HEADER    MEMBRANE PROTEIN                        13-DEC-19   6TPN              
TITLE     CRYSTAL STRUCTURE OF THE OREXIN-2 RECEPTOR IN COMPLEX WITH HTL6641 AT 
TITLE    2 2.61 A RESOLUTION                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OREXIN RECEPTOR TYPE 2,GLGA GLYCOGEN SYNTHASE,OREXIN       
COMPND   3 RECEPTOR TYPE 2;                                                     
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: OX2R,HYPOCRETIN RECEPTOR TYPE 2,GLYCOGEN SYNTHASE,OX2R,     
COMPND   6 HYPOCRETIN RECEPTOR TYPE 2;                                          
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 /   
SOURCE   3 ORSAY);                                                              
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   6 GENE: HCRTR2, PAB2292;                                               
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    7TM, GPCR, MEMBRANE PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE,         
AUTHOR   2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI,          
AUTHOR   3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR,           
AUTHOR   4 J.A.CHRISTOPHER                                                      
REVDAT   3   11-MAR-20 6TPN    1       JRNL                                     
REVDAT   2   29-JAN-20 6TPN    1       JRNL                                     
REVDAT   1   01-JAN-20 6TPN    0                                                
JRNL        AUTH   M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,       
JRNL        AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,  
JRNL        AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,         
JRNL        AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER                             
JRNL        TITL   COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES     
JRNL        TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.      
JRNL        REF    J.MED.CHEM.                   V.  63  1528 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   31860301                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B01787                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 60.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11692                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.190                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 607                             
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 41.4750 -  4.1385    0.97     4613   234  0.1943 0.2365        
REMARK   3     2  4.1385 -  3.2853    0.89     4051   247  0.2216 0.2640        
REMARK   3     3  3.2853 -  2.8701    0.43     1940    94  0.2723 0.2656        
REMARK   3     4  2.8701 -  2.6080    0.11      481    32  0.3015 0.2711        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.990           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 43 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2828 241.1950  10.4361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5824 T22:   0.4334                                     
REMARK   3      T33:   1.1439 T12:   0.1965                                     
REMARK   3      T13:  -0.0635 T23:  -0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6976 L22:   2.9601                                     
REMARK   3      L33:   1.3746 L12:   1.4554                                     
REMARK   3      L13:   0.9166 L23:   0.3476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5615 S12:  -1.2947 S13:   0.3901                       
REMARK   3      S21:   0.9890 S22:  -0.1102 S23:   0.3310                       
REMARK   3      S31:   0.2392 S32:  -0.1995 S33:  -0.5073                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 53 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  78.3258 239.8581  -4.6765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9074 T22:   0.5398                                     
REMARK   3      T33:   1.0432 T12:   0.0091                                     
REMARK   3      T13:   0.0720 T23:   0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1701 L22:   6.8143                                     
REMARK   3      L33:   4.4134 L12:  -2.5577                                     
REMARK   3      L13:  -1.9605 L23:   5.0197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1310 S12:   0.1298 S13:   0.1246                       
REMARK   3      S21:  -1.4301 S22:   0.1749 S23:   0.4159                       
REMARK   3      S31:  -0.3117 S32:  -0.2078 S33:  -0.0951                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 122 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  84.5267 212.2760   2.8264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2253 T22:   0.0261                                     
REMARK   3      T33:   0.6404 T12:   0.0152                                     
REMARK   3      T13:  -0.0308 T23:   0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4334 L22:   2.5265                                     
REMARK   3      L33:   1.4764 L12:  -1.7036                                     
REMARK   3      L13:  -0.0234 L23:   1.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0751 S12:  -0.1101 S13:  -0.2962                       
REMARK   3      S21:  -0.2138 S22:   0.0010 S23:   0.2090                       
REMARK   3      S31:   0.0633 S32:  -0.1317 S33:   0.0761                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 156 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  98.0755 212.1887   5.9472              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2497 T22:   0.1367                                     
REMARK   3      T33:   0.6267 T12:   0.0521                                     
REMARK   3      T13:   0.0118 T23:   0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1856 L22:   5.1954                                     
REMARK   3      L33:   1.2521 L12:  -3.3306                                     
REMARK   3      L13:  -1.7056 L23:   2.1118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1754 S12:  -0.3416 S13:  -0.1355                       
REMARK   3      S21:  -0.1321 S22:   0.3241 S23:  -0.2605                       
REMARK   3      S31:  -0.0117 S32:  -0.0016 S33:  -0.0377                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 109.2627 190.9442   2.9939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3296 T22:   0.3559                                     
REMARK   3      T33:   0.8723 T12:   0.0766                                     
REMARK   3      T13:  -0.0627 T23:  -0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1587 L22:   2.0593                                     
REMARK   3      L33:   5.9706 L12:  -1.7994                                     
REMARK   3      L13:  -3.8488 L23:   2.3705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5315 S12:  -0.1527 S13:   0.4200                       
REMARK   3      S21:   0.3582 S22:   0.1565 S23:   0.4131                       
REMARK   3      S31:   0.9148 S32:  -0.1242 S33:   0.1838                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 166 THROUGH 183 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 100.4302 206.4630  13.2169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5608 T22:   0.3855                                     
REMARK   3      T33:   0.4310 T12:   0.1724                                     
REMARK   3      T13:   0.0191 T23:  -0.0962                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8053 L22:   5.9622                                     
REMARK   3      L33:   2.3108 L12:  -0.1358                                     
REMARK   3      L13:   0.8867 L23:  -0.2316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9294 S12:   0.0426 S13:  -0.1270                       
REMARK   3      S21:   0.8920 S22:   1.0124 S23:  -0.6283                       
REMARK   3      S31:   0.2124 S32:   0.5810 S33:   0.0565                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  91.7034 236.6048   8.8399              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4924 T22:   0.2720                                     
REMARK   3      T33:   1.1615 T12:   0.0679                                     
REMARK   3      T13:  -0.2236 T23:  -0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9620 L22:   3.1333                                     
REMARK   3      L33:   1.9945 L12:  -3.0468                                     
REMARK   3      L13:  -0.3406 L23:   0.2791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4797 S12:   0.2001 S13:   1.3526                       
REMARK   3      S21:   0.1189 S22:   0.1143 S23:  -1.0807                       
REMARK   3      S31:  -0.6497 S32:  -0.5601 S33:  -0.2650                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 232 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 105.4470 227.4424   3.5650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4010 T22:   0.3014                                     
REMARK   3      T33:   0.9584 T12:   0.0022                                     
REMARK   3      T13:   0.0334 T23:  -0.1256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2715 L22:   4.1949                                     
REMARK   3      L33:   2.0033 L12:  -1.8716                                     
REMARK   3      L13:  -0.4953 L23:   2.2124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2823 S12:  -0.2637 S13:   0.7001                       
REMARK   3      S21:  -0.0456 S22:   0.6470 S23:  -0.0618                       
REMARK   3      S31:  -0.4927 S32:   0.3211 S33:  -0.3312                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 233 THROUGH 1003 )                
REMARK   3    ORIGIN FOR THE GROUP (A): 106.9564 198.7914 -10.3045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3193 T22:   0.1858                                     
REMARK   3      T33:   0.7937 T12:   0.0231                                     
REMARK   3      T13:   0.0079 T23:  -0.1023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6268 L22:   8.2005                                     
REMARK   3      L33:   2.3714 L12:  -1.0472                                     
REMARK   3      L13:  -0.1453 L23:   3.6227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3227 S12:   0.5437 S13:  -0.2364                       
REMARK   3      S21:  -0.8683 S22:  -0.2006 S23:  -0.4452                       
REMARK   3      S31:  -0.2352 S32:   0.0380 S33:  -0.0754                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1005 THROUGH 1027 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 106.9055 167.6366 -26.7123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7936 T22:   0.5491                                     
REMARK   3      T33:   0.9435 T12:   0.0524                                     
REMARK   3      T13:  -0.0289 T23:  -0.1258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8207 L22:   4.5331                                     
REMARK   3      L33:   0.8018 L12:  -2.8476                                     
REMARK   3      L13:  -0.4784 L23:   1.0520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2072 S12:   0.9186 S13:  -0.2117                       
REMARK   3      S21:  -1.0247 S22:  -0.6070 S23:   1.4338                       
REMARK   3      S31:   0.2395 S32:  -0.7329 S33:   0.3731                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1028 THROUGH 1060 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 125.1528 171.5965 -18.3145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4740 T22:   0.0125                                     
REMARK   3      T33:   0.7117 T12:  -0.0069                                     
REMARK   3      T13:   0.0713 T23:  -0.1268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1023 L22:   3.0869                                     
REMARK   3      L33:   2.5986 L12:  -1.9849                                     
REMARK   3      L13:   0.0252 L23:  -0.7066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1207 S12:   0.1268 S13:   0.0125                       
REMARK   3      S21:  -0.2958 S22:  -0.1968 S23:  -0.2325                       
REMARK   3      S31:   0.0373 S32:  -0.0376 S33:  -0.1611                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1061 THROUGH 1076 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 125.1099 165.4438 -20.3481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4991 T22:   0.1440                                     
REMARK   3      T33:   0.8480 T12:   0.0468                                     
REMARK   3      T13:   0.1942 T23:  -0.0742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8815 L22:   6.0884                                     
REMARK   3      L33:   2.6334 L12:  -1.1288                                     
REMARK   3      L13:   0.1657 L23:  -0.0787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0884 S12:   0.2138 S13:  -0.5876                       
REMARK   3      S21:  -0.5089 S22:  -0.4691 S23:  -0.7176                       
REMARK   3      S31:   0.1167 S32:   0.1314 S33:  -0.0620                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1077 THROUGH 1117 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 121.6139 172.6298 -25.2925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5393 T22:   0.1942                                     
REMARK   3      T33:   0.7233 T12:  -0.0129                                     
REMARK   3      T13:   0.0393 T23:  -0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8171 L22:   2.4264                                     
REMARK   3      L33:   1.1349 L12:  -0.6278                                     
REMARK   3      L13:  -0.4226 L23:   0.7635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1221 S12:   1.0123 S13:   0.2663                       
REMARK   3      S21:  -0.6423 S22:  -0.4176 S23:  -0.0114                       
REMARK   3      S31:  -0.1053 S32:  -0.1831 S33:  -0.2724                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1118 THROUGH 1149 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 113.6602 178.6066 -11.2609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3234 T22:   0.0774                                     
REMARK   3      T33:   0.9172 T12:  -0.1442                                     
REMARK   3      T13:   0.1550 T23:  -0.0862                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0865 L22:   2.1526                                     
REMARK   3      L33:   0.9081 L12:  -0.2014                                     
REMARK   3      L13:   0.4304 L23:   0.6888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0320 S12:   0.0056 S13:   0.0515                       
REMARK   3      S21:  -0.1401 S22:  -0.0120 S23:   0.5557                       
REMARK   3      S31:  -0.0811 S32:  -0.1421 S33:  -0.1741                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1150 THROUGH 1180 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 117.8975 166.0244  -7.7414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4864 T22:   0.0495                                     
REMARK   3      T33:   0.8714 T12:   0.0096                                     
REMARK   3      T13:   0.1948 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6277 L22:   4.9760                                     
REMARK   3      L33:   1.5102 L12:  -1.1576                                     
REMARK   3      L13:  -0.4650 L23:   0.6730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0404 S12:  -0.1424 S13:  -0.3598                       
REMARK   3      S21:   0.7052 S22:  -0.1647 S23:   0.2571                       
REMARK   3      S31:   0.3554 S32:  -0.1128 S33:   0.0382                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1181 THROUGH 328 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  99.5072 195.7909  -8.6148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2786 T22:   0.2212                                     
REMARK   3      T33:   0.6322 T12:  -0.0352                                     
REMARK   3      T13:   0.0105 T23:  -0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7947 L22:   6.8751                                     
REMARK   3      L33:   0.8928 L12:  -3.3478                                     
REMARK   3      L13:  -0.7082 L23:   0.5540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0039 S12:   0.2236 S13:  -0.3745                       
REMARK   3      S21:   0.2562 S22:  -0.1223 S23:   0.2067                       
REMARK   3      S31:   0.0704 S32:  -0.0951 S33:   0.0770                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 329 THROUGH 367 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  91.4404 222.9678  -7.5066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5209 T22:   0.2496                                     
REMARK   3      T33:   0.7135 T12:   0.0513                                     
REMARK   3      T13:  -0.0034 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7011 L22:   3.3803                                     
REMARK   3      L33:   1.9446 L12:  -0.6471                                     
REMARK   3      L13:   0.0708 L23:   1.2350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2788 S12:   0.2166 S13:   0.4550                       
REMARK   3      S21:  -0.6031 S22:  -0.1137 S23:  -0.1381                       
REMARK   3      S31:  -0.6200 S32:   0.0983 S33:  -0.0794                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 368 THROUGH 388 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  76.4023 195.2696  -0.3606              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5512 T22:   0.2597                                     
REMARK   3      T33:   1.4155 T12:  -0.0618                                     
REMARK   3      T13:  -0.0082 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8264 L22:   7.0003                                     
REMARK   3      L33:   4.3866 L12:  -2.0616                                     
REMARK   3      L13:   2.8159 L23:   0.8868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2615 S12:  -0.3308 S13:  -1.2225                       
REMARK   3      S21:   0.5872 S22:  -0.0337 S23:   1.7580                       
REMARK   3      S31:   0.5968 S32:  -0.7779 S33:   1.0063                       
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 6TPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105850.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0-6.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96863                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11699                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.608                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.488                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5WQC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRISODIUM CITRATE BUFFER 150      
REMARK 280  -300 MM LITHIUM NITRATE OR 150-300 MM POTASSIUM NITRATE 28-43 %     
REMARK 280  (V/V) POLYETHYLENE GLYCOL 400, LIPIDIC CUBIC PHASE, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.16350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.16350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.47250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.97500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.47250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.97500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.16350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.47250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       86.97500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.16350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.47250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       86.97500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     GLN A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ASP A    14                                                      
REMARK 465     TRP A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     LEU A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     HIS A   393                                                      
REMARK 465     HIS A   394                                                      
REMARK 465     HIS A   395                                                      
REMARK 465     HIS A   396                                                      
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    LYS A  51      -60.64   -127.41                                   
REMARK 500    GLU A 217       20.24    -79.00                                   
REMARK 500    TYR A 232      -61.94   -126.95                                   
REMARK 500    CYS A 252      -63.53    -99.95                                   
REMARK 500    GLN A1045      -83.60   -109.84                                   
REMARK 500    SER A1111      -54.70   -139.03                                   
REMARK 500    PHE A1124      -37.60   -133.61                                   
REMARK 500    THR A1151     -168.33   -107.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1206                                                       
REMARK 610     OLA A 1207                                                       
REMARK 610     OLA A 1209                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NU8 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209                
DBREF  6TPN A    1   254  UNP    O43614   OX2R_HUMAN       1    254             
DBREF  6TPN A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  6TPN A  294   388  UNP    O43614   OX2R_HUMAN     294    388             
SEQADV 6TPN GLN A  -10  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -9  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN LEU A   -8  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -7  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN TYR A   -6  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN LYS A   -5  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -4  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -3  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -2  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   -1  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN LYS A    0  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN ASP A   14  UNP  O43614    ASN    14 ENGINEERED MUTATION            
SEQADV 6TPN ASP A   22  UNP  O43614    ASN    22 ENGINEERED MUTATION            
SEQADV 6TPN LEU A   28  UNP  O43614    PHE    28 ENGINEERED MUTATION            
SEQADV 6TPN ASP A   30  UNP  O43614    ASN    30 ENGINEERED MUTATION            
SEQADV 6TPN ALA A   54  UNP  O43614    GLU    54 ENGINEERED MUTATION            
SEQADV 6TPN LEU A   91  UNP  O43614    TYR    91 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  100  UNP  O43614    ASP   100 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  142  UNP  O43614    VAL   142 ENGINEERED MUTATION            
SEQADV 6TPN LEU A  170  UNP  O43614    ARG   170 ENGINEERED MUTATION            
SEQADV 6TPN ASP A  202  UNP  O43614    ASN   202 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  206  UNP  O43614    LEU   206 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  219  UNP  O43614    TYR   219 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  233  UNP  O43614    MET   233 ENGINEERED MUTATION            
SEQADV 6TPN LEU A  242  UNP  O43614    ALA   242 ENGINEERED MUTATION            
SEQADV 6TPN VAL A  308  UNP  O43614    ILE   308 ENGINEERED MUTATION            
SEQADV 6TPN VAL A  310  UNP  O43614    LEU   310 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  318  UNP  O43614    LEU   318 ENGINEERED MUTATION            
SEQADV 6TPN ALA A  347  UNP  O43614    THR   347 ENGINEERED MUTATION            
SEQADV 6TPN TRP A  381  UNP  O43614    CYS   381 ENGINEERED MUTATION            
SEQADV 6TPN TRP A  382  UNP  O43614    CYS   382 ENGINEERED MUTATION            
SEQADV 6TPN TRP A  383  UNP  O43614    CYS   383 ENGINEERED MUTATION            
SEQADV 6TPN HIS A  389  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  390  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  391  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  392  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  393  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  394  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  395  UNP  O43614              EXPRESSION TAG                 
SEQADV 6TPN HIS A  396  UNP  O43614              EXPRESSION TAG                 
SEQRES   1 A  564  GLN ASP LEU ASP TYR LYS ASP ASP ASP ASP LYS MET SER          
SEQRES   2 A  564  GLY THR LYS LEU GLU ASP SER PRO PRO CYS ARG ASP TRP          
SEQRES   3 A  564  SER SER ALA SER GLU LEU ASP GLU THR GLN GLU PRO LEU          
SEQRES   4 A  564  LEU ASP PRO THR ASP TYR ASP ASP GLU GLU PHE LEU ARG          
SEQRES   5 A  564  TYR LEU TRP ARG GLU TYR LEU HIS PRO LYS GLU TYR ALA          
SEQRES   6 A  564  TRP VAL LEU ILE ALA GLY TYR ILE ILE VAL PHE VAL VAL          
SEQRES   7 A  564  ALA LEU ILE GLY ASN VAL LEU VAL CYS VAL ALA VAL TRP          
SEQRES   8 A  564  LYS ASN HIS HIS MET ARG THR VAL THR ASN LEU PHE ILE          
SEQRES   9 A  564  VAL ASN LEU SER LEU ALA ALA VAL LEU VAL THR ILE THR          
SEQRES  10 A  564  CYS LEU PRO ALA THR LEU VAL VAL ASP ILE THR GLU THR          
SEQRES  11 A  564  TRP PHE PHE GLY GLN SER LEU CYS LYS VAL ILE PRO TYR          
SEQRES  12 A  564  LEU GLN THR VAL SER VAL SER VAL SER ALA LEU THR LEU          
SEQRES  13 A  564  SER CYS ILE ALA LEU ASP ARG TRP TYR ALA ILE CYS HIS          
SEQRES  14 A  564  PRO LEU MET PHE LYS SER THR ALA LYS ARG ALA LEU ASN          
SEQRES  15 A  564  SER ILE VAL ILE ILE TRP ILE VAL SER CYS ILE ILE MET          
SEQRES  16 A  564  ILE PRO GLN ALA ILE VAL MET GLU CYS SER THR VAL PHE          
SEQRES  17 A  564  PRO GLY LEU ALA ASP LYS THR THR ALA PHE THR VAL CYS          
SEQRES  18 A  564  ASP GLU ARG TRP GLY GLY GLU ILE ALA PRO LYS MET TYR          
SEQRES  19 A  564  HIS ILE CYS PHE PHE LEU VAL THR TYR ALA ALA PRO LEU          
SEQRES  20 A  564  CYS LEU MET VAL LEU LEU TYR LEU GLN ILE PHE ARG LYS          
SEQRES  21 A  564  LEU TRP CYS ARG GLN GLY ILE ASP YCM SER PHE TRP ASN          
SEQRES  22 A  564  GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS          
SEQRES  23 A  564  SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR          
SEQRES  24 A  564  PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY          
SEQRES  25 A  564  VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER          
SEQRES  26 A  564  LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY          
SEQRES  27 A  564  LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU          
SEQRES  28 A  564  GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET          
SEQRES  29 A  564  LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL          
SEQRES  30 A  564  ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY          
SEQRES  31 A  564  LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO          
SEQRES  32 A  564  ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR          
SEQRES  33 A  564  ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY          
SEQRES  34 A  564  GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER          
SEQRES  35 A  564  ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS          
SEQRES  36 A  564  ARG ALA MET SER PHE SER LYS GLN ILE ARG ALA ARG ARG          
SEQRES  37 A  564  LYS THR ALA ARG MET LEU MET VAL VAL VAL LEU VAL PHE          
SEQRES  38 A  564  ALA ILE CYS TYR ALA PRO ILE SER ILE LEU ASN VAL LEU          
SEQRES  39 A  564  LYS ARG VAL PHE GLY MET PHE ALA HIS THR GLU ASP ARG          
SEQRES  40 A  564  GLU THR VAL TYR ALA TRP PHE ALA PHE SER HIS TRP LEU          
SEQRES  41 A  564  VAL TYR ALA ASN SER ALA ALA ASN PRO ILE ILE TYR ASN          
SEQRES  42 A  564  PHE LEU SER GLY LYS PHE ARG GLU GLU PHE LYS ALA ALA          
SEQRES  43 A  564  PHE SER TRP TRP TRP LEU GLY VAL HIS HIS HIS HIS HIS          
SEQRES  44 A  564  HIS HIS HIS HIS HIS                                          
MODRES 6TPN YCM A 1004  CYS  MODIFIED RESIDUE                                   
HET    YCM  A1004      10                                                       
HET    NU8  A1201      33                                                       
HET    NO3  A1202       4                                                       
HET    NO3  A1203       4                                                       
HET    PG4  A1204      13                                                       
HET    PG4  A1205      13                                                       
HET    OLA  A1206      13                                                       
HET    OLA  A1207      10                                                       
HET    OLA  A1208      20                                                       
HET    OLA  A1209      13                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     NU8 2-(5,6-DIMETHOXYPYRIDIN-3-YL)-1,1-BIS(OXIDANYLIDENE)-4-          
HETNAM   2 NU8  [[2,4,6-TRIS(FLUORANYL)PHENYL]METHYL]PYRIDO[2,3-E][1,           
HETNAM   3 NU8  2,4]THIADIAZIN-3-ONE                                            
HETNAM     NO3 NITRATE ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     OLA OLEIC ACID                                                       
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
FORMUL   1  YCM    C5 H10 N2 O3 S                                               
FORMUL   2  NU8    C20 H15 F3 N4 O5 S                                           
FORMUL   3  NO3    2(N O3 1-)                                                   
FORMUL   5  PG4    2(C8 H18 O5)                                                 
FORMUL   7  OLA    4(C18 H34 O2)                                                
FORMUL  11  HOH   *46(H2 O)                                                     
HELIX    1 AA1 GLU A   38  TRP A   44  1                                   7    
HELIX    2 AA2 TYR A   53  ASN A   82  1                                  30    
HELIX    3 AA3 HIS A   83  ARG A   86  5                                   4    
HELIX    4 AA4 THR A   87  CYS A  107  1                                  21    
HELIX    5 AA5 CYS A  107  GLU A  118  1                                  12    
HELIX    6 AA6 PHE A  122  CYS A  157  1                                  36    
HELIX    7 AA7 THR A  165  MET A  184  1                                  20    
HELIX    8 AA8 MET A  184  VAL A  190  1                                   7    
HELIX    9 AA9 ILE A  218  TYR A  232  1                                  15    
HELIX   10 AB1 TYR A  232  CYS A  252  1                                  21    
HELIX   11 AB2 SER A 1015  PHE A 1027  1                                  13    
HELIX   12 AB3 GLY A 1047  SER A 1059  1                                  13    
HELIX   13 AB4 SER A 1060  GLN A 1065  5                                   6    
HELIX   14 AB5 ASP A 1076  HIS A 1090  1                                  15    
HELIX   15 AB6 SER A 1101  GLY A 1110  1                                  10    
HELIX   16 AB7 GLY A 1125  CYS A 1133  1                                   9    
HELIX   17 AB8 VAL A 1143  ILE A 1150  1                                   8    
HELIX   18 AB9 ASP A 1162  SER A 1177  1                                  16    
HELIX   19 AC1 LEU A 1181  VAL A  329  1                                  52    
HELIX   20 AC2 ASP A  338  SER A  368  1                                  31    
HELIX   21 AC3 SER A  368  LEU A  384  1                                  17    
SHEET    1 AA1 2 MET A 191  VAL A 196  0                                        
SHEET    2 AA1 2 PHE A 207  GLU A 212 -1  O  VAL A 209   N  SER A 194           
SHEET    1 AA2 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA2 6 MET A1067  ILE A1072  1  N  ILE A1071   O  LYS A1094           
SHEET    3 AA2 6 VAL A1033  ILE A1038  1  N  PHE A1037   O  ILE A1070           
SHEET    4 AA2 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA2 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6 AA2 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  PRO A1138           
SSBOND   1 CYS A  127    CYS A  210                          1555   1555  2.04  
LINK         C   ASP A1003                 N   YCM A1004     1555   1555  1.43  
LINK         C   YCM A1004                 N   SER A1005     1555   1555  1.33  
SITE     1 AC1 14 THR A 111  PRO A 131  GLN A 134  THR A 135                    
SITE     2 AC1 14 VAL A 138  GLN A 187  CYS A 210  HIS A 224                    
SITE     3 AC1 14 PHE A 227  TYR A 317  ILE A 320  ASN A 324                    
SITE     4 AC1 14 HIS A 350  TYR A 354                                          
SITE     1 AC2  2 ASP A1180  LEU A1181                                          
SITE     1 AC3  5 ASP A 211  LYS A 327  ARG A 328  PHE A 333                    
SITE     2 AC3  5 PHE A 346                                                     
SITE     1 AC4  6 TRP A  44  PRO A 159  ARG A1147  ILE A1156                    
SITE     2 AC4  6 LEU A1157  LYS A1172                                          
SITE     1 AC5  2 VAL A  56  LEU A  57                                          
SITE     1 AC6  2 SER A 125  ILE A 189                                          
SITE     1 AC7  3 CYS A 147  SER A 172  VAL A 230                               
SITE     1 AC8  5 GLU A  46  TRP A 153  TYR A 154  HIS A 158                    
SITE     2 AC8  5 GLN A 245                                                     
CRYST1   90.945  173.950   78.327  90.00  90.00  90.00 C 2 2 21      8          
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      0.010996  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005749  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012767        0.00000                         
ATOM      1  N   THR A  32      70.598 246.480  20.778  1.00104.39           N  
ANISOU    1  N   THR A  32    11175  13461  15029   2499    209  -4779       N  
ATOM      2  CA  THR A  32      70.468 246.051  19.389  1.00 98.05           C  
ANISOU    2  CA  THR A  32    10391  12085  14778   2456    159  -4317       C  
ATOM      3  C   THR A  32      71.844 245.951  18.724  1.00 90.93           C  
ANISOU    3  C   THR A  32     9661  10881  14008   2484   -235  -3869       C  
ATOM      4  O   THR A  32      72.235 246.798  17.918  1.00 82.69           O  
ANISOU    4  O   THR A  32     8486   9406  13525   2538   -597  -3985       O  
ATOM      5  CB  THR A  32      69.546 247.007  18.591  1.00 98.36           C  
ANISOU    5  CB  THR A  32    10102  11685  15585   2498     78  -4750       C  
ATOM      6  OG1 THR A  32      69.644 246.723  17.188  1.00 82.82           O  
ANISOU    6  OG1 THR A  32     8153   9193  14123   2446    -71  -4295       O  
ATOM      7  CG2 THR A  32      69.896 248.476  18.861  1.00100.84           C  
ANISOU    7  CG2 THR A  32    10189  11888  16238   2630   -294  -5386       C  
ATOM      8  N   ASP A  33      72.569 244.891  19.068  1.00 90.29           N  
ANISOU    8  N   ASP A  33     9852  11029  13427   2436   -160  -3333       N  
ATOM      9  CA  ASP A  33      73.944 244.710  18.622  1.00 89.27           C  
ANISOU    9  CA  ASP A  33     9878  10693  13347   2467   -500  -2925       C  
ATOM     10  C   ASP A  33      73.992 243.919  17.319  1.00 86.71           C  
ANISOU   10  C   ASP A  33     9615   9927  13403   2396   -462  -2403       C  
ATOM     11  O   ASP A  33      73.251 242.948  17.136  1.00 87.53           O  
ANISOU   11  O   ASP A  33     9774  10040  13444   2303   -112  -2132       O  
ATOM     12  CB  ASP A  33      74.759 244.003  19.709  1.00 93.86           C  
ANISOU   12  CB  ASP A  33    10688  11750  13226   2464   -478  -2626       C  
ATOM     13  CG  ASP A  33      76.110 243.519  19.213  1.00 93.06           C  
ANISOU   13  CG  ASP A  33    10746  11424  13188   2487   -759  -2104       C  
ATOM     14  OD1 ASP A  33      76.393 242.309  19.338  1.00 93.51           O  
ANISOU   14  OD1 ASP A  33    10985  11570  12974   2433   -599  -1545       O  
ATOM     15  OD2 ASP A  33      76.882 244.347  18.686  1.00 92.45           O  
ANISOU   15  OD2 ASP A  33    10588  11064  13474   2555  -1139  -2248       O  
ATOM     16  N   TYR A  34      74.873 244.347  16.414  1.00 85.40           N  
ANISOU   16  N   TYR A  34     9422   9391  13636   2425   -821  -2284       N  
ATOM     17  CA  TYR A  34      75.015 243.731  15.101  1.00 85.44           C  
ANISOU   17  CA  TYR A  34     9451   9009  14003   2347   -820  -1864       C  
ATOM     18  C   TYR A  34      76.281 242.887  14.980  1.00 87.81           C  
ANISOU   18  C   TYR A  34     9944   9292  14126   2351   -922  -1364       C  
ATOM     19  O   TYR A  34      76.688 242.547  13.863  1.00 84.36           O  
ANISOU   19  O   TYR A  34     9501   8545  14008   2298   -996  -1083       O  
ATOM     20  CB  TYR A  34      74.993 244.799  14.005  1.00 83.31           C  
ANISOU   20  CB  TYR A  34     8965   8341  14346   2342  -1125  -2058       C  
ATOM     21  CG  TYR A  34      73.759 245.671  14.008  1.00 84.99           C  
ANISOU   21  CG  TYR A  34     8940   8486  14868   2349  -1072  -2535       C  
ATOM     22  CD1 TYR A  34      72.505 245.136  13.747  1.00 83.72           C  
ANISOU   22  CD1 TYR A  34     8723   8313  14776   2271   -726  -2532       C  
ATOM     23  CD2 TYR A  34      73.853 247.035  14.253  1.00 87.79           C  
ANISOU   23  CD2 TYR A  34     9095   8754  15506   2436  -1380  -2999       C  
ATOM     24  CE1 TYR A  34      71.376 245.933  13.742  1.00 85.56           C  
ANISOU   24  CE1 TYR A  34     8703   8467  15338   2286   -686  -2973       C  
ATOM     25  CE2 TYR A  34      72.732 247.839  14.249  1.00 89.11           C  
ANISOU   25  CE2 TYR A  34     9005   8815  16040   2457  -1346  -3452       C  
ATOM     26  CZ  TYR A  34      71.497 247.286  13.993  1.00 87.89           C  
ANISOU   26  CZ  TYR A  34     8794   8665  15937   2386   -997  -3434       C  
ATOM     27  OH  TYR A  34      70.383 248.093  13.990  1.00 89.90           O  
ANISOU   27  OH  TYR A  34     8828   8904  16427   2294   -963  -3767       O  
ATOM     28  N   ASP A  35      76.921 242.548  16.103  1.00 93.17           N  
ANISOU   28  N   ASP A  35    10774  10319  14307   2406   -934  -1255       N  
ATOM     29  CA  ASP A  35      78.076 241.657  16.039  1.00 93.83           C  
ANISOU   29  CA  ASP A  35    11017  10372  14262   2418  -1022   -753       C  
ATOM     30  C   ASP A  35      77.661 240.234  15.685  1.00 95.34           C  
ANISOU   30  C   ASP A  35    11306  10467  14453   2331   -675   -307       C  
ATOM     31  O   ASP A  35      78.463 239.474  15.128  1.00 93.12           O  
ANISOU   31  O   ASP A  35    11085   9978  14317   2326   -727     81       O  
ATOM     32  CB  ASP A  35      78.836 241.661  17.369  1.00 96.62           C  
ANISOU   32  CB  ASP A  35    11488  11145  14079   2491  -1155   -720       C  
ATOM     33  CG  ASP A  35      79.500 242.995  17.663  1.00 96.10           C  
ANISOU   33  CG  ASP A  35    11321  11131  14061   2578  -1551  -1143       C  
ATOM     34  OD1 ASP A  35      79.208 243.982  16.956  1.00 93.34           O  
ANISOU   34  OD1 ASP A  35    10796  10502  14166   2583  -1696  -1488       O  
ATOM     35  OD2 ASP A  35      80.320 243.055  18.605  1.00 98.58           O  
ANISOU   35  OD2 ASP A  35    11716  11760  13980   2634  -1736  -1116       O  
ATOM     36  N   ASP A  36      76.416 239.862  15.989  1.00100.78           N  
ANISOU   36  N   ASP A  36    11982  11287  15022   2259   -319   -378       N  
ATOM     37  CA  ASP A  36      75.972 238.491  15.763  1.00101.25           C  
ANISOU   37  CA  ASP A  36    12119  11254  15096   2165     17     39       C  
ATOM     38  C   ASP A  36      75.791 238.196  14.279  1.00 98.60           C  
ANISOU   38  C   ASP A  36    11695  10471  15297   2095     50    108       C  
ATOM     39  O   ASP A  36      76.074 237.081  13.824  1.00 98.10           O  
ANISOU   39  O   ASP A  36    11690  10216  15368   2048    173    484       O  
ATOM     40  CB  ASP A  36      74.669 238.240  16.524  1.00102.94           C  
ANISOU   40  CB  ASP A  36    12318  11757  15037   2090    390    -72       C  
ATOM     41  CG  ASP A  36      73.682 239.380  16.373  1.00101.48           C  
ANISOU   41  CG  ASP A  36    11948  11588  15020   2094    407   -649       C  
ATOM     42  OD1 ASP A  36      73.180 239.591  15.249  1.00 98.03           O  
ANISOU   42  OD1 ASP A  36    11383  10801  15061   2051    405   -763       O  
ATOM     43  OD2 ASP A  36      73.412 240.071  17.378  1.00104.69           O  
ANISOU   43  OD2 ASP A  36    12318  12367  15093   2136    412   -998       O  
ATOM     44  N   GLU A  37      75.328 239.180  13.508  1.00 94.43           N  
ANISOU   44  N   GLU A  37    11006   9778  15094   2080    -72   -254       N  
ATOM     45  CA  GLU A  37      74.981 238.982  12.104  1.00 90.60           C  
ANISOU   45  CA  GLU A  37    10413   8953  15058   1981    -35   -220       C  
ATOM     46  C   GLU A  37      76.168 239.356  11.218  1.00 86.39           C  
ANISOU   46  C   GLU A  37     9846   8215  14763   2000   -370   -137       C  
ATOM     47  O   GLU A  37      76.525 240.533  11.102  1.00 85.85           O  
ANISOU   47  O   GLU A  37     9684   8130  14806   2047   -680   -368       O  
ATOM     48  CB  GLU A  37      73.732 239.783  11.730  1.00 92.45           C  
ANISOU   48  CB  GLU A  37    10466   9137  15525   1929     18   -595       C  
ATOM     49  CG  GLU A  37      73.746 241.255  12.125  1.00 96.30           C  
ANISOU   49  CG  GLU A  37    10833   9702  16053   2021   -261  -1007       C  
ATOM     50  CD  GLU A  37      72.458 241.964  11.749  1.00 99.17           C  
ANISOU   50  CD  GLU A  37    10982   9972  16728   1977   -203  -1355       C  
ATOM     51  OE1 GLU A  37      71.375 241.385  11.977  1.00101.44           O  
ANISOU   51  OE1 GLU A  37    11248  10344  16949   1917    143  -1385       O  
ATOM     52  OE2 GLU A  37      72.525 243.093  11.219  1.00 99.47           O  
ANISOU   52  OE2 GLU A  37    10849   9834  17111   1998   -512  -1578       O  
ATOM     53  N   GLU A  38      76.783 238.344  10.609  1.00 83.16           N  
ANISOU   53  N   GLU A  38     9489   7649  14458   1958   -302    184       N  
ATOM     54  CA  GLU A  38      77.740 238.540   9.529  1.00 77.60           C  
ANISOU   54  CA  GLU A  38     8751   6865  13869   1865   -517    245       C  
ATOM     55  C   GLU A  38      77.098 238.386   8.160  1.00 70.85           C  
ANISOU   55  C   GLU A  38     7819   6014  13087   1600   -399    180       C  
ATOM     56  O   GLU A  38      77.586 238.966   7.184  1.00 69.78           O  
ANISOU   56  O   GLU A  38     7618   5960  12934   1440   -576    137       O  
ATOM     57  CB  GLU A  38      78.899 237.542   9.660  1.00 80.78           C  
ANISOU   57  CB  GLU A  38     9262   7250  14181   1902   -507    564       C  
ATOM     58  CG  GLU A  38      80.030 237.744   8.662  1.00 82.09           C  
ANISOU   58  CG  GLU A  38     9414   7509  14269   1744   -674    572       C  
ATOM     59  CD  GLU A  38      80.880 238.951   8.986  1.00 86.41           C  
ANISOU   59  CD  GLU A  38     9943   8159  14731   1803  -1002    472       C  
ATOM     60  OE1 GLU A  38      81.059 239.245  10.188  1.00 90.24           O  
ANISOU   60  OE1 GLU A  38    10467   8651  15171   2021  -1143    475       O  
ATOM     61  OE2 GLU A  38      81.367 239.606   8.040  1.00 86.41           O  
ANISOU   61  OE2 GLU A  38     9864   8230  14737   1628  -1132    395       O  
ATOM     62  N   PHE A  39      75.999 237.631   8.081  1.00 64.68           N  
ANISOU   62  N   PHE A  39     7014   5147  12416   1555   -105    185       N  
ATOM     63  CA  PHE A  39      75.333 237.384   6.807  1.00 58.32           C  
ANISOU   63  CA  PHE A  39     6107   4349  11704   1318     -9    123       C  
ATOM     64  C   PHE A  39      74.677 238.650   6.266  1.00 54.13           C  
ANISOU   64  C   PHE A  39     5435   3886  11244   1218   -193    -98       C  
ATOM     65  O   PHE A  39      74.664 238.873   5.049  1.00 51.28           O  
ANISOU   65  O   PHE A  39     4962   3573  10947   1026   -287   -107       O  
ATOM     66  CB  PHE A  39      74.306 236.261   6.979  1.00 58.41           C  
ANISOU   66  CB  PHE A  39     6116   4242  11836   1294    351    179       C  
ATOM     67  CG  PHE A  39      73.576 235.895   5.718  1.00 55.01           C  
ANISOU   67  CG  PHE A  39     5557   3815  11529   1064    451     99       C  
ATOM     68  CD1 PHE A  39      74.254 235.357   4.636  1.00 51.84           C  
ANISOU   68  CD1 PHE A  39     5112   3444  11140    927    420    153       C  
ATOM     69  CD2 PHE A  39      72.205 236.068   5.623  1.00 55.48           C  
ANISOU   69  CD2 PHE A  39     5509   3846  11724    999    586    -51       C  
ATOM     70  CE1 PHE A  39      73.581 235.015   3.478  1.00 51.25           C  
ANISOU   70  CE1 PHE A  39     4887   3372  11215    739    509     57       C  
ATOM     71  CE2 PHE A  39      71.528 235.727   4.469  1.00 54.71           C  
ANISOU   71  CE2 PHE A  39     5273   3753  11764    797    656   -118       C  
ATOM     72  CZ  PHE A  39      72.216 235.200   3.396  1.00 52.83           C  
ANISOU   72  CZ  PHE A  39     4989   3545  11539    673    615    -66       C  
ATOM     73  N   LEU A  40      74.129 239.491   7.152  1.00 54.08           N  
ANISOU   73  N   LEU A  40     5400   3877  11271   1351   -252   -282       N  
ATOM     74  CA  LEU A  40      73.515 240.738   6.702  1.00 51.41           C  
ANISOU   74  CA  LEU A  40     4905   3579  11050   1251   -452   -487       C  
ATOM     75  C   LEU A  40      74.553 241.685   6.117  1.00 49.81           C  
ANISOU   75  C   LEU A  40     4666   3441  10817   1161   -791   -445       C  
ATOM     76  O   LEU A  40      74.276 242.394   5.143  1.00 48.91           O  
ANISOU   76  O   LEU A  40     4402   3342  10840    980   -955   -466       O  
ATOM     77  CB  LEU A  40      72.768 241.415   7.854  1.00 53.39           C  
ANISOU   77  CB  LEU A  40     5104   3816  11367   1427   -429   -763       C  
ATOM     78  CG  LEU A  40      71.302 241.025   8.056  1.00 54.64           C  
ANISOU   78  CG  LEU A  40     5169   3933  11659   1423   -130   -908       C  
ATOM     79  CD1 LEU A  40      71.179 239.730   8.850  1.00 56.91           C  
ANISOU   79  CD1 LEU A  40     5560   4162  11901   1560    244   -787       C  
ATOM     80  CD2 LEU A  40      70.534 242.156   8.724  1.00 56.79           C  
ANISOU   80  CD2 LEU A  40     5292   4240  12047   1511   -207  -1274       C  
ATOM     81  N   ARG A  41      75.753 241.714   6.701  1.00 50.10           N  
ANISOU   81  N   ARG A  41     4818   3508  10709   1280   -904   -367       N  
ATOM     82  CA  ARG A  41      76.824 242.520   6.132  1.00 52.84           C  
ANISOU   82  CA  ARG A  41     5124   3912  11041   1173  -1189   -311       C  
ATOM     83  C   ARG A  41      77.286 241.964   4.792  1.00 50.05           C  
ANISOU   83  C   ARG A  41     4727   3597  10694    977  -1156   -130       C  
ATOM     84  O   ARG A  41      77.773 242.721   3.945  1.00 46.41           O  
ANISOU   84  O   ARG A  41     4154   3167  10312    820  -1369    -94       O  
ATOM     85  CB  ARG A  41      77.999 242.603   7.104  1.00 56.09           C  
ANISOU   85  CB  ARG A  41     5654   4349  11308   1348  -1308   -277       C  
ATOM     86  CG  ARG A  41      77.626 243.071   8.500  1.00 61.99           C  
ANISOU   86  CG  ARG A  41     6417   5071  12067   1586  -1356   -500       C  
ATOM     87  CD  ARG A  41      78.869 243.230   9.353  1.00 67.14           C  
ANISOU   87  CD  ARG A  41     7151   5764  12597   1750  -1549   -466       C  
ATOM     88  NE  ARG A  41      78.609 242.992  10.768  1.00 73.97           N  
ANISOU   88  NE  ARG A  41     8056   6628  13423   2054  -1519   -607       N  
ATOM     89  CZ  ARG A  41      79.562 242.892  11.689  1.00 79.41           C  
ANISOU   89  CZ  ARG A  41     8811   7369  13990   2262  -1697   -559       C  
ATOM     90  NH1 ARG A  41      79.241 242.672  12.956  1.00 84.03           N  
ANISOU   90  NH1 ARG A  41     9502   8229  14196   2348  -1564   -660       N  
ATOM     91  NH2 ARG A  41      80.836 243.008  11.341  1.00 79.13           N  
ANISOU   91  NH2 ARG A  41     8822   7378  13868   2167  -1874   -372       N  
ATOM     92  N   TYR A  42      77.148 240.651   4.583  1.00 48.73           N  
ANISOU   92  N   TYR A  42     4621   3410  10485    983   -893    -29       N  
ATOM     93  CA  TYR A  42      77.488 240.077   3.285  1.00 46.87           C  
ANISOU   93  CA  TYR A  42     4296   3200  10312    812   -847     70       C  
ATOM     94  C   TYR A  42      76.435 240.412   2.237  1.00 48.47           C  
ANISOU   94  C   TYR A  42     4311   3392  10712    637   -871      7       C  
ATOM     95  O   TYR A  42      76.765 240.562   1.054  1.00 48.11           O  
ANISOU   95  O   TYR A  42     4121   3374  10784    479   -980     69       O  
ATOM     96  CB  TYR A  42      77.670 238.563   3.404  1.00 48.85           C  
ANISOU   96  CB  TYR A  42     4641   3402  10517    867   -566    160       C  
ATOM     97  CG  TYR A  42      77.617 237.839   2.077  1.00 50.55           C  
ANISOU   97  CG  TYR A  42     4718   3612  10878    700   -453    169       C  
ATOM     98  CD1 TYR A  42      78.640 237.975   1.146  1.00 51.47           C  
ANISOU   98  CD1 TYR A  42     4728   3778  11051    607   -579    216       C  
ATOM     99  CD2 TYR A  42      76.539 237.026   1.751  1.00 51.35           C  
ANISOU   99  CD2 TYR A  42     4768   3647  11097    638   -214    110       C  
ATOM    100  CE1 TYR A  42      78.590 237.319  -0.071  1.00 52.60           C  
ANISOU  100  CE1 TYR A  42     4707   3896  11383    476   -470    184       C  
ATOM    101  CE2 TYR A  42      76.481 236.366   0.538  1.00 51.48           C  
ANISOU  101  CE2 TYR A  42     4631   3647  11284    496   -110     69       C  
ATOM    102  CZ  TYR A  42      77.509 236.516  -0.369  1.00 53.78           C  
ANISOU  102  CZ  TYR A  42     4808   3979  11646    424   -236     95       C  
ATOM    103  OH  TYR A  42      77.454 235.861  -1.577  1.00 57.00           O  
ANISOU  103  OH  TYR A  42     5034   4350  12274    299   -118      9       O  
ATOM    104  N   LEU A  43      75.170 240.536   2.650  1.00 51.68           N  
ANISOU  104  N   LEU A  43     4695   3750  11191    667   -779   -110       N  
ATOM    105  CA  LEU A  43      74.120 240.993   1.743  1.00 52.21           C  
ANISOU  105  CA  LEU A  43     4560   3798  11477    511   -848   -168       C  
ATOM    106  C   LEU A  43      74.329 242.444   1.324  1.00 51.81           C  
ANISOU  106  C   LEU A  43     4377   3757  11551    409  -1203   -165       C  
ATOM    107  O   LEU A  43      74.027 242.806   0.181  1.00 50.74           O  
ANISOU  107  O   LEU A  43     4059   3605  11616    230  -1350    -99       O  
ATOM    108  CB  LEU A  43      72.754 240.815   2.402  1.00 54.75           C  
ANISOU  108  CB  LEU A  43     4879   4060  11865    576   -660   -311       C  
ATOM    109  CG  LEU A  43      72.250 239.382   2.581  1.00 57.22           C  
ANISOU  109  CG  LEU A  43     5268   4324  12149    603   -298   -298       C  
ATOM    110  CD1 LEU A  43      71.178 239.326   3.656  1.00 59.58           C  
ANISOU  110  CD1 LEU A  43     5602   4561  12475    718   -109   -429       C  
ATOM    111  CD2 LEU A  43      71.713 238.838   1.263  1.00 57.80           C  
ANISOU  111  CD2 LEU A  43     5171   4390  12402    420   -228   -290       C  
ATOM    112  N   TRP A  44      74.849 243.280   2.228  1.00 67.35           N  
ANISOU  112  N   TRP A  44     7288   6247  12057    796    504    367       N  
ATOM    113  CA  TRP A  44      75.173 244.670   1.922  1.00 67.72           C  
ANISOU  113  CA  TRP A  44     7435   6256  12039    825    430    392       C  
ATOM    114  C   TRP A  44      76.382 244.811   1.007  1.00 68.17           C  
ANISOU  114  C   TRP A  44     7824   6224  11855    724    582    366       C  
ATOM    115  O   TRP A  44      76.629 245.914   0.507  1.00 69.12           O  
ANISOU  115  O   TRP A  44     8150   6229  11886    705    581    381       O  
ATOM    116  CB  TRP A  44      75.418 245.448   3.216  1.00 67.89           C  
ANISOU  116  CB  TRP A  44     7188   6395  12213    963    553    373       C  
ATOM    117  CG  TRP A  44      74.168 245.974   3.837  1.00 71.38           C  
ANISOU  117  CG  TRP A  44     7383   6861  12877   1048    371    408       C  
ATOM    118  CD1 TRP A  44      73.005 245.295   4.029  1.00 72.66           C  
ANISOU  118  CD1 TRP A  44     7374   7018  13215   1031    269    387       C  
ATOM    119  CD2 TRP A  44      73.956 247.292   4.363  1.00 73.70           C  
ANISOU  119  CD2 TRP A  44     7551   7178  13274   1149    303    427       C  
ATOM    120  NE1 TRP A  44      72.075 246.106   4.634  1.00 73.46           N  
ANISOU  120  NE1 TRP A  44     7231   7149  13533   1118    132    378       N  
ATOM    121  CE2 TRP A  44      72.635 247.338   4.851  1.00 73.02           C  
ANISOU  121  CE2 TRP A  44     7213   7115  13416   1205    132    425       C  
