9217   7208    -48  -2144   -514       C  
ATOM   4450  CD  PRO B 267     -17.242 -32.866 -52.834  1.00 66.38           C  
ANISOU 4450  CD  PRO B 267     8820   9043   7357   -286  -2282   -793       C  
ATOM   4451  N   TRP B 268     -13.322 -33.971 -53.452  1.00 65.86           N  
ANISOU 4451  N   TRP B 268     9199   8455   7369    -88  -2180  -1456       N  
ATOM   4452  CA  TRP B 268     -11.964 -33.845 -52.947  1.00 64.33           C  
ANISOU 4452  CA  TRP B 268     9151   7940   7351     38  -2078  -1499       C  
ATOM   4453  C   TRP B 268     -10.951 -33.731 -54.087  1.00 67.05           C  
ANISOU 4453  C   TRP B 268     9455   8517   7506    153  -2003  -1669       C  
ATOM   4454  O   TRP B 268      -9.744 -33.755 -53.858  1.00 66.89           O  
ANISOU 4454  O   TRP B 268     9520   8273   7624    253  -1925  -1769       O  
ATOM   4455  CB  TRP B 268     -11.614 -35.030 -52.040  1.00 62.70           C  
ANISOU 4455  CB  TRP B 268     9114   7272   7437    -62  -2183  -1720       C  
ATOM   4456  CG  TRP B 268     -12.676 -35.353 -51.034  1.00 61.06           C  
ANISOU 4456  CG  TRP B 268     8937   6891   7373   -224  -2261  -1580       C  
ATOM   4457  CD1 TRP B 268     -13.483 -36.448 -51.026  1.00 62.40           C  
ANISOU 4457  CD1 TRP B 268     9104   6995   7611   -431  -2409  -1744       C  
ATOM   4458  CD2 TRP B 268     -13.050 -34.570 -49.896  1.00 58.29           C  
ANISOU 4458  CD2 TRP B 268     8609   6426   7113   -207  -2177  -1263       C  
ATOM   4459  NE1 TRP B 268     -14.336 -36.399 -49.952  1.00 61.29           N  
ANISOU 4459  NE1 TRP B 268     8979   6721   7587   -550  -2415  -1514       N  
ATOM   4460  CE2 TRP B 268     -14.090 -35.254 -49.242  1.00 58.76           C  
ANISOU 4460  CE2 TRP B 268     8675   6386   7267   -409  -2270  -1232       C  
ATOM   4461  CE3 TRP B 268     -12.606 -33.357 -49.367  1.00 55.91           C  
ANISOU 4461  CE3 TRP B 268     8313   6097   6835    -53  -2021  -1027       C  
ATOM   4462  CZ2 TRP B 268     -14.695 -34.765 -48.087  1.00 57.53           C  
ANISOU 4462  CZ2 TRP B 268     8526   6147   7185   -452  -2200   -976       C  
ATOM   4463  CZ3 TRP B 268     -13.206 -32.873 -48.219  1.00 54.71           C  
ANISOU 4463  CZ3 TRP B 268     8173   5839   6777    -92  -1962   -811       C  
ATOM   4464  CH2 TRP B 268     -14.239 -33.575 -47.593  1.00 55.57           C  
ANISOU 4464  CH2 TRP B 268     8285   5893   6937   -286  -2045   -787       C  
ATOM   4465  N   HIS B 269     -11.444 -33.610 -55.315  1.00 70.14           N  
ANISOU 4465  N   HIS B 269     9696   9392   7563    133  -2025  -1698       N  
ATOM   4466  CA  HIS B 269     -10.565 -33.435 -56.461  1.00 72.46           C  
ANISOU 4466  CA  HIS B 269     9929  10001   7604    227  -1930  -1832       C  
ATOM   4467  C   HIS B 269     -10.238 -31.961 -56.639  1.00 72.38           C  
ANISOU 4467  C   HIS B 269     9844  10159   7497    385  -1748  -1403       C  
ATOM   4468  O   HIS B 269      -9.398 -31.594 -57.459  1.00 73.58           O  
ANISOU 4468  O   HIS B 269     9944  10549   7463    472  -1621  -1413       O  
ATOM   4469  CB  HIS B 269     -11.215 -33.990 -57.727  1.00 76.20           C  
ANISOU 4469  CB  HIS B 269    10269  10977   7708    119  -2043  -2068       C  
ATOM   4470  CG  HIS B 269     -12.510 -33.328 -58.082  1.00 77.46           C  
ANISOU 4470  CG  HIS B 269    10265  11529   7635     81  -2113  -1737       C  
ATOM   4471  ND1 HIS B 269     -13.733 -33.817 -57.672  1.00 78.03           N  
ANISOU 4471  ND1 HIS B 269    10296  11559   7793    -74  -2278  -1754       N  
ATOM   4472  CD2 HIS B 269     -12.775 -32.222 -58.817  1.00 78.70           C  
ANISOU 4472  CD2 HIS B 269    10272  12132   7499    182  -2044  -1360       C  
ATOM   4473  CE1 HIS B 269     -14.693 -33.038 -58.136  1.00 79.20           C  
ANISOU 4473  CE1 HIS B 269    10261  12120   7712    -53  -2314  -1424       C  
ATOM   4474  NE2 HIS B 269     -14.139 -32.062 -58.833  1.00 79.68           N  
ANISOU 4474  NE2 HIS B 269    10257  12472   7544    109  -2181  -1165       N  
ATOM   4475  N   LEU B 270     -10.905 -31.123 -55.856  1.00 71.42           N  
ANISOU 4475  N   LEU B 270     9708   9900   7526    416  -1721  -1031       N  
ATOM   4476  CA  LEU B 270     -10.704 -29.683 -55.925  1.00 71.80           C  
ANISOU 4476  CA  LEU B 270     9682  10026   7574    563  -1549   -608       C  
ATOM   4477  C   LEU B 270      -9.364 -29.257 -55.327  1.00 70.54           C  
ANISOU 4477  C   LEU B 270     9624   9516   7662    659  -1388   -613       C  
ATOM   4478  O   LEU B 270      -8.736 -28.315 -55.806  1.00 71.22           O  
ANISOU 4478  O   LEU B 270     9642   9720   7696    762  -1222   -393       O  
ATOM   4479  CB  LEU B 270     -11.855 -28.961 -55.229  1.00 70.84           C  
ANISOU 4479  CB  LEU B 270     9496   9829   7592    574  -1563   -272       C  
ATOM   4480  CG  LEU B 270     -13.233 -29.185 -55.849  1.00 72.91           C  
ANISOU 4480  CG  LEU B 270     9600  10482   7621    495  -1719   -201       C  
ATOM   4481  CD1 LEU B 270     -14.317 -28.490 -55.041  1.00 71.97           C  
ANISOU 4481  CD1 LEU B 270     9398  10246   7701    523  -1711    102       C  
ATOM   4482  CD2 LEU B 270     -13.246 -28.701 -57.285  1.00 75.81           C  
ANISOU 4482  CD2 LEU B 270     9808  11393   7606    561  -1706    -29       C  
ATOM   4483  N   GLY B 271      -8.928 -29.955 -54.283  1.00 69.07           N  
ANISOU 4483  N   GLY B 271     9587   8911   7747    616  -1443   -845       N  
ATOM   4484  CA  GLY B 271      -7.669 -29.636 -53.633  1.00 67.60           C  
ANISOU 4484  CA  GLY B 271     9479   8404   7801    696  -1329   -878       C  
ATOM   4485  C   GLY B 271      -7.836 -28.557 -52.585  1.00 65.58           C  
ANISOU 4485  C   GLY B 271     9239   7898   7781    742  -1235   -586       C  
ATOM   4486  O   GLY B 271      -7.517 -28.759 -51.414  1.00 63.64           O  
ANISOU 4486  O   GLY B 271     9106   7304   7772    720  -1268   -669       O  
ATOM   4487  N   LYS B 272      -8.328 -27.400 -53.011  1.00 66.47           N  
ANISOU 4487  N   LYS B 272     9230   8196   7831    809  -1120   -245       N  
ATOM   4488  CA  LYS B 272      -8.640 -26.325 -52.085  1.00 65.90           C  
ANISOU 4488  CA  LYS B 272     9145   7886   8006    858  -1019      5       C  
ATOM   4489  C   LYS B 272     -10.147 -26.111 -52.080  1.00 66.72           C  
ANISOU 4489  C   LYS B 272     9158   8143   8047    841  -1081    205       C  
ATOM   4490  O   LYS B 272     -10.756 -25.954 -53.140  1.00 69.09           O  
ANISOU 4490  O   LYS B 272     9328   8806   8119    866  -1108    370       O  
ATOM   4491  CB  LYS B 272      -7.916 -25.036 -52.485  1.00 67.16           C  
ANISOU 4491  CB  LYS B 272     9216   8042   8260    968   -809    258       C  
ATOM   4492  CG  LYS B 272      -8.150 -23.872 -51.529  1.00 66.98           C  
ANISOU 4492  CG  LYS B 272     9173   7725   8554   1022   -685    461       C  
ATOM   4493  CD  LYS B 272      -7.375 -22.621 -51.936  1.00 68.71           C  
ANISOU 4493  CD  LYS B 272     9300   7879   8929   1109   -472    705       C  
ATOM   4494  CE  LYS B 272      -7.659 -21.466 -50.974  1.00 68.54           C  
ANISOU 4494  CE  LYS B 272     9247   7525   9271   1158   -345    851       C  
ATOM   4495  NZ  LYS B 272      -6.916 -20.219 -51.307  1.00 69.94           N  
ANISOU 4495  NZ  LYS B 272     9331   7565   9680   1224   -131   1088       N  
ATOM   4496  N   LEU B 273     -10.748 -26.117 -50.893  1.00 64.89           N  
ANISOU 4496  N   LEU B 273     8979   7675   8003    795  -1105    188       N  
ATOM   4497  CA  LEU B 273     -12.192 -25.933 -50.777  1.00 65.11           C  
ANISOU 4497  CA  LEU B 273     8894   7837   8009    778  -1150    354       C  
ATOM   4498  C   LEU B 273     -12.640 -25.524 -49.380  1.00 63.38           C  
ANISOU 4498  C   LEU B 273     8706   7337   8037    762  -1082    371       C  
ATOM   4499  O   LEU B 273     -11.892 -25.638 -48.410  1.00 61.86           O  
ANISOU 4499  O   LEU B 273     8654   6864   7987    728  -1049    211       O  
ATOM   4500  CB  LEU B 273     -12.932 -27.199 -51.189  1.00 65.59           C  
ANISOU 4500  CB  LEU B 273     8953   8117   7854    637  -1350    178       C  
ATOM   4501  CG  LEU B 273     -12.625 -28.439 -50.365  1.00 64.13           C  
ANISOU 4501  CG  LEU B 273     8945   7685   7735    492  -1464   -132       C  
ATOM   4502  CD1 LEU B 273     -13.882 -29.257 -50.213  1.00 65.30           C  
ANISOU 4502  CD1 LEU B 273     9049   7941   7821    337  -1608   -186       C  
ATOM   4503  CD2 LEU B 273     -11.549 -29.250 -51.045  1.00 64.46           C  
ANISOU 4503  CD2 LEU B 273     9074   7739   7677    480  -1524   -388       C  
ATOM   4504  N   GLU B 274     -13.878 -25.054 -49.296  1.00 63.59           N  
ANISOU 4504  N   GLU B 274     8584   7479   8098    789  -1064    556       N  
ATOM   4505  CA  GLU B 274     -14.445 -24.586 -48.044  1.00 62.41           C  
ANISOU 4505  CA  GLU B 274     8423   7126   8164    783   -968    562       C  
ATOM   4506  C   GLU B 274     -15.840 -25.181 -47.891  1.00 63.27           C  
ANISOU 4506  C   GLU B 274     8429   7425   8187    681  -1070    571       C  
ATOM   4507  O   GLU B 274     -16.798 -24.692 -48.494  1.00 64.86           O  
ANISOU 4507  O   GLU B 274     8421   7849   8374    760  -1070    782       O  
ATOM   4508  CB  GLU B 274     -14.520 -23.059 -48.054  1.00 62.67           C  
ANISOU 4508  CB  GLU B 274     8316   7058   8436    966   -772    802       C  
ATOM   4509  CG  GLU B 274     -14.658 -22.416 -46.685  1.00 61.48           C  
ANISOU 4509  CG  GLU B 274     8182   6630   8547    975   -621    714       C  
ATOM   4510  CD  GLU B 274     -13.328 -22.213 -45.995  1.00 59.33           C  
ANISOU 4510  CD  GLU B 274     8076   6074   8393    954   -546    527       C  
ATOM   4511  OE1 GLU B 274     -12.285 -22.495 -46.616  1.00 58.77           O  
ANISOU 4511  OE1 GLU B 274     8088   6002   8239    952   -594    494       O  
ATOM   4512  OE2 GLU B 274     -13.324 -21.770 -44.829  1.00 58.51           O  
ANISOU 4512  OE2 GLU B 274     8002   5774   8456    935   -437    394       O  
ATOM   4513  N   MET B 275     -15.955 -26.242 -47.097  1.00 62.41           N  
ANISOU 4513  N   MET B 275     8450   7232   8032    501  -1162    365       N  
ATOM   4514  CA  MET B 275     -17.238 -26.924 -46.949  1.00 63.03           C  
ANISOU 4514  CA  MET B 275     8427   7483   8038    361  -1257    361       C  
ATOM   4515  C   MET B 275     -17.946 -26.580 -45.641  1.00 61.63           C  
ANISOU 4515  C   MET B 275     8211   7202   8004    317  -1130    371       C  
ATOM   4516  O   MET B 275     -17.316 -26.450 -44.592  1.00 59.87           O  
ANISOU 4516  O   MET B 275     8136   6749   7863    295  -1042    269       O  
ATOM   4517  CB  MET B 275     -17.090 -28.442 -47.124  1.00 63.40           C  
ANISOU 4517  CB  MET B 275     8607   7540   7942    160  -1453    154       C  
ATOM   4518  CG  MET B 275     -16.664 -29.216 -45.891  1.00 62.28           C  
ANISOU 4518  CG  MET B 275     8672   7123   7867     12  -1473      5       C  
ATOM   4519  SD  MET B 275     -17.903 -30.436 -45.402  1.00 64.92           S  
ANISOU 4519  SD  MET B 275     8973   7524   8169   -262  -1591    -39       S  
ATOM   4520  CE  MET B 275     -17.075 -31.242 -44.038  1.00 41.93           C  
ANISOU 4520  CE  MET B 275     6336   4270   5326   -396  -1617   -136       C  
ATOM   4521  N   ASP B 276     -19.262 -26.413 -45.728  1.00 62.65           N  
ANISOU 4521  N   ASP B 276     8116   7540   8148    306  -1119    486       N  
ATOM   4522  CA  ASP B 276     -20.074 -26.066 -44.562  1.00 62.60           C  
ANISOU 4522  CA  ASP B 276     8022   7498   8266    268   -971    484       C  
ATOM   4523  C   ASP B 276     -21.526 -26.505 -44.724  1.00 64.11           C  
ANISOU 4523  C   ASP B 276     7983   7961   8416    158  -1033    549       C  
ATOM   4524  O   ASP B 276     -21.832 -27.371 -45.542  1.00 64.99           O  
ANISOU 4524  O   ASP B 276     8059   8252   8383     42  -1224    536       O  
ATOM   4525  CB  ASP B 276     -19.996 -24.565 -44.262  1.00 62.53           C  
ANISOU 4525  CB  ASP B 276     7905   7368   8487    498   -750    574       C  
ATOM   4526  CG  ASP B 276     -20.205 -23.707 -45.492  1.00 63.73           C  
ANISOU 4526  CG  ASP B 276     7858   7644   8713    716   -755    816       C  
ATOM   4527  OD1 ASP B 276     -20.741 -24.213 -46.498  1.00 64.63           O  
ANISOU 4527  OD1 ASP B 276     7857   8032   8667    685   -924    920       O  
ATOM   4528  OD2 ASP B 276     -19.837 -22.516 -45.449  1.00 64.08           O  
ANISOU 4528  OD2 ASP B 276     7854   7514   8981    911   -594    910       O  
ATOM   4529  N   PHE B 277     -22.417 -25.901 -43.947  1.00 64.62           N  
ANISOU 4529  N   PHE B 277     7870   8066   8618    190   -865    588       N  
ATOM   4530  CA  PHE B 277     -23.810 -26.318 -43.959  1.00 66.32           C  
ANISOU 4530  CA  PHE B 277     7837   8543   8817     70   -902    637       C  
ATOM   4531  C   PHE B 277     -24.788 -25.168 -44.225  1.00 68.30           C  
ANISOU 4531  C   PHE B 277     7740   8950   9261    295   -782    808       C  
ATOM   4532  O   PHE B 277     -25.224 -24.470 -43.308  1.00 69.15           O  
ANISOU 4532  O   PHE B 277     7736   8994   9542    365   -563    776       O  
ATOM   4533  CB  PHE B 277     -24.137 -27.062 -42.665  1.00 66.66           C  
ANISOU 4533  CB  PHE B 277     7970   8540   8817   -182   -828    508       C  
ATOM   4534  CG  PHE B 277     -23.261 -28.255 -42.430  1.00 65.52           C  
ANISOU 4534  CG  PHE B 277     8142   8229   8526   -394   -972    392       C  
ATOM   4535  CD1 PHE B 277     -22.098 -28.143 -41.688  1.00 64.10           C  
ANISOU 4535  CD1 PHE B 277     8230   7793   8332   -370   -912    303       C  
ATOM   4536  CD2 PHE B 277     -23.587 -29.486 -42.970  1.00 66.74           C  