ATOM    122  CE3 TRP A  44      74.755 248.436   4.466  1.00 74.24           C  
ANISOU  122  CE3 TRP A  44     7684   7237  13288   1180    400    413       C  
ATOM    123  CZ2 TRP A  44      72.095 248.481   5.432  1.00 72.59           C  
ANISOU  123  CZ2 TRP A  44     6984   7089  13509   1317     19    439       C  
ATOM    124  CZ3 TRP A  44      74.214 249.572   5.045  1.00 73.54           C  
ANISOU  124  CZ3 TRP A  44     7441   7163  13337   1284    299    439       C  
ATOM    125  CH2 TRP A  44      72.898 249.584   5.522  1.00 72.77           C  
ANISOU  125  CH2 TRP A  44     7107   7104  13438   1365     92    466       C  
ATOM    126  N   ARG A  45      77.141 243.735   0.789  1.00 63.61           N  
ANISOU  126  N   ARG A  45     7327   5670  11170    657    751    313       N  
ATOM    127  CA  ARG A  45      78.254 243.740  -0.147  1.00 62.61           C  
ANISOU  127  CA  ARG A  45     7505   5446  10840    531    928    252       C  
ATOM    128  C   ARG A  45      78.060 242.802  -1.329  1.00 63.81           C  
ANISOU  128  C   ARG A  45     7958   5482  10806    416    834    298       C  
ATOM    129  O   ARG A  45      78.875 242.838  -2.259  1.00 65.61           O  
ANISOU  129  O   ARG A  45     8505   5583  10839    299    982    262       O  
ATOM    130  CB  ARG A  45      79.561 243.354   0.565  1.00 62.35           C  
ANISOU  130  CB  ARG A  45     7300   5555  10835    576   1218     71       C  
ATOM    131  CG  ARG A  45      79.848 244.139   1.833  1.00 62.26           C  
ANISOU  131  CG  ARG A  45     6960   5689  11008    738   1294    -35       C  
ATOM    132  CD  ARG A  45      81.110 243.632   2.523  1.00 61.46           C  
ANISOU  132  CD  ARG A  45     6681   5751  10921    867   1498   -293       C  
ATOM    133  NE  ARG A  45      80.931 242.323   3.150  1.00 60.62           N  
ANISOU  133  NE  ARG A  45     6534   5742  10759   1044   1462   -265       N  
ATOM    134  CZ  ARG A  45      81.318 241.170   2.611  1.00 62.15           C  
ANISOU  134  CZ  ARG A  45     6903   5911  10798   1002   1520   -289       C  
ATOM    135  NH1 ARG A  45      81.909 241.153   1.424  1.00 63.24           N  
ANISOU  135  NH1 ARG A  45     7245   5950  10835    783   1604   -344       N  
ATOM    136  NH2 ARG A  45      81.117 240.032   3.263  1.00 62.76           N  
ANISOU  136  NH2 ARG A  45     7002   6035  10809   1184   1528   -257       N  
ATOM    137  N   GLU A  46      77.004 241.981  -1.326  1.00 64.52           N  
ANISOU  137  N   GLU A  46     7952   5596  10968    434    622    343       N  
ATOM    138  CA  GLU A  46      76.845 240.909  -2.306  1.00 66.55           C  
ANISOU  138  CA  GLU A  46     8428   5773  11086    332    543    341       C  
ATOM    139  C   GLU A  46      76.825 241.421  -3.739  1.00 67.55           C  
ANISOU  139  C   GLU A  46     9005   5703  10959    287    387    376       C  
ATOM    140  O   GLU A  46      77.166 240.679  -4.668  1.00 68.28           O  
ANISOU  140  O   GLU A  46     9376   5708  10860    197    409    366       O  
ATOM    141  CB  GLU A  46      75.557 240.140  -2.009  1.00 70.01           C  
ANISOU  141  CB  GLU A  46     8629   6248  11723    343    355    315       C  
ATOM    142  CG  GLU A  46      75.459 238.767  -2.647  1.00 75.60           C  
ANISOU  142  CG  GLU A  46     9451   6909  12364    230    362    268       C  
ATOM    143  CD  GLU A  46      74.218 238.024  -2.192  1.00 81.55           C  
ANISOU  143  CD  GLU A  46     9913   7677  13395    198    286    172       C  
ATOM    144  OE1 GLU A  46      73.277 238.690  -1.712  1.00 83.68           O  
ANISOU  144  OE1 GLU A  46     9925   7977  13892    262    129    124       O  
ATOM    145  OE2 GLU A  46      74.184 236.780  -2.302  1.00 83.36           O  
ANISOU  145  OE2 GLU A  46    10169   7871  13635     97    418    119       O  
ATOM    146  N   TYR A  47      76.426 242.677  -3.942  1.00 69.26           N  
ANISOU  146  N   TYR A  47     9356   5824  11138    378    235    419       N  
ATOM    147  CA  TYR A  47      76.321 243.219  -5.290  1.00 73.33           C  
ANISOU  147  CA  TYR A  47    10423   6096  11343    414     79    461       C  
ATOM    148  C   TYR A  47      77.681 243.471  -5.926  1.00 76.30           C  
ANISOU  148  C   TYR A  47    11214   6299  11479    273    475    469       C  
ATOM    149  O   TYR A  47      77.769 243.558  -7.155  1.00 79.41           O  
ANISOU  149  O   TYR A  47    12165   6452  11556    275    438    507       O  
ATOM    150  CB  TYR A  47      75.508 244.516  -5.267  1.00 75.00           C  
ANISOU  150  CB  TYR A  47    10725   6223  11548    603   -181    498       C  
ATOM    151  CG  TYR A  47      76.183 245.664  -4.541  1.00 74.72           C  
ANISOU  151  CG  TYR A  47    10634   6172  11584    584    118    532       C  
ATOM    152  CD1 TYR A  47      76.117 245.777  -3.157  1.00 73.11           C  
ANISOU  152  CD1 TYR A  47     9877   6196  11706    596    198    501       C  
ATOM    153  CD2 TYR A  47      76.877 246.640  -5.244  1.00 76.80           C  
ANISOU  153  CD2 TYR A  47    11432   6162  11586    555    352    573       C  
ATOM    154  CE1 TYR A  47      76.732 246.827  -2.494  1.00 72.45           C  
ANISOU  154  CE1 TYR A  47     9715   6110  11705    589    449    490       C  
ATOM    155  CE2 TYR A  47      77.494 247.692  -4.589  1.00 77.09           C  
ANISOU  155  CE2 TYR A  47    11392   6168  11731    507    663    552       C  
ATOM    156  CZ  TYR A  47      77.418 247.780  -3.215  1.00 74.55           C  
ANISOU  156  CZ  TYR A  47    10457   6116  11754    530    682    500       C  
ATOM    157  OH  TYR A  47      78.029 248.826  -2.560  1.00 74.69           O  
ANISOU  157  OH  TYR A  47    10369   6115  11895    493    968    438       O  
ATOM    158  N   LEU A  48      78.743 243.585  -5.125  1.00 76.20           N  
ANISOU  158  N   LEU A  48    10948   6391  11613    167    859    392       N  
ATOM    159  CA  LEU A  48      80.034 243.985  -5.674  1.00 77.13           C  
ANISOU  159  CA  LEU A  48    11388   6332  11586      6   1289    309       C  
ATOM    160  C   LEU A  48      80.728 242.835  -6.393  1.00 79.79           C  
ANISOU  160  C   LEU A  48    11895   6643  11779   -129   1438    251       C  
ATOM    161  O   LEU A  48      81.481 243.070  -7.346  1.00 82.78           O  
ANISOU  161  O   LEU A  48    12733   6777  11943   -265   1724    212       O  
ATOM    162  CB  LEU A  48      80.930 244.542  -4.563  1.00 73.60           C  
ANISOU  162  CB  LEU A  48    10537   6030  11398    -37   1615    142       C  
ATOM    163  CG  LEU A  48      80.629 245.970  -4.094  1.00 73.30           C  
ANISOU  163  CG  LEU A  48    10477   5921  11454     31   1627    168       C  
ATOM    164  CD1 LEU A  48      80.874 246.112  -2.600  1.00 71.51           C  
ANISOU  164  CD1 LEU A  48     9634   5982  11554    113   1678     35       C  
ATOM    165  CD2 LEU A  48      81.467 246.976  -4.869  1.00 74.80           C  
ANISOU  165  CD2 LEU A  48    11144   5780  11495   -133   2050     89       C  
ATOM    166  N   HIS A  49      80.491 241.597  -5.963  1.00 80.18           N  
ANISOU  166  N   HIS A  49    11623   6908  11934   -100   1292    238       N  
ATOM    167  CA  HIS A  49      81.176 240.425  -6.514  1.00 80.99           C  
ANISOU  167  CA  HIS A  49    11840   7014  11919   -211   1433    173       C  
ATOM    168  C   HIS A  49      80.185 239.284  -6.722  1.00 81.20           C  
ANISOU  168  C   HIS A  49    11822   7105  11927   -159   1100    258       C  
ATOM    169  O   HIS A  49      80.206 238.279  -6.001  1.00 78.31           O  
ANISOU  169  O   HIS A  49    11141   6917  11698   -136   1122    215       O  
ATOM    170  CB  HIS A  49      82.323 239.996  -5.595  1.00 79.20           C  
ANISOU  170  CB  HIS A  49    11236   6990  11865   -227   1735    -30       C  
ATOM    171  CG  HIS A  49      83.426 241.006  -5.483  1.00 80.10           C  
ANISOU  171  CG  HIS A  49    11337   7043  12053   -319   2107   -230       C  
ATOM    172  ND1 HIS A  49      84.580 240.928  -6.232  1.00 81.64           N  
ANISOU  172  ND1 HIS A  49    11755   7104  12162   -503   2476   -419       N  
ATOM    173  CD2 HIS A  49      83.557 242.108  -4.705  1.00 80.17           C  
ANISOU  173  CD2 HIS A  49    11114   7097  12251   -274   2203   -317       C  
ATOM    174  CE1 HIS A  49      85.371 241.940  -5.923  1.00 82.74           C  
ANISOU  174  CE1 HIS A  49    11779   7197  12460   -587   2809   -645       C  
ATOM    175  NE2 HIS A  49      84.774 242.671  -5.000  1.00 81.86           N  
ANISOU  175  NE2 HIS A  49    11395   7197  12510   -445   2639   -582       N  
ATOM    176  N   PRO A  50      79.298 239.407  -7.708  1.00 83.89           N  
ANISOU  176  N   PRO A  50    12498   7283  12093   -116    795    343       N  
ATOM    177  CA  PRO A  50      78.423 238.286  -8.059  1.00 85.46           C  
ANISOU  177  CA  PRO A  50    12645   7526  12301    -98    501    337       C  
ATOM    178  C   PRO A  50      79.176 237.272  -8.903  1.00 87.52           C  
ANISOU  178  C   PRO A  50    13185   7714  12356   -226    661    310       C  
ATOM    179  O   PRO A  50      80.165 237.585  -9.567  1.00 88.75           O  
ANISOU  179  O   PRO A  50    13703   7718  12299   -314    926    307       O  
ATOM    180  CB  PRO A  50      77.295 238.935  -8.874  1.00 88.33           C  
ANISOU  180  CB  PRO A  50    13281   7744  12534     57     72    359       C  
ATOM    181  CG  PRO A  50      77.578 240.421  -8.870  1.00 88.83           C  
ANISOU  181  CG  PRO A  50    13589   7669  12491    133    170    429       C  
ATOM    182  CD  PRO A  50      79.032 240.578  -8.554  1.00 86.96           C  
ANISOU  182  CD  PRO A  50    13365   7423  12254    -43    694    413       C  
ATOM    183  N   LYS A  51      78.691 236.033  -8.867  1.00 88.38           N  
ANISOU  183  N   LYS A  51    13122   7909  12548   -255    538    270       N  
ATOM    184  CA  LYS A  51      79.350 234.962  -9.604  1.00 89.74           C  
ANISOU  184  CA  LYS A  51    13530   8027  12540   -370    676    243       C  
ATOM    185  C   LYS A  51      78.342 234.243 -10.489  1.00 95.45           C  
ANISOU  185  C   LYS A  51    14391   8679  13196   -356    323    202       C  
ATOM    186  O   LYS A  51      78.481 234.202 -11.716  1.00 97.14           O  
ANISOU  186  O   LYS A  51    15068   8723  13118   -355    224    209       O  
ATOM    187  CB  LYS A  51      80.006 233.969  -8.642  1.00 85.35           C  
ANISOU  187  CB  LYS A  51    12661   7639  12130   -412    954    192       C  
ATOM    188  CG  LYS A  51      80.645 234.610  -7.424  1.00 82.80           C  
ANISOU  188  CG  LYS A  51    12039   7455  11965   -333   1178    159       C  
ATOM    189  CD  LYS A  51      82.040 234.072  -7.176  1.00 82.91           C  
ANISOU  189  CD  LYS A  51    12037   7546  11919   -345   1505     38       C  
ATOM    190  CE  LYS A  51      82.603 234.608  -5.874  1.00 82.40           C  
ANISOU  190  CE  LYS A  51    11627   7650  12030   -199   1659    -66       C  
ATOM    191  NZ  LYS A  51      84.064 234.363  -5.738  1.00 83.09           N  
ANISOU  191  NZ  LYS A  51    11674   7820  12076   -173   1938   -291       N  
ATOM    192  N   GLU A  52      77.329 233.667  -9.847  1.00100.62           N  
ANISOU  192  N   GLU A  52    14647   9448  14135   -343    157    122       N  
ATOM    193  CA  GLU A  52      76.253 232.917 -10.481  1.00105.59           C  
ANISOU  193  CA  GLU A  52    15244  10046  14829   -346   -169    -23       C  
ATOM    194  C   GLU A  52      76.758 231.679 -11.218  1.00107.13           C  
ANISOU  194  C   GLU A  52    15666  10180  14857   -471    -56    -50       C  
ATOM    195  O   GLU A  52      75.972 230.974 -11.860  1.00108.49           O  
ANISOU  195  O   GLU A  52    15835  10316  15071   -489   -310   -206       O  
ATOM    196  CB  GLU A  52      75.438 233.813 -11.413  1.00110.97           C  
ANISOU  196  CB  GLU A  52    16172  10623  15369   -158   -633    -90       C  
ATOM    197  CG  GLU A  52      73.967 233.430 -11.465  1.00115.40           C  
ANISOU  197  CG  GLU A  52    16391  11244  16213    -93  -1041   -357       C  
ATOM    198  CD  GLU A  52      73.403 233.093 -10.091  1.00115.85           C  
ANISOU  198  CD  GLU A  52    15841  11445  16734   -206   -855   -437       C  
ATOM    199  OE1 GLU A  52      73.353 231.894  -9.738  1.00116.00           O  
ANISOU  199  OE1 GLU A  52    15656  11483  16934   -386   -619   -517       O  
ATOM    200  OE2 GLU A  52      73.002 234.029  -9.366  1.00116.14           O  
ANISOU  200  OE2 GLU A  52    15649  11545  16935   -109   -914   -419       O  
ATOM    201  N   TYR A  53      78.057 231.400 -11.140  1.00100.47           N  
ANISOU  201  N   TYR A  53    14991   9334  13849   -551    313     54       N  
ATOM    202  CA  TYR A  53      78.498 230.019 -11.254  1.00 96.77           C  
ANISOU  202  CA  TYR A  53    14554   8871  13345   -671    507     20       C  
ATOM    203  C   TYR A  53      78.430 229.320  -9.906  1.00 91.63           C  
ANISOU  203  C   TYR A  53    13529   8334  12953   -686    755      4       C  
ATOM    204  O   TYR A  53      78.964 228.216  -9.749  1.00 90.89           O  
ANISOU  204  O   TYR A  53    13489   8239  12808   -739    991     -7       O  
ATOM    205  CB  TYR A  53      79.911 229.930 -11.856  1.00 98.46           C  
ANISOU  205  CB  TYR A  53    15126   9022  13261   -725    775     79       C  
ATOM    206  CG  TYR A  53      81.061 230.375 -10.969  1.00 99.34           C  
ANISOU  206  CG  TYR A  53    15103   9234  13407   -700   1123     98       C  
ATOM    207  CD1 TYR A  53      81.711 229.472 -10.135  1.00 98.50           C  
ANISOU  207  CD1 TYR A  53    14811   9246  13370   -678   1376     49       C  
ATOM    208  CD2 TYR A  53      81.523 231.686 -10.997  1.00100.92           C  
ANISOU  208  CD2 TYR A  53    15392   9394  13559   -672   1200    122       C  
ATOM    209  CE1 TYR A  53      82.765 229.867  -9.334  1.00 97.48           C  
ANISOU  209  CE1 TYR A  53    14530   9231  13275   -590   1627    -17       C  
ATOM    210  CE2 TYR A  53      82.582 232.090 -10.197  1.00 99.66           C  
ANISOU  210  CE2 TYR A  53    15046   9339  13481   -651   1509     51       C  
ATOM    211  CZ  TYR A  53      83.198 231.174  -9.368  1.00 97.79           C  
ANISOU  211  CZ  TYR A  53    14573   9258  13326   -592   1688    -40       C  
ATOM    212  OH  TYR A  53      84.249 231.559  -8.568  1.00 96.43           O  
ANISOU  212  OH  TYR A  53    14186   9214  13238   -507   1929   -190       O  
ATOM    213  N   ALA A  54      77.764 229.958  -8.936  1.00 59.82           N  
ANISOU  213  N   ALA A  54     8672   4866   9191   1515   -847    712       N  
ATOM    214  CA  ALA A  54      77.603 229.377  -7.610  1.00 54.76           C  
ANISOU  214  CA  ALA A  54     7820   4348   8638   1339   -897    520       C  
ATOM    215  C   ALA A  54      76.741 228.126  -7.647  1.00 51.75           C  
ANISOU  215  C   ALA A  54     7325   4099   8240   1346  -1090    348       C  
ATOM    216  O   ALA A  54      76.957 227.204  -6.854  1.00 50.36           O  
ANISOU  216  O   ALA A  54     6997   4009   8129   1199  -1073    249       O  
ATOM    217  CB  ALA A  54      76.997 230.406  -6.655  1.00 53.17           C  
ANISOU  217  CB  ALA A  54     7519   4154   8530   1308   -962    447       C  
ATOM    218  N   TRP A  55      75.762 228.068  -8.553  1.00 51.08           N  
ANISOU  218  N   TRP A  55     7309   4033   8065   1523  -1283    299       N  
ATOM    219  CA  TRP A  55      74.893 226.897  -8.587  1.00 50.67           C  
ANISOU  219  CA  TRP A  55     7142   4095   8015   1535  -1480     93       C  
ATOM    220  C   TRP A  55      75.624 225.687  -9.152  1.00 49.61           C  
ANISOU  220  C   TRP A  55     7049   3966   7835   1518  -1430     99       C  
ATOM    221  O   TRP A  55      75.383 224.554  -8.720  1.00 47.76           O  
ANISOU  221  O   TRP A  55     6660   3804   7682   1424  -1490    -51       O  
ATOM    222  CB  TRP A  55      73.614 227.198  -9.376  1.00 55.06           C  
ANISOU  222  CB  TRP A  55     7760   4689   8472   1745  -1731    -14       C  
ATOM    223  CG  TRP A  55      73.755 227.266 -10.875  1.00 60.57           C  
ANISOU  223  CG  TRP A  55     8700   5357   8959   1973  -1788     75       C  
ATOM    224  CD1 TRP A  55      73.910 228.390 -11.634  1.00 63.90           C  
ANISOU  224  CD1 TRP A  55     9326   5698   9256   2128  -1748    263       C  
ATOM    225  CD2 TRP A  55      73.713 226.165 -11.795  1.00 62.25           C  
ANISOU  225  CD2 TRP A  55     8977   5631   9044   2091  -1907    -28       C  
ATOM    226  NE1 TRP A  55      73.981 228.056 -12.966  1.00 66.45           N  
ANISOU  226  NE1 TRP A  55     9855   6047   9346   2343  -1830    299       N  
ATOM    227  CE2 TRP A  55      73.864 226.697 -13.091  1.00 65.61           C  
ANISOU  227  CE2 TRP A  55     9668   6035   9224   2334  -1936    105       C  
ATOM    228  CE3 TRP A  55      73.570 224.780 -11.647  1.00 61.25           C  
ANISOU  228  CE3 TRP A  55     8707   5576   8990   2022  -1988   -222       C  
ATOM    229  CZ2 TRP A  55      73.876 225.896 -14.229  1.00 67.89           C  
ANISOU  229  CZ2 TRP A  55    10097   6399   9300   2530  -2055     29       C  
ATOM    230  CZ3 TRP A  55      73.584 223.987 -12.778  1.00 62.42           C  
ANISOU  230  CZ3 TRP A  55     8971   5772   8973   2202  -2110   -310       C  
ATOM    231  CH2 TRP A  55      73.736 224.547 -14.052  1.00 66.54           C  
ANISOU  231  CH2 TRP A  55     9770   6298   9213   2465  -2149   -195       C  
ATOM    232  N   VAL A  56      76.536 225.904 -10.104  1.00 49.92           N  
ANISOU  232  N   VAL A  56     7289   3919   7759   1608  -1311    276       N  
ATOM    233  CA  VAL A  56      77.303 224.785 -10.636  1.00 49.69           C  
ANISOU  233  CA  VAL A  56     7305   3890   7686   1601  -1261    275       C  
ATOM    234  C   VAL A  56      78.335 224.295  -9.631  1.00 47.36           C  
ANISOU  234  C   VAL A  56     6882   3589   7524   1366  -1053    302       C  
ATOM    235  O   VAL A  56      78.747 223.131  -9.690  1.00 37.00           O  
ANISOU  235  O   VAL A  56     5522   2305   6231   1309  -1042    233       O  
ATOM    236  CB  VAL A  56      77.969 225.157 -11.977  1.00 52.69           C  
ANISOU  236  CB  VAL A  56     7949   4192   7880   1784  -1200    462       C  
ATOM    237  CG1 VAL A  56      79.329 225.804 -11.755  1.00 51.21           C  
ANISOU  237  CG1 VAL A  56     7805   3878   7776   1660   -902    697       C  
ATOM    238  CG2 VAL A  56      78.102 223.926 -12.854  1.00 55.02           C  
ANISOU  238  CG2 VAL A  56     8323   4541   8040   1901  -1303    356       C  
ATOM    239  N   LEU A  57      78.755 225.155  -8.700  1.00 46.90           N  
ANISOU  239  N   LEU A  57     6772   3506   7541   1242   -905    376       N  
ATOM    240  CA  LEU A  57      79.662 224.781  -7.620  1.00 43.22           C  
ANISOU  240  CA  LEU A  57     6188   3078   7154   1040   -756    360       C  
ATOM    241  C   LEU A  57      78.924 224.154  -6.444  1.00 42.10           C  
ANISOU  241  C   LEU A  57     5815   3065   7117    921   -863    198       C  
ATOM    242  O   LEU A  57      79.426 223.204  -5.836  1.00 40.43           O  
ANISOU  242  O   LEU A  57     5492   2918   6953    796   -808    154       O  
ATOM    243  CB  LEU A  57      80.449 226.003  -7.142  1.00 41.41           C  
ANISOU  243  CB  LEU A  57     6017   2778   6938    983   -598    468       C  
ATOM    244  CG  LEU A  57      81.644 225.724  -6.228  1.00 40.72           C  
ANISOU  244  CG  LEU A  57     5844   2731   6897    804   -471    449       C  
ATOM    245  CD1 LEU A  57      82.899 225.426  -7.040  1.00 42.89           C  
ANISOU  245  CD1 LEU A  57     6274   2918   7105    802   -333    551       C  
ATOM    246  CD2 LEU A  57      81.883 226.875  -5.263  1.00 40.38           C  
ANISOU  246  CD2 LEU A  57     5735   2680   6927    730   -441    443       C  
ATOM    247  N   ILE A  58      77.738 224.668  -6.114  1.00 43.62           N  
ANISOU  247  N   ILE A  58     5932   3293   7350    967  -1011    116       N  
ATOM    248  CA  ILE A  58      76.941 224.070  -5.046  1.00 43.19           C  
ANISOU  248  CA  ILE A  58     5657   3344   7410    871  -1107    -26       C  
ATOM    249  C   ILE A  58      76.474 222.678  -5.449  1.00 44.80           C  
ANISOU  249  C   ILE A  58     5790   3580   7650    874  -1207   -136       C  
ATOM    250  O   ILE A  58      76.494 221.742  -4.640  1.00 44.31           O  
ANISOU  250  O   ILE A  58     5568   3579   7689    751  -1179   -192       O  
ATOM    251  CB  ILE A  58      75.758 224.988  -4.684  1.00 43.33           C  
ANISOU  251  CB  ILE A  58     5615   3380   7471    933  -1247    -99       C  
ATOM    252  CG1 ILE A  58      76.266 226.248  -3.984  1.00 42.36           C  
ANISOU  252  CG1 ILE A  58     5507   3229   7360    896  -1147    -21       C  
ATOM    253  CG2 ILE A  58      74.746 224.257  -3.806  1.00 42.56           C  
ANISOU  253  CG2 ILE A  58     5294   3373   7505    865  -1359   -255       C  
ATOM    254  CD1 ILE A  58      75.266 227.375  -3.967  1.00 42.11           C  
ANISOU  254  CD1 ILE A  58     5482   3176   7343    996  -1273    -63       C  
ATOM    255  N   ALA A  59      76.054 222.518  -6.707  1.00 46.14           N  
ANISOU  255  N   ALA A  59     6080   3708   7743   1030  -1330   -174       N  
ATOM    256  CA  ALA A  59      75.659 221.203  -7.200  1.00 45.96           C  
ANISOU  256  CA  ALA A  59     5993   3706   7764   1050  -1445   -314       C  
ATOM    257  C   ALA A  59      76.836 220.240  -7.195  1.00 46.63           C  
ANISOU  257  C   ALA A  59     6086   3776   7855    950  -1292   -256       C  
ATOM    258  O   ALA A  59      76.697 219.078  -6.797  1.00 48.97           O  
ANISOU  258  O   ALA A  59     6232   4106   8267    854  -1305   -349       O  
ATOM    259  CB  ALA A  59      75.073 221.324  -8.606  1.00 47.05           C  
ANISOU  259  CB  ALA A  59     6280   3822   7775   1280  -1632   -388       C  
ATOM    260  N   GLY A  60      78.006 220.706  -7.632  1.00 44.72           N  
ANISOU  260  N   GLY A  60     6012   3476   7504    971  -1137   -100       N  
ATOM    261  CA  GLY A  60      79.183 219.856  -7.619  1.00 42.12           C  
ANISOU  261  CA  GLY A  60     5690   3136   7178    880   -990    -54       C  
ATOM    262  C   GLY A  60      79.682 219.549  -6.222  1.00 37.53           C  
ANISOU  262  C   GLY A  60     4949   2631   6682    688   -866    -37       C  
ATOM    263  O   GLY A  60      80.332 218.524  -6.006  1.00 35.36           O  
ANISOU  263  O   GLY A  60     4617   2380   6439    604   -796    -50       O  
ATOM    264  N   TYR A  61      79.394 220.424  -5.258  1.00 37.11           N  
ANISOU  264  N   TYR A  61     4823   2620   6656    637   -851    -14       N  
ATOM    265  CA  TYR A  61      79.826 220.165  -3.892  1.00 34.74           C  
ANISOU  265  CA  TYR A  61     4372   2407   6420    498   -764     -8       C  
ATOM    266  C   TYR A  61      78.878 219.218  -3.170  1.00 33.68           C  
ANISOU  266  C   TYR A  61     4046   2335   6415    443   -847   -104       C  
ATOM    267  O   TYR A  61      79.312 218.460  -2.295  1.00 32.15           O  
ANISOU  267  O   TYR A  61     3744   2200   6274    351   -771    -92       O  
ATOM    268  CB  TYR A  61      79.955 221.476  -3.118  1.00 36.92           C  
ANISOU  268  CB  TYR A  61     4638   2699   6689    483   -726     36       C  
ATOM    269  CG  TYR A  61      81.371 221.985  -2.977  1.00 40.22           C  
ANISOU  269  CG  TYR A  61     5128   3099   7055    440   -579    120       C  
ATOM    270  CD1 TYR A  61      81.932 222.812  -3.940  1.00 41.77           C  
ANISOU  270  CD1 TYR A  61     5508   3186   7176    505   -515    205       C  
ATOM    271  CD2 TYR A  61      82.142 221.650  -1.872  1.00 41.85           C  
ANISOU  271  CD2 TYR A  61     5213   3386   7302    345   -509    112       C  
ATOM    272  CE1 TYR A  61      83.225 223.288  -3.810  1.00 43.01           C  
ANISOU  272  CE1 TYR A  61     5709   3311   7320    452   -389    265       C  
ATOM    273  CE2 TYR A  61      83.437 222.120  -1.731  1.00 41.90           C  
ANISOU  273  CE2 TYR A  61     5254   3375   7290    308   -402    158       C  
ATOM    274  CZ  TYR A  61      83.973 222.939  -2.704  1.00 42.97           C  
ANISOU  274  CZ  TYR A  61     5556   3399   7374    350   -343    228       C  
ATOM    275  OH  TYR A  61      85.258 223.410  -2.571  1.00 44.48           O  
ANISOU  275  OH  TYR A  61     5755   3559   7586    300   -241    263       O  
ATOM    276  N   ILE A  62      77.591 219.248  -3.517  1.00 34.78           N  
ANISOU  276  N   ILE A  62     4141   2456   6619    508  -1003   -201       N  
ATOM    277  CA  ILE A  62      76.639 218.309  -2.933  1.00 36.87           C  
ANISOU  277  CA  ILE A  62     4209   2750   7049    454  -1074   -301       C  
ATOM    278  C   ILE A  62      76.880 216.906  -3.474  1.00 38.46           C  
ANISOU  278  C   ILE A  62     4386   2925   7303    428  -1070   -346       C  
ATOM    279  O   ILE A  62      76.894 215.926  -2.720  1.00 38.81           O  
ANISOU  279  O   ILE A  62     4288   2995   7464    336  -1008   -345       O  
ATOM    280  CB  ILE A  62      75.197 218.772  -3.202  1.00 38.32           C  
ANISOU  280  CB  ILE A  62     4336   2918   7306    538  -1256   -426       C  
ATOM    281  CG1 ILE A  62      74.927 220.103  -2.500  1.00 39.30           C  
ANISOU  281  CG1 ILE A  62     4460   3072   7401    555  -1257   -392       C  
ATOM    282  CG2 ILE A  62      74.203 217.707  -2.765  1.00 37.00           C  
ANISOU  282  CG2 ILE A  62     3949   2754   7353    482  -1321   -549       C  
ATOM    283  CD1 ILE A  62      73.682 220.807  -2.988  1.00 41.14           C  
ANISOU  283  CD1 ILE A  62     4694   3290   7649    671  -1440   -506       C  
ATOM    284  N   ILE A  63      77.070 216.794  -4.792  1.00 38.40           N  
ANISOU  284  N   ILE A  63     4520   2859   7213    526  -1136   -385       N  
ATOM    285  CA  ILE A  63      77.336 215.497  -5.413  1.00 38.13           C  
ANISOU  285  CA  ILE A  63     4468   2792   7228    518  -1150   -455       C  
ATOM    286  C   ILE A  63      78.557 214.847  -4.776  1.00 36.69           C  
ANISOU  286  C   ILE A  63     4273   2639   7026    406   -968   -347       C  
ATOM    287  O   ILE A  63      78.535 213.669  -4.400  1.00 29.28           O  
ANISOU  287  O   ILE A  63     3210   1709   6206    332   -942   -380       O  
ATOM    288  CB  ILE A  63      77.514 215.661  -6.933  1.00 40.47           C  
ANISOU  288  CB  ILE A  63     4951   3025   7400    680  -1247   -509       C  
ATOM    289  CG1 ILE A  63      76.174 215.981  -7.594  1.00 33.75           C  
ANISOU  289  CG1 ILE A  63     4084   2166   6572    822  -1478   -672       C  
ATOM    290  CG2 ILE A  63      78.127 214.409  -7.537  1.00 32.46           C  
ANISOU  290  CG2 ILE A  63     3942   1979   6411    675  -1232   -573       C  
ATOM    291  CD1 ILE A  63      76.315 216.547  -8.982  1.00 35.34           C  
ANISOU  291  CD1 ILE A  63     4513   2335   6581   1041  -1580   -688       C  
ATOM    292  N   VAL A  64      79.640 215.613  -4.638  1.00 37.84           N  
ANISOU  292  N   VAL A  64     4542   2802   7033    400   -843   -223       N  
ATOM    293  CA  VAL A  64      80.855 215.087  -4.021  1.00 35.56           C  
ANISOU  293  CA  VAL A  64     4240   2556   6715    314   -693   -145       C  
ATOM    294  C   VAL A  64      80.610 214.747  -2.557  1.00 33.06           C  
ANISOU  294  C   VAL A  64     3753   2317   6490    225   -649   -120       C  
ATOM    295  O   VAL A  64      81.093 213.725  -2.054  1.00 30.39           O  
ANISOU  295  O   VAL A  64     3347   2004   6196    171   -583   -101       O  
ATOM    296  CB  VAL A  64      82.013 216.089  -4.188  1.00 35.55           C  
ANISOU  296  CB  VAL A  64     4382   2547   6576    331   -584    -46       C  
ATOM    297  CG1 VAL A  64      83.099 215.837  -3.156  1.00 34.42           C  
ANISOU  297  CG1 VAL A  64     4177   2478   6423    245   -464     10       C  
ATOM    298  CG2 VAL A  64      82.586 215.996  -5.593  1.00 36.81           C  
ANISOU  298  CG2 VAL A  64     4710   2613   6663    417   -575    -44       C  
ATOM    299  N   PHE A  65      79.842 215.586  -1.855  1.00 35.38           N  
ANISOU  299  N   PHE A  65     3981   2641   6820    228   -687   -118       N  
ATOM    300  CA  PHE A  65      79.574 215.342  -0.439  1.00 35.99           C  
ANISOU  300  CA  PHE A  65     3905   2777   6992    170   -642    -91       C  
ATOM    301  C   PHE A  65      78.878 214.004  -0.226  1.00 39.50           C  
ANISOU  301  C   PHE A  65     4210   3195   7603    132   -654   -130       C  
ATOM    302  O   PHE A  65      79.229 213.251   0.690  1.00 40.97           O  
ANISOU  302  O   PHE A  65     4319   3406   7841     88   -563    -71       O  
ATOM    303  CB  PHE A  65      78.733 216.480   0.145  1.00 32.85           C  
ANISOU  303  CB  PHE A  65     3457   2397   6628    194   -700   -108       C  
ATOM    304  CG  PHE A  65      78.385 216.299   1.602  1.00 30.59           C  
ANISOU  304  CG  PHE A  65     3016   2152   6453    155   -654    -84       C  
ATOM    305  CD1 PHE A  65      77.214 215.660   1.978  1.00 32.14           C  
ANISOU  305  CD1 PHE A  65     3059   2319   6835    136   -686   -128       C  
ATOM    306  CD2 PHE A  65      79.225 216.773   2.594  1.00 29.52           C  
ANISOU  306  CD2 PHE A  65     2882   2071   6263    146   -576    -26       C  
ATOM    307  CE1 PHE A  65      76.893 215.493   3.313  1.00 32.55           C  
ANISOU  307  CE1 PHE A  65     2979   2386   7004    112   -619    -87       C  
ATOM    308  CE2 PHE A  65      78.903 216.609   3.928  1.00 30.97           C  
ANISOU  308  CE2 PHE A  65     2940   2276   6550    133   -536     -2       C  
ATOM    309  CZ  PHE A  65      77.737 215.969   4.286  1.00 31.51           C  
ANISOU  309  CZ  PHE A  65     2874   2307   6792    117   -545    -20       C  
ATOM    310  N   VAL A  66      77.886 213.689  -1.060  1.00 39.19           N  
ANISOU  310  N   VAL A  66     4131   3094   7663    158   -770   -235       N  
ATOM    311  CA  VAL A  66      77.147 212.441  -0.888  1.00 39.33           C  
ANISOU  311  CA  VAL A  66     3987   3068   7886    118   -780   -290       C  
ATOM    312  C   VAL A  66      78.021 211.247  -1.260  1.00 36.60           C  
ANISOU  312  C   VAL A  66     3678   2702   7527     93   -717   -273       C  
ATOM    313  O   VAL A  66      78.074 210.246  -0.536  1.00 34.12           O  
ANISOU  313  O   VAL A  66     3264   2378   7324     44   -631   -226       O  
ATOM    314  CB  VAL A  66      75.845 212.468  -1.711  1.00 42.69           C  
ANISOU  314  CB  VAL A  66     4339   3434   8449    164   -947   -451       C  
ATOM    315  CG1 VAL A  66      75.052 211.191  -1.490  1.00 31.23           C  
ANISOU  315  CG1 VAL A  66     2685   1925   7256    117   -943   -522       C  
ATOM    316  CG2 VAL A  66      75.010 213.688  -1.347  1.00 29.96           C  
ANISOU  316  CG2 VAL A  66     2697   1843   6843    200  -1021   -479       C  
ATOM    317  N   VAL A  67      78.724 211.340  -2.391  1.00 36.54           N  
ANISOU  317  N   VAL A  67     3820   2675   7388    137   -755   -307       N  
ATOM    318  CA  VAL A  67      79.513 210.211  -2.878  1.00 34.81           C  
ANISOU  318  CA  VAL A  67     3630   2425   7170    123   -717   -321       C  
ATOM    319  C   VAL A  67      80.696 209.940  -1.956  1.00 33.78           C  
ANISOU  319  C   VAL A  67     3526   2352   6957     79   -570   -194       C  
ATOM    320  O   VAL A  67      81.064 208.783  -1.717  1.00 35.80           O  
ANISOU  320  O   VAL A  67     3731   2587   7283     48   -519   -181       O  
ATOM    321  CB  VAL A  67      79.964 210.468  -4.329  1.00 31.64           C  
ANISOU  321  CB  VAL A  67     3389   1979   6656    204   -792   -397       C  
ATOM    322  CG1 VAL A  67      80.926 209.387  -4.797  1.00 29.67           C  
ANISOU  322  CG1 VAL A  67     3175   1700   6399    196   -746   -415       C  
ATOM    323  CG2 VAL A  67      78.756 210.545  -5.251  1.00 30.94           C  
ANISOU  323  CG2 VAL A  67     3266   1833   6658    279   -975   -562       C  
ATOM    324  N   ALA A  68      81.309 210.998  -1.420  1.00 26.58           N  
ANISOU  324  N   ALA A  68     2685   1505   5908     85   -513   -112       N  
ATOM    325  CA  ALA A  68      82.446 210.814  -0.525  1.00 39.51           C  
ANISOU  325  CA  ALA A  68     4334   3200   7478     62   -403    -24       C  
ATOM    326  C   ALA A  68      82.012 210.238   0.817  1.00 39.67           C  
ANISOU  326  C   ALA A  68     4222   3237   7615     30   -351     34       C  
ATOM    327  O   ALA A  68      82.717 209.404   1.396  1.00 39.95           O  
ANISOU  327  O   ALA A  68     4243   3276   7661     18   -281     86       O  
ATOM    328  CB  ALA A  68      83.182 212.138  -0.327  1.00 24.77           C  
ANISOU  328  CB  ALA A  68     2554   1386   5471     81   -370     18       C  
ATOM    329  N   LEU A  69      80.858 210.671   1.332  1.00 39.86           N  
ANISOU  329  N   LEU A  69     4151   3258   7737     26   -381     30       N  
ATOM    330  CA  LEU A  69      80.393 210.164   2.620  1.00 38.02           C  
ANISOU  330  CA  LEU A  69     3794   3019   7635      5   -309    102       C  
ATOM    331  C   LEU A  69      79.895 208.727   2.498  1.00 40.37           C  
ANISOU  331  C   LEU A  69     4001   3234   8105    -24   -284     95       C  
ATOM    332  O   LEU A  69      80.247 207.866   3.313  1.00 42.04           O  
ANISOU  332  O   LEU A  69     4179   3424   8370    -36   -189    183       O  
ATOM    333  CB  LEU A  69      79.297 211.074   3.179  1.00 36.62           C  
ANISOU  333  CB  LEU A  69     3529   2848   7538     12   -340     93       C  
ATOM    334  CG  LEU A  69      78.976 210.904   4.664  1.00 36.80           C  
ANISOU  334  CG  LEU A  69     3443   2866   7673      7   -243    191       C  
ATOM    335  CD1 LEU A  69      80.108 211.447   5.524  1.00 35.85           C  
ANISOU  335  CD1 LEU A  69     3396   2813   7414     35   -192    259       C  
ATOM    336  CD2 LEU A  69      77.660 211.576   5.014  1.00 38.01           C  
ANISOU  336  CD2 LEU A  69     3478   2996   7969     10   -278    156       C  
ATOM    337  N   ILE A  70      79.079 208.449   1.477  1.00 40.70           N  
ANISOU  337  N   ILE A  70     3999   3215   8249    -29   -374    -15       N  
ATOM    338  CA  ILE A  70      78.566 207.096   1.271  1.00 40.47           C  
ANISOU  338  CA  ILE A  70     3865   3093   8419    -57   -361    -51       C  
ATOM    339  C   ILE A  70      79.703 206.142   0.927  1.00 43.08           C  
ANISOU  339  C   ILE A  70     4277   3407   8684    -60   -327    -35       C  
ATOM    340  O   ILE A  70      79.847 205.073   1.532  1.00 44.80           O  
ANISOU  340  O   ILE A  70     4442   3573   9007    -83   -242     33       O  
ATOM    341  CB  ILE A  70      77.479 207.092   0.179  1.00 38.59           C  
ANISOU  341  CB  ILE A  70     3553   2794   8317    -46   -495   -215       C  
ATOM    342  CG1 ILE A  70      76.249 207.877   0.635  1.00 38.54           C  
ANISOU  342  CG1 ILE A  70     3430   2787   8426    -41   -527   -243       C  
ATOM    343  CG2 ILE A  70      77.091 205.667  -0.188  1.00 37.40           C  
ANISOU  343  CG2 ILE A  70     3290   2539   8381    -70   -495   -285       C  
ATOM    344  CD1 ILE A  70      75.551 207.268   1.828  1.00 39.83           C  
ANISOU  344  CD1 ILE A  70     3436   2896   8800    -77   -397   -158       C  
ATOM    345  N   GLY A  71      80.534 206.524  -0.046  1.00 40.69           N  
ANISOU  345  N   GLY A  71     4107   3138   8217    -33   -386    -91       N  
ATOM    346  CA  GLY A  71      81.582 205.626  -0.507  1.00 38.94           C  
ANISOU  346  CA  GLY A  71     3950   2891   7955    -30   -366   -101       C  
ATOM    347  C   GLY A  71      82.596 205.292   0.571  1.00 38.94           C  
ANISOU  347  C   GLY A  71     3981   2927   7888    -35   -257     23       C  
ATOM    348  O   GLY A  71      82.930 204.124   0.786  1.00 40.10           O  
ANISOU  348  O   GLY A  71     4100   3015   8122    -47   -215     48       O  
ATOM    349  N   ASN A  72      83.096 206.316   1.271  1.00 38.22           N  
ANISOU  349  N   ASN A  72     3943   2921   7656    -19   -219     93       N  
ATOM    350  CA  ASN A  72      84.167 206.088   2.239  1.00 36.01           C  
ANISOU  350  CA  ASN A  72     3696   2675   7311     -6   -141    184       C  
ATOM    351  C   ASN A  72      83.687 205.305   3.454  1.00 36.73           C  
ANISOU  351  C   ASN A  72     3698   2720   7539    -17    -63    288       C  
ATOM    352  O   ASN A  72      84.459 204.529   4.028  1.00 38.78           O  
ANISOU  352  O   ASN A  72     3978   2954   7803     -2     -7    355       O  
ATOM    353  CB  ASN A  72      84.784 207.416   2.681  1.00 34.09           C  
ANISOU  353  CB  ASN A  72     3510   2523   6920     18   -134    207       C  
ATOM    354  CG  ASN A  72      85.663 208.034   1.613  1.00 33.84           C  
ANISOU  354  CG  ASN A  72     3583   2518   6758     33   -166    141       C  
ATOM    355  OD1 ASN A  72      86.782 207.581   1.374  1.00 32.51           O  
ANISOU  355  OD1 ASN A  72     3462   2344   6548     44   -142    133       O  
ATOM    356  ND2 ASN A  72      85.159 209.079   0.966  1.00 34.14           N  
ANISOU  356  ND2 ASN A  72     3656   2570   6744     38   -214    100       N  
ATOM    357  N   VAL A  73      82.432 205.493   3.866  1.00 35.73           N  
ANISOU  357  N   VAL A  73     3472   2568   7535    -34    -50    311       N  
ATOM    358  CA  VAL A  73      81.907 204.726   4.994  1.00 38.70           C  
ANISOU  358  CA  VAL A  73     3760   2879   8065    -42     54    432       C  
ATOM    359  C   VAL A  73      81.709 203.269   4.599  1.00 40.02           C  
ANISOU  359  C   VAL A  73     3881   2931   8395    -72     76    422       C  
ATOM    360  O   VAL A  73      81.959 202.355   5.395  1.00 32.89           O  
ANISOU  360  O   VAL A  73     2967   1964   7566    -67    171    539       O  
ATOM    361  CB  VAL A  73      80.604 205.361   5.515  1.00 39.08           C  
ANISOU  361  CB  VAL A  73     3699   2922   8228    -53     78    457       C  
ATOM    362  CG1 VAL A  73      79.854 204.391   6.421  1.00 41.60           C  
ANISOU  362  CG1 VAL A  73     3909   3140   8758    -69    208    581       C  
ATOM    363  CG2 VAL A  73      80.907 206.647   6.265  1.00 29.29           C  
ANISOU  363  CG2 VAL A  73     2496   1776   6857    -16     80    498       C  
ATOM    364  N   LEU A  74      81.260 203.030   3.365  1.00 40.90           N  
ANISOU  364  N   LEU A  74     3963   3002   8574    -94    -15    283       N  
ATOM    365  CA  LEU A  74      81.182 201.665   2.859  1.00 41.89           C  
ANISOU  365  CA  LEU A  74     4039   3011   8865   -118    -16    241       C  
ATOM    366  C   LEU A  74      82.546 200.989   2.867  1.00 41.92           C  
ANISOU  366  C   LEU A  74     4144   3011   8773    -96      2    275       C  
ATOM    367  O   LEU A  74      82.633 199.767   3.033  1.00 35.15           O  
ANISOU  367  O   LEU A  74     3251   2045   8059   -109     46    310       O  
ATOM    368  CB  LEU A  74      80.602 201.657   1.445  1.00 34.22           C  
ANISOU  368  CB  LEU A  74     3027   2008   7966   -126   -142     58       C  
ATOM    369  CG  LEU A  74      79.118 201.974   1.269  1.00 43.62           C  
ANISOU  369  CG  LEU A  74     4081   3161   9332   -144   -182    -17       C  
ATOM    370  CD1 LEU A  74      78.794 202.066  -0.208  1.00 44.01           C  
ANISOU  370  CD1 LEU A  74     4119   3193   9411   -127   -338   -216       C  
ATOM    371  CD2 LEU A  74      78.262 200.918   1.943  1.00 37.39           C  
ANISOU  371  CD2 LEU A  74     3142   2242   8823   -184    -82     39       C  
ATOM    372  N   VAL A  75      83.619 201.764   2.691  1.00 31.85           N  
ANISOU  372  N   VAL A  75     2986   1838   7277    -62    -31    260       N  
ATOM    373  CA  VAL A  75      84.966 201.199   2.711  1.00 39.58           C  
ANISOU  373  CA  VAL A  75     4050   2813   8175    -34    -17    278       C  
ATOM    374  C   VAL A  75      85.304 200.676   4.101  1.00 40.49           C  
ANISOU  374  C   VAL A  75     4169   2896   8320    -13     83    436       C  
ATOM    375  O   VAL A  75      85.826 199.565   4.253  1.00 33.53           O  
ANISOU  375  O   VAL A  75     3301   1929   7512     -3    111    474       O  
ATOM    376  CB  VAL A  75      85.995 202.243   2.236  1.00 36.69           C  
ANISOU  376  CB  VAL A  75     3790   2556   7596     -3    -60    225       C  
ATOM    377  CG1 VAL A  75      87.404 201.807   2.613  1.00 29.76           C  
ANISOU  377  CG1 VAL A  75     2978   1681   6650     34    -31    261       C  
ATOM    378  CG2 VAL A  75      85.887 202.450   0.735  1.00 36.27           C  
ANISOU  378  CG2 VAL A  75     3762   2498   7520     -8   -146     85       C  
ATOM    379  N   CYS A  76      85.024 201.474   5.134  1.00 40.17           N  
ANISOU  379  N   CYS A  76     4120   2916   8229      4    136    534       N  
ATOM    380  CA  CYS A  76      85.265 201.024   6.502  1.00 40.78           C  
ANISOU  380  CA  CYS A  76     4206   2956   8333     45    237    702       C  
ATOM    381  C   CYS A  76      84.390 199.830   6.847  1.00 43.28           C  
ANISOU  381  C   CYS A  76     4441   3135   8870     14    325    795       C  
ATOM    382  O   CYS A  76      84.853 198.865   7.465  1.00 44.21           O  
ANISOU  382  O   CYS A  76     4591   3169   9038     45    392    909       O  
ATOM    383  CB  CYS A  76      85.008 202.164   7.486  1.00 41.36           C  
ANISOU  383  CB  CYS A  76     4273   3115   8328     79    276    781       C  
ATOM    384  SG  CYS A  76      85.967 203.654   7.164  1.00 39.64           S  
ANISOU  384  SG  CYS A  76     4131   3037   7894    110    183    671       S  
ATOM    385  N   VAL A  77      83.118 199.877   6.449  1.00 44.07           N  
ANISOU  385  N   VAL A  77     4430   3197   9117    -42    325    748       N  
ATOM    386  CA  VAL A  77      82.185 198.808   6.792  1.00 47.82           C  
ANISOU  386  CA  VAL A  77     4801   3527   9841    -78    424    831       C  
ATOM    387  C   VAL A  77      82.592 197.505   6.119  1.00 50.55           C  
ANISOU  387  C   VAL A  77     5150   3752  10305    -98    394    775       C  
ATOM    388  O   VAL A  77      82.570 196.436   6.742  1.00 52.07           O  
ANISOU  388  O   VAL A  77     5326   3818  10640    -98    495    903       O  
ATOM    389  CB  VAL A  77      80.748 199.214   6.419  1.00 48.67           C  
ANISOU  389  CB  VAL A  77     4773   3617  10101   -129    414    756       C  
ATOM    390  CG1 VAL A  77      79.818 198.018   6.519  1.00 49.87           C  
ANISOU  390  CG1 VAL A  77     4798   3597  10552   -178    505    797       C  
ATOM    391  CG2 VAL A  77      80.269 200.338   7.321  1.00 49.87           C  
ANISOU  391  CG2 VAL A  77     4906   3857  10184   -105    474    847       C  
ATOM    392  N   ALA A  78      82.976 197.571   4.842  1.00 49.68           N  
ANISOU  392  N   ALA A  78     5062   3671  10143   -109    262    591       N  
ATOM    393  CA  ALA A  78      83.318 196.360   4.105  1.00 50.33           C  
ANISOU  393  CA  ALA A  78     5131   3634  10357   -122    221    513       C  
ATOM    394  C   ALA A  78      84.554 195.672   4.668  1.00 51.70           C  
ANISOU  394  C   ALA A  78     5410   3772  10462    -75    260    613       C  
ATOM    395  O   ALA A  78      84.712 194.459   4.490  1.00 54.71           O  
ANISOU  395  O   ALA A  78     5768   4012  11006    -84    270    613       O  
ATOM    396  CB  ALA A  78      83.531 196.685   2.626  1.00 38.92           C  
ANISOU  396  CB  ALA A  78     3697   2241   8849   -124     75    302       C  
ATOM    397  N   VAL A  79      85.429 196.411   5.341  1.00 52.05           N  
ANISOU  397  N   VAL A  79     5562   3928  10288    -19    274    688       N  
ATOM    398  CA  VAL A  79      86.624 195.810   5.922  1.00 53.28           C  
ANISOU  398  CA  VAL A  79     5818   4048  10379     46    298    776       C  
ATOM    399  C   VAL A  79      86.351 195.282   7.324  1.00 57.45           C  
ANISOU  399  C   VAL A  79     6354   4494  10982     81    435   1003       C  
ATOM    400  O   VAL A  79      86.781 194.180   7.673  1.00 60.44           O  
ANISOU  400  O   VAL A  79     6770   4746  11449    112    477   1092       O  
ATOM    401  CB  VAL A  79      87.777 196.831   5.914  1.00 49.15           C  
ANISOU  401  CB  VAL A  79     5395   3673   9608    103    238    726       C  
ATOM    402  CG1 VAL A  79      88.978 196.286   6.667  1.00 49.10           C  
ANISOU  402  CG1 VAL A  79     5485   3629   9540    192    259    817       C  
ATOM    403  CG2 VAL A  79      88.151 197.173   4.483  1.00 46.77           C  
ANISOU  403  CG2 VAL A  79     5098   3428   9246     77    129    529       C  
ATOM    404  N   TRP A  80      85.626 196.040   8.146  1.00 61.04           N  
ANISOU  404  N   TRP A  80     6775   5012  11407     85    514   1111       N  
ATOM    405  CA  TRP A  80      85.328 195.579   9.493  1.00 67.69           C  
ANISOU  405  CA  TRP A  80     7627   5783  12309    135    668   1353       C  
ATOM    406  C   TRP A  80      84.247 194.509   9.524  1.00 70.48           C  
ANISOU  406  C   TRP A  80     7871   5965  12943     67    775   1430       C  
ATOM    407  O   TRP A  80      84.045 193.892  10.575  1.00 71.97           O  
ANISOU  407  O   TRP A  80     8074   6066  13206    108    925   1654       O  
ATOM    408  CB  TRP A  80      84.921 196.757  10.378  1.00 71.64           C  
ANISOU  408  CB  TRP A  80     8119   6410  12690    176    728   1450       C  
ATOM    409  CG  TRP A  80      86.050 197.706  10.656  1.00 74.05           C  
ANISOU  409  CG  TRP A  80     8533   6856  12748    266    648   1414       C  
ATOM    410  CD1 TRP A  80      86.094 199.038  10.361  1.00 72.42           C  
ANISOU  410  CD1 TRP A  80     8317   6787  12411    258    567   1294       C  
ATOM    411  CD2 TRP A  80      87.305 197.390  11.276  1.00 76.15           C  
ANISOU  411  CD2 TRP A  80     8923   7124  12887    388    634   1488       C  
ATOM    412  NE1 TRP A  80      87.294 199.573  10.767  1.00 71.81           N  
ANISOU  412  NE1 TRP A  80     8339   6794  12151    358    511   1283       N  
ATOM    413  CE2 TRP A  80      88.055 198.582  11.331  1.00 74.05           C  
ANISOU  413  CE2 TRP A  80     8704   7001  12430    447    544   1395       C  
ATOM    414  CE3 TRP A  80      87.864 196.217  11.794  1.00 78.11           C  
ANISOU  414  CE3 TRP A  80     9248   7258  13173    463    682   1621       C  
ATOM    415  CZ2 TRP A  80      89.336 198.633  11.881  1.00 74.38           C  
ANISOU  415  CZ2 TRP A  80     8853   7083  12326    585    494   1413       C  
ATOM    416  CZ3 TRP A  80      89.135 196.270  12.340  1.00 77.50           C  
ANISOU  416  CZ3 TRP A  80     9293   7225  12931    609    627   1648       C  
ATOM    417  CH2 TRP A  80      89.856 197.469  12.379  1.00 75.90           C  
ANISOU  417  CH2 TRP A  80     9121   7173  12546    672    530   1536       C  
ATOM    418  N   LYS A  81      83.542 194.284   8.416  1.00 72.10           N  
ANISOU  418  N   LYS A  81     7965   6118  13312    -25    707   1256       N  
ATOM    419  CA  LYS A  81      82.587 193.183   8.358  1.00 76.22           C  
ANISOU  419  CA  LYS A  81     8366   6452  14143    -90    796   1298       C  
ATOM    420  C   LYS A  81      83.273 191.882   7.964  1.00 78.16           C  
ANISOU  420  C   LYS A  81     8646   6544  14506    -87    765   1277       C  
ATOM    421  O   LYS A  81      83.107 190.858   8.633  1.00 80.42           O  
ANISOU  421  O   LYS A  81     8923   6667  14964    -84    892   1446       O  
ATOM    422  CB  LYS A  81      81.455 193.502   7.378  1.00 77.40           C  
ANISOU  422  CB  LYS A  81     8363   6599  14445   -172    728   1109       C  
ATOM    423  CG  LYS A  81      80.276 194.230   7.998  1.00 80.39           C  
ANISOU  423  CG  LYS A  81     8648   7017  14881   -194    830   1186       C  
ATOM    424  CD  LYS A  81      79.134 194.376   7.002  1.00 82.92           C  
ANISOU  424  CD  LYS A  81     8811   7302  15394   -263    753    985       C  
ATOM    425  CE  LYS A  81      77.922 195.050   7.631  1.00 83.77           C  
ANISOU  425  CE  LYS A  81     8814   7430  15587   -283    859   1053       C  
ATOM    426  NZ  LYS A  81      76.822 195.240   6.643  1.00 83.56           N  
ANISOU  426  NZ  LYS A  81     8635   7367  15748   -337    765    836       N  
ATOM    427  N   ASN A  82      84.049 191.907   6.886  1.00 77.06           N  
ANISOU  427  N   ASN A  82     8547   6451  14282    -84    606   1078       N  
ATOM    428  CA  ASN A  82      84.683 190.706   6.361  1.00 82.45           C  
ANISOU  428  CA  ASN A  82     9247   6989  15091    -80    558   1022       C  
ATOM    429  C   ASN A  82      86.099 190.588   6.912  1.00 83.23           C  
ANISOU  429  C   ASN A  82     9515   7118  14989     18    546   1111       C  
ATOM    430  O   ASN A  82      86.922 191.491   6.727  1.00 83.11           O  
ANISOU  430  O   ASN A  82     9586   7267  14725     66    462   1035       O  
ATOM    431  CB  ASN A  82      84.696 190.730   4.834  1.00 84.95           C  
ANISOU  431  CB  ASN A  82     9500   7329  15449   -116    398    751       C  
ATOM    432  CG  ASN A  82      85.261 189.457   4.236  1.00 89.51           C  
ANISOU  432  CG  ASN A  82    10070   7746  16193   -111    345    673       C  
ATOM    433  OD1 ASN A  82      85.435 188.455   4.929  1.00 93.31           O  
ANISOU  433  OD1 ASN A  82    10574   8067  16814    -97    433    821       O  
ATOM    434  ND2 ASN A  82      85.546 189.489   2.941  1.00 88.85           N  
ANISOU  434  ND2 ASN A  82     9958   7701  16101   -114    201    444       N  
ATOM    435  N   HIS A  83      86.382 189.469   7.583  1.00 84.45           N  
ANISOU  435  N   HIS A  83     9716   7105  15268     55    629   1270       N  
ATOM    436  CA  HIS A  83      87.713 189.242   8.132  1.00 84.33           C  
ANISOU  436  CA  HIS A  83     9863   7095  15084    170    608   1353       C  
ATOM    437  C   HIS A  83      88.715 188.808   7.071  1.00 80.84           C  
ANISOU  437  C   HIS A  83     9453   6633  14631    187    463   1155       C  
ATOM    438  O   HIS A  83      89.924 188.921   7.298  1.00 79.67           O  
ANISOU  438  O   HIS A  83     9429   6538  14305    288    410   1158       O  
ATOM    439  CB  HIS A  83      87.653 188.201   9.250  1.00 90.65           C  
ANISOU  439  CB  HIS A  83    10718   7716  16010    224    749   1613       C  
ATOM    440  CG  HIS A  83      86.854 188.641  10.438  1.00 94.60           C  
ANISOU  440  CG  HIS A  83    11209   8252  16481    241    914   1846       C  
ATOM    441  ND1 HIS A  83      87.410 189.328  11.496  1.00 94.74           N  
ANISOU  441  ND1 HIS A  83    11350   8400  16245    366    951   2000       N  
ATOM    442  CD2 HIS A  83      85.539 188.495  10.733  1.00 97.21           C  
ANISOU  442  CD2 HIS A  83    11412   8509  17013    159   1057   1947       C  
ATOM    443  CE1 HIS A  83      86.472 189.584  12.391  1.00 96.22           C  
ANISOU  443  CE1 HIS A  83    11493   8601  16465    364   1116   2196       C  
ATOM    444  NE2 HIS A  83      85.328 189.089  11.953  1.00 97.49           N  
ANISOU  444  NE2 HIS A  83    11500   8637  16903    235   1189   2170       N  
ATOM    445  N   HIS A  84      88.243 188.316   5.923  1.00 77.18           N  
ANISOU  445  N   HIS A  84     8872   6093  14362    105    397    976       N  
ATOM    446  CA  HIS A  84      89.138 188.054   4.802  1.00 74.48           C  
ANISOU  446  CA  HIS A  84     8544   5761  13994    126    260    768       C  
ATOM    447  C   HIS A  84      89.688 189.339   4.198  1.00 67.93           C  
ANISOU  447  C   HIS A  84     7754   5158  12899    143    170    627       C  
ATOM    448  O   HIS A  84      90.686 189.291   3.470  1.00 65.26           O  
ANISOU  448  O   HIS A  84     7457   4857  12482    185     79    490       O  
ATOM    449  CB  HIS A  84      88.416 187.245   3.721  1.00 77.49           C  
ANISOU  449  CB  HIS A  84     8775   6008  14659     48    206    603       C  
ATOM    450  CG  HIS A  84      88.200 185.806   4.080  1.00 81.39           C  
ANISOU  450  CG  HIS A  84     9231   6246  15447     38    270    698       C  
ATOM    451  ND1 HIS A  84      89.145 184.831   3.843  1.00 82.76           N  
ANISOU  451  ND1 HIS A  84     9459   6293  15691     96    215    659       N  
ATOM    452  CD2 HIS A  84      87.142 185.176   4.645  1.00 83.88           C  
ANISOU  452  CD2 HIS A  84     9454   6396  16022    -22    391    833       C  
ATOM    453  CE1 HIS A  84      88.681 183.664   4.254  1.00 85.71           C  
ANISOU  453  CE1 HIS A  84     9784   6429  16354     72    295    769       C  
ATOM    454  NE2 HIS A  84      87.467 183.846   4.745  1.00 87.14           N  
ANISOU  454  NE2 HIS A  84     9871   6579  16658     -3    409    880       N  
ATOM    455  N   MET A  85      89.065 190.483   4.487  1.00 65.78           N  
ANISOU  455  N   MET A  85     7464   5029  12502    113    202    661       N  
ATOM    456  CA  MET A  85      89.469 191.769   3.932  1.00 60.26           C  
ANISOU  456  CA  MET A  85     6795   4528  11571    121    130    542       C  
ATOM    457  C   MET A  85      90.523 192.487   4.763  1.00 53.97           C  
ANISOU  457  C   MET A  85     6119   3845  10543    207    145    627       C  
ATOM    458  O   MET A  85      91.071 193.490   4.299  1.00 51.17           O  
ANISOU  458  O   MET A  85     5791   3636  10014    218     90    527       O  
ATOM    459  CB  MET A  85      88.248 192.685   3.786  1.00 61.29           C  
ANISOU  459  CB  MET A  85     6844   4746  11698     54    145    522       C  
ATOM    460  CG  MET A  85      87.255 192.246   2.725  1.00 65.55           C  
ANISOU  460  CG  MET A  85     7255   5208  12444    -15     92    377       C  
ATOM    461  SD  MET A  85      87.586 192.963   1.106  1.00 67.47           S  
ANISOU  461  SD  MET A  85     7502   5571  12563    -10    -52    131       S  
ATOM    462  CE  MET A  85      86.780 194.553   1.273  1.00 66.98           C  
ANISOU  462  CE  MET A  85     7435   5673  12340    -34    -41    152       C  
ATOM    463  N   ARG A  86      90.823 192.006   5.970  1.00 52.22           N  
ANISOU  463  N   ARG A  86     5966   3551  10324    276    217    809       N  
ATOM    464  CA  ARG A  86      91.695 192.729   6.896  1.00 52.45           C  
ANISOU  464  CA  ARG A  86     6097   3686  10147    379    225    892       C  
ATOM    465  C   ARG A  86      93.172 192.503   6.565  1.00 51.82           C  
ANISOU  465  C   ARG A  86     6091   3615   9985    467    144    795       C  
ATOM    466  O   ARG A  86      93.952 191.990   7.365  1.00 50.23           O  
ANISOU  466  O   ARG A  86     5978   3355   9752    586    151    892       O  
ATOM    467  CB  ARG A  86      91.386 192.326   8.331  1.00 57.61           C  
ANISOU  467  CB  ARG A  86     6802   4264  10824    449    332   1135       C  
ATOM    468  CG  ARG A  86      89.963 192.625   8.764  1.00 61.55           C  
ANISOU  468  CG  ARG A  86     7215   4764  11408    372    435   1244       C  
ATOM    469  CD  ARG A  86      89.807 192.466  10.264  1.00 66.49           C  
ANISOU  469  CD  ARG A  86     7905   5357  12002    469    556   1503       C  
ATOM    470  NE  ARG A  86      88.444 192.745  10.702  1.00 70.14           N  
ANISOU  470  NE  ARG A  86     8272   5821  12559    400    677   1617       N  
ATOM    471  CZ  ARG A  86      88.063 192.784  11.974  1.00 75.08           C  
ANISOU  471  CZ  ARG A  86     8927   6447  13155    476    813   1856       C  
ATOM    472  NH1 ARG A  86      88.945 192.565  12.940  1.00 78.12           N  
ANISOU  472  NH1 ARG A  86     9445   6836  13400    639    830   2007       N  
ATOM    473  NH2 ARG A  86      86.800 193.045  12.281  1.00 76.04           N  
ANISOU  473  NH2 ARG A  86     8942   6569  13380    408    934   1945       N  
ATOM    474  N   THR A  87      93.549 192.910   5.357  1.00 52.60           N  
ANISOU  474  N   THR A  87     6150   3788  10048    422     69    603       N  
ATOM    475  CA  THR A  87      94.942 192.892   4.942  1.00 50.95           C  
ANISOU  475  CA  THR A  87     5983   3611   9764    496      4    492       C  
ATOM    476  C   THR A  87      95.602 194.228   5.274  1.00 49.44           C  
ANISOU  476  C   THR A  87     5816   3584   9385    538     -7    467       C  
ATOM    477  O   THR A  87      94.933 195.236   5.516  1.00 49.91           O  
ANISOU  477  O   THR A  87     5851   3740   9371    491     19    499       O  
ATOM    478  CB  THR A  87      95.064 192.604   3.443  1.00 40.00           C  
ANISOU  478  CB  THR A  87     4537   2211   8450    437    -59    302       C  
ATOM    479  OG1 THR A  87      94.746 193.784   2.696  1.00 38.00           O  
ANISOU  479  OG1 THR A  87     4244   2097   8096    373    -74    207       O  
ATOM    480  CG2 THR A  87      94.113 191.488   3.036  1.00 41.92           C  
ANISOU  480  CG2 THR A  87     4720   2301   8906    375    -55    300       C  
ATOM    481  N   VAL A  88      96.937 194.221   5.288  1.00 49.06           N  
ANISOU  481  N   VAL A  88     5802   3560   9279    633    -50    401       N  
ATOM    482  CA  VAL A  88      97.685 195.441   5.591  1.00 48.56           C  
ANISOU  482  CA  VAL A  88     5738   3636   9076    679    -64    356       C  
ATOM    483  C   VAL A  88      97.372 196.530   4.573  1.00 47.41           C  
ANISOU  483  C   VAL A  88     5528   3598   8888    565    -66    243       C  
ATOM    484  O   VAL A  88      97.269 197.714   4.917  1.00 44.94           O  
ANISOU  484  O   VAL A  88     5201   3389   8484    552    -53    252       O  
ATOM    485  CB  VAL A  88      99.194 195.142   5.657  1.00 49.27           C  
ANISOU  485  CB  VAL A  88     5848   3723   9151    802   -112    276       C  
ATOM    486  CG1 VAL A  88      99.556 194.522   6.996  1.00 51.11           C  
ANISOU  486  CG1 VAL A  88     6166   3897   9355    969   -117    410       C  
ATOM    487  CG2 VAL A  88      99.599 194.213   4.519  1.00 49.82           C  
ANISOU  487  CG2 VAL A  88     5891   3712   9328    774   -142    158       C  
ATOM    488  N   THR A  89      97.212 196.148   3.304  1.00 48.02           N  
ANISOU  488  N   THR A  89     5572   3643   9029    498    -85    136       N  
ATOM    489  CA  THR A  89      96.873 197.123   2.274  1.00 45.30           C  
ANISOU  489  CA  THR A  89     5192   3388   8633    417    -86     42       C  
ATOM    490  C   THR A  89      95.502 197.738   2.528  1.00 45.89           C  
ANISOU  490  C   THR A  89     5254   3502   8681    348    -62    118       C  
ATOM    491  O   THR A  89      95.310 198.945   2.338  1.00 45.57           O  
ANISOU  491  O   THR A  89     5204   3561   8550    314    -53     98       O  
ATOM    492  CB  THR A  89      96.919 196.468   0.892  1.00 48.39           C  
ANISOU  492  CB  THR A  89     5562   3724   9098    392   -120    -87       C  
ATOM    493  OG1 THR A  89      98.204 195.872   0.684  1.00 51.01           O  
ANISOU  493  OG1 THR A  89     5896   4020   9467    464   -141   -167       O  
ATOM    494  CG2 THR A  89      96.671 197.503  -0.198  1.00 50.83           C  
ANISOU  494  CG2 THR A  89     5862   4115   9335    342   -118   -176       C  
ATOM    495  N   ASN A  90      94.539 196.928   2.974  1.00 45.90           N  
ANISOU  495  N   ASN A  90     5248   3418   8775    328    -45    207       N  
ATOM    496  CA  ASN A  90      93.178 197.425   3.156  1.00 41.35           C  
ANISOU  496  CA  ASN A  90     4637   2869   8204    263    -20    265       C  
ATOM    497  C   ASN A  90      93.016 198.175   4.472  1.00 40.02           C  
ANISOU  497  C   ASN A  90     4486   2762   7958    294     24    389       C  
ATOM    498  O   ASN A  90      92.260 199.150   4.539  1.00 38.26           O  
ANISOU  498  O   ASN A  90     4238   2618   7683    253     35    398       O  
ATOM    499  CB  ASN A  90      92.181 196.269   3.076  1.00 40.63           C  
ANISOU  499  CB  ASN A  90     4503   2649   8285    223     -9    300       C  
ATOM    500  CG  ASN A  90      92.008 195.750   1.664  1.00 41.23           C  
ANISOU  500  CG  ASN A  90     4539   2675   8450    188    -69    149       C  
ATOM    501  OD1 ASN A  90      92.578 196.293   0.719  1.00 38.02           O  
ANISOU  501  OD1 ASN A  90     4152   2336   7959    196   -110     31       O  
ATOM    502  ND2 ASN A  90      91.227 194.685   1.514  1.00 44.84           N  
ANISOU  502  ND2 ASN A  90     4938   3004   9097    155    -72    151       N  
ATOM    503  N   LEU A  91      93.704 197.734   5.529  1.00 42.13           N  
ANISOU  503  N   LEU A  91     4800   2990   8216    383     44    482       N  
ATOM    504  CA  LEU A  91      93.651 198.459   6.796  1.00 43.04           C  
ANISOU  504  CA  LEU A  91     4938   3165   8250    446     76    591       C  
ATOM    505  C   LEU A  91      94.170 199.884   6.635  1.00 41.56           C  
ANISOU  505  C   LEU A  91     4735   3109   7948    445     44    499       C  
ATOM    506  O   LEU A  91      93.639 200.820   7.245  1.00 39.47           O  
ANISOU  506  O   LEU A  91     4454   2913   7631    445     61    544       O  
ATOM    507  CB  LEU A  91      94.449 197.705   7.862  1.00 44.04           C  
ANISOU  507  CB  LEU A  91     5136   3227   8369    584     84    694       C  
ATOM    508  CG  LEU A  91      93.833 196.406   8.392  1.00 44.23           C  
ANISOU  508  CG  LEU A  91     5186   3108   8509    601    141    845       C  
ATOM    509  CD1 LEU A  91      94.901 195.522   9.010  1.00 38.76           C  
ANISOU  509  CD1 LEU A  91     4582   2339   7806    750    119    902       C  
ATOM    510  CD2 LEU A  91      92.754 196.721   9.410  1.00 44.43           C  
ANISOU  510  CD2 LEU A  91     5199   3145   8535    605    224   1012       C  
ATOM    511  N   PHE A  92      95.207 200.067   5.814  1.00 41.58           N  
ANISOU  511  N   PHE A  92     4733   3138   7928    445      5    371       N  
ATOM    512  CA  PHE A  92      95.642 201.412   5.452  1.00 38.64           C  
ANISOU  512  CA  PHE A  92     4330   2869   7484    420    -10    280       C  
ATOM    513  C   PHE A  92      94.574 202.139   4.645  1.00 37.36           C  
ANISOU  513  C   PHE A  92     4143   2752   7300    320     -3    253       C  
ATOM    514  O   PHE A  92      94.318 203.328   4.871  1.00 37.45           O  
ANISOU  514  O   PHE A  92     4135   2837   7256    303      0    250       O  
ATOM    515  CB  PHE A  92      96.942 201.344   4.657  1.00 39.23           C  
ANISOU  515  CB  PHE A  92     4391   2943   7571    436    -31    158       C  
ATOM    516  CG  PHE A  92      98.171 201.268   5.509  1.00 39.41           C  
ANISOU  516  CG  PHE A  92     4415   2969   7591    549    -54    143       C  
ATOM    517  CD1 PHE A  92      98.349 202.136   6.575  1.00 38.48           C  
ANISOU  517  CD1 PHE A  92     4284   2914   7421    616    -64    167       C  
ATOM    518  CD2 PHE A  92      99.153 200.332   5.240  1.00 37.94           C  
ANISOU  518  CD2 PHE A  92     4236   2725   7453    609    -75     88       C  
ATOM    519  CE1 PHE A  92      99.485 202.070   7.358  1.00 36.63           C  
ANISOU  519  CE1 PHE A  92     4045   2698   7177    752   -102    129       C  
ATOM    520  CE2 PHE A  92     100.288 200.261   6.019  1.00 36.69           C  
ANISOU  520  CE2 PHE A  92     4073   2579   7287    737   -109     58       C  
ATOM    521  CZ  PHE A  92     100.455 201.132   7.080  1.00 36.04           C  
ANISOU  521  CZ  PHE A  92     3978   2572   7144    815   -125     75       C  
ATOM    522  N   ILE A  93      93.949 201.439   3.693  1.00 38.47           N  
ANISOU  522  N   ILE A  93     4284   2842   7492    268    -10    223       N  
ATOM    523  CA  ILE A  93      92.907 202.037   2.863  1.00 38.47           C  
ANISOU  523  CA  ILE A  93     4270   2874   7471    201    -20    187       C  
ATOM    524  C   ILE A  93      91.744 202.522   3.717  1.00 40.22           C  
ANISOU  524  C   ILE A  93     4465   3124   7692    182      0    275       C  
ATOM    525  O   ILE A  93      91.107 203.534   3.398  1.00 39.15           O  
ANISOU  525  O   ILE A  93     4320   3049   7507    150    -11    250       O  
ATOM    526  CB  ILE A  93      92.462 201.021   1.792  1.00 39.10           C  
ANISOU  526  CB  ILE A  93     4346   2874   7635    173    -46    126       C  
ATOM    527  CG1 ILE A  93      93.504 200.951   0.677  1.00 39.25           C  
ANISOU  527  CG1 ILE A  93     4392   2886   7634    191    -65     14       C  
ATOM    528  CG2 ILE A  93      91.082 201.353   1.237  1.00 39.47           C  
ANISOU  528  CG2 ILE A  93     4369   2927   7702    122    -67    107       C  
ATOM    529  CD1 ILE A  93      93.307 199.786  -0.252  1.00 41.18           C  
ANISOU  529  CD1 ILE A  93     4629   3036   7981    188   -102    -63       C  
ATOM    530  N   VAL A  94      91.456 201.823   4.818  1.00 43.12           N  
ANISOU  530  N   VAL A  94     4823   3439   8121    212     35    385       N  
ATOM    531  CA  VAL A  94      90.455 202.307   5.763  1.00 41.49           C  
ANISOU  531  CA  VAL A  94     4585   3254   7924    208     71    481       C  
ATOM    532  C   VAL A  94      90.920 203.604   6.417  1.00 40.93           C  
ANISOU  532  C   VAL A  94     4522   3277   7754    249     64    479       C  
ATOM    533  O   VAL A  94      90.149 204.565   6.532  1.00 40.04           O  
ANISOU  533  O   VAL A  94     4379   3218   7618    223     62    478       O  
ATOM    534  CB  VAL A  94      90.140 201.226   6.810  1.00 39.15           C  
ANISOU  534  CB  VAL A  94     4288   2866   7721    247    134    625       C  
ATOM    535  CG1 VAL A  94      89.285 201.803   7.922  1.00 37.56           C  
ANISOU  535  CG1 VAL A  94     4055   2693   7523    268    191    743       C  
ATOM    536  CG2 VAL A  94      89.437 200.056   6.155  1.00 40.29           C  
ANISOU  536  CG2 VAL A  94     4395   2903   8009    190    144    617       C  
ATOM    537  N   ASN A  95      92.183 203.657   6.857  1.00 40.25           N  
ANISOU  537  N   ASN A  95     4467   3203   7625    320     51    464       N  
ATOM    538  CA  ASN A  95      92.725 204.895   7.409  1.00 40.31           C  
ANISOU  538  CA  ASN A  95     4464   3287   7566    364     30    430       C  
ATOM    539  C   ASN A  95      92.783 205.997   6.359  1.00 39.18           C  
ANISOU  539  C   ASN A  95     4298   3201   7387    290      6    320       C  
ATOM    540  O   ASN A  95      92.831 207.180   6.716  1.00 40.10           O  
ANISOU  540  O   ASN A  95     4390   3372   7475    297     -8    292       O  
ATOM    541  CB  ASN A  95      94.114 204.641   8.012  1.00 42.75           C  
ANISOU  541  CB  ASN A  95     4796   3589   7857    471      9    410       C  
ATOM    542  CG  ASN A  95      94.607 205.800   8.872  1.00 44.82           C  
ANISOU  542  CG  ASN A  95     5033   3925   8072    551    -22    371       C  
ATOM    543  OD1 ASN A  95      94.079 206.058   9.955  1.00 45.27           O  
ANISOU  543  OD1 ASN A  95     5094   4010   8095    636    -17    449       O  
ATOM    544  ND2 ASN A  95      95.640 206.489   8.399  1.00 45.65           N  
ANISOU  544  ND2 ASN A  95     5100   4060   8185    536    -52    245       N  
ATOM    545  N   LEU A  96      92.766 205.634   5.075  1.00 38.66           N  
ANISOU  545  N   LEU A  96     4249   3116   7325    233      1    262       N  
ATOM    546  CA  LEU A  96      92.624 206.619   4.012  1.00 37.46           C  
ANISOU  546  CA  LEU A  96     4103   3006   7126    184    -10    190       C  
ATOM    547  C   LEU A  96      91.194 207.142   3.923  1.00 38.15           C  
ANISOU  547  C   LEU A  96     4183   3115   7199    148    -21    216       C  
ATOM    548  O   LEU A  96      90.987 208.317   3.596  1.00 37.98           O  
ANISOU  548  O   LEU A  96     4166   3135   7129    131    -33    186       O  
ATOM    549  CB  LEU A  96      93.057 206.003   2.680  1.00 37.60           C  
ANISOU  549  CB  LEU A  96     4156   2984   7147    166    -11    125       C  
ATOM    550  CG  LEU A  96      93.618 206.903   1.580  1.00 37.88           C  
ANISOU  550  CG  LEU A  96     4218   3035   7138    149      2     56       C  
ATOM    551  CD1 LEU A  96      94.910 207.566   2.029  1.00 38.13           C  
ANISOU  551  CD1 LEU A  96     4207   3089   7191    169     29     26       C  
ATOM    552  CD2 LEU A  96      93.844 206.088   0.320  1.00 38.69           C  
ANISOU  552  CD2 LEU A  96     4365   3080   7257    147      1     -1       C  
ATOM    553  N   SER A  97      90.205 206.292   4.218  1.00 38.86           N  
ANISOU  553  N   SER A  97     4253   3164   7349    137    -16    272       N  
ATOM    554  CA  SER A  97      88.808 206.715   4.205  1.00 38.27           C  
ANISOU  554  CA  SER A  97     4146   3098   7296    106    -27    290       C  
ATOM    555  C   SER A  97      88.404 207.406   5.503  1.00 38.12           C  
ANISOU  555  C   SER A  97     4086   3113   7286    131     -7    358       C  
ATOM    556  O   SER A  97      87.491 208.239   5.494  1.00 39.37           O  
ANISOU  556  O   SER A  97     4216   3299   7445    114    -25    349       O  
ATOM    557  CB  SER A  97      87.894 205.515   3.945  1.00 40.26           C  
ANISOU  557  CB  SER A  97     4365   3274   7657     79    -22    310       C  
ATOM    558  OG  SER A  97      88.075 205.006   2.635  1.00 41.33           O  
ANISOU  558  OG  SER A  97     4534   3373   7797     62    -59    225       O  
ATOM    559  N   LEU A  98      89.058 207.070   6.621  1.00 37.02           N  
ANISOU  559  N   LEU A  98     3945   2963   7157    188     25    424       N  
ATOM    560  CA  LEU A  98      88.777 207.761   7.877  1.00 35.29           C  
ANISOU  560  CA  LEU A  98     3698   2772   6940    241     40    485       C  
ATOM    561  C   LEU A  98      89.101 209.245   7.772  1.00 35.18           C  
ANISOU  561  C   LEU A  98     3677   2822   6867    241     -7    398       C  
ATOM    562  O   LEU A  98      88.316 210.092   8.214  1.00 37.21           O  
ANISOU  562  O   LEU A  98     3899   3105   7133    246    -18    404       O  
ATOM    563  CB  LEU A  98      89.563 207.126   9.023  1.00 33.24           C  
ANISOU  563  CB  LEU A  98     3465   2490   6676    343     71    568       C  
ATOM    564  CG  LEU A  98      89.041 205.797   9.564  1.00 32.64           C  
ANISOU  564  CG  LEU A  98     3391   2337   6672    367    143    709       C  
ATOM    565  CD1 LEU A  98      90.035 205.228  10.555  1.00 34.32           C  
ANISOU  565  CD1 LEU A  98     3660   2538   6841    502    157    786       C  
ATOM    566  CD2 LEU A  98      87.681 205.984  10.214  1.00 31.12           C  
ANISOU  566  CD2 LEU A  98     3140   2139   6547    363    205    814       C  
ATOM    567  N   ALA A  99      90.251 209.583   7.186  1.00 32.95           N  
ANISOU  567  N   ALA A  99     3418   2557   6545    235    -30    315       N  
ATOM    568  CA  ALA A  99      90.587 210.988   6.999  1.00 31.17           C  
ANISOU  568  CA  ALA A  99     3175   2373   6297    224    -61    236       C  
ATOM    569  C   ALA A  99      89.684 211.650   5.966  1.00 28.19           C  
ANISOU  569  C   ALA A  99     2814   2009   5890    165    -77    211       C  
ATOM    570  O   ALA A  99      89.438 212.857   6.046  1.00 22.77           O  
ANISOU  570  O   ALA A  99     2109   1345   5197    162   -102    177       O  
ATOM    571  CB  ALA A  99      92.048 211.134   6.582  1.00 33.08           C  
ANISOU  571  CB  ALA A  99     3418   2611   6540    228    -60    165       C  
ATOM    572  N   ALA A 100      89.187 210.893   4.988  1.00 29.64           N  
ANISOU  572  N   ALA A 100     3035   2167   6058    131    -72    218       N  
ATOM    573  CA  ALA A 100      88.341 211.502   3.969  1.00 30.92           C  
ANISOU  573  CA  ALA A 100     3232   2331   6185    101   -101    188       C  
ATOM    574  C   ALA A 100      86.942 211.783   4.502  1.00 31.70           C  
ANISOU  574  C   ALA A 100     3279   2434   6331     98   -125    215       C  
ATOM    575  O   ALA A 100      86.273 212.710   4.030  1.00 30.03           O  
ANISOU  575  O   ALA A 100     3082   2231   6097     91   -163    185       O  
ATOM    576  CB  ALA A 100      88.275 210.606   2.731  1.00 32.76           C  
ANISOU  576  CB  ALA A 100     3522   2523   6405     82   -104    166       C  
ATOM    577  N   VAL A 101      86.475 210.980   5.461  1.00 33.47           N  
ANISOU  577  N   VAL A 101     3445   2640   6632    107    -97    278       N  
ATOM    578  CA  VAL A 101      85.200 211.261   6.111  1.00 33.11           C  
ANISOU  578  CA  VAL A 101     3329   2588   6662    108   -101    313       C  
ATOM    579  C   VAL A 101      85.320 212.468   7.034  1.00 32.41           C  
ANISOU  579  C   VAL A 101     3217   2538   6560    146   -117    304       C  
ATOM    580  O   VAL A 101      84.360 213.232   7.200  1.00 34.97           O  
ANISOU  580  O   VAL A 101     3500   2867   6919    146   -148    288       O  
ATOM    581  CB  VAL A 101      84.715 210.005   6.857  1.00 34.06           C  
ANISOU  581  CB  VAL A 101     3394   2656   6890    112    -35    409       C  
ATOM    582  CG1 VAL A 101      83.597 210.351   7.820  1.00 34.15           C  
ANISOU  582  CG1 VAL A 101     3320   2656   7001    128     -5    471       C  
ATOM    583  CG2 VAL A 101      84.248 208.959   5.867  1.00 34.65           C  
ANISOU  583  CG2 VAL A 101     3465   2677   7022     67    -40    386       C  
ATOM    584  N   LEU A 102      86.496 212.675   7.629  1.00 29.05           N  
ANISOU  584  N   LEU A 102     2809   2131   6096    187   -108    296       N  
ATOM    585  CA  LEU A 102      86.680 213.797   8.543  1.00 28.86           C  
ANISOU  585  CA  LEU A 102     2758   2137   6070    241   -138    260       C  
ATOM    586  C   LEU A 102      86.579 215.131   7.815  1.00 29.81           C  
ANISOU  586  C   LEU A 102     2886   2274   6167    206   -193    174       C  
ATOM    587  O   LEU A 102      86.009 216.091   8.346  1.00 33.60           O  
ANISOU  587  O   LEU A 102     3331   2767   6670    232   -233    139       O  
ATOM    588  CB  LEU A 102      88.026 213.678   9.254  1.00 27.58           C  
ANISOU  588  CB  LEU A 102     2608   1989   5884    308   -134    242       C  
ATOM    589  CG  LEU A 102      88.425 214.800  10.215  1.00 27.01           C  
ANISOU  589  CG  LEU A 102     2502   1961   5800    393   -184    162       C  
ATOM    590  CD1 LEU A 102      87.506 214.820  11.424  1.00 26.13           C  
ANISOU  590  CD1 LEU A 102     2358   1898   5671    507   -179    213       C  
ATOM    591  CD2 LEU A 102      89.875 214.639  10.640  1.00 25.01           C  
ANISOU  591  CD2 LEU A 102     2251   1724   5528    459   -196    109       C  
ATOM    592  N   VAL A 103      87.129 215.217   6.606  1.00 26.91           N  
ANISOU  592  N   VAL A 103     2573   1901   5751    163   -190    146       N  
ATOM    593  CA  VAL A 103      87.094 216.480   5.877  1.00 22.39           C  
ANISOU  593  CA  VAL A 103     2028   1327   5152    148   -221     96       C  
ATOM    594  C   VAL A 103      85.751 216.679   5.197  1.00 31.64           C  
ANISOU  594  C   VAL A 103     3226   2487   6308    135   -258    104       C  
ATOM    595  O   VAL A 103      85.255 217.807   5.099  1.00 31.70           O  
ANISOU  595  O   VAL A 103     3236   2489   6319    144   -302     73       O  
ATOM    596  CB  VAL A 103      88.254 216.551   4.869  1.00 30.47           C  
ANISOU  596  CB  VAL A 103     3112   2332   6132    127   -183     81       C  
ATOM    597  CG1 VAL A 103      89.541 216.882   5.584  1.00 30.39           C  
ANISOU  597  CG1 VAL A 103     3039   2324   6183    142   -169     37       C  
ATOM    598  CG2 VAL A 103      88.376 215.245   4.102  1.00 32.85           C  
ANISOU  598  CG2 VAL A 103     3469   2621   6391    112   -151    113       C  
ATOM    599  N   THR A 104      85.144 215.594   4.718  1.00 33.42           N  
ANISOU  599  N   THR A 104     3466   2698   6535    118   -249    135       N  
ATOM    600  CA  THR A 104      83.847 215.703   4.061  1.00 33.17           C  
ANISOU  600  CA  THR A 104     3440   2641   6520    111   -300    121       C  
ATOM    601  C   THR A 104      82.797 216.291   4.995  1.00 36.87           C  
ANISOU  601  C   THR A 104     3819   3118   7073    127   -338    112       C  
ATOM    602  O   THR A 104      81.904 217.019   4.547  1.00 38.41           O  
ANISOU  602  O   THR A 104     4019   3296   7278    135   -402     75       O  
ATOM    603  CB  THR A 104      83.405 214.331   3.549  1.00 28.27           C  
ANISOU  603  CB  THR A 104     2813   1989   5939     89   -290    136       C  
ATOM    604  OG1 THR A 104      84.472 213.728   2.806  1.00 27.66           O  
ANISOU  604  OG1 THR A 104     2814   1902   5792     82   -255    135       O  
ATOM    605  CG2 THR A 104      82.198 214.472   2.642  1.00 23.73           C  
ANISOU  605  CG2 THR A 104     2244   1373   5397     89   -363     92       C  
ATOM    606  N   ILE A 105      82.912 216.017   6.291  1.00 38.51           N  
ANISOU  606  N   ILE A 105     3953   3340   7341    143   -301    144       N  
ATOM    607  CA  ILE A 105      81.958 216.503   7.284  1.00 36.69           C  
ANISOU  607  CA  ILE A 105     3638   3108   7193    174   -321    138       C  
ATOM    608  C   ILE A 105      82.324 217.896   7.778  1.00 35.50           C  
ANISOU  608  C   ILE A 105     3495   2987   7008    214   -370     70       C  
ATOM    609  O   ILE A 105      81.480 218.796   7.818  1.00 36.39           O  
ANISOU  609  O   ILE A 105     3582   3098   7145    232   -432     16       O  
ATOM    610  CB  ILE A 105      81.865 215.500   8.455  1.00 35.69           C  
ANISOU  610  CB  ILE A 105     3449   2972   7139    203   -239    226       C  
ATOM    611  CG1 ILE A 105      81.316 214.157   7.970  1.00 34.65           C  
ANISOU  611  CG1 ILE A 105     3285   2790   7092    153   -189    288       C  
ATOM    612  CG2 ILE A 105      81.018 216.078   9.586  1.00 35.72           C  
ANISOU  612  CG2 ILE A 105     3378   2995   7199    275   -240    224       C  
ATOM    613  CD1 ILE A 105      81.408 213.051   8.998  1.00 36.72           C  
ANISOU  613  CD1 ILE A 105     3502   3022   7426    181    -78    414       C  
ATOM    614  N   THR A 106      83.581 218.099   8.163  1.00 35.41           N  
ANISOU  614  N   THR A 106     3506   2995   6954    232   -351     55       N  
ATOM    615  CA  THR A 106      83.984 219.328   8.838  1.00 37.68           C  
ANISOU  615  CA  THR A 106     3772   3302   7242    278   -400    -29       C  
ATOM    616  C   THR A 106      84.439 220.418   7.870  1.00 39.74           C  
ANISOU  616  C   THR A 106     4072   3537   7490    240   -433    -76       C  
ATOM    617  O   THR A 106      84.038 221.579   8.007  1.00 42.70           O  
ANISOU  617  O   THR A 106     4427   3904   7893    259   -494   -141       O  
ATOM    618  CB  THR A 106      85.102 219.031   9.851  1.00 36.85           C  
ANISOU  618  CB  THR A 106     3651   3228   7121    340   -374    -43       C  
ATOM    619  OG1 THR A 106      86.258 218.542   9.163  1.00 36.56           O  
ANISOU  619  OG1 THR A 106     3651   3168   7070    288   -336    -23       O  
ATOM    620  CG2 THR A 106      84.644 217.988  10.861  1.00 35.37           C  
ANISOU  620  CG2 THR A 106     3439   3081   6917    424   -322     38       C  
ATOM    621  N   CYS A 107      85.270 220.065   6.888  1.00 38.88           N  
ANISOU  621  N   CYS A 107     4024   3412   7337    199   -386    -39       N  
ATOM    622  CA  CYS A 107      85.921 221.067   6.050  1.00 38.34           C  
ANISOU  622  CA  CYS A 107     4002   3308   7258    183   -380    -58       C  
ATOM    623  C   CYS A 107      85.181 221.349   4.748  1.00 34.32           C  
ANISOU  623  C   CYS A 107     3599   2760   6680    175   -388    -19       C  
ATOM    624  O   CYS A 107      85.279 222.465   4.221  1.00 31.37           O  
ANISOU  624  O   CYS A 107     3274   2337   6309    182   -396    -27       O  
ATOM    625  CB  CYS A 107      87.352 220.628   5.732  1.00 42.07           C  
ANISOU  625  CB  CYS A 107     4488   3771   7724    161   -311    -47       C  
ATOM    626  SG  CYS A 107      88.371 220.295   7.189  1.00 43.82           S  
ANISOU  626  SG  CYS A 107     4601   4021   8029    188   -318   -111       S  
ATOM    627  N   LEU A 108      84.455 220.368   4.209  1.00 33.81           N  
ANISOU  627  N   LEU A 108     3575   2703   6569    168   -389     18       N  
ATOM    628  CA  LEU A 108      83.800 220.558   2.915  1.00 32.53           C  
ANISOU  628  CA  LEU A 108     3523   2492   6345    177   -411     37       C  
ATOM    629  C   LEU A 108      82.726 221.640   2.943  1.00 32.81           C  
ANISOU  629  C   LEU A 108     3553   2503   6409    212   -493      5       C  
ATOM    630  O   LEU A 108      82.744 222.513   2.056  1.00 32.77           O  
ANISOU  630  O   LEU A 108     3657   2434   6362    236   -499     22       O  
ATOM    631  CB  LEU A 108      83.239 219.220   2.415  1.00 30.03           C  
ANISOU  631  CB  LEU A 108     3217   2178   6013    165   -415     53       C  
ATOM    632  CG  LEU A 108      82.580 219.209   1.031  1.00 30.36           C  
ANISOU  632  CG  LEU A 108     3370   2158   6007    190   -457     53       C  
ATOM    633  CD1 LEU A 108      82.869 217.898   0.322  1.00 33.44           C  
ANISOU  633  CD1 LEU A 108     3797   2533   6376    174   -429     60       C  
ATOM    634  CD2 LEU A 108      81.076 219.434   1.126  1.00 27.23           C  
ANISOU  634  CD2 LEU A 108     2915   1753   5677    217   -560      9       C  
ATOM    635  N   PRO A 109      81.773 221.654   3.885  1.00 31.95           N  
ANISOU  635  N   PRO A 109     3334   2429   6377    224   -554    -37       N  
ATOM    636  CA  PRO A 109      80.767 222.730   3.861  1.00 31.03           C  
ANISOU  636  CA  PRO A 109     3211   2287   6290    265   -643    -84       C  
ATOM    637  C   PRO A 109      81.357 224.113   4.078  1.00 32.01           C  
ANISOU  637  C   PRO A 109     3352   2382   6430    282   -648   -106       C  
ATOM    638  O   PRO A 109      80.851 225.089   3.508  1.00 31.04           O  
ANISOU  638  O   PRO A 109     3293   2203   6299    320   -699   -114       O  
ATOM    639  CB  PRO A 109      79.805 222.338   4.992  1.00 30.01           C  
ANISOU  639  CB  PRO A 109     2945   2201   6254    271   -684   -133       C  
ATOM    640  CG  PRO A 109      80.045 220.887   5.221  1.00 30.47           C  
ANISOU  640  CG  PRO A 109     2966   2282   6329    233   -614    -83       C  
ATOM    641  CD  PRO A 109      81.499 220.691   4.967  1.00 31.41           C  
ANISOU  641  CD  PRO A 109     3152   2408   6376    210   -539    -40       C  
ATOM    642  N   ALA A 110      82.422 224.229   4.876  1.00 32.84           N  
ANISOU  642  N   ALA A 110     3394   2509   6574    262   -603   -124       N  
ATOM    643  CA  ALA A 110      83.009 225.539   5.137  1.00 36.03           C  
ANISOU  643  CA  ALA A 110     3779   2870   7040    273   -615   -167       C  
ATOM    644  C   ALA A 110      83.747 226.083   3.920  1.00 36.69           C  
ANISOU  644  C   ALA A 110     3993   2864   7084    261   -546    -98       C  
ATOM    645  O   ALA A 110      83.845 227.304   3.749  1.00 38.91           O  
ANISOU  645  O   ALA A 110     4297   3068   7419    277   -559   -109       O  
ATOM    646  CB  ALA A 110      83.949 225.461   6.340  1.00 37.28           C  
ANISOU  646  CB  ALA A 110     3819   3070   7277    262   -604   -232       C  
ATOM    647  N   THR A 111      84.275 225.201   3.070  1.00 35.65           N  
ANISOU  647  N   THR A 111     3954   2727   6867    236   -468    -28       N  
ATOM    648  CA  THR A 111      84.915 225.650   1.840  1.00 35.94           C  
ANISOU  648  CA  THR A 111     4141   2662   6855    233   -392     44       C  
ATOM    649  C   THR A 111      83.889 226.090   0.804  1.00 36.75           C  
ANISOU  649  C   THR A 111     4390   2689   6884    290   -432     90       C  
ATOM    650  O   THR A 111      84.153 227.017   0.029  1.00 38.54           O  
ANISOU  650  O   THR A 111     4742   2800   7103    313   -392    146       O  
ATOM    651  CB  THR A 111      85.804 224.540   1.272  1.00 35.05           C  
ANISOU  651  CB  THR A 111     4078   2562   6676    198   -305     88       C  
ATOM    652  OG1 THR A 111      86.701 224.078   2.289  1.00 34.74           O  
ANISOU  652  OG1 THR A 111     3897   2592   6710    164   -282     40       O  
ATOM    653  CG2 THR A 111      86.619 225.051   0.091  1.00 34.84           C  
ANISOU  653  CG2 THR A 111     4198   2417   6621    193   -212    160       C  
ATOM    654  N   LEU A 112      82.719 225.448   0.778  1.00 35.34           N  
ANISOU  654  N   LEU A 112     4195   2562   6669    319   -513     66       N  
ATOM    655  CA  LEU A 112      81.665 225.870  -0.138  1.00 37.86           C  
ANISOU  655  CA  LEU A 112     4629   2814   6940    395   -580     86       C  
ATOM    656  C   LEU A 112      81.222 227.298   0.155  1.00 42.62           C  
ANISOU  656  C   LEU A 112     5227   3362   7605    438   -635     65       C  
ATOM    657  O   LEU A 112      81.006 228.093  -0.768  1.00 46.30           O  
ANISOU  657  O   LEU A 112     5843   3717   8031    507   -633    125       O  
ATOM    658  CB  LEU A 112      80.481 224.910  -0.043  1.00 37.32           C  
ANISOU  658  CB  LEU A 112     4488   2815   6876    410   -677     32       C  
ATOM    659  CG  LEU A 112      79.229 225.258  -0.844  1.00 39.09           C  
ANISOU  659  CG  LEU A 112     4783   2990   7080    503   -790     14       C  
ATOM    660  CD1 LEU A 112      79.546 225.385  -2.326  1.00 41.82           C  
ANISOU  660  CD1 LEU A 112     5337   3228   7324    578   -749     99       C  
ATOM    661  CD2 LEU A 112      78.181 224.192  -0.609  1.00 36.40           C  
ANISOU  661  CD2 LEU A 112     4322   2715   6792    494   -885    -67       C  
ATOM    662  N   VAL A 113      81.093 227.643   1.438  1.00 41.86           N  
ANISOU  662  N   VAL A 113     4965   3332   7609    411   -685    -18       N  
ATOM    663  CA  VAL A 113      80.635 228.977   1.809  1.00 41.87           C  
ANISOU  663  CA  VAL A 113     4938   3283   7688    454   -755    -63       C  
ATOM    664  C   VAL A 113      81.704 230.016   1.506  1.00 42.32           C  
ANISOU  664  C   VAL A 113     5065   3221   7792    440   -669    -11       C  
ATOM    665  O   VAL A 113      81.407 231.101   0.991  1.00 31.89           O  
ANISOU  665  O   VAL A 113     3841   1784   6490    495   -685     22       O  
ATOM    666  CB  VAL A 113      80.227 229.006   3.292  1.00 28.75           C  
ANISOU  666  CB  VAL A 113     3078   1720   6127    439   -836   -184       C  
ATOM    667  CG1 VAL A 113      79.693 230.381   3.665  1.00 31.47           C  
ANISOU  667  CG1 VAL A 113     3387   2013   6558    489   -926   -253       C  
ATOM    668  CG2 VAL A 113      79.197 227.929   3.577  1.00 27.98           C  
ANISOU  668  CG2 VAL A 113     2912   1714   6003    443   -896   -223       C  
ATOM    669  N   VAL A 114      82.964 229.704   1.816  1.00 41.04           N  
ANISOU  669  N   VAL A 114     4852   3074   7669    371   -577     -5       N  
ATOM    670  CA  VAL A 114      84.023 230.703   1.706  1.00 40.60           C  
ANISOU  670  CA  VAL A 114     4810   2903   7715    343   -501     17       C  
ATOM    671  C   VAL A 114      84.328 231.016   0.246  1.00 40.01           C  
ANISOU  671  C   VAL A 114     4964   2679   7557    365   -404    154       C  
ATOM    672  O   VAL A 114      84.521 232.180  -0.123  1.00 40.76           O  
ANISOU  672  O   VAL A 114     5135   2627   7725    382   -373    199       O  
ATOM    673  CB  VAL A 114      85.279 230.234   2.465  1.00 39.79           C  
ANISOU  673  CB  VAL A 114     4561   2861   7698    272   -444    -34       C  
ATOM    674  CG1 VAL A 114      86.501 231.007   2.001  1.00 41.99           C  
ANISOU  674  CG1 VAL A 114     4867   3005   8082    230   -334      8       C  
ATOM    675  CG2 VAL A 114      85.080 230.412   3.961  1.00 39.07           C  
ANISOU  675  CG2 VAL A 114     4258   2862   7727    277   -547   -175       C  
ATOM    676  N   ASP A 115      84.366 229.995  -0.609  1.00 40.89           N  
ANISOU  676  N   ASP A 115     5196   2813   7528    372   -357    223       N  
ATOM    677  CA  ASP A 115      84.708 230.221  -2.008  1.00 44.12           C  
ANISOU  677  CA  ASP A 115     5836   3076   7851    408   -267    355       C  
ATOM    678  C   ASP A 115      83.593 230.907  -2.790  1.00 45.87           C  
ANISOU  678  C   ASP A 115     6229   3199   8000    532   -325    418       C  
ATOM    679  O   ASP A 115      83.805 231.257  -3.957  1.00 48.74           O  
ANISOU  679  O   ASP A 115     6812   3418   8288    595   -260    546       O  
ATOM    680  CB  ASP A 115      85.083 228.895  -2.676  1.00 46.87           C  
ANISOU  680  CB  ASP A 115     6251   3474   8081    395   -217    393       C  
ATOM    681  CG  ASP A 115      86.398 228.329  -2.153  1.00 51.51           C  
ANISOU  681  CG  ASP A 115     6707   4123   8742    290   -134    358       C  
ATOM    682  OD1 ASP A 115      87.047 228.987  -1.311  1.00 53.54           O  
ANISOU  682  OD1 ASP A 115     6818   4377   9147    236   -115    304       O  
ATOM    683  OD2 ASP A 115      86.785 227.223  -2.590  1.00 52.47           O  
ANISOU  683  OD2 ASP A 115     6858   4289   8788    273    -95    375       O  
ATOM    684  N   ILE A 116      82.427 231.114  -2.185  1.00 43.88           N  
ANISOU  684  N   ILE A 116     5881   3017   7774    579   -452    335       N  
ATOM    685  CA  ILE A 116      81.324 231.837  -2.806  1.00 44.43           C  
ANISOU  685  CA  ILE A 116     6074   3006   7802    710   -524    376       C  
ATOM    686  C   ILE A 116      81.099 233.185  -2.131  1.00 44.40           C  
ANISOU  686  C   ILE A 116     6001   2934   7935    718   -573    331       C  
ATOM    687  O   ILE A 116      81.013 234.217  -2.798  1.00 49.39           O  
ANISOU  687  O   ILE A 116     6792   3402   8570    798   -545    423       O  
ATOM    688  CB  ILE A 116      80.032 230.990  -2.794  1.00 43.21           C  
ANISOU  688  CB  ILE A 116     5851   2978   7589    769   -660    302       C  
ATOM    689  CG1 ILE A 116      80.248 229.687  -3.560  1.00 40.47           C  
ANISOU  689  CG1 ILE A 116     5573   2672   7133    772   -620    341       C  
ATOM    690  CG2 ILE A 116      78.866 231.769  -3.390  1.00 45.23           C  
ANISOU  690  CG2 ILE A 116     6199   3166   7822    916   -762    324       C  
ATOM    691  CD1 ILE A 116      79.024 228.813  -3.606  1.00 40.46           C  
ANISOU  691  CD1 ILE A 116     5488   2776   7110    818   -767    253       C  
ATOM    692  N   THR A 117      81.008 233.191  -0.800  1.00 41.40           N  
ANISOU  692  N   THR A 117     5387   2670   7673    647   -649    192       N  
ATOM    693  CA  THR A 117      80.753 234.427  -0.072  1.00 44.73           C  
ANISOU  693  CA  THR A 117     5715   3037   8243    660   -720    119       C  
ATOM    694  C   THR A 117      82.023 235.231   0.176  1.00 46.34           C  
ANISOU  694  C   THR A 117     5888   3125   8594    586   -622    135       C  
ATOM    695  O   THR A 117      81.947 236.451   0.361  1.00 50.11           O  
ANISOU  695  O   THR A 117     6355   3481   9203    612   -650    117       O  
ATOM    696  CB  THR A 117      80.076 234.122   1.266  1.00 43.33           C  
ANISOU  696  CB  THR A 117     5302   3027   8135    636   -856    -48       C  
ATOM    697  OG1 THR A 117      80.897 233.224   2.022  1.00 42.81           O  
ANISOU  697  OG1 THR A 117     5100   3076   8089    543   -809    -95       O  
ATOM    698  CG2 THR A 117      78.714 233.487   1.043  1.00 41.22           C  
ANISOU  698  CG2 THR A 117     5043   2852   7768    704   -969    -81       C  
ATOM    699  N   GLU A 118      83.186 234.576   0.190  1.00 43.91           N  
ANISOU  699  N   GLU A 118     5547   2846   8289    496   -514    157       N  
ATOM    700  CA  GLU A 118      84.454 235.227   0.525  1.00 44.84           C  
ANISOU  700  CA  GLU A 118     5577   2873   8587    414   -430    143       C  
ATOM    701  C   GLU A 118      84.398 235.853   1.918  1.00 43.97           C  
ANISOU  701  C   GLU A 118     5217   2815   8674    398   -537    -27       C  
ATOM    702  O   GLU A 118      84.947 236.928   2.161  1.00 39.81           O  
ANISOU  702  O   GLU A 118     4621   2160   8344    375   -519    -59       O  
ATOM    703  CB  GLU A 118      84.840 236.264  -0.532  1.00 51.50           C  
ANISOU  703  CB  GLU A 118     6617   3480   9470    433   -330    283       C  
ATOM    704  CG  GLU A 118      84.903 235.690  -1.938  1.00 57.14           C  
ANISOU  704  CG  GLU A 118     7595   4132   9984    472   -238    451       C  
ATOM    705  CD  GLU A 118      84.934 236.756  -3.017  1.00 63.74           C  
ANISOU  705  CD  GLU A 118     8670   4726  10821    533   -173    612       C  
ATOM    706  OE1 GLU A 118      85.715 237.722  -2.889  1.00 66.83           O  
ANISOU  706  OE1 GLU A 118     9012   4969  11413    468   -102    632       O  
ATOM    707  OE2 GLU A 118      84.171 236.627  -3.997  1.00 65.08           O  
ANISOU  707  OE2 GLU A 118     9075   4849  10804    657   -195    720       O  
ATOM    708  N   THR A 119      83.727 235.168   2.841  1.00 44.43           N  
ANISOU  708  N   THR A 119     5136   3055   8691    412   -651   -141       N  
ATOM    709  CA  THR A 119      83.553 235.643   4.204  1.00 44.74           C  
ANISOU  709  CA  THR A 119     4949   3163   8887    417   -776   -317       C  
ATOM    710  C   THR A 119      83.669 234.457   5.151  1.00 44.11           C  
ANISOU  710  C   THR A 119     4727   3273   8758    391   -812   -405       C  
ATOM    711  O   THR A 119      83.421 233.313   4.763  1.00 43.45           O  
ANISOU  711  O   THR A 119     4722   3274   8511    384   -775   -333       O  
ATOM    712  CB  THR A 119      82.191 236.339   4.385  1.00 42.42           C  
ANISOU  712  CB  THR A 119     4664   2862   8593    499   -915   -375       C  
ATOM    713  OG1 THR A 119      81.933 237.190   3.261  1.00 44.29           O  
ANISOU  713  OG1 THR A 119     5096   2918   8813    546   -869   -250       O  
ATOM    714  CG2 THR A 119      82.175 237.178   5.653  1.00 40.97           C  
ANISOU  714  CG2 THR A 119     4266   2697   8603    509  -1038   -564       C  
ATOM    715  N   TRP A 120      84.052 234.730   6.397  1.00 44.30           N  
ANISOU  715  N   TRP A 120     4547   3353   8930    384   -888   -567       N  
ATOM    716  CA  TRP A 120      84.154 233.696   7.422  1.00 44.38           C  
ANISOU  716  CA  TRP A 120     4440   3526   8896    376   -929   -661       C  
ATOM    717  C   TRP A 120      83.026 233.894   8.426  1.00 46.29           C  
ANISOU  717  C   TRP A 120     4602   3857   9128    435  -1079   -805       C  
ATOM    718  O   TRP A 120      82.989 234.905   9.136  1.00 49.84           O  
ANISOU  718  O   TRP A 120     4941   4281   9716    462  -1178   -954       O  
ATOM    719  CB  TRP A 120      85.515 233.727   8.111  1.00 33.46           C  
ANISOU  719  CB  TRP A 120     2904   2147   7662    338   -907   -758       C  
ATOM    720  CG  TRP A 120      85.698 232.573   9.038  1.00 38.09           C  
ANISOU  720  CG  TRP A 120     3423   2878   8169    338   -933   -831       C  
ATOM    721  CD1 TRP A 120      85.687 232.606  10.401  1.00 38.22           C  
ANISOU  721  CD1 TRP A 120     3320   2980   8223    373  -1045  -1024       C  
ATOM    722  CD2 TRP A 120      85.887 231.201   8.670  1.00 40.09           C  
ANISOU  722  CD2 TRP A 120     3761   3197   8273    313   -843   -715       C  
ATOM    723  NE1 TRP A 120      85.873 231.339  10.905  1.00 38.48           N  
ANISOU  723  NE1 TRP A 120     3382   3116   8124    379  -1015  -1018       N  
ATOM    724  CE2 TRP A 120      85.998 230.459   9.862  1.00 39.25           C  
ANISOU  724  CE2 TRP A 120     3583   3200   8130    336   -895   -827       C  
ATOM    725  CE3 TRP A 120      85.981 230.529   7.446  1.00 42.57           C  
ANISOU  725  CE3 TRP A 120     4221   3484   8469    281   -725   -539       C  
ATOM    726  CZ2 TRP A 120      86.197 229.078   9.868  1.00 40.00           C  
ANISOU  726  CZ2 TRP A 120     3734   3365   8101    326   -827   -748       C  
ATOM    727  CZ3 TRP A 120      86.180 229.156   7.453  1.00 41.20           C  
ANISOU  727  CZ3 TRP A 120     4079   3393   8181    265   -673   -484       C  
ATOM    728  CH2 TRP A 120      86.285 228.447   8.656  1.00 39.49           C  
ANISOU  728  CH2 TRP A 120     3775   3272   7959    284   -722   -579       C  
ATOM    729  N   PHE A 121      82.115 232.923   8.494  1.00 44.82           N  
ANISOU  729  N   PHE A 121     4470   3773   8788    455  -1091   -775       N  
ATOM    730  CA  PHE A 121      80.933 233.018   9.341  1.00 44.43           C  
ANISOU  730  CA  PHE A 121     4372   3807   8702    516  -1203   -900       C  
ATOM    731  C   PHE A 121      81.028 232.172  10.607  1.00 44.10           C  
ANISOU  731  C   PHE A 121     4266   3896   8593    539  -1206  -1004       C  
ATOM    732  O   PHE A 121      80.054 232.108  11.364  1.00 44.22           O  
ANISOU  732  O   PHE A 121     4265   4000   8537    610  -1258  -1097       O  
ATOM    733  CB  PHE A 121      79.685 232.599   8.557  1.00 43.52           C  
ANISOU  733  CB  PHE A 121     4359   3702   8473    541  -1208   -807       C  
ATOM    734  CG  PHE A 121      79.410 233.433   7.337  1.00 43.33           C  
ANISOU  734  CG  PHE A 121     4447   3552   8465    557  -1211   -712       C  
ATOM    735  CD1 PHE A 121      78.595 234.551   7.413  1.00 43.17           C  
ANISOU  735  CD1 PHE A 121     4413   3482   8507    618  -1320   -793       C  
ATOM    736  CD2 PHE A 121      79.941 233.081   6.109  1.00 44.13           C  
ANISOU  736  CD2 PHE A 121     4690   3580   8498    525  -1100   -546       C  
ATOM    737  CE1 PHE A 121      78.330 235.310   6.288  1.00 44.63           C  
ANISOU  737  CE1 PHE A 121     4730   3535   8693    652  -1316   -694       C  
ATOM    738  CE2 PHE A 121      79.679 233.836   4.982  1.00 45.48           C  
ANISOU  738  CE2 PHE A 121     5008   3622   8651    562  -1087   -452       C  
ATOM    739  CZ  PHE A 121      78.873 234.951   5.071  1.00 45.73           C  
ANISOU  739  CZ  PHE A 121     5031   3594   8751    628  -1194   -519       C  
ATOM    740  N   PHE A 122      82.170 231.537  10.867  1.00 44.47           N  
ANISOU  740  N   PHE A 122     4291   3962   8642    503  -1139   -988       N  
ATOM    741  CA  PHE A 122      82.239 230.461  11.847  1.00 43.82           C  
ANISOU  741  CA  PHE A 122     4206   4004   8439    550  -1104  -1021       C  
ATOM    742  C   PHE A 122      83.053 230.794  13.092  1.00 45.38           C  
ANISOU  742  C   PHE A 122     4326   4264   8653    609  -1151  -1198       C  
ATOM    743  O   PHE A 122      83.179 229.937  13.976  1.00 44.96           O  
ANISOU  743  O   PHE A 122     4281   4345   8458    692  -1110  -1210       O  
ATOM    744  CB  PHE A 122      82.797 229.201  11.180  1.00 41.90           C  
ANISOU  744  CB  PHE A 122     4025   3757   8140    489   -990   -856       C  
ATOM    745  CG  PHE A 122      82.145 228.883   9.864  1.00 43.55           C  
ANISOU  745  CG  PHE A 122     4319   3913   8316    441   -949   -701       C  
ATOM    746  CD1 PHE A 122      82.816 229.098   8.672  1.00 45.65           C  
ANISOU  746  CD1 PHE A 122     4642   4092   8610    383   -890   -594       C  
ATOM    747  CD2 PHE A 122      80.854 228.382   9.817  1.00 43.60           C  
ANISOU  747  CD2 PHE A 122     4354   3965   8248    473   -961   -672       C  
ATOM    748  CE1 PHE A 122      82.216 228.807   7.457  1.00 46.05           C  
ANISOU  748  CE1 PHE A 122     4808   4108   8580    370   -854   -469       C  
ATOM    749  CE2 PHE A 122      80.246 228.089   8.605  1.00 43.14           C  
ANISOU  749  CE2 PHE A 122     4374   3863   8156    442   -945   -561       C  
ATOM    750  CZ  PHE A 122      80.928 228.302   7.425  1.00 44.10           C  
ANISOU  750  CZ  PHE A 122     4580   3906   8270    399   -896   -463       C  
ATOM    751  N   GLY A 123      83.610 231.997  13.194  1.00 41.31           N  
ANISOU  751  N   GLY A 123     4533   4280   6882   1308   -225    424       N  
ATOM    752  CA  GLY A 123      84.247 232.437  14.417  1.00 42.76           C  
ANISOU  752  CA  GLY A 123     4625   4541   7080   1365   -223    323       C  
ATOM    753  C   GLY A 123      85.736 232.139  14.469  1.00 43.83           C  
ANISOU  753  C   GLY A 123     4713   4634   7307   1338   -209    201       C  
ATOM    754  O   GLY A 123      86.295 231.396  13.660  1.00 44.89           O  
ANISOU  754  O   GLY A 123     4883   4687   7487   1266   -186    229       O  
ATOM    755  N   GLN A 124      86.381 232.736  15.474  1.00 44.80           N  
ANISOU  755  N   GLN A 124     4742   4823   7458   1407   -235     35       N  
ATOM    756  CA  GLN A 124      87.833 232.645  15.595  1.00 46.53           C  
ANISOU  756  CA  GLN A 124     4878   5005   7797   1383   -240   -158       C  
ATOM    757  C   GLN A 124      88.286 231.219  15.887  1.00 46.13           C  
ANISOU  757  C   GLN A 124     4823   5052   7652   1422   -310   -102       C  
ATOM    758  O   GLN A 124      89.299 230.759  15.346  1.00 45.46           O  
ANISOU  758  O   GLN A 124     4713   4881   7680   1348   -290   -176       O  
ATOM    759  CB  GLN A 124      88.318 233.596  16.689  1.00 50.20           C  
ANISOU  759  CB  GLN A 124     5233   5549   8292   1461   -294   -394       C  
ATOM    760  CG  GLN A 124      89.800 233.488  17.004  1.00 55.45           C  
ANISOU  760  CG  GLN A 124     5781   6209   9079   1445   -345   -652       C  
ATOM    761  CD  GLN A 124      90.663 234.275  16.038  1.00 59.31           C  
ANISOU  761  CD  GLN A 124     6216   6454   9866   1271   -191   -806       C  
ATOM    762  OE1 GLN A 124      91.535 233.719  15.371  1.00 59.24           O  
ANISOU  762  OE1 GLN A 124     6191   6339   9981   1177   -133   -838       O  
ATOM    763  NE2 GLN A 124      90.427 235.578  15.963  1.00 61.12           N  
ANISOU  763  NE2 GLN A 124     6426   6582  10217   1226    -91   -888       N  
ATOM    764  N   SER A 125      87.546 230.502  16.737  1.00 46.30           N  
ANISOU  764  N   SER A 125     4877   5236   7478   1547   -358     38       N  
ATOM    765  CA  SER A 125      87.956 229.155  17.125  1.00 45.40           C  
ANISOU  765  CA  SER A 125     4781   5206   7265   1622   -386    109       C  
ATOM    766  C   SER A 125      87.935 228.201  15.936  1.00 42.73           C  
ANISOU  766  C   SER A 125     4490   4746   7001   1470   -339    227       C  
ATOM    767  O   SER A 125      88.877 227.427  15.735  1.00 42.80           O  
ANISOU  767  O   SER A 125     4483   4733   7048   1451   -353    189       O  
ATOM    768  CB  SER A 125      87.060 228.639  18.252  1.00 47.90           C  
ANISOU  768  CB  SER A 125     5150   5673   7376   1815   -373    264       C  
ATOM    769  OG  SER A 125      87.376 229.272  19.481  1.00 50.49           O  
ANISOU  769  OG  SER A 125     5424   6096   7664   1946   -420    167       O  
ATOM    770  N   LEU A 126      86.871 228.241  15.132  1.00 42.51           N  
ANISOU  770  N   LEU A 126     4516   4642   6993   1369   -292    355       N  
ATOM    771  CA  LEU A 126      86.802 227.380  13.956  1.00 40.94           C  
ANISOU  771  CA  LEU A 126     4361   4338   6855   1242   -263    442       C  
ATOM    772  C   LEU A 126      87.703 227.856  12.823  1.00 38.58           C  
ANISOU  772  C   LEU A 126     4090   3883   6687   1148   -224    354       C  
ATOM    773  O   LEU A 126      87.934 227.092  11.880  1.00 38.22           O  
ANISOU  773  O   LEU A 126     4092   3754   6674   1073   -203    400       O  
ATOM    774  CB  LEU A 126      85.357 227.272  13.463  1.00 42.30           C  
ANISOU  774  CB  LEU A 126     4565   4495   7011   1199   -254    554       C  
ATOM    775  CG  LEU A 126      84.448 226.324  14.249  1.00 44.86           C  
ANISOU  775  CG  LEU A 126     4853   4892   7301   1241   -223    662       C  
ATOM    776  CD1 LEU A 126      82.989 226.551  13.895  1.00 45.14           C  
ANISOU  776  CD1 LEU A 126     4863   4902   7387   1209   -220    706       C  
ATOM    777  CD2 LEU A 126      84.841 224.882  13.981  1.00 45.42           C  
ANISOU  777  CD2 LEU A 126     4914   4925   7420   1193   -191    720       C  
ATOM    778  N   CYS A 127      88.211 229.090  12.890  1.00 37.42           N  
ANISOU  778  N   CYS A 127     3919   3673   6626   1157   -187    220       N  
ATOM    779  CA  CYS A 127      89.194 229.557  11.918  1.00 38.04           C  
ANISOU  779  CA  CYS A 127     4030   3564   6859   1072    -73    125       C  
ATOM    780  C   CYS A 127      90.551 228.892  12.111  1.00 38.02           C  
ANISOU  780  C   CYS A 127     3936   3549   6961   1041    -79      0       C  
ATOM    781  O   CYS A 127      91.349 228.845  11.168  1.00 37.15           O  
ANISOU  781  O   CYS A 127     3866   3281   6968    949     39    -39       O  
ATOM    782  CB  CYS A 127      89.325 231.081  12.004  1.00 39.40           C  
ANISOU  782  CB  CYS A 127     4189   3649   7133   1073     20      1       C  
ATOM    783  SG  CYS A 127      90.696 231.824  11.076  1.00 39.35           S  
ANISOU  783  SG  CYS A 127     4203   3399   7350    953    250   -149       S  
ATOM    784  N   LYS A 128      90.826 228.377  13.309  1.00 38.57           N  
ANISOU  784  N   LYS A 128     3907   3789   6960   1137   -202    -62       N  
ATOM    785  CA  LYS A 128      92.035 227.603  13.569  1.00 36.47           C  
ANISOU  785  CA  LYS A 128     3564   3547   6748   1145   -247   -179       C  
ATOM    786  C   LYS A 128      91.799 226.110  13.397  1.00 37.44           C  
ANISOU  786  C   LYS A 128     3749   3720   6758   1153   -274      3       C  