ANISOU 4536  CD2 PHE B 277     8308   8468   8583   -610  -1178    363       C  
ATOM   4537  CE1 PHE B 277     -21.282 -29.239 -41.477  1.00 63.07           C  
ANISOU 4537  CE1 PHE B 277     8366   7496   8102   -535  -1060    224       C  
ATOM   4538  CE2 PHE B 277     -22.775 -30.588 -42.764  1.00 65.83           C  
ANISOU 4538  CE2 PHE B 277     8471   8145   8397   -782  -1310    260       C  
ATOM   4539  CZ  PHE B 277     -21.621 -30.463 -42.016  1.00 63.94           C  
ANISOU 4539  CZ  PHE B 277     8490   7650   8153   -732  -1254    209       C  
ATOM   4540  N   ASP B 278     -25.105 -24.981 -45.503  1.00 68.88           N  
ANISOU 4540  N   ASP B 278     7634   9237   9298    414   -932    986       N  
ATOM   4541  CA  ASP B 278     -26.080 -23.999 -45.960  1.00 71.11           C  
ANISOU 4541  CA  ASP B 278     7554   9702   9763    641   -882   1211       C  
ATOM   4542  C   ASP B 278     -26.469 -24.435 -47.364  1.00 72.49           C  
ANISOU 4542  C   ASP B 278     7576  10226   9741    628  -1149   1359       C  
ATOM   4543  O   ASP B 278     -25.840 -25.329 -47.924  1.00 71.61           O  
ANISOU 4543  O   ASP B 278     7666  10158   9384    473  -1323   1250       O  
ATOM   4544  CB  ASP B 278     -25.474 -22.593 -45.979  1.00 70.50           C  
ANISOU 4544  CB  ASP B 278     7477   9376   9936    948   -706   1346       C  
ATOM   4545  CG  ASP B 278     -26.523 -21.501 -46.145  1.00 73.32           C  
ANISOU 4545  CG  ASP B 278     7447   9824  10586   1205   -605   1570       C  
ATOM   4546  OD1 ASP B 278     -27.730 -21.802 -46.009  1.00 75.17           O  
ANISOU 4546  OD1 ASP B 278     7410  10314  10838   1141   -633   1576       O  
ATOM   4547  OD2 ASP B 278     -26.139 -20.338 -46.396  1.00 73.67           O  
ANISOU 4547  OD2 ASP B 278     7446   9668  10878   1473   -492   1743       O  
ATOM   4548  N   PHE B 279     -27.504 -23.829 -47.935  1.00 74.99           N  
ANISOU 4548  N   PHE B 279     7524  10807  10160    792  -1190   1590       N  
ATOM   4549  CA  PHE B 279     -27.889 -24.173 -49.295  1.00 76.81           C  
ANISOU 4549  CA  PHE B 279     7585  11437  10162    785  -1462   1741       C  
ATOM   4550  C   PHE B 279     -26.913 -23.536 -50.268  1.00 76.75           C  
ANISOU 4550  C   PHE B 279     7694  11402  10064    989  -1505   1944       C  
ATOM   4551  O   PHE B 279     -26.210 -22.593 -49.916  1.00 76.33           O  
ANISOU 4551  O   PHE B 279     7752  11024  10225   1182  -1311   2036       O  
ATOM   4552  CB  PHE B 279     -29.305 -23.689 -49.599  1.00 80.57           C  
ANISOU 4552  CB  PHE B 279     7597  12238  10776    912  -1512   1960       C  
ATOM   4553  CG  PHE B 279     -30.341 -24.219 -48.656  1.00 81.36           C  
ANISOU 4553  CG  PHE B 279     7526  12400  10987    718  -1438   1783       C  
ATOM   4554  CD1 PHE B 279     -30.962 -25.432 -48.901  1.00 82.15           C  
ANISOU 4554  CD1 PHE B 279     7546  12784  10881    407  -1637   1628       C  
ATOM   4555  CD2 PHE B 279     -30.702 -23.499 -47.529  1.00 81.51           C  
ANISOU 4555  CD2 PHE B 279     7446  12200  11322    833  -1154   1756       C  
ATOM   4556  CE1 PHE B 279     -31.917 -25.922 -48.036  1.00 82.97           C  
ANISOU 4556  CE1 PHE B 279     7478  12952  11096    204  -1552   1493       C  
ATOM   4557  CE2 PHE B 279     -31.658 -23.983 -46.660  1.00 82.36           C  
ANISOU 4557  CE2 PHE B 279     7380  12409  11505    642  -1059   1601       C  
ATOM   4558  CZ  PHE B 279     -32.266 -25.198 -46.915  1.00 83.14           C  
ANISOU 4558  CZ  PHE B 279     7401  12790  11398    322  -1256   1492       C  
ATOM   4559  N   CYS B 280     -26.858 -24.055 -51.488  1.00 77.49           N  
ANISOU 4559  N   CYS B 280     7757  11850   9837    927  -1750   1998       N  
ATOM   4560  CA  CYS B 280     -26.103 -23.388 -52.536  1.00 77.70           C  
ANISOU 4560  CA  CYS B 280     7825  11959   9739   1123  -1790   2257       C  
ATOM   4561  C   CYS B 280     -26.931 -22.216 -53.030  1.00 80.84           C  
ANISOU 4561  C   CYS B 280     7858  12540  10319   1417  -1794   2698       C  
ATOM   4562  O   CYS B 280     -28.159 -22.245 -52.954  1.00 83.35           O  
ANISOU 4562  O   CYS B 280     7856  13092  10723   1423  -1871   2762       O  
ATOM   4563  CB  CYS B 280     -25.796 -24.345 -53.682  1.00 78.54           C  
ANISOU 4563  CB  CYS B 280     8001  12442   9398    953  -2041   2140       C  
ATOM   4564  SG  CYS B 280     -24.688 -25.696 -53.235  1.00 70.74           S  
ANISOU 4564  SG  CYS B 280     7436  11188   8256    656  -2044   1643       S  
ATOM   4565  N   ASP B 281     -26.257 -21.186 -53.527  1.00 80.93           N  
ANISOU 4565  N   ASP B 281     7902  12432  10418   1661  -1708   3018       N  
ATOM   4566  CA  ASP B 281     -26.917 -19.946 -53.925  1.00 84.02           C  
ANISOU 4566  CA  ASP B 281     7966  12887  11071   1979  -1684   3492       C  
ATOM   4567  C   ASP B 281     -28.019 -20.154 -54.962  1.00 87.79           C  
ANISOU 4567  C   ASP B 281     8081  13971  11302   2004  -1976   3740       C  
ATOM   4568  O   ASP B 281     -27.744 -20.416 -56.131  1.00 89.54           O  
ANISOU 4568  O   ASP B 281     8355  14546  11120   1939  -2143   3826       O  
ATOM   4569  CB  ASP B 281     -25.885 -18.949 -54.448  1.00 84.04           C  
ANISOU 4569  CB  ASP B 281     8093  12679  11160   2186  -1569   3820       C  
ATOM   4570  CG  ASP B 281     -24.874 -18.557 -53.396  1.00 80.36           C  
ANISOU 4570  CG  ASP B 281     7920  11610  11005   2187  -1280   3598       C  
ATOM   4571  OD1 ASP B 281     -25.056 -17.498 -52.760  1.00 81.08           O  
ANISOU 4571  OD1 ASP B 281     7904  11328  11574   2398  -1072   3729       O  
ATOM   4572  OD2 ASP B 281     -23.899 -19.311 -53.202  1.00 76.94           O  
ANISOU 4572  OD2 ASP B 281     7807  11077  10351   1981  -1266   3274       O  
ATOM   4573  N   GLY B 282     -29.268 -20.035 -54.524  1.00 89.31           N  
ANISOU 4573  N   GLY B 282     7944  14260  11732   2060  -1995   3769       N  
ATOM   4574  CA  GLY B 282     -30.400 -20.179 -55.419  1.00 92.97           C  
ANISOU 4574  CA  GLY B 282     8111  15211  12002   2036  -2219   3894       C  
ATOM   4575  C   GLY B 282     -30.792 -21.620 -55.680  1.00 92.10           C  
ANISOU 4575  C   GLY B 282     7956  15549  11490   1706  -2483   3574       C  
ATOM   4576  O   GLY B 282     -31.251 -21.957 -56.768  1.00 95.27           O  
ANISOU 4576  O   GLY B 282     8270  16374  11555   1611  -2692   3589       O  
ATOM   4577  N   THR B 283     -30.606 -22.473 -54.680  1.00 88.14           N  
ANISOU 4577  N   THR B 283     7632  14821  11037   1464  -2396   3164       N  
ATOM   4578  CA  THR B 283     -31.036 -23.861 -54.778  1.00 87.57           C  
ANISOU 4578  CA  THR B 283     7556  15036  10679   1099  -2593   2789       C  
ATOM   4579  C   THR B 283     -31.996 -24.207 -53.650  1.00 87.23           C  
ANISOU 4579  C   THR B 283     7348  14872  10924    961  -2483   2584       C  
ATOM   4580  O   THR B 283     -32.084 -23.495 -52.652  1.00 86.19           O  
ANISOU 4580  O   THR B 283     7203  14376  11170   1114  -2216   2632       O  
ATOM   4581  CB  THR B 283     -29.854 -24.827 -54.722  1.00 83.64           C  
ANISOU 4581  CB  THR B 283     7511  14335   9933    847  -2580   2413       C  
ATOM   4582  OG1 THR B 283     -29.023 -24.490 -53.607  1.00 79.78           O  
ANISOU 4582  OG1 THR B 283     7326  13263   9722    899  -2284   2313       O  
ATOM   4583  CG2 THR B 283     -29.038 -24.737 -55.991  1.00 84.40           C  
ANISOU 4583  CG2 THR B 283     7719  14698   9653    915  -2722   2546       C  
ATOM   4584  N   THR B 284     -32.715 -25.308 -53.818  1.00 88.29           N  
ANISOU 4584  N   THR B 284     7346  15323  10877    654  -2680   2338       N  
ATOM   4585  CA  THR B 284     -33.672 -25.752 -52.820  1.00 88.73           C  
ANISOU 4585  CA  THR B 284     7219  15324  11169    469  -2584   2151       C  
ATOM   4586  C   THR B 284     -33.444 -27.219 -52.489  1.00 88.27           C  
ANISOU 4586  C   THR B 284     7413  15182  10946     36  -2644   1722       C  
ATOM   4587  O   THR B 284     -33.451 -28.071 -53.375  1.00 89.89           O  
ANISOU 4587  O   THR B 284     7615  15689  10849   -173  -2908   1562       O  
ATOM   4588  CB  THR B 284     -35.117 -25.561 -53.310  1.00 92.66           C  
ANISOU 4588  CB  THR B 284     7159  16326  11722    523  -2770   2337       C  
ATOM   4589  OG1 THR B 284     -35.273 -26.179 -54.594  1.00 94.78           O  
ANISOU 4589  OG1 THR B 284     7315  17105  11591    386  -3128   2314       O  
ATOM   4590  CG2 THR B 284     -35.443 -24.083 -53.428  1.00 94.60           C  
ANISOU 4590  CG2 THR B 284     7126  16567  12251    976  -2676   2780       C  
ATOM   4591  N   VAL B 285     -33.230 -27.510 -51.212  1.00 86.65           N  
ANISOU 4591  N   VAL B 285     7420  14563  10941   -101  -2399   1536       N  
ATOM   4592  CA  VAL B 285     -33.075 -28.889 -50.772  1.00 86.58           C  
ANISOU 4592  CA  VAL B 285     7634  14418  10845   -508  -2439   1187       C  
ATOM   4593  C   VAL B 285     -34.154 -29.220 -49.751  1.00 88.34           C  
ANISOU 4593  C   VAL B 285     7625  14644  11294   -710  -2306   1118       C  
ATOM   4594  O   VAL B 285     -34.490 -28.396 -48.903  1.00 88.37           O  
ANISOU 4594  O   VAL B 285     7508  14527  11540   -532  -2056   1247       O  
ATOM   4595  CB  VAL B 285     -31.681 -29.143 -50.164  1.00 83.28           C  
ANISOU 4595  CB  VAL B 285     7731  13505  10406   -541  -2288   1035       C  
ATOM   4596  CG1 VAL B 285     -31.472 -30.624 -49.904  1.00 83.23           C  
ANISOU 4596  CG1 VAL B 285     7950  13355  10321   -942  -2380    712       C  
ATOM   4597  CG2 VAL B 285     -30.600 -28.625 -51.086  1.00 70.00           C  
ANISOU 4597  CG2 VAL B 285     6243  11813   8540   -308  -2358   1135       C  
ATOM   4598  N   VAL B 286     -34.709 -30.423 -49.847  1.00 90.27           N  
ANISOU 4598  N   VAL B 286     7791  15035  11471  -1090  -2463    899       N  
ATOM   4599  CA  VAL B 286     -35.717 -30.870 -48.899  1.00 92.42           C  
ANISOU 4599  CA  VAL B 286     7847  15326  11944  -1342  -2333    835       C  
ATOM   4600  C   VAL B 286     -35.427 -32.294 -48.444  1.00 92.36           C  
ANISOU 4600  C   VAL B 286     8117  15069  11904  -1780  -2363    564       C  
ATOM   4601  O   VAL B 286     -34.518 -32.951 -48.952  1.00 78.20           O  
ANISOU 4601  O   VAL B 286     6647  13111   9953  -1873  -2511    399       O  
ATOM   4602  CB  VAL B 286     -37.130 -30.803 -49.499  1.00 85.13           C  
ANISOU 4602  CB  VAL B 286     6357  14923  11066  -1380  -2502    910       C  
ATOM   4603  CG1 VAL B 286     -37.560 -29.361 -49.691  1.00 86.43           C  
ANISOU 4603  CG1 VAL B 286     6200  15275  11366   -932  -2426   1224       C  
ATOM   4604  CG2 VAL B 286     -37.178 -31.557 -50.814  1.00 87.23           C  
ANISOU 4604  CG2 VAL B 286     6556  15515  11072  -1552  -2877    765       C  
ATOM   4605  N   VAL B 287     -36.206 -32.765 -47.479  1.00 93.89           N  
ANISOU 4605  N   VAL B 287     8173  15231  12270  -2046  -2212    531       N  
ATOM   4606  CA  VAL B 287     -36.052 -34.117 -46.969  1.00 93.70           C  
ANISOU 4606  CA  VAL B 287     8379  14950  12274  -2479  -2228    337       C  
ATOM   4607  C   VAL B 287     -37.185 -34.977 -47.510  1.00 98.50           C  
ANISOU 4607  C   VAL B 287     8616  15879  12928  -2827  -2435    207       C  
ATOM   4608  O   VAL B 287     -38.346 -34.788 -47.147  1.00101.53           O  
ANISOU 4608  O   VAL B 287     8590  16531  13454  -2908  -2345    292       O  
ATOM   4609  CB  VAL B 287     -36.094 -34.139 -45.437  1.00 92.01           C  
ANISOU 4609  CB  VAL B 287     8288  14474  12198  -2592  -1900    414       C  
ATOM   4610  CG1 VAL B 287     -35.402 -35.381 -44.908  1.00 90.66           C  
ANISOU 4610  CG1 VAL B 287     8519  13900  12028  -2932  -1915    291       C  
ATOM   4611  CG2 VAL B 287     -35.436 -32.891 -44.879  1.00 88.83           C  
ANISOU 4611  CG2 VAL B 287     8038  13924  11790  -2192  -1663    556       C  
ATOM   4612  N   THR B 288     -36.849 -35.917 -48.385  1.00 99.72           N  
ANISOU 4612  N   THR B 288     8895  16017  12977  -3036  -2708    -28       N  
ATOM   4613  CA  THR B 288     -37.862 -36.763 -48.999  1.00104.67           C  
ANISOU 4613  CA  THR B 288     9173  16951  13647  -3387  -2936   -211       C  
ATOM   4614  C   THR B 288     -37.364 -38.193 -49.143  1.00104.95           C  
ANISOU 4614  C   THR B 288     9499  16653  13725  -3778  -3077   -517       C  
ATOM   4615  O   THR B 288     -36.301 -38.432 -49.710  1.00103.61           O  
ANISOU 4615  O   THR B 288     9668  16287  13413  -3685  -3193   -673       O  
ATOM   4616  CB  THR B 288     -38.274 -36.227 -50.378  1.00107.87           C  
ANISOU 4616  CB  THR B 288     9240  17899  13847  -3187  -3218   -220       C  
ATOM   4617  OG1 THR B 288     -38.676 -34.857 -50.260  1.00107.85           O  
ANISOU 4617  OG1 THR B 288     8974  18144  13860  -2783  -3091    100       O  
ATOM   4618  CG2 THR B 288     -39.428 -37.039 -50.937  1.00113.32           C  
ANISOU 4618  CG2 THR B 288     9507  18962  14586  -3562  -3456   -421       C  
ATOM   4619  N   GLU B 289     -38.142 -39.139 -48.629  1.00106.97           N  
ANISOU 4619  N   GLU B 289     9606  16832  14205  -4215  -3054   -601       N  
ATOM   4620  CA  GLU B 289     -37.789 -40.552 -48.693  1.00107.50           C  
ANISOU 4620  CA  GLU B 289     9913  16523  14408  -4619  -3176   -881       C  
ATOM   4621  C   GLU B 289     -37.784 -41.030 -50.145  1.00108.90           C  
ANISOU 4621  C   GLU B 289    10042  16875  14461  -4597  -3473  -1235       C  
ATOM   4622  O   GLU B 289     -37.137 -42.022 -50.483  1.00109.34           O  
ANISOU 4622  O   GLU B 289    10401  16550  14593  -4715  -3561  -1524       O  