ATOM    787  O   LYS A 128      92.638 225.414  12.819  1.00 36.44           O  
ANISOU  787  O   LYS A 128     3612   3514   6721   1085   -246    -25       O  
ATOM    788  CB  LYS A 128      92.548 227.877  14.986  1.00 36.16           C  
ANISOU  788  CB  LYS A 128     3420   3680   6640   1294   -376   -367       C  
ATOM    789  CG  LYS A 128      92.435 229.320  15.431  1.00 37.09           C  
ANISOU  789  CG  LYS A 128     3473   3793   6825   1306   -376   -534       C  
ATOM    790  CD  LYS A 128      93.707 230.094  15.154  1.00 36.67           C  
ANISOU  790  CD  LYS A 128     3287   3598   7049   1193   -325   -826       C  
ATOM    791  CE  LYS A 128      94.563 230.224  16.406  1.00 37.25           C  
ANISOU  791  CE  LYS A 128     3227   3824   7100   1313   -507  -1108       C  
ATOM    792  NZ  LYS A 128      95.856 230.908  16.123  1.00 39.38           N  
ANISOU  792  NZ  LYS A 128     3325   3937   7701   1169   -464  -1427       N  
ATOM    793  N   VAL A 129      90.658 225.616  13.879  1.00 38.51           N  
ANISOU  793  N   VAL A 129     3943   3968   6722   1225   -301    180       N  
ATOM    794  CA  VAL A 129      90.421 224.176  13.930  1.00 36.66           C  
ANISOU  794  CA  VAL A 129     3750   3775   6404   1241   -295    331       C  
ATOM    795  C   VAL A 129      90.186 223.612  12.539  1.00 37.36           C  
ANISOU  795  C   VAL A 129     3889   3723   6583   1078   -238    417       C  
ATOM    796  O   VAL A 129      90.779 222.599  12.161  1.00 38.33           O  
ANISOU  796  O   VAL A 129     4013   3806   6745   1035   -224    437       O  
ATOM    797  CB  VAL A 129      89.249 223.858  14.875  1.00 36.22           C  
ANISOU  797  CB  VAL A 129     3734   3836   6193   1358   -285    470       C  
ATOM    798  CG1 VAL A 129      88.790 222.422  14.686  1.00 27.97           C  
ANISOU  798  CG1 VAL A 129     2722   2757   5146   1319   -217    627       C  
ATOM    799  CG2 VAL A 129      89.655 224.099  16.316  1.00 37.72           C  
ANISOU  799  CG2 VAL A 129     3916   4185   6233   1598   -349    393       C  
ATOM    800  N   ILE A 130      89.314 224.252  11.766  1.00 37.03           N  
ANISOU  800  N   ILE A 130     3898   3615   6555   1013   -215    458       N  
ATOM    801  CA  ILE A 130      88.963 223.720  10.439  1.00 33.81           C  
ANISOU  801  CA  ILE A 130     3561   3103   6181    919   -195    515       C  
ATOM    802  C   ILE A 130      90.184 223.606   9.543  1.00 35.72           C  
ANISOU  802  C   ILE A 130     3846   3220   6508    855   -139    444       C  
ATOM    803  O   ILE A 130      90.439 222.502   9.013  1.00 36.77           O  
ANISOU  803  O   ILE A 130     3991   3322   6659    807   -137    479       O  
ATOM    804  CB  ILE A 130      87.821 224.546   9.819  1.00 30.64           C  
ANISOU  804  CB  ILE A 130     3228   2675   5738    928   -212    539       C  
ATOM    805  CG1 ILE A 130      86.513 224.295  10.572  1.00 29.55           C  
ANISOU  805  CG1 ILE A 130     3022   2639   5564    964   -250    609       C  
ATOM    806  CG2 ILE A 130      87.647 224.182   8.359  1.00 29.54           C  
ANISOU  806  CG2 ILE A 130     3197   2434   5595    899   -221    545       C  
ATOM    807  CD1 ILE A 130      85.357 225.092  10.052  1.00 28.92           C  
ANISOU  807  CD1 ILE A 130     2982   2547   5459    992   -293    605       C  
ATOM    808  N   PRO A 131      91.000 224.648   9.324  1.00 36.41           N  
ANISOU  808  N   PRO A 131     3948   3213   6672    844    -61    335       N  
ATOM    809  CA  PRO A 131      92.191 224.469   8.483  1.00 37.24           C  
ANISOU  809  CA  PRO A 131     4091   3182   6875    769     46    264       C  
ATOM    810  C   PRO A 131      93.213 223.525   9.084  1.00 38.59           C  
ANISOU  810  C   PRO A 131     4137   3394   7129    761      4    198       C  
ATOM    811  O   PRO A 131      93.954 222.878   8.337  1.00 41.81           O  
ANISOU  811  O   PRO A 131     4577   3719   7591    692     67    185       O  
ATOM    812  CB  PRO A 131      92.746 225.891   8.350  1.00 37.24           C  
ANISOU  812  CB  PRO A 131     4103   3072   6974    751    182    145       C  
ATOM    813  CG  PRO A 131      91.619 226.789   8.673  1.00 36.61           C  
ANISOU  813  CG  PRO A 131     4059   3043   6807    819    142    195       C  
ATOM    814  CD  PRO A 131      90.842 226.060   9.726  1.00 36.02           C  
ANISOU  814  CD  PRO A 131     3886   3152   6647    883    -28    263       C  
ATOM    815  N   TYR A 132      93.301 223.454  10.414  1.00 38.16           N  
ANISOU  815  N   TYR A 132     3964   3480   7053    855   -100    147       N  
ATOM    816  CA  TYR A 132      94.146 222.446  11.043  1.00 37.09           C  
ANISOU  816  CA  TYR A 132     3751   3420   6924    904   -165     99       C  
ATOM    817  C   TYR A 132      93.657 221.039  10.723  1.00 36.75           C  
ANISOU  817  C   TYR A 132     3768   3394   6799    882   -167    275       C  
ATOM    818  O   TYR A 132      94.467 220.113  10.606  1.00 39.61           O  
ANISOU  818  O   TYR A 132     4107   3737   7206    869   -165    257       O  
ATOM    819  CB  TYR A 132      94.183 222.669  12.554  1.00 37.80           C  
ANISOU  819  CB  TYR A 132     3768   3693   6902   1076   -281     23       C  
ATOM    820  CG  TYR A 132      94.996 221.651  13.314  1.00 38.67           C  
ANISOU  820  CG  TYR A 132     3842   3911   6942   1200   -359    -18       C  
ATOM    821  CD1 TYR A 132      96.378 221.760  13.399  1.00 41.11           C  
ANISOU  821  CD1 TYR A 132     4043   4196   7380   1200   -405   -251       C  
ATOM    822  CD2 TYR A 132      94.382 220.584  13.954  1.00 38.10           C  
ANISOU  822  CD2 TYR A 132     3846   3948   6682   1329   -368    167       C  
ATOM    823  CE1 TYR A 132      97.128 220.827  14.098  1.00 41.49           C  
ANISOU  823  CE1 TYR A 132     4071   4355   7336   1344   -494   -293       C  
ATOM    824  CE2 TYR A 132      95.122 219.647  14.653  1.00 38.73           C  
ANISOU  824  CE2 TYR A 132     3928   4120   6668   1491   -416    154       C  
ATOM    825  CZ  TYR A 132      96.494 219.773  14.723  1.00 40.78           C  
ANISOU  825  CZ  TYR A 132     4089   4383   7024   1506   -495    -72       C  
ATOM    826  OH  TYR A 132      97.228 218.841  15.420  1.00 42.75           O  
ANISOU  826  OH  TYR A 132     4347   4732   7163   1688   -552    -81       O  
ATOM    827  N   LEU A 133      92.345 220.861  10.561  1.00 33.69           N  
ANISOU  827  N   LEU A 133     3441   3035   6322    871   -164    421       N  
ATOM    828  CA  LEU A 133      91.813 219.528  10.304  1.00 34.10           C  
ANISOU  828  CA  LEU A 133     3513   3089   6356    836   -149    545       C  
ATOM    829  C   LEU A 133      92.048 219.087   8.864  1.00 34.48           C  
ANISOU  829  C   LEU A 133     3614   3009   6477    719   -117    534       C  
ATOM    830  O   LEU A 133      92.190 217.887   8.606  1.00 36.03           O  
ANISOU  830  O   LEU A 133     3797   3183   6708    682   -103    577       O  
ATOM    831  CB  LEU A 133      90.322 219.482  10.645  1.00 36.25           C  
ANISOU  831  CB  LEU A 133     3784   3413   6574    857   -147    651       C  
ATOM    832  CG  LEU A 133      89.971 219.526  12.136  1.00 38.11           C  
ANISOU  832  CG  LEU A 133     4002   3775   6704   1001   -136    705       C  
ATOM    833  CD1 LEU A 133      88.466 219.528  12.333  1.00 27.17           C  
ANISOU  833  CD1 LEU A 133     2600   2396   5328    995    -92    801       C  
ATOM    834  CD2 LEU A 133      90.610 218.361  12.869  1.00 27.66           C  
ANISOU  834  CD2 LEU A 133     2683   2488   5336   1096   -101    757       C  
ATOM    835  N   GLN A 134      92.208 220.056   7.974  1.00 34.77           N  
ANISOU  835  N   GLN A 134     3737   2958   6517    683    -88    478       N  
ATOM    836  CA  GLN A 134      92.432 219.684   6.560  1.00 36.15           C  
ANISOU  836  CA  GLN A 134     4019   3024   6692    624    -44    463       C  
ATOM    837  C   GLN A 134      93.914 219.618   6.248  1.00 36.45           C  
ANISOU  837  C   GLN A 134     4047   2990   6812    572     44    386       C  
ATOM    838  O   GLN A 134      94.224 219.166   5.190  1.00 39.94           O  
ANISOU  838  O   GLN A 134     4534   3383   7257    527     69    392       O  
ATOM    839  CB  GLN A 134      91.787 220.617   5.547  1.00 39.51           C  
ANISOU  839  CB  GLN A 134     4606   3380   7027    661    -15    452       C  
ATOM    840  CG  GLN A 134      91.714 219.923   4.203  1.00 46.47           C  
ANISOU  840  CG  GLN A 134     5659   4156   7843    666     27    439       C  
ATOM    841  CD  GLN A 134      91.245 220.790   3.076  1.00 53.21           C  
ANISOU  841  CD  GLN A 134     6712   4953   8555    788      3    449       C  
ATOM    842  OE1 GLN A 134      90.859 221.920   3.282  1.00 56.88           O  
ANISOU  842  OE1 GLN A 134     7172   5458   8981    846    -39    465       O  
ATOM    843  NE2 GLN A 134      91.282 220.262   1.872  1.00 54.91           N  
ANISOU  843  NE2 GLN A 134     7118   5070   8675    859     23    434       N  
ATOM    844  N   THR A 135      94.774 220.150   7.098  1.00 34.25           N  
ANISOU  844  N   THR A 135     3688   2700   6625    581     85    286       N  
ATOM    845  CA  THR A 135      96.213 220.005   6.815  1.00 36.77           C  
ANISOU  845  CA  THR A 135     3950   2946   7076    526    166    172       C  
ATOM    846  C   THR A 135      96.638 218.682   7.434  1.00 38.88           C  
ANISOU  846  C   THR A 135     4115   3282   7377    553     77    185       C  
ATOM    847  O   THR A 135      97.453 218.009   6.842  1.00 40.49           O  
ANISOU  847  O   THR A 135     4313   3426   7645    494    130    152       O  
ATOM    848  CB  THR A 135      96.992 221.233   7.264  1.00 37.71           C  
ANISOU  848  CB  THR A 135     3959   3029   7339    528    219      1       C  
ATOM    849  OG1 THR A 135      96.611 221.521   8.596  1.00 43.14           O  
ANISOU  849  OG1 THR A 135     4541   3848   8003    639     72    -30       O  
ATOM    850  CG2 THR A 135      96.698 222.407   6.376  1.00 28.19           C  
ANISOU  850  CG2 THR A 135     2880   1720   6110    487    384     -1       C  
ATOM    851  N   VAL A 136      96.058 218.339   8.579  1.00 38.37           N  
ANISOU  851  N   VAL A 136     3991   3350   7239    658    -35    243       N  
ATOM    852  CA  VAL A 136      96.310 217.033   9.180  1.00 36.71           C  
ANISOU  852  CA  VAL A 136     3743   3211   6995    720    -83    301       C  
ATOM    853  C   VAL A 136      95.797 215.929   8.268  1.00 34.46           C  
ANISOU  853  C   VAL A 136     3521   2870   6703    627    -36    422       C  
ATOM    854  O   VAL A 136      96.449 214.891   8.093  1.00 33.57           O  
ANISOU  854  O   VAL A 136     3390   2729   6636    606    -16    428       O  
ATOM    855  CB  VAL A 136      95.673 216.952  10.579  1.00 36.08           C  
ANISOU  855  CB  VAL A 136     3651   3292   6765    886   -155    371       C  
ATOM    856  CG1 VAL A 136      95.670 215.516  11.076  1.00 32.92           C  
ANISOU  856  CG1 VAL A 136     3274   2939   6296    965   -139    490       C  
ATOM    857  CG2 VAL A 136      96.420 217.847  11.551  1.00 39.02           C  
ANISOU  857  CG2 VAL A 136     3949   3755   7121   1019   -242    195       C  
ATOM    858  N   SER A 137      94.628 216.142   7.657  1.00 34.31           N  
ANISOU  858  N   SER A 137     3565   2836   6636    581    -31    490       N  
ATOM    859  CA  SER A 137      94.054 215.128   6.781  1.00 34.96           C  
ANISOU  859  CA  SER A 137     3677   2871   6734    514    -20    544       C  
ATOM    860  C   SER A 137      94.845 214.976   5.490  1.00 34.12           C  
ANISOU  860  C   SER A 137     3653   2669   6644    444     26    471       C  
ATOM    861  O   SER A 137      94.929 213.869   4.947  1.00 34.24           O  
ANISOU  861  O   SER A 137     3665   2651   6694    403     33    482       O  
ATOM    862  CB  SER A 137      92.599 215.465   6.471  1.00 36.46           C  
ANISOU  862  CB  SER A 137     3888   3069   6895    520    -65    578       C  
ATOM    863  OG  SER A 137      92.043 214.512   5.584  1.00 39.65           O  
ANISOU  863  OG  SER A 137     4287   3411   7367    476    -88    571       O  
ATOM    864  N   VAL A 138      95.463 216.051   5.028  1.00 32.70           N  
ANISOU  864  N   VAL A 138     3555   2435   6437    436     86    397       N  
ATOM    865  CA  VAL A 138      96.296 215.971   3.797  1.00 35.05           C  
ANISOU  865  CA  VAL A 138     3957   2638   6722    388    186    340       C  
ATOM    866  C   VAL A 138      97.628 215.311   4.147  1.00 35.60           C  
ANISOU  866  C   VAL A 138     3912   2703   6911    347    224    289       C  
ATOM    867  O   VAL A 138      98.203 214.718   3.261  1.00 36.60           O  
ANISOU  867  O   VAL A 138     4080   2789   7038    305    268    280       O  
ATOM    868  CB  VAL A 138      96.506 217.344   3.151  1.00 37.34           C  
ANISOU  868  CB  VAL A 138     4374   2853   6961    400    306    289       C  
ATOM    869  CG1 VAL A 138      97.659 217.310   2.181  1.00 27.73           C  
ANISOU  869  CG1 VAL A 138     3250   1539   5746    357    465    236       C  
ATOM    870  CG2 VAL A 138      95.249 217.820   2.456  1.00 39.30           C  
ANISOU  870  CG2 VAL A 138     4789   3083   7061    479    262    341       C  
ATOM    871  N   SER A 139      98.114 215.493   5.378  1.00 34.85           N  
ANISOU  871  N   SER A 139     3674   2647   6919    383    188    240       N  
ATOM    872  CA  SER A 139      99.344 214.836   5.810  1.00 34.34           C  
ANISOU  872  CA  SER A 139     3493   2572   6981    384    187    160       C  
ATOM    873  C   SER A 139      99.125 213.348   6.052  1.00 32.97           C  
ANISOU  873  C   SER A 139     3305   2442   6782    407    133    264       C  
ATOM    874  O   SER A 139      99.957 212.523   5.657  1.00 33.36           O  
ANISOU  874  O   SER A 139     3332   2450   6894    368    171    234       O  
ATOM    875  CB  SER A 139      99.884 215.511   7.069  1.00 35.75           C  
ANISOU  875  CB  SER A 139     3536   2799   7247    477    109     37       C  
ATOM    876  OG  SER A 139     101.086 214.893   7.491  1.00 38.41           O  
ANISOU  876  OG  SER A 139     3760   3138   7696    511     70    -81       O  
ATOM    877  N   VAL A 140      98.019 212.985   6.705  1.00 30.52           N  
ANISOU  877  N   VAL A 140     3000   2206   6389    469     74    387       N  
ATOM    878  CA  VAL A 140      97.701 211.572   6.891  1.00 26.93           C  
ANISOU  878  CA  VAL A 140     2533   1769   5931    480     83    495       C  
ATOM    879  C   VAL A 140      97.552 210.789   5.596  1.00 36.75           C  
ANISOU  879  C   VAL A 140     3822   2940   7201    365    126    489       C  
ATOM    880  O   VAL A 140      97.993 209.638   5.489  1.00 36.94           O  
ANISOU  880  O   VAL A 140     3819   2939   7278    341    158    508       O  
ATOM    881  CB  VAL A 140      96.451 211.414   7.779  1.00 33.16           C  
ANISOU  881  CB  VAL A 140     3318   2629   6650    556     76    622       C  
ATOM    882  CG1 VAL A 140      95.942 209.979   7.745  1.00 27.66           C  
ANISOU  882  CG1 VAL A 140     2599   1901   6011    533    150    726       C  
ATOM    883  CG2 VAL A 140      96.756 211.833   9.204  1.00 33.70           C  
ANISOU  883  CG2 VAL A 140     3379   2804   6621    734     30    627       C  
ATOM    884  N   SER A 141      96.959 211.409   4.597  1.00 37.49           N  
ANISOU  884  N   SER A 141     4003   3005   7237    324    120    452       N  
ATOM    885  CA  SER A 141      96.677 210.829   3.266  1.00 34.19           C  
ANISOU  885  CA  SER A 141     3665   2524   6801    276    126    422       C  
ATOM    886  C   SER A 141      97.947 210.594   2.453  1.00 30.46           C  
ANISOU  886  C   SER A 141     3239   2003   6333    235    203    358       C  
ATOM    887  O   SER A 141      97.982 209.700   1.661  1.00 32.53           O  
ANISOU  887  O   SER A 141     3497   2235   6628    205    210    352       O  
ATOM    888  CB  SER A 141      95.810 211.781   2.523  1.00 36.11           C  
ANISOU  888  CB  SER A 141     4044   2732   6945    308     90    390       C  
ATOM    889  OG  SER A 141      95.119 211.137   1.484  1.00 38.82           O  
ANISOU  889  OG  SER A 141     4409   3023   7317    321     13    364       O  
ATOM    890  N   ALA A 142      98.938 211.454   2.614  1.00 28.68           N  
ANISOU  890  N   ALA A 142     3034   1758   6103    231    275    298       N  
ATOM    891  CA  ALA A 142     100.182 211.357   1.857  1.00 31.07           C  
ANISOU  891  CA  ALA A 142     3369   2004   6432    189    381    228       C  
ATOM    892  C   ALA A 142     101.035 210.284   2.522  1.00 33.10           C  
ANISOU  892  C   ALA A 142     3475   2282   6819    178    366    219       C  
ATOM    893  O   ALA A 142     101.674 209.478   1.835  1.00 34.07           O  
ANISOU  893  O   ALA A 142     3618   2370   6956    142    419    195       O  
ATOM    894  CB  ALA A 142     100.963 212.664   1.743  1.00 27.93           C  
ANISOU  894  CB  ALA A 142     2992   1560   6058    180    499    149       C  
ATOM    895  N   LEU A 143     101.067 210.259   3.855  1.00 34.50           N  
ANISOU  895  N   LEU A 143     3525   2505   7079    234    292    238       N  
ATOM    896  CA  LEU A 143     101.900 209.295   4.567  1.00 34.53           C  
ANISOU  896  CA  LEU A 143     3422   2510   7186    275    265    230       C  
ATOM    897  C   LEU A 143     101.312 207.888   4.545  1.00 36.48           C  
ANISOU  897  C   LEU A 143     3682   2770   7408    277    263    349       C  
ATOM    898  O   LEU A 143     102.066 206.908   4.580  1.00 36.92           O  
ANISOU  898  O   LEU A 143     3696   2801   7529    282    285    346       O  
ATOM    899  CB  LEU A 143     102.112 209.760   6.007  1.00 32.51           C  
ANISOU  899  CB  LEU A 143     3084   2306   6961    406    168    198       C  
ATOM    900  CG  LEU A 143     102.811 211.112   6.146  1.00 29.80           C  
ANISOU  900  CG  LEU A 143     2671   1942   6711    402    165     22       C  
ATOM    901  CD1 LEU A 143     102.790 211.581   7.590  1.00 30.38           C  
ANISOU  901  CD1 LEU A 143     2681   2122   6742    578     22    -36       C  
ATOM    902  CD2 LEU A 143     104.239 211.030   5.626  1.00 29.77           C  
ANISOU  902  CD2 LEU A 143     2574   1862   6877    330    236   -139       C  
ATOM    903  N   THR A 144      99.982 207.764   4.492  1.00 36.62           N  
ANISOU  903  N   THR A 144     3736   2813   7364    271    247    438       N  
ATOM    904  CA  THR A 144      99.366 206.443   4.386  1.00 36.66           C  
ANISOU  904  CA  THR A 144     3714   2803   7412    253    277    517       C  
ATOM    905  C   THR A 144      99.572 205.853   2.996  1.00 35.43           C  
ANISOU  905  C   THR A 144     3600   2596   7265    171    299    442       C  
ATOM    906  O   THR A 144      99.821 204.650   2.857  1.00 40.07           O  
ANISOU  906  O   THR A 144     4143   3156   7927    154    340    458       O  
ATOM    907  CB  THR A 144      97.871 206.521   4.714  1.00 37.84           C  
ANISOU  907  CB  THR A 144     3845   2969   7564    265    267    592       C  
ATOM    908  OG1 THR A 144      97.691 207.118   6.004  1.00 28.20           O  
ANISOU  908  OG1 THR A 144     2620   1807   6287    368    257    668       O  
ATOM    909  CG2 THR A 144      97.250 205.126   4.718  1.00 28.99           C  
ANISOU  909  CG2 THR A 144     2647   1801   6568    244    340    653       C  
ATOM    910  N   LEU A 145      99.471 206.686   1.957  1.00 33.37           N  
ANISOU  910  N   LEU A 145     3451   2312   6915    142    283    364       N  
ATOM    911  CA  LEU A 145      99.740 206.219   0.601  1.00 33.74           C  
ANISOU  911  CA  LEU A 145     3597   2295   6927    106    306    293       C  
ATOM    912  C   LEU A 145     101.198 205.815   0.425  1.00 36.38           C  
ANISOU  912  C   LEU A 145     3921   2617   7286     83    387    256       C  
ATOM    913  O   LEU A 145     101.499 204.906  -0.358  1.00 38.04           O  
ANISOU  913  O   LEU A 145     4160   2784   7509     57    414    225       O  
ATOM    914  CB  LEU A 145      99.359 207.300  -0.410  1.00 30.66           C  
ANISOU  914  CB  LEU A 145     3391   1853   6404    132    296    242       C  
ATOM    915  CG  LEU A 145      97.876 207.390  -0.773  1.00 31.10           C  
ANISOU  915  CG  LEU A 145     3480   1875   6462    172    185    227       C  
ATOM    916  CD1 LEU A 145      97.506 208.803  -1.200  1.00 32.43           C  
ANISOU  916  CD1 LEU A 145     3821   2014   6489    244    175    214       C  
ATOM    917  CD2 LEU A 145      97.539 206.396  -1.875  1.00 30.38           C  
ANISOU  917  CD2 LEU A 145     3431   1690   6423    184    133    142       C  
ATOM    918  N   SER A 146     102.114 206.477   1.136  1.00 36.64           N  
ANISOU  918  N   SER A 146     3893   2673   7358     97    421    237       N  
ATOM    919  CA  SER A 146     103.521 206.101   1.060  1.00 37.26           C  
ANISOU  919  CA  SER A 146     3911   2725   7521     79    490    176       C  
ATOM    920  C   SER A 146     103.785 204.796   1.801  1.00 38.58           C  
ANISOU  920  C   SER A 146     3963   2901   7795    104    460    227       C  
ATOM    921  O   SER A 146     104.607 203.983   1.362  1.00 39.25           O  
ANISOU  921  O   SER A 146     4027   2956   7932     82    509    194       O  
ATOM    922  CB  SER A 146     104.397 207.223   1.619  1.00 36.35           C  
ANISOU  922  CB  SER A 146     3718   2602   7491     91    522     92       C  
ATOM    923  OG  SER A 146     104.193 208.436   0.913  1.00 37.05           O  
ANISOU  923  OG  SER A 146     3925   2665   7488     72    597     60       O  
ATOM    924  N   CYS A 147     103.099 204.578   2.930  1.00 39.46           N  
ANISOU  924  N   CYS A 147     4020   3044   7930    166    402    321       N  
ATOM    925  CA  CYS A 147     103.277 203.333   3.673  1.00 40.38           C  
ANISOU  925  CA  CYS A 147     4078   3148   8117    223    414    405       C  
ATOM    926  C   CYS A 147     102.699 202.144   2.922  1.00 39.76           C  
ANISOU  926  C   CYS A 147     4005   3044   8059    164    467    441       C  
ATOM    927  O   CYS A 147     103.169 201.015   3.100  1.00 40.54           O  
ANISOU  927  O   CYS A 147     4063   3110   8231    182    517    478       O  
ATOM    928  CB  CYS A 147     102.642 203.439   5.061  1.00 42.66           C  
ANISOU  928  CB  CYS A 147     4366   3474   8369    347    382    520       C  
ATOM    929  SG  CYS A 147     103.615 204.383   6.258  1.00 45.65           S  
ANISOU  929  SG  CYS A 147     4723   3898   8723    515    273    438       S  
ATOM    930  N   ILE A 148     101.682 202.371   2.092  1.00 39.33           N  
ANISOU  930  N   ILE A 148     3997   2990   7958    110    447    414       N  
ATOM    931  CA  ILE A 148     101.149 201.295   1.263  1.00 41.18           C  
ANISOU  931  CA  ILE A 148     4217   3177   8255     65    468    390       C  
ATOM    932  C   ILE A 148     102.171 200.890   0.211  1.00 45.00           C  
ANISOU  932  C   ILE A 148     4758   3628   8712     27    493    302       C  
ATOM    933  O   ILE A 148     102.428 199.699  -0.005  1.00 47.76           O  
ANISOU  933  O   ILE A 148     5057   3941   9148     13    537    301       O  
ATOM    934  CB  ILE A 148      99.814 201.717   0.626  1.00 37.28           C  
ANISOU  934  CB  ILE A 148     3752   2660   7754     42    401    342       C  
ATOM    935  CG1 ILE A 148      98.733 201.827   1.697  1.00 32.81           C  
ANISOU  935  CG1 ILE A 148     3089   2111   7265     72    411    435       C  
ATOM    936  CG2 ILE A 148      99.393 200.723  -0.441  1.00 38.63           C  
ANISOU  936  CG2 ILE A 148     3903   2751   8024      3    387    252       C  
ATOM    937  CD1 ILE A 148      97.438 202.400   1.188  1.00 30.89           C  
ANISOU  937  CD1 ILE A 148     2847   1841   7051     59    327    371       C  
ATOM    938  N   ALA A 149     102.779 201.877  -0.451  1.00 44.61           N  
ANISOU  938  N   ALA A 149     4820   3579   8551     15    494    233       N  
ATOM    939  CA  ALA A 149     103.847 201.584  -1.401  1.00 47.11           C  
ANISOU  939  CA  ALA A 149     5204   3853   8842    -12    558    163       C  
ATOM    940  C   ALA A 149     105.043 200.944  -0.705  1.00 48.91           C  
ANISOU  940  C   ALA A 149     5310   4093   9182     -1    606    175       C  
ATOM    941  O   ALA A 149     105.649 200.003  -1.233  1.00 49.75           O  
ANISOU  941  O   ALA A 149     5408   4165   9330    -20    651    148       O  
ATOM    942  CB  ALA A 149     104.266 202.866  -2.122  1.00 30.10           C  
ANISOU  942  CB  ALA A 149     3196   1672   6568    -14    607    108       C  
ATOM    943  N   LEU A 150     105.392 201.441   0.486  1.00 49.89           N  
ANISOU  943  N   LEU A 150     5341   4247   9370     44    583    203       N  
ATOM    944  CA  LEU A 150     106.503 200.879   1.247  1.00 49.03           C  
ANISOU  944  CA  LEU A 150     5118   4115   9395     83    594    198       C  
ATOM    945  C   LEU A 150     106.220 199.419   1.591  1.00 49.08           C  
ANISOU  945  C   LEU A 150     5090   4099   9460    110    614    292       C  
ATOM    946  O   LEU A 150     107.043 198.534   1.326  1.00 48.65           O  
ANISOU  946  O   LEU A 150     5000   4007   9477    102    658    266       O  
ATOM    947  CB  LEU A 150     106.716 201.699   2.519  1.00 46.16           C  
ANISOU  947  CB  LEU A 150     4690   3763   9086    161    522    194       C  
ATOM    948  CG  LEU A 150     108.144 202.039   2.935  1.00 46.92           C  
ANISOU  948  CG  LEU A 150     4678   3822   9329    195    498     58       C  
ATOM    949  CD1 LEU A 150     108.808 202.900   1.881  1.00 47.53           C  
ANISOU  949  CD1 LEU A 150     4741   3884   9434     99    596    -72       C  
ATOM    950  CD2 LEU A 150     108.141 202.746   4.277  1.00 48.23           C  
ANISOU  950  CD2 LEU A 150     4807   4014   9503    331    370     27       C  
ATOM    951  N   ASP A 151     105.046 199.149   2.173  1.00 47.60           N  
ANISOU  951  N   ASP A 151     4905   3923   9257    142    609    403       N  
ATOM    952  CA  ASP A 151     104.692 197.780   2.540  1.00 46.74           C  
ANISOU  952  CA  ASP A 151     4759   3773   9227    171    685    504       C  
ATOM    953  C   ASP A 151     104.688 196.866   1.320  1.00 42.51           C  
ANISOU  953  C   ASP A 151     4213   3205   8734     89    725    433       C  
ATOM    954  O   ASP A 151     105.150 195.721   1.392  1.00 41.02           O  
ANISOU  954  O   ASP A 151     3981   2969   8636    102    797    465       O  
ATOM    955  CB  ASP A 151     103.340 197.765   3.267  1.00 51.51           C  
ANISOU  955  CB  ASP A 151     5357   4382   9833    212    722    624       C  
ATOM    956  CG  ASP A 151     102.714 196.375   3.335  1.00 57.38           C  
ANISOU  956  CG  ASP A 151     6036   5062  10706    194    846    684       C  
ATOM    957  OD1 ASP A 151     103.294 195.482   3.993  1.00 59.04           O  
ANISOU  957  OD1 ASP A 151     6201   5251  10981    109    832    588       O  
ATOM    958  OD2 ASP A 151     101.641 196.169   2.728  1.00 60.49           O  
ANISOU  958  OD2 ASP A 151     6432   5411  11142    286    963    819       O  
ATOM    959  N   ARG A 152     104.182 197.356   0.185  1.00 39.49           N  
ANISOU  959  N   ARG A 152     3892   2833   8278     24    676    335       N  
ATOM    960  CA  ARG A 152     104.142 196.526  -1.014  1.00 38.04           C  
ANISOU  960  CA  ARG A 152     3730   2599   8124    -28    690    251       C  
ATOM    961  C   ARG A 152     105.527 196.250  -1.586  1.00 38.08           C  
ANISOU  961  C   ARG A 152     3770   2591   8106    -41    729    195       C  
ATOM    962  O   ARG A 152     105.781 195.160  -2.113  1.00 36.46           O  
ANISOU  962  O   ARG A 152     3540   2340   7973    -61    772    168       O  
ATOM    963  CB  ARG A 152     103.255 197.206  -2.060  1.00 36.32           C  
ANISOU  963  CB  ARG A 152     3611   2362   7827    -62    612    159       C  
ATOM    964  CG  ARG A 152     101.760 197.127  -1.781  1.00 38.20           C  
ANISOU  964  CG  ARG A 152     3767   2579   8169    -61    571    168       C  
ATOM    965  CD  ARG A 152     101.243 195.699  -1.871  1.00 40.81           C  
ANISOU  965  CD  ARG A 152     3956   2835   8717    -79    627    145       C  
ATOM    966  NE  ARG A 152     101.278 195.010  -0.585  1.00 44.09           N  
ANISOU  966  NE  ARG A 152     4255   3253   9244    -40    754    288       N  
ATOM    967  CZ  ARG A 152     101.311 193.690  -0.452  1.00 47.64           C  
ANISOU  967  CZ  ARG A 152     4599   3634   9869    -38    870    312       C  
ATOM    968  NH1 ARG A 152     101.325 192.916  -1.529  1.00 48.31           N  
ANISOU  968  NH1 ARG A 152     4653   3655  10048    -82    852    182       N  
ATOM    969  NH2 ARG A 152     101.340 193.142   0.754  1.00 49.75           N  
ANISOU  969  NH2 ARG A 152     4806   3882  10215     20   1018    468       N  
ATOM    970  N   TRP A 153     106.435 197.226  -1.490  1.00 38.92           N  
ANISOU  970  N   TRP A 153     3914   2727   8148    -32    730    166       N  
ATOM    971  CA  TRP A 153     107.787 197.037  -2.007  1.00 39.37           C  
ANISOU  971  CA  TRP A 153     3973   2759   8227    -47    792    100       C  
ATOM    972  C   TRP A 153     108.582 196.065  -1.145  1.00 41.49           C  
ANISOU  972  C   TRP A 153     4111   3008   8646     -8    819    143       C  
ATOM    973  O   TRP A 153     109.344 195.245  -1.669  1.00 42.22           O  
ANISOU  973  O   TRP A 153     4185   3064   8792    -25    873    106       O  
ATOM    974  CB  TRP A 153     108.507 198.384  -2.103  1.00 37.66           C  
ANISOU  974  CB  TRP A 153     3788   2555   7967    -51    818     38       C  
ATOM    975  CG  TRP A 153     109.885 198.272  -2.681  1.00 35.75           C  
ANISOU  975  CG  TRP A 153     3523   2272   7788    -72    917    -43       C  
ATOM    976  CD1 TRP A 153     110.224 198.308  -4.002  1.00 36.35           C  
ANISOU  976  CD1 TRP A 153     3731   2298   7784   -108   1011    -93       C  
ATOM    977  CD2 TRP A 153     111.109 198.097  -1.957  1.00 34.87           C  
ANISOU  977  CD2 TRP A 153     3243   2145   7862    -50    937    -91       C  
ATOM    978  NE1 TRP A 153     111.583 198.169  -4.146  1.00 37.04           N  
ANISOU  978  NE1 TRP A 153     3729   2351   7992   -118   1115   -160       N  
ATOM    979  CE2 TRP A 153     112.150 198.038  -2.906  1.00 36.34           C  
ANISOU  979  CE2 TRP A 153     3439   2285   8083    -86   1060   -174       C  
ATOM    980  CE3 TRP A 153     111.426 197.987  -0.600  1.00 33.80           C  
ANISOU  980  CE3 TRP A 153     2958   2007   7877      7    854    -81       C  
ATOM    981  CZ2 TRP A 153     113.485 197.874  -2.539  1.00 35.26           C  
ANISOU  981  CZ2 TRP A 153     3126   2113   8158    -81   1104   -263       C  
ATOM    982  CZ3 TRP A 153     112.751 197.823  -0.238  1.00 34.90           C  
ANISOU  982  CZ3 TRP A 153     2947   2097   8214     22    861   -181       C  
ATOM    983  CH2 TRP A 153     113.764 197.769  -1.204  1.00 35.58           C  
ANISOU  983  CH2 TRP A 153     3002   2151   8365    -30    987   -279       C  
ATOM    984  N   TYR A 154     108.428 196.145   0.180  1.00 42.93           N  
ANISOU  984  N   TYR A 154     4226   3197   8890     58    783    228       N  
ATOM    985  CA  TYR A 154     109.103 195.199   1.063  1.00 45.19           C  
ANISOU  985  CA  TYR A 154     4443   3431   9295    129    804    291       C  
ATOM    986  C   TYR A 154     108.554 193.785   0.932  1.00 47.65           C  
ANISOU  986  C   TYR A 154     4748   3704   9653    127    886    377       C  
ATOM    987  O   TYR A 154     109.252 192.830   1.288  1.00 48.10           O  
ANISOU  987  O   TYR A 154     4775   3705   9798    175    935    419       O  
ATOM    988  CB  TYR A 154     108.998 195.663   2.517  1.00 44.65           C  
ANISOU  988  CB  TYR A 154     4382   3364   9219    255    737    371       C  
ATOM    989  CG  TYR A 154     110.112 196.590   2.944  1.00 46.00           C  
ANISOU  989  CG  TYR A 154     4503   3532   9442    311    641    240       C  
ATOM    990  CD1 TYR A 154     110.103 197.930   2.582  1.00 45.07           C  
ANISOU  990  CD1 TYR A 154     4363   3451   9311    241    610    131       C  
ATOM    991  CD2 TYR A 154     111.172 196.125   3.714  1.00 49.87           C  
ANISOU  991  CD2 TYR A 154     4965   3988   9996    459    577    199       C  
ATOM    992  CE1 TYR A 154     111.122 198.782   2.971  1.00 47.74           C  
ANISOU  992  CE1 TYR A 154     4608   3775   9755    277    537    -31       C  
ATOM    993  CE2 TYR A 154     112.194 196.969   4.108  1.00 52.29           C  
ANISOU  993  CE2 TYR A 154     5184   4305  10377    528    458     10       C  
ATOM    994  CZ  TYR A 154     112.165 198.296   3.734  1.00 51.21           C  
ANISOU  994  CZ  TYR A 154     4986   4188  10285    414    447   -113       C  
ATOM    995  OH  TYR A 154     113.184 199.135   4.128  1.00 52.54           O  
ANISOU  995  OH  TYR A 154     5026   4359  10577    460    342   -339       O  
ATOM    996  N   ALA A 155     107.330 193.628   0.429  1.00 48.97           N  
ANISOU  996  N   ALA A 155     4933   3884   9789     78    902    387       N  
ATOM    997  CA  ALA A 155     106.736 192.305   0.292  1.00 35.65           C  
ANISOU  997  CA  ALA A 155     3195   2139   8210     70    995    433       C  
ATOM    998  C   ALA A 155     106.971 191.690  -1.080  1.00 35.79           C  
ANISOU  998  C   ALA A 155     3220   2132   8248     -2    998    308       C  
ATOM    999  O   ALA A 155     107.050 190.461  -1.193  1.00 36.86           O  
ANISOU  999  O   ALA A 155     3295   2205   8507     -1   1083    324       O  
ATOM   1000  CB  ALA A 155     105.233 192.371   0.571  1.00 35.92           C  
ANISOU 1000  CB  ALA A 155     3199   2167   8280     66   1018    482       C  
ATOM   1001  N   ILE A 156     107.085 192.508  -2.120  1.00 35.01           N  
ANISOU 1001  N   ILE A 156     3213   2063   8026    -51    924    194       N  
ATOM   1002  CA  ILE A 156     107.222 192.018  -3.485  1.00 35.44           C  
ANISOU 1002  CA  ILE A 156     3325   2074   8068   -104    925     82       C  
ATOM   1003  C   ILE A 156     108.667 192.082  -3.970  1.00 40.14           C  
ANISOU 1003  C   ILE A 156     3966   2669   8617   -111    965     36       C  
ATOM   1004  O   ILE A 156     109.143 191.155  -4.627  1.00 43.10           O  
ANISOU 1004  O   ILE A 156     4335   2995   9047   -131   1012     -8       O  
ATOM   1005  CB  ILE A 156     106.279 192.808  -4.418  1.00 35.27           C  
ANISOU 1005  CB  ILE A 156     3414   2039   7947   -137    840     -5       C  
ATOM   1006  CG1 ILE A 156     104.824 192.566  -4.020  1.00 37.57           C  
ANISOU 1006  CG1 ILE A 156     3607   2308   8359   -136    806      6       C  
ATOM   1007  CG2 ILE A 156     106.503 192.424  -5.872  1.00 36.57           C  
ANISOU 1007  CG2 ILE A 156     3686   2126   8084   -169    834   -127       C  
ATOM   1008  CD1 ILE A 156     103.832 193.416  -4.781  1.00 37.51           C  
ANISOU 1008  CD1 ILE A 156     3690   2276   8288   -149    695    -91       C  
ATOM   1009  N   CYS A 157     109.385 193.157  -3.651  1.00 42.26           N  
ANISOU 1009  N   CYS A 157     2937   3971   9147    365  -1214    118       N  
ATOM   1010  CA  CYS A 157     110.717 193.388  -4.198  1.00 39.15           C  
ANISOU 1010  CA  CYS A 157     2682   3511   8682    416  -1225    212       C  
ATOM   1011  C   CYS A 157     111.844 193.020  -3.243  1.00 39.45           C  
ANISOU 1011  C   CYS A 157     2834   3492   8661    493  -1182    133       C  
ATOM   1012  O   CYS A 157     112.866 192.485  -3.687  1.00 41.63           O  
ANISOU 1012  O   CYS A 157     3214   3761   8843    536  -1190    186       O  
ATOM   1013  CB  CYS A 157     110.868 194.852  -4.622  1.00 39.87           C  
ANISOU 1013  CB  CYS A 157     2761   3581   8807    450  -1209    272       C  
ATOM   1014  SG  CYS A 157     110.185 195.233  -6.252  1.00 42.34           S  
ANISOU 1014  SG  CYS A 157     3001   4004   9083    484  -1267    443       S  
ATOM   1015  N   HIS A 158     111.692 193.291  -1.950  1.00 38.76           N  
ANISOU 1015  N   HIS A 158     2729   3407   8592    543  -1136      0       N  
ATOM   1016  CA  HIS A 158     112.768 193.007  -1.009  1.00 40.02           C  
ANISOU 1016  CA  HIS A 158     2978   3601   8625    678  -1105    -97       C  
ATOM   1017  C   HIS A 158     113.015 191.501  -0.928  1.00 42.86           C  
ANISOU 1017  C   HIS A 158     3480   3921   8883    809  -1069    -55       C  
ATOM   1018  O   HIS A 158     112.064 190.716  -0.834  1.00 45.92           O  
ANISOU 1018  O   HIS A 158     3932   4227   9290    753   -984    -46       O  
ATOM   1019  CB  HIS A 158     112.451 193.561   0.374  1.00 38.44           C  
ANISOU 1019  CB  HIS A 158     2724   3435   8444    731  -1067   -252       C  
ATOM   1020  CG  HIS A 158     113.647 193.647   1.275  1.00 46.90           C  
ANISOU 1020  CG  HIS A 158     3832   4631   9357    888  -1059   -386       C  
ATOM   1021  ND1 HIS A 158     114.067 192.593   2.059  1.00 47.28           N  
ANISOU 1021  ND1 HIS A 158     4004   4758   9203   1119  -1021   -424       N  
ATOM   1022  CD2 HIS A 158     114.520 194.658   1.503  1.00 47.39           C  
ANISOU 1022  CD2 HIS A 158     3808   4763   9435    879  -1071   -509       C  
ATOM   1023  CE1 HIS A 158     115.144 192.955   2.735  1.00 39.85           C  
ANISOU 1023  CE1 HIS A 158     3027   4006   8109   1257  -1040   -564       C  
ATOM   1024  NE2 HIS A 158     115.439 194.203   2.416  1.00 39.88           N  
ANISOU 1024  NE2 HIS A 158     2878   4002   8271   1085  -1073   -640       N  
ATOM   1025  N   PRO A 159     114.279 191.073  -0.951  1.00 43.41           N  
ANISOU 1025  N   PRO A 159     3685   4054   8755    955  -1064    -45       N  
ATOM   1026  CA  PRO A 159     114.578 189.632  -1.031  1.00 44.58           C  
ANISOU 1026  CA  PRO A 159     4104   4118   8717   1102   -967     36       C  
ATOM   1027  C   PRO A 159     114.087 188.827   0.157  1.00 48.83           C  
ANISOU 1027  C   PRO A 159     4902   4618   9034   1210   -766    -24       C  
ATOM   1028  O   PRO A 159     113.905 187.608   0.025  1.00 51.36           O  
ANISOU 1028  O   PRO A 159     5578   4826   9110   1193   -553     49       O  
ATOM   1029  CB  PRO A 159     116.111 189.598  -1.131  1.00 42.65           C  
ANISOU 1029  CB  PRO A 159     3905   4027   8272   1287  -1013     27       C  
ATOM   1030  CG  PRO A 159     116.493 190.964  -1.628  1.00 42.07           C  
ANISOU 1030  CG  PRO A 159     3604   4058   8323   1097  -1103    -30       C  
ATOM   1031  CD  PRO A 159     115.493 191.900  -1.031  1.00 43.16           C  
ANISOU 1031  CD  PRO A 159     3596   4162   8642    970  -1105   -114       C  
ATOM   1032  N   LEU A 160     113.871 189.456   1.313  1.00 50.62           N  
ANISOU 1032  N   LEU A 160     4992   4911   9329   1323   -790   -157       N  
ATOM   1033  CA  LEU A 160     113.331 188.743   2.463  1.00 52.27           C  
ANISOU 1033  CA  LEU A 160     5467   5068   9327   1439   -572   -202       C  
ATOM   1034  C   LEU A 160     111.821 188.553   2.393  1.00 53.38           C  
ANISOU 1034  C   LEU A 160     5629   5061   9592   1136   -427   -216       C  
ATOM   1035  O   LEU A 160     111.294 187.706   3.124  1.00 55.05           O  
ANISOU 1035  O   LEU A 160     6144   5160   9611   1162   -156   -237       O  
ATOM   1036  CB  LEU A 160     113.701 189.465   3.762  1.00 53.40           C  
ANISOU 1036  CB  LEU A 160     5450   5377   9464   1695   -652   -361       C  
ATOM   1037  CG  LEU A 160     115.026 189.054   4.411  1.00 56.30           C  
ANISOU 1037  CG  LEU A 160     5946   5953   9491   2115   -659   -406       C  
ATOM   1038  CD1 LEU A 160     116.220 189.582   3.626  1.00 56.29           C  
ANISOU 1038  CD1 LEU A 160     5751   6159   9479   2071   -831   -415       C  
ATOM   1039  CD2 LEU A 160     115.089 189.505   5.865  1.00 58.92           C  
ANISOU 1039  CD2 LEU A 160     6203   6485   9698   2347   -660   -575       C  
ATOM   1040  N   MET A 161     111.121 189.305   1.541  1.00 52.70           N  
ANISOU 1040  N   MET A 161     5235   4990   9798    872   -575   -217       N  
ATOM   1041  CA  MET A 161     109.679 189.148   1.347  1.00 56.09           C  
ANISOU 1041  CA  MET A 161     5605   5375  10332    585   -467   -274       C  
ATOM   1042  C   MET A 161     108.935 189.278   2.677  1.00 59.23           C  
ANISOU 1042  C   MET A 161     6015   5745  10743    625   -333   -399       C  
ATOM   1043  O   MET A 161     108.293 188.343   3.163  1.00 59.18           O  
ANISOU 1043  O   MET A 161     6279   5626  10582    534    -42   -452       O  
ATOM   1044  CB  MET A 161     109.365 187.809   0.672  1.00 59.14           C  
ANISOU 1044  CB  MET A 161     6295   5658  10520    384   -230   -248       C  
ATOM   1045  CG  MET A 161     110.217 187.501  -0.552  1.00 59.81           C  
ANISOU 1045  CG  MET A 161     6438   5755  10532    379   -328   -120       C  
ATOM   1046  SD  MET A 161     109.660 188.329  -2.052  1.00 60.70           S  
ANISOU 1046  SD  MET A 161     6146   6026  10891    156   -589    -91       S  
ATOM   1047  CE  MET A 161     108.135 187.451  -2.386  1.00 62.05           C  
ANISOU 1047  CE  MET A 161     6338   6232  11009   -225   -361   -266       C  
ATOM   1048  N   PHE A 162     109.044 190.468   3.266  1.00 60.71           N  
ANISOU 1048  N   PHE A 162     5924   6018  11124    753   -514   -457       N  
ATOM   1049  CA  PHE A 162     108.440 190.720   4.569  1.00 60.46           C  
ANISOU 1049  CA  PHE A 162     5882   5980  11111    824   -415   -578       C  
ATOM   1050  C   PHE A 162     106.921 190.625   4.491  1.00 65.19           C  
ANISOU 1050  C   PHE A 162     6383   6555  11833    544   -291   -656       C  
ATOM   1051  O   PHE A 162     106.298 191.110   3.544  1.00 66.93           O  
ANISOU 1051  O   PHE A 162     6330   6858  12242    360   -422   -648       O  
ATOM   1052  CB  PHE A 162     108.849 192.100   5.085  1.00 55.25           C  
ANISOU 1052  CB  PHE A 162     4909   5417  10665    974   -629   -655       C  
ATOM   1053  CG  PHE A 162     110.298 192.200   5.467  1.00 51.17           C  
ANISOU 1053  CG  PHE A 162     4455   5006   9983   1235   -713   -679       C  
ATOM   1054  CD1 PHE A 162     110.712 191.864   6.746  1.00 52.55           C  
ANISOU 1054  CD1 PHE A 162     4785   5255   9926   1513   -624   -776       C  
ATOM   1055  CD2 PHE A 162     111.244 192.638   4.554  1.00 48.14           C  
ANISOU 1055  CD2 PHE A 162     4033   4719   9541   1159   -844   -612       C  
ATOM   1056  CE1 PHE A 162     112.041 191.958   7.107  1.00 52.72           C  
ANISOU 1056  CE1 PHE A 162     4860   5508   9662   1722   -698   -821       C  
ATOM   1057  CE2 PHE A 162     112.576 192.734   4.909  1.00 48.17           C  
ANISOU 1057  CE2 PHE A 162     4093   4901   9309   1330   -887   -673       C  
ATOM   1058  CZ  PHE A 162     112.975 192.393   6.188  1.00 50.68           C  
ANISOU 1058  CZ  PHE A 162     4506   5354   9394   1614   -829   -784       C  
ATOM   1059  N   LYS A 163     106.329 189.993   5.501  1.00 69.74           N  
ANISOU 1059  N   LYS A 163     7180   7041  12277    536    -23   -743       N  
ATOM   1060  CA  LYS A 163     104.880 189.844   5.613  1.00 73.28           C  
ANISOU 1060  CA  LYS A 163     7531   7484  12828    258    147   -875       C  
ATOM   1061  C   LYS A 163     104.431 190.589   6.868  1.00 74.47           C  
ANISOU 1061  C   LYS A 163     7559   7654  13083    384    149   -973       C  
ATOM   1062  O   LYS A 163     104.507 190.054   7.979  1.00 75.57           O  
ANISOU 1062  O   LYS A 163     7996   7683  13032    526    383  -1004       O  
ATOM   1063  CB  LYS A 163     104.480 188.371   5.655  1.00 77.71           C  
ANISOU 1063  CB  LYS A 163     8494   7874  13158     70    555   -924       C  
ATOM   1064  CG  LYS A 163     104.566 187.674   4.306  1.00 80.59           C  
ANISOU 1064  CG  LYS A 163     8909   8244  13468   -161    577   -893       C  
ATOM   1065  CD  LYS A 163     104.184 186.206   4.405  1.00 86.84           C  
ANISOU 1065  CD  LYS A 163    10142   8813  14041   -378   1060   -977       C  
ATOM   1066  CE  LYS A 163     105.294 185.387   5.047  1.00 90.32           C  
ANISOU 1066  CE  LYS A 163    11128   9024  14166    -45   1283   -813       C  
ATOM   1067  NZ  LYS A 163     104.959 183.938   5.118  1.00 94.08           N  
ANISOU 1067  NZ  LYS A 163    12119   9208  14419   -233   1836   -868       N  
ATOM   1068  N   SER A 164     103.972 191.826   6.691  1.00 70.22           N  
ANISOU 1068  N   SER A 164     6608   7246  12826    365    -89  -1009       N  
ATOM   1069  CA  SER A 164     103.555 192.640   7.822  1.00 69.04           C  
ANISOU 1069  CA  SER A 164     6318   7114  12800    480    -99  -1107       C  
ATOM   1070  C   SER A 164     102.274 192.089   8.437  1.00 68.08           C  
ANISOU 1070  C   SER A 164     6255   6958  12655    289    183  -1247       C  
ATOM   1071  O   SER A 164     101.520 191.343   7.807  1.00 69.26           O  
ANISOU 1071  O   SER A 164     6421   7121  12772      8    344  -1311       O  
ATOM   1072  CB  SER A 164     103.347 194.092   7.392  1.00 70.85           C  
ANISOU 1072  CB  SER A 164     6131   7451  13337    512   -369  -1098       C  
ATOM   1073  OG  SER A 164     104.532 194.634   6.833  1.00 72.09           O  
ANISOU 1073  OG  SER A 164     6313   7613  13467    626   -560   -983       O  
ATOM   1074  N   THR A 165     102.033 192.469   9.687  1.00 67.05           N  
ANISOU 1074  N   THR A 165     6142   6796  12538    425    261  -1329       N  
ATOM   1075  CA  THR A 165     100.864 192.036  10.437  1.00 69.63           C  
ANISOU 1075  CA  THR A 165     6533   7073  12851    266    557  -1473       C  
ATOM   1076  C   THR A 165      99.896 193.198  10.614  1.00 71.03           C  
ANISOU 1076  C   THR A 165     6280   7395  13315    220    412  -1577       C  
ATOM   1077  O   THR A 165     100.220 194.357  10.342  1.00 71.36           O  
ANISOU 1077  O   THR A 165     6045   7523  13546    362    121  -1521       O  
ATOM   1078  CB  THR A 165     101.270 191.472  11.804  1.00 51.58           C  
ANISOU 1078  CB  THR A 165     4654   4632  10310    498    813  -1476       C  
ATOM   1079  OG1 THR A 165     101.874 192.508  12.589  1.00 50.71           O  
ANISOU 1079  OG1 THR A 165     4402   4607  10257    799    587  -1482       O  
ATOM   1080  CG2 THR A 165     102.256 190.330  11.635  1.00 65.07           C  
ANISOU 1080  CG2 THR A 165     6819   6209  11697    628    975  -1347       C  
ATOM   1081  N   ALA A 166      98.687 192.869  11.079  1.00 65.11           N  
ANISOU 1081  N   ALA A 166     9535   6185   9017   1997   1849   -972       N  
ATOM   1082  CA  ALA A 166      97.688 193.902  11.332  1.00 60.08           C  
ANISOU 1082  CA  ALA A 166     9017   5600   8210   1891   1924   -693       C  
ATOM   1083  C   ALA A 166      98.064 194.759  12.533  1.00 57.54           C  
ANISOU 1083  C   ALA A 166     8764   5394   7704   2138   1706   -567       C  
ATOM   1084  O   ALA A 166      97.729 195.949  12.574  1.00 53.47           O  
ANISOU 1084  O   ALA A 166     8267   5005   7044   2066   1696   -486       O  
ATOM   1085  CB  ALA A 166      96.313 193.266  11.540  1.00 44.47           C  
ANISOU 1085  CB  ALA A 166     7215   3393   6287   1821   2115   -361       C  
ATOM   1086  N   LYS A 167      98.751 194.175  13.516  1.00 61.10           N  
ANISOU 1086  N   LYS A 167     9267   5783   8167   2419   1526   -558       N  
ATOM   1087  CA  LYS A 167      99.230 194.959  14.649  1.00 62.05           C  
ANISOU 1087  CA  LYS A 167     9471   6000   8103   2636   1304   -482       C  
ATOM   1088  C   LYS A 167     100.241 196.005  14.194  1.00 62.11           C  
ANISOU 1088  C   LYS A 167     9267   6198   8134   2599   1153   -769       C  
ATOM   1089  O   LYS A 167     100.175 197.169  14.604  1.00 62.39           O  
ANISOU 1089  O   LYS A 167     9360   6350   7994   2620   1045   -704       O  
ATOM   1090  CB  LYS A 167      99.839 194.031  15.702  1.00 65.74           C  
ANISOU 1090  CB  LYS A 167    10047   6338   8594   2921   1154   -429       C  
ATOM   1091  CG  LYS A 167     100.451 194.743  16.899  1.00 67.24           C  
ANISOU 1091  CG  LYS A 167    10366   6616   8567   3159    904   -376       C  
ATOM   1092  CD  LYS A 167     100.938 193.739  17.934  1.00 72.36           C  
ANISOU 1092  CD  LYS A 167    11172   7114   9207   3435    776   -287       C  
ATOM   1093  CE  LYS A 167     102.098 192.902  17.407  1.00 75.84           C  
ANISOU 1093  CE  LYS A 167    11357   7455  10004   3493    680   -562       C  
ATOM   1094  NZ  LYS A 167     103.374 193.672  17.363  1.00 76.68           N  
ANISOU 1094  NZ  LYS A 167    11263   7694  10178   3571    449   -812       N  
ATOM   1095  N   ARG A 168     101.177 195.608  13.329  1.00 60.01           N  
ANISOU 1095  N   ARG A 168     8749   5963   8090   2543   1162  -1101       N  
ATOM   1096  CA  ARG A 168     102.181 196.549  12.845  1.00 61.68           C  
ANISOU 1096  CA  ARG A 168     8733   6358   8346   2498   1074  -1379       C  
ATOM   1097  C   ARG A 168     101.566 197.615  11.943  1.00 59.40           C  
ANISOU 1097  C   ARG A 168     8420   6227   7924   2222   1219  -1397       C  
ATOM   1098  O   ARG A 168     102.086 198.734  11.866  1.00 59.03           O  
ANISOU 1098  O   ARG A 168     8280   6333   7814   2212   1101  -1512       O  
ATOM   1099  CB  ARG A 168     103.291 195.791  12.115  1.00 67.75           C  
ANISOU 1099  CB  ARG A 168     9228   7121   9391   2493   1140  -1720       C  
ATOM   1100  CG  ARG A 168     104.472 196.651  11.699  1.00 72.59           C  
ANISOU 1100  CG  ARG A 168     9606   7935  10039   2478   1064  -1957       C  
ATOM   1101  CD  ARG A 168     105.421 195.893  10.783  1.00 78.98           C  
ANISOU 1101  CD  ARG A 168    10176   8811  11023   2428   1184  -2223       C  
ATOM   1102  NE  ARG A 168     106.409 196.788  10.190  1.00 81.22           N  
ANISOU 1102  NE  ARG A 168    10086   9373  11403   2272   1100  -2496       N  
ATOM   1103  CZ  ARG A 168     107.597 197.048  10.725  1.00 83.93           C  
ANISOU 1103  CZ  ARG A 168    10216   9755  11919   2470    848  -2614       C  
ATOM   1104  NH1 ARG A 168     107.952 196.473  11.865  1.00 86.39           N  
ANISOU 1104  NH1 ARG A 168    10677   9864  12284   2816    630  -2476       N  
ATOM   1105  NH2 ARG A 168     108.431 197.881  10.117  1.00 84.22           N  
ANISOU 1105  NH2 ARG A 168     9868  10034  12097   2293    817  -2873       N  
ATOM   1106  N   ALA A 169     100.462 197.296  11.262  1.00 53.70           N  
ANISOU 1106  N   ALA A 169     7787   5449   7168   1984   1467  -1268       N  
ATOM   1107  CA  ALA A 169      99.807 198.278  10.402  1.00 45.98           C  
ANISOU 1107  CA  ALA A 169     6755   4624   6093   1606   1580  -1220       C  
ATOM   1108  C   ALA A 169      99.018 199.306  11.203  1.00 44.46           C  
ANISOU 1108  C   ALA A 169     6742   4419   5731   1683   1486   -929       C  
ATOM   1109  O   ALA A 169      98.935 200.470  10.797  1.00 44.25           O  
ANISOU 1109  O   ALA A 169     6602   4575   5635   1433   1400   -918       O  
ATOM   1110  CB  ALA A 169      98.887 197.575   9.401  1.00 39.57           C  
ANISOU 1110  CB  ALA A 169     5947   3753   5336   1272   1819  -1174       C  
ATOM   1111  N   LEU A 170      98.428 198.897  12.331  1.00 45.38           N  
ANISOU 1111  N   LEU A 170     7103   4357   5784   1970   1473   -674       N  
ATOM   1112  CA  LEU A 170      97.682 199.828  13.173  1.00 41.26           C  
ANISOU 1112  CA  LEU A 170     6750   3837   5088   2057   1406   -413       C  
ATOM   1113  C   LEU A 170      98.605 200.724  13.987  1.00 40.38           C  
ANISOU 1113  C   LEU A 170     6645   3832   4865   2265   1098   -520       C  
ATOM   1114  O   LEU A 170      98.282 201.896  14.207  1.00 40.26           O  
ANISOU 1114  O   LEU A 170     6692   3870   4736   2257   1021   -454       O  
ATOM   1115  CB  LEU A 170      96.737 199.061  14.101  1.00 40.17           C  
ANISOU 1115  CB  LEU A 170     6817   3560   4885   2182   1503    -91       C  
ATOM   1116  CG  LEU A 170      95.473 198.494  13.451  1.00 39.84           C  
ANISOU 1116  CG  LEU A 170     6795   3377   4964   1971   1806    103       C  
ATOM   1117  CD1 LEU A 170      94.895 197.368  14.291  1.00 43.03           C  
ANISOU 1117  CD1 LEU A 170     7353   3642   5357   2107   1912    342       C  
ATOM   1118  CD2 LEU A 170      94.442 199.593  13.248  1.00 38.51           C  
ANISOU 1118  CD2 LEU A 170     6645   3224   4763   1830   1914    282       C  
ATOM   1119  N   ASN A 171      99.747 200.202  14.441  1.00 42.35           N  
ANISOU 1119  N   ASN A 171     6831   4086   5172   2453    908   -688       N  
ATOM   1120  CA  ASN A 171     100.701 201.045  15.154  1.00 46.88           C  
ANISOU 1120  CA  ASN A 171     7399   4739   5675   2636    591   -809       C  
ATOM   1121  C   ASN A 171     101.340 202.073  14.230  1.00 47.78           C  
ANISOU 1121  C   ASN A 171     7287   4990   5877   2494    512  -1079       C  
ATOM   1122  O   ASN A 171     101.621 203.198  14.658  1.00 40.45           O  
ANISOU 1122  O   ASN A 171     6386   4114   4867   2564    272  -1121       O  
ATOM   1123  CB  ASN A 171     101.771 200.188  15.825  1.00 52.17           C  
ANISOU 1123  CB  ASN A 171     8047   5356   6418   2870    409   -907       C  
ATOM   1124  CG  ASN A 171     101.308 199.627  17.150  1.00 58.87           C  
ANISOU 1124  CG  ASN A 171     9208   6106   7052   3090    370   -645       C  
ATOM   1125  OD1 ASN A 171     100.728 198.545  17.210  1.00 60.40           O  
ANISOU 1125  OD1 ASN A 171     9489   6188   7272   3089    561   -494       O  
ATOM   1126  ND2 ASN A 171     101.548 200.372  18.223  1.00 63.05           N  
ANISOU 1126  ND2 ASN A 171     9931   6681   7345   3282    127   -606       N  
ATOM   1127  N   SER A 172     101.582 201.711  12.969  1.00 40.01           N  
ANISOU 1127  N   SER A 172     6045   4104   5054   2207    689  -1250       N  
ATOM   1128  CA  SER A 172     102.028 202.707  12.004  1.00 39.26           C  
ANISOU 1128  CA  SER A 172     5642   4243   5032   1810    630  -1389       C  
ATOM   1129  C   SER A 172     100.927 203.715  11.711  1.00 41.35           C  
ANISOU 1129  C   SER A 172     5985   4552   5173   1533    678  -1162       C  
ATOM   1130  O   SER A 172     101.211 204.885  11.430  1.00 41.34           O  
ANISOU 1130  O   SER A 172     5842   4682   5183   1326    517  -1198       O  
ATOM   1131  CB  SER A 172     102.477 202.023  10.715  1.00 68.13           C  
ANISOU 1131  CB  SER A 172     9017   8028   8843   1502    845  -1590       C  
ATOM   1132  OG  SER A 172     103.368 200.957  10.988  1.00 70.00           O  
ANISOU 1132  OG  SER A 172     9185   8179   9234   1790    835  -1791       O  
ATOM   1133  N   ILE A 173      99.668 203.279  11.777  1.00 39.91           N  
ANISOU 1133  N   ILE A 173     6010   4243   4913   1526    887   -918       N  
ATOM   1134  CA  ILE A 173      98.548 204.184  11.553  1.00 38.66           C  
ANISOU 1134  CA  ILE A 173     5909   4096   4684   1301    928   -687       C  
ATOM   1135  C   ILE A 173      98.429 205.179  12.698  1.00 40.56           C  
ANISOU 1135  C   ILE A 173     6342   4265   4805   1588    724   -599       C  
ATOM   1136  O   ILE A 173      98.185 206.372  12.481  1.00 39.63           O  
ANISOU 1136  O   ILE A 173     6165   4212   4682   1399    605   -547       O  
ATOM   1137  CB  ILE A 173      97.253 203.375  11.357  1.00 37.36           C  
ANISOU 1137  CB  ILE A 173     5872   3794   4528   1233   1204   -454       C  
ATOM   1138  CG1 ILE A 173      97.146 202.912   9.902  1.00 35.44           C  
ANISOU 1138  CG1 ILE A 173     5424   3662   4378    786   1346   -536       C  
ATOM   1139  CG2 ILE A 173      96.033 204.184  11.787  1.00 36.03           C  
ANISOU 1139  CG2 ILE A 173     5844   3544   4300   1242   1233   -170       C  
ATOM   1140  CD1 ILE A 173      96.078 201.871   9.668  1.00 34.49           C  
ANISOU 1140  CD1 ILE A 173     5403   3380   4323    724   1578   -371       C  
ATOM   1141  N   VAL A 174      98.600 204.707  13.934  1.00 42.30           N  
ANISOU 1141  N   VAL A 174     6820   4339   4915   2053    671   -583       N  
ATOM   1142  CA  VAL A 174      98.592 205.610  15.081  1.00 36.51           C  
ANISOU 1142  CA  VAL A 174     6318   3537   4016   2363    459   -549       C  
ATOM   1143  C   VAL A 174      99.702 206.645  14.943  1.00 40.42           C  
ANISOU 1143  C   VAL A 174     6618   4157   4583   2268    111   -786       C  
ATOM   1144  O   VAL A 174      99.496 207.841  15.182  1.00 40.13           O  
ANISOU 1144  O   VAL A 174     6627   4119   4503   2235    -54   -763       O  
ATOM   1145  CB  VAL A 174      98.721 204.812  16.391  1.00 38.52           C  
ANISOU 1145  CB  VAL A 174     6759   3760   4117   2625    397   -440       C  
ATOM   1146  CG1 VAL A 174      98.998 205.742  17.558  1.00 39.99           C  
ANISOU 1146  CG1 VAL A 174     7128   3969   4096   2830    117   -459       C  
ATOM   1147  CG2 VAL A 174      97.458 204.008  16.642  1.00 38.32           C  
ANISOU 1147  CG2 VAL A 174     6872   3664   4022   2597    707   -145       C  
ATOM   1148  N   ILE A 175     100.890 206.201  14.528  1.00 42.97           N  
ANISOU 1148  N   ILE A 175     6696   4576   5056   2213      4  -1019       N  
ATOM   1149  CA  ILE A 175     102.037 207.100  14.434  1.00 43.81           C  
ANISOU 1149  CA  ILE A 175     6571   4788   5287   2126   -324  -1243       C  
ATOM   1150  C   ILE A 175     101.804 208.160  13.365  1.00 42.01           C  
ANISOU 1150  C   ILE A 175     6104   4698   5160   1637   -303  -1204       C  
ATOM   1151  O   ILE A 175     102.176 209.327  13.537  1.00 42.66           O  
ANISOU 1151  O   ILE A 175     6126   4794   5290   1574   -575  -1263       O  
ATOM   1152  CB  ILE A 175     103.319 206.290  14.169  1.00 43.61           C  
ANISOU 1152  CB  ILE A 175     6284   4832   5453   2173   -387  -1489       C  
ATOM   1153  CG1 ILE A 175     103.695 205.499  15.417  1.00 42.91           C  
ANISOU 1153  CG1 ILE A 175     6456   4577   5270   2702   -546  -1524       C  
ATOM   1154  CG2 ILE A 175     104.462 207.197  13.743  1.00 42.01           C  
ANISOU 1154  CG2 ILE A 175     5727   4771   5466   1956   -645  -1702       C  
ATOM   1155  CD1 ILE A 175     104.686 204.416  15.153  1.00 44.68           C  
ANISOU 1155  CD1 ILE A 175     6455   4816   5704   2792   -534  -1716       C  
ATOM   1156  N   ILE A 176     101.175 207.773  12.253  1.00 39.66           N  
ANISOU 1156  N   ILE A 176     5687   4488   4895   1283     -4  -1098       N  
ATOM   1157  CA  ILE A 176     100.892 208.721  11.177  1.00 38.08           C  
ANISOU 1157  CA  ILE A 176     5294   4417   4758    804     14  -1022       C  
ATOM   1158  C   ILE A 176     100.048 209.881  11.688  1.00 37.56           C  
ANISOU 1158  C   ILE A 176     5409   4238   4624    841   -126   -841       C  
ATOM   1159  O   ILE A 176     100.297 211.046  11.354  1.00 37.99           O  
ANISOU 1159  O   ILE A 176     5331   4339   4765    606   -318   -847       O  
ATOM   1160  CB  ILE A 176     100.208 207.999  10.001  1.00 37.99           C  
ANISOU 1160  CB  ILE A 176     5207   4490   4737    463    335   -923       C  
ATOM   1161  CG1 ILE A 176     101.218 207.129   9.251  1.00 40.69           C  
ANISOU 1161  CG1 ILE A 176     5311   4979   5171    340    462  -1162       C  
ATOM   1162  CG2 ILE A 176      99.536 209.004   9.072  1.00 32.85           C  
ANISOU 1162  CG2 ILE A 176     4472   3920   4089     21    331   -749       C  
ATOM   1163  CD1 ILE A 176     100.581 206.091   8.354  1.00 40.76           C  
ANISOU 1163  CD1 ILE A 176     5333   5015   5140    135    768  -1122       C  
ATOM   1164  N   TRP A 177      99.041 209.584  12.511  1.00 37.19           N  
ANISOU 1164  N   TRP A 177     5662   4028   4441   1141    -16   -674       N  
ATOM   1165  CA  TRP A 177      98.204 210.650  13.050  1.00 35.65           C  
ANISOU 1165  CA  TRP A 177     5641   3712   4194   1224   -109   -523       C  
ATOM   1166  C   TRP A 177      98.970 211.507  14.048  1.00 38.75           C  
ANISOU 1166  C   TRP A 177     6145   4031   4548   1504   -461   -693       C  
ATOM   1167  O   TRP A 177      98.786 212.729  14.094  1.00 40.58           O  
ANISOU 1167  O   TRP A 177     6379   4208   4831   1414   -649   -671       O  
ATOM   1168  CB  TRP A 177      96.953 210.061  13.695  1.00 33.37           C  
ANISOU 1168  CB  TRP A 177     5622   3274   3782   1486    152   -304       C  
ATOM   1169  CG  TRP A 177      95.925 209.645  12.702  1.00 31.64           C  
ANISOU 1169  CG  TRP A 177     5286   3082   3655   1155    420    -95       C  
ATOM   1170  CD1 TRP A 177      95.729 208.393  12.201  1.00 32.06           C  
ANISOU 1170  CD1 TRP A 177     5291   3159   3731   1065    660    -60       C  
ATOM   1171  CD2 TRP A 177      94.948 210.485  12.080  1.00 30.75           C  
ANISOU 1171  CD2 TRP A 177     5087   2953   3644    867    436    103       C  
ATOM   1172  NE1 TRP A 177      94.687 208.400  11.306  1.00 30.24           N  
ANISOU 1172  NE1 TRP A 177     4957   2934   3598    730    809    140       N  
ATOM   1173  CE2 TRP A 177      94.192 209.673  11.214  1.00 30.94           C  
ANISOU 1173  CE2 TRP A 177     5014   3003   3740    605    670    253       C  
ATOM   1174  CE3 TRP A 177      94.639 211.846  12.172  1.00 32.88           C  
ANISOU 1174  CE3 TRP A 177     5354   3166   3974    810    248    164       C  
ATOM   1175  CZ2 TRP A 177      93.145 210.175  10.446  1.00 33.54           C  
ANISOU 1175  CZ2 TRP A 177     5236   3316   4193    290    701    472       C  
ATOM   1176  CZ3 TRP A 177      93.601 212.342  11.409  1.00 34.27           C  
ANISOU 1176  CZ3 TRP A 177     5418   3318   4287    509    299    390       C  
ATOM   1177  CH2 TRP A 177      92.866 211.510  10.557  1.00 35.04           C  
ANISOU 1177  CH2 TRP A 177     5413   3454   4448    252    513    547       C  
ATOM   1178  N   ILE A 178      99.835 210.888  14.854  1.00 40.67           N  
ANISOU 1178  N   ILE A 178     6487   4249   4715   1848   -585   -869       N  
ATOM   1179  CA  ILE A 178     100.632 211.649  15.812  1.00 43.39           C  
ANISOU 1179  CA  ILE A 178     6948   4518   5022   2117   -979  -1058       C  
ATOM   1180  C   ILE A 178     101.587 212.584  15.083  1.00 42.23           C  
ANISOU 1180  C   ILE A 178     6448   4469   5126   1760  -1248  -1210       C  
ATOM   1181  O   ILE A 178     101.762 213.747  15.469  1.00 40.37           O  
ANISOU 1181  O   ILE A 178     6258   4147   4934   1774  -1550  -1276       O  
ATOM   1182  CB  ILE A 178     101.384 210.695  16.759  1.00 46.88           C  
ANISOU 1182  CB  ILE A 178     7556   4913   5343   2546  -1090  -1198       C  
ATOM   1183  CG1 ILE A 178     100.395 209.925  17.632  1.00 46.94           C  
ANISOU 1183  CG1 ILE A 178     7919   4845   5071   2830   -824   -974       C  
ATOM   1184  CG2 ILE A 178     102.389 211.464  17.608  1.00 43.26           C  
ANISOU 1184  CG2 ILE A 178     7162   4391   4885   2770  -1574  -1431       C  
ATOM   1185  CD1 ILE A 178     101.023 208.779  18.385  1.00 42.60           C  
ANISOU 1185  CD1 ILE A 178     7443   4339   4404   3032   -857   -983       C  
ATOM   1186  N   VAL A 179     102.217 212.092  14.015  1.00 40.90           N  
ANISOU 1186  N   VAL A 179     5930   4477   5135   1431  -1126  -1267       N  
ATOM   1187  CA  VAL A 179     103.158 212.912  13.257  1.00 43.41           C  
ANISOU 1187  CA  VAL A 179     5885   4908   5703   1062  -1317  -1385       C  
ATOM   1188  C   VAL A 179     102.432 214.068  12.580  1.00 41.29           C  
ANISOU 1188  C   VAL A 179     5573   4629   5487    692  -1316  -1202       C  
ATOM   1189  O   VAL A 179     102.874 215.222  12.640  1.00 40.71           O  
ANISOU 1189  O   VAL A 179     5406   4500   5560    568  -1614  -1256       O  
ATOM   1190  CB  VAL A 179     103.918 212.051  12.232  1.00 43.37           C  
ANISOU 1190  CB  VAL A 179     5531   5107   5841    804  -1103  -1483       C  
ATOM   1191  CG1 VAL A 179     104.682 212.936  11.265  1.00 41.11           C  
ANISOU 1191  CG1 VAL A 179     4867   4963   5792    344  -1189  -1533       C  
ATOM   1192  CG2 VAL A 179     104.859 211.089  12.940  1.00 41.92           C  
ANISOU 1192  CG2 VAL A 179     5329   4903   5697   1179  -1200  -1696       C  
ATOM   1193  N   SER A 180     101.309 213.772  11.921  1.00 38.50           N  
ANISOU 1193  N   SER A 180     5280   4308   5041    507  -1007   -976       N  
ATOM   1194  CA  SER A 180     100.559 214.812  11.223  1.00 37.15           C  
ANISOU 1194  CA  SER A 180     5065   4115   4934    156  -1021   -773       C  
ATOM   1195  C   SER A 180     100.073 215.888  12.185  1.00 36.80           C  
ANISOU 1195  C   SER A 180     5256   3846   4879    403  -1272   -743       C  
ATOM   1196  O   SER A 180     100.135 217.083  11.875  1.00 37.17           O  
ANISOU 1196  O   SER A 180     5209   3835   5081    165  -1488   -700       O  
ATOM   1197  CB  SER A 180      99.377 214.192  10.476  1.00 36.46           C  
ANISOU 1197  CB  SER A 180     5023   4075   4756    -26   -685   -541       C  
ATOM   1198  OG  SER A 180      99.816 213.259   9.506  1.00 36.91           O  
ANISOU 1198  OG  SER A 180     4884   4331   4808   -280   -463   -596       O  
ATOM   1199  N   CYS A 181      99.584 215.482  13.360  1.00 37.79           N  
ANISOU 1199  N   CYS A 181     5706   3834   4821    884  -1238   -765       N  
ATOM   1200  CA  CYS A 181      99.069 216.453  14.319  1.00 41.31           C  
ANISOU 1200  CA  CYS A 181     6418   4065   5214   1161  -1431   -765       C  
ATOM   1201  C   CYS A 181     100.169 217.353  14.862  1.00 47.62           C  
ANISOU 1201  C   CYS A 181     7194   4783   6115   1238  -1875  -1010       C  
ATOM   1202  O   CYS A 181      99.903 218.500  15.234  1.00 49.82           O  
ANISOU 1202  O   CYS A 181     7587   4888   6455   1280  -2104  -1025       O  
ATOM   1203  CB  CYS A 181      98.355 215.737  15.464  1.00 41.30           C  
ANISOU 1203  CB  CYS A 181     6789   3957   4945   1666  -1245   -735       C  
ATOM   1204  SG  CYS A 181      96.709 215.140  15.039  1.00 40.37           S  
ANISOU 1204  SG  CYS A 181     6726   3827   4787   1600   -775   -404       S  
ATOM   1205  N   ILE A 182     101.403 216.859  14.915  1.00 49.63           N  
ANISOU 1205  N   ILE A 182     7289   5143   6425   1258  -2018  -1210       N  
ATOM   1206  CA  ILE A 182     102.504 217.680  15.400  1.00 43.67           C  
ANISOU 1206  CA  ILE A 182     6463   4304   5823   1305  -2477  -1447       C  
ATOM   1207  C   ILE A 182     102.977 218.643  14.321  1.00 54.07           C  
ANISOU 1207  C   ILE A 182     7408   5673   7465    774  -2605  -1403       C  
ATOM   1208  O   ILE A 182     103.132 219.845  14.566  1.00 45.63           O  
ANISOU 1208  O   ILE A 182     6356   4436   6547    717  -2937  -1457       O  
ATOM   1209  CB  ILE A 182     103.656 216.790  15.895  1.00 45.24           C  
ANISOU 1209  CB  ILE A 182     6597   4579   6012   1541  -2610  -1669       C  
ATOM   1210  CG1 ILE A 182     103.239 216.056  17.167  1.00 52.63           C  
ANISOU 1210  CG1 ILE A 182     7981   5412   6602   2105  -2581  -1706       C  
ATOM   1211  CG2 ILE A 182     104.904 217.623  16.129  1.00 48.16           C  
ANISOU 1211  CG2 ILE A 182     6764   4888   6645   1476  -3095  -1903       C  
ATOM   1212  CD1 ILE A 182     104.181 214.948  17.549  1.00 54.28           C  
ANISOU 1212  CD1 ILE A 182     8143   5695   6788   2343  -2648  -1857       C  
ATOM   1213  N   ILE A 183     103.217 218.130  13.111  1.00 51.58           N  
ANISOU 1213  N   ILE A 183     6768   5579   7250    377  -2339  -1303       N  
ATOM   1214  CA  ILE A 183     103.836 218.939  12.069  1.00 50.34           C  
ANISOU 1214  CA  ILE A 183     6247   5503   7376   -138  -2430  -1255       C  
ATOM   1215  C   ILE A 183     102.899 220.011  11.532  1.00 50.69           C  
ANISOU 1215  C   ILE A 183     6348   5437   7474   -422  -2444  -1010       C  
ATOM   1216  O   ILE A 183     103.362 220.964  10.894  1.00 51.32           O  
ANISOU 1216  O   ILE A 183     6199   5503   7797   -808  -2613   -952       O  
ATOM   1217  CB  ILE A 183     104.340 218.053  10.915  1.00 47.42           C  
ANISOU 1217  CB  ILE A 183     5555   5419   7045   -469  -2097  -1228       C  
ATOM   1218  CG1 ILE A 183     103.176 217.291  10.275  1.00 43.54           C  
ANISOU 1218  CG1 ILE A 183     5197   5023   6323   -555  -1691  -1014       C  
ATOM   1219  CG2 ILE A 183     105.423 217.105  11.405  1.00 48.23           C  
ANISOU 1219  CG2 ILE A 183     5531   5604   7189   -202  -2130  -1489       C  
ATOM   1220  CD1 ILE A 183     103.559 216.542   9.017  1.00 41.52           C  
ANISOU 1220  CD1 ILE A 183     4669   5036   6070   -925  -1365   -990       C  
ATOM   1221  N   MET A 184     101.593 219.884  11.758  1.00 40.61           N  
ANISOU 1221  N   MET A 184     4236   3056   8139   -404   -151   -652       N  
ATOM   1222  CA  MET A 184     100.634 220.886  11.316  1.00 41.41           C  
ANISOU 1222  CA  MET A 184     4266   3148   8319   -423   -223   -610       C  
ATOM   1223  C   MET A 184     100.212 221.819  12.442  1.00 43.06           C  
ANISOU 1223  C   MET A 184     4459   3259   8644   -244   -489   -782       C  
ATOM   1224  O   MET A 184      99.300 222.630  12.257  1.00 41.00           O  
ANISOU 1224  O   MET A 184     4159   2978   8442   -231   -566   -782       O  
ATOM   1225  CB  MET A 184      99.413 220.208  10.693  1.00 39.49           C  
ANISOU 1225  CB  MET A 184     4109   3038   7857   -551      3   -579       C  
ATOM   1226  CG  MET A 184      99.753 219.383   9.462  1.00 39.72           C  
ANISOU 1226  CG  MET A 184     4165   3204   7725   -707    223   -414       C  
ATOM   1227  SD  MET A 184     100.754 220.313   8.284  1.00 41.56           S  
ANISOU 1227  SD  MET A 184     4261   3389   8140   -732    161   -196       S  
ATOM   1228  CE  MET A 184     101.192 219.045   7.100  1.00 40.31           C  
ANISOU 1228  CE  MET A 184     4195   3402   7718   -859    405    -64       C  
ATOM   1229  N   ILE A 185     100.860 221.714  13.606  1.00 45.88           N  
ANISOU 1229  N   ILE A 185     4859   3569   9005    -85   -645   -937       N  
ATOM   1230  CA  ILE A 185     100.591 222.670  14.684  1.00 46.83           C  
ANISOU 1230  CA  ILE A 185     4977   3632   9186    118   -937  -1106       C  
ATOM   1231  C   ILE A 185     100.940 224.095  14.292  1.00 50.97           C  
ANISOU 1231  C   ILE A 185     5289   4052  10027    105  -1164  -1045       C  
ATOM   1232  O   ILE A 185     100.154 225.004  14.604  1.00 54.14           O  
ANISOU 1232  O   ILE A 185     5684   4423  10465    193  -1329  -1114       O  
ATOM   1233  CB  ILE A 185     101.292 222.207  15.977  1.00 43.87           C  
ANISOU 1233  CB  ILE A 185     4714   3267   8689    309  -1055  -1279       C  
ATOM   1234  CG1 ILE A 185     100.357 221.290  16.763  1.00 42.58           C  
ANISOU 1234  CG1 ILE A 185     4811   3198   8169    450   -885  -1375       C  
ATOM   1235  CG2 ILE A 185     101.719 223.399  16.821  1.00 46.10           C  
ANISOU 1235  CG2 ILE A 185     4895   3483   9138    471  -1428  -1419       C  
ATOM   1236  CD1 ILE A 185     101.048 220.533  17.856  1.00 45.79           C  
ANISOU 1236  CD1 ILE A 185     5381   3645   8370    643   -889  -1481       C  
ATOM   1237  N   PRO A 186     102.067 224.387  13.625  1.00 51.00           N  
ANISOU 1237  N   PRO A 186     5116   3988  10272     16  -1174   -915       N  
ATOM   1238  CA  PRO A 186     102.313 225.783  13.223  1.00 52.37           C  
ANISOU 1238  CA  PRO A 186     5090   4039  10770     15  -1353   -842       C  
ATOM   1239  C   PRO A 186     101.223 226.360  12.340  1.00 52.86           C  
ANISOU 1239  C   PRO A 186     5160   4103  10823    -57  -1263   -708       C  
ATOM   1240  O   PRO A 186     101.037 227.583  12.330  1.00 54.96           O  
ANISOU 1240  O   PRO A 186     5317   4262  11303    -13  -1448   -706       O  
ATOM   1241  CB  PRO A 186     103.659 225.708  12.488  1.00 53.61           C  
ANISOU 1241  CB  PRO A 186     5088   4138  11144    -72  -1272   -687       C  
ATOM   1242  CG  PRO A 186     103.823 224.277  12.116  1.00 51.32           C  
ANISOU 1242  CG  PRO A 186     4938   3972  10588   -160   -994   -624       C  
ATOM   1243  CD  PRO A 186     103.208 223.528  13.259  1.00 49.94           C  
ANISOU 1243  CD  PRO A 186     4953   3872  10149    -62  -1029   -834       C  
ATOM   1244  N   GLN A 187     100.462 225.526  11.648  1.00 51.04           N  
ANISOU 1244  N   GLN A 187     5048   3986  10357   -169   -995   -609       N  
ATOM   1245  CA  GLN A 187      99.398 226.085  10.782  1.00 47.95           C  
ANISOU 1245  CA  GLN A 187     4658   3605   9956   -231   -926   -502       C  
ATOM   1246  C   GLN A 187      98.300 226.634  11.684  1.00 46.31           C  
ANISOU 1246  C   GLN A 187     4510   3375   9710   -101  -1108   -681       C  
ATOM   1247  O   GLN A 187      97.837 227.728  11.438  1.00 45.85           O  
ANISOU 1247  O   GLN A 187     4390   3243   9787    -80  -1215   -637       O  
ATOM   1248  CB  GLN A 187      98.818 225.015   9.869  1.00 45.89           C  
ANISOU 1248  CB  GLN A 187     4495   3496   9444   -384   -622   -393       C  
ATOM   1249  CG  GLN A 187      97.785 225.564   8.914  1.00 46.59           C  
ANISOU 1249  CG  GLN A 187     4562   3614   9525   -461   -549   -279       C  
ATOM   1250  CD  GLN A 187      98.418 226.390   7.829  1.00 50.76           C  
ANISOU 1250  CD  GLN A 187     4983   4091  10214   -521   -489    -31       C  
ATOM   1251  OE1 GLN A 187      99.621 226.583   7.793  1.00 52.23           O  
ANISOU 1251  OE1 GLN A 187     5158   4312  10375   -576   -358     90       O  
ATOM   1252  NE2 GLN A 187      97.605 226.869   6.912  1.00 53.48           N  
ANISOU 1252  NE2 GLN A 187     5252   4339  10729   -496   -578     50       N  
ATOM   1253  N   ALA A 188      97.954 225.902  12.730  1.00 45.08           N  
ANISOU 1253  N   ALA A 188     4490   3282   9355     10  -1139   -881       N  
ATOM   1254  CA  ALA A 188      96.904 226.366  13.632  1.00 38.14           C  
ANISOU 1254  CA  ALA A 188     3702   2408   8380    187  -1300  -1062       C  
ATOM   1255  C   ALA A 188      97.294 227.654  14.347  1.00 48.35           C  
ANISOU 1255  C   ALA A 188     4922   3602   9845    332  -1637  -1158       C  
ATOM   1256  O   ALA A 188      96.439 228.517  14.576  1.00 49.38           O  
ANISOU 1256  O   ALA A 188     5074   3710   9980    435  -1785  -1223       O  
ATOM   1257  CB  ALA A 188      96.570 225.275  14.647  1.00 37.22           C  
ANISOU 1257  CB  ALA A 188     3774   2397   7970    310  -1202  -1225       C  
ATOM   1258  N   ILE A 189      98.572 227.806  14.703  1.00 48.59           N  
ANISOU 1258  N   ILE A 189     4859   3576  10028    340  -1768  -1181       N  
ATOM   1259  CA  ILE A 189      99.033 229.043  15.327  1.00 49.83           C  
ANISOU 1259  CA  ILE A 189     4907   3623  10403    443  -2102  -1290       C  
ATOM   1260  C   ILE A 189      98.914 230.213  14.362  1.00 51.61           C  
ANISOU 1260  C   ILE A 189     4970   3716  10922    348  -2143  -1132       C  
ATOM   1261  O   ILE A 189      98.653 231.348  14.778  1.00 52.85           O  
ANISOU 1261  O   ILE A 189     5091   3786  11204    436  -2391  -1226       O  
ATOM   1262  CB  ILE A 189     100.483 228.879  15.819  1.00 48.18           C  
ANISOU 1262  CB  ILE A 189     4588   3369  10350    459  -2228  -1357       C  
ATOM   1263  CG1 ILE A 189     100.645 227.571  16.587  1.00 44.63           C  
ANISOU 1263  CG1 ILE A 189     4321   3048   9588    538  -2122  -1468       C  
ATOM   1264  CG2 ILE A 189     100.902 230.053  16.690  1.00 48.33           C  
ANISOU 1264  CG2 ILE A 189     4502   3282  10577    586  -2614  -1539       C  
ATOM   1265  CD1 ILE A 189     102.082 227.187  16.799  1.00 45.55           C  
ANISOU 1265  CD1 ILE A 189     4324   3127   9855    523  -2184  -1496       C  
ATOM   1266  N   VAL A 190      99.087 229.960  13.064  1.00 51.13           N  
ANISOU 1266  N   VAL A 190     4834   3642  10952    181  -1893   -887       N  
ATOM   1267  CA  VAL A 190      99.242 231.046  12.101  1.00 50.90           C  
ANISOU 1267  CA  VAL A 190     4648   3473  11218    101  -1900   -700       C  
ATOM   1268  C   VAL A 190      97.891 231.599  11.661  1.00 49.31           C  
ANISOU 1268  C   VAL A 190     4520   3267  10947    113  -1888   -657       C  
ATOM   1269  O   VAL A 190      97.752 232.805  11.427  1.00 47.81           O  
ANISOU 1269  O   VAL A 190     4248   2942  10976    128  -2020   -609       O  
ATOM   1270  CB  VAL A 190     100.088 230.562  10.908  1.00 50.11           C  
ANISOU 1270  CB  VAL A 190     4460   3374  11206    -48  -1632   -447       C  
ATOM   1271  CG1 VAL A 190      99.655 231.232   9.624  1.00 52.00           C  
ANISOU 1271  CG1 VAL A 190     4647   3551  11562   -134  -1495   -204       C  
ATOM   1272  CG2 VAL A 190     101.560 230.830  11.168  1.00 52.01           C  
ANISOU 1272  CG2 VAL A 190     4524   3508  11731    -39  -1737   -455       C  
ATOM   1273  N   MET A 191      96.882 230.737  11.543  1.00 46.07           N  
ANISOU 1273  N   MET A 191     4259   2990  10257    109  -1730   -680       N  
ATOM   1274  CA  MET A 191      95.559 231.185  11.125  1.00 46.42           C  
ANISOU 1274  CA  MET A 191     4361   3030  10248    140  -1725   -656       C  
ATOM   1275  C   MET A 191      95.024 232.239  12.085  1.00 47.70           C  
ANISOU 1275  C   MET A 191     4570   3135  10420    322  -2017   -844       C  
ATOM   1276  O   MET A 191      95.171 232.126  13.304  1.00 46.51           O  
ANISOU 1276  O   MET A 191     4496   3036  10142    454  -2177  -1059       O  
ATOM   1277  CB  MET A 191      94.591 230.003  11.050  1.00 44.49           C  
ANISOU 1277  CB  MET A 191     4241   2934   9730    122  -1532   -714       C  
ATOM   1278  CG  MET A 191      94.998 228.929  10.057  1.00 43.86           C  
ANISOU 1278  CG  MET A 191     4138   2940   9586    -84  -1235   -543       C  
ATOM   1279  SD  MET A 191      95.187 229.550   8.375  1.00 45.31           S  
ANISOU 1279  SD  MET A 191     4200   3054   9962   -228  -1098   -213       S  
ATOM   1280  CE  MET A 191      93.512 230.054   7.997  1.00 45.38           C  
ANISOU 1280  CE  MET A 191     4238   3035   9970   -180  -1149   -236       C  
ATOM   1281  N   GLU A 192      94.412 233.279  11.524  1.00 50.70           N  
ANISOU 1281  N   GLU A 192     4922   3415  10926    341  -2080   -755       N  
ATOM   1282  CA  GLU A 192      93.868 234.368  12.320  1.00 55.46           C  
ANISOU 1282  CA  GLU A 192     5588   3967  11518    512  -2342   -918       C  
ATOM   1283  C   GLU A 192      92.613 234.904  11.649  1.00 56.49           C  
ANISOU 1283  C   GLU A 192     5772   4093  11598    584  -2304   -834       C  
ATOM   1284  O   GLU A 192      92.567 235.061  10.426  1.00 56.95           O  
ANISOU 1284  O   GLU A 192     5756   4082  11801    478  -2152   -594       O  
ATOM   1285  CB  GLU A 192      94.890 235.494  12.514  1.00 60.54           C  
ANISOU 1285  CB  GLU A 192     6096   4424  12483    480  -2542   -914       C  
ATOM   1286  CG  GLU A 192      95.861 235.264  13.663  1.00 64.59           C  
ANISOU 1286  CG  GLU A 192     6579   4953  13010    530  -2721  -1113       C  
ATOM   1287  CD  GLU A 192      95.270 235.629  15.011  1.00 68.31           C  
ANISOU 1287  CD  GLU A 192     7208   5485  13264    747  -2976  -1394       C  
ATOM   1288  OE1 GLU A 192      95.046 236.834  15.256  1.00 71.72           O  
ANISOU 1288  OE1 GLU A 192     7632   5796  13821    822  -3188  -1463       O  
ATOM   1289  OE2 GLU A 192      95.024 234.711  15.823  1.00 67.40           O  
ANISOU 1289  OE2 GLU A 192     7235   5539  12836    857  -2945  -1536       O  
ATOM   1290  N   CYS A 193      91.602 235.180  12.468  1.00 56.70           N  
ANISOU 1290  N   CYS A 193     5933   4218  11391    796  -2435  -1021       N  
ATOM   1291  CA  CYS A 193      90.309 235.682  12.019  1.00 56.64           C  
ANISOU 1291  CA  CYS A 193     5975   4270  11276    939  -2424   -977       C  
ATOM   1292  C   CYS A 193      90.233 237.175  12.315  1.00 59.41           C  
ANISOU 1292  C   CYS A 193     6357   4482  11734   1036  -2643  -1012       C  
ATOM   1293  O   CYS A 193      90.231 237.577  13.483  1.00 59.61           O  
ANISOU 1293  O   CYS A 193     6472   4525  11653   1166  -2840  -1226       O  
ATOM   1294  CB  CYS A 193      89.177 234.929  12.716  1.00 55.82           C  
ANISOU 1294  CB  CYS A 193     5973   4423  10811   1138  -2379  -1150       C  
ATOM   1295  SG  CYS A 193      87.529 235.269  12.073  1.00 57.41           S  
ANISOU 1295  SG  CYS A 193     6151   4822  10842   1339  -2334  -1092       S  
ATOM   1296  N   SER A 194      90.179 237.995  11.266  1.00 61.28           N  
ANISOU 1296  N   SER A 194     6529   4578  12178    987  -2601   -796       N  
ATOM   1297  CA  SER A 194      90.234 239.441  11.423  1.00 66.38           C  
ANISOU 1297  CA  SER A 194     7190   5043  12988   1052  -2781   -802       C  
ATOM   1298  C   SER A 194      89.117 240.113  10.636  1.00 66.90           C  
ANISOU 1298  C   SER A 194     7305   5142  12972   1200  -2727   -657       C  
ATOM   1299  O   SER A 194      88.666 239.608   9.605  1.00 64.57           O  
ANISOU 1299  O   SER A 194     6965   4948  12622   1193  -2538   -464       O  
ATOM   1300  CB  SER A 194      91.587 239.998  10.965  1.00 71.35           C  
ANISOU 1300  CB  SER A 194     7661   5418  14032    849  -2782   -656       C  
ATOM   1301  OG  SER A 194      91.788 239.747   9.586  1.00 72.75           O  
ANISOU 1301  OG  SER A 194     7748   5552  14342    717  -2526   -345       O  
ATOM   1302  N   THR A 195      88.678 241.265  11.142  1.00 70.82           N  
ANISOU 1302  N   THR A 195     7886   5569  13452   1357  -2907   -754       N  
ATOM   1303  CA  THR A 195      87.700 242.112  10.470  1.00 73.27           C  
ANISOU 1303  CA  THR A 195     8249   5897  13693   1526  -2881   -617       C  
ATOM   1304  C   THR A 195      88.448 243.132   9.620  1.00 76.53           C  
ANISOU 1304  C   THR A 195     8590   6004  14482   1415  -2839   -378       C  
ATOM   1305  O   THR A 195      89.334 243.830  10.123  1.00 75.98           O  
ANISOU 1305  O   THR A 195     8476   5700  14692   1322  -2979   -452       O  
ATOM   1306  CB  THR A 195      86.800 242.824  11.481  1.00 74.20           C  
ANISOU 1306  CB  THR A 195     8510   6109  13576   1771  -3074   -840       C  
ATOM   1307  OG1 THR A 195      87.608 243.461  12.482  1.00 76.68           O  
ANISOU 1307  OG1 THR A 195     8844   6223  14068   1728  -3297  -1027       O  
ATOM   1308  CG2 THR A 195      85.861 241.827  12.147  1.00 70.65           C  
ANISOU 1308  CG2 THR A 195     8120   6006  12718   1917  -3040  -1011       C  
ATOM   1309  N   VAL A 196      88.094 243.212   8.337  1.00 80.98           N  
ANISOU 1309  N   VAL A 196     9127   6587  15053   1445  -2643    -88       N  
ATOM   1310  CA  VAL A 196      88.787 244.059   7.373  1.00 89.37           C  
ANISOU 1310  CA  VAL A 196    10131   7382  16446   1355  -2520    203       C  
ATOM   1311  C   VAL A 196      87.835 245.197   6.998  1.00 98.48           C  
ANISOU 1311  C   VAL A 196    11394   8511  17511   1602  -2547    301       C  
ATOM   1312  O   VAL A 196      86.715 244.972   6.516  1.00 97.95           O  
ANISOU 1312  O   VAL A 196    11380   8699  17137   1809  -2489    367       O  
ATOM   1313  CB  VAL A 196      89.299 243.248   6.164  1.00 88.03           C  
ANISOU 1313  CB  VAL A 196     9858   7247  16345   1211  -2241    499       C  
ATOM   1314  CG1 VAL A 196      88.201 242.593   5.334  1.00 87.90           C  
ANISOU 1314  CG1 VAL A 196     9878   7374  16145   1401  -2069    777       C  
ATOM   1315  CG2 VAL A 196      90.185 244.105   5.292  1.00 90.98           C  
ANISOU 1315  CG2 VAL A 196    10102   7342  17124    979  -2140    663       C  
ATOM   1316  N   PHE A 197      88.260 246.421   7.290  1.00108.27           N  
ANISOU 1316  N   PHE A 197    12654   9465  19017   1597  -2657    286       N  
ATOM   1317  CA  PHE A 197      87.418 247.604   7.184  1.00115.79           C  
ANISOU 1317  CA  PHE A 197    13733  10360  19903   1839  -2719    327       C  
ATOM   1318  C   PHE A 197      87.341 248.149   5.761  1.00123.38           C  
ANISOU 1318  C   PHE A 197    14706  11223  20948   1913  -2473    720       C  
ATOM   1319  O   PHE A 197      86.259 248.578   5.339  1.00124.02           O  
ANISOU 1319  O   PHE A 197    14898  11450  20774   2185  -2449    809       O  
ATOM   1320  CB  PHE A 197      87.933 248.688   8.132  1.00118.57           C  
ANISOU 1320  CB  PHE A 197    14097  10430  20525   1810  -2953    133       C  
ATOM   1321  CG  PHE A 197      87.800 248.343   9.591  1.00119.08           C  
ANISOU 1321  CG  PHE A 197    14198  10624  20424   1837  -3220   -256       C  
ATOM   1322  CD1 PHE A 197      86.589 248.498  10.249  1.00119.59           C  
ANISOU 1322  CD1 PHE A 197    14413  10911  20116   2094  -3345   -439       C  
ATOM   1323  CD2 PHE A 197      88.893 247.885  10.310  1.00119.69           C  
ANISOU 1323  CD2 PHE A 197    14155  10620  20703   1630  -3338   -428       C  
ATOM   1324  CE1 PHE A 197      86.469 248.192  11.600  1.00119.61           C  
ANISOU 1324  CE1 PHE A 197    14469  11043  19937   2144  -3562   -775       C  
ATOM   1325  CE2 PHE A 197      88.781 247.577  11.659  1.00119.67           C  
ANISOU 1325  CE2 PHE A 197    14206  10749  20514   1695  -3578   -771       C  
ATOM   1326  CZ  PHE A 197      87.568 247.731  12.304  1.00119.52           C  
ANISOU 1326  CZ  PHE A 197    14361  10940  20111   1952  -3680   -938       C  
ATOM   1327  N   PRO A 198      88.449 248.188   4.993  1.00126.69           N  
ANISOU 1327  N   PRO A 198    15015  11422  21700   1706  -2279    972       N  
ATOM   1328  CA  PRO A 198      88.258 248.698   3.631  1.00130.23           C  
ANISOU 1328  CA  PRO A 198    15511  11817  22153   1834  -2020   1364       C  
ATOM   1329  C   PRO A 198      87.497 247.724   2.735  1.00128.49           C  
ANISOU 1329  C   PRO A 198    15304  11954  21563   1974  -1857   1529       C  
ATOM   1330  O   PRO A 198      86.701 248.172   1.910  1.00130.18           O  
ANISOU 1330  O   PRO A 198    15613  12277  21574   2241  -1757   1738       O  
ATOM   1331  CB  PRO A 198      89.691 248.889   3.125  1.00132.86           C  
ANISOU 1331  CB  PRO A 198    15698  11859  22924   1568  -1839   1576       C  
ATOM   1332  CG  PRO A 198      90.493 247.910   3.907  1.00130.17           C  
ANISOU 1332  CG  PRO A 198    15207  11570  22681   1309  -1943   1341       C  
ATOM   1333  CD  PRO A 198      89.872 247.920   5.275  1.00127.94           C  
ANISOU 1333  CD  PRO A 198    15000  11383  22227   1396  -2273    936       C  
ATOM   1334  N   LYS A 203      81.710 248.466   0.527  1.00 88.82           N  
ANISOU 1334  N   LYS A 203    10568   8355  14825   3543  -1937   1770       N  
ATOM   1335  CA  LYS A 203      82.515 249.683   0.497  1.00 93.48           C  
ANISOU 1335  CA  LYS A 203    11298   8456  15763   3486  -1851   1935       C  
ATOM   1336  C   LYS A 203      83.038 250.012   1.893  1.00 94.76           C  
ANISOU 1336  C   LYS A 203    11472   8334  16198   3253  -2041   1631       C  
ATOM   1337  O   LYS A 203      84.151 249.630   2.258  1.00 93.01           O  
ANISOU 1337  O   LYS A 203    11170   7878  16290   2925  -2024   1579       O  
ATOM   1338  CB  LYS A 203      81.701 250.857  -0.059  1.00 96.27           C  
ANISOU 1338  CB  LYS A 203    11814   8828  15934   3870  -1825   2102       C  
ATOM   1339  CG  LYS A 203      82.521 252.108  -0.356  1.00 99.81           C  
ANISOU 1339  CG  LYS A 203    12408   8774  16739   3832  -1695   2325       C  
ATOM   1340  CD  LYS A 203      81.621 253.300  -0.642  1.00102.55           C  
ANISOU 1340  CD  LYS A 203    12946   9127  16891   4229  -1719   2417       C  
ATOM   1341  CE  LYS A 203      82.428 254.542  -0.976  1.00 94.17           C  
ANISOU 1341  CE  LYS A 203    12027   7550  16203   4183  -1589   2640       C  
ATOM   1342  NZ  LYS A 203      83.028 254.464  -2.334  1.00 95.95           N  
ANISOU 1342  NZ  LYS A 203    12256   7707  16492   4162  -1304   3025       N  
ATOM   1343  N   THR A 204      82.225 250.727   2.672  1.00 97.27           N  
ANISOU 1343  N   THR A 204    11881   8700  16376   3440  -2225   1428       N  
ATOM   1344  CA  THR A 204      82.560 251.040   4.055  1.00 97.31           C  
ANISOU 1344  CA  THR A 204    11904   8507  16562   3280  -2437   1111       C  
ATOM   1345  C   THR A 204      82.108 249.963   5.032  1.00 94.39           C  
ANISOU 1345  C   THR A 204    11456   8463  15946   3211  -2598    774       C  
ATOM   1346  O   THR A 204      82.521 249.991   6.196  1.00 92.13           O  
ANISOU 1346  O   THR A 204    11179   8042  15785   3065  -2766    507       O  
ATOM   1347  CB  THR A 204      81.941 252.382   4.464  1.00 99.05           C  
ANISOU 1347  CB  THR A 204    12270   8606  16759   3516  -2547   1063       C  
ATOM   1348  OG1 THR A 204      80.518 252.322   4.314  1.00 98.53           O  
ANISOU 1348  OG1 THR A 204    12227   8968  16242   3831  -2577   1034       O  
ATOM   1349  CG2 THR A 204      82.492 253.507   3.600  1.00102.35           C  
ANISOU 1349  CG2 THR A 204    12784   8640  17463   3572  -2380   1384       C  
ATOM   1350  N   THR A 205      81.278 249.021   4.591  1.00 95.20           N  
ANISOU 1350  N   THR A 205    11476   8999  15695   3324  -2552    775       N  
ATOM   1351  CA  THR A 205      80.812 247.943   5.454  1.00 91.58           C  
ANISOU 1351  CA  THR A 205    10938   8864  14993   3262  -2662    471       C  
ATOM   1352  C   THR A 205      81.899 246.879   5.568  1.00 89.17           C  
ANISOU 1352  C   THR A 205    10532   8446  14903   2944  -2608    441       C  
ATOM   1353  O   THR A 205      82.270 246.249   4.572  1.00 88.33           O  
ANISOU 1353  O   THR A 205    10331   8379  14852   2864  -2449    654       O  
ATOM   1354  CB  THR A 205      79.515 247.350   4.906  1.00 90.37           C  
ANISOU 1354  CB  THR A 205    10699   9238  14398   3483  -2635    459       C  
ATOM   1355  OG1 THR A 205      79.676 247.045   3.515  1.00 90.09           O  
ANISOU 1355  OG1 THR A 205    10591   9275  14363   3526  -2479    744       O  
ATOM   1356  CG2 THR A 205      78.370 248.343   5.070  1.00 91.87           C  
ANISOU 1356  CG2 THR A 205    10981   9585  14341   3778  -2711    420       C  
ATOM   1357  N   ALA A 206      82.414 246.689   6.779  1.00 86.19           N  
ANISOU 1357  N   ALA A 206    10176   7939  14632   2782  -2737    183       N  
ATOM   1358  CA  ALA A 206      83.498 245.750   7.005  1.00 83.03           C  
ANISOU 1358  CA  ALA A 206     9689   7420  14438   2488  -2697    135       C  
ATOM   1359  C   ALA A 206      82.969 244.321   7.066  1.00 78.58           C  
ANISOU 1359  C   ALA A 206     9024   7240  13593   2477  -2651     20       C  
ATOM   1360  O   ALA A 206      81.777 244.079   7.275  1.00 78.74           O  
ANISOU 1360  O   ALA A 206     9036   7623  13260   2674  -2690   -106       O  
ATOM   1361  CB  ALA A 206      84.246 246.091   8.295  1.00 84.73           C  
ANISOU 1361  CB  ALA A 206     9960   7391  14842   2356  -2875   -113       C  
ATOM   1362  N   PHE A 207      83.879 243.366   6.874  1.00 74.60           N  
ANISOU 1362  N   PHE A 207     8425   6662  13259   2235  -2555     62       N  
ATOM   1363  CA  PHE A 207      83.525 241.955   6.911  1.00 68.61           C  
ANISOU 1363  CA  PHE A 207     7550   6225  12292   2194  -2496    -44       C  
ATOM   1364  C   PHE A 207      84.708 241.146   7.423  1.00 64.65           C  
ANISOU 1364  C   PHE A 207     7019   5539  12006   1921  -2465   -121       C  
ATOM   1365  O   PHE A 207      85.863 241.569   7.320  1.00 63.93           O  
ANISOU 1365  O   PHE A 207     6941   5111  12240   1739  -2444    -14       O  
ATOM   1366  CB  PHE A 207      83.073 241.444   5.535  1.00 67.67           C  
ANISOU 1366  CB  PHE A 207     7330   6420  11962   2184  -2282    170       C  
ATOM   1367  CG  PHE A 207      84.144 241.492   4.480  1.00 67.52           C  
ANISOU 1367  CG  PHE A 207     7283   6159  12214   2013  -2101    485       C  
ATOM   1368  CD1 PHE A 207      84.815 240.340   4.102  1.00 64.61           C  
ANISOU 1368  CD1 PHE A 207     6840   5893  11817   1745  -1905    530       C  
ATOM   1369  CD2 PHE A 207      84.469 242.686   3.856  1.00 69.11           C  
ANISOU 1369  CD2 PHE A 207     7535   6025  12698   2137  -2105    752       C  
ATOM   1370  CE1 PHE A 207      85.795 240.380   3.127  1.00 65.17           C  
ANISOU 1370  CE1 PHE A 207     6884   5757  12121   1615  -1719    836       C  
ATOM   1371  CE2 PHE A 207      85.449 242.732   2.882  1.00 69.49           C  
ANISOU 1371  CE2 PHE A 207     7550   5850  13004   2001  -1897   1076       C  
ATOM   1372  CZ  PHE A 207      86.113 241.577   2.517  1.00 67.95           C  
ANISOU 1372  CZ  PHE A 207     7277   5781  12761   1746  -1704   1119       C  
ATOM   1373  N   THR A 208      84.401 239.974   7.968  1.00 61.75           N  
ANISOU 1373  N   THR A 208     6596   5421  11446   1900  -2450   -309       N  
ATOM   1374  CA  THR A 208      85.366 239.147   8.678  1.00 53.48           C  
ANISOU 1374  CA  THR A 208     5549   4250  10519   1697  -2434   -434       C  
ATOM   1375  C   THR A 208      85.924 238.072   7.753  1.00 51.85           C  
ANISOU 1375  C   THR A 208     5239   4153  10308   1435  -2178   -269       C  
ATOM   1376  O   THR A 208      85.185 237.468   6.971  1.00 62.33           O  
ANISOU 1376  O   THR A 208     6512   5869  11300   1387  -1981   -203       O  
ATOM   1377  CB  THR A 208      84.707 238.500   9.900  1.00 57.01           C  
ANISOU 1377  CB  THR A 208     6047   4943  10671   1810  -2492   -724       C  
ATOM   1378  OG1 THR A 208      84.040 239.506  10.671  1.00 58.65           O  
ANISOU 1378  OG1 THR A 208     6388   5173  10722   2013  -2643   -850       O  
ATOM   1379  CG2 THR A 208      85.740 237.827  10.769  1.00 57.33           C  
ANISOU 1379  CG2 THR A 208     6133   4842  10807   1648  -2499   -859       C  
ATOM   1380  N   VAL A 209      87.232 237.829   7.854  1.00 51.57           N  
ANISOU 1380  N   VAL A 209     5181   3803  10608   1251  -2172   -222       N  
ATOM   1381  CA  VAL A 209      87.917 236.870   6.996  1.00 50.25           C  
ANISOU 1381  CA  VAL A 209     4942   3722  10430    987  -1912    -53       C  
ATOM   1382  C   VAL A 209      88.925 236.076   7.812  1.00 57.47           C  
ANISOU 1382  C   VAL A 209     5855   4480  11502    838  -1937   -197       C  
ATOM   1383  O   VAL A 209      89.477 236.562   8.802  1.00 59.67           O  
ANISOU 1383  O   VAL A 209     6182   4538  11953    871  -2136   -356       O  
ATOM   1384  CB  VAL A 209      88.623 237.564   5.811  1.00 62.40           C  
ANISOU 1384  CB  VAL A 209     6431   5011  12267    922  -1806    288       C  
ATOM   1385  CG1 VAL A 209      87.628 237.878   4.711  1.00 62.49           C  
ANISOU 1385  CG1 VAL A 209     6446   5318  11978   1047  -1675    463       C  
ATOM   1386  CG2 VAL A 209      89.315 238.829   6.289  1.00 54.38           C  
ANISOU 1386  CG2 VAL A 209     5445   3591  11624    944  -1987    291       C  
ATOM   1387  N   CYS A 210      89.176 234.848   7.370  1.00 55.95           N  
ANISOU 1387  N   CYS A 210     5624   4508  11127    635  -1700   -153       N  
ATOM   1388  CA  CYS A 210      90.096 233.925   8.022  1.00 54.14           C  
ANISOU 1388  CA  CYS A 210     5399   4187  10983    493  -1675   -270       C  
ATOM   1389  C   CYS A 210      91.230 233.603   7.058  1.00 53.29           C  
ANISOU 1389  C   CYS A 210     5213   3937  11096    270  -1494    -23       C  
ATOM   1390  O   CYS A 210      90.981 233.196   5.918  1.00 53.34           O  
ANISOU 1390  O   CYS A 210     5187   4172  10910    180  -1266    166       O  
ATOM   1391  CB  CYS A 210      89.360 232.653   8.450  1.00 51.41           C  
ANISOU 1391  CB  CYS A 210     5090   4227  10215    462  -1530   -446       C  
ATOM   1392  SG  CYS A 210      90.371 231.312   9.132  1.00 49.06           S  
ANISOU 1392  SG  CYS A 210     4825   3887   9929    302  -1430   -564       S  
ATOM   1393  N   ASP A 211      92.468 233.802   7.506  1.00 52.88           N  
ANISOU 1393  N   ASP A 211     5124   3594  11377    193  -1587    -34       N  
ATOM   1394  CA  ASP A 211      93.622 233.638   6.632  1.00 55.24           C  
ANISOU 1394  CA  ASP A 211     5320   3846  11825      6  -1396    212       C  
ATOM   1395  C   ASP A 211      94.866 233.417   7.482  1.00 53.11           C  
ANISOU 1395  C   ASP A 211     4993   3580  11606    -47  -1468     82       C  
ATOM   1396  O   ASP A 211      94.844 233.566   8.706  1.00 51.03           O  
ANISOU 1396  O   ASP A 211     4772   3322  11296     55  -1683   -171       O  
ATOM   1397  CB  ASP A 211      93.795 234.853   5.714  1.00 62.96           C  
ANISOU 1397  CB  ASP A 211     6229   4668  13026     28  -1362    482       C  
ATOM   1398  CG  ASP A 211      94.747 234.585   4.569  1.00 68.37           C  
ANISOU 1398  CG  ASP A 211     6820   5351  13808   -112  -1096    783       C  
ATOM   1399  OD1 ASP A 211      94.836 233.417   4.136  1.00 68.81           O  
ANISOU 1399  OD1 ASP A 211     6896   5554  13695   -212   -910    832       O  
ATOM   1400  OD2 ASP A 211      95.417 235.537   4.116  1.00 72.57           O  
ANISOU 1400  OD2 ASP A 211     7260   5741  14572   -116  -1063    962       O  
ATOM   1401  N   GLU A 212      95.955 233.047   6.809  1.00 53.42           N  
ANISOU 1401  N   GLU A 212     4942   3629  11725   -169  -1285    264       N  
ATOM   1402  CA  GLU A 212      97.248 232.922   7.465  1.00 53.84           C  
ANISOU 1402  CA  GLU A 212     4914   3663  11881   -182  -1352    178       C  
ATOM   1403  C   GLU A 212      97.804 234.304   7.783  1.00 55.69           C  
ANISOU 1403  C   GLU A 212     5016   3695  12447   -134  -1554    169       C  
ATOM   1404  O   GLU A 212      97.754 235.210   6.946  1.00 57.85           O  
ANISOU 1404  O   GLU A 212     5223   3842  12917   -156  -1493    376       O  
ATOM   1405  CB  GLU A 212      98.228 232.158   6.573  1.00 54.95           C  
ANISOU 1405  CB  GLU A 212     5004   3872  12004   -293  -1091    378       C  
ATOM   1406  CG  GLU A 212      97.840 230.719   6.269  1.00 54.41           C  
ANISOU 1406  CG  GLU A 212     5065   4009  11599   -366   -885    370       C  
ATOM   1407  CD  GLU A 212      98.895 230.002   5.448  1.00 56.18           C  
ANISOU 1407  CD  GLU A 212     5262   4308  11775   -452   -653    545       C  
ATOM   1408  OE1 GLU A 212     100.089 230.339   5.597  1.00 58.46           O  
ANISOU 1408  OE1 GLU A 212     5438   4503  12271   -435   -694    576       O  
ATOM   1409  OE2 GLU A 212      98.535 229.110   4.650  1.00 55.71           O  
ANISOU 1409  OE2 GLU A 212     5284   4403  11480   -532   -440    641       O  
ATOM   1410  N   ARG A 213      98.336 234.468   8.993  1.00 57.10           N  
ANISOU 1410  N   ARG A 213     6026   4067  11601   1101    296  -1059       N  
ATOM   1411  CA  ARG A 213      98.952 235.724   9.413  1.00 62.14           C  
ANISOU 1411  CA  ARG A 213     6715   4599  12298   1093    255  -1240       C  
ATOM   1412  C   ARG A 213     100.321 235.420  10.004  1.00 62.35           C  
ANISOU 1412  C   ARG A 213     6700   4730  12261   1095    255  -1483       C  
ATOM   1413  O   ARG A 213     100.422 234.901  11.120  1.00 62.89           O  
ANISOU 1413  O   ARG A 213     6773   4974  12148   1285    275  -1570       O  
ATOM   1414  CB  ARG A 213      98.073 236.465  10.418  1.00 69.10           C  
ANISOU 1414  CB  ARG A 213     7641   5482  13131   1281    257  -1252       C  
ATOM   1415  CG  ARG A 213      96.723 236.879   9.860  1.00 75.91           C  
ANISOU 1415  CG  ARG A 213     8527   6246  14070   1290    234  -1063       C  
ATOM   1416  CD  ARG A 213      96.878 237.760   8.633  1.00 80.45           C  
ANISOU 1416  CD  ARG A 213     9180   6606  14781   1117    155  -1011       C  
ATOM   1417  NE  ARG A 213      95.608 237.962   7.944  1.00 83.24           N  
ANISOU 1417  NE  ARG A 213     9564   6890  15174   1146     97   -837       N  
ATOM   1418  CZ  ARG A 213      95.473 238.652   6.818  1.00 85.26           C  
ANISOU 1418  CZ  ARG A 213     9946   6967  15482   1047     16   -750       C  
ATOM   1419  NH1 ARG A 213      96.532 239.211   6.249  1.00 86.35           N  
ANISOU 1419  NH1 ARG A 213    10202   6967  15641    883     24   -800       N  
ATOM   1420  NH2 ARG A 213      94.278 238.784   6.260  1.00 85.61           N  
ANISOU 1420  NH2 ARG A 213    10014   6970  15543   1119    -65   -625       N  
ATOM   1421  N   TRP A 214     101.371 235.747   9.261  1.00 62.92           N  
ANISOU 1421  N   TRP A 214     6751   4699  12456    888    238  -1598       N  
ATOM   1422  CA  TRP A 214     102.736 235.487   9.681  1.00 64.47           C  
ANISOU 1422  CA  TRP A 214     6870   5001  12626    860    221  -1873       C  
ATOM   1423  C   TRP A 214     103.419 236.777  10.105  1.00 69.34           C  
ANISOU 1423  C   TRP A 214     7479   5519  13347    811    183  -2117       C  
ATOM   1424  O   TRP A 214     103.102 237.862   9.608  1.00 74.53           O  
ANISOU 1424  O   TRP A 214     8210   5972  14136    696    198  -2051       O  
ATOM   1425  CB  TRP A 214     103.550 234.847   8.554  1.00 64.94           C  
ANISOU 1425  CB  TRP A 214     6880   5040  12756    633    254  -1870       C  
ATOM   1426  CG  TRP A 214     103.015 233.551   8.052  1.00 62.85           C  
ANISOU 1426  CG  TRP A 214     6608   4867  12407    661    280  -1652       C  
ATOM   1427  CD1 TRP A 214     102.005 233.373   7.153  1.00 61.43           C  
ANISOU 1427  CD1 TRP A 214     6484   4598  12259    607    292  -1365       C  
ATOM   1428  CD2 TRP A 214     103.484 232.244   8.394  1.00 49.89           C  
ANISOU 1428  CD2 TRP A 214     4902   3434  10619    752    283  -1712       C  
ATOM   1429  NE1 TRP A 214     101.808 232.034   6.923  1.00 59.08           N  
ANISOU 1429  NE1 TRP A 214     6139   4433  11875    644    311  -1248       N  
ATOM   1430  CE2 TRP A 214     102.705 231.320   7.673  1.00 48.35           C  
ANISOU 1430  CE2 TRP A 214     4718   3251  10402    732    317  -1446       C  
ATOM   1431  CE3 TRP A 214     104.485 231.765   9.245  1.00 55.02           C  
ANISOU 1431  CE3 TRP A 214     5499   4278  11129    862    242  -1968       C  
ATOM   1432  CZ2 TRP A 214     102.893 229.945   7.776  1.00 47.01           C  
ANISOU 1432  CZ2 TRP A 214     4511   3259  10092    804    339  -1417       C  
ATOM   1433  CZ3 TRP A 214     104.671 230.401   9.347  1.00 53.26           C  
ANISOU 1433  CZ3 TRP A 214     5264   4242  10730    951    250  -1932       C  
ATOM   1434  CH2 TRP A 214     103.879 229.506   8.616  1.00 47.25           C  
ANISOU 1434  CH2 TRP A 214     4518   3469   9968    915    311  -1654       C  
ATOM   1435  N   GLY A 215     104.373 236.643  11.020  1.00 68.59           N  
ANISOU 1435  N   GLY A 215     7307   5582  13173    905    124  -2403       N  
ATOM   1436  CA  GLY A 215     105.271 237.735  11.330  1.00 73.82           C  
ANISOU 1436  CA  GLY A 215     7908   6177  13963    819     80  -2686       C  
ATOM   1437  C   GLY A 215     106.474 237.708  10.410  1.00 79.07           C  
ANISOU 1437  C   GLY A 215     8465   6799  14781    529    132  -2832       C  
ATOM   1438  O   GLY A 215     107.306 236.798  10.491  1.00 77.61           O  
ANISOU 1438  O   GLY A 215     8171   6795  14524    533    100  -2982       O  
ATOM   1439  N   GLY A 216     106.571 238.691   9.519  1.00 85.65           N  
ANISOU 1439  N   GLY A 216     9348   7405  15788    280    225  -2770       N  
ATOM   1440  CA  GLY A 216     107.653 238.723   8.553  1.00 92.69           C  
ANISOU 1440  CA  GLY A 216    10174   8259  16783    -19    334  -2850       C  
ATOM   1441  C   GLY A 216     107.405 237.811   7.370  1.00 94.95           C  
ANISOU 1441  C   GLY A 216    10538   8537  17002   -150    414  -2581       C  
ATOM   1442  O   GLY A 216     107.026 236.650   7.546  1.00 96.33           O  
ANISOU 1442  O   GLY A 216    10688   8850  17062     -3    355  -2501       O  
ATOM   1443  N   GLU A 217     107.613 238.328   6.154  1.00 92.03           N  
ANISOU 1443  N   GLU A 217    10287   8011  16669   -412    553  -2427       N  
ATOM   1444  CA  GLU A 217     107.373 237.581   4.924  1.00 89.69           C  
ANISOU 1444  CA  GLU A 217    10106   7703  16270   -535    621  -2151       C  
ATOM   1445  C   GLU A 217     108.491 236.607   4.593  1.00 85.35           C  
ANISOU 1445  C   GLU A 217     9406   7335  15688   -656    668  -2291       C  
ATOM   1446  O   GLU A 217     108.612 236.192   3.434  1.00 83.48           O  
ANISOU 1446  O   GLU A 217     9271   7082  15364   -816    759  -2100       O  
ATOM   1447  CB  GLU A 217     107.155 238.547   3.756  1.00 93.82           C  
ANISOU 1447  CB  GLU A 217    10879   7996  16772   -723    744  -1926       C  
ATOM   1448  CG  GLU A 217     105.916 239.423   3.890  1.00 97.77           C  
ANISOU 1448  CG  GLU A 217    11561   8314  17271   -589    677  -1747       C  
ATOM   1449  CD  GLU A 217     105.870 240.537   2.861  1.00102.46           C  
ANISOU 1449  CD  GLU A 217    12436   8661  17834   -755    792  -1589       C  
ATOM   1450  OE1 GLU A 217     105.505 240.267   1.697  1.00103.14           O  
ANISOU 1450  OE1 GLU A 217    12729   8675  17784   -818    821  -1335       O  
ATOM   1451  OE2 GLU A 217     106.209 241.685   3.219  1.00105.53           O  
ANISOU 1451  OE2 GLU A 217    12854   8919  18324   -811    848  -1728       O  