ATOM   4623  CB  GLU B 289     -38.771 -41.370 -47.847  1.00111.36           C  
ANISOU 4623  CB  GLU B 289    10209  16905  15199  -5066  -3054   -845       C  
ATOM   4624  CG  GLU B 289     -38.430 -42.847 -47.687  1.00113.45           C  
ANISOU 4624  CG  GLU B 289    10788  16605  15713  -5386  -3077  -1064       C  
ATOM   4625  CD  GLU B 289     -39.473 -43.597 -46.872  1.00117.58           C  
ANISOU 4625  CD  GLU B 289    11112  17018  16544  -5768  -2918   -979       C  
ATOM   4626  OE1 GLU B 289     -40.314 -42.935 -46.229  1.00118.24           O  
ANISOU 4626  OE1 GLU B 289    10874  17428  16624  -5789  -2741   -727       O  
ATOM   4627  OE2 GLU B 289     -39.457 -44.847 -46.875  1.00120.35           O  
ANISOU 4627  OE2 GLU B 289    11609  16956  17162  -6035  -2956  -1167       O  
ATOM   4628  N   ASP B 290     -38.497 -40.303 -51.000  1.00109.78           N  
ANISOU 4628  N   ASP B 290     9790  17526  14394  -4379  -3600  -1200       N  
ATOM   4629  CA  ASP B 290     -38.586 -40.628 -52.420  1.00111.70           C  
ANISOU 4629  CA  ASP B 290     9986  17987  14466  -4296  -3861  -1489       C  
ATOM   4630  C   ASP B 290     -37.299 -40.281 -53.172  1.00107.84           C  
ANISOU 4630  C   ASP B 290     9833  17462  13681  -3999  -3944  -1567       C  
ATOM   4631  O   ASP B 290     -37.019 -40.840 -54.233  1.00109.82           O  
ANISOU 4631  O   ASP B 290    10192  17730  13802  -3989  -4123  -1869       O  
ATOM   4632  CB  ASP B 290     -39.780 -39.901 -53.047  1.00114.81           C  
ANISOU 4632  CB  ASP B 290     9894  18973  14754  -4145  -3967  -1355       C  
ATOM   4633  CG  ASP B 290     -39.940 -40.203 -54.520  1.00118.36           C  
ANISOU 4633  CG  ASP B 290    10291  19695  14984  -4081  -4243  -1613       C  
ATOM   4634  OD1 ASP B 290     -39.634 -41.342 -54.924  1.00120.20           O  
ANISOU 4634  OD1 ASP B 290    10734  19648  15287  -4309  -4350  -1974       O  
ATOM   4635  OD2 ASP B 290     -40.371 -39.302 -55.271  1.00119.66           O  
ANISOU 4635  OD2 ASP B 290    10206  20343  14916  -3800  -4349  -1441       O  
ATOM   4636  N   CYS B 291     -36.518 -39.361 -52.615  1.00102.75           N  
ANISOU 4636  N   CYS B 291     9341  16766  12932  -3765  -3806  -1294       N  
ATOM   4637  CA  CYS B 291     -35.278 -38.912 -53.246  1.00 99.39           C  
ANISOU 4637  CA  CYS B 291     9215  16317  12234  -3469  -3852  -1321       C  
ATOM   4638  C   CYS B 291     -34.295 -40.060 -53.458  1.00 98.81           C  
ANISOU 4638  C   CYS B 291     9549  15771  12221  -3618  -3894  -1695       C  
ATOM   4639  O   CYS B 291     -34.360 -41.075 -52.768  1.00 99.68           O  
ANISOU 4639  O   CYS B 291     9785  15453  12637  -3927  -3838  -1837       O  
ATOM   4640  CB  CYS B 291     -34.621 -37.820 -52.402  1.00 94.60           C  
ANISOU 4640  CB  CYS B 291     8767  15556  11621  -3168  -3624   -954       C  
ATOM   4641  SG  CYS B 291     -33.303 -36.939 -53.243  1.00 87.86           S  
ANISOU 4641  SG  CYS B 291     8181  14763  10437  -2723  -3643   -880       S  
ATOM   4642  N   GLY B 292     -33.386 -39.895 -54.413  1.00 97.73           N  
ANISOU 4642  N   GLY B 292     9611  15703  11819  -3382  -3977  -1833       N  
ATOM   4643  CA  GLY B 292     -32.412 -40.927 -54.722  1.00 91.41           C  
ANISOU 4643  CA  GLY B 292     9169  14476  11086  -3464  -4014  -2201       C  
ATOM   4644  C   GLY B 292     -31.490 -41.221 -53.557  1.00109.77           C  
ANISOU 4644  C   GLY B 292    11833  16232  13643  -3540  -3851  -2154       C  
ATOM   4645  O   GLY B 292     -31.363 -40.407 -52.643  1.00106.55           O  
ANISOU 4645  O   GLY B 292    11451  15792  13240  -3457  -3707  -1803       O  
ATOM   4646  N   ASN B 293     -30.852 -42.387 -53.581  1.00102.51           N  
ANISOU 4646  N   ASN B 293    13017  15430  10504  -6410  -1392    956       N  
ATOM   4647  CA  ASN B 293     -29.900 -42.750 -52.535  1.00100.50           C  
ANISOU 4647  CA  ASN B 293    13039  14866  10280  -6374  -1327   1039       C  
ATOM   4648  C   ASN B 293     -28.597 -41.970 -52.687  1.00 96.34           C  
ANISOU 4648  C   ASN B 293    12612  14218   9776  -6113  -1320   1048       C  
ATOM   4649  O   ASN B 293     -28.383 -41.300 -53.698  1.00 94.90           O  
ANISOU 4649  O   ASN B 293    12319  14150   9587  -5987  -1378    999       O  
ATOM   4650  CB  ASN B 293     -29.619 -44.255 -52.548  1.00102.15           C  
ANISOU 4650  CB  ASN B 293    13580  14714  10517  -6556  -1410   1006       C  
ATOM   4651  CG  ASN B 293     -28.949 -44.738 -51.268  1.00100.88           C  
ANISOU 4651  CG  ASN B 293    13661  14299  10370  -6561  -1334   1121       C  
ATOM   4652  OD1 ASN B 293     -29.197 -44.206 -50.186  1.00 99.89           O  
ANISOU 4652  OD1 ASN B 293    13399  14336  10220  -6535  -1212   1225       O  
ATOM   4653  ND2 ASN B 293     -28.090 -45.743 -51.390  1.00101.02           N  
ANISOU 4653  ND2 ASN B 293    14033  13932  10417  -6582  -1416   1093       N  
ATOM   4654  N   ARG B 294     -27.734 -42.057 -51.680  1.00 94.21           N  
ANISOU 4654  N   ARG B 294    12535  13732   9530  -6039  -1251   1115       N  
ATOM   4655  CA  ARG B 294     -26.457 -41.356 -51.705  1.00 90.62           C  
ANISOU 4655  CA  ARG B 294    12172  13143   9116  -5805  -1236   1119       C  
ATOM   4656  C   ARG B 294     -25.528 -41.870 -52.802  1.00 89.29           C  
ANISOU 4656  C   ARG B 294    12249  12738   8940  -5758  -1365   1036       C  
ATOM   4657  O   ARG B 294     -25.384 -43.079 -52.995  1.00 91.12           O  
ANISOU 4657  O   ARG B 294    12742  12733   9148  -5880  -1450    985       O  
ATOM   4658  CB  ARG B 294     -25.767 -41.413 -50.334  1.00 89.68           C  
ANISOU 4658  CB  ARG B 294    12197  12865   9011  -5744  -1144   1189       C  
ATOM   4659  CG  ARG B 294     -25.685 -42.797 -49.716  1.00 91.43           C  
ANISOU 4659  CG  ARG B 294    12710  12838   9192  -5912  -1169   1224       C  
ATOM   4660  CD  ARG B 294     -24.959 -42.770 -48.377  1.00 90.28           C  
ANISOU 4660  CD  ARG B 294    12687  12582   9035  -5835  -1085   1300       C  
ATOM   4661  NE  ARG B 294     -23.505 -42.747 -48.526  1.00 87.94           N  
ANISOU 4661  NE  ARG B 294    12633  12016   8764  -5654  -1123   1263       N  
ATOM   4662  CZ  ARG B 294     -22.709 -41.833 -47.979  1.00 85.57           C  
ANISOU 4662  CZ  ARG B 294    12275  11737   8501  -5466  -1053   1266       C  
ATOM   4663  NH1 ARG B 294     -21.398 -41.887 -48.164  1.00 83.86           N  
ANISOU 4663  NH1 ARG B 294    12278  11275   8310  -5319  -1093   1229       N  
ATOM   4664  NH2 ARG B 294     -23.222 -40.865 -47.241  1.00 85.24           N  
ANISOU 4664  NH2 ARG B 294    11947  11965   8476  -5429   -948   1296       N  
ATOM   4665  N   GLY B 295     -24.917 -40.935 -53.524  1.00 86.15           N  
ANISOU 4665  N   GLY B 295    11753  12413   8567  -5583  -1384   1024       N  
ATOM   4666  CA  GLY B 295     -23.961 -41.255 -54.569  1.00 85.00           C  
ANISOU 4666  CA  GLY B 295    11806  12102   8388  -5513  -1509    944       C  
ATOM   4667  C   GLY B 295     -22.921 -40.158 -54.636  1.00 82.05           C  
ANISOU 4667  C   GLY B 295    11377  11716   8083  -5186  -1429    998       C  
ATOM   4668  O   GLY B 295     -22.880 -39.311 -53.749  1.00 81.31           O  
ANISOU 4668  O   GLY B 295    11137  11676   8083  -5100  -1304   1076       O  
ATOM   4669  N   PRO B 296     -22.082 -40.162 -55.684  1.00 80.82           N  
ANISOU 4669  N   PRO B 296    11324  11497   7887  -4958  -1486    951       N  
ATOM   4670  CA  PRO B 296     -21.017 -39.168 -55.848  1.00 78.19           C  
ANISOU 4670  CA  PRO B 296    10938  11135   7637  -4615  -1392   1019       C  
ATOM   4671  C   PRO B 296     -21.545 -37.755 -55.694  1.00 76.76           C  
ANISOU 4671  C   PRO B 296    10408  11185   7571  -4497  -1277   1130       C  
ATOM   4672  O   PRO B 296     -22.675 -37.482 -56.093  1.00 78.06           O  
ANISOU 4672  O   PRO B 296    10351  11611   7696  -4586  -1300   1146       O  
ATOM   4673  CB  PRO B 296     -20.559 -39.388 -57.286  1.00 79.01           C  
ANISOU 4673  CB  PRO B 296    11104  11287   7628  -4445  -1482    968       C  
ATOM   4674  CG  PRO B 296     -20.855 -40.810 -57.553  1.00 81.23           C  
ANISOU 4674  CG  PRO B 296    11626  11453   7785  -4671  -1640    818       C  
ATOM   4675  CD  PRO B 296     -22.128 -41.103 -56.815  1.00 82.57           C  
ANISOU 4675  CD  PRO B 296    11697  11696   7980  -5014  -1648    823       C  
ATOM   4676  N   SER B 297     -20.741 -36.874 -55.113  1.00 74.28           N  
ANISOU 4676  N   SER B 297    10043  10772   7408  -4293  -1164   1190       N  
ATOM   4677  CA  SER B 297     -21.178 -35.507 -54.883  1.00 73.18           C  
ANISOU 4677  CA  SER B 297     9592  10795   7419  -4165  -1062   1278       C  
ATOM   4678  C   SER B 297     -21.362 -34.793 -56.213  1.00 74.29           C  
ANISOU 4678  C   SER B 297     9552  11122   7553  -3981  -1067   1370       C  
ATOM   4679  O   SER B 297     -20.506 -34.866 -57.091  1.00 73.90           O  
ANISOU 4679  O   SER B 297     9601  11011   7468  -3817  -1082   1401       O  
ATOM   4680  CB  SER B 297     -20.170 -34.760 -54.014  1.00 70.73           C  
ANISOU 4680  CB  SER B 297     9278  10300   7296  -3987   -960   1289       C  
ATOM   4681  OG  SER B 297     -20.729 -33.561 -53.509  1.00 70.34           O  
ANISOU 4681  OG  SER B 297     8947  10372   7406  -3906   -877   1330       O  
ATOM   4682  N   LEU B 298     -22.492 -34.116 -56.364  1.00 76.04           N  
ANISOU 4682  N   LEU B 298     9503  11598   7790  -3993  -1053   1422       N  
ATOM   4683  CA  LEU B 298     -22.778 -33.402 -57.596  1.00 77.58           C  
ANISOU 4683  CA  LEU B 298     9511  12002   7962  -3800  -1057   1536       C  
ATOM   4684  C   LEU B 298     -22.524 -31.915 -57.418  1.00 77.09           C  
ANISOU 4684  C   LEU B 298     9240  11911   8141  -3552   -934   1675       C  
ATOM   4685  O   LEU B 298     -22.430 -31.420 -56.295  1.00 76.50           O  
ANISOU 4685  O   LEU B 298     9115  11713   8238  -3557   -865   1640       O  
ATOM   4686  CB  LEU B 298     -24.223 -33.643 -58.031  1.00 80.39           C  
ANISOU 4686  CB  LEU B 298     9695  12684   8166  -3950  -1141   1501       C  
ATOM   4687  CG  LEU B 298     -24.585 -35.088 -58.375  1.00 82.47           C  
ANISOU 4687  CG  LEU B 298    10137  12978   8218  -4213  -1283   1352       C  
ATOM   4688  CD1 LEU B 298     -26.019 -35.194 -58.835  1.00 85.02           C  
ANISOU 4688  CD1 LEU B 298    10235  13653   8416  -4354  -1367   1311       C  
ATOM   4689  CD2 LEU B 298     -23.662 -35.624 -59.441  1.00 82.63           C  
ANISOU 4689  CD2 LEU B 298    10358  12916   8123  -4080  -1351   1329       C  
ATOM   4690  N   ARG B 299     -22.398 -31.213 -58.538  1.00 77.49           N  
ANISOU 4690  N   ARG B 299     9170  12071   8203  -3326   -911   1831       N  
ATOM   4691  CA  ARG B 299     -22.242 -29.769 -58.534  1.00 62.09           C  
ANISOU 4691  CA  ARG B 299     7013  10076   6503  -3088   -802   1995       C  
ATOM   4692  C   ARG B 299     -23.557 -29.166 -58.995  1.00 72.53           C  
ANISOU 4692  C   ARG B 299     8074  11706   7776  -3029   -825   2072       C  
ATOM   4693  O   ARG B 299     -24.250 -29.749 -59.822  1.00 73.86           O  
ANISOU 4693  O   ARG B 299     8220  12143   7702  -3085   -918   2057       O  
ATOM   4694  CB  ARG B 299     -21.119 -29.372 -59.490  1.00 62.51           C  
ANISOU 4694  CB  ARG B 299     7109  10030   6611  -2863   -741   2169       C  
ATOM   4695  CG  ARG B 299     -20.720 -27.908 -59.446  1.00 62.92           C  
ANISOU 4695  CG  ARG B 299     6982   9941   6983  -2639   -617   2359       C  
ATOM   4696  CD  ARG B 299     -19.628 -27.622 -60.465  1.00 62.45           C  
ANISOU 4696  CD  ARG B 299     6955   9820   6952  -2448   -546   2564       C  
ATOM   4697  NE  ARG B 299     -20.104 -27.797 -61.833  1.00 74.57           N  
ANISOU 4697  NE  ARG B 299     8435  11670   8226  -2338   -588   2706       N  
ATOM   4698  CZ  ARG B 299     -19.344 -27.670 -62.916  1.00 76.16           C  
ANISOU 4698  CZ  ARG B 299     8648  11934   8355  -2158   -534   2903       C  
ATOM   4699  NH1 ARG B 299     -18.058 -27.374 -62.796  1.00 75.66           N  
ANISOU 4699  NH1 ARG B 299     8642  11627   8480  -2088   -431   2986       N  
ATOM   4700  NH2 ARG B 299     -19.869 -27.843 -64.120  1.00 78.32           N  
ANISOU 4700  NH2 ARG B 299     8859  12545   8355  -2041   -584   3012       N  
ATOM   4701  N   THR B 300     -23.904 -28.006 -58.454  1.00 72.90           N  
ANISOU 4701  N   THR B 300     7920  11722   8056  -2902   -753   2134       N  
ATOM   4702  CA  THR B 300     -25.148 -27.336 -58.820  1.00 75.04           C  
ANISOU 4702  CA  THR B 300     7930  12285   8298  -2804   -773   2207       C  
ATOM   4703  C   THR B 300     -25.227 -26.962 -60.303  1.00 76.54           C  
ANISOU 4703  C   THR B 300     8035  12664   8382  -2585   -783   2426       C  
ATOM   4704  O   THR B 300     -26.319 -26.866 -60.864  1.00 78.68           O  
ANISOU 4704  O   THR B 300     8130  13269   8496  -2542   -846   2455       O  
ATOM   4705  CB  THR B 300     -25.359 -26.080 -57.979  1.00 75.39           C  
ANISOU 4705  CB  THR B 300     7790  12211   8644  -2656   -695   2227       C  
ATOM   4706  OG1 THR B 300     -24.145 -25.321 -57.951  1.00 74.90           O  
ANISOU 4706  OG1 THR B 300     7787  11805   8868  -2488   -602   2341       O  
ATOM   4707  CG2 THR B 300     -25.732 -26.459 -56.567  1.00 74.43           C  
ANISOU 4707  CG2 THR B 300     7675  12071   8532  -2858   -704   1999       C  
ATOM   4708  N   THR B 301     -24.072 -26.754 -60.931  1.00 75.71           N  
ANISOU 4708  N   THR B 301     8039  12379   8349  -2437   -719   2583       N  
ATOM   4709  CA  THR B 301     -24.021 -26.390 -62.347  1.00 68.70           C  
ANISOU 4709  CA  THR B 301     7076  11685   7342  -2204   -708   2826       C  
ATOM   4710  C   THR B 301     -23.505 -27.539 -63.214  1.00 76.65           C  
ANISOU 4710  C   THR B 301     8268  12811   8044  -2265   -779   2773       C  
ATOM   4711  O   THR B 301     -22.571 -28.237 -62.828  1.00 75.23           O  
ANISOU 4711  O   THR B 301     8302  12408   7873  -2386   -775   2655       O  
ATOM   4712  CB  THR B 301     -23.127 -25.165 -62.579  1.00 72.15           C  
ANISOU 4712  CB  THR B 301     7454  11872   8086  -1955   -565   3103       C  
ATOM   4713  OG1 THR B 301     -21.753 -25.552 -62.486  1.00 67.45           O  
ANISOU 4713  OG1 THR B 301     7052  11017   7557  -2001   -509   3093       O  
ATOM   4714  CG2 THR B 301     -23.417 -24.088 -61.548  1.00 72.22           C  
ANISOU 4714  CG2 THR B 301     7324  11662   8452  -1908   -506   3091       C  
ATOM   4715  N   THR B 302     -24.110 -27.732 -64.384  1.00 78.61           N  
ANISOU 4715  N   THR B 302     8428  13424   8015  -2156   -854   2844       N  
ATOM   4716  CA  THR B 302     -23.684 -28.800 -65.294  1.00 79.19           C  
ANISOU 4716  CA  THR B 302     8660  13651   7779  -2176   -941   2764       C  
ATOM   4717  C   THR B 302     -22.602 -28.342 -66.267  1.00 79.89           C  
ANISOU 4717  C   THR B 302     8770  13730   7854  -1903   -838   3030       C  
ATOM   4718  O   THR B 302     -22.206 -27.179 -66.265  1.00 79.65           O  
ANISOU 4718  O   THR B 302     8629  13559   8077  -1717   -695   3302       O  
ATOM   4719  CB  THR B 302     -24.864 -29.394 -66.098  1.00 81.26           C  
ANISOU 4719  CB  THR B 302     8816  14353   7707  -2208  -1101   2648       C  
ATOM   4720  OG1 THR B 302     -24.357 -30.249 -67.131  1.00 82.50           O  
ANISOU 4720  OG1 THR B 302     9106  14669   7572  -2149  -1182   2587       O  
ATOM   4721  CG2 THR B 302     -25.682 -28.302 -66.738  1.00 82.86           C  
ANISOU 4721  CG2 THR B 302     8740  14845   7897  -1949  -1071   2885       C  
ATOM   4722  N   ALA B 303     -22.134 -29.266 -67.102  1.00 81.28           N  
ANISOU 4722  N   ALA B 303     9082  14061   7739  -1878   -912   2948       N  
ATOM   4723  CA  ALA B 303     -21.083 -28.967 -68.068  1.00 83.04           C  
ANISOU 4723  CA  ALA B 303     9321  14339   7892  -1620   -813   3189       C  
ATOM   4724  C   ALA B 303     -21.532 -27.921 -69.080  1.00 86.82           C  
ANISOU 4724  C   ALA B 303     9561  15116   8311  -1317   -744   3535       C  
ATOM   4725  O   ALA B 303     -20.708 -27.232 -69.674  1.00 87.45           O  
ANISOU 4725  O   ALA B 303     9593  15179   8455  -1092   -600   3850       O  
ATOM   4726  CB  ALA B 303     -20.636 -30.234 -68.777  1.00 83.61           C  
ANISOU 4726  CB  ALA B 303     9573  14576   7618  -1632   -932   2984       C  
ATOM   4727  N   SER B 304     -22.842 -27.813 -69.278  1.00 89.45           N  
ANISOU 4727  N   SER B 304     9736  15734   8516  -1311   -846   3490       N  
ATOM   4728  CA  SER B 304     -23.386 -26.816 -70.186  1.00 93.05           C  
ANISOU 4728  CA  SER B 304     9962  16489   8905  -1005   -794   3818       C  
ATOM   4729  C   SER B 304     -23.536 -25.482 -69.468  1.00 93.09           C  
ANISOU 4729  C   SER B 304     9834  16208   9326   -940   -658   4051       C  
ATOM   4730  O   SER B 304     -23.356 -24.425 -70.068  1.00 94.92           O  
ANISOU 4730  O   SER B 304     9938  16469   9659   -665   -534   4432       O  
ATOM   4731  CB  SER B 304     -24.736 -27.266 -70.744  1.00 95.84           C  
ANISOU 4731  CB  SER B 304    10181  17306   8929   -999   -976   3653       C  
ATOM   4732  OG  SER B 304     -25.754 -27.181 -69.761  1.00 95.38           O  
ANISOU 4732  OG  SER B 304    10038  17174   9028  -1206  -1037   3471       O  
ATOM   4733  N   GLY B 305     -23.864 -25.533 -68.181  1.00 91.63           N  
ANISOU 4733  N   GLY B 305     9683  15749   9385  -1184   -682   3823       N  
ATOM   4734  CA  GLY B 305     -23.994 -24.320 -67.397  1.00 92.25           C  
ANISOU 4734  CA  GLY B 305     9645  15537   9869  -1126   -573   3973       C  
ATOM   4735  C   GLY B 305     -25.346 -24.140 -66.735  1.00 94.34           C  
ANISOU 4735  C   GLY B 305     9759  15923  10164  -1206   -663   3805       C  
ATOM   4736  O   GLY B 305     -25.583 -23.127 -66.082  1.00 94.14           O  
ANISOU 4736  O   GLY B 305     9622  15689  10458  -1130   -594   3893       O  
ATOM   4737  N   LYS B 306     -26.235 -25.115 -66.900  1.00 96.34           N  
ANISOU 4737  N   LYS B 306     9997  16514  10093  -1359   -821   3551       N  
ATOM   4738  CA  LYS B 306     -27.553 -25.050 -66.270  1.00 97.97           C  
ANISOU 4738  CA  LYS B 306    10037  16890  10298  -1464   -907   3374       C  
ATOM   4739  C   LYS B 306     -27.439 -25.180 -64.751  1.00 95.88           C  
ANISOU 4739  C   LYS B 306     9852  16284  10293  -1725   -878   3151       C  
ATOM   4740  O   LYS B 306     -26.521 -25.824 -64.249  1.00 93.50           O  
ANISOU 4740  O   LYS B 306     9768  15706  10050  -1908   -855   3029       O  
ATOM   4741  CB  LYS B 306     -28.487 -26.132 -66.822  1.00 99.32           C  
ANISOU 4741  CB  LYS B 306    10161  17502  10073  -1605  -1086   3143       C  
ATOM   4742  CG  LYS B 306     -28.732 -26.060 -68.322  1.00101.69           C  
ANISOU 4742  CG  LYS B 306    10354  18223  10059  -1330  -1142   3315       C  
ATOM   4743  CD  LYS B 306     -30.058 -26.716 -68.695  1.00103.73           C  
ANISOU 4743  CD  LYS B 306    10446  18963  10004  -1428  -1328   3084       C  
ATOM   4744  CE  LYS B 306     -30.128 -28.162 -68.237  1.00103.14           C  
ANISOU 4744  CE  LYS B 306    10530  18851   9808  -1834  -1456   2699       C  
ATOM   4745  NZ  LYS B 306     -29.111 -29.014 -68.911  1.00103.52           N  
ANISOU 4745  NZ  LYS B 306    10816  18833   9685  -1846  -1489   2644       N  
ATOM   4746  N   LEU B 307     -28.372 -24.566 -64.027  1.00 96.71           N  
ANISOU 4746  N   LEU B 307     9773  16437  10536  -1715   -882   3096       N  
ATOM   4747  CA  LEU B 307     -28.364 -24.602 -62.563  1.00 94.57           C  
ANISOU 4747  CA  LEU B 307     9541  15908  10485  -1923   -852   2888       C  
ATOM   4748  C   LEU B 307     -29.500 -25.457 -62.006  1.00 93.89           C  
ANISOU 4748  C   LEU B 307     9373  16106  10195  -2197   -963   2612       C  
ATOM   4749  O   LEU B 307     -30.670 -25.186 -62.260  1.00 95.67           O  
ANISOU 4749  O   LEU B 307     9363  16684  10303  -2124  -1024   2606       O  
ATOM   4750  CB  LEU B 307     -28.459 -23.185 -61.995  1.00 95.51           C  
ANISOU 4750  CB  LEU B 307     9508  15825  10958  -1695   -759   3013       C  
ATOM   4751  CG  LEU B 307     -28.624 -23.049 -60.481  1.00 74.05           C  
ANISOU 4751  CG  LEU B 307     6771  12918   8447  -1843   -738   2783       C  
ATOM   4752  CD1 LEU B 307     -27.429 -23.633 -59.754  1.00 71.47           C  
ANISOU 4752  CD1 LEU B 307     6693  12234   8229  -2042   -692   2662       C  
ATOM   4753  CD2 LEU B 307     -28.832 -21.596 -60.085  1.00 75.27           C  
ANISOU 4753  CD2 LEU B 307     6752  12909   8939  -1567   -674   2887       C  
ATOM   4754  N   ILE B 308     -29.153 -26.483 -61.237  1.00 91.78           N  
ANISOU 4754  N   ILE B 308     9292  15689   9890  -2512   -985   2398       N  
ATOM   4755  CA  ILE B 308     -30.156 -27.376 -60.669  1.00 92.73           C  
ANISOU 4755  CA  ILE B 308     9350  16046   9836  -2817  -1074   2163       C  
ATOM   4756  C   ILE B 308     -30.748 -26.789 -59.388  1.00 92.34           C  
ANISOU 4756  C   ILE B 308     9141  15981   9961  -2848  -1017   2077       C  
ATOM   4757  O   ILE B 308     -30.134 -26.855 -58.329  1.00 90.94           O  
ANISOU 4757  O   ILE B 308     9095  15514   9945  -2951   -951   1995       O  
ATOM   4758  CB  ILE B 308     -29.558 -28.761 -60.377  1.00 92.43           C  
ANISOU 4758  CB  ILE B 308     9592  15839   9687  -3140  -1121   1995       C  
ATOM   4759  CG1 ILE B 308     -28.838 -29.304 -61.614  1.00 93.27           C  
ANISOU 4759  CG1 ILE B 308     9868  15941   9628  -3067  -1177   2055       C  
ATOM   4760  CG2 ILE B 308     -30.636 -29.719 -59.903  1.00 93.84           C  
ANISOU 4760  CG2 ILE B 308     9699  16261   9696  -3481  -1212   1789       C  
ATOM   4761  CD1 ILE B 308     -29.733 -29.490 -62.823  1.00 96.12           C  
ANISOU 4761  CD1 ILE B 308    10062  16737   9722  -2997  -1296   2061       C  
ATOM   4762  N   THR B 309     -31.946 -26.221 -59.490  1.00 93.83           N  
ANISOU 4762  N   THR B 309     9039  16514  10100  -2738  -1049   2083       N  
ATOM   4763  CA  THR B 309     -32.556 -25.508 -58.370  1.00 93.91           C  
ANISOU 4763  CA  THR B 309     8859  16558  10266  -2691   -996   2005       C  
ATOM   4764  C   THR B 309     -33.291 -26.422 -57.394  1.00 94.57           C  
ANISOU 4764  C   THR B 309     8890  16832  10209  -3047  -1022   1787       C  
ATOM   4765  O   THR B 309     -33.562 -26.033 -56.258  1.00 94.53           O  
ANISOU 4765  O   THR B 309     8783  16816  10315  -3052   -962   1694       O  
ATOM   4766  CB  THR B 309     -33.535 -24.426 -58.859  1.00 95.69           C  
ANISOU 4766  CB  THR B 309     8775  17078  10504  -2376  -1014   2109       C  
ATOM   4767  OG1 THR B 309     -34.549 -25.028 -59.673  1.00 97.77           O  
ANISOU 4767  OG1 THR B 309     8880  17803  10464  -2467  -1128   2072       O  
ATOM   4768  CG2 THR B 309     -32.804 -23.378 -59.673  1.00 95.43           C  
ANISOU 4768  CG2 THR B 309     8786  16812  10661  -2009   -962   2369       C  
ATOM   4769  N   GLU B 310     -33.617 -27.633 -57.831  1.00 95.72           N  
ANISOU 4769  N   GLU B 310     9100  17156  10115  -3342  -1112   1705       N  
ATOM   4770  CA  GLU B 310     -34.394 -28.540 -56.992  1.00 96.96           C  
ANISOU 4770  CA  GLU B 310     9189  17506  10144  -3711  -1134   1536       C  
ATOM   4771  C   GLU B 310     -33.596 -29.761 -56.549  1.00 95.19           C  
ANISOU 4771  C   GLU B 310     9292  16986   9891  -4037  -1135   1461       C  
ATOM   4772  O   GLU B 310     -33.229 -30.607 -57.366  1.00 95.00           O  
ANISOU 4772  O   GLU B 310     9451  16893   9752  -4159  -1218   1449       O  
ATOM   4773  CB  GLU B 310     -35.680 -28.957 -57.706  1.00100.69           C  
ANISOU 4773  CB  GLU B 310     9408  18465  10385  -3833  -1248   1475       C  
ATOM   4774  CG  GLU B 310     -36.667 -27.811 -57.887  1.00103.75           C  
ANISOU 4774  CG  GLU B 310     9433  19208  10779  -3530  -1247   1523       C  
ATOM   4775  CD  GLU B 310     -37.577 -27.986 -59.093  1.00107.23           C  
ANISOU 4775  CD  GLU B 310     9662  20085  10996  -3494  -1379   1518       C  
ATOM   4776  OE1 GLU B 310     -37.343 -28.908 -59.901  1.00107.67           O  
ANISOU 4776  OE1 GLU B 310     9865  20142  10905  -3666  -1476   1477       O  
ATOM   4777  OE2 GLU B 310     -38.529 -27.191 -59.239  1.00109.53           O  
ANISOU 4777  OE2 GLU B 310     9632  20732  11252  -3272  -1396   1538       O  
ATOM   4778  N   TRP B 311     -33.342 -29.839 -55.244  1.00 93.90           N  
ANISOU 4778  N   TRP B 311     9195  16661   9822  -4151  -1046   1405       N  
ATOM   4779  CA  TRP B 311     -32.565 -30.928 -54.655  1.00 92.14           C  
ANISOU 4779  CA  TRP B 311     9284  16142   9583  -4427  -1035   1353       C  
ATOM   4780  C   TRP B 311     -33.302 -31.574 -53.491  1.00 92.44           C  
ANISOU 4780  C   TRP B 311     9241  16343   9538  -4746   -998   1271       C  
ATOM   4781  O   TRP B 311     -34.283 -31.032 -52.990  1.00 93.84           O  
ANISOU 4781  O   TRP B 311     9113  16847   9695  -4714   -959   1244       O  
ATOM   4782  CB  TRP B 311     -31.221 -30.406 -54.160  1.00 90.04           C  
ANISOU 4782  CB  TRP B 311     9232  15464   9516  -4221   -951   1393       C  
ATOM   4783  CG  TRP B 311     -30.370 -29.853 -55.238  1.00 89.40           C  
ANISOU 4783  CG  TRP B 311     9247  15194   9526  -3944   -965   1504       C  
ATOM   4784  CD1 TRP B 311     -30.489 -28.635 -55.832  1.00 89.91           C  
ANISOU 4784  CD1 TRP B 311     9127  15326   9707  -3613   -943   1614       C  
ATOM   4785  CD2 TRP B 311     -29.252 -30.495 -55.855  1.00 88.22           C  
ANISOU 4785  CD2 TRP B 311     9397  14766   9355  -3964   -996   1534       C  
ATOM   4786  NE1 TRP B 311     -29.516 -28.480 -56.786  1.00 89.18           N  
ANISOU 4786  NE1 TRP B 311     9194  15025   9665  -3441   -946   1736       N  
ATOM   4787  CE2 TRP B 311     -28.742 -29.610 -56.820  1.00 88.05           C  
ANISOU 4787  CE2 TRP B 311     9340  14685   9429  -3647   -979   1677       C  
ATOM   4788  CE3 TRP B 311     -28.634 -31.736 -55.686  1.00 87.55           C  
ANISOU 4788  CE3 TRP B 311     9607  14478   9180  -4207  -1036   1461       C  
ATOM   4789  CZ2 TRP B 311     -27.641 -29.925 -57.614  1.00 87.08           C  
ANISOU 4789  CZ2 TRP B 311     9445  14350   9293  -3568   -992   1743       C  
ATOM   4790  CZ3 TRP B 311     -27.543 -32.047 -56.474  1.00 86.53           C  
ANISOU 4790  CZ3 TRP B 311     9713  14121   9044  -4110  -1064   1501       C  
ATOM   4791  CH2 TRP B 311     -27.058 -31.147 -57.425  1.00 86.20           C  
ANISOU 4791  CH2 TRP B 311     9608  14067   9078  -3796  -1038   1638       C  
ATOM   4792  N   CYS B 312     -32.808 -32.727 -53.052  1.00 91.33           N  
ANISOU 4792  N   CYS B 312     9395  15957   9349  -5005   -996   1241       N  
ATOM   4793  CA  CYS B 312     -33.447 -33.473 -51.978  1.00 92.05           C  
ANISOU 4793  CA  CYS B 312     9539  16086   9351  -5187   -924   1193       C  
ATOM   4794  C   CYS B 312     -32.488 -34.430 -51.285  1.00 89.84           C  
ANISOU 4794  C   CYS B 312     9640  15418   9078  -5313   -893   1198       C  
ATOM   4795  O   CYS B 312     -31.345 -34.610 -51.710  1.00 87.93           O  
ANISOU 4795  O   CYS B 312     9640  14869   8899  -5268   -935   1214       O  
ATOM   4796  CB  CYS B 312     -34.640 -34.265 -52.520  1.00 95.18           C  