ATOM   1452  N   ILE A 218     109.300 236.232   5.578  1.00 83.89           N  
ANISOU 1452  N   ILE A 218     8997   7333  15545   -560    591  -2626       N  
ATOM   1453  CA  ILE A 218     110.353 235.250   5.383  1.00 81.44           C  
ANISOU 1453  CA  ILE A 218     8525   7225  15195   -631    603  -2793       C  
ATOM   1454  C   ILE A 218     109.917 233.866   5.847  1.00 75.85           C  
ANISOU 1454  C   ILE A 218     7778   6680  14360   -415    470  -2766       C  
ATOM   1455  O   ILE A 218     110.232 232.868   5.201  1.00 74.27           O  
ANISOU 1455  O   ILE A 218     7556   6583  14082   -493    495  -2702       O  
ATOM   1456  CB  ILE A 218     111.648 235.709   6.093  1.00 85.24           C  
ANISOU 1456  CB  ILE A 218     8776   7824  15789   -648    589  -3207       C  
ATOM   1457  CG1 ILE A 218     112.829 234.812   5.714  1.00 84.41           C  
ANISOU 1457  CG1 ILE A 218     8498   7924  15649   -741    623  -3378       C  
ATOM   1458  CG2 ILE A 218     111.463 235.790   7.600  1.00 85.92           C  
ANISOU 1458  CG2 ILE A 218     8767   8013  15866   -353    389  -3442       C  
ATOM   1459  CD1 ILE A 218     113.522 235.227   4.434  1.00 84.88           C  
ANISOU 1459  CD1 ILE A 218     8611   7891  15748  -1042    861  -3285       C  
ATOM   1460  N   ALA A 219     109.176 233.788   6.953  1.00 72.13           N  
ANISOU 1460  N   ALA A 219     7324   6240  13839   -127    346  -2793       N  
ATOM   1461  CA  ALA A 219     108.754 232.483   7.453  1.00 68.01           C  
ANISOU 1461  CA  ALA A 219     6807   5887  13148    119    260  -2740       C  
ATOM   1462  C   ALA A 219     107.729 231.784   6.555  1.00 63.71           C  
ANISOU 1462  C   ALA A 219     6385   5254  12568     84    316  -2364       C  
ATOM   1463  O   ALA A 219     107.872 230.564   6.351  1.00 63.01           O  
ANISOU 1463  O   ALA A 219     6268   5353  12322    120    298  -2292       O  
ATOM   1464  CB  ALA A 219     108.247 232.608   8.893  1.00 69.87           C  
ANISOU 1464  CB  ALA A 219     7072   6233  13244    453    151  -2809       C  
ATOM   1465  N   PRO A 220     106.716 232.451   5.975  1.00 61.71           N  
ANISOU 1465  N   PRO A 220     6266   4800  12381     19    362  -2083       N  
ATOM   1466  CA  PRO A 220     105.735 231.685   5.182  1.00 58.57           C  
ANISOU 1466  CA  PRO A 220     5955   4398  11902     22    370  -1732       C  
ATOM   1467  C   PRO A 220     106.327 231.022   3.954  1.00 58.05           C  
ANISOU 1467  C   PRO A 220     5897   4371  11789   -210    417  -1641       C  
ATOM   1468  O   PRO A 220     105.898 229.921   3.587  1.00 57.18           O  
ANISOU 1468  O   PRO A 220     5788   4383  11554   -159    389  -1456       O  
ATOM   1469  CB  PRO A 220     104.686 232.742   4.803  1.00 57.64           C  
ANISOU 1469  CB  PRO A 220     5975   4059  11865      7    378  -1520       C  
ATOM   1470  CG  PRO A 220     105.394 234.032   4.864  1.00 60.17           C  
ANISOU 1470  CG  PRO A 220     6319   4275  12269   -130    422  -1693       C  
ATOM   1471  CD  PRO A 220     106.342 233.877   6.026  1.00 62.19           C  
ANISOU 1471  CD  PRO A 220     6409   4682  12536    -28    384  -2052       C  
ATOM   1472  N   LYS A 221     107.287 231.673   3.294  1.00 59.65           N  
ANISOU 1472  N   LYS A 221     6110   4498  12057   -458    502  -1751       N  
ATOM   1473  CA  LYS A 221     107.917 231.075   2.124  1.00 58.98           C  
ANISOU 1473  CA  LYS A 221     6049   4481  11881   -663    572  -1662       C  
ATOM   1474  C   LYS A 221     108.733 229.843   2.496  1.00 59.65           C  
ANISOU 1474  C   LYS A 221     5959   4784  11920   -629    527  -1868       C  
ATOM   1475  O   LYS A 221     108.805 228.890   1.713  1.00 59.23           O  
ANISOU 1475  O   LYS A 221     5922   4824  11758   -697    532  -1727       O  
ATOM   1476  CB  LYS A 221     108.787 232.114   1.418  1.00 61.43           C  
ANISOU 1476  CB  LYS A 221     6431   4710  12200   -893    716  -1718       C  
ATOM   1477  CG  LYS A 221     108.019 233.354   0.986  1.00 64.22           C  
ANISOU 1477  CG  LYS A 221     7005   4824  12571   -922    757  -1522       C  
ATOM   1478  CD  LYS A 221     108.838 234.214   0.038  1.00 65.37           C  
ANISOU 1478  CD  LYS A 221     7290   4856  12690  -1160    935  -1520       C  
ATOM   1479  CE  LYS A 221     108.013 235.375  -0.496  1.00 64.73           C  
ANISOU 1479  CE  LYS A 221     7489   4515  12591  -1170    964  -1306       C  
ATOM   1480  NZ  LYS A 221     108.691 236.092  -1.611  1.00 59.25           N  
ANISOU 1480  NZ  LYS A 221     7007   3670  11835  -1392   1154  -1245       N  
ATOM   1481  N   MET A 222     109.350 229.841   3.680  1.00 61.24           N  
ANISOU 1481  N   MET A 222     6013   5117  12138   -484    463  -2190       N  
ATOM   1482  CA  MET A 222     110.037 228.640   4.145  1.00 58.46           C  
ANISOU 1482  CA  MET A 222     5533   5043  11636   -361    383  -2361       C  
ATOM   1483  C   MET A 222     109.042 227.528   4.451  1.00 57.01           C  
ANISOU 1483  C   MET A 222     5420   4990  11251   -125    315  -2110       C  
ATOM   1484  O   MET A 222     109.287 226.360   4.130  1.00 55.35           O  
ANISOU 1484  O   MET A 222     5186   4945  10899   -114    292  -2057       O  
ATOM   1485  CB  MET A 222     110.872 228.950   5.386  1.00 59.33           C  
ANISOU 1485  CB  MET A 222     5501   5253  11789   -203    296  -2784       C  
ATOM   1486  CG  MET A 222     111.744 230.182   5.273  1.00 64.49           C  
ANISOU 1486  CG  MET A 222     6059   5819  12627   -401    369  -3010       C  
ATOM   1487  SD  MET A 222     113.249 229.934   4.319  1.00 70.40           S  
ANISOU 1487  SD  MET A 222     6661   6714  13373   -661    485  -3151       S  
ATOM   1488  CE  MET A 222     113.953 231.580   4.387  1.00 73.76           C  
ANISOU 1488  CE  MET A 222     7018   7019  13989   -808    614  -3328       C  
ATOM   1489  N   TYR A 223     107.910 227.877   5.066  1.00 57.01           N  
ANISOU 1489  N   TYR A 223     5502   4905  11253     59    300  -1961       N  
ATOM   1490  CA  TYR A 223     106.962 226.863   5.519  1.00 55.88           C  
ANISOU 1490  CA  TYR A 223     5408   4864  10958    289    280  -1763       C  
ATOM   1491  C   TYR A 223     106.244 226.211   4.345  1.00 54.46           C  
ANISOU 1491  C   TYR A 223     5279   4646  10766    164    307  -1438       C  
ATOM   1492  O   TYR A 223     106.127 224.981   4.281  1.00 54.38           O  
ANISOU 1492  O   TYR A 223     5259   4779  10623    236    298  -1347       O  
ATOM   1493  CB  TYR A 223     105.960 227.489   6.488  1.00 58.28           C  
ANISOU 1493  CB  TYR A 223     5771   5072  11302    507    288  -1717       C  
ATOM   1494  CG  TYR A 223     104.880 226.546   6.972  1.00 59.74           C  
ANISOU 1494  CG  TYR A 223     6007   5316  11376    728    327  -1511       C  
ATOM   1495  CD1 TYR A 223     105.118 225.669   8.023  1.00 59.85           C  
ANISOU 1495  CD1 TYR A 223     6054   5506  11181    976    328  -1616       C  
ATOM   1496  CD2 TYR A 223     103.618 226.542   6.387  1.00 59.07           C  
ANISOU 1496  CD2 TYR A 223     5951   5105  11389    691    369  -1223       C  
ATOM   1497  CE1 TYR A 223     104.134 224.811   8.473  1.00 59.08           C  
ANISOU 1497  CE1 TYR A 223     6051   5479  10919   1123    408  -1392       C  
ATOM   1498  CE2 TYR A 223     102.628 225.686   6.831  1.00 57.82           C  
ANISOU 1498  CE2 TYR A 223     5814   5000  11153    856    435  -1054       C  
ATOM   1499  CZ  TYR A 223     102.892 224.823   7.875  1.00 58.12           C  
ANISOU 1499  CZ  TYR A 223     5917   5232  10933   1046    473  -1124       C  
ATOM   1500  OH  TYR A 223     101.917 223.966   8.329  1.00 57.23           O  
ANISOU 1500  OH  TYR A 223     5876   5181  10687   1163    578   -939       O  
ATOM   1501  N   HIS A 224     105.752 227.020   3.403  1.00 54.04           N  
ANISOU 1501  N   HIS A 224     5298   4391  10845     -7    332  -1271       N  
ATOM   1502  CA  HIS A 224     104.986 226.478   2.286  1.00 53.69           C  
ANISOU 1502  CA  HIS A 224     5315   4294  10789    -83    320   -985       C  
ATOM   1503  C   HIS A 224     105.856 225.713   1.296  1.00 54.24           C  
ANISOU 1503  C   HIS A 224     5375   4464  10771   -263    326   -982       C  
ATOM   1504  O   HIS A 224     105.321 224.976   0.460  1.00 55.21           O  
ANISOU 1504  O   HIS A 224     5535   4595  10848   -289    294   -774       O  
ATOM   1505  CB  HIS A 224     104.227 227.601   1.580  1.00 54.02           C  
ANISOU 1505  CB  HIS A 224     5478   4081  10968   -164    318   -828       C  
ATOM   1506  CG  HIS A 224     102.975 228.019   2.293  1.00 54.87           C  
ANISOU 1506  CG  HIS A 224     5588   4099  11161     36    291   -745       C  
ATOM   1507  ND1 HIS A 224     101.797 227.309   2.201  1.00 54.00           N  
ANISOU 1507  ND1 HIS A 224     5449   4001  11067    163    256   -559       N  
ATOM   1508  CD2 HIS A 224     102.719 229.070   3.109  1.00 55.99           C  
ANISOU 1508  CD2 HIS A 224     5744   4135  11396    129    303   -842       C  
ATOM   1509  CE1 HIS A 224     100.870 227.908   2.927  1.00 54.85           C  
ANISOU 1509  CE1 HIS A 224     5546   4019  11275    320    261   -545       C  
ATOM   1510  NE2 HIS A 224     101.403 228.978   3.488  1.00 56.26           N  
ANISOU 1510  NE2 HIS A 224     5762   4125  11488    311    283   -706       N  
ATOM   1511  N   ILE A 225     107.178 225.876   1.363  1.00 53.62           N  
ANISOU 1511  N   ILE A 225     5233   4458  10682   -383    363  -1229       N  
ATOM   1512  CA  ILE A 225     108.070 224.949   0.674  1.00 52.30           C  
ANISOU 1512  CA  ILE A 225     5020   4439  10414   -508    371  -1273       C  
ATOM   1513  C   ILE A 225     108.090 223.612   1.402  1.00 51.08           C  
ANISOU 1513  C   ILE A 225     4788   4520  10100   -304    303  -1314       C  
ATOM   1514  O   ILE A 225     108.002 222.545   0.784  1.00 52.32           O  
ANISOU 1514  O   ILE A 225     4953   4772  10155   -323    279  -1180       O  
ATOM   1515  CB  ILE A 225     109.485 225.543   0.551  1.00 53.05           C  
ANISOU 1515  CB  ILE A 225     5038   4533  10587   -700    448  -1565       C  
ATOM   1516  CG1 ILE A 225     109.487 226.711  -0.435  1.00 55.10           C  
ANISOU 1516  CG1 ILE A 225     5435   4546  10955   -925    568  -1462       C  
ATOM   1517  CG2 ILE A 225     110.484 224.465   0.126  1.00 51.10           C  
ANISOU 1517  CG2 ILE A 225     4697   4488  10229   -776    444  -1678       C  
ATOM   1518  CD1 ILE A 225     110.809 227.438  -0.519  1.00 58.29           C  
ANISOU 1518  CD1 ILE A 225     5784   4991  11372  -1075    688  -1707       C  
ATOM   1519  N   CYS A 226     108.190 223.653   2.735  1.00 49.76           N  
ANISOU 1519  N   CYS A 226     4574   4435   9898    -89    273  -1499       N  
ATOM   1520  CA  CYS A 226     108.192 222.419   3.513  1.00 49.44           C  
ANISOU 1520  CA  CYS A 226     4521   4587   9676    141    230  -1534       C  
ATOM   1521  C   CYS A 226     106.824 221.747   3.496  1.00 47.29           C  
ANISOU 1521  C   CYS A 226     4320   4269   9378    258    259  -1231       C  
ATOM   1522  O   CYS A 226     106.730 220.528   3.680  1.00 46.78           O  
ANISOU 1522  O   CYS A 226     4271   4329   9176    374    258  -1174       O  
ATOM   1523  CB  CYS A 226     108.633 222.702   4.953  1.00 51.57           C  
ANISOU 1523  CB  CYS A 226     4774   4933   9889    381    189  -1816       C  
ATOM   1524  SG  CYS A 226     110.363 223.204   5.135  1.00 52.39           S  
ANISOU 1524  SG  CYS A 226     4732   5135  10039    294    121  -2271       S  
ATOM   1525  N   PHE A 227     105.770 222.506   3.220  1.00 46.55           N  
ANISOU 1525  N   PHE A 227     4265   3990   9431    234    288  -1054       N  
ATOM   1526  CA  PHE A 227     104.414 221.905   3.136  1.00 44.06           C  
ANISOU 1526  CA  PHE A 227     3971   3616   9154    316    316   -799       C  
ATOM   1527  C   PHE A 227     104.303 221.180   1.796  1.00 43.97           C  
ANISOU 1527  C   PHE A 227     3953   3614   9139    157    273   -629       C  
ATOM   1528  O   PHE A 227     103.820 220.056   1.749  1.00 45.44           O  
ANISOU 1528  O   PHE A 227     4121   3869   9276    228    284   -520       O  
ATOM   1529  CB  PHE A 227     103.327 222.973   3.276  1.00 42.52           C  
ANISOU 1529  CB  PHE A 227     3798   3223   9135    346    333   -698       C  
ATOM   1530  CG  PHE A 227     101.917 222.449   3.359  1.00 39.98           C  
ANISOU 1530  CG  PHE A 227     3452   2837   8900    463    376   -501       C  
ATOM   1531  CD1 PHE A 227     101.308 222.248   4.577  1.00 40.64           C  
ANISOU 1531  CD1 PHE A 227     3538   2932   8974    685    483   -520       C  
ATOM   1532  CD2 PHE A 227     101.196 222.162   2.220  1.00 39.69           C  
ANISOU 1532  CD2 PHE A 227     3395   2720   8967    361    316   -317       C  
ATOM   1533  CE1 PHE A 227     100.022 221.752   4.649  1.00 41.57           C  
ANISOU 1533  CE1 PHE A 227     3643   3050   9104    718    548   -348       C  
ATOM   1534  CE2 PHE A 227      99.914 221.658   2.298  1.00 40.24           C  
ANISOU 1534  CE2 PHE A 227     3397   2723   9169    462    352   -183       C  
ATOM   1535  CZ  PHE A 227      99.325 221.463   3.512  1.00 40.33           C  
ANISOU 1535  CZ  PHE A 227     3415   2820   9090    599    480   -198       C  
ATOM   1536  N   PHE A 228     104.753 221.824   0.731  1.00 41.68           N  
ANISOU 1536  N   PHE A 228     3697   3243   8896    -52    236   -611       N  
ATOM   1537  CA  PHE A 228     104.700 221.197  -0.586  1.00 36.82           C  
ANISOU 1537  CA  PHE A 228     3111   2628   8253   -186    186   -459       C  
ATOM   1538  C   PHE A 228     105.550 219.931  -0.636  1.00 46.07           C  
ANISOU 1538  C   PHE A 228     4233   4009   9263   -193    178   -534       C  
ATOM   1539  O   PHE A 228     105.196 218.965  -1.321  1.00 34.89           O  
ANISOU 1539  O   PHE A 228     2815   2633   7810   -205    134   -396       O  
ATOM   1540  CB  PHE A 228     105.151 222.205  -1.642  1.00 37.83           C  
ANISOU 1540  CB  PHE A 228     3338   2612   8422   -390    189   -444       C  
ATOM   1541  CG  PHE A 228     105.146 221.671  -3.043  1.00 45.56           C  
ANISOU 1541  CG  PHE A 228     4395   3573   9342   -507    139   -292       C  
ATOM   1542  CD1 PHE A 228     103.961 221.553  -3.752  1.00 44.53           C  
ANISOU 1542  CD1 PHE A 228     4325   3323   9271   -447     43    -86       C  
ATOM   1543  CD2 PHE A 228     106.330 221.313  -3.661  1.00 44.89           C  
ANISOU 1543  CD2 PHE A 228     4321   3586   9149   -662    180   -379       C  
ATOM   1544  CE1 PHE A 228     103.956 221.072  -5.046  1.00 43.43           C  
ANISOU 1544  CE1 PHE A 228     4278   3164   9059   -521    -28     37       C  
ATOM   1545  CE2 PHE A 228     106.332 220.831  -4.953  1.00 44.45           C  
ANISOU 1545  CE2 PHE A 228     4362   3511   9018   -752    140   -239       C  
ATOM   1546  CZ  PHE A 228     105.142 220.711  -5.647  1.00 43.48           C  
ANISOU 1546  CZ  PHE A 228     4323   3268   8931   -672     27    -27       C  
ATOM   1547  N   LEU A 229     106.669 219.914   0.093  1.00 45.67           N  
ANISOU 1547  N   LEU A 229     4137   4094   9123   -168    202   -775       N  
ATOM   1548  CA  LEU A 229     107.565 218.760   0.062  1.00 42.77           C  
ANISOU 1548  CA  LEU A 229     3727   3929   8595   -156    175   -881       C  
ATOM   1549  C   LEU A 229     106.986 217.585   0.839  1.00 41.14           C  
ANISOU 1549  C   LEU A 229     3531   3813   8288     66    179   -815       C  
ATOM   1550  O   LEU A 229     106.854 216.478   0.305  1.00 40.65           O  
ANISOU 1550  O   LEU A 229     3471   3818   8156     56    155   -704       O  
ATOM   1551  CB  LEU A 229     108.936 219.147   0.616  1.00 42.41           C  
ANISOU 1551  CB  LEU A 229     3614   3993   8506   -172    175  -1205       C  
ATOM   1552  CG  LEU A 229     109.789 220.072  -0.253  1.00 43.34           C  
ANISOU 1552  CG  LEU A 229     3705   4034   8726   -434    221  -1311       C  
ATOM   1553  CD1 LEU A 229     110.893 220.709   0.569  1.00 38.76           C  
ANISOU 1553  CD1 LEU A 229     3019   3515   8192   -421    228  -1672       C  
ATOM   1554  CD2 LEU A 229     110.369 219.300  -1.423  1.00 43.90           C  
ANISOU 1554  CD2 LEU A 229     3774   4187   8719   -595    222  -1261       C  
ATOM   1555  N   VAL A 230     106.630 217.808   2.105  1.00 42.29           N  
ANISOU 1555  N   VAL A 230     3700   3944   8422    272    226   -880       N  
ATOM   1556  CA  VAL A 230     106.192 216.712   2.962  1.00 44.76           C  
ANISOU 1556  CA  VAL A 230     4070   4321   8615    499    281   -835       C  
ATOM   1557  C   VAL A 230     104.851 216.146   2.504  1.00 44.06           C  
ANISOU 1557  C   VAL A 230     3976   4118   8646    485    340   -564       C  
ATOM   1558  O   VAL A 230     104.613 214.937   2.607  1.00 43.80           O  
ANISOU 1558  O   VAL A 230     3971   4135   8535    568    385   -488       O  
ATOM   1559  CB  VAL A 230     106.140 217.188   4.428  1.00 48.15           C  
ANISOU 1559  CB  VAL A 230     4566   4742   8988    742    336   -974       C  
ATOM   1560  CG1 VAL A 230     105.514 216.132   5.326  1.00 49.67           C  
ANISOU 1560  CG1 VAL A 230     4873   4944   9056    988    453   -885       C  
ATOM   1561  CG2 VAL A 230     107.536 217.538   4.917  1.00 48.58           C  
ANISOU 1561  CG2 VAL A 230     4604   4931   8924    792    242  -1297       C  
ATOM   1562  N   THR A 231     103.963 216.989   1.982  1.00 43.78           N  
ANISOU 1562  N   THR A 231     3901   3920   8813    389    334   -435       N  
ATOM   1563  CA  THR A 231     102.611 216.541   1.665  1.00 34.30           C  
ANISOU 1563  CA  THR A 231     2657   2600   7774    405    376   -233       C  
ATOM   1564  C   THR A 231     102.453 216.053   0.231  1.00 33.60           C  
ANISOU 1564  C   THR A 231     2526   2499   7741    242    264   -112       C  
ATOM   1565  O   THR A 231     101.614 215.184  -0.028  1.00 44.08           O  
ANISOU 1565  O   THR A 231     3799   3787   9163    269    282      5       O  
ATOM   1566  CB  THR A 231     101.604 217.666   1.919  1.00 54.84           C  
ANISOU 1566  CB  THR A 231     5232   5028  10576    438    405   -181       C  
ATOM   1567  OG1 THR A 231     101.884 218.769   1.046  1.00 55.16           O  
ANISOU 1567  OG1 THR A 231     5288   4996  10677    281    290   -188       O  
ATOM   1568  CG2 THR A 231     101.688 218.133   3.360  1.00 54.65           C  
ANISOU 1568  CG2 THR A 231     5263   5010  10490    622    518   -299       C  
ATOM   1569  N   TYR A 232     103.229 216.583  -0.710  1.00 33.46           N  
ANISOU 1569  N   TYR A 232     2538   2501   7676     79    161   -146       N  
ATOM   1570  CA  TYR A 232     103.037 216.253  -2.117  1.00 39.08           C  
ANISOU 1570  CA  TYR A 232     3251   3178   8420    -50     48    -26       C  
ATOM   1571  C   TYR A 232     104.320 215.769  -2.778  1.00 39.80           C  
ANISOU 1571  C   TYR A 232     3378   3416   8327   -171      6   -101       C  
ATOM   1572  O   TYR A 232     104.373 214.620  -3.229  1.00 42.64           O  
ANISOU 1572  O   TYR A 232     3718   3862   8622   -173    -35    -54       O  
ATOM   1573  CB  TYR A 232     102.461 217.469  -2.858  1.00 39.88           C  
ANISOU 1573  CB  TYR A 232     3402   3094   8655   -118    -24     52       C  
ATOM   1574  CG  TYR A 232     102.016 217.170  -4.271  1.00 39.25           C  
ANISOU 1574  CG  TYR A 232     3359   2946   8607   -184   -162    182       C  
ATOM   1575  CD1 TYR A 232     100.807 216.533  -4.519  1.00 39.90           C  
ANISOU 1575  CD1 TYR A 232     3350   2962   8846    -96   -234    276       C  
ATOM   1576  CD2 TYR A 232     102.801 217.532  -5.357  1.00 39.52           C  
ANISOU 1576  CD2 TYR A 232     3522   2968   8523   -323   -214    193       C  
ATOM   1577  CE1 TYR A 232     100.396 216.260  -5.809  1.00 41.29           C  
ANISOU 1577  CE1 TYR A 232     3562   3076   9049   -121   -399    363       C  
ATOM   1578  CE2 TYR A 232     102.399 217.263  -6.650  1.00 39.84           C  
ANISOU 1578  CE2 TYR A 232     3640   2940   8557   -344   -352    309       C  
ATOM   1579  CZ  TYR A 232     101.196 216.628  -6.872  1.00 39.86           C  
ANISOU 1579  CZ  TYR A 232     3548   2890   8705   -230   -467    386       C  
ATOM   1580  OH  TYR A 232     100.796 216.361  -8.160  1.00 38.00           O  
ANISOU 1580  OH  TYR A 232     3391   2587   8460   -218   -641    470       O  
ATOM   1581  N   ALA A 233     105.360 216.603  -2.838  1.00 36.24           N  
ANISOU 1581  N   ALA A 233     3904   2457   7408   -182    260    223       N  
ATOM   1582  CA  ALA A 233     106.556 216.299  -3.616  1.00 31.75           C  
ANISOU 1582  CA  ALA A 233     3358   1794   6911   -220    472    239       C  
ATOM   1583  C   ALA A 233     107.238 215.015  -3.165  1.00 37.79           C  
ANISOU 1583  C   ALA A 233     3888   2676   7793   -234    445    156       C  
ATOM   1584  O   ALA A 233     107.297 214.041  -3.925  1.00 38.31           O  
ANISOU 1584  O   ALA A 233     3985   2708   7863   -222    488    138       O  
ATOM   1585  CB  ALA A 233     107.554 217.456  -3.542  1.00 33.32           C  
ANISOU 1585  CB  ALA A 233     3556   1904   7200   -281    661    265       C  
ATOM   1586  N   ALA A 234     107.762 215.010  -1.937  1.00 36.79           N  
ANISOU 1586  N   ALA A 234     3567   2655   7758   -236    356    103       N  
ATOM   1587  CA  ALA A 234     108.518 213.856  -1.458  1.00 35.86           C  
ANISOU 1587  CA  ALA A 234     3279   2592   7756   -215    295     24       C  
ATOM   1588  C   ALA A 234     107.728 212.550  -1.480  1.00 34.89           C  
ANISOU 1588  C   ALA A 234     3181   2547   7528   -189    170     10       C  
ATOM   1589  O   ALA A 234     108.303 211.529  -1.895  1.00 33.24           O  
ANISOU 1589  O   ALA A 234     2905   2319   7405   -181    200    -37       O  
ATOM   1590  CB  ALA A 234     109.063 214.148  -0.053  1.00 34.37           C  
ANISOU 1590  CB  ALA A 234     2963   2443   7653   -191    161    -24       C  
ATOM   1591  N   PRO A 235     106.453 212.488  -1.068  1.00 35.07           N  
ANISOU 1591  N   PRO A 235     3279   2641   7406   -176     51     25       N  
ATOM   1592  CA  PRO A 235     105.754 211.193  -1.146  1.00 33.96           C  
ANISOU 1592  CA  PRO A 235     3144   2548   7211   -161    -27    -14       C  
ATOM   1593  C   PRO A 235     105.600 210.684  -2.567  1.00 32.65           C  
ANISOU 1593  C   PRO A 235     3028   2307   7070   -153     39    -21       C  
ATOM   1594  O   PRO A 235     105.786 209.486  -2.815  1.00 31.79           O  
ANISOU 1594  O   PRO A 235     2875   2210   6993   -145     23    -67       O  
ATOM   1595  CB  PRO A 235     104.394 211.488  -0.496  1.00 34.32           C  
ANISOU 1595  CB  PRO A 235     3234   2644   7163   -158   -108    -25       C  
ATOM   1596  CG  PRO A 235     104.638 212.670   0.365  1.00 35.61           C  
ANISOU 1596  CG  PRO A 235     3404   2815   7311   -169   -111      6       C  
ATOM   1597  CD  PRO A 235     105.614 213.502  -0.406  1.00 36.68           C  
ANISOU 1597  CD  PRO A 235     3533   2874   7529   -178     -7     49       C  
ATOM   1598  N   LEU A 236     105.276 211.570  -3.511  1.00 33.00           N  
ANISOU 1598  N   LEU A 236     3213   2240   7084   -143    107     22       N  
ATOM   1599  CA  LEU A 236     105.030 211.130  -4.880  1.00 36.18           C  
ANISOU 1599  CA  LEU A 236     3771   2511   7465    -95    148     12       C  
ATOM   1600  C   LEU A 236     106.296 210.566  -5.514  1.00 41.36           C  
ANISOU 1600  C   LEU A 236     4409   3098   8206   -124    336      8       C  
ATOM   1601  O   LEU A 236     106.253 209.524  -6.180  1.00 44.61           O  
ANISOU 1601  O   LEU A 236     4842   3477   8633    -92    333    -47       O  
ATOM   1602  CB  LEU A 236     104.474 212.285  -5.711  1.00 37.01           C  
ANISOU 1602  CB  LEU A 236     4151   2447   7465    -15    163     73       C  
ATOM   1603  CG  LEU A 236     103.896 211.901  -7.073  1.00 38.66           C  
ANISOU 1603  CG  LEU A 236     4628   2483   7579    143    112     42       C  
ATOM   1604  CD1 LEU A 236     102.703 210.968  -6.906  1.00 36.63           C  
ANISOU 1604  CD1 LEU A 236     4229   2329   7360    206   -144   -105       C  
ATOM   1605  CD2 LEU A 236     103.510 213.146  -7.852  1.00 41.74           C  
ANISOU 1605  CD2 LEU A 236     5391   2661   7808    288    110    122       C  
ATOM   1606  N   CYS A 237     107.437 211.233  -5.308  1.00 41.08           N  
ANISOU 1606  N   CYS A 237     4307   3035   8267   -181    507     33       N  
ATOM   1607  CA  CYS A 237     108.702 210.728  -5.836  1.00 43.05           C  
ANISOU 1607  CA  CYS A 237     4469   3210   8679   -217    722    -21       C  
ATOM   1608  C   CYS A 237     109.065 209.383  -5.217  1.00 40.45           C  
ANISOU 1608  C   CYS A 237     3908   2999   8461   -201    577   -118       C  
ATOM   1609  O   CYS A 237     109.615 208.508  -5.895  1.00 40.62           O  
ANISOU 1609  O   CYS A 237     3887   2962   8585   -203    682   -186       O  
ATOM   1610  CB  CYS A 237     109.816 211.749  -5.592  1.00 46.71           C  
ANISOU 1610  CB  CYS A 237     4839   3616   9293   -273    923    -28       C  
ATOM   1611  SG  CYS A 237     109.743 213.214  -6.654  1.00 53.21           S  
ANISOU 1611  SG  CYS A 237     6009   4222   9987   -309   1223     91       S  
ATOM   1612  N   LEU A 238     108.768 209.204  -3.928  1.00 37.40           N  
ANISOU 1612  N   LEU A 238     3416   2750   8042   -176    350   -125       N  
ATOM   1613  CA  LEU A 238     109.011 207.922  -3.277  1.00 34.63           C  
ANISOU 1613  CA  LEU A 238     2947   2468   7742   -143    195   -192       C  
ATOM   1614  C   LEU A 238     108.124 206.833  -3.867  1.00 37.23           C  
ANISOU 1614  C   LEU A 238     3353   2819   7974   -132    137   -208       C  
ATOM   1615  O   LEU A 238     108.590 205.723  -4.151  1.00 39.96           O  
ANISOU 1615  O   LEU A 238     3627   3148   8408   -119    129   -276       O  
ATOM   1616  CB  LEU A 238     108.775 208.047  -1.771  1.00 32.40           C  
ANISOU 1616  CB  LEU A 238     2657   2268   7385   -123      3   -174       C  
ATOM   1617  CG  LEU A 238     108.944 206.779  -0.933  1.00 33.09           C  
ANISOU 1617  CG  LEU A 238     2724   2378   7470    -98   -168   -218       C  
ATOM   1618  CD1 LEU A 238     110.414 206.506  -0.661  1.00 35.39           C  
ANISOU 1618  CD1 LEU A 238     2836   2595   8017    -64   -219   -308       C  
ATOM   1619  CD2 LEU A 238     108.162 206.891   0.363  1.00 30.27           C  
ANISOU 1619  CD2 LEU A 238     2505   2067   6929   -115   -294   -176       C  
ATOM   1620  N   MET A 239     106.838 207.136  -4.063  1.00 35.03           N  
ANISOU 1620  N   MET A 239     3198   2561   7552   -129     83   -173       N  
ATOM   1621  CA  MET A 239     105.905 206.120  -4.540  1.00 32.19           C  
ANISOU 1621  CA  MET A 239     2874   2209   7149   -107      1   -230       C  
ATOM   1622  C   MET A 239     106.161 205.767  -5.998  1.00 32.11           C  
ANISOU 1622  C   MET A 239     2951   2070   7179    -78    103   -272       C  
ATOM   1623  O   MET A 239     106.041 204.600  -6.386  1.00 33.23           O  
ANISOU 1623  O   MET A 239     3065   2212   7348    -56     55   -352       O  
ATOM   1624  CB  MET A 239     104.466 206.592  -4.338  1.00 30.60           C  
ANISOU 1624  CB  MET A 239     2728   2035   6865    -93    -99   -238       C  
ATOM   1625  CG  MET A 239     104.013 206.536  -2.891  1.00 30.40           C  
ANISOU 1625  CG  MET A 239     2658   2111   6783   -116   -160   -229       C  
ATOM   1626  SD  MET A 239     102.325 207.109  -2.635  1.00 32.76           S  
ANISOU 1626  SD  MET A 239     2955   2422   7071   -107   -223   -287       S  
ATOM   1627  CE  MET A 239     102.592 208.868  -2.431  1.00 33.02           C  
ANISOU 1627  CE  MET A 239     3040   2436   7070   -111   -196   -195       C  
ATOM   1628  N   VAL A 240     106.517 206.755  -6.821  1.00 30.79           N  
ANISOU 1628  N   VAL A 240     2939   1767   6994    -63    266   -220       N  
ATOM   1629  CA  VAL A 240     106.833 206.473  -8.219  1.00 32.70           C  
ANISOU 1629  CA  VAL A 240     3369   1833   7224      2    427   -254       C  
ATOM   1630  C   VAL A 240     108.032 205.539  -8.312  1.00 39.02           C  
ANISOU 1630  C   VAL A 240     3994   2637   8195    -53    565   -330       C  
ATOM   1631  O   VAL A 240     108.057 204.614  -9.134  1.00 39.86           O  
ANISOU 1631  O   VAL A 240     4162   2679   8305      3    598   -418       O  
ATOM   1632  CB  VAL A 240     107.068 207.785  -8.994  1.00 39.81           C  
ANISOU 1632  CB  VAL A 240     4556   2541   8031     35    652   -158       C  
ATOM   1633  CG1 VAL A 240     107.665 207.500 -10.365  1.00 42.17           C  
ANISOU 1633  CG1 VAL A 240     5111   2625   8286     99    943   -187       C  
ATOM   1634  CG2 VAL A 240     105.767 208.558  -9.142  1.00 39.21           C  
ANISOU 1634  CG2 VAL A 240     4700   2418   7779    162    451   -118       C  
ATOM   1635  N   LEU A 241     109.035 205.751  -7.459  1.00 38.20           N  
ANISOU 1635  N   LEU A 241     3662   2603   8249   -130    616   -330       N  
ATOM   1636  CA  LEU A 241     110.218 204.897  -7.473  1.00 38.87           C  
ANISOU 1636  CA  LEU A 241     3535   2677   8558   -151    702   -443       C  
ATOM   1637  C   LEU A 241     109.925 203.497  -6.946  1.00 40.01           C  
ANISOU 1637  C   LEU A 241     3568   2932   8703   -113    447   -504       C  
ATOM   1638  O   LEU A 241     110.530 202.527  -7.415  1.00 42.62           O  
ANISOU 1638  O   LEU A 241     3808   3220   9164   -105    496   -612       O  
ATOM   1639  CB  LEU A 241     111.342 205.548  -6.673  1.00 34.65           C  
ANISOU 1639  CB  LEU A 241     2780   2155   8231   -179    764   -474       C  
ATOM   1640  CG  LEU A 241     112.253 206.465  -7.480  1.00 43.09           C  
ANISOU 1640  CG  LEU A 241     3864   3062   9444   -243   1159   -506       C  
ATOM   1641  CD1 LEU A 241     112.980 207.411  -6.551  1.00 42.93           C  
ANISOU 1641  CD1 LEU A 241     3662   3060   9589   -245   1152   -529       C  
ATOM   1642  CD2 LEU A 241     113.246 205.641  -8.290  1.00 46.44           C  
ANISOU 1642  CD2 LEU A 241     4160   3378  10105   -268   1409   -671       C  
ATOM   1643  N   LEU A 242     109.004 203.363  -5.988  1.00 39.75           N  
ANISOU 1643  N   LEU A 242     3560   3019   8525    -96    213   -446       N  
ATOM   1644  CA  LEU A 242     108.665 202.039  -5.472  1.00 39.49           C  
ANISOU 1644  CA  LEU A 242     3488   3053   8463    -72     28   -488       C  
ATOM   1645  C   LEU A 242     107.739 201.281  -6.414  1.00 40.56           C  
ANISOU 1645  C   LEU A 242     3719   3169   8524    -52     10   -544       C  
ATOM   1646  O   LEU A 242     107.908 200.072  -6.608  1.00 41.88           O  
ANISOU 1646  O   LEU A 242     3837   3332   8743    -36    -42   -624       O  
ATOM   1647  CB  LEU A 242     108.022 202.150  -4.090  1.00 39.37           C  
ANISOU 1647  CB  LEU A 242     3521   3125   8312    -72   -130   -419       C  
ATOM   1648  CG  LEU A 242     108.905 202.708  -2.975  1.00 42.04           C  
ANISOU 1648  CG  LEU A 242     3800   3464   8709    -66   -190   -392       C  
ATOM   1649  CD1 LEU A 242     108.154 202.778  -1.651  1.00 42.66           C  
ANISOU 1649  CD1 LEU A 242     4015   3587   8605    -82   -313   -328       C  
ATOM   1650  CD2 LEU A 242     110.171 201.878  -2.839  1.00 43.35           C  
ANISOU 1650  CD2 LEU A 242     3819   3570   9083    -35   -259   -485       C  
ATOM   1651  N   TYR A 243     106.753 201.964  -7.002  1.00 40.06           N  
ANISOU 1651  N   TYR A 243     3795   3075   8352    -33     18   -526       N  
ATOM   1652  CA  TYR A 243     105.805 201.281  -7.877  1.00 39.67           C  
ANISOU 1652  CA  TYR A 243     3833   2990   8251     32    -64   -627       C  
ATOM   1653  C   TYR A 243     106.409 200.950  -9.234  1.00 40.90           C  
ANISOU 1653  C   TYR A 243     4104   3015   8421    113     69   -710       C  
ATOM   1654  O   TYR A 243     105.975 199.988  -9.878  1.00 42.49           O  
ANISOU 1654  O   TYR A 243     4337   3207   8599    188    -16   -832       O  
ATOM   1655  CB  TYR A 243     104.540 202.123  -8.062  1.00 39.45           C  
ANISOU 1655  CB  TYR A 243     3916   2947   8125     86   -162   -631       C  
ATOM   1656  CG  TYR A 243     103.592 202.068  -6.886  1.00 38.66           C  
ANISOU 1656  CG  TYR A 243     3692   2967   8031     23   -273   -626       C  
ATOM   1657  CD1 TYR A 243     102.986 200.876  -6.516  1.00 40.67           C  
ANISOU 1657  CD1 TYR A 243     3848   3277   8327      4   -342   -712       C  
ATOM   1658  CD2 TYR A 243     103.294 203.208  -6.153  1.00 40.58           C  
ANISOU 1658  CD2 TYR A 243     3940   3244   8233     -7   -266   -540       C  
ATOM   1659  CE1 TYR A 243     102.117 200.818  -5.443  1.00 41.38           C  
ANISOU 1659  CE1 TYR A 243     3882   3431   8410    -37   -352   -711       C  
ATOM   1660  CE2 TYR A 243     102.424 203.161  -5.080  1.00 41.66           C  
ANISOU 1660  CE2 TYR A 243     4001   3463   8365    -44   -307   -550       C  
ATOM   1661  CZ  TYR A 243     101.839 201.964  -4.728  1.00 41.29           C  
ANISOU 1661  CZ  TYR A 243     3892   3447   8351    -58   -326   -634       C  
ATOM   1662  OH  TYR A 243     100.973 201.914  -3.658  1.00 41.25           O  
ANISOU 1662  OH  TYR A 243     3873   3475   8324    -98   -286   -649       O  
ATOM   1663  N   LEU A 244     107.396 201.727  -9.689  1.00 40.94           N  
ANISOU 1663  N   LEU A 244     4183   2910   8463    106    310   -663       N  
ATOM   1664  CA  LEU A 244     108.071 201.385 -10.936  1.00 44.44           C  
ANISOU 1664  CA  LEU A 244     4763   3206   8915    180    537   -755       C  
ATOM   1665  C   LEU A 244     108.838 200.076 -10.805  1.00 43.98           C  
ANISOU 1665  C   LEU A 244     4481   3206   9024    135    528   -866       C  
ATOM   1666  O   LEU A 244     108.906 199.293 -11.759  1.00 45.32           O  
ANISOU 1666  O   LEU A 244     4742   3318   9160    225    589   -992       O  
ATOM   1667  CB  LEU A 244     109.010 202.515 -11.363  1.00 48.12           C  
ANISOU 1667  CB  LEU A 244     5352   3518   9414    136    902   -689       C  
ATOM   1668  CG  LEU A 244     108.403 203.612 -12.242  1.00 50.09           C  
ANISOU 1668  CG  LEU A 244     6023   3655   9355    251   1010   -596       C  
ATOM   1669  CD1 LEU A 244     109.438 204.684 -12.538  1.00 50.86           C  
ANISOU 1669  CD1 LEU A 244     6244   3603   9479    149   1443   -513       C  
ATOM   1670  CD2 LEU A 244     107.843 203.029 -13.533  1.00 52.18           C  
ANISOU 1670  CD2 LEU A 244     6618   3944   9264    442    958   -675       C  
ATOM   1671  N   GLN A 245     109.426 199.821  -9.634  1.00 42.66           N  
ANISOU 1671  N   GLN A 245     4049   3145   9017     32    430   -835       N  
ATOM   1672  CA  GLN A 245     110.076 198.534  -9.413  1.00 43.07           C  
ANISOU 1672  CA  GLN A 245     3912   3234   9217     23    349   -940       C  
ATOM   1673  C   GLN A 245     109.056 197.414  -9.253  1.00 41.31           C  
ANISOU 1673  C   GLN A 245     3724   3089   8881     60    110   -967       C  
ATOM   1674  O   GLN A 245     109.348 196.258  -9.582  1.00 42.42           O  
ANISOU 1674  O   GLN A 245     3808   3223   9089     86     71  -1075       O  
ATOM   1675  CB  GLN A 245     110.984 198.602  -8.186  1.00 45.36           C  
ANISOU 1675  CB  GLN A 245     3970   3579   9686    -25    260   -918       C  
ATOM   1676  CG  GLN A 245     112.136 199.586  -8.310  1.00 51.02           C  
ANISOU 1676  CG  GLN A 245     4557   4216  10612    -70    502   -952       C  
ATOM   1677  CD  GLN A 245     113.214 199.338  -7.273  1.00 55.48           C  
ANISOU 1677  CD  GLN A 245     4843   4805  11433    -60    355  -1027       C  
ATOM   1678  OE1 GLN A 245     113.119 198.404  -6.478  1.00 56.02           O  
ANISOU 1678  OE1 GLN A 245     4882   4927  11475    -14     70  -1031       O  
ATOM   1679  NE2 GLN A 245     114.249 200.170  -7.281  1.00 58.30           N  
ANISOU 1679  NE2 GLN A 245     5014   5092  12046    -89    550  -1104       N  
ATOM   1680  N   ILE A 246     107.865 197.735  -8.746  1.00 39.88           N  
ANISOU 1680  N   ILE A 246     3619   2975   8559     55    -28   -891       N  
ATOM   1681  CA  ILE A 246     106.808 196.736  -8.622  1.00 39.08           C  
ANISOU 1681  CA  ILE A 246     3526   2927   8397     70   -193   -946       C  
ATOM   1682  C   ILE A 246     106.222 196.407  -9.990  1.00 39.88           C  
ANISOU 1682  C   ILE A 246     3743   2971   8437    173   -202  -1088       C  
ATOM   1683  O   ILE A 246     105.959 195.240 -10.302  1.00 41.57           O  
ANISOU 1683  O   ILE A 246     3921   3199   8675    200   -286  -1201       O  
ATOM   1684  CB  ILE A 246     105.732 197.227  -7.637  1.00 31.21           C  
ANISOU 1684  CB  ILE A 246     2542   2003   7315     30   -279   -861       C  
ATOM   1685  CG1 ILE A 246     106.283 197.207  -6.210  1.00 30.40           C  
ANISOU 1685  CG1 ILE A 246     2407   1942   7203    -14   -301   -749       C  
ATOM   1686  CG2 ILE A 246     104.468 196.385  -7.752  1.00 31.44           C  
ANISOU 1686  CG2 ILE A 246     2559   2054   7331     42   -380   -964       C  
ATOM   1687  CD1 ILE A 246     105.447 197.970  -5.220  1.00 38.31           C  
ANISOU 1687  CD1 ILE A 246     3472   2992   8093    -47   -313   -661       C  
ATOM   1688  N   PHE A 247     106.018 197.424 -10.830  1.00 39.61           N  
ANISOU 1688  N   PHE A 247     3891   2862   8298    267   -127  -1092       N  
ATOM   1689  CA  PHE A 247     105.530 197.176 -12.183  1.00 41.81           C  
ANISOU 1689  CA  PHE A 247     4365   3072   8447    451   -165  -1246       C  
ATOM   1690  C   PHE A 247     106.526 196.342 -12.978  1.00 43.42           C  
ANISOU 1690  C   PHE A 247     4592   3221   8686    498     -8  -1348       C  
ATOM   1691  O   PHE A 247     106.149 195.377 -13.653  1.00 41.19           O  
ANISOU 1691  O   PHE A 247     4344   2955   8353    594   -117  -1503       O  
ATOM   1692  CB  PHE A 247     105.243 198.503 -12.891  1.00 42.71           C  
ANISOU 1692  CB  PHE A 247     4763   3074   8393    596   -109  -1215       C  
ATOM   1693  CG  PHE A 247     104.983 198.360 -14.368  1.00 45.42           C  
ANISOU 1693  CG  PHE A 247     5432   3388   8437    820   -134  -1336       C  
ATOM   1694  CD1 PHE A 247     103.721 198.036 -14.836  1.00 45.70           C  
ANISOU 1694  CD1 PHE A 247     5538   3457   8368    990   -468  -1506       C  
ATOM   1695  CD2 PHE A 247     106.002 198.554 -15.288  1.00 48.39           C  
ANISOU 1695  CD2 PHE A 247     6062   3709   8616    856    183  -1295       C  
ATOM   1696  CE1 PHE A 247     103.482 197.902 -16.191  1.00 49.74           C  
ANISOU 1696  CE1 PHE A 247     6406   3952   8541   1228   -552  -1623       C  
ATOM   1697  CE2 PHE A 247     105.768 198.421 -16.645  1.00 51.74           C  
ANISOU 1697  CE2 PHE A 247     6883   4108   8667   1068    172  -1387       C  
ATOM   1698  CZ  PHE A 247     104.507 198.096 -17.096  1.00 52.46           C  
ANISOU 1698  CZ  PHE A 247     7081   4237   8612   1272   -230  -1546       C  
ATOM   1699  N   ARG A 248     107.811 196.695 -12.899  1.00 49.41           N  
ANISOU 1699  N   ARG A 248     5301   3918   9555    423    256  -1289       N  
ATOM   1700  CA  ARG A 248     108.826 196.003 -13.688  1.00 52.58           C  
ANISOU 1700  CA  ARG A 248     5698   4257  10021    456    468  -1417       C  
ATOM   1701  C   ARG A 248     108.909 194.527 -13.320  1.00 51.42           C  
ANISOU 1701  C   ARG A 248     5335   4205   9995    413    277  -1501       C  
ATOM   1702  O   ARG A 248     109.131 193.673 -14.187  1.00 55.65           O  
ANISOU 1702  O   ARG A 248     5919   4720  10506    498    325  -1653       O  
ATOM   1703  CB  ARG A 248     110.183 196.683 -13.500  1.00 56.99           C  
ANISOU 1703  CB  ARG A 248     6150   4742  10760    341    792  -1373       C  
ATOM   1704  CG  ARG A 248     111.315 196.043 -14.285  1.00 63.95           C  
ANISOU 1704  CG  ARG A 248     6979   5560  11759    345   1074  -1537       C  
ATOM   1705  CD  ARG A 248     111.171 196.310 -15.772  1.00 70.06           C  
ANISOU 1705  CD  ARG A 248     8161   6231  12227    484   1370  -1611       C  
ATOM   1706  NE  ARG A 248     111.899 195.335 -16.577  1.00 74.76           N  
ANISOU 1706  NE  ARG A 248     8733   6790  12883    521   1569  -1812       N  
ATOM   1707  CZ  ARG A 248     111.991 195.385 -17.901  1.00 79.04           C  
ANISOU 1707  CZ  ARG A 248     9663   7295  13075    615   1857  -1869       C  
ATOM   1708  NH1 ARG A 248     111.405 196.370 -18.568  1.00 81.47           N  
ANISOU 1708  NH1 ARG A 248    10449   7578  12927    700   1946  -1728       N  
ATOM   1709  NH2 ARG A 248     112.669 194.455 -18.558  1.00 80.38           N  
ANISOU 1709  NH2 ARG A 248     9782   7429  13329    639   2048  -2072       N  
ATOM   1710  N   LYS A 249     108.724 194.207 -12.038  1.00 47.06           N  
ANISOU 1710  N   LYS A 249     4589   3743   9549    292     77  -1404       N  
ATOM   1711  CA  LYS A 249     108.822 192.820 -11.598  1.00 45.86           C  
ANISOU 1711  CA  LYS A 249     4291   3639   9496    259    -84  -1460       C  
ATOM   1712  C   LYS A 249     107.592 192.018 -12.002  1.00 46.24           C  
ANISOU 1712  C   LYS A 249     4409   3723   9438    316   -251  -1548       C  
ATOM   1713  O   LYS A 249     107.707 190.965 -12.639  1.00 47.42           O  
ANISOU 1713  O   LYS A 249     4548   3864   9607    371   -281  -1683       O  
ATOM   1714  CB  LYS A 249     109.023 192.760 -10.083  1.00 44.27           C  
ANISOU 1714  CB  LYS A 249     3956   3485   9378    162   -214  -1328       C  
ATOM   1715  CG  LYS A 249     108.846 191.363  -9.511  1.00 44.82           C  
ANISOU 1715  CG  LYS A 249     3980   3569   9481    159   -385  -1353       C  
ATOM   1716  CD  LYS A 249     109.484 191.223  -8.145  1.00 45.89           C  
ANISOU 1716  CD  LYS A 249     4070   3695   9672    133   -493  -1254       C  
ATOM   1717  CE  LYS A 249     109.455 189.772  -7.692  1.00 47.22           C  
ANISOU 1717  CE  LYS A 249     4274   3819   9851    154   -638  -1284       C  
ATOM   1718  NZ  LYS A 249     110.279 189.527  -6.478  1.00 48.69           N  
ANISOU 1718  NZ  LYS A 249     4485   3940  10074    169   -786  -1226       N  
ATOM   1719  N   LEU A 250     106.403 192.501 -11.641  1.00 45.90           N  
ANISOU 1719  N   LEU A 250     4408   3721   9311    301   -361  -1498       N  
ATOM   1720  CA  LEU A 250     105.192 191.708 -11.826  1.00 44.48           C  
ANISOU 1720  CA  LEU A 250     4208   3577   9114    325   -525  -1613       C  
ATOM   1721  C   LEU A 250     104.755 191.659 -13.286  1.00 46.55           C  
ANISOU 1721  C   LEU A 250     4619   3817   9249    503   -582  -1802       C  
ATOM   1722  O   LEU A 250     104.329 190.606 -13.771  1.00 49.28           O  
ANISOU 1722  O   LEU A 250     4927   4181   9615    549   -695  -1954       O  
ATOM   1723  CB  LEU A 250     104.070 192.260 -10.944  1.00 40.67           C  
ANISOU 1723  CB  LEU A 250     3677   3143   8635    253   -595  -1541       C  
ATOM   1724  CG  LEU A 250     104.263 192.072  -9.438  1.00 37.22           C  
ANISOU 1724  CG  LEU A 250     3172   2726   8244    133   -546  -1374       C  
ATOM   1725  CD1 LEU A 250     103.227 192.869  -8.670  1.00 37.15           C  
ANISOU 1725  CD1 LEU A 250     3158   2755   8204     86   -541  -1311       C  
ATOM   1726  CD2 LEU A 250     104.190 190.598  -9.065  1.00 35.67           C  
ANISOU 1726  CD2 LEU A 250     2939   2505   8110    107   -575  -1413       C  
ATOM   1727  N   TRP A 251     104.859 192.777 -14.004  1.00 46.76           N  
ANISOU 1727  N   TRP A 251     4855   3794   9118    631   -508  -1797       N  
ATOM   1728  CA  TRP A 251     104.371 192.819 -15.379  1.00 49.42           C  
ANISOU 1728  CA  TRP A 251     5437   4095   9245    868   -600  -1979       C  
ATOM   1729  C   TRP A 251     105.382 192.229 -16.358  1.00 51.82           C  
ANISOU 1729  C   TRP A 251     5877   4335   9478    969   -420  -2082       C  
ATOM   1730  O   TRP A 251     105.021 191.423 -17.222  1.00 53.58           O  
ANISOU 1730  O   TRP A 251     6186   4572   9598   1103   -548  -2267       O  
ATOM   1731  CB  TRP A 251     104.026 194.258 -15.772  1.00 51.56           C  
ANISOU 1731  CB  TRP A 251     5972   4297   9320   1011   -604  -1936       C  
ATOM   1732  CG  TRP A 251     102.596 194.643 -15.508  1.00 54.64           C  
ANISOU 1732  CG  TRP A 251     6306   4756   9697   1046   -900  -1990       C  
ATOM   1733  CD1 TRP A 251     101.558 194.593 -16.394  1.00 58.41           C  
ANISOU 1733  CD1 TRP A 251     6925   5253  10016   1262  -1195  -2192       C  
ATOM   1734  CD2 TRP A 251     102.046 195.138 -14.277  1.00 53.59           C  
ANISOU 1734  CD2 TRP A 251     5946   4685   9732    863   -931  -1872       C  
ATOM   1735  NE1 TRP A 251     100.400 195.025 -15.795  1.00 58.59           N  
ANISOU 1735  NE1 TRP A 251     6764   5344  10153   1213  -1402  -2225       N  
ATOM   1736  CE2 TRP A 251     100.672 195.366 -14.496  1.00 55.53           C  
ANISOU 1736  CE2 TRP A 251     6160   4977   9960    964  -1215  -2030       C  
ATOM   1737  CE3 TRP A 251     102.582 195.410 -13.014  1.00 51.47           C  
ANISOU 1737  CE3 TRP A 251     5506   4436   9615    637   -758  -1668       C  
ATOM   1738  CZ2 TRP A 251      99.827 195.855 -13.499  1.00 54.58           C  
ANISOU 1738  CZ2 TRP A 251     5822   4912  10003    829  -1273  -1999       C  
ATOM   1739  CZ3 TRP A 251     101.741 195.895 -12.025  1.00 50.60           C  
ANISOU 1739  CZ3 TRP A 251     5242   4383   9602    521   -825  -1616       C  
ATOM   1740  CH2 TRP A 251     100.379 196.111 -12.274  1.00 51.68           C  
ANISOU 1740  CH2 TRP A 251     5329   4553   9752    607  -1052  -1785       C  
ATOM   1741  N   CYS A 252     106.651 192.619 -16.238  1.00 51.97           N  
ANISOU 1741  N   CYS A 252     5893   4285   9570    896   -110  -1987       N  
ATOM   1742  CA  CYS A 252     107.666 192.292 -17.236  1.00 56.84           C  
ANISOU 1742  CA  CYS A 252     6650   4817  10128    981    166  -2109       C  
ATOM   1743  C   CYS A 252     108.535 191.109 -16.821  1.00 57.94           C  
ANISOU 1743  C   CYS A 252     6493   5010  10511    848    204  -2137       C  
ATOM   1744  O   CYS A 252     108.530 190.067 -17.484  1.00 59.24           O  
ANISOU 1744  O   CYS A 252     6677   5191  10639    927    149  -2295       O  
ATOM   1745  CB  CYS A 252     108.536 193.526 -17.506  1.00 59.88           C  
ANISOU 1745  CB  CYS A 252     7227   5136  10388    942    553  -1973       C  
ATOM   1746  SG  CYS A 252     107.614 194.974 -18.075  1.00 60.73           S  
ANISOU 1746  SG  CYS A 252     7801   5247  10028   1080    498  -1831       S  
ATOM   1747  N   ARG A 253     109.291 191.258 -15.729  1.00 58.03           N  
ANISOU 1747  N   ARG A 253     6246   5040  10764    667    260  -2000       N  
ATOM   1748  CA  ARG A 253     110.260 190.237 -15.341  1.00 58.14           C  
ANISOU 1748  CA  ARG A 253     6007   5072  11012    576    263  -2049       C  
ATOM   1749  C   ARG A 253     109.585 188.932 -14.934  1.00 57.31           C  
ANISOU 1749  C   ARG A 253     5798   5031  10946    559    -40  -2082       C  
ATOM   1750  O   ARG A 253     110.186 187.860 -15.067  1.00 57.56           O  
ANISOU 1750  O   ARG A 253     5715   5057  11099    557    -61  -2183       O  
ATOM   1751  CB  ARG A 253     111.143 190.761 -14.208  1.00 59.24           C  
ANISOU 1751  CB  ARG A 253     5923   5205  11380    427    304  -1925       C  
ATOM   1752  CG  ARG A 253     111.992 191.966 -14.595  1.00 64.94           C  
ANISOU 1752  CG  ARG A 253     6683   5845  12145    403    662  -1919       C  
ATOM   1753  CD  ARG A 253     113.071 191.599 -15.607  1.00 72.79           C  
ANISOU 1753  CD  ARG A 253     7658   6771  13226    426    989  -2108       C  
ATOM   1754  NE  ARG A 253     113.813 192.773 -16.059  1.00 79.56           N  
ANISOU 1754  NE  ARG A 253     8592   7525  14112    373   1431  -2111       N  
ATOM   1755  CZ  ARG A 253     114.825 193.322 -15.394  1.00 83.95           C  
ANISOU 1755  CZ  ARG A 253     8874   8047  14978    222   1557  -2102       C  
ATOM   1756  NH1 ARG A 253     115.222 192.804 -14.240  1.00 84.23           N  
ANISOU 1756  NH1 ARG A 253     8581   8141  15281    147   1226  -2096       N  
ATOM   1757  NH2 ARG A 253     115.441 194.391 -15.880  1.00 87.12           N  
ANISOU 1757  NH2 ARG A 253     9359   8335  15409    148   2014  -2113       N  
ATOM   1758  N   GLN A 254     108.347 188.996 -14.442  1.00 56.75           N  
ANISOU 1758  N   GLN A 254     5756   5008  10798    537   -248  -2012       N  
ATOM   1759  CA  GLN A 254     107.575 187.804 -14.115  1.00 57.17           C  
ANISOU 1759  CA  GLN A 254     5724   5098  10900    505   -463  -2059       C  
ATOM   1760  C   GLN A 254     106.373 187.633 -15.037  1.00 58.83           C  
ANISOU 1760  C   GLN A 254     6051   5337  10966    622   -589  -2208       C  
ATOM   1761  O   GLN A 254     105.402 186.964 -14.672  1.00 59.63           O  
ANISOU 1761  O   GLN A 254     6057   5469  11133    573   -752  -2244       O  
ATOM   1762  CB  GLN A 254     107.130 187.842 -12.654  1.00 57.20           C  
ANISOU 1762  CB  GLN A 254     5628   5122  10982    370   -561  -1889       C  
ATOM   1763  CG  GLN A 254     107.486 186.585 -11.881  1.00 59.15           C  
ANISOU 1763  CG  GLN A 254     5783   5339  11353    320   -645  -1867       C  
ATOM   1764  CD  GLN A 254     107.653 186.837 -10.396  1.00 58.96           C  
ANISOU 1764  CD  GLN A 254     5762   5296  11343    242   -673  -1677       C  
ATOM   1765  OE1 GLN A 254     108.537 186.267  -9.757  1.00 60.07           O  
ANISOU 1765  OE1 GLN A 254     5882   5382  11559    244   -731  -1643       O  
ATOM   1766  NE2 GLN A 254     106.801 187.690  -9.839  1.00 57.31           N  
ANISOU 1766  NE2 GLN A 254     5607   5123  11047    193   -650  -1572       N  
ATOM   1767  N   GLY A1001     106.423 188.223 -16.227  1.00 61.58           N  
ANISOU 1767  N   GLY A1001     6619   5661  11118    792   -509  -2313       N  
ATOM   1768  CA  GLY A1001     105.338 188.102 -17.176  1.00 64.01           C  
ANISOU 1768  CA  GLY A1001     7078   5992  11250    959   -696  -2486       C  
ATOM   1769  C   GLY A1001     105.037 186.846 -17.965  1.00 67.24           C  
ANISOU 1769  C   GLY A1001     7456   6415  11677   1024   -787  -2671       C  
ATOM   1770  O   GLY A1001     105.171 186.826 -19.192  1.00 70.43           O  
ANISOU 1770  O   GLY A1001     8055   6781  11923   1173   -670  -2794       O  
ATOM   1771  N   ILE A1002     104.633 185.791 -17.267  1.00 65.53           N  
ANISOU 1771  N   ILE A1002     7010   6237  11651    910   -958  -2698       N  
ATOM   1772  CA  ILE A1002     104.476 184.465 -17.851  1.00 69.06           C  
ANISOU 1772  CA  ILE A1002     7396   6692  12152    958  -1068  -2876       C  
ATOM   1773  C   ILE A1002     103.206 184.452 -18.697  1.00 76.79           C  
ANISOU 1773  C   ILE A1002     8440   7715  13021   1113  -1323  -3081       C  
ATOM   1774  O   ILE A1002     102.100 184.649 -18.182  1.00 76.88           O  
ANISOU 1774  O   ILE A1002     8297   7760  13152   1051  -1472  -3094       O  
ATOM   1775  CB  ILE A1002     104.437 183.382 -16.761  1.00 64.15           C  
ANISOU 1775  CB  ILE A1002     6520   6052  11800    770  -1088  -2801       C  
ATOM   1776  CG1 ILE A1002     103.993 182.041 -17.347  1.00 64.96           C  
ANISOU 1776  CG1 ILE A1002     6541   6155  11986    818  -1224  -2996       C  
ATOM   1777  CG2 ILE A1002     103.557 183.814 -15.585  1.00 60.03           C  
ANISOU 1777  CG2 ILE A1002     5876   5541  11394    628  -1111  -2668       C  
ATOM   1778  CD1 ILE A1002     105.102 181.278 -18.027  1.00 50.94           C  
ANISOU 1778  CD1 ILE A1002     4824   4350  10181    889  -1148  -3076       C  
ATOM   1779  N   ASP A1003     103.366 184.231 -20.000  1.00 82.72           N  
ANISOU 1779  N   ASP A1003     9420   8461  13549   1328  -1373  -3260       N  
ATOM   1780  CA  ASP A1003     102.232 184.181 -20.919  1.00 89.37           C  
ANISOU 1780  CA  ASP A1003    10359   9342  14255   1527  -1683  -3483       C  
ATOM   1781  C   ASP A1003     101.637 182.775 -20.961  1.00 98.72           C  
ANISOU 1781  C   ASP A1003    11272  10555  15682   1476  -1860  -3650       C  
ATOM   1782  O   ASP A1003     102.063 181.933 -21.752  1.00100.00           O  
ANISOU 1782  O   ASP A1003    11520  10705  15770   1573  -1865  -3779       O  
ATOM   1783  CB  ASP A1003     102.661 184.621 -22.324  1.00 89.85           C  
ANISOU 1783  CB  ASP A1003    10884   9363  13893   1814  -1662  -3596       C  
ATOM   1784  CG  ASP A1003     101.511 184.618 -23.321  1.00 89.83           C  