ANISOU 4796  CB  CYS B 312     9850  16716   9599  -5385   -982   1148       C  
ATOM   4797  SG  CYS B 312     -34.263 -35.304 -53.956  1.00 85.21           S  
ANISOU 4797  SG  CYS B 312     8825  15275   8277  -5525  -1135   1108       S  
ATOM   4798  N   CYS B 313     -32.982 -35.050 -50.218  1.00 90.09           N  
ANISOU 4798  N   CYS B 313     9706  15493   9032  -5466   -822   1195       N  
ATOM   4799  CA  CYS B 313     -32.270 -36.115 -49.529  1.00 88.55           C  
ANISOU 4799  CA  CYS B 313     9854  14978   8812  -5607   -804   1220       C  
ATOM   4800  C   CYS B 313     -33.267 -37.008 -48.799  1.00 90.39           C  
ANISOU 4800  C   CYS B 313    10061  15356   8928  -5850   -762   1245       C  
ATOM   4801  O   CYS B 313     -34.346 -36.561 -48.413  1.00 80.05           O  
ANISOU 4801  O   CYS B 313     8448  14409   7558  -5863   -708   1242       O  
ATOM   4802  CB  CYS B 313     -31.279 -35.533 -48.529  1.00 73.24           C  
ANISOU 4802  CB  CYS B 313     7983  12892   6952  -5451   -724   1232       C  
ATOM   4803  SG  CYS B 313     -32.045 -34.545 -47.236  1.00112.14           S  
ANISOU 4803  SG  CYS B 313    12549  18205  11854  -5361   -600   1216       S  
ATOM   4804  N   ARG B 314     -32.900 -38.270 -48.613  1.00 89.91           N  
ANISOU 4804  N   ARG B 314    10309  15013   8840  -6038   -790   1278       N  
ATOM   4805  CA  ARG B 314     -33.749 -39.209 -47.897  1.00 91.53           C  
ANISOU 4805  CA  ARG B 314    10511  15306   8961  -6293   -752   1334       C  
ATOM   4806  C   ARG B 314     -33.796 -38.898 -46.412  1.00 90.76           C  
ANISOU 4806  C   ARG B 314    10323  15358   8804  -6268   -627   1406       C  
ATOM   4807  O   ARG B 314     -34.865 -38.685 -45.849  1.00 92.25           O  
ANISOU 4807  O   ARG B 314    10238  15902   8910  -6340   -558   1430       O  
ATOM   4808  CB  ARG B 314     -33.241 -40.633 -48.077  1.00 92.24           C  
ANISOU 4808  CB  ARG B 314    10966  15010   9069  -6485   -822   1359       C  
ATOM   4809  CG  ARG B 314     -33.213 -41.120 -49.501  1.00 92.56           C  
ANISOU 4809  CG  ARG B 314    11105  14911   9151  -6541   -954   1269       C  
ATOM   4810  CD  ARG B 314     -33.098 -42.626 -49.522  1.00 94.97           C  
ANISOU 4810  CD  ARG B 314    11704  14898   9481  -6784  -1017   1284       C  
ATOM   4811  NE  ARG B 314     -32.977 -43.150 -50.877  1.00 95.91           N  
ANISOU 4811  NE  ARG B 314    11932  14867   9640  -6832  -1156   1167       N  
ATOM   4812  CZ  ARG B 314     -33.125 -44.431 -51.194  1.00 99.07           C  
ANISOU 4812  CZ  ARG B 314    12523  15030  10088  -7058  -1240   1131       C  
ATOM   4813  NH1 ARG B 314     -33.410 -45.320 -50.254  1.00101.68           N  
ANISOU 4813  NH1 ARG B 314    12957  15234  10443  -7266  -1192   1232       N  
ATOM   4814  NH2 ARG B 314     -32.996 -44.823 -52.454  1.00 99.75           N  
ANISOU 4814  NH2 ARG B 314    12685  15012  10206  -7076  -1378    991       N  
ATOM   4815  N   SER B 315     -32.626 -38.879 -45.781  1.00 88.61           N  
ANISOU 4815  N   SER B 315    10269  14840   8561  -6163   -599   1433       N  
ATOM   4816  CA  SER B 315     -32.544 -38.730 -44.333  1.00 88.66           C  
ANISOU 4816  CA  SER B 315    10220  14980   8488  -6155   -486   1502       C  
ATOM   4817  C   SER B 315     -31.600 -37.621 -43.887  1.00 85.51           C  
ANISOU 4817  C   SER B 315     9772  14575   8143  -5896   -438   1446       C  
ATOM   4818  O   SER B 315     -31.387 -37.440 -42.690  1.00 85.14           O  
ANISOU 4818  O   SER B 315     9677  14651   8020  -5870   -345   1483       O  
ATOM   4819  CB  SER B 315     -32.095 -40.044 -43.693  1.00 89.82           C  
ANISOU 4819  CB  SER B 315    10686  14849   8590  -6337   -485   1614       C  
ATOM   4820  OG  SER B 315     -30.705 -40.246 -43.876  1.00 87.12           O  
ANISOU 4820  OG  SER B 315    10665  14119   8317  -6222   -536   1594       O  
ATOM   4821  N   CYS B 316     -31.033 -36.883 -44.838  1.00 83.68           N  
ANISOU 4821  N   CYS B 316     9535  14215   8043  -5712   -499   1361       N  
ATOM   4822  CA  CYS B 316     -30.107 -35.809 -44.492  1.00 82.10           C  
ANISOU 4822  CA  CYS B 316     9276  13974   7945  -5480   -463   1299       C  
ATOM   4823  C   CYS B 316     -30.821 -34.749 -43.659  1.00 83.95           C  
ANISOU 4823  C   CYS B 316     9118  14630   8148  -5380   -369   1249       C  
ATOM   4824  O   CYS B 316     -32.048 -34.753 -43.557  1.00 86.69           O  
ANISOU 4824  O   CYS B 316     9233  15310   8397  -5460   -339   1264       O  
ATOM   4825  CB  CYS B 316     -29.519 -35.169 -45.748  1.00 79.88           C  
ANISOU 4825  CB  CYS B 316     9014  13508   7829  -5313   -545   1241       C  
ATOM   4826  SG  CYS B 316     -30.434 -33.725 -46.325  1.00110.24           S  
ANISOU 4826  SG  CYS B 316    12413  17709  11765  -5140   -542   1181       S  
ATOM   4827  N   THR B 317     -30.053 -33.846 -43.060  1.00 82.34           N  
ANISOU 4827  N   THR B 317     8824  14430   8031  -5201   -327   1172       N  
ATOM   4828  CA  THR B 317     -30.630 -32.785 -42.245  1.00 83.54           C  
ANISOU 4828  CA  THR B 317     8636  14938   8168  -4980   -257   1062       C  
ATOM   4829  C   THR B 317     -30.250 -31.407 -42.778  1.00 81.66           C  
ANISOU 4829  C   THR B 317     8273  14586   8169  -4599   -305    914       C  
ATOM   4830  O   THR B 317     -29.139 -31.208 -43.256  1.00 69.53           O  
ANISOU 4830  O   THR B 317     6951  12668   6801  -4452   -357    884       O  
ATOM   4831  CB  THR B 317     -30.204 -32.916 -40.778  1.00 84.98           C  
ANISOU 4831  CB  THR B 317     8868  15197   8222  -4906   -172   1033       C  
ATOM   4832  OG1 THR B 317     -28.788 -33.120 -40.710  1.00 83.73           O  
ANISOU 4832  OG1 THR B 317     9040  14620   8153  -4784   -213   1003       O  
ATOM   4833  CG2 THR B 317     -30.901 -34.099 -40.132  1.00 87.27           C  
ANISOU 4833  CG2 THR B 317     9182  15715   8263  -5273    -93   1217       C  
ATOM   4834  N   LEU B 318     -31.184 -30.465 -42.699  1.00 82.72           N  
ANISOU 4834  N   LEU B 318     8054  15051   8323  -4441   -285    831       N  
ATOM   4835  CA  LEU B 318     -30.962 -29.117 -43.216  1.00 81.71           C  
ANISOU 4835  CA  LEU B 318     7791  14812   8444  -4082   -330    713       C  
ATOM   4836  C   LEU B 318     -30.431 -28.201 -42.111  1.00 81.52           C  
ANISOU 4836  C   LEU B 318     7689  14767   8520  -3764   -299    517       C  
ATOM   4837  O   LEU B 318     -30.790 -28.374 -40.946  1.00 82.79           O  
ANISOU 4837  O   LEU B 318     7741  15218   8497  -3781   -233    455       O  
ATOM   4838  CB  LEU B 318     -32.256 -28.553 -43.817  1.00 83.19           C  
ANISOU 4838  CB  LEU B 318     7644  15347   8617  -4043   -345    719       C  
ATOM   4839  CG  LEU B 318     -32.958 -29.416 -44.875  1.00 83.61           C  
ANISOU 4839  CG  LEU B 318     7708  15509   8553  -4355   -390    871       C  
ATOM   4840  CD1 LEU B 318     -34.303 -28.831 -45.296  1.00 85.52           C  
ANISOU 4840  CD1 LEU B 318     7572  16173   8747  -4294   -404    853       C  
ATOM   4841  CD2 LEU B 318     -32.072 -29.619 -46.091  1.00 81.32           C  
ANISOU 4841  CD2 LEU B 318     7688  14811   8398  -4349   -471    947       C  
ATOM   4842  N   PRO B 319     -29.567 -27.225 -42.460  1.00 80.28           N  
ANISOU 4842  N   PRO B 319     7575  14276   8654  -3472   -348    417       N  
ATOM   4843  CA  PRO B 319     -29.013 -26.862 -43.774  1.00 78.18           C  
ANISOU 4843  CA  PRO B 319     7420  13666   8619  -3397   -409    502       C  
ATOM   4844  C   PRO B 319     -28.125 -27.939 -44.375  1.00 76.37           C  
ANISOU 4844  C   PRO B 319     7536  13137   8342  -3616   -433    641       C  
ATOM   4845  O   PRO B 319     -27.407 -28.624 -43.654  1.00 75.59           O  
ANISOU 4845  O   PRO B 319     7642  12924   8154  -3704   -415    618       O  
ATOM   4846  CB  PRO B 319     -28.170 -25.622 -43.467  1.00 77.60           C  
ANISOU 4846  CB  PRO B 319     7305  13321   8858  -3048   -427    333       C  
ATOM   4847  CG  PRO B 319     -28.737 -25.073 -42.229  1.00 79.58           C  
ANISOU 4847  CG  PRO B 319     7318  13871   9048  -2890   -398    129       C  
ATOM   4848  CD  PRO B 319     -29.152 -26.263 -41.426  1.00 80.52           C  
ANISOU 4848  CD  PRO B 319     7489  14293   8810  -3162   -339    183       C  
ATOM   4849  N   PRO B 320     -28.170 -28.078 -45.702  1.00 75.44           N  
ANISOU 4849  N   PRO B 320     7480  12912   8271  -3676   -480    778       N  
ATOM   4850  CA  PRO B 320     -27.503 -29.175 -46.404  1.00 73.85           C  
ANISOU 4850  CA  PRO B 320     7586  12483   7991  -3886   -516    897       C  
ATOM   4851  C   PRO B 320     -25.989 -29.056 -46.412  1.00 70.85           C  
ANISOU 4851  C   PRO B 320     7442  11699   7780  -3747   -524    866       C  
ATOM   4852  O   PRO B 320     -25.448 -27.954 -46.353  1.00 70.13           O  
ANISOU 4852  O   PRO B 320     7260  11449   7935  -3482   -516    791       O  
ATOM   4853  CB  PRO B 320     -28.041 -29.042 -47.828  1.00 74.92           C  
ANISOU 4853  CB  PRO B 320     7645  12680   8142  -3895   -568   1013       C  
ATOM   4854  CG  PRO B 320     -28.372 -27.605 -47.968  1.00 75.85           C  
ANISOU 4854  CG  PRO B 320     7496  12860   8464  -3586   -556    973       C  
ATOM   4855  CD  PRO B 320     -28.888 -27.186 -46.628  1.00 76.76           C  
ANISOU 4855  CD  PRO B 320     7419  13193   8553  -3518   -507    822       C  
ATOM   4856  N   LEU B 321     -25.322 -30.202 -46.486  1.00 69.62           N  
ANISOU 4856  N   LEU B 321     7581  11373   7500  -3931   -545    920       N  
ATOM   4857  CA  LEU B 321     -23.872 -30.257 -46.595  1.00 67.81           C  
ANISOU 4857  CA  LEU B 321     7582  10787   7394  -3819   -560    899       C  
ATOM   4858  C   LEU B 321     -23.463 -29.721 -47.963  1.00 67.16           C  
ANISOU 4858  C   LEU B 321     7497  10541   7480  -3688   -587    990       C  
ATOM   4859  O   LEU B 321     -23.688 -30.376 -48.979  1.00 66.74           O  
ANISOU 4859  O   LEU B 321     7538  10509   7310  -3818   -631   1098       O  
ATOM   4860  CB  LEU B 321     -23.394 -31.706 -46.421  1.00 67.63           C  
ANISOU 4860  CB  LEU B 321     7877  10649   7169  -4044   -585    945       C  
ATOM   4861  CG  LEU B 321     -21.959 -32.044 -45.998  1.00 66.34           C  
ANISOU 4861  CG  LEU B 321     7966  10195   7046  -3953   -594    890       C  
ATOM   4862  CD1 LEU B 321     -21.840 -33.517 -45.641  1.00 66.62           C  
ANISOU 4862  CD1 LEU B 321     8286  10178   6848  -4186   -618    948       C  
ATOM   4863  CD2 LEU B 321     -20.956 -31.698 -47.079  1.00 65.18           C  
ANISOU 4863  CD2 LEU B 321     7903   9792   7071  -3803   -623    921       C  
ATOM   4864  N   ARG B 322     -22.865 -28.532 -47.985  1.00 67.41           N  
ANISOU 4864  N   ARG B 322     7413  10414   7786  -3431   -563    947       N  
ATOM   4865  CA  ARG B 322     -22.411 -27.941 -49.244  1.00 67.56           C  
ANISOU 4865  CA  ARG B 322     7417  10275   7978  -3292   -567   1074       C  
ATOM   4866  C   ARG B 322     -20.903 -27.738 -49.303  1.00 66.38           C  
ANISOU 4866  C   ARG B 322     7409   9797   8016  -3169   -553   1057       C  
ATOM   4867  O   ARG B 322     -20.241 -27.553 -48.275  1.00 65.79           O  
ANISOU 4867  O   ARG B 322     7357   9604   8038  -3108   -541    906       O  
ATOM   4868  CB  ARG B 322     -23.126 -26.616 -49.537  1.00 68.96           C  
ANISOU 4868  CB  ARG B 322     7304  10541   8357  -3095   -547   1105       C  
ATOM   4869  CG  ARG B 322     -22.506 -25.397 -48.870  1.00 68.99           C  
ANISOU 4869  CG  ARG B 322     7186  10334   8693  -2863   -516    988       C  
ATOM   4870  CD  ARG B 322     -23.168 -24.106 -49.330  1.00 70.44           C  
ANISOU 4870  CD  ARG B 322     7115  10546   9103  -2653   -505   1049       C  
ATOM   4871  NE  ARG B 322     -22.652 -22.938 -48.622  1.00 71.26           N  
ANISOU 4871  NE  ARG B 322     7097  10422   9556  -2441   -491    902       N  
ATOM   4872  CZ  ARG B 322     -22.990 -21.683 -48.897  1.00 73.34           C  
ANISOU 4872  CZ  ARG B 322     7161  10600  10104  -2223   -485    934       C  
ATOM   4873  NH1 ARG B 322     -23.845 -21.417 -49.873  1.00 74.85           N  
ANISOU 4873  NH1 ARG B 322     7248  10943  10248  -2168   -485   1127       N  
ATOM   4874  NH2 ARG B 322     -22.467 -20.689 -48.196  1.00 74.11           N  
ANISOU 4874  NH2 ARG B 322     7163  10454  10541  -2050   -488    764       N  
ATOM   4875  N   TYR B 323     -20.376 -27.770 -50.522  1.00 66.69           N  
ANISOU 4875  N   TYR B 323     7524   9724   8091  -3127   -555   1210       N  
ATOM   4876  CA  TYR B 323     -18.959 -27.535 -50.757  1.00 67.01           C  
ANISOU 4876  CA  TYR B 323     7663   9487   8312  -3011   -530   1226       C  
ATOM   4877  C   TYR B 323     -18.760 -26.280 -51.599  1.00 70.17           C  
ANISOU 4877  C   TYR B 323     7883   9778   9003  -2815   -480   1373       C  
ATOM   4878  O   TYR B 323     -19.148 -26.250 -52.760  1.00 70.80           O  
ANISOU 4878  O   TYR B 323     7931   9960   9011  -2792   -477   1560       O  
ATOM   4879  CB  TYR B 323     -18.339 -28.718 -51.500  1.00 65.16           C  
ANISOU 4879  CB  TYR B 323     7685   9214   7857  -3112   -565   1295       C  
ATOM   4880  CG  TYR B 323     -18.462 -30.053 -50.804  1.00 63.80           C  
ANISOU 4880  CG  TYR B 323     7733   9092   7414  -3309   -619   1189       C  
ATOM   4881  CD1 TYR B 323     -17.431 -30.546 -50.023  1.00 62.46           C  
ANISOU 4881  CD1 TYR B 323     7739   8758   7234  -3302   -626   1076       C  
ATOM   4882  CD2 TYR B 323     -19.597 -30.833 -50.953  1.00 64.26           C  
ANISOU 4882  CD2 TYR B 323     7821   9361   7235  -3504   -664   1212       C  
ATOM   4883  CE1 TYR B 323     -17.533 -31.769 -49.396  1.00 62.20           C  
ANISOU 4883  CE1 TYR B 323     7924   8749   6960  -3469   -672   1015       C  
ATOM   4884  CE2 TYR B 323     -19.707 -32.058 -50.330  1.00 63.97           C  
ANISOU 4884  CE2 TYR B 323     7992   9333   6982  -3704   -707   1147       C  
ATOM   4885  CZ  TYR B 323     -18.672 -32.520 -49.551  1.00 62.85           C  
ANISOU 4885  CZ  TYR B 323     8042   9006   6832  -3677   -708   1062       C  
ATOM   4886  OH  TYR B 323     -18.774 -33.739 -48.924  1.00 62.84           O  
ANISOU 4886  OH  TYR B 323     8263   8992   6621  -3861   -747   1030       O  
ATOM   4887  N   ARG B 324     -18.155 -25.245 -51.026  1.00 72.89           N  
ANISOU 4887  N   ARG B 324     8104   9913   9678  -2673   -444   1294       N  
ATOM   4888  CA  ARG B 324     -17.800 -24.073 -51.822  1.00 76.38           C  
ANISOU 4888  CA  ARG B 324     8397  10183  10442  -2502   -387   1464       C  
ATOM   4889  C   ARG B 324     -16.381 -24.215 -52.359  1.00 78.80           C  
ANISOU 4889  C   ARG B 324     8814  10282  10845  -2479   -347   1552       C  
ATOM   4890  O   ARG B 324     -15.411 -24.179 -51.600  1.00 78.36           O  
ANISOU 4890  O   ARG B 324     8795  10046  10931  -2473   -347   1392       O  
ATOM   4891  CB  ARG B 324     -17.948 -22.779 -51.016  1.00 77.01           C  
ANISOU 4891  CB  ARG B 324     8263  10113  10884  -2360   -376   1334       C  
ATOM   4892  CG  ARG B 324     -19.386 -22.442 -50.650  1.00 77.65           C  
ANISOU 4892  CG  ARG B 324     8188  10423  10893  -2328   -406   1274       C  
ATOM   4893  CD  ARG B 324     -19.531 -21.009 -50.159  1.00 78.95           C  
ANISOU 4893  CD  ARG B 324     8131  10409  11457  -2131   -399   1180       C  
ATOM   4894  NE  ARG B 324     -18.658 -20.719 -49.025  1.00 78.70           N  
ANISOU 4894  NE  ARG B 324     8094  10168  11638  -2101   -418    912       N  
ATOM   4895  CZ  ARG B 324     -18.682 -19.585 -48.332  1.00 80.28           C  
ANISOU 4895  CZ  ARG B 324     8118  10199  12186  -1941   -438    731       C  
ATOM   4896  NH1 ARG B 324     -17.848 -19.411 -47.316  1.00 80.26           N  
ANISOU 4896  NH1 ARG B 324     8110  10037  12347  -1918   -470    458       N  
ATOM   4897  NH2 ARG B 324     -19.538 -18.624 -48.649  1.00 81.95           N  
ANISOU 4897  NH2 ARG B 324     8153  10403  12579  -1789   -438    804       N  
ATOM   4898  N   GLY B 325     -16.265 -24.388 -53.672  1.00 82.12           N  
ANISOU 4898  N   GLY B 325     9272  10764  11167  -2453   -315   1800       N  
ATOM   4899  CA  GLY B 325     -14.970 -24.577 -54.300  1.00 84.83           C  
ANISOU 4899  CA  GLY B 325     9704  10975  11555  -2421   -267   1906       C  
ATOM   4900  C   GLY B 325     -14.630 -23.540 -55.355  1.00 88.88           C  
ANISOU 4900  C   GLY B 325    10061  11387  12323  -2277   -171   2198       C  
ATOM   4901  O   GLY B 325     -14.943 -22.358 -55.209  1.00 90.42           O  
ANISOU 4901  O   GLY B 325    10068  11444  12843  -2182   -134   2258       O  
ATOM   4902  N   GLU B 326     -13.977 -23.993 -56.420  1.00 90.95           N  
ANISOU 4902  N   GLU B 326    10405  11720  12433  -2250   -130   2385       N  
ATOM   4903  CA  GLU B 326     -13.550 -23.122 -57.508  1.00 94.24           C  
ANISOU 4903  CA  GLU B 326    10684  12079  13045  -2114    -20   2712       C  
ATOM   4904  C   GLU B 326     -14.641 -23.026 -58.568  1.00 95.46           C  
ANISOU 4904  C   GLU B 326    10783  12492  12997  -2033    -22   2944       C  
ATOM   4905  O   GLU B 326     -15.038 -21.932 -58.973  1.00 96.93           O  
ANISOU 4905  O   GLU B 326    10794  12617  13417  -1908     40   3165       O  
ATOM   4906  CB  GLU B 326     -12.265 -23.668 -58.133  1.00 95.64           C  
ANISOU 4906  CB  GLU B 326    10954  12262  13124  -2102     34   2798       C  
ATOM   4907  CG  GLU B 326     -11.659 -22.792 -59.219  1.00 99.08           C  
ANISOU 4907  CG  GLU B 326    11235  12650  13762  -1972    173   3164       C  
ATOM   4908  CD  GLU B 326     -10.946 -21.576 -58.660  1.00101.40           C  
ANISOU 4908  CD  GLU B 326    11351  12587  14590  -1961    256   3195       C  
ATOM   4909  OE1 GLU B 326     -10.703 -21.539 -57.436  1.00100.80           O  
ANISOU 4909  OE1 GLU B 326    11286  12323  14691  -2043    196   2888       O  
ATOM   4910  OE2 GLU B 326     -10.628 -20.658 -59.446  1.00103.89           O  
ANISOU 4910  OE2 GLU B 326    11512  12812  15151  -1870    379   3527       O  
ATOM   4911  N   ASP B 327     -15.126 -24.183 -59.007  1.00 94.90           N  
ANISOU 4911  N   ASP B 327    10858  12703  12495  -2097   -102   2884       N  
ATOM   4912  CA  ASP B 327     -16.158 -24.239 -60.034  1.00 96.08           C  
ANISOU 4912  CA  ASP B 327    10954  13152  12400  -2023   -128   3060       C  
ATOM   4913  C   ASP B 327     -17.565 -23.974 -59.495  1.00 95.55           C  
ANISOU 4913  C   ASP B 327    10789  13188  12327  -2058   -198   2955       C  
ATOM   4914  O   ASP B 327     -18.541 -24.045 -60.242  1.00 97.18           O  
ANISOU 4914  O   ASP B 327    10932  13673  12320  -2004   -238   3061       O  
ATOM   4915  CB  ASP B 327     -16.117 -25.579 -60.775  1.00 95.92           C  
ANISOU 4915  CB  ASP B 327    11115  13396  11935  -2076   -204   3007       C  
ATOM   4916  CG  ASP B 327     -15.892 -26.752 -59.849  1.00 93.92           C  
ANISOU 4916  CG  ASP B 327    11076  13078  11530  -2268   -299   2684       C  
ATOM   4917  OD1 ASP B 327     -16.043 -26.579 -58.623  1.00 93.06           O  
ANISOU 4917  OD1 ASP B 327    10962  12803  11596  -2366   -316   2501       O  
ATOM   4918  OD2 ASP B 327     -15.569 -27.851 -60.348  1.00 93.28           O  
ANISOU 4918  OD2 ASP B 327    11172  13119  11151  -2306   -360   2614       O  
ATOM   4919  N   GLY B 328     -17.669 -23.671 -58.204  1.00 93.08           N  
ANISOU 4919  N   GLY B 328    10448  12687  12231  -2133   -216   2737       N  
ATOM   4920  CA  GLY B 328     -18.949 -23.312 -57.623  1.00 91.98           C  
ANISOU 4920  CA  GLY B 328    10185  12657  12108  -2142   -269   2633       C  
ATOM   4921  C   GLY B 328     -19.369 -24.187 -56.460  1.00 89.28           C  
ANISOU 4921  C   GLY B 328     9942  12380  11599  -2338   -352   2320       C  
ATOM   4922  O   GLY B 328     -18.542 -24.850 -55.840  1.00 88.30           O  
ANISOU 4922  O   GLY B 328     9978  12125  11445  -2447   -362   2164       O  
ATOM   4923  N   CYS B 329     -20.667 -24.193 -56.175  1.00 87.79           N  
ANISOU 4923  N   CYS B 329     9648  12417  11292  -2376   -406   2246       N  
ATOM   4924  CA  CYS B 329     -21.197 -24.901 -55.018  1.00 84.50           C  
ANISOU 4924  CA  CYS B 329     9284  12092  10731  -2560   -465   1985       C  
ATOM   4925  C   CYS B 329     -21.558 -26.354 -55.327  1.00 81.37           C  
ANISOU 4925  C   CYS B 329     9058  11912   9946  -2773   -541   1929       C  
ATOM   4926  O   CYS B 329     -22.050 -26.669 -56.408  1.00 81.98           O  
ANISOU 4926  O   CYS B 329     9122  12198   9827  -2769   -578   2051       O  
ATOM   4927  CB  CYS B 329     -22.414 -24.163 -54.461  1.00 85.87           C  
ANISOU 4927  CB  CYS B 329     9230  12417  10980  -2497   -478   1920       C  
ATOM   4928  SG  CYS B 329     -22.952 -24.732 -52.836  1.00146.18           S  
ANISOU 4928  SG  CYS B 329    16876  20160  18504  -2676   -514   1618       S  
ATOM   4929  N   TRP B 330     -21.304 -27.228 -54.360  1.00 77.79           N  
ANISOU 4929  N   TRP B 330     8764  11402   9390  -2952   -570   1741       N  
ATOM   4930  CA  TRP B 330     -21.588 -28.652 -54.475  1.00 75.04           C  
ANISOU 4930  CA  TRP B 330     8604  11185   8722  -3180   -647   1670       C  
ATOM   4931  C   TRP B 330     -22.456 -29.077 -53.303  1.00 74.33           C  
ANISOU 4931  C   TRP B 330     8482  11225   8534  -3365   -669   1515       C  
ATOM   4932  O   TRP B 330     -22.599 -28.337 -52.335  1.00 74.64           O  
ANISOU 4932  O   TRP B 330     8385  11238   8736  -3292   -625   1435       O  
ATOM   4933  CB  TRP B 330     -20.288 -29.449 -54.445  1.00 71.61           C  
ANISOU 4933  CB  TRP B 330     8437  10526   8244  -3217   -654   1626       C  
ATOM   4934  CG  TRP B 330     -19.411 -29.203 -55.617  1.00 69.40           C  
ANISOU 4934  CG  TRP B 330     8192  10169   8007  -3055   -626   1780       C  
ATOM   4935  CD1 TRP B 330     -18.819 -28.028 -55.964  1.00 68.75           C  
ANISOU 4935  CD1 TRP B 330     7968   9962   8192  -2845   -540   1921       C  
ATOM   4936  CD2 TRP B 330     -19.013 -30.162 -56.601  1.00 68.23           C  
ANISOU 4936  CD2 TRP B 330     8225  10071   7628  -3083   -682   1812       C  
ATOM   4937  NE1 TRP B 330     -18.082 -28.193 -57.111  1.00 68.45           N  
ANISOU 4937  NE1 TRP B 330     7999   9924   8084  -2746   -522   2069       N  
ATOM   4938  CE2 TRP B 330     -18.183 -29.497 -57.520  1.00 68.09           C  
ANISOU 4938  CE2 TRP B 330     8152  10000   7721  -2874   -613   1988       C  
ATOM   4939  CE3 TRP B 330     -19.280 -31.519 -56.794  1.00 67.66           C  
ANISOU 4939  CE3 TRP B 330     8355  10078   7276  -3263   -786   1705       C  
ATOM   4940  CZ2 TRP B 330     -17.619 -30.144 -58.618  1.00 68.04           C  
ANISOU 4940  CZ2 TRP B 330     8272  10063   7516  -2816   -642   2050       C  
ATOM   4941  CZ3 TRP B 330     -18.720 -32.157 -57.881  1.00 67.75           C  
ANISOU 4941  CZ3 TRP B 330     8506  10120   7116  -3204   -832   1737       C  
ATOM   4942  CH2 TRP B 330     -17.899 -31.472 -58.779  1.00 67.92           C  
ANISOU 4942  CH2 TRP B 330     8457  10135   7216  -2971   -759   1904       C  
ATOM   4943  N   TYR B 331     -23.027 -30.271 -53.385  1.00 73.79           N  
ANISOU 4943  N   TYR B 331     8532  11300   8205  -3602   -738   1471       N  
ATOM   4944  CA  TYR B 331     -23.837 -30.790 -52.292  1.00 73.90           C  
ANISOU 4944  CA  TYR B 331     8521  11452   8108  -3811   -745   1362       C  
ATOM   4945  C   TYR B 331     -23.306 -32.129 -51.802  1.00 72.86           C  
ANISOU 4945  C   TYR B 331     8686  11175   7824  -4022   -781   1295       C  
ATOM   4946  O   TYR B 331     -22.477 -32.752 -52.459  1.00 71.97           O  
ANISOU 4946  O   TYR B 331     8794  10891   7659  -4017   -824   1313       O  
ATOM   4947  CB  TYR B 331     -25.305 -30.900 -52.711  1.00 76.14           C  
ANISOU 4947  CB  TYR B 331     8606  12079   8245  -3936   -787   1385       C  
ATOM   4948  CG  TYR B 331     -26.079 -29.617 -52.506  1.00 77.56           C  
ANISOU 4948  CG  TYR B 331     8465  12442   8562  -3752   -740   1401       C  
ATOM   4949  CD1 TYR B 331     -25.935 -28.882 -51.339  1.00 77.72           C  
ANISOU 4949  CD1 TYR B 331     8388  12400   8742  -3640   -674   1313       C  
ATOM   4950  CD2 TYR B 331     -26.940 -29.135 -53.481  1.00 79.06           C  
ANISOU 4950  CD2 TYR B 331     8450  12873   8717  -3662   -772   1488       C  
ATOM   4951  CE1 TYR B 331     -26.633 -27.709 -51.143  1.00 78.94           C  
ANISOU 4951  CE1 TYR B 331     8258  12701   9033  -3448   -644   1301       C  
ATOM   4952  CE2 TYR B 331     -27.642 -27.959 -53.294  1.00 80.29           C  
ANISOU 4952  CE2 TYR B 331     8323  13181   9003  -3465   -737   1502       C  
ATOM   4953  CZ  TYR B 331     -27.484 -27.251 -52.122  1.00 80.29           C  
ANISOU 4953  CZ  TYR B 331     8241  13089   9178  -3359   -674   1404       C  
ATOM   4954  OH  TYR B 331     -28.177 -26.080 -51.921  1.00 81.76           O  
ANISOU 4954  OH  TYR B 331     8152  13408   9505  -3139   -651   1391       O  
ATOM   4955  N   GLY B 332     -23.780 -32.562 -50.640  1.00 73.42           N  
ANISOU 4955  N   GLY B 332     8759  11321   7815  -4189   -762   1226       N  
ATOM   4956  CA  GLY B 332     -23.338 -33.817 -50.058  1.00 73.47           C  
ANISOU 4956  CA  GLY B 332     9050  11180   7684  -4383   -789   1191       C  
ATOM   4957  C   GLY B 332     -23.694 -35.030 -50.895  1.00 74.57           C  
ANISOU 4957  C   GLY B 332     9360  11321   7650  -4618   -884   1218       C  
ATOM   4958  O   GLY B 332     -24.450 -34.927 -51.862  1.00 75.53           O  
ANISOU 4958  O   GLY B 332     9344  11625   7728  -4654   -932   1246       O  
ATOM   4959  N   MET B 333     -23.142 -36.181 -50.520  1.00 74.55           N  
ANISOU 4959  N   MET B 333     9658  11113   7554  -4763   -921   1197       N  
ATOM   4960  CA  MET B 333     -23.393 -37.428 -51.230  1.00 76.25           C  
ANISOU 4960  CA  MET B 333    10072  11265   7633  -4993  -1029   1189       C  
ATOM   4961  C   MET B 333     -24.857 -37.830 -51.125  1.00 79.03           C  
ANISOU 4961  C   MET B 333    10277  11861   7891  -5212  -1038   1195       C  
ATOM   4962  O   MET B 333     -25.419 -38.410 -52.050  1.00 81.04           O  
ANISOU 4962  O   MET B 333    10545  12176   8071  -5336  -1129   1167       O  
ATOM   4963  CB  MET B 333     -22.510 -38.547 -50.678  1.00 76.33           C  
ANISOU 4963  CB  MET B 333    10445  10971   7585  -5072  -1061   1170       C  
ATOM   4964  CG  MET B 333     -21.037 -38.397 -50.985  1.00 74.66           C  
ANISOU 4964  CG  MET B 333    10416  10519   7434  -4798  -1069   1135       C  
ATOM   4965  SD  MET B 333     -20.080 -39.829 -50.463  1.00 61.12           S  
ANISOU 4965  SD  MET B 333     9138   8461   5625  -4872  -1133   1104       S  
ATOM   4966  CE  MET B 333     -20.876 -41.106 -51.419  1.00 79.97           C  
ANISOU 4966  CE  MET B 333    11679  10808   7897  -5167  -1276   1074       C  
ATOM   4967  N   GLU B 334     -25.469 -37.505 -49.993  1.00 79.32           N  
ANISOU 4967  N   GLU B 334    10159  12053   7927  -5230   -944   1216       N  
ATOM   4968  CA  GLU B 334     -26.858 -37.863 -49.739  1.00 81.67           C  
ANISOU 4968  CA  GLU B 334    10300  12600   8133  -5405   -929   1228       C  
ATOM   4969  C   GLU B 334     -27.822 -37.026 -50.574  1.00 81.84           C  