ANISOU 1784  CG  ASP A1003    11041   9396  13695   2069  -2059  -3829       C  
ATOM   1785  OD1 ASP A1003     100.337 184.566 -22.895  1.00 88.98           O  
ANISOU 1785  OD1 ASP A1003    10646   9348  13815   2027  -2343  -3905       O  
ATOM   1786  OD2 ASP A1003     101.786 184.665 -24.539  1.00 91.55           O  
ANISOU 1786  OD2 ASP A1003    11678   9573  13535   2321  -2082  -3948       O  
HETATM 1787  N   YCM A1004     100.534 182.515 -20.088  1.00 52.98           N  
HETATM 1788  CA  YCM A1004     100.008 181.178 -19.957  1.00 54.44           C  
HETATM 1789  CB  YCM A1004      99.121 181.049 -18.721  1.00 57.84           C  
HETATM 1790  SG  YCM A1004      99.873 181.488 -17.181  1.00 61.76           S  
HETATM 1791  CD  YCM A1004      98.805 180.788 -15.962  1.00 68.55           C  
HETATM 1792  CE  YCM A1004      98.732 179.277 -16.010  1.00 73.88           C  
HETATM 1793  OZ1 YCM A1004      99.738 178.597 -16.310  1.00 75.07           O  
HETATM 1794  NZ2 YCM A1004      97.541 178.670 -15.721  1.00 75.45           N  
HETATM 1795  C   YCM A1004      99.222 180.723 -21.181  1.00 51.08           C  
HETATM 1796  O   YCM A1004      98.887 179.552 -21.383  1.00 52.54           O  
ATOM   1797  N   SER A1005      98.916 181.699 -22.030  1.00107.88           N  
ANISOU 1797  N   SER A1005    10864  11684  18441   1572  -1146   -517       N  
ATOM   1798  CA  SER A1005      98.195 181.438 -23.268  1.00105.58           C  
ANISOU 1798  CA  SER A1005    10559  11499  18058   1667  -1555   -665       C  
ATOM   1799  C   SER A1005      99.103 180.746 -24.277  1.00 98.82           C  
ANISOU 1799  C   SER A1005    10104  10689  16753   1722  -1608   -593       C  
ATOM   1800  O   SER A1005      98.629 180.073 -25.192  1.00102.43           O  
ANISOU 1800  O   SER A1005    10594  11224  17100   1756  -1902   -785       O  
ATOM   1801  CB  SER A1005      97.644 182.738 -23.855  1.00109.32           C  
ANISOU 1801  CB  SER A1005    10936  12038  18563   1927  -1863   -571       C  
ATOM   1802  OG  SER A1005      96.843 183.421 -22.907  1.00110.02           O  
ANISOU 1802  OG  SER A1005    10656  12082  19065   1885  -1805   -632       O  
ATOM   1803  N   PHE A1006     100.413 180.918 -24.109  1.00 89.91           N  
ANISOU 1803  N   PHE A1006     9274   9506  15382   1746  -1331   -333       N  
ATOM   1804  CA  PHE A1006     101.396 180.270 -24.967  1.00 84.46           C  
ANISOU 1804  CA  PHE A1006     8976   8843  14271   1795  -1312   -238       C  
ATOM   1805  C   PHE A1006     102.047 179.066 -24.296  1.00 82.40           C  
ANISOU 1805  C   PHE A1006     8816   8510  13984   1548  -1003   -320       C  
ATOM   1806  O   PHE A1006     102.120 177.988 -24.893  1.00 81.10           O  
ANISOU 1806  O   PHE A1006     8798   8382  13634   1484  -1084   -460       O  
ATOM   1807  CB  PHE A1006     102.475 181.274 -25.399  1.00 78.37           C  
ANISOU 1807  CB  PHE A1006     8480   8040  13257   2014  -1209    120       C  
ATOM   1808  CG  PHE A1006     103.442 180.725 -26.412  1.00 75.30           C  
ANISOU 1808  CG  PHE A1006     8503   7682  12427   2113  -1189    245       C  
ATOM   1809  CD1 PHE A1006     104.603 180.085 -26.008  1.00 70.58           C  
ANISOU 1809  CD1 PHE A1006     8107   7001  11709   1976   -863    322       C  
ATOM   1810  CD2 PHE A1006     103.185 180.843 -27.768  1.00 77.94           C  
ANISOU 1810  CD2 PHE A1006     9034   8130  12452   2370  -1499    279       C  
ATOM   1811  CE1 PHE A1006     105.487 179.573 -26.936  1.00 69.32           C  
ANISOU 1811  CE1 PHE A1006     8318   6866  11155   2070   -828    436       C  
ATOM   1812  CE2 PHE A1006     104.068 180.336 -28.702  1.00 78.30           C  
ANISOU 1812  CE2 PHE A1006     9476   8205  12068   2489  -1461    400       C  
ATOM   1813  CZ  PHE A1006     105.221 179.700 -28.285  1.00 74.26           C  
ANISOU 1813  CZ  PHE A1006     9144   7605  11467   2327  -1115    482       C  
ATOM   1814  N   TRP A1007     102.527 179.233 -23.063  1.00 81.58           N  
ANISOU 1814  N   TRP A1007     8645   8298  14052   1432   -662   -246       N  
ATOM   1815  CA  TRP A1007     103.176 178.150 -22.325  1.00 80.81           C  
ANISOU 1815  CA  TRP A1007     8661   8123  13920   1232   -351   -308       C  
ATOM   1816  C   TRP A1007     102.089 177.257 -21.735  1.00 86.54           C  
ANISOU 1816  C   TRP A1007     9112   8826  14945   1027   -326   -589       C  
ATOM   1817  O   TRP A1007     101.732 177.336 -20.557  1.00 85.62           O  
ANISOU 1817  O   TRP A1007     8789   8634  15110    936   -102   -634       O  
ATOM   1818  CB  TRP A1007     104.103 178.712 -21.257  1.00 77.63           C  
ANISOU 1818  CB  TRP A1007     8309   7616  13571   1245    -31   -140       C  
ATOM   1819  CG  TRP A1007     105.153 179.621 -21.821  1.00 74.69           C  
ANISOU 1819  CG  TRP A1007     8153   7223  13002   1434    -30    127       C  
ATOM   1820  CD1 TRP A1007     105.161 180.986 -21.788  1.00 70.84           C  
ANISOU 1820  CD1 TRP A1007     7564   6705  12647   1603    -84    291       C  
ATOM   1821  CD2 TRP A1007     106.340 179.230 -22.521  1.00 52.82           C  
ANISOU 1821  CD2 TRP A1007     5727   4436   9907   1477     55    267       C  
ATOM   1822  NE1 TRP A1007     106.284 181.468 -22.417  1.00 66.88           N  
ANISOU 1822  NE1 TRP A1007     7310   6150  11950   1742    -18    533       N  
ATOM   1823  CE2 TRP A1007     107.024 180.410 -22.876  1.00 52.64           C  
ANISOU 1823  CE2 TRP A1007     5783   4358   9860   1671     74    525       C  
ATOM   1824  CE3 TRP A1007     106.892 177.996 -22.878  1.00 60.08           C  
ANISOU 1824  CE3 TRP A1007     6887   5369  10574   1373    132    201       C  
ATOM   1825  CZ2 TRP A1007     108.232 180.392 -23.572  1.00 56.46           C  
ANISOU 1825  CZ2 TRP A1007     6570   4792  10091   1764    191    725       C  
ATOM   1826  CZ3 TRP A1007     108.091 177.980 -23.568  1.00 51.70           C  
ANISOU 1826  CZ3 TRP A1007     6136   4279   9229   1470    223    390       C  
ATOM   1827  CH2 TRP A1007     108.747 179.169 -23.907  1.00 51.65           C  
ANISOU 1827  CH2 TRP A1007     6194   4211   9219   1663    264    653       C  
ATOM   1828  N   ASN A1008     101.552 176.390 -22.590  1.00 94.44           N  
ANISOU 1828  N   ASN A1008    10108   9878  15896    972   -556   -786       N  
ATOM   1829  CA  ASN A1008     100.429 175.540 -22.234  1.00100.46           C  
ANISOU 1829  CA  ASN A1008    10566  10592  17011    782   -572  -1076       C  
ATOM   1830  C   ASN A1008     100.689 174.127 -22.736  1.00107.74           C  
ANISOU 1830  C   ASN A1008    11654  11492  17790    648   -575  -1236       C  
ATOM   1831  O   ASN A1008     101.493 173.905 -23.644  1.00108.63           O  
ANISOU 1831  O   ASN A1008    12093  11672  17510    747   -689  -1157       O  
ATOM   1832  CB  ASN A1008      99.117 176.093 -22.811  1.00102.62           C  
ANISOU 1832  CB  ASN A1008    10522  10938  17533    873   -964  -1245       C  
ATOM   1833  CG  ASN A1008      97.892 175.491 -22.156  1.00103.24           C  
ANISOU 1833  CG  ASN A1008    10187  10922  18118    673   -905  -1523       C  
ATOM   1834  OD1 ASN A1008      97.642 175.703 -20.970  1.00102.19           O  
ANISOU 1834  OD1 ASN A1008     9865  10698  18263    583   -592  -1483       O  
ATOM   1835  ND2 ASN A1008      97.114 174.745 -22.930  1.00106.34           N  
ANISOU 1835  ND2 ASN A1008    10429  11324  18652    623  -1204  -1815       N  
ATOM   1836  N   GLU A1009      99.995 173.166 -22.125  1.00114.49           N  
ANISOU 1836  N   GLU A1009    12278  12236  18987    428   -423  -1457       N  
ATOM   1837  CA  GLU A1009     100.209 171.763 -22.462  1.00115.64           C  
ANISOU 1837  CA  GLU A1009    12548  12322  19067    275   -385  -1624       C  
ATOM   1838  C   GLU A1009      99.510 171.363 -23.754  1.00118.04           C  
ANISOU 1838  C   GLU A1009    12772  12701  19379    328   -859  -1891       C  
ATOM   1839  O   GLU A1009      99.965 170.437 -24.437  1.00119.77           O  
ANISOU 1839  O   GLU A1009    13211  12926  19371    301   -943  -1989       O  
ATOM   1840  CB  GLU A1009      99.723 170.874 -21.317  1.00117.71           C  
ANISOU 1840  CB  GLU A1009    12592  12403  19731     31     -8  -1748       C  
ATOM   1841  CG  GLU A1009     100.184 171.326 -19.943  1.00116.81           C  
ANISOU 1841  CG  GLU A1009    12520  12219  19644     29    431  -1526       C  
ATOM   1842  CD  GLU A1009      99.174 171.015 -18.853  1.00120.93           C  
ANISOU 1842  CD  GLU A1009    12693  12589  20666   -118    723  -1640       C  
ATOM   1843  OE1 GLU A1009      98.646 169.883 -18.823  1.00124.40           O  
ANISOU 1843  OE1 GLU A1009    12994  12895  21376   -305    827  -1837       O  
ATOM   1844  OE2 GLU A1009      98.899 171.914 -18.031  1.00121.34           O  
ANISOU 1844  OE2 GLU A1009    12605  12641  20859    -37    862  -1530       O  
ATOM   1845  N   SER A1010      98.412 172.038 -24.105  1.00115.94           N  
ANISOU 1845  N   SER A1010    12196  12491  19367    424  -1189  -2032       N  
ATOM   1846  CA  SER A1010      97.589 171.591 -25.225  1.00117.58           C  
ANISOU 1846  CA  SER A1010    12265  12749  19660    485  -1671  -2361       C  
ATOM   1847  C   SER A1010      98.290 171.730 -26.569  1.00115.87           C  
ANISOU 1847  C   SER A1010    12452  12699  18873    748  -2009  -2291       C  
ATOM   1848  O   SER A1010      97.899 171.055 -27.527  1.00119.77           O  
ANISOU 1848  O   SER A1010    12948  13233  19327    809  -2378  -2578       O  
ATOM   1849  CB  SER A1010      96.269 172.363 -25.252  1.00120.78           C  
ANISOU 1849  CB  SER A1010    12241  13176  20474    558  -1959  -2529       C  
ATOM   1850  OG  SER A1010      95.477 172.056 -24.119  1.00121.23           O  
ANISOU 1850  OG  SER A1010    11892  13060  21110    313  -1656  -2649       O  
ATOM   1851  N   TYR A1011      99.313 172.579 -26.666  1.00110.54           N  
ANISOU 1851  N   TYR A1011    12116  12110  17776    922  -1884  -1927       N  
ATOM   1852  CA  TYR A1011      99.961 172.822 -27.949  1.00108.47           C  
ANISOU 1852  CA  TYR A1011    12247  11994  16973   1211  -2154  -1814       C  
ATOM   1853  C   TYR A1011     100.832 171.661 -28.411  1.00107.20           C  
ANISOU 1853  C   TYR A1011    12418  11822  16490   1154  -2074  -1857       C  
ATOM   1854  O   TYR A1011     101.445 171.763 -29.479  1.00108.81           O  
ANISOU 1854  O   TYR A1011    12986  12143  16215   1403  -2254  -1754       O  
ATOM   1855  CB  TYR A1011     100.801 174.098 -27.879  1.00103.40           C  
ANISOU 1855  CB  TYR A1011    11833  11402  16053   1403  -1989  -1397       C  
ATOM   1856  CG  TYR A1011      99.988 175.363 -27.727  1.00103.09           C  
ANISOU 1856  CG  TYR A1011    11530  11400  16240   1540  -2153  -1342       C  
ATOM   1857  CD1 TYR A1011      99.642 175.843 -26.470  1.00100.46           C  
ANISOU 1857  CD1 TYR A1011    10889  10969  16310   1373  -1889  -1294       C  
ATOM   1858  CD2 TYR A1011      99.566 176.079 -28.840  1.00106.11           C  
ANISOU 1858  CD2 TYR A1011    11990  11914  16413   1866  -2573  -1337       C  
ATOM   1859  CE1 TYR A1011      98.900 177.000 -26.325  1.00101.23           C  
ANISOU 1859  CE1 TYR A1011    10743  11099  16623   1501  -2040  -1250       C  
ATOM   1860  CE2 TYR A1011      98.822 177.239 -28.705  1.00107.40           C  
ANISOU 1860  CE2 TYR A1011    11916  12106  16786   2001  -2727  -1285       C  
ATOM   1861  CZ  TYR A1011      98.492 177.694 -27.444  1.00105.06           C  
ANISOU 1861  CZ  TYR A1011    11293  11708  16916   1804  -2460  -1245       C  
ATOM   1862  OH  TYR A1011      97.753 178.846 -27.293  1.00106.59           O  
ANISOU 1862  OH  TYR A1011    11245  11927  17329   1938  -2611  -1200       O  
ATOM   1863  N   LEU A1012     100.895 170.572 -27.655  1.00105.45           N  
ANISOU 1863  N   LEU A1012    12096  11460  16510    855  -1797  -1994       N  
ATOM   1864  CA  LEU A1012     101.729 169.429 -27.992  1.00105.03           C  
ANISOU 1864  CA  LEU A1012    12343  11379  16185    780  -1692  -2038       C  
ATOM   1865  C   LEU A1012     100.887 168.303 -28.588  1.00108.04           C  
ANISOU 1865  C   LEU A1012    12550  11725  16774    702  -2015  -2476       C  
ATOM   1866  O   LEU A1012      99.658 168.374 -28.661  1.00111.68           O  
ANISOU 1866  O   LEU A1012    12628  12166  17639    685  -2297  -2756       O  
ATOM   1867  CB  LEU A1012     102.486 168.945 -26.752  1.00101.48           C  
ANISOU 1867  CB  LEU A1012    11943  10781  15833    527  -1151  -1882       C  
ATOM   1868  CG  LEU A1012     103.526 169.918 -26.192  1.00 97.92           C  
ANISOU 1868  CG  LEU A1012    11700  10346  15159    614   -843  -1488       C  
ATOM   1869  CD1 LEU A1012     103.810 169.616 -24.730  1.00 95.73           C  
ANISOU 1869  CD1 LEU A1012    11329   9916  15127    390   -377  -1414       C  
ATOM   1870  CD2 LEU A1012     104.808 169.858 -27.009  1.00 96.49           C  
ANISOU 1870  CD2 LEU A1012    11977  10239  14446    777   -824  -1289       C  
ATOM   1871  N   THR A1013     101.577 167.252 -29.026  1.00105.05           N  
ANISOU 1871  N   THR A1013    12445  11329  16140    660  -1980  -2551       N  
ATOM   1872  CA  THR A1013     100.936 166.113 -29.669  1.00108.02           C  
ANISOU 1872  CA  THR A1013    12698  11660  16685    603  -2296  -2980       C  
ATOM   1873  C   THR A1013     101.524 164.822 -29.122  1.00107.67           C  
ANISOU 1873  C   THR A1013    12740  11450  16718    326  -1938  -3030       C  
ATOM   1874  O   THR A1013     102.747 164.686 -29.023  1.00100.98           O  
ANISOU 1874  O   THR A1013    12272  10624  15473    338  -1652  -2763       O  
ATOM   1875  CB  THR A1013     101.112 166.160 -31.192  1.00108.33           C  
ANISOU 1875  CB  THR A1013    13050  11888  16223    956  -2782  -3081       C  
ATOM   1876  OG1 THR A1013     102.496 166.365 -31.508  1.00104.93           O  
ANISOU 1876  OG1 THR A1013    13123  11547  15199   1103  -2560  -2721       O  
ATOM   1877  CG2 THR A1013     100.281 167.283 -31.799  1.00110.78           C  
ANISOU 1877  CG2 THR A1013    13228  12342  16522   1248  -3208  -3119       C  
ATOM   1878  N   GLY A1014     100.654 163.882 -28.771  1.00115.25           N  
ANISOU 1878  N   GLY A1014    13340  12231  18220     84  -1945  -3373       N  
ATOM   1879  CA  GLY A1014     101.089 162.566 -28.347  1.00118.18           C  
ANISOU 1879  CA  GLY A1014    13776  12421  18706   -166  -1639  -3459       C  
ATOM   1880  C   GLY A1014     101.402 162.493 -26.865  1.00114.76           C  
ANISOU 1880  C   GLY A1014    13278  11822  18503   -410  -1028  -3208       C  
ATOM   1881  O   GLY A1014     100.938 163.296 -26.051  1.00119.68           O  
ANISOU 1881  O   GLY A1014    13670  12422  19383   -443   -855  -3071       O  
ATOM   1882  N   SER A1015     102.205 161.493 -26.515  1.00105.73           N  
ANISOU 1882  N   SER A1015    12359  10562  17252   -558   -703  -3157       N  
ATOM   1883  CA  SER A1015     102.638 161.278 -25.143  1.00102.80           C  
ANISOU 1883  CA  SER A1015    12010  10033  17017   -743   -121  -2924       C  
ATOM   1884  C   SER A1015     104.064 161.784 -24.956  1.00 99.71           C  
ANISOU 1884  C   SER A1015    12065   9762  16060   -608    100  -2550       C  
ATOM   1885  O   SER A1015     104.804 162.002 -25.919  1.00 95.13           O  
ANISOU 1885  O   SER A1015    11798   9346  15003   -420   -131  -2480       O  
ATOM   1886  CB  SER A1015     102.549 159.797 -24.772  1.00103.76           C  
ANISOU 1886  CB  SER A1015    12067   9908  17448   -993    128  -3116       C  
ATOM   1887  OG  SER A1015     103.457 159.027 -25.539  1.00102.26           O  
ANISOU 1887  OG  SER A1015    12239   9764  16852   -947     24  -3161       O  
ATOM   1888  N   ARG A1016     104.447 161.958 -23.685  1.00101.38           N  
ANISOU 1888  N   ARG A1016    12299   9877  16344   -689    563  -2317       N  
ATOM   1889  CA  ARG A1016     105.709 162.625 -23.377  1.00 99.52           C  
ANISOU 1889  CA  ARG A1016    12407   9738  15667   -548    756  -1984       C  
ATOM   1890  C   ARG A1016     106.913 161.789 -23.786  1.00 94.77           C  
ANISOU 1890  C   ARG A1016    12202   9137  14669   -540    839  -1940       C  
ATOM   1891  O   ARG A1016     107.937 162.346 -24.198  1.00 88.82           O  
ANISOU 1891  O   ARG A1016    11744   8510  13495   -371    805  -1736       O  
ATOM   1892  CB  ARG A1016     105.781 162.966 -21.888  1.00 58.37           C  
ANISOU 1892  CB  ARG A1016     7119   4419  10639   -602   1193  -1798       C  
ATOM   1893  CG  ARG A1016     106.916 163.921 -21.541  1.00 62.24           C  
ANISOU 1893  CG  ARG A1016     7870   5007  10770   -426   1317  -1497       C  
ATOM   1894  CD  ARG A1016     106.822 164.426 -20.115  1.00 58.80           C  
ANISOU 1894  CD  ARG A1016     7326   4489  10527   -422   1662  -1358       C  
ATOM   1895  NE  ARG A1016     107.871 165.396 -19.818  1.00 56.09           N  
ANISOU 1895  NE  ARG A1016     7188   4226   9899   -241   1726  -1118       N  
ATOM   1896  CZ  ARG A1016     107.777 166.697 -20.073  1.00 59.41           C  
ANISOU 1896  CZ  ARG A1016     7516   4762  10297    -92   1533  -1008       C  
ATOM   1897  NH1 ARG A1016     106.680 167.188 -20.633  1.00 52.18           N  
ANISOU 1897  NH1 ARG A1016     6327   3913   9585    -87   1250  -1110       N  
ATOM   1898  NH2 ARG A1016     108.781 167.507 -19.768  1.00 60.39           N  
ANISOU 1898  NH2 ARG A1016     7806   4917  10222     61   1615   -809       N  
ATOM   1899  N   ASP A1017     106.821 160.463 -23.678  1.00 94.09           N  
ANISOU 1899  N   ASP A1017    12120   8895  14737   -719    966  -2123       N  
ATOM   1900  CA  ASP A1017     107.900 159.612 -24.168  1.00 92.61           C  
ANISOU 1900  CA  ASP A1017    12297   8709  14181   -709   1005  -2114       C  
ATOM   1901  C   ASP A1017     107.885 159.487 -25.684  1.00 90.24           C  
ANISOU 1901  C   ASP A1017    12109   8555  13622   -580    547  -2283       C  
ATOM   1902  O   ASP A1017     108.924 159.183 -26.280  1.00 87.86           O  
ANISOU 1902  O   ASP A1017    12161   8323  12897   -483    533  -2208       O  
ATOM   1903  CB  ASP A1017     107.822 158.224 -23.528  1.00 95.32           C  
ANISOU 1903  CB  ASP A1017    12617   8818  14780   -932   1309  -2247       C  
ATOM   1904  CG  ASP A1017     108.526 158.163 -22.187  1.00 94.76           C  
ANISOU 1904  CG  ASP A1017    12694   8638  14674   -962   1804  -2007       C  
ATOM   1905  OD1 ASP A1017     109.055 159.202 -21.740  1.00 93.29           O  
ANISOU 1905  OD1 ASP A1017    12597   8553  14294   -818   1885  -1770       O  
ATOM   1906  OD2 ASP A1017     108.553 157.070 -21.582  1.00 95.85           O  
ANISOU 1906  OD2 ASP A1017    12862   8577  14981  -1111   2105  -2064       O  
ATOM   1907  N   GLU A1018     106.735 159.720 -26.318  1.00 87.70           N  
ANISOU 1907  N   GLU A1018    11503   8281  13539   -550    169  -2518       N  
ATOM   1908  CA  GLU A1018     106.702 159.762 -27.775  1.00 86.75           C  
ANISOU 1908  CA  GLU A1018    11521   8327  13113   -347   -307  -2672       C  
ATOM   1909  C   GLU A1018     107.375 161.027 -28.297  1.00 81.20           C  
ANISOU 1909  C   GLU A1018    11066   7835  11950    -65   -406  -2374       C  
ATOM   1910  O   GLU A1018     108.051 160.994 -29.331  1.00 80.65           O  
ANISOU 1910  O   GLU A1018    11323   7896  11423    137   -586  -2336       O  
ATOM   1911  CB  GLU A1018     105.258 159.653 -28.263  1.00 92.71           C  
ANISOU 1911  CB  GLU A1018    11884   9061  14280   -367   -711  -3042       C  
ATOM   1912  CG  GLU A1018     105.103 159.174 -29.698  1.00 98.19           C  
ANISOU 1912  CG  GLU A1018    12701   9864  14742   -189  -1214  -3339       C  
ATOM   1913  CD  GLU A1018     103.658 158.877 -30.046  1.00104.18           C  
ANISOU 1913  CD  GLU A1018    13020  10550  16012   -240  -1610  -3777       C  
ATOM   1914  OE1 GLU A1018     103.231 157.715 -29.880  1.00106.46           O  
ANISOU 1914  OE1 GLU A1018    13110  10634  16706   -459  -1579  -4079       O  
ATOM   1915  OE2 GLU A1018     102.944 159.812 -30.465  1.00106.61           O  
ANISOU 1915  OE2 GLU A1018    13165  10987  16353    -58  -1945  -3824       O  
ATOM   1916  N   ARG A1019     107.227 162.145 -27.579  1.00 74.72           N  
ANISOU 1916  N   ARG A1019    10102   7036  11253    -39   -263  -2151       N  
ATOM   1917  CA  ARG A1019     107.929 163.371 -27.951  1.00 70.75           C  
ANISOU 1917  CA  ARG A1019     9814   6686  10380    209   -289  -1840       C  
ATOM   1918  C   ARG A1019     109.404 163.343 -27.566  1.00 66.15           C  
ANISOU 1918  C   ARG A1019     9565   6074   9494    220     78  -1557       C  
ATOM   1919  O   ARG A1019     110.226 163.959 -28.252  1.00 58.14           O  
ANISOU 1919  O   ARG A1019     8823   5167   8101    437     45  -1343       O  
ATOM   1920  CB  ARG A1019     107.260 164.588 -27.307  1.00 69.48           C  
ANISOU 1920  CB  ARG A1019     9367   6541  10493    236   -275  -1719       C  
ATOM   1921  CG  ARG A1019     105.860 164.884 -27.819  1.00 69.97           C  
ANISOU 1921  CG  ARG A1019     9106   6658  10820    288   -683  -1968       C  
ATOM   1922  CD  ARG A1019     105.284 166.148 -27.192  1.00 72.94           C  
ANISOU 1922  CD  ARG A1019     9221   7055  11439    331   -655  -1825       C  
ATOM   1923  NE  ARG A1019     103.941 165.918 -26.667  1.00 71.66           N  
ANISOU 1923  NE  ARG A1019     8611   6796  11821    161   -727  -2087       N  
ATOM   1924  CZ  ARG A1019     103.662 165.761 -25.377  1.00 73.56           C  
ANISOU 1924  CZ  ARG A1019     8626   6883  12440    -51   -366  -2063       C  
ATOM   1925  NH1 ARG A1019     104.634 165.823 -24.478  1.00 62.28           N  
ANISOU 1925  NH1 ARG A1019     7391   5396  10877    -98     48  -1809       N  
ATOM   1926  NH2 ARG A1019     102.413 165.549 -24.983  1.00 76.96           N  
ANISOU 1926  NH2 ARG A1019     8640   7211  13390   -193   -415  -2299       N  
ATOM   1927  N   LYS A1020     109.760 162.650 -26.482  1.00 64.63           N  
ANISOU 1927  N   LYS A1020     9358   5728   9473     11    438  -1549       N  
ATOM   1928  CA  LYS A1020     111.149 162.657 -26.031  1.00 61.94           C  
ANISOU 1928  CA  LYS A1020     9304   5350   8881     37    765  -1309       C  
ATOM   1929  C   LYS A1020     112.046 161.891 -26.994  1.00 62.68           C  
ANISOU 1929  C   LYS A1020     9748   5487   8583    109    712  -1330       C  
ATOM   1930  O   LYS A1020     113.065 162.417 -27.459  1.00 52.28           O  
ANISOU 1930  O   LYS A1020     8688   4239   6938    283    767  -1109       O  
ATOM   1931  CB  LYS A1020     111.260 162.073 -24.621  1.00 60.48           C  
ANISOU 1931  CB  LYS A1020     9038   4992   8949   -160   1142  -1312       C  
ATOM   1932  CG  LYS A1020     112.660 162.181 -24.023  1.00 47.81           C  
ANISOU 1932  CG  LYS A1020     7696   3344   7126   -105   1453  -1091       C  
ATOM   1933  CD  LYS A1020     112.757 161.521 -22.655  1.00 46.30           C  
ANISOU 1933  CD  LYS A1020     7473   2987   7131   -248   1805  -1111       C  
ATOM   1934  CE  LYS A1020     113.058 160.035 -22.769  1.00 46.80           C  
ANISOU 1934  CE  LYS A1020     7709   2949   7125   -381   1913  -1257       C  
ATOM   1935  NZ  LYS A1020     113.473 159.459 -21.459  1.00 45.69           N  
ANISOU 1935  NZ  LYS A1020     7561   2786   7014   -438   2222  -1158       N  
ATOM   1936  N   LYS A1021     111.683 160.642 -27.302  1.00 65.08           N  
ANISOU 1936  N   LYS A1021    10054   5733   8941    -18    620  -1598       N  
ATOM   1937  CA  LYS A1021     112.515 159.817 -28.173  1.00 55.84           C  
ANISOU 1937  CA  LYS A1021     9217   4596   7404     48    574  -1644       C  
ATOM   1938  C   LYS A1021     112.636 160.429 -29.562  1.00 67.86           C  
ANISOU 1938  C   LYS A1021    10929   6306   8547    335    255  -1592       C  
ATOM   1939  O   LYS A1021     113.689 160.327 -30.203  1.00 68.61           O  
ANISOU 1939  O   LYS A1021    11365   6457   8248    482    321  -1456       O  
ATOM   1940  CB  LYS A1021     111.942 158.401 -28.252  1.00 58.00           C  
ANISOU 1940  CB  LYS A1021     9408   4756   7873   -140    496  -1979       C  
ATOM   1941  CG  LYS A1021     111.859 157.698 -26.907  1.00 56.41           C  
ANISOU 1941  CG  LYS A1021     9065   4343   8024   -398    865  -2004       C  
ATOM   1942  CD  LYS A1021     111.099 156.388 -27.017  1.00 59.24           C  
ANISOU 1942  CD  LYS A1021     9273   4556   8679   -590    784  -2342       C  
ATOM   1943  CE  LYS A1021     110.803 155.803 -25.646  1.00 66.91           C  
ANISOU 1943  CE  LYS A1021    10068   5297  10057   -824   1181  -2341       C  
ATOM   1944  NZ  LYS A1021     109.868 154.645 -25.725  1.00 69.48           N  
ANISOU 1944  NZ  LYS A1021    10160   5439  10800  -1024   1118  -2672       N  
ATOM   1945  N   SER A1022     111.570 161.074 -30.042  1.00 69.01           N  
ANISOU 1945  N   SER A1022    10871   6546   8802    442    -78  -1692       N  
ATOM   1946  CA  SER A1022     111.656 161.800 -31.303  1.00 69.34           C  
ANISOU 1946  CA  SER A1022    11116   6768   8460    770   -363  -1602       C  
ATOM   1947  C   SER A1022     112.676 162.929 -31.214  1.00 67.61           C  
ANISOU 1947  C   SER A1022    11084   6584   8020    930   -106  -1190       C  
ATOM   1948  O   SER A1022     113.448 163.155 -32.154  1.00 68.36           O  
ANISOU 1948  O   SER A1022    11508   6767   7697   1176   -115  -1024       O  
ATOM   1949  CB  SER A1022     110.278 162.345 -31.685  1.00 70.80           C  
ANISOU 1949  CB  SER A1022    11018   7034   8847    860   -766  -1789       C  
ATOM   1950  OG  SER A1022     109.301 161.319 -31.661  1.00 72.95           O  
ANISOU 1950  OG  SER A1022    11046   7232   9440    685   -985  -2195       O  
ATOM   1951  N   LEU A1023     112.705 163.637 -30.080  1.00 65.41           N  
ANISOU 1951  N   LEU A1023    10595   6221   8038    806    141  -1025       N  
ATOM   1952  CA  LEU A1023     113.635 164.751 -29.914  1.00 63.88           C  
ANISOU 1952  CA  LEU A1023    10517   6024   7732    945    377   -666       C  
ATOM   1953  C   LEU A1023     115.075 164.259 -29.862  1.00 64.03           C  
ANISOU 1953  C   LEU A1023    10830   5973   7525    936    688   -523       C  
ATOM   1954  O   LEU A1023     115.966 164.840 -30.493  1.00 64.37           O  
ANISOU 1954  O   LEU A1023    11107   6046   7305   1143    790   -274       O  
ATOM   1955  CB  LEU A1023     113.289 165.530 -28.647  1.00 60.86           C  
ANISOU 1955  CB  LEU A1023     9822   5556   7745    816    538   -585       C  
ATOM   1956  CG  LEU A1023     114.028 166.841 -28.391  1.00 59.49           C  
ANISOU 1956  CG  LEU A1023     9672   5357   7574    956    727   -259       C  
ATOM   1957  CD1 LEU A1023     113.405 167.956 -29.211  1.00 62.47           C  
ANISOU 1957  CD1 LEU A1023    10002   5847   7886   1189    475   -148       C  
ATOM   1958  CD2 LEU A1023     113.999 167.171 -26.908  1.00 57.87           C  
ANISOU 1958  CD2 LEU A1023     9220   5033   7734    792    954   -239       C  
ATOM   1959  N   LEU A1024     115.322 163.190 -29.101  1.00 63.21           N  
ANISOU 1959  N   LEU A1024    10714   5761   7543    707    862   -670       N  
ATOM   1960  CA  LEU A1024     116.674 162.652 -28.984  1.00 62.97           C  
ANISOU 1960  CA  LEU A1024    10947   5656   7323    693   1145   -565       C  
ATOM   1961  C   LEU A1024     117.193 162.156 -30.328  1.00 67.27           C  
ANISOU 1961  C   LEU A1024    11825   6292   7444    869   1035   -568       C  
ATOM   1962  O   LEU A1024     118.356 162.392 -30.677  1.00 70.03           O  
ANISOU 1962  O   LEU A1024    12414   6627   7568   1002   1237   -351       O  
ATOM   1963  CB  LEU A1024     116.701 161.527 -27.949  1.00 47.74           C  
ANISOU 1963  CB  LEU A1024     8953   3594   5591    437   1323   -743       C  
ATOM   1964  CG  LEU A1024     116.566 161.917 -26.478  1.00 45.35           C  
ANISOU 1964  CG  LEU A1024     8419   3179   5634    307   1540   -696       C  
ATOM   1965  CD1 LEU A1024     116.187 160.708 -25.646  1.00 45.07           C  
ANISOU 1965  CD1 LEU A1024     8314   3024   5788     83   1662   -904       C  
ATOM   1966  CD2 LEU A1024     117.861 162.525 -25.971  1.00 45.75           C  
ANISOU 1966  CD2 LEU A1024     8586   3164   5632    395   1807   -466       C  
ATOM   1967  N   SER A1025     116.347 161.469 -31.099  1.00 67.76           N  
ANISOU 1967  N   SER A1025    11899   6438   7407    890    715   -824       N  
ATOM   1968  CA  SER A1025     116.781 160.950 -32.392  1.00 72.48           C  
ANISOU 1968  CA  SER A1025    12834   7135   7569   1094    579   -861       C  
ATOM   1969  C   SER A1025     117.181 162.059 -33.354  1.00 75.00           C  
ANISOU 1969  C   SER A1025    13361   7565   7571   1433    556   -574       C  
ATOM   1970  O   SER A1025     117.947 161.806 -34.291  1.00 76.81           O  
ANISOU 1970  O   SER A1025    13932   7849   7404   1639    600   -484       O  
ATOM   1971  CB  SER A1025     115.676 160.096 -33.015  1.00 77.30           C  
ANISOU 1971  CB  SER A1025    13378   7811   8180   1081    177  -1238       C  
ATOM   1972  OG  SER A1025     115.339 159.008 -32.173  1.00 77.48           O  
ANISOU 1972  OG  SER A1025    13217   7695   8526    768    245  -1489       O  
ATOM   1973  N   LYS A1026     116.677 163.279 -33.150  1.00 76.53           N  
ANISOU 1973  N   LYS A1026    13363   7783   7931   1511    510   -417       N  
ATOM   1974  CA  LYS A1026     117.091 164.396 -33.992  1.00 78.34           C  
ANISOU 1974  CA  LYS A1026    13786   8082   7896   1838    548   -101       C  
ATOM   1975  C   LYS A1026     118.545 164.767 -33.734  1.00 75.64           C  
ANISOU 1975  C   LYS A1026    13597   7619   7522   1859    990    218       C  
ATOM   1976  O   LYS A1026     119.263 165.165 -34.659  1.00 76.71           O  
ANISOU 1976  O   LYS A1026    14022   7783   7340   2132   1112    461       O  
ATOM   1977  CB  LYS A1026     116.176 165.598 -33.759  1.00 80.15           C  
ANISOU 1977  CB  LYS A1026    13750   8345   8360   1898    397    -21       C  
ATOM   1978  CG  LYS A1026     114.743 165.373 -34.205  1.00 85.58           C  
ANISOU 1978  CG  LYS A1026    14290   9156   9070   1944    -72   -329       C  
ATOM   1979  CD  LYS A1026     113.882 166.598 -33.947  1.00 88.05           C  
ANISOU 1979  CD  LYS A1026    14335   9495   9623   2009   -207   -239       C  
ATOM   1980  CE  LYS A1026     112.487 166.424 -34.531  1.00 92.46           C  
ANISOU 1980  CE  LYS A1026    14757  10181  10193   2106   -706   -554       C  
ATOM   1981  NZ  LYS A1026     111.620 167.610 -34.280  1.00 93.57           N  
ANISOU 1981  NZ  LYS A1026    14628  10348  10576   2175   -849   -477       N  
ATOM   1982  N   PHE A1027     118.996 164.636 -32.488  1.00 71.57           N  
ANISOU 1982  N   PHE A1027    12892   6959   7341   1595   1239    213       N  
ATOM   1983  CA  PHE A1027     120.379 164.901 -32.121  1.00 69.73           C  
ANISOU 1983  CA  PHE A1027    12753   6588   7152   1594   1629    447       C  
ATOM   1984  C   PHE A1027     121.258 163.661 -32.204  1.00 72.03           C  
ANISOU 1984  C   PHE A1027    13271   6836   7260   1512   1776    342       C  
ATOM   1985  O   PHE A1027     122.422 163.716 -31.796  1.00 72.32           O  
ANISOU 1985  O   PHE A1027    13361   6744   7372   1484   2089    482       O  
ATOM   1986  CB  PHE A1027     120.449 165.487 -30.708  1.00 64.23           C  
ANISOU 1986  CB  PHE A1027    11743   5757   6905   1406   1791    479       C  
ATOM   1987  CG  PHE A1027     119.543 166.664 -30.490  1.00 61.34           C  
ANISOU 1987  CG  PHE A1027    11123   5422   6761   1460   1647    555       C  
ATOM   1988  CD1 PHE A1027     119.762 167.859 -31.151  1.00 60.78           C  
ANISOU 1988  CD1 PHE A1027    11104   5353   6637   1703   1697    842       C  
ATOM   1989  CD2 PHE A1027     118.481 166.579 -29.605  1.00 59.61           C  
ANISOU 1989  CD2 PHE A1027    10613   5214   6822   1274   1491    352       C  
ATOM   1990  CE1 PHE A1027     118.930 168.946 -30.944  1.00 60.58           C  
ANISOU 1990  CE1 PHE A1027    10846   5349   6823   1757   1562    911       C  
ATOM   1991  CE2 PHE A1027     117.648 167.663 -29.395  1.00 59.74           C  
ANISOU 1991  CE2 PHE A1027    10389   5259   7051   1327   1359    415       C  
ATOM   1992  CZ  PHE A1027     117.873 168.847 -30.064  1.00 59.74           C  
ANISOU 1992  CZ  PHE A1027    10444   5269   6986   1566   1380    688       C  
ATOM   1993  N   GLY A1028     120.735 162.552 -32.714  1.00 77.44           N  
ANISOU 1993  N   GLY A1028    12190   6616  10619    566    501  -2552       N  
ATOM   1994  CA  GLY A1028     121.534 161.348 -32.844  1.00 79.76           C  
ANISOU 1994  CA  GLY A1028    12663   6821  10821    652    538  -2521       C  
ATOM   1995  C   GLY A1028     121.718 160.595 -31.547  1.00 79.03           C  
ANISOU 1995  C   GLY A1028    12413   6702  10911    682    119  -2437       C  
ATOM   1996  O   GLY A1028     122.785 160.009 -31.315  1.00 78.85           O  
ANISOU 1996  O   GLY A1028    12235   6668  11054    789    114  -2433       O  
ATOM   1997  N   MET A1029     120.705 160.597 -30.686  1.00 75.68           N  
ANISOU 1997  N   MET A1029    11921   6245  10590    418    130  -2398       N  
ATOM   1998  CA  MET A1029     120.745 159.909 -29.406  1.00 73.72           C  
ANISOU 1998  CA  MET A1029    11529   5943  10540    280    100  -2289       C  
ATOM   1999  C   MET A1029     119.560 158.959 -29.297  1.00 74.19           C  
ANISOU 1999  C   MET A1029    11615   5892  10684     72     41  -2421       C  
ATOM   2000  O   MET A1029     118.494 159.204 -29.872  1.00 74.21           O  
ANISOU 2000  O   MET A1029    11616   5909  10672    -26     -9  -2584       O  
ATOM   2001  CB  MET A1029     120.719 160.906 -28.239  1.00 70.72           C  
ANISOU 2001  CB  MET A1029    10889   5700  10279    187    135  -2089       C  
ATOM   2002  CG  MET A1029     121.758 162.009 -28.333  1.00 67.09           C  
ANISOU 2002  CG  MET A1029    10362   5337   9790    335    202  -1973       C  
ATOM   2003  SD  MET A1029     121.521 163.291 -27.091  1.00 62.24           S  
ANISOU 2003  SD  MET A1029     9505   4875   9267    209    240  -1771       S  
ATOM   2004  CE  MET A1029     123.015 164.250 -27.309  1.00 61.55           C  
ANISOU 2004  CE  MET A1029     9360   4839   9186    355    358  -1642       C  
ATOM   2005  N   ASP A1030     119.755 157.869 -28.559  1.00 76.45           N  
ANISOU 2005  N   ASP A1030    11850   6090  11109      1     41  -2364       N  
ATOM   2006  CA  ASP A1030     118.689 156.928 -28.266  1.00 82.64           C  
ANISOU 2006  CA  ASP A1030    12580   6770  12049   -205    -20  -2457       C  
ATOM   2007  C   ASP A1030     118.063 157.274 -26.917  1.00 78.11           C  
ANISOU 2007  C   ASP A1030    11696   6304  11677   -363     -2  -2297       C  
ATOM   2008  O   ASP A1030     118.463 158.226 -26.242  1.00 74.10           O  
ANISOU 2008  O   ASP A1030    11050   5947  11159   -318     62  -2129       O  
ATOM   2009  CB  ASP A1030     119.211 155.487 -28.298  1.00 91.10           C  
ANISOU 2009  CB  ASP A1030    13806   7648  13160   -179    -13  -2499       C  
ATOM   2010  CG  ASP A1030     120.349 155.249 -27.321  1.00 94.52           C  
ANISOU 2010  CG  ASP A1030    14126   8114  13673    -94     81  -2290       C  
ATOM   2011  OD1 ASP A1030     121.264 156.098 -27.248  1.00 94.00           O  
ANISOU 2011  OD1 ASP A1030    13996   8184  13535     46    142  -2177       O  
ATOM   2012  OD2 ASP A1030     120.335 154.208 -26.631  1.00 96.99           O  
ANISOU 2012  OD2 ASP A1030    14393   8316  14142   -179    109  -2247       O  
ATOM   2013  N   GLU A1031     117.072 156.481 -26.520  1.00 81.04           N  
ANISOU 2013  N   GLU A1031    11960   6589  12243   -544    -52  -2357       N  
ATOM   2014  CA  GLU A1031     116.259 156.815 -25.357  1.00 79.79           C  
ANISOU 2014  CA  GLU A1031    11510   6523  12283   -680    -28  -2241       C  
ATOM   2015  C   GLU A1031     117.101 156.871 -24.087  1.00 76.82           C  
ANISOU 2015  C   GLU A1031    11025   6216  11949   -632    117  -2005       C  
ATOM   2016  O   GLU A1031     118.097 156.159 -23.939  1.00 75.98           O  
ANISOU 2016  O   GLU A1031    11018   6035  11815   -556    185  -1943       O  
ATOM   2017  CB  GLU A1031     115.118 155.807 -25.214  1.00 85.09           C  
ANISOU 2017  CB  GLU A1031    12082   7057  13192   -874   -100  -2352       C  
ATOM   2018  CG  GLU A1031     115.538 154.362 -25.415  1.00 91.87           C  
ANISOU 2018  CG  GLU A1031    13115   7694  14097   -894    -93  -2408       C  
ATOM   2019  CD  GLU A1031     114.351 153.447 -25.595  1.00 98.49           C  
ANISOU 2019  CD  GLU A1031    13882   8374  15164  -1095   -202  -2566       C  
ATOM   2020  OE1 GLU A1031     113.752 153.042 -24.577  1.00100.29           O  
ANISOU 2020  OE1 GLU A1031    13892   8566  15649  -1230   -148  -2462       O  
ATOM   2021  OE2 GLU A1031     114.000 153.158 -26.758  1.00102.03           O  
ANISOU 2021  OE2 GLU A1031    14484   8737  15548  -1117   -338  -2802       O  
ATOM   2022  N   GLY A1032     116.696 157.756 -23.177  1.00 70.82           N  
ANISOU 2022  N   GLY A1032    10053   5602  11252   -665    164  -1888       N  
ATOM   2023  CA  GLY A1032     117.432 158.014 -21.950  1.00 65.09           C  
ANISOU 2023  CA  GLY A1032     9218   4970  10544   -613    297  -1685       C  
ATOM   2024  C   GLY A1032     116.896 159.222 -21.201  1.00 58.58           C  
ANISOU 2024  C   GLY A1032     8211   4304   9743   -624    318  -1607       C  
ATOM   2025  O   GLY A1032     116.205 160.056 -21.798  1.00 45.62           O  
ANISOU 2025  O   GLY A1032     6551   2720   8062   -634    228  -1697       O  
ATOM   2026  N   VAL A1033     117.193 159.332 -19.906  1.00 53.49           N  
ANISOU 2026  N   VAL A1033     7440   3721   9163   -610    434  -1454       N  
ATOM   2027  CA  VAL A1033     116.676 160.439 -19.103  1.00 48.37           C  
ANISOU 2027  CA  VAL A1033     6637   3200   8543   -605    458  -1392       C  
ATOM   2028  C   VAL A1033     117.361 161.724 -19.559  1.00 42.89           C  
ANISOU 2028  C   VAL A1033     6022   2626   7649   -497    409  -1372       C  
ATOM   2029  O   VAL A1033     118.577 161.876 -19.420  1.00 40.03           O  
ANISOU 2029  O   VAL A1033     5728   2301   7180   -412    451  -1284       O  
ATOM   2030  CB  VAL A1033     116.874 160.192 -17.601  1.00 46.83           C  
ANISOU 2030  CB  VAL A1033     6318   3018   8457   -598    601  -1250       C  
ATOM   2031  CG1 VAL A1033     118.275 159.682 -17.303  1.00 45.27           C  
ANISOU 2031  CG1 VAL A1033     6213   2812   8175   -517    674  -1154       C  
ATOM   2032  CG2 VAL A1033     116.568 161.455 -16.791  1.00 45.61           C  
ANISOU 2032  CG2 VAL A1033     6051   2987   8292   -552    621  -1194       C  
ATOM   2033  N   THR A1034     116.578 162.652 -20.105  1.00 41.26           N  
ANISOU 2033  N   THR A1034     5792   2470   7416   -504    323  -1453       N  
ATOM   2034  CA  THR A1034     117.126 163.822 -20.780  1.00 41.57           C  
ANISOU 2034  CA  THR A1034     5930   2584   7282   -409    274  -1450       C  
ATOM   2035  C   THR A1034     117.189 165.016 -19.836  1.00 39.37           C  
ANISOU 2035  C   THR A1034     5557   2416   6987   -363    301  -1350       C  
ATOM   2036  O   THR A1034     116.210 165.329 -19.150  1.00 39.57           O  
ANISOU 2036  O   THR A1034     5443   2466   7126   -401    305  -1363       O  
ATOM   2037  CB  THR A1034     116.289 164.178 -22.011  1.00 43.04           C  
ANISOU 2037  CB  THR A1034     6169   2746   7437   -422    162  -1609       C  
ATOM   2038  OG1 THR A1034     116.152 163.024 -22.847  1.00 44.44           O  
ANISOU 2038  OG1 THR A1034     6446   2806   7633   -468    120  -1731       O  
ATOM   2039  CG2 THR A1034     116.964 165.291 -22.806  1.00 41.75           C  
ANISOU 2039  CG2 THR A1034     6134   2627   7103   -308    139  -1598       C  
ATOM   2040  N   PHE A1035     118.336 165.688 -19.817  1.00 36.24           N  
ANISOU 2040  N   PHE A1035     5232   2069   6468   -280    317  -1262       N  
ATOM   2041  CA  PHE A1035     118.528 166.900 -19.037  1.00 38.45           C  
ANISOU 2041  CA  PHE A1035     5460   2434   6714   -233    318  -1183       C  
ATOM   2042  C   PHE A1035     118.760 168.074 -19.978  1.00 34.47           C  
ANISOU 2042  C   PHE A1035     5048   1946   6102   -174    258  -1200       C  
ATOM   2043  O   PHE A1035     119.467 167.945 -20.983  1.00 34.84           O  
ANISOU 2043  O   PHE A1035     5207   1950   6081   -136    256  -1214       O  
ATOM   2044  CB  PHE A1035     119.707 166.758 -18.072  1.00 37.75           C  
ANISOU 2044  CB  PHE A1035     5354   2373   6617   -200    383  -1069       C  
ATOM   2045  CG  PHE A1035     119.536 165.658 -17.060  1.00 41.19           C  
ANISOU 2045  CG  PHE A1035     5709   2778   7162   -238    464  -1038       C  
ATOM   2046  CD1 PHE A1035     120.021 164.384 -17.312  1.00 41.34           C  
ANISOU 2046  CD1 PHE A1035     5761   2725   7224   -259    520  -1037       C  
ATOM   2047  CD2 PHE A1035     118.904 165.901 -15.850  1.00 41.66           C  
ANISOU 2047  CD2 PHE A1035     5663   2859   7308   -239    502  -1014       C  
ATOM   2048  CE1 PHE A1035     119.872 163.372 -16.382  1.00 39.79           C  
ANISOU 2048  CE1 PHE A1035     5501   2480   7138   -289    607   -996       C  
ATOM   2049  CE2 PHE A1035     118.751 164.893 -14.917  1.00 41.23           C  
ANISOU 2049  CE2 PHE A1035     5535   2752   7379   -264    606   -974       C  
ATOM   2050  CZ  PHE A1035     119.236 163.627 -15.183  1.00 39.69           C  
ANISOU 2050  CZ  PHE A1035     5376   2486   7219   -294    661   -959       C  
ATOM   2051  N   MET A1036     118.167 169.219 -19.646  1.00 37.19           N  
ANISOU 2051  N   MET A1036     5349   2336   6447   -151    221  -1202       N  
ATOM   2052  CA  MET A1036     118.167 170.381 -20.527  1.00 37.65           C  
ANISOU 2052  CA  MET A1036     5488   2388   6430    -94    171  -1223       C  
ATOM   2053  C   MET A1036     118.581 171.632 -19.765  1.00 37.56           C  
ANISOU 2053  C   MET A1036     5464   2417   6391    -49    163  -1138       C  
ATOM   2054  O   MET A1036     118.044 171.921 -18.691  1.00 32.64           O  
ANISOU 2054  O   MET A1036     4757   1832   5814    -50    159  -1131       O  
ATOM   2055  CB  MET A1036     116.785 170.585 -21.155  1.00 40.41           C  
ANISOU 2055  CB  MET A1036     5806   2724   6824   -104    109  -1355       C  
ATOM   2056  CG  MET A1036     116.613 171.934 -21.816  1.00 40.82           C  
ANISOU 2056  CG  MET A1036     5919   2768   6821    -24     63  -1373       C  
ATOM   2057  SD  MET A1036     114.893 172.288 -22.210  1.00 42.70           S  
ANISOU 2057  SD  MET A1036     6054   3016   7155    -16    -36  -1540       S  
ATOM   2058  CE  MET A1036     115.036 173.969 -22.809  1.00 42.78           C  
ANISOU 2058  CE  MET A1036     6161   3003   7089    113    -67  -1515       C  
ATOM   2059  N   PHE A1037     119.534 172.370 -20.331  1.00 38.33           N  
ANISOU 2059  N   PHE A1037     5646   2485   6432     -4    163  -1082       N  
ATOM   2060  CA  PHE A1037     119.954 173.674 -19.833  1.00 37.43           C  
ANISOU 2060  CA  PHE A1037     5539   2377   6305     29    141  -1016       C  
ATOM   2061  C   PHE A1037     119.676 174.709 -20.913  1.00 38.73           C  
ANISOU 2061  C   PHE A1037     5788   2481   6447     86    115  -1038       C  
ATOM   2062  O   PHE A1037     120.027 174.499 -22.080  1.00 33.70           O  
ANISOU 2062  O   PHE A1037     5227   1782   5794    117    137  -1053       O  
ATOM   2063  CB  PHE A1037     121.443 173.667 -19.462  1.00 31.89           C  
ANISOU 2063  CB  PHE A1037     4832   1667   5617     20    172   -921       C  
ATOM   2064  CG  PHE A1037     122.006 175.025 -19.114  1.00 38.65           C  
ANISOU 2064  CG  PHE A1037     5697   2495   6493     38    143   -866       C  
ATOM   2065  CD1 PHE A1037     122.478 175.876 -20.105  1.00 37.19           C  
ANISOU 2065  CD1 PHE A1037     5576   2232   6323     65    145   -828       C  
ATOM   2066  CD2 PHE A1037     122.091 175.435 -17.792  1.00 31.67           C  
ANISOU 2066  CD2 PHE A1037     4750   1637   5647     32    119   -862       C  
ATOM   2067  CE1 PHE A1037     122.998 177.119 -19.786  1.00 34.83           C  
ANISOU 2067  CE1 PHE A1037     5282   1884   6067     66    118   -773       C  
ATOM   2068  CE2 PHE A1037     122.615 176.675 -17.467  1.00 32.04           C  
ANISOU 2068  CE2 PHE A1037     4810   1636   5726     41     80   -830       C  
ATOM   2069  CZ  PHE A1037     123.068 177.517 -18.464  1.00 33.08           C  
ANISOU 2069  CZ  PHE A1037     5007   1693   5871     47     79   -782       C  
ATOM   2070  N   ILE A1038     119.051 175.822 -20.531  1.00 38.89           N  
ANISOU 2070  N   ILE A1038     5802   2503   6471    121     76  -1045       N  
ATOM   2071  CA  ILE A1038     118.754 176.902 -21.468  1.00 39.97           C  
ANISOU 2071  CA  ILE A1038     6018   2567   6603    193     58  -1057       C  
ATOM   2072  C   ILE A1038     119.085 178.227 -20.786  1.00 39.61           C  
ANISOU 2072  C   ILE A1038     5987   2493   6570    216     37   -988       C  
ATOM   2073  O   ILE A1038     118.426 178.617 -19.815  1.00 38.78           O  
ANISOU 2073  O   ILE A1038     5832   2430   6471    228      5  -1018       O  
ATOM   2074  CB  ILE A1038     117.295 176.872 -21.963  1.00 41.22           C  
ANISOU 2074  CB  ILE A1038     6148   2736   6778    233     17  -1182       C  
ATOM   2075  CG1 ILE A1038     117.016 178.047 -22.904  1.00 35.66           C  
ANISOU 2075  CG1 ILE A1038     5526   1947   6075    341     -3  -1190       C  
ATOM   2076  CG2 ILE A1038     116.298 176.800 -20.802  1.00 34.30           C  
ANISOU 2076  CG2 ILE A1038     5145   1934   5952    216    -20  -1230       C  
ATOM   2077  CD1 ILE A1038     116.323 177.640 -24.188  1.00 36.91           C  
ANISOU 2077  CD1 ILE A1038     5716   2077   6231    404    -32  -1317       C  
ATOM   2078  N   GLY A1039     120.119 178.906 -21.274  1.00 34.23           N  
ANISOU 2078  N   GLY A1039     5367   1725   5913    226     53   -902       N  
ATOM   2079  CA  GLY A1039     120.542 180.155 -20.675  1.00 38.18           C  
ANISOU 2079  CA  GLY A1039     5883   2173   6450    229     28   -844       C  
ATOM   2080  C   GLY A1039     121.887 180.626 -21.182  1.00 40.36           C  
ANISOU 2080  C   GLY A1039     6181   2347   6807    205     52   -737       C  
ATOM   2081  O   GLY A1039     122.677 179.833 -21.704  1.00 42.31           O  
ANISOU 2081  O   GLY A1039     6401   2590   7085    179     99   -699       O  
ATOM   2082  N   ARG A1040     122.154 181.921 -21.031  1.00 43.02           N  
ANISOU 2082  N   ARG A1040     6551   2589   7206    214     27   -685       N  
ATOM   2083  CA  ARG A1040     123.406 182.495 -21.501  1.00 48.05           C  
ANISOU 2083  CA  ARG A1040     7179   3106   7973    177     52   -568       C  
ATOM   2084  C   ARG A1040     124.583 181.890 -20.745  1.00 50.46           C  
ANISOU 2084  C   ARG A1040     7367   3458   8346     81     61   -542       C  
ATOM   2085  O   ARG A1040     124.451 181.438 -19.604  1.00 50.80           O  
ANISOU 2085  O   ARG A1040     7366   3601   8335     52     24   -610       O  
ATOM   2086  CB  ARG A1040     123.381 184.018 -21.331  1.00 53.50           C  
ANISOU 2086  CB  ARG A1040     7922   3673   8734    192     12   -527       C  
ATOM   2087  CG  ARG A1040     124.408 184.766 -22.170  1.00 60.11           C  
ANISOU 2087  CG  ARG A1040     8757   4346   9736    170     52   -378       C  
ATOM   2088  CD  ARG A1040     124.018 186.222 -22.378  1.00 65.87           C  
ANISOU 2088  CD  ARG A1040     9584   4928  10514    223     21   -333       C  
ATOM   2089  NE  ARG A1040     124.148 187.009 -21.156  1.00 70.76           N  
ANISOU 2089  NE  ARG A1040    10185   5525  11174    164    -53   -391       N  
ATOM   2090  CZ  ARG A1040     125.215 187.739 -20.848  1.00 74.84           C  
ANISOU 2090  CZ  ARG A1040    10642   5924  11868     69    -78   -324       C  
ATOM   2091  NH1 ARG A1040     126.251 187.788 -21.675  1.00 77.84           N  
ANISOU 2091  NH1 ARG A1040    10956   6208  12413     15    -12   -170       N  
ATOM   2092  NH2 ARG A1040     125.244 188.422 -19.712  1.00 75.05           N  
ANISOU 2092  NH2 ARG A1040    10659   5922  11933     34   -164   -410       N  
ATOM   2093  N   PHE A1041     125.746 181.870 -21.396  1.00 52.48           N  
ANISOU 2093  N   PHE A1041     7565   3634   8742     46    126   -432       N  
ATOM   2094  CA  PHE A1041     126.959 181.315 -20.794  1.00 53.54           C  
ANISOU 2094  CA  PHE A1041     7566   3795   8981    -34    151   -396       C  
ATOM   2095  C   PHE A1041     127.651 182.434 -20.028  1.00 60.10           C  
ANISOU 2095  C   PHE A1041     8340   4541   9953   -101     83   -366       C  
ATOM   2096  O   PHE A1041     128.542 183.114 -20.539  1.00 58.24           O  
ANISOU 2096  O   PHE A1041     8044   4179   9906   -144    121   -248       O  
ATOM   2097  CB  PHE A1041     127.863 180.698 -21.856  1.00 52.65           C  
ANISOU 2097  CB  PHE A1041     7391   3634   8979    -28    288   -287       C  
ATOM   2098  CG  PHE A1041     127.269 179.490 -22.528  1.00 49.84           C  
ANISOU 2098  CG  PHE A1041     7092   3349   8495     41    348   -347       C  
ATOM   2099  CD1 PHE A1041     126.141 178.874 -22.006  1.00 46.50           C  
ANISOU 2099  CD1 PHE A1041     6728   3041   7897     60    269   -481       C  
ATOM   2100  CD2 PHE A1041     127.839 178.968 -23.677  1.00 50.22           C  
ANISOU 2100  CD2 PHE A1041     7132   3337   8611     91    503   -265       C  
ATOM   2101  CE1 PHE A1041     125.589 177.768 -22.618  1.00 44.94           C  
ANISOU 2101  CE1 PHE A1041     6577   2892   7608    108    307   -550       C  
ATOM   2102  CE2 PHE A1041     127.293 177.859 -24.294  1.00 49.13           C  
ANISOU 2102  CE2 PHE A1041     7065   3246   8357    162    550   -350       C  
ATOM   2103  CZ  PHE A1041     126.166 177.259 -23.763  1.00 46.47           C  
ANISOU 2103  CZ  PHE A1041     6780   3018   7857    160    433   -501       C  
ATOM   2104  N   ASP A1042     127.231 182.624 -18.782  1.00 69.07           N  
ANISOU 2104  N   ASP A1042     9488   5735  11019   -107    -14   -471       N  
ATOM   2105  CA  ASP A1042     127.698 183.716 -17.942  1.00 69.59           C  
ANISOU 2105  CA  ASP A1042     9521   5711  11209   -155   -108   -489       C  
ATOM   2106  C   ASP A1042     128.810 183.249 -17.008  1.00 70.23           C  
ANISOU 2106  C   ASP A1042     9458   5812  11415   -218   -151   -502       C  
ATOM   2107  O   ASP A1042     128.922 182.064 -16.683  1.00 69.48           O  
ANISOU 2107  O   ASP A1042     9318   5826  11254   -205   -116   -525       O  
ATOM   2108  CB  ASP A1042     126.542 184.298 -17.121  1.00 68.88           C  
ANISOU 2108  CB  ASP A1042     9521   5645  11004    -94   -186   -607       C  
ATOM   2109  CG  ASP A1042     125.458 184.907 -17.992  1.00 70.55           C  
ANISOU 2109  CG  ASP A1042     9872   5819  11114    -21   -151   -594       C  
ATOM   2110  OD1 ASP A1042     125.751 185.238 -19.160  1.00 72.60           O  
ANISOU 2110  OD1 ASP A1042    10156   5981  11447    -22    -98   -489       O  
ATOM   2111  OD2 ASP A1042     124.316 185.062 -17.509  1.00 71.33           O  
ANISOU 2111  OD2 ASP A1042    10026   5969  11107     52   -179   -685       O  
ATOM   2112  N   ARG A1043     129.636 184.206 -16.577  1.00 66.93           N  
ANISOU 2112  N   ARG A1043     8962   5270  11198   -283   -237   -488       N  
ATOM   2113  CA  ARG A1043     130.718 183.904 -15.645  1.00 65.59           C  
ANISOU 2113  CA  ARG A1043     8638   5093  11189   -338   -317   -512       C  
ATOM   2114  C   ARG A1043     130.209 183.751 -14.215  1.00 62.68           C  
ANISOU 2114  C   ARG A1043     8309   4797  10710   -286   -435   -666       C  
ATOM   2115  O   ARG A1043     130.687 182.883 -13.478  1.00 64.18           O  
ANISOU 2115  O   ARG A1043     8415   5049  10921   -280   -462   -702       O  
ATOM   2116  CB  ARG A1043     131.794 184.988 -15.707  1.00 70.07           C  
ANISOU 2116  CB  ARG A1043     9086   5484  12053   -433   -392   -446       C  
ATOM   2117  CG  ARG A1043     132.620 184.981 -16.987  1.00 73.55           C  
ANISOU 2117  CG  ARG A1043     9424   5846  12676   -487   -253   -257       C  
ATOM   2118  CD  ARG A1043     133.563 186.175 -17.040  1.00 78.73           C  
ANISOU 2118  CD  ARG A1043     9956   6310  13646   -591   -325   -174       C  
ATOM   2119  NE  ARG A1043     134.831 185.925 -16.361  1.00 80.84           N  
ANISOU 2119  NE  ARG A1043     9999   6544  14174   -666   -411   -163       N  
ATOM   2120  CZ  ARG A1043     135.563 186.872 -15.785  1.00 84.07           C  
ANISOU 2120  CZ  ARG A1043    10292   6803  14848   -756   -575   -178       C  
ATOM   2121  NH1 ARG A1043     136.709 186.564 -15.195  1.00 86.58           N  
ANISOU 2121  NH1 ARG A1043    10389   7090  15417   -818   -670   -168       N  