ANISOU 4969  C   GLU B 334     9987  12939   8168  -5373   -946   1219       C  
ATOM   4970  O   GLU B 334     -28.989 -37.387 -50.737  1.00 84.15           O  
ANISOU 4970  O   GLU B 334    10145  13448   8379  -5523   -963   1211       O  
ATOM   4971  CB  GLU B 334     -27.189 -37.678 -48.256  1.00 82.56           C  
ANISOU 4971  CB  GLU B 334    10316  12839   8216  -5427   -818   1260       C  
ATOM   4972  CG  GLU B 334     -25.991 -37.377 -47.364  1.00 80.86           C  
ANISOU 4972  CG  GLU B 334    10232  12438   8054  -5293   -765   1258       C  
ATOM   4973  CD  GLU B 334     -25.148 -38.600 -47.074  1.00 81.05           C  
ANISOU 4973  CD  GLU B 334    10639  12141   8016  -5370   -806   1283       C  
ATOM   4974  OE1 GLU B 334     -24.298 -38.952 -47.916  1.00 79.99           O  
ANISOU 4974  OE1 GLU B 334    10721  11754   7918  -5313   -886   1253       O  
ATOM   4975  OE2 GLU B 334     -25.326 -39.214 -46.001  1.00 82.43           O  
ANISOU 4975  OE2 GLU B 334    10895  12328   8098  -5485   -758   1342       O  
ATOM   4976  N   ILE B 335     -27.330 -35.910 -51.102  1.00 79.50           N  
ANISOU 4976  N   ILE B 335     9548  12675   7984  -5180   -944   1230       N  
ATOM   4977  CA  ILE B 335     -28.190 -34.952 -51.786  1.00 79.76           C  
ANISOU 4977  CA  ILE B 335     9233  13029   8043  -5111   -956   1248       C  
ATOM   4978  C   ILE B 335     -28.233 -35.165 -53.289  1.00 79.74           C  
ANISOU 4978  C   ILE B 335     9248  13064   7985  -5099  -1070   1247       C  
ATOM   4979  O   ILE B 335     -27.201 -35.171 -53.959  1.00 78.28           O  
ANISOU 4979  O   ILE B 335     9254  12654   7836  -4927  -1099   1258       O  
ATOM   4980  CB  ILE B 335     -27.756 -33.520 -51.506  1.00 78.64           C  
ANISOU 4980  CB  ILE B 335     8926  12882   8072  -4776   -873   1266       C  
ATOM   4981  CG1 ILE B 335     -27.595 -33.318 -50.001  1.00 78.33           C  
ANISOU 4981  CG1 ILE B 335     8873  12816   8072  -4771   -778   1228       C  
ATOM   4982  CG2 ILE B 335     -28.765 -32.541 -52.083  1.00 80.00           C  
ANISOU 4982  CG2 ILE B 335     8753  13375   8268  -4636   -876   1290       C  
ATOM   4983  CD1 ILE B 335     -27.105 -31.951 -49.625  1.00 77.30           C  
ANISOU 4983  CD1 ILE B 335     8601  12628   8140  -4431   -711   1197       C  
ATOM   4984  N   ARG B 336     -29.444 -35.325 -53.812  1.00 81.51           N  
ANISOU 4984  N   ARG B 336     9262  13602   8109  -5241  -1130   1224       N  
ATOM   4985  CA  ARG B 336     -29.628 -35.624 -55.223  1.00 81.93           C  
ANISOU 4985  CA  ARG B 336     9308  13754   8067  -5239  -1258   1193       C  
ATOM   4986  C   ARG B 336     -30.515 -34.577 -55.872  1.00 83.07           C  
ANISOU 4986  C   ARG B 336     9095  14269   8197  -5044  -1261   1232       C  
ATOM   4987  O   ARG B 336     -31.292 -33.915 -55.191  1.00 83.47           O  
ANISOU 4987  O   ARG B 336     8886  14542   8286  -5028  -1190   1250       O  
ATOM   4988  CB  ARG B 336     -30.235 -37.020 -55.388  1.00 83.34           C  
ANISOU 4988  CB  ARG B 336     9631  13908   8125  -5524  -1338   1094       C  
ATOM   4989  CG  ARG B 336     -29.460 -38.140 -54.701  1.00 82.34           C  
ANISOU 4989  CG  ARG B 336     9892  13379   8015  -5640  -1320   1070       C  
ATOM   4990  CD  ARG B 336     -28.133 -38.443 -55.386  1.00 80.63           C  
ANISOU 4990  CD  ARG B 336     9947  12884   7804  -5566  -1406   1046       C  
ATOM   4991  NE  ARG B 336     -27.107 -37.455 -55.068  1.00 78.28           N  
ANISOU 4991  NE  ARG B 336     9655  12473   7616  -5311  -1319   1129       N  
ATOM   4992  CZ  ARG B 336     -25.851 -37.506 -55.496  1.00 77.25           C  
ANISOU 4992  CZ  ARG B 336     9755  12087   7510  -5103  -1330   1129       C  
ATOM   4993  NH1 ARG B 336     -24.994 -36.556 -55.150  1.00 75.19           N  
ANISOU 4993  NH1 ARG B 336     9475  11717   7379  -4827  -1223   1202       N  
ATOM   4994  NH2 ARG B 336     -25.450 -38.506 -56.265  1.00 78.41           N  
ANISOU 4994  NH2 ARG B 336    10138  12094   7559  -5169  -1452   1041       N  
ATOM   4995  N   PRO B 337     -30.386 -34.405 -57.194  1.00 83.91           N  
ANISOU 4995  N   PRO B 337     9186  14460   8237  -4864  -1343   1247       N  
ATOM   4996  CA  PRO B 337     -31.304 -33.506 -57.893  1.00 85.82           C  
ANISOU 4996  CA  PRO B 337     9092  15082   8434  -4674  -1363   1295       C  
ATOM   4997  C   PRO B 337     -32.711 -34.072 -57.813  1.00 88.57           C  
ANISOU 4997  C   PRO B 337     9213  15786   8652  -4976  -1440   1188       C  
ATOM   4998  O   PRO B 337     -32.914 -35.261 -58.064  1.00 89.53           O  
ANISOU 4998  O   PRO B 337     9457  15890   8671  -5282  -1548   1070       O  
ATOM   4999  CB  PRO B 337     -30.791 -33.532 -59.337  1.00 86.18           C  
ANISOU 4999  CB  PRO B 337     9222  15142   8380  -4467  -1448   1327       C  
ATOM   5000  CG  PRO B 337     -30.009 -34.791 -59.448  1.00 73.77           C  
ANISOU 5000  CG  PRO B 337     7993  13289   6749  -4665  -1521   1220       C  
ATOM   5001  CD  PRO B 337     -29.399 -35.003 -58.105  1.00 83.27           C  
ANISOU 5001  CD  PRO B 337     9381  14163   8096  -4794  -1419   1225       C  
ATOM   5002  N   LEU B 338     -33.663 -33.226 -57.444  1.00 90.04           N  
ANISOU 5002  N   LEU B 338     9068  16286   8859  -4891  -1388   1220       N  
ATOM   5003  CA  LEU B 338     -35.030 -33.663 -57.215  1.00 93.45           C  
ANISOU 5003  CA  LEU B 338     9275  17049   9184  -5123  -1414   1125       C  
ATOM   5004  C   LEU B 338     -35.630 -34.326 -58.450  1.00 96.30           C  
ANISOU 5004  C   LEU B 338     9591  17616   9382  -5198  -1560   1023       C  
ATOM   5005  O   LEU B 338     -36.201 -35.414 -58.363  1.00 98.14           O  
ANISOU 5005  O   LEU B 338     9922  17803   9564  -5446  -1574    903       O  
ATOM   5006  CB  LEU B 338     -35.889 -32.476 -56.779  1.00 94.33           C  
ANISOU 5006  CB  LEU B 338     9010  17500   9330  -4929  -1344   1173       C  
ATOM   5007  CG  LEU B 338     -37.346 -32.755 -56.422  1.00 84.23           C  
ANISOU 5007  CG  LEU B 338     7519  16536   7949  -5046  -1310   1082       C  
ATOM   5008  CD1 LEU B 338     -37.437 -33.922 -55.466  1.00 84.75           C  
ANISOU 5008  CD1 LEU B 338     7822  16372   8008  -5351  -1236   1024       C  
ATOM   5009  CD2 LEU B 338     -37.981 -31.519 -55.813  1.00 84.69           C  
ANISOU 5009  CD2 LEU B 338     7241  16879   8057  -4814  -1231   1121       C  
ATOM   5010  N   LYS B 339     -35.481 -33.671 -59.597  1.00 96.62           N  
ANISOU 5010  N   LYS B 339     9491  17875   9346  -4954  -1665   1076       N  
ATOM   5011  CA  LYS B 339     -36.131 -34.120 -60.820  1.00 99.20           C  
ANISOU 5011  CA  LYS B 339     9712  18491   9487  -4958  -1814    966       C  
ATOM   5012  C   LYS B 339     -35.135 -34.447 -61.923  1.00 98.13           C  
ANISOU 5012  C   LYS B 339     9815  18206   9264  -4820  -1918    963       C  
ATOM   5013  O   LYS B 339     -35.212 -35.508 -62.538  1.00 99.72           O  
ANISOU 5013  O   LYS B 339    10138  18395   9354  -5003  -2046    792       O  
ATOM   5014  CB  LYS B 339     -37.124 -33.061 -61.300  1.00101.05           C  
ANISOU 5014  CB  LYS B 339     9537  19218   9640  -4697  -1837   1025       C  
ATOM   5015  CG  LYS B 339     -38.169 -32.696 -60.259  1.00102.24           C  
ANISOU 5015  CG  LYS B 339     9462  19523   9860  -4752  -1711   1009       C  
ATOM   5016  CD  LYS B 339     -39.049 -31.546 -60.716  1.00104.27           C  
ANISOU 5016  CD  LYS B 339     9323  20247  10048  -4436  -1736   1075       C  
ATOM   5017  CE  LYS B 339     -40.080 -31.196 -59.653  1.00105.92           C  
ANISOU 5017  CE  LYS B 339     9312  20626  10306  -4473  -1615   1036       C  
ATOM   5018  NZ  LYS B 339     -40.927 -30.036 -60.045  1.00108.09           N  
ANISOU 5018  NZ  LYS B 339     9206  21338  10524  -4128  -1638   1094       N  
ATOM   5019  N   GLU B 340     -34.208 -33.528 -62.170  1.00 95.90           N  
ANISOU 5019  N   GLU B 340     9630  17749   9060  -4437  -1818   1149       N  
ATOM   5020  CA  GLU B 340     -33.213 -33.694 -63.224  1.00 94.86           C  
ANISOU 5020  CA  GLU B 340     9716  17485   8840  -4223  -1867   1186       C  
ATOM   5021  C   GLU B 340     -32.433 -34.992 -63.060  1.00 93.51           C  
ANISOU 5021  C   GLU B 340     9899  16964   8664  -4496  -1928   1033       C  
ATOM   5022  O   GLU B 340     -32.003 -35.326 -61.959  1.00 91.64           O  
ANISOU 5022  O   GLU B 340     9842  16396   8581  -4693  -1846   1028       O  
ATOM   5023  CB  GLU B 340     -32.245 -32.510 -63.228  1.00 92.80           C  
ANISOU 5023  CB  GLU B 340     9514  17016   8730  -3833  -1711   1438       C  
ATOM   5024  CG  GLU B 340     -31.220 -32.552 -64.344  1.00 92.54           C  
ANISOU 5024  CG  GLU B 340     9661  16904   8596  -3580  -1733   1521       C  
ATOM   5025  CD  GLU B 340     -31.835 -32.343 -65.705  1.00 95.31           C  
ANISOU 5025  CD  GLU B 340     9807  17709   8699  -3356  -1845   1544       C  
ATOM   5026  OE1 GLU B 340     -31.279 -32.855 -66.696  1.00 96.08           O  
ANISOU 5026  OE1 GLU B 340    10039  17853   8615  -3255  -1927   1504       O  
ATOM   5027  OE2 GLU B 340     -32.874 -31.659 -65.783  1.00 97.00           O  
ANISOU 5027  OE2 GLU B 340     9716  18257   8884  -3257  -1854   1597       O  
ATOM   5028  N   LYS B 341     -32.278 -35.729 -64.155  1.00 94.52           N  
ANISOU 5028  N   LYS B 341    10123  17184   8606  -4487  -2082    899       N  
ATOM   5029  CA  LYS B 341     -31.499 -36.959 -64.141  1.00 93.74           C  
ANISOU 5029  CA  LYS B 341    10374  16748   8496  -4691  -2162    737       C  
ATOM   5030  C   LYS B 341     -30.083 -36.632 -63.710  1.00 90.20           C  
ANISOU 5030  C   LYS B 341    10195  15892   8187  -4503  -2017    892       C  
ATOM   5031  O   LYS B 341     -29.491 -35.677 -64.203  1.00 89.02           O  
ANISOU 5031  O   LYS B 341     9999  15783   8041  -4139  -1926   1081       O  
ATOM   5032  CB  LYS B 341     -31.487 -37.595 -65.529  1.00 96.13           C  
ANISOU 5032  CB  LYS B 341    10709  17257   8558  -4603  -2353    564       C  
ATOM   5033  CG  LYS B 341     -30.676 -38.877 -65.615  1.00 96.36           C  
ANISOU 5033  CG  LYS B 341    11105  16936   8570  -4773  -2459    366       C  
ATOM   5034  CD  LYS B 341     -30.610 -39.384 -67.045  1.00 99.06           C  
ANISOU 5034  CD  LYS B 341    11461  17520   8656  -4613  -2650    177       C  
ATOM   5035  CE  LYS B 341     -29.991 -40.768 -67.110  1.00 99.99           C  
ANISOU 5035  CE  LYS B 341    11937  17246   8808  -4764  -2752    -72       C  
ATOM   5036  NZ  LYS B 341     -29.881 -41.268 -68.510  1.00102.70           N  
ANISOU 5036  NZ  LYS B 341    12301  17790   8929  -4535  -2916   -288       N  
ATOM   5037  N   GLU B 342     -29.543 -37.419 -62.785  1.00 88.99           N  
ANISOU 5037  N   GLU B 342    10312  15351   8151  -4751  -1994    822       N  
ATOM   5038  CA  GLU B 342     -28.234 -37.115 -62.214  1.00 86.42           C  
ANISOU 5038  CA  GLU B 342    10217  14650   7967  -4593  -1857    949       C  
ATOM   5039  C   GLU B 342     -27.106 -37.287 -63.229  1.00 85.64           C  
ANISOU 5039  C   GLU B 342    10312  14465   7760  -4326  -1895    949       C  
ATOM   5040  O   GLU B 342     -26.011 -36.757 -63.044  1.00 72.73           O  
ANISOU 5040  O   GLU B 342     8789  12618   6226  -4108  -1773   1090       O  
ATOM   5041  CB  GLU B 342     -27.968 -37.967 -60.970  1.00 86.04           C  
ANISOU 5041  CB  GLU B 342    10408  14244   8041  -4908  -1833    877       C  
ATOM   5042  CG  GLU B 342     -27.488 -39.376 -61.261  1.00 87.45           C  
ANISOU 5042  CG  GLU B 342    10909  14178   8140  -5087  -1977    687       C  
ATOM   5043  CD  GLU B 342     -27.047 -40.112 -60.011  1.00 86.73           C  
ANISOU 5043  CD  GLU B 342    11081  13695   8176  -5331  -1930    675       C  
ATOM   5044  OE1 GLU B 342     -26.265 -41.075 -60.136  1.00 87.13           O  
ANISOU 5044  OE1 GLU B 342    11452  13451   8203  -5371  -2012    567       O  
ATOM   5045  OE2 GLU B 342     -27.483 -39.735 -58.905  1.00 85.86           O  
ANISOU 5045  OE2 GLU B 342    10858  13587   8177  -5462  -1815    772       O  
ATOM   5046  N   GLU B 343     -27.382 -38.020 -64.304  1.00 87.52           N  
ANISOU 5046  N   GLU B 343    10571  14894   7789  -4340  -2069    777       N  
ATOM   5047  CA  GLU B 343     -26.386 -38.250 -65.344  1.00 87.10           C  
ANISOU 5047  CA  GLU B 343    10680  14830   7585  -4071  -2118    751       C  
ATOM   5048  C   GLU B 343     -26.211 -37.025 -66.227  1.00 87.20           C  
ANISOU 5048  C   GLU B 343    10473  15139   7518  -3666  -2025    986       C  
ATOM   5049  O   GLU B 343     -25.308 -36.969 -67.060  1.00 87.44           O  
ANISOU 5049  O   GLU B 343    10594  15201   7429  -3391  -2015   1040       O  
ATOM   5050  CB  GLU B 343     -26.763 -39.458 -66.198  1.00 89.21           C  
ANISOU 5050  CB  GLU B 343    11035  15217   7645  -4204  -2352    452       C  
ATOM   5051  CG  GLU B 343     -26.739 -40.776 -65.448  1.00 89.00           C  
ANISOU 5051  CG  GLU B 343    11284  14821   7712  -4585  -2453    232       C  
ATOM   5052  CD  GLU B 343     -26.445 -41.950 -66.357  1.00 90.81           C  
ANISOU 5052  CD  GLU B 343    11721  15012   7769  -4592  -2667    -58       C  
ATOM   5053  OE1 GLU B 343     -26.204 -41.720 -67.562  1.00 91.85           O  
ANISOU 5053  OE1 GLU B 343    11777  15439   7684  -4278  -2729    -92       O  
ATOM   5054  OE2 GLU B 343     -26.447 -43.099 -65.867  1.00 91.46           O  
ANISOU 5054  OE2 GLU B 343    12045  14762   7945  -4885  -2766   -248       O  
ATOM   5055  N   ASN B 344     -27.089 -36.048 -66.046  1.00 87.47           N  
ANISOU 5055  N   ASN B 344    10214  15401   7619  -3621  -1954   1137       N  
ATOM   5056  CA  ASN B 344     -26.956 -34.785 -66.746  1.00 87.78           C  
ANISOU 5056  CA  ASN B 344    10048  15669   7634  -3240  -1846   1410       C  
ATOM   5057  C   ASN B 344     -26.109 -33.823 -65.918  1.00 85.52           C  
ANISOU 5057  C   ASN B 344     9801  15064   7630  -3118  -1636   1649       C  
ATOM   5058  O   ASN B 344     -25.829 -32.706 -66.343  1.00 85.38           O  
ANISOU 5058  O   ASN B 344     9644  15128   7670  -2816  -1518   1912       O  
ATOM   5059  CB  ASN B 344     -28.334 -34.186 -67.023  1.00 90.00           C  
ANISOU 5059  CB  ASN B 344     9991  16361   7846  -3213  -1889   1448       C  
ATOM   5060  CG  ASN B 344     -29.335 -35.224 -67.490  1.00 93.10           C  
ANISOU 5060  CG  ASN B 344    10321  17031   8024  -3447  -2107   1151       C  
ATOM   5061  OD1 ASN B 344     -28.960 -36.301 -67.948  1.00 94.28           O  
ANISOU 5061  OD1 ASN B 344    10670  17117   8034  -3544  -2242    933       O  
ATOM   5062  ND2 ASN B 344     -30.617 -34.899 -67.386  1.00 83.93           N  
ANISOU 5062  ND2 ASN B 344     8869  16182   6840  -3533  -2151   1126       N  
ATOM   5063  N   LEU B 345     -25.698 -34.274 -64.735  1.00 83.92           N  
ANISOU 5063  N   LEU B 345     9787  14493   7607  -3354  -1596   1555       N  
ATOM   5064  CA  LEU B 345     -24.926 -33.439 -63.815  1.00 81.68           C  
ANISOU 5064  CA  LEU B 345     9534  13901   7600  -3270  -1420   1720       C  
ATOM   5065  C   LEU B 345     -23.466 -33.869 -63.697  1.00 81.44           C  
ANISOU 5065  C   LEU B 345     9784  13546   7616  -3217  -1375   1708       C  
ATOM   5066  O   LEU B 345     -23.107 -35.006 -64.006  1.00 81.50           O  
ANISOU 5066  O   LEU B 345    10008  13493   7463  -3313  -1488   1529       O  
ATOM   5067  CB  LEU B 345     -25.565 -33.420 -62.423  1.00 79.21           C  
ANISOU 5067  CB  LEU B 345     9176  13459   7459  -3528  -1386   1643       C  
ATOM   5068  CG  LEU B 345     -26.771 -32.506 -62.205  1.00 78.57           C  
ANISOU 5068  CG  LEU B 345     8775  13640   7439  -3497  -1355   1721       C  
ATOM   5069  CD1 LEU B 345     -28.022 -33.099 -62.812  1.00 80.37           C  
ANISOU 5069  CD1 LEU B 345     8855  14241   7439  -3646  -1506   1586       C  
ATOM   5070  CD2 LEU B 345     -26.973 -32.242 -60.729  1.00 76.75           C  
ANISOU 5070  CD2 LEU B 345     8517  13229   7415  -3654  -1269   1687       C  
ATOM   5071  N   VAL B 346     -22.631 -32.946 -63.234  1.00 81.75           N  
ANISOU 5071  N   VAL B 346     9804  13371   7884  -3058  -1218   1885       N  
ATOM   5072  CA  VAL B 346     -21.207 -33.208 -63.087  1.00 82.89           C  
ANISOU 5072  CA  VAL B 346    10169  13235   8092  -2984  -1161   1888       C  
ATOM   5073  C   VAL B 346     -20.898 -33.725 -61.686  1.00 84.07           C  
ANISOU 5073  C   VAL B 346    10497  13059   8388  -3210  -1152   1739       C  
ATOM   5074  O   VAL B 346     -21.362 -33.167 -60.694  1.00 83.43           O  
ANISOU 5074  O   VAL B 346    10304  12908   8488  -3298  -1090   1755       O  
ATOM   5075  CB  VAL B 346     -20.380 -31.945 -63.379  1.00 82.45           C  
ANISOU 5075  CB  VAL B 346     9985  13119   8222  -2700   -997   2161       C  
ATOM   5076  CG1 VAL B 346     -18.896 -32.268 -63.393  1.00 81.54           C  
ANISOU 5076  CG1 VAL B 346    10064  12780   8136  -2614   -945   2158       C  
ATOM   5077  CG2 VAL B 346     -20.801 -31.343 -64.709  1.00 67.33           C  
ANISOU 5077  CG2 VAL B 346     7874  11550   6160  -2462   -990   2361       C  
ATOM   5078  N   ASN B 347     -20.120 -34.800 -61.615  1.00 86.61           N  
ANISOU 5078  N   ASN B 347    11094  13202   8613  -3281  -1218   1591       N  
ATOM   5079  CA  ASN B 347     -19.751 -35.396 -60.339  1.00 88.31           C  
ANISOU 5079  CA  ASN B 347    11506  13117   8930  -3470  -1216   1465       C  
ATOM   5080  C   ASN B 347     -18.252 -35.607 -60.232  1.00 90.97           C  
ANISOU 5080  C   ASN B 347    12041  13215   9310  -3327  -1173   1457       C  
ATOM   5081  O   ASN B 347     -17.508 -35.349 -61.176  1.00 91.05           O  
ANISOU 5081  O   ASN B 347    12031  13300   9262  -3100  -1142   1545       O  
ATOM   5082  CB  ASN B 347     -20.472 -36.732 -60.128  1.00 88.58           C  
ANISOU 5082  CB  ASN B 347    11712  13137   8809  -3763  -1367   1264       C  
ATOM   5083  CG  ASN B 347     -20.162 -37.742 -61.218  1.00 89.35           C  
ANISOU 5083  CG  ASN B 347    11990  13278   8682  -3724  -1507   1134       C  
ATOM   5084  OD1 ASN B 347     -19.207 -38.509 -61.114  1.00 88.60           O  
ANISOU 5084  OD1 ASN B 347    12158  12957   8548  -3696  -1545   1037       O  
ATOM   5085  ND2 ASN B 347     -20.974 -37.750 -62.269  1.00 91.13           N  
ANISOU 5085  ND2 ASN B 347    12070  13812   8746  -3700  -1594   1112       N  
ATOM   5086  N   SER B 348     -17.818 -36.080 -59.070  1.00 94.01           N  
ANISOU 5086  N   SER B 348    12601  13340   9780  -3452  -1167   1358       N  
ATOM   5087  CA  SER B 348     -16.420 -36.419 -58.855  1.00 96.80           C  
ANISOU 5087  CA  SER B 348    13153  13471  10157  -3328  -1145   1316       C  
ATOM   5088  C   SER B 348     -16.069 -37.679 -59.639  1.00100.78           C  
ANISOU 5088  C   SER B 348    13907  13961  10423  -3320  -1282   1176       C  
ATOM   5089  O   SER B 348     -16.607 -38.752 -59.372  1.00101.37           O  
ANISOU 5089  O   SER B 348    14167  13954  10395  -3532  -1403   1029       O  
ATOM   5090  CB  SER B 348     -16.162 -36.633 -57.364  1.00 96.17           C  
ANISOU 5090  CB  SER B 348    13189  13151  10199  -3454  -1118   1241       C  
ATOM   5091  OG  SER B 348     -14.817 -36.998 -57.123  1.00 95.74           O  
ANISOU 5091  OG  SER B 348    13322  12901  10155  -3323  -1109   1186       O  
ATOM   5092  N   LEU B 349     -15.173 -37.539 -60.613  1.00103.88           N  
ANISOU 5092  N   LEU B 349    14298  14435  10736  -3073  -1261   1222       N  
ATOM   5093  CA  LEU B 349     -14.752 -38.666 -61.440  1.00107.26           C  
ANISOU 5093  CA  LEU B 349    14949  14879  10927  -3004  -1394   1067       C  
ATOM   5094  C   LEU B 349     -13.488 -39.315 -60.887  1.00107.11           C  
ANISOU 5094  C   LEU B 349    15181  14599  10917  -2924  -1403    964       C  
ATOM   5095  O   LEU B 349     -13.500 -39.900 -59.804  1.00106.79           O  
ANISOU 5095  O   LEU B 349    15323  14311  10942  -3088  -1440    871       O  
ATOM   5096  CB  LEU B 349     -14.511 -38.215 -62.881  1.00109.28           C  
ANISOU 5096  CB  LEU B 349    15050  15438  11034  -2748  -1370   1169       C  
ATOM   5097  CG  LEU B 349     -15.691 -37.560 -63.596  1.00110.69           C  
ANISOU 5097  CG  LEU B 349    14972  15923  11161  -2763  -1368   1284       C  
ATOM   5098  CD1 LEU B 349     -15.297 -37.138 -65.000  1.00112.22           C  
ANISOU 5098  CD1 LEU B 349    15028  16429  11181  -2469  -1332   1414       C  
ATOM   5099  CD2 LEU B 349     -16.873 -38.509 -63.634  1.00112.11           C  
ANISOU 5099  CD2 LEU B 349    15240  16148  11209  -3011  -1545   1083       C  
TER    5100      LEU B 349                                                      
HETATM 5101  C1  NAG A 401      13.106 -37.431 -21.862  1.00 67.37           C  
HETATM 5102  C2  NAG A 401      13.862 -36.533 -20.880  1.00 70.37           C  
HETATM 5103  C3  NAG A 401      15.309 -36.998 -20.737  1.00 71.45           C  
HETATM 5104  C4  NAG A 401      15.354 -38.475 -20.364  1.00 71.74           C  
HETATM 5105  C5  NAG A 401      14.556 -39.289 -21.379  1.00 71.18           C  
HETATM 5106  C6  NAG A 401      14.468 -40.755 -21.020  1.00 71.74           C  
HETATM 5107  C7  NAG A 401      13.440 -34.142 -20.503  1.00 73.27           C  
HETATM 5108  C8  NAG A 401      13.066 -34.527 -19.101  1.00 73.71           C  
HETATM 5109  N2  NAG A 401      13.813 -35.141 -21.308  1.00 71.86           N  
HETATM 5110  O3  NAG A 401      15.969 -36.221 -19.744  1.00 71.78           O  
HETATM 5111  O4  NAG A 401      16.700 -38.939 -20.335  1.00 71.86           O  
HETATM 5112  O5  NAG A 401      13.209 -38.797 -21.437  1.00 69.69           O  
HETATM 5113  O6  NAG A 401      13.283 -41.347 -21.535  1.00 71.93           O  
HETATM 5114  O7  NAG A 401      13.406 -32.978 -20.888  1.00 73.77           O  
HETATM 5115  C1  NAG B 401     -29.053 -23.643 -34.190  1.00 59.60           C  
HETATM 5116  C2  NAG B 401     -28.764 -22.280 -34.805  1.00 62.04           C  
HETATM 5117  C3  NAG B 401     -30.062 -21.489 -34.949  1.00 62.88           C  
HETATM 5118  C4  NAG B 401     -31.096 -22.296 -35.720  1.00 63.40           C  
HETATM 5119  C5  NAG B 401     -31.276 -23.670 -35.078  1.00 63.02           C  
HETATM 5120  C6  NAG B 401     -32.188 -24.576 -35.873  1.00 63.77           C  
HETATM 5121  C7  NAG B 401     -26.630 -21.114 -34.504  1.00 64.06           C  
HETATM 5122  C8  NAG B 401     -25.758 -20.356 -33.551  1.00 64.26           C  
HETATM 5123  N2  NAG B 401     -27.800 -21.541 -34.015  1.00 63.22           N  
HETATM 5124  O3  NAG B 401     -29.800 -20.259 -35.617  1.00 63.17           O  
HETATM 5125  O4  NAG B 401     -32.342 -21.608 -35.721  1.00 63.90           O  
HETATM 5126  O5  NAG B 401     -30.008 -24.339 -34.986  1.00 61.69           O  
HETATM 5127  O6  NAG B 401     -33.119 -23.823 -36.639  1.00 64.13           O  
HETATM 5128  O7  NAG B 401     -26.293 -21.332 -35.666  1.00 64.11           O  
CONECT   29   90                                                                
CONECT   90   29                                                                
CONECT  403  933                                                                
CONECT  933  403                                                                
CONECT 1183 1532                                                                
CONECT 1399 5101                                                                
CONECT 1532 1183                                                                
CONECT 1998 2362                                                                
CONECT 2075 2231                                                                
CONECT 2231 2075                                                                
CONECT 2237 2260                                                                
CONECT 2260 2237                                                                
CONECT 2362 1998                                                                
CONECT 2558 2650                                                                
CONECT 2650 2558                                                                
CONECT 2963 3466                                                                
CONECT 3466 2963                                                                
CONECT 3749 4098                                                                
CONECT 3965 5115                                                                
CONECT 4098 3749                                                                
CONECT 4564 4928                                                                
CONECT 4641 4797                                                                
CONECT 4797 4641                                                                
CONECT 4803 4826                                                                
CONECT 4826 4803                                                                
CONECT 4928 4564                                                                
CONECT 5101 1399 5102 5112                                                      
CONECT 5102 5101 5103 5109                                                      
CONECT 5103 5102 5104 5110                                                      
CONECT 5104 5103 5105 5111                                                      
CONECT 5105 5104 5106 5112                                                      
CONECT 5106 5105 5113                                                           
CONECT 5107 5108 5109 5114                                                      
CONECT 5108 5107                                                                
CONECT 5109 5102 5107                                                           
CONECT 5110 5103                                                                
CONECT 5111 5104                                                                
CONECT 5112 5101 5105                                                           
CONECT 5113 5106                                                                
CONECT 5114 5107                                                                
CONECT 5115 3965 5116 5126                                                      
CONECT 5116 5115 5117 5123                                                      
CONECT 5117 5116 5118 5124                                                      
CONECT 5118 5117 5119 5125                                                      
CONECT 5119 5118 5120 5126                                                      
CONECT 5120 5119 5127                                                           
CONECT 5121 5122 5123 5128                                                      
CONECT 5122 5121                                                                
CONECT 5123 5116 5121                                                           
CONECT 5124 5117                                                                
CONECT 5125 5118                                                                
CONECT 5126 5115 5119                                                           
CONECT 5127 5120                                                                
CONECT 5128 5121                                                                
MASTER      626    0    2   12   43    0    2    6 5126    2   54   58          
END                                                                             



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