ATOM   2122  NH2 ARG A1043     135.140 188.129 -15.785  1.00 85.27           N  
ANISOU 2122  NH2 ARG A1043    10547   6823  15028   -782   -657   -210       N  
ATOM   2123  N   GLY A1044     129.243 184.572 -13.804  1.00 58.74           N  
ANISOU 2123  N   GLY A1044     7933   4280  10107   -235   -498   -754       N  
ATOM   2124  CA  GLY A1044     128.786 184.518 -12.427  1.00 57.53           C  
ANISOU 2124  CA  GLY A1044     7808   4176   9876   -168   -609   -896       C  
ATOM   2125  C   GLY A1044     127.337 184.200 -12.115  1.00 56.54           C  
ANISOU 2125  C   GLY A1044     7806   4109   9567    -64   -591   -972       C  
ATOM   2126  O   GLY A1044     126.995 183.947 -10.955  1.00 42.01           O  
ANISOU 2126  O   GLY A1044     6013   2246   7701     -1   -701  -1087       O  
ATOM   2127  N   GLN A1045     126.477 184.190 -13.136  1.00 53.88           N  
ANISOU 2127  N   GLN A1045     7520   3845   9106    -37   -461   -914       N  
ATOM   2128  CA  GLN A1045     125.030 184.337 -13.019  1.00 50.23           C  
ANISOU 2128  CA  GLN A1045     7155   3439   8493     59   -437   -975       C  
ATOM   2129  C   GLN A1045     124.287 183.042 -13.330  1.00 43.64           C  
ANISOU 2129  C   GLN A1045     6321   2742   7516     90   -328   -956       C  
ATOM   2130  O   GLN A1045     123.930 182.299 -12.412  1.00 39.52           O  
ANISOU 2130  O   GLN A1045     5789   2306   6922    136   -326  -1010       O  
ATOM   2131  CB  GLN A1045     124.537 185.462 -13.931  1.00 53.84           C  
ANISOU 2131  CB  GLN A1045     7694   3794   8970     72   -423   -940       C  
ATOM   2132  CG  GLN A1045     124.627 186.841 -13.303  1.00 59.35           C  
ANISOU 2132  CG  GLN A1045     8430   4357   9764     89   -546  -1008       C  
ATOM   2133  CD  GLN A1045     124.490 187.959 -14.318  1.00 64.94           C  
ANISOU 2133  CD  GLN A1045     9215   4921  10538     81   -520   -939       C  
ATOM   2134  OE1 GLN A1045     125.290 188.071 -15.247  1.00 67.69           O  
ANISOU 2134  OE1 GLN A1045     9541   5191  10987      1   -472   -824       O  
ATOM   2135  NE2 GLN A1045     123.475 188.795 -14.142  1.00 66.69           N  
ANISOU 2135  NE2 GLN A1045     9533   5101  10707    177   -544  -1001       N  
ATOM   2136  N   LYS A1046     124.041 182.765 -14.616  1.00 44.29           N  
ANISOU 2136  N   LYS A1046     6428   2836   7564     72   -243   -882       N  
ATOM   2137  CA  LYS A1046     123.185 181.635 -14.979  1.00 43.83           C  
ANISOU 2137  CA  LYS A1046     6377   2891   7386    102   -167   -885       C  
ATOM   2138  C   LYS A1046     123.804 180.296 -14.594  1.00 44.96           C  
ANISOU 2138  C   LYS A1046     6444   3108   7533     67   -133   -870       C  
ATOM   2139  O   LYS A1046     123.075 179.332 -14.331  1.00 43.84           O  
ANISOU 2139  O   LYS A1046     6294   3051   7312     95    -95   -898       O  
ATOM   2140  CB  LYS A1046     122.870 181.671 -16.474  1.00 43.08           C  
ANISOU 2140  CB  LYS A1046     6339   2772   7256    102   -108   -826       C  
ATOM   2141  CG  LYS A1046     121.971 182.829 -16.888  1.00 46.07           C  
ANISOU 2141  CG  LYS A1046     6813   3088   7605    166   -123   -841       C  
ATOM   2142  CD  LYS A1046     120.581 182.711 -16.279  1.00 49.12           C  
ANISOU 2142  CD  LYS A1046     7207   3553   7902    245   -131   -926       C  
ATOM   2143  CE  LYS A1046     119.639 183.765 -16.845  1.00 51.85           C  
ANISOU 2143  CE  LYS A1046     7627   3836   8238    329   -136   -940       C  
ATOM   2144  NZ  LYS A1046     120.054 185.149 -16.483  1.00 54.26           N  
ANISOU 2144  NZ  LYS A1046     7983   4019   8615    342   -183   -934       N  
ATOM   2145  N   GLY A1047     125.133 180.209 -14.567  1.00 45.93           N  
ANISOU 2145  N   GLY A1047     6503   3186   7761      8   -141   -821       N  
ATOM   2146  CA  GLY A1047     125.801 179.073 -13.962  1.00 44.16           C  
ANISOU 2146  CA  GLY A1047     6209   3015   7554     -8   -117   -813       C  
ATOM   2147  C   GLY A1047     126.009 177.871 -14.860  1.00 40.93           C  
ANISOU 2147  C   GLY A1047     5774   2653   7125    -29    -19   -756       C  
ATOM   2148  O   GLY A1047     125.886 176.729 -14.409  1.00 36.59           O  
ANISOU 2148  O   GLY A1047     5200   2167   6537    -15     20   -768       O  
ATOM   2149  N   VAL A1048     126.329 178.103 -16.133  1.00 43.36           N  
ANISOU 2149  N   VAL A1048     6098   2916   7461    -53     26   -692       N  
ATOM   2150  CA  VAL A1048     126.647 176.973 -17.000  1.00 46.74           C  
ANISOU 2150  CA  VAL A1048     6512   3371   7874    -59    117   -649       C  
ATOM   2151  C   VAL A1048     127.969 176.338 -16.584  1.00 51.05           C  
ANISOU 2151  C   VAL A1048     6964   3910   8524    -86    151   -599       C  
ATOM   2152  O   VAL A1048     128.186 175.139 -16.806  1.00 54.37           O  
ANISOU 2152  O   VAL A1048     7365   4368   8927    -75    226   -586       O  
ATOM   2153  CB  VAL A1048     126.660 177.411 -18.478  1.00 33.66           C  
ANISOU 2153  CB  VAL A1048     4924   1653   6211    -50    159   -594       C  
ATOM   2154  CG1 VAL A1048     127.892 178.252 -18.785  1.00 34.98           C  
ANISOU 2154  CG1 VAL A1048     5022   1711   6559    -90    178   -501       C  
ATOM   2155  CG2 VAL A1048     126.588 176.198 -19.390  1.00 33.38           C  
ANISOU 2155  CG2 VAL A1048     4901   1643   6140    -26    245   -594       C  
ATOM   2156  N   ASP A1049     128.867 177.114 -15.967  1.00 50.33           N  
ANISOU 2156  N   ASP A1049     6807   3758   8559   -119     93   -578       N  
ATOM   2157  CA  ASP A1049     130.138 176.557 -15.515  1.00 46.58           C  
ANISOU 2157  CA  ASP A1049     6202   3257   8240   -140    116   -539       C  
ATOM   2158  C   ASP A1049     129.934 175.541 -14.401  1.00 44.34           C  
ANISOU 2158  C   ASP A1049     5917   3043   7889   -102    105   -594       C  
ATOM   2159  O   ASP A1049     130.730 174.606 -14.259  1.00 43.33           O  
ANISOU 2159  O   ASP A1049     5708   2911   7843    -94    167   -558       O  
ATOM   2160  CB  ASP A1049     131.071 177.673 -15.044  1.00 47.88           C  
ANISOU 2160  CB  ASP A1049     6266   3320   8605   -191     21   -522       C  
ATOM   2161  CG  ASP A1049     130.440 178.550 -13.987  1.00 49.37           C  
ANISOU 2161  CG  ASP A1049     6517   3505   8737   -177   -119   -623       C  
ATOM   2162  OD1 ASP A1049     129.623 179.423 -14.350  1.00 50.32           O  
ANISOU 2162  OD1 ASP A1049     6738   3610   8772   -171   -141   -642       O  
ATOM   2163  OD2 ASP A1049     130.741 178.352 -12.791  1.00 50.09           O  
ANISOU 2163  OD2 ASP A1049     6561   3598   8873   -158   -205   -687       O  
ATOM   2164  N   VAL A1050     128.881 175.711 -13.599  1.00 43.49           N  
ANISOU 2164  N   VAL A1050     5893   2982   7651    -66     43   -671       N  
ATOM   2165  CA  VAL A1050     128.542 174.709 -12.595  1.00 42.30           C  
ANISOU 2165  CA  VAL A1050     5751   2882   7441    -17     56   -709       C  
ATOM   2166  C   VAL A1050     128.064 173.430 -13.269  1.00 41.32           C  
ANISOU 2166  C   VAL A1050     5651   2814   7236    -10    165   -681       C  
ATOM   2167  O   VAL A1050     128.423 172.321 -12.856  1.00 42.85           O  
ANISOU 2167  O   VAL A1050     5809   3015   7457     12    223   -664       O  
ATOM   2168  CB  VAL A1050     127.486 175.262 -11.620  1.00 42.78           C  
ANISOU 2168  CB  VAL A1050     5886   2961   7408     34    -16   -791       C  
ATOM   2169  CG1 VAL A1050     127.169 174.235 -10.545  1.00 42.17           C  
ANISOU 2169  CG1 VAL A1050     5813   2910   7298    101     13   -818       C  
ATOM   2170  CG2 VAL A1050     127.961 176.564 -10.995  1.00 46.19           C  
ANISOU 2170  CG2 VAL A1050     6299   3321   7929     32   -142   -841       C  
ATOM   2171  N   LEU A1051     127.249 173.563 -14.319  1.00 37.92           N  
ANISOU 2171  N   LEU A1051     5258   2400   6752    -24    193   -690       N  
ATOM   2172  CA  LEU A1051     126.766 172.387 -15.034  1.00 35.82           C  
ANISOU 2172  CA  LEU A1051     5005   2164   6443    -24    279   -690       C  
ATOM   2173  C   LEU A1051     127.896 171.690 -15.778  1.00 37.29           C  
ANISOU 2173  C   LEU A1051     5160   2319   6689    -30    362   -629       C  
ATOM   2174  O   LEU A1051     127.966 170.456 -15.795  1.00 41.47           O  
ANISOU 2174  O   LEU A1051     5684   2858   7214    -17    435   -625       O  
ATOM   2175  CB  LEU A1051     125.653 172.782 -16.002  1.00 31.46           C  
ANISOU 2175  CB  LEU A1051     4512   1621   5820    -28    266   -729       C  
ATOM   2176  CG  LEU A1051     125.147 171.662 -16.910  1.00 35.30           C  
ANISOU 2176  CG  LEU A1051     5027   2116   6271    -33    329   -751       C  
ATOM   2177  CD1 LEU A1051     124.404 170.612 -16.102  1.00 31.29           C  
ANISOU 2177  CD1 LEU A1051     4490   1641   5759    -37    354   -784       C  
ATOM   2178  CD2 LEU A1051     124.269 172.225 -18.003  1.00 31.60           C  
ANISOU 2178  CD2 LEU A1051     4634   1635   5737    -26    294   -790       C  
ATOM   2179  N   LEU A1052     128.788 172.463 -16.403  1.00 33.55           N  
ANISOU 2179  N   LEU A1052     4665   1795   6287    -45    366   -576       N  
ATOM   2180  CA  LEU A1052     129.916 171.867 -17.111  1.00 33.07           C  
ANISOU 2180  CA  LEU A1052     4543   1684   6339    -37    481   -511       C  
ATOM   2181  C   LEU A1052     130.836 171.121 -16.154  1.00 38.29           C  
ANISOU 2181  C   LEU A1052     5112   2337   7100    -23    516   -482       C  
ATOM   2182  O   LEU A1052     131.361 170.054 -16.494  1.00 36.54           O  
ANISOU 2182  O   LEU A1052     4871   2099   6914      7    630   -450       O  
ATOM   2183  CB  LEU A1052     130.689 172.944 -17.872  1.00 38.13           C  
ANISOU 2183  CB  LEU A1052     5133   2244   7111    -57    505   -441       C  
ATOM   2184  CG  LEU A1052     129.955 173.645 -19.016  1.00 38.21           C  
ANISOU 2184  CG  LEU A1052     5237   2228   7051    -49    503   -447       C  
ATOM   2185  CD1 LEU A1052     130.778 174.820 -19.505  1.00 35.46           C  
ANISOU 2185  CD1 LEU A1052     4822   1780   6870    -75    528   -353       C  
ATOM   2186  CD2 LEU A1052     129.662 172.679 -20.155  1.00 37.84           C  
ANISOU 2186  CD2 LEU A1052     5266   2174   6937      2    609   -465       C  
ATOM   2187  N   LYS A1053     131.043 171.665 -14.951  1.00 39.64           N  
ANISOU 2187  N   LYS A1053     5235   2504   7323    -31    419   -499       N  
ATOM   2188  CA  LYS A1053     131.843 170.961 -13.953  1.00 37.98           C  
ANISOU 2188  CA  LYS A1053     4944   2272   7216      0    435   -481       C  
ATOM   2189  C   LYS A1053     131.150 169.688 -13.487  1.00 37.67           C  
ANISOU 2189  C   LYS A1053     4973   2279   7061     43    486   -507       C  
ATOM   2190  O   LYS A1053     131.810 168.676 -13.229  1.00 39.86           O  
ANISOU 2190  O   LYS A1053     5209   2531   7406     82    571   -466       O  
ATOM   2191  CB  LYS A1053     132.126 171.870 -12.757  1.00 38.75           C  
ANISOU 2191  CB  LYS A1053     4989   2335   7400     -4    292   -521       C  
ATOM   2192  CG  LYS A1053     133.252 172.864 -12.958  1.00 42.95           C  
ANISOU 2192  CG  LYS A1053     5385   2780   8154    -53    236   -478       C  
ATOM   2193  CD  LYS A1053     133.657 173.477 -11.626  1.00 47.60           C  
ANISOU 2193  CD  LYS A1053     5905   3315   8865    -46     64   -542       C  
ATOM   2194  CE  LYS A1053     134.844 174.409 -11.778  1.00 51.91           C  
ANISOU 2194  CE  LYS A1053     6276   3756   9693   -113    -24   -499       C  
ATOM   2195  NZ  LYS A1053     135.352 174.882 -10.460  1.00 55.01           N  
ANISOU 2195  NZ  LYS A1053     6580   4078  10244   -100   -239   -585       N  
ATOM   2196  N   ALA A1054     129.820 169.720 -13.365  1.00 36.93           N  
ANISOU 2196  N   ALA A1054     4972   2241   6819     38    444   -564       N  
ATOM   2197  CA  ALA A1054     129.094 168.548 -12.887  1.00 37.21           C  
ANISOU 2197  CA  ALA A1054     5047   2300   6792     65    497   -578       C  
ATOM   2198  C   ALA A1054     129.116 167.415 -13.904  1.00 38.05           C  
ANISOU 2198  C   ALA A1054     5174   2397   6884     58    605   -559       C  
ATOM   2199  O   ALA A1054     129.134 166.241 -13.520  1.00 38.59           O  
ANISOU 2199  O   ALA A1054     5244   2446   6972     83    681   -541       O  
ATOM   2200  CB  ALA A1054     127.653 168.924 -12.547  1.00 37.47           C  
ANISOU 2200  CB  ALA A1054     5138   2376   6723     58    437   -636       C  
ATOM   2201  N   ILE A1055     129.105 167.742 -15.197  1.00 38.87           N  
ANISOU 2201  N   ILE A1055     5308   2499   6962     34    615   -567       N  
ATOM   2202  CA  ILE A1055     129.132 166.710 -16.227  1.00 39.96           C  
ANISOU 2202  CA  ILE A1055     5492   2607   7085     45    707   -573       C  
ATOM   2203  C   ILE A1055     130.465 165.972 -16.215  1.00 41.23           C  
ANISOU 2203  C   ILE A1055     5601   2714   7351     90    825   -507       C  
ATOM   2204  O   ILE A1055     130.515 164.761 -16.465  1.00 43.32           O  
ANISOU 2204  O   ILE A1055     5905   2944   7611    118    910   -509       O  
ATOM   2205  CB  ILE A1055     128.821 167.335 -17.600  1.00 39.24           C  
ANISOU 2205  CB  ILE A1055     5460   2504   6946     35    692   -603       C  
ATOM   2206  CG1 ILE A1055     127.347 167.743 -17.670  1.00 32.57           C  
ANISOU 2206  CG1 ILE A1055     4657   1693   6025      0    608   -679       C  
ATOM   2207  CG2 ILE A1055     129.172 166.382 -18.733  1.00 33.89           C  
ANISOU 2207  CG2 ILE A1055     4840   1764   6271     74    797   -615       C  
ATOM   2208  CD1 ILE A1055     126.995 168.557 -18.893  1.00 32.69           C  
ANISOU 2208  CD1 ILE A1055     4744   1692   5985      6    569   -707       C  
ATOM   2209  N   GLU A1056     131.559 166.672 -15.905  1.00 39.96           N  
ANISOU 2209  N   GLU A1056     5345   2531   7308    101    833   -445       N  
ATOM   2210  CA  GLU A1056     132.858 166.010 -15.822  1.00 40.85           C  
ANISOU 2210  CA  GLU A1056     5382   2586   7554    155    955   -367       C  
ATOM   2211  C   GLU A1056     132.947 165.121 -14.588  1.00 39.45           C  
ANISOU 2211  C   GLU A1056     5191   2405   7395    195    964   -352       C  
ATOM   2212  O   GLU A1056     133.584 164.060 -14.624  1.00 41.64           O  
ANISOU 2212  O   GLU A1056     5463   2637   7720    255   1084   -303       O  
ATOM   2213  CB  GLU A1056     133.980 167.048 -15.820  1.00 42.07           C  
ANISOU 2213  CB  GLU A1056     5403   2698   7885    147    953   -296       C  
ATOM   2214  CG  GLU A1056     134.070 167.851 -17.105  1.00 44.08           C  
ANISOU 2214  CG  GLU A1056     5662   2926   8160    125    995   -274       C  
ATOM   2215  CD  GLU A1056     135.501 168.126 -17.522  1.00 48.23           C  
ANISOU 2215  CD  GLU A1056     6038   3367   8918    153   1123   -147       C  
ATOM   2216  OE1 GLU A1056     136.413 167.429 -17.026  1.00 50.65           O  
ANISOU 2216  OE1 GLU A1056     6252   3640   9350    205   1202    -81       O  
ATOM   2217  OE2 GLU A1056     135.714 169.037 -18.347  1.00 49.80           O  
ANISOU 2217  OE2 GLU A1056     6203   3526   9192    130   1156    -95       O  
ATOM   2218  N   ILE A1057     132.327 165.542 -13.484  1.00 38.03           N  
ANISOU 2218  N   ILE A1057     5014   2258   7178    181    853   -387       N  
ATOM   2219  CA  ILE A1057     132.203 164.670 -12.320  1.00 38.24           C  
ANISOU 2219  CA  ILE A1057     5051   2268   7210    235    878   -369       C  
ATOM   2220  C   ILE A1057     131.456 163.397 -12.696  1.00 40.26           C  
ANISOU 2220  C   ILE A1057     5388   2517   7390    231    967   -381       C  
ATOM   2221  O   ILE A1057     131.917 162.280 -12.431  1.00 41.09           O  
ANISOU 2221  O   ILE A1057     5499   2571   7541    288   1073   -328       O  
ATOM   2222  CB  ILE A1057     131.498 165.407 -11.167  1.00 36.66           C  
ANISOU 2222  CB  ILE A1057     4862   2092   6973    238    758   -415       C  
ATOM   2223  CG1 ILE A1057     132.360 166.560 -10.647  1.00 35.89           C  
ANISOU 2223  CG1 ILE A1057     4683   1968   6987    250    649   -418       C  
ATOM   2224  CG2 ILE A1057     131.147 164.432 -10.054  1.00 36.37           C  
ANISOU 2224  CG2 ILE A1057     4856   2029   6935    309    815   -387       C  
ATOM   2225  CD1 ILE A1057     131.616 167.501  -9.724  1.00 34.52           C  
ANISOU 2225  CD1 ILE A1057     4548   1810   6759    259    513   -493       C  
ATOM   2226  N   LEU A1058     130.294 163.550 -13.336  1.00 34.32           N  
ANISOU 2226  N   LEU A1058     4698   1801   6541    166    921   -449       N  
ATOM   2227  CA  LEU A1058     129.448 162.402 -13.644  1.00 41.67           C  
ANISOU 2227  CA  LEU A1058     5693   2702   7438    145    977   -477       C  
ATOM   2228  C   LEU A1058     130.055 161.514 -14.722  1.00 41.86           C  
ANISOU 2228  C   LEU A1058     5765   2665   7475    170   1069   -475       C  
ATOM   2229  O   LEU A1058     129.819 160.301 -14.723  1.00 43.11           O  
ANISOU 2229  O   LEU A1058     5970   2757   7650    179   1139   -477       O  
ATOM   2230  CB  LEU A1058     128.062 162.874 -14.082  1.00 41.73           C  
ANISOU 2230  CB  LEU A1058     5737   2750   7369     75    891   -554       C  
ATOM   2231  CG  LEU A1058     127.229 163.633 -13.049  1.00 33.51           C  
ANISOU 2231  CG  LEU A1058     4664   1755   6315     63    823   -565       C  
ATOM   2232  CD1 LEU A1058     126.120 164.423 -13.728  1.00 33.04           C  
ANISOU 2232  CD1 LEU A1058     4620   1736   6199      7    745   -638       C  
ATOM   2233  CD2 LEU A1058     126.650 162.671 -12.027  1.00 40.00           C  
ANISOU 2233  CD2 LEU A1058     5471   2529   7200     76    907   -534       C  
ATOM   2234  N   SER A1059     130.835 162.103 -15.620  1.00 43.26           N  
ANISOU 2234  N   SER A1059     5935   2845   7658    188   1081   -470       N  
ATOM   2235  CA  SER A1059     131.423 161.391 -16.783  1.00 47.78           C  
ANISOU 2235  CA  SER A1059     6573   3349   8233    234   1179   -480       C  
ATOM   2236  C   SER A1059     132.320 160.231 -16.356  1.00 53.58           C  
ANISOU 2236  C   SER A1059     7297   4017   9043    313   1311   -408       C  
ATOM   2237  O   SER A1059     132.639 159.404 -17.195  1.00 55.48           O  
ANISOU 2237  O   SER A1059     7619   4183   9277    365   1398   -426       O  
ATOM   2238  CB  SER A1059     132.163 162.345 -17.655  1.00 47.34           C  
ANISOU 2238  CB  SER A1059     6498   3296   8194    256   1207   -463       C  
ATOM   2239  OG  SER A1059     133.233 162.930 -16.945  1.00 45.51           O  
ANISOU 2239  OG  SER A1059     6138   3080   8073    270   1226   -373       O  
ATOM   2240  N   SER A1060     132.780 160.244 -15.114  1.00 57.40           N  
ANISOU 2240  N   SER A1060     7697   4516   9597    341   1323   -330       N  
ATOM   2241  CA  SER A1060     133.626 159.188 -14.578  1.00 58.62           C  
ANISOU 2241  CA  SER A1060     7842   4606   9825    434   1445   -247       C  
ATOM   2242  C   SER A1060     132.826 158.025 -14.008  1.00 56.62           C  
ANISOU 2242  C   SER A1060     7659   4301   9553    426   1472   -257       C  
ATOM   2243  O   SER A1060     133.404 157.168 -13.331  1.00 57.68           O  
ANISOU 2243  O   SER A1060     7789   4380   9746    508   1569   -174       O  
ATOM   2244  CB  SER A1060     134.556 159.754 -13.499  1.00 59.67           C  
ANISOU 2244  CB  SER A1060     7853   4760  10060    490   1437   -154       C  
ATOM   2245  OG  SER A1060     133.830 160.136 -12.342  1.00 60.32           O  
ANISOU 2245  OG  SER A1060     7921   4877  10119    461   1338   -170       O  
ATOM   2246  N   LYS A1061     131.523 157.971 -14.268  1.00 66.44           N  
ANISOU 2246  N   LYS A1061     7225   4894  13124    445   1304    533       N  
ATOM   2247  CA  LYS A1061     130.652 156.943 -13.724  1.00 66.38           C  
ANISOU 2247  CA  LYS A1061     7414   4840  12968    425   1263    489       C  
ATOM   2248  C   LYS A1061     129.936 156.203 -14.847  1.00 63.87           C  
ANISOU 2248  C   LYS A1061     7184   4529  12554    446   1476    302       C  
ATOM   2249  O   LYS A1061     129.759 156.723 -15.952  1.00 61.69           O  
ANISOU 2249  O   LYS A1061     6906   4333  12201    456   1619    179       O  
ATOM   2250  CB  LYS A1061     129.628 157.546 -12.754  1.00 67.37           C  
ANISOU 2250  CB  LYS A1061     7741   5033  12824    316   1101    485       C  
ATOM   2251  CG  LYS A1061     130.228 157.955 -11.420  1.00 68.92           C  
ANISOU 2251  CG  LYS A1061     7953   5169  13065    299    843    674       C  
ATOM   2252  CD  LYS A1061     129.612 159.238 -10.893  1.00 66.06           C  
ANISOU 2252  CD  LYS A1061     7727   4906  12465    204    718    659       C  
ATOM   2253  CE  LYS A1061     130.309 159.687  -9.618  1.00 66.68           C  
ANISOU 2253  CE  LYS A1061     7850   4902  12584    192    431    842       C  
ATOM   2254  NZ  LYS A1061     129.862 161.036  -9.178  1.00 64.76           N  
ANISOU 2254  NZ  LYS A1061     7744   4739  12124    108    305    825       N  
ATOM   2255  N   LYS A1062     129.529 154.967 -14.549  1.00 65.41           N  
ANISOU 2255  N   LYS A1062     7483   4621  12748    455   1479    284       N  
ATOM   2256  CA  LYS A1062     128.763 154.184 -15.512  1.00 64.61           C  
ANISOU 2256  CA  LYS A1062     7488   4500  12561    460   1626    100       C  
ATOM   2257  C   LYS A1062     127.340 154.698 -15.664  1.00 60.92           C  
ANISOU 2257  C   LYS A1062     7156   4149  11844    350   1605    -51       C  
ATOM   2258  O   LYS A1062     126.709 154.444 -16.697  1.00 61.22           O  
ANISOU 2258  O   LYS A1062     7265   4202  11795    353   1696   -229       O  
ATOM   2259  CB  LYS A1062     128.744 152.710 -15.107  1.00 67.91           C  
ANISOU 2259  CB  LYS A1062     7976   4747  13080    492   1623    132       C  
ATOM   2260  CG  LYS A1062     129.425 151.795 -16.108  1.00 72.50           C  
ANISOU 2260  CG  LYS A1062     8519   5217  13811    618   1778     74       C  
ATOM   2261  CD  LYS A1062     129.204 150.335 -15.763  1.00 77.19           C  
ANISOU 2261  CD  LYS A1062     9224   5629  14475    639   1769     77       C  
ATOM   2262  CE  LYS A1062     129.883 149.423 -16.771  1.00 81.13           C  
ANISOU 2262  CE  LYS A1062     9716   6004  15108    782   1919      8       C  
ATOM   2263  NZ  LYS A1062     129.637 147.987 -16.465  1.00 83.86           N  
ANISOU 2263  NZ  LYS A1062    10192   6149  15520    803   1903      2       N  
ATOM   2264  N   GLU A1063     126.823 155.414 -14.664  1.00 57.90           N  
ANISOU 2264  N   GLU A1063     6819   3835  11345    261   1477     14       N  
ATOM   2265  CA  GLU A1063     125.503 156.019 -14.769  1.00 55.83           C  
ANISOU 2265  CA  GLU A1063     6649   3686  10876    167   1466   -119       C  
ATOM   2266  C   GLU A1063     125.467 157.166 -15.767  1.00 55.75           C  
ANISOU 2266  C   GLU A1063     6614   3810  10760    185   1502   -225       C  
ATOM   2267  O   GLU A1063     124.376 157.648 -16.091  1.00 56.37           O  
ANISOU 2267  O   GLU A1063     6762   3977  10679    130   1491   -361       O  
ATOM   2268  CB  GLU A1063     125.038 156.515 -13.398  1.00 55.97           C  
ANISOU 2268  CB  GLU A1063     6748   3725  10793     84   1343     -9       C  
ATOM   2269  CG  GLU A1063     124.696 155.406 -12.411  1.00 61.01           C  
ANISOU 2269  CG  GLU A1063     7485   4223  11472     44   1330     79       C  
ATOM   2270  CD  GLU A1063     125.922 154.717 -11.843  1.00 67.43           C  
ANISOU 2270  CD  GLU A1063     8281   4896  12445    125   1264    256       C  
ATOM   2271  OE1 GLU A1063     126.798 155.414 -11.288  1.00 68.85           O  
ANISOU 2271  OE1 GLU A1063     8427   5086  12648    160   1135    392       O  
ATOM   2272  OE2 GLU A1063     126.012 153.476 -11.958  1.00 70.89           O  
ANISOU 2272  OE2 GLU A1063     8736   5199  12999    156   1325    258       O  
ATOM   2273  N   PHE A1064     126.624 157.606 -16.265  1.00 54.88           N  
ANISOU 2273  N   PHE A1064     6401   3700  10751    264   1553   -160       N  
ATOM   2274  CA  PHE A1064     126.654 158.719 -17.207  1.00 53.95           C  
ANISOU 2274  CA  PHE A1064     6289   3685  10527    284   1610   -238       C  
ATOM   2275  C   PHE A1064     126.029 158.331 -18.542  1.00 55.05           C  
ANISOU 2275  C   PHE A1064     6541   3828  10546    325   1712   -437       C  
ATOM   2276  O   PHE A1064     125.319 159.135 -19.156  1.00 52.80           O  
ANISOU 2276  O   PHE A1064     6353   3639  10071    314   1692   -558       O  
ATOM   2277  CB  PHE A1064     128.095 159.196 -17.399  1.00 57.42           C  
ANISOU 2277  CB  PHE A1064     6570   4090  11156    351   1677   -100       C  
ATOM   2278  CG  PHE A1064     128.217 160.450 -18.213  1.00 59.29           C  
ANISOU 2278  CG  PHE A1064     6820   4409  11298    362   1749   -140       C  
ATOM   2279  CD1 PHE A1064     127.760 161.662 -17.718  1.00 59.36           C  
ANISOU 2279  CD1 PHE A1064     6876   4510  11166    291   1618   -129       C  
ATOM   2280  CD2 PHE A1064     128.801 160.421 -19.468  1.00 46.35           C  
ANISOU 2280  CD2 PHE A1064     5179   2736   9697    454   1958   -181       C  
ATOM   2281  CE1 PHE A1064     127.872 162.820 -18.464  1.00 42.70           C  
ANISOU 2281  CE1 PHE A1064     4801   2455   8969    304   1684   -157       C  
ATOM   2282  CE2 PHE A1064     128.918 161.574 -20.218  1.00 47.91           C  
ANISOU 2282  CE2 PHE A1064     5421   2986   9795    470   2046   -200       C  
ATOM   2283  CZ  PHE A1064     128.453 162.776 -19.715  1.00 44.05           C  
ANISOU 2283  CZ  PHE A1064     4970   2586   9182    392   1903   -188       C  
ATOM   2284  N   GLN A1065     126.266 157.100 -18.998  1.00 60.49           N  
ANISOU 2284  N   GLN A1065     7247   4404  11332    386   1796   -480       N  
ATOM   2285  CA  GLN A1065     125.732 156.639 -20.275  1.00 62.60           C  
ANISOU 2285  CA  GLN A1065     7665   4647  11473    444   1855   -677       C  
ATOM   2286  C   GLN A1065     124.231 156.393 -20.240  1.00 60.89           C  
ANISOU 2286  C   GLN A1065     7552   4457  11128    358   1733   -836       C  
ATOM   2287  O   GLN A1065     123.654 156.066 -21.283  1.00 60.70           O  
ANISOU 2287  O   GLN A1065     7668   4407  10990    405   1721  -1019       O  
ATOM   2288  CB  GLN A1065     126.461 155.369 -20.720  1.00 68.71           C  
ANISOU 2288  CB  GLN A1065     8445   5268  12392    545   1971   -677       C  
ATOM   2289  CG  GLN A1065     127.939 155.589 -21.009  1.00 73.70           C  
ANISOU 2289  CG  GLN A1065     8956   5865  13182    652   2134   -540       C  
ATOM   2290  CD  GLN A1065     128.175 156.682 -22.039  1.00 77.24           C  
ANISOU 2290  CD  GLN A1065     9465   6395  13486    711   2244   -585       C  
ATOM   2291  OE1 GLN A1065     127.437 156.798 -23.017  1.00 78.14           O  
ANISOU 2291  OE1 GLN A1065     9783   6540  13365    753   2233   -765       O  
ATOM   2292  NE2 GLN A1065     129.204 157.494 -21.817  1.00 78.47           N  
ANISOU 2292  NE2 GLN A1065     9451   6571  13793    720   2337   -418       N  
ATOM   2293  N   GLU A1066     123.591 156.528 -19.080  1.00 59.00           N  
ANISOU 2293  N   GLU A1066     7252   4253  10913    242   1641   -772       N  
ATOM   2294  CA  GLU A1066     122.138 156.507 -19.010  1.00 57.44           C  
ANISOU 2294  CA  GLU A1066     7101   4091  10632    150   1554   -910       C  
ATOM   2295  C   GLU A1066     121.524 157.885 -19.206  1.00 56.84           C  
ANISOU 2295  C   GLU A1066     7052   4166  10380    132   1483   -972       C  
ATOM   2296  O   GLU A1066     120.322 157.981 -19.478  1.00 58.80           O  
ANISOU 2296  O   GLU A1066     7333   4448  10560     87   1408  -1123       O  
ATOM   2297  CB  GLU A1066     121.676 155.935 -17.666  1.00 46.08           C  
ANISOU 2297  CB  GLU A1066     5601   2598   9308     43   1535   -809       C  
ATOM   2298  CG  GLU A1066     121.923 154.444 -17.492  1.00 55.12           C  
ANISOU 2298  CG  GLU A1066     6756   3571  10617     47   1584   -780       C  
ATOM   2299  CD  GLU A1066     121.365 153.914 -16.185  1.00 55.59           C  
ANISOU 2299  CD  GLU A1066     6799   3563  10759    -59   1579   -675       C  
ATOM   2300  OE1 GLU A1066     122.163 153.521 -15.308  1.00 55.68           O  
ANISOU 2300  OE1 GLU A1066     6812   3498  10848    -36   1584   -494       O  
ATOM   2301  OE2 GLU A1066     120.126 153.902 -16.030  1.00 55.48           O  
ANISOU 2301  OE2 GLU A1066     6777   3563  10741   -160   1570   -771       O  
ATOM   2302  N   MET A1067     122.319 158.942 -19.096  1.00 55.16           N  
ANISOU 2302  N   MET A1067     6816   4027  10113    170   1498   -863       N  
ATOM   2303  CA  MET A1067     121.830 160.311 -19.135  1.00 48.89           C  
ANISOU 2303  CA  MET A1067     6061   3360   9156    156   1426   -896       C  
ATOM   2304  C   MET A1067     122.056 160.937 -20.509  1.00 47.74           C  
ANISOU 2304  C   MET A1067     6033   3250   8856    264   1449   -997       C  
ATOM   2305  O   MET A1067     122.908 160.505 -21.289  1.00 48.21           O  
ANISOU 2305  O   MET A1067     6128   3243   8948    355   1557   -992       O  
ATOM   2306  CB  MET A1067     122.522 161.152 -18.058  1.00 44.90           C  
ANISOU 2306  CB  MET A1067     5486   2890   8684    123   1405   -710       C  
ATOM   2307  CG  MET A1067     122.444 160.557 -16.656  1.00 43.21           C  
ANISOU 2307  CG  MET A1067     5219   2621   8578     49   1371   -587       C  
ATOM   2308  SD  MET A1067     123.631 161.289 -15.508  1.00 43.32           S  
ANISOU 2308  SD  MET A1067     5192   2622   8647     47   1296   -356       S  
ATOM   2309  CE  MET A1067     123.215 160.438 -13.986  1.00 42.86           C  
ANISOU 2309  CE  MET A1067     5178   2477   8632    -24   1243   -247       C  
ATOM   2310  N   ARG A1068     121.266 161.968 -20.795  1.00 46.88           N  
ANISOU 2310  N   ARG A1068     6004   3238   8570    269   1355  -1088       N  
ATOM   2311  CA  ARG A1068     121.402 162.772 -22.000  1.00 40.74           C  
ANISOU 2311  CA  ARG A1068     5382   2497   7601    384   1357  -1169       C  
ATOM   2312  C   ARG A1068     121.324 164.237 -21.604  1.00 39.13           C  
ANISOU 2312  C   ARG A1068     5189   2386   7294    364   1303  -1107       C  
ATOM   2313  O   ARG A1068     120.521 164.607 -20.742  1.00 44.61           O  
ANISOU 2313  O   ARG A1068     5833   3137   7982    285   1205  -1111       O  
ATOM   2314  CB  ARG A1068     120.307 162.443 -23.022  1.00 41.85           C  
ANISOU 2314  CB  ARG A1068     5679   2633   7588    453   1242  -1393       C  
ATOM   2315  CG  ARG A1068     120.110 160.956 -23.279  1.00 44.63           C  
ANISOU 2315  CG  ARG A1068     6032   2873   8051    448   1251  -1482       C  
ATOM   2316  CD  ARG A1068     121.121 160.414 -24.276  1.00 45.82           C  
ANISOU 2316  CD  ARG A1068     6303   2934   8171    584   1373  -1492       C  
ATOM   2317  NE  ARG A1068     120.875 159.009 -24.591  1.00 48.53           N  
ANISOU 2317  NE  ARG A1068     6692   3150   8596    596   1359  -1600       N  
ATOM   2318  CZ  ARG A1068     121.489 157.991 -23.996  1.00 49.22           C  
ANISOU 2318  CZ  ARG A1068     6658   3145   8898    547   1464  -1500       C  
ATOM   2319  NH1 ARG A1068     122.392 158.220 -23.053  1.00 46.83           N  
ANISOU 2319  NH1 ARG A1068     6179   2866   8747    491   1575  -1290       N  
ATOM   2320  NH2 ARG A1068     121.204 156.744 -24.346  1.00 50.36           N  
ANISOU 2320  NH2 ARG A1068     6873   3157   9106    564   1440  -1613       N  
ATOM   2321  N   PHE A1069     122.158 165.070 -22.225  1.00 39.27           N  
ANISOU 2321  N   PHE A1069     5278   2402   7242    438   1386  -1049       N  
ATOM   2322  CA  PHE A1069     122.264 166.474 -21.847  1.00 41.62           C  
ANISOU 2322  CA  PHE A1069     5594   2753   7468    416   1347   -973       C  
ATOM   2323  C   PHE A1069     122.097 167.366 -23.067  1.00 41.03           C  
ANISOU 2323  C   PHE A1069     5723   2699   7166    538   1344  -1066       C  
ATOM   2324  O   PHE A1069     122.760 167.162 -24.090  1.00 41.83           O  
ANISOU 2324  O   PHE A1069     5911   2745   7237    635   1488  -1074       O  
ATOM   2325  CB  PHE A1069     123.603 166.761 -21.157  1.00 42.46           C  
ANISOU 2325  CB  PHE A1069     5556   2802   7776    362   1456   -762       C  
ATOM   2326  CG  PHE A1069     123.744 166.097 -19.820  1.00 37.56           C  
ANISOU 2326  CG  PHE A1069     4774   2160   7336    264   1400   -659       C  
ATOM   2327  CD1 PHE A1069     124.361 164.863 -19.706  1.00 38.70           C  
ANISOU 2327  CD1 PHE A1069     4806   2228   7669    268   1486   -605       C  
ATOM   2328  CD2 PHE A1069     123.247 166.702 -18.680  1.00 36.32           C  
ANISOU 2328  CD2 PHE A1069     4612   2047   7139    187   1260   -618       C  
ATOM   2329  CE1 PHE A1069     124.486 164.248 -18.477  1.00 38.60           C  
ANISOU 2329  CE1 PHE A1069     4684   2185   7799    198   1419   -504       C  
ATOM   2330  CE2 PHE A1069     123.369 166.094 -17.450  1.00 45.36           C  
ANISOU 2330  CE2 PHE A1069     5667   3159   8408    117   1205   -518       C  
ATOM   2331  CZ  PHE A1069     123.989 164.865 -17.347  1.00 47.12           C  
ANISOU 2331  CZ  PHE A1069     5784   3306   8813    124   1278   -457       C  
ATOM   2332  N   ILE A1070     121.208 168.349 -22.948  1.00 40.44           N  
ANISOU 2332  N   ILE A1070     5738   2698   6929    548   1191  -1134       N  
ATOM   2333  CA  ILE A1070     120.994 169.380 -23.959  1.00 41.72           C  
ANISOU 2333  CA  ILE A1070     6108   2879   6866    671   1153  -1211       C  
ATOM   2334  C   ILE A1070     121.378 170.711 -23.326  1.00 42.06           C  
ANISOU 2334  C   ILE A1070     6144   2924   6912    615   1157  -1082       C  
ATOM   2335  O   ILE A1070     120.690 171.193 -22.416  1.00 41.00           O  
ANISOU 2335  O   ILE A1070     5973   2844   6759    556   1016  -1088       O  
ATOM   2336  CB  ILE A1070     119.544 169.414 -24.461  1.00 41.11           C  
ANISOU 2336  CB  ILE A1070     6162   2863   6594    764    932  -1421       C  
ATOM   2337  CG1 ILE A1070     119.113 168.035 -24.956  1.00 43.44           C  
ANISOU 2337  CG1 ILE A1070     6466   3122   6916    795    904  -1549       C  
ATOM   2338  CG2 ILE A1070     119.398 170.434 -25.575  1.00 39.66           C  
ANISOU 2338  CG2 ILE A1070     6196   2687   6185    920    867  -1512       C  
ATOM   2339  CD1 ILE A1070     119.835 167.598 -26.203  1.00 46.89           C  
ANISOU 2339  CD1 ILE A1070     7044   3489   7283    925   1006  -1599       C  
ATOM   2340  N   ILE A1071     122.467 171.305 -23.802  1.00 43.22           N  
ANISOU 2340  N   ILE A1071     6337   2994   7089    634   1338   -961       N  
ATOM   2341  CA  ILE A1071     122.972 172.573 -23.290  1.00 46.37           C  
ANISOU 2341  CA  ILE A1071     6746   3353   7521    572   1354   -825       C  
ATOM   2342  C   ILE A1071     122.718 173.631 -24.355  1.00 50.65           C  
ANISOU 2342  C   ILE A1071     7536   3883   7824    688   1368   -881       C  
ATOM   2343  O   ILE A1071     123.362 173.632 -25.411  1.00 52.80           O  
ANISOU 2343  O   ILE A1071     7924   4087   8049    767   1584   -846       O  
ATOM   2344  CB  ILE A1071     124.459 172.486 -22.931  1.00 46.66           C  
ANISOU 2344  CB  ILE A1071     6612   3279   7837    487   1557   -614       C  
ATOM   2345  CG1 ILE A1071     124.696 171.311 -21.987  1.00 47.38           C  
ANISOU 2345  CG1 ILE A1071     6472   3381   8148    404   1523   -570       C  
ATOM   2346  CG2 ILE A1071     124.935 173.783 -22.302  1.00 37.72           C  
ANISOU 2346  CG2 ILE A1071     5480   2088   6765    401   1511   -477       C  
ATOM   2347  CD1 ILE A1071     126.124 170.842 -21.976  1.00 50.35           C  
ANISOU 2347  CD1 ILE A1071     6655   3654   8823    377   1728   -401       C  
ATOM   2348  N   ILE A1072     121.786 174.540 -24.079  1.00 51.16           N  
ANISOU 2348  N   ILE A1072     7696   4008   7736    709   1158   -962       N  
ATOM   2349  CA  ILE A1072     121.358 175.557 -25.033  1.00 51.17           C  
ANISOU 2349  CA  ILE A1072     7932   4010   7502    829   1123  -1032       C  
ATOM   2350  C   ILE A1072     121.817 176.916 -24.521  1.00 54.95           C  
ANISOU 2350  C   ILE A1072     8478   4411   7987    761   1141   -885       C  
ATOM   2351  O   ILE A1072     121.400 177.352 -23.440  1.00 52.50           O  
ANISOU 2351  O   ILE A1072     8094   4135   7720    689    965   -884       O  
ATOM   2352  CB  ILE A1072     119.837 175.532 -25.235  1.00 46.29           C  
ANISOU 2352  CB  ILE A1072     7333   3515   6742    927    848  -1268       C  
ATOM   2353  CG1 ILE A1072     119.359 174.095 -25.453  1.00 45.50           C  
ANISOU 2353  CG1 ILE A1072     7135   3461   6692    960    783  -1407       C  
ATOM   2354  CG2 ILE A1072     119.449 176.421 -26.405  1.00 47.45           C  
ANISOU 2354  CG2 ILE A1072     7706   3664   6659   1050    839  -1340       C  
ATOM   2355  CD1 ILE A1072     117.866 173.938 -25.391  1.00 45.37           C  
ANISOU 2355  CD1 ILE A1072     7074   3535   6630   1033    505  -1631       C  
ATOM   2356  N   GLY A1073     122.669 177.587 -25.287  1.00 61.54           N  
ANISOU 2356  N   GLY A1073     9478   5129   8776    785   1362   -756       N  
ATOM   2357  CA  GLY A1073     123.102 178.909 -24.885  1.00 62.81           C  
ANISOU 2357  CA  GLY A1073     9725   5188   8951    713   1365   -615       C  
ATOM   2358  C   GLY A1073     124.237 179.424 -25.743  1.00 66.19           C  
ANISOU 2358  C   GLY A1073    10296   5451   9402    718   1689   -434       C  
ATOM   2359  O   GLY A1073     124.771 178.728 -26.612  1.00 68.21           O  
ANISOU 2359  O   GLY A1073    10580   5669   9670    786   1953   -408       O  
ATOM   2360  N   LYS A1074     124.596 180.675 -25.466  1.00 59.29           N  
ANISOU 2360  N   LYS A1074     9515   4469   8543    642   1676   -303       N  
ATOM   2361  CA  LYS A1074     125.660 181.376 -26.166  1.00 59.20           C  
ANISOU 2361  CA  LYS A1074     9627   4277   8590    615   1985   -100       C  
ATOM   2362  C   LYS A1074     126.375 182.162 -25.078  1.00 57.01           C  
ANISOU 2362  C   LYS A1074     9228   3907   8527    417   1856     58       C  
ATOM   2363  O   LYS A1074     125.925 182.210 -23.932  1.00 52.71           O  
ANISOU 2363  O   LYS A1074     8659   3430   7940    368   1529    -21       O  
ATOM   2364  CB  LYS A1074     125.124 182.066 -27.434  1.00 62.66           C  
ANISOU 2364  CB  LYS A1074    10486   4687   8634    799   2075   -143       C  
ATOM   2365  CG  LYS A1074     126.146 182.842 -28.265  1.00 66.79           C  
ANISOU 2365  CG  LYS A1074    11204   5004   9169    789   2448     81       C  
ATOM   2366  CD  LYS A1074     126.930 181.943 -29.213  1.00 68.41           C  
ANISOU 2366  CD  LYS A1074    11418   5141   9434    872   2877    150       C  
ATOM   2367  CE  LYS A1074     127.920 182.754 -30.043  1.00 71.08           C  
ANISOU 2367  CE  LYS A1074    11949   5266   9794    865   3305    393       C  
ATOM   2368  NZ  LYS A1074     128.966 183.397 -29.198  1.00 71.31           N  
ANISOU 2368  NZ  LYS A1074    11630   5203  10262    602   3328    613       N  
ATOM   2369  N   GLY A1075     127.506 182.766 -25.433  1.00 59.33           N  
ANISOU 2369  N   GLY A1075     9427   4053   9063    301   2107    281       N  
ATOM   2370  CA  GLY A1075     128.095 183.812 -24.619  1.00 58.46           C  
ANISOU 2370  CA  GLY A1075     9208   3863   9143    100   1934    425       C  
ATOM   2371  C   GLY A1075     129.600 183.757 -24.474  1.00 59.80           C  
ANISOU 2371  C   GLY A1075     9044   3941   9736    -80   2116    648       C  
ATOM   2372  O   GLY A1075     130.332 183.952 -25.449  1.00 63.50           O  
ANISOU 2372  O   GLY A1075     9544   4307  10276    -62   2489    789       O  
ATOM   2373  N   ASP A1076     130.066 183.498 -23.255  1.00 59.39           N  
ANISOU 2373  N   ASP A1076     8678   3932   9955   -241   1851    680       N  
ATOM   2374  CA  ASP A1076     131.490 183.506 -22.961  1.00 62.27           C  
ANISOU 2374  CA  ASP A1076     8680   4233  10745   -414   1925    872       C  
ATOM   2375  C   ASP A1076     132.217 182.537 -23.891  1.00 63.66           C  
ANISOU 2375  C   ASP A1076     8666   4392  11128   -320   2376    950       C  
ATOM   2376  O   ASP A1076     131.819 181.368 -23.993  1.00 62.18           O  
ANISOU 2376  O   ASP A1076     8445   4284  10895   -192   2448    839       O  
ATOM   2377  CB  ASP A1076     131.721 183.124 -21.496  1.00 61.87           C  
ANISOU 2377  CB  ASP A1076     8376   4254  10880   -543   1541    851       C  
ATOM   2378  CG  ASP A1076     133.151 183.347 -21.047  1.00 66.16           C  
ANISOU 2378  CG  ASP A1076     8558   4726  11853   -725   1508   1030       C  
ATOM   2379  OD1 ASP A1076     134.068 182.745 -21.642  1.00 69.03           O  
ANISOU 2379  OD1 ASP A1076     8637   5066  12526   -701   1822   1142       O  
ATOM   2380  OD2 ASP A1076     133.356 184.131 -20.095  1.00 66.98           O  
ANISOU 2380  OD2 ASP A1076     8669   4788  11991   -881   1170   1050       O  
ATOM   2381  N   PRO A1077     133.257 182.984 -24.599  1.00 59.60           N  
ANISOU 2381  N   PRO A1077     7176   4367  11103   -274    575   1892       N  
ATOM   2382  CA  PRO A1077     133.930 182.080 -25.544  1.00 50.50           C  
ANISOU 2382  CA  PRO A1077     6111   3281   9796   -279    763   2051       C  
ATOM   2383  C   PRO A1077     134.608 180.900 -24.869  1.00 64.58           C  
ANISOU 2383  C   PRO A1077     7891   5160  11487   -300    819   1844       C  
ATOM   2384  O   PRO A1077     134.651 179.813 -25.460  1.00 67.20           O  
ANISOU 2384  O   PRO A1077     8328   5560  11645   -294    943   1871       O  
ATOM   2385  CB  PRO A1077     134.948 182.992 -26.245  1.00 56.98           C  
ANISOU 2385  CB  PRO A1077     6816   4026  10809   -292    881   2333       C  
ATOM   2386  CG  PRO A1077     134.466 184.391 -25.986  1.00 58.31           C  
ANISOU 2386  CG  PRO A1077     6876   4064  11215   -282    746   2378       C  
ATOM   2387  CD  PRO A1077     133.813 184.345 -24.641  1.00 52.75           C  
ANISOU 2387  CD  PRO A1077     6134   3372  10538   -284    566   2036       C  
ATOM   2388  N   GLU A1078     135.137 181.076 -23.654  1.00 59.84           N  
ANISOU 2388  N   GLU A1078     7156   4563  11017   -315    739   1653       N  
ATOM   2389  CA  GLU A1078     135.790 179.969 -22.960  1.00 59.08           C  
ANISOU 2389  CA  GLU A1078     7045   4557  10845   -320    781   1490       C  
ATOM   2390  C   GLU A1078     134.799 178.853 -22.657  1.00 57.28           C  
ANISOU 2390  C   GLU A1078     6962   4419  10382   -305    738   1322       C  
ATOM   2391  O   GLU A1078     135.035 177.688 -22.999  1.00 56.48           O  
ANISOU 2391  O   GLU A1078     6929   4375  10156   -300    852   1309       O  
ATOM   2392  CB  GLU A1078     136.447 180.459 -21.667  1.00 60.00           C  
ANISOU 2392  CB  GLU A1078     6979   4658  11160   -328    688   1347       C  
ATOM   2393  CG  GLU A1078     137.636 181.388 -21.855  1.00 65.92           C  
ANISOU 2393  CG  GLU A1078     7544   5305  12196   -344    749   1481       C  
ATOM   2394  CD  GLU A1078     137.226 182.809 -22.187  1.00 73.23           C  
ANISOU 2394  CD  GLU A1078     8399   6107  13317   -351    688   1598       C  
ATOM   2395  OE1 GLU A1078     137.308 183.191 -23.373  1.00 77.34           O  
ANISOU 2395  OE1 GLU A1078     8961   6573  13853   -354    794   1846       O  
ATOM   2396  OE2 GLU A1078     136.811 183.541 -21.264  1.00 74.81           O  
ANISOU 2396  OE2 GLU A1078     8492   6262  13671   -349    540   1453       O  
ATOM   2397  N   LEU A1079     133.677 179.196 -22.014  1.00 57.18           N  
ANISOU 2397  N   LEU A1079     6980   4411  10337   -296    586   1187       N  
ATOM   2398  CA  LEU A1079     132.680 178.189 -21.667  1.00 56.30           C  
ANISOU 2398  CA  LEU A1079     6988   4376  10028   -284    547   1024       C  
ATOM   2399  C   LEU A1079     132.106 177.526 -22.913  1.00 58.18           C  
ANISOU 2399  C   LEU A1079     7370   4600  10137   -274    641   1121       C  
ATOM   2400  O   LEU A1079     131.786 176.331 -22.896  1.00 60.51           O  
ANISOU 2400  O   LEU A1079     7739   4949  10305   -271    694   1013       O  
ATOM   2401  CB  LEU A1079     131.573 178.822 -20.822  1.00 38.96           C  
ANISOU 2401  CB  LEU A1079     4775   2178   7851   -275    384    880       C  
ATOM   2402  CG  LEU A1079     132.020 179.377 -19.467  1.00 38.66           C  
ANISOU 2402  CG  LEU A1079     4578   2154   7955   -281    297    757       C  
ATOM   2403  CD1 LEU A1079     130.961 180.286 -18.857  1.00 38.72           C  
ANISOU 2403  CD1 LEU A1079     4533   2132   8046   -270    155    646       C  
ATOM   2404  CD2 LEU A1079     132.358 178.241 -18.516  1.00 49.22           C  
ANISOU 2404  CD2 LEU A1079     5918   3594   9189   -279    320    632       C  
ATOM   2405  N   GLU A1080     131.973 178.281 -24.007  1.00 57.48           N  
ANISOU 2405  N   GLU A1080     7308   4430  10102   -265    675   1339       N  
ATOM   2406  CA  GLU A1080     131.595 177.677 -25.280  1.00 58.91           C  
ANISOU 2406  CA  GLU A1080     7609   4595  10181   -246    803   1486       C  
ATOM   2407  C   GLU A1080     132.568 176.570 -25.665  1.00 58.04           C  
ANISOU 2407  C   GLU A1080     7498   4533  10020   -258   1011   1503       C  
ATOM   2408  O   GLU A1080     132.160 175.447 -25.980  1.00 58.27           O  
ANISOU 2408  O   GLU A1080     7609   4578   9954   -248   1112   1414       O  
ATOM   2409  CB  GLU A1080     131.547 178.737 -26.382  1.00 65.83           C  
ANISOU 2409  CB  GLU A1080     8493   5401  11117   -222    831   1805       C  
ATOM   2410  CG  GLU A1080     130.381 179.704 -26.321  1.00 72.07           C  
ANISOU 2410  CG  GLU A1080     9297   6121  11966   -186    648   1826       C  
ATOM   2411  CD  GLU A1080     130.333 180.606 -27.542  1.00 80.80           C  
ANISOU 2411  CD  GLU A1080    10417   7179  13103   -141    689   2207       C  
ATOM   2412  OE1 GLU A1080     129.595 180.281 -28.496  1.00 83.79           O  
ANISOU 2412  OE1 GLU A1080    10909   7577  13351    -79    725   2388       O  
ATOM   2413  OE2 GLU A1080     131.054 181.626 -27.557  1.00 84.76           O  
ANISOU 2413  OE2 GLU A1080    10809   7636  13762   -157    697   2350       O  
ATOM   2414  N   GLY A1081     133.869 176.877 -25.645  1.00 56.01           N  
ANISOU 2414  N   GLY A1081     7134   4284   9862   -275   1094   1601       N  
ATOM   2415  CA  GLY A1081     134.865 175.878 -25.997  1.00 54.42           C  
ANISOU 2415  CA  GLY A1081     6910   4122   9646   -278   1303   1614       C  
ATOM   2416  C   GLY A1081     134.853 174.688 -25.059  1.00 51.97           C  
ANISOU 2416  C   GLY A1081     6590   3864   9291   -274   1278   1352       C  
ATOM   2417  O   GLY A1081     135.105 173.555 -25.476  1.00 52.41           O  
ANISOU 2417  O   GLY A1081     6673   3932   9309   -263   1456   1309       O  
ATOM   2418  N   TRP A1082     134.562 174.928 -23.779  1.00 48.73           N  
ANISOU 2418  N   TRP A1082     6137   3487   8890   -277   1081   1187       N  
ATOM   2419  CA  TRP A1082     134.422 173.833 -22.826  1.00 44.65           C  
ANISOU 2419  CA  TRP A1082     5617   3040   8309   -266   1049    988       C  
ATOM   2420  C   TRP A1082     133.207 172.974 -23.157  1.00 44.36           C  
ANISOU 2420  C   TRP A1082     5697   3005   8151   -259   1069    879       C  
ATOM   2421  O   TRP A1082     133.262 171.744 -23.051  1.00 37.14           O  
ANISOU 2421  O   TRP A1082     4788   2118   7207   -247   1166    773       O  
ATOM   2422  CB  TRP A1082     134.334 174.401 -21.406  1.00 42.52           C  
ANISOU 2422  CB  TRP A1082     5277   2809   8069   -268    865    882       C  
ATOM   2423  CG  TRP A1082     134.461 173.394 -20.291  1.00 39.30           C  
ANISOU 2423  CG  TRP A1082     4839   2474   7619   -252    847    750       C  
ATOM   2424  CD1 TRP A1082     134.506 172.035 -20.406  1.00 37.39           C  
ANISOU 2424  CD1 TRP A1082     4625   2262   7321   -235    956    700       C  
ATOM   2425  CD2 TRP A1082     134.562 173.679 -18.889  1.00 38.97           C  
ANISOU 2425  CD2 TRP A1082     4718   2467   7620   -247    727    671       C  
ATOM   2426  NE1 TRP A1082     134.624 171.458 -19.165  1.00 37.05           N  
ANISOU 2426  NE1 TRP A1082     4533   2271   7272   -218    904    623       N  
ATOM   2427  CE2 TRP A1082     134.662 172.445 -18.217  1.00 36.32           C  
ANISOU 2427  CE2 TRP A1082     4380   2184   7235   -226    767    609       C  
ATOM   2428  CE3 TRP A1082     134.576 174.859 -18.137  1.00 40.85           C  
ANISOU 2428  CE3 TRP A1082     4871   2683   7967   -257    602    648       C  
ATOM   2429  CZ2 TRP A1082     134.775 172.356 -16.830  1.00 33.74           C  
ANISOU 2429  CZ2 TRP A1082     3985   1886   6948   -214    689    554       C  
ATOM   2430  CZ3 TRP A1082     134.688 174.768 -16.759  1.00 41.25           C  
ANISOU 2430  CZ3 TRP A1082     4841   2764   8070   -246    524    559       C  
ATOM   2431  CH2 TRP A1082     134.786 173.525 -16.121  1.00 34.02           C  
ANISOU 2431  CH2 TRP A1082     3941   1898   7088   -226    568    525       C  
ATOM   2432  N   ALA A1083     132.106 173.602 -23.582  1.00 46.02           N  
ANISOU 2432  N   ALA A1083     5989   3172   8324   -262    986    899       N  
ATOM   2433  CA  ALA A1083     130.898 172.845 -23.900  1.00 44.00           C  
ANISOU 2433  CA  ALA A1083     5829   2897   7991   -254   1002    772       C  
ATOM   2434  C   ALA A1083     131.057 172.060 -25.196  1.00 45.00           C  
ANISOU 2434  C   ALA A1083     6020   2954   8124   -246   1254    824       C  
ATOM   2435  O   ALA A1083     130.595 170.918 -25.295  1.00 38.66           O  
ANISOU 2435  O   ALA A1083     5253   2138   7296   -244   1354    643       O  
ATOM   2436  CB  ALA A1083     129.695 173.782 -23.985  1.00 37.67           C  
ANISOU 2436  CB  ALA A1083     5083   2048   7181   -247    841    778       C  
ATOM   2437  N   ARG A1084     131.697 172.658 -26.205  1.00 49.10           N  
ANISOU 2437  N   ARG A1084     6552   3427   8675   -241   1389   1070       N  
ATOM   2438  CA  ARG A1084     131.978 171.931 -27.438  1.00 54.30           C  
ANISOU 2438  CA  ARG A1084     7291   4031   9310   -233   1708   1149       C  
ATOM   2439  C   ARG A1084     133.034 170.849 -27.239  1.00 60.93           C  
ANISOU 2439  C   ARG A1084     8055   4896  10200   -243   1882   1033       C  
ATOM   2440  O   ARG A1084     133.082 169.894 -28.023  1.00 63.57           O  
ANISOU 2440  O   ARG A1084     8455   5185  10513   -246   2154    949       O  
ATOM   2441  CB  ARG A1084     132.424 172.899 -28.538  1.00 53.50           C  
ANISOU 2441  CB  ARG A1084     7220   3937   9170   -219   1833   1525       C  
ATOM   2442  CG  ARG A1084     131.357 173.892 -28.983  1.00 52.34           C  
ANISOU 2442  CG  ARG A1084     7136   3842   8907   -172   1652   1664       C  
ATOM   2443  CD  ARG A1084     130.149 173.196 -29.598  1.00 52.37           C  
ANISOU 2443  CD  ARG A1084     7223   4098   8576   -110   1581   1391       C  
ATOM   2444  NE  ARG A1084     129.155 174.157 -30.070  1.00 54.79           N  
ANISOU 2444  NE  ARG A1084     7571   4497   8751    -43   1381   1530       N  
ATOM   2445  CZ  ARG A1084     127.970 173.826 -30.571  1.00 56.68           C  
ANISOU 2445  CZ  ARG A1084     7862   4950   8724     21   1257   1318       C  
ATOM   2446  NH1 ARG A1084     127.619 172.551 -30.668  1.00 56.34           N  
ANISOU 2446  NH1 ARG A1084     7832   5037   8539     16   1322    937       N  
ATOM   2447  NH2 ARG A1084     127.132 174.772 -30.974  1.00 58.86           N  
ANISOU 2447  NH2 ARG A1084     8159   5296   8908     94   1064   1481       N  
ATOM   2448  N   SER A1085     133.883 170.982 -26.213  1.00 60.56           N  
ANISOU 2448  N   SER A1085     7874   4922  10214   -242   1743   1009       N  
ATOM   2449  CA  SER A1085     134.868 169.947 -25.915  1.00 41.29           C  
ANISOU 2449  CA  SER A1085     5345   2497   7846   -229   1879    916       C  
ATOM   2450  C   SER A1085     134.214 168.730 -25.273  1.00 57.94           C  
ANISOU 2450  C   SER A1085     7459   4620   9937   -218   1850    668       C  
ATOM   2451  O   SER A1085     134.612 167.592 -25.545  1.00 64.32           O  
ANISOU 2451  O   SER A1085     8238   5388  10811   -206   2050    561       O  
ATOM   2452  CB  SER A1085     135.960 170.507 -25.005  1.00 40.78           C  
ANISOU 2452  CB  SER A1085     5143   2490   7861   -222   1747    985       C  
ATOM   2453  OG  SER A1085     137.056 169.616 -24.909  1.00 56.62           O  
ANISOU 2453  OG  SER A1085     7054   4490   9969   -197   1905    951       O  
ATOM   2454  N   LEU A1086     133.215 168.949 -24.415  1.00 50.92           N  
ANISOU 2454  N   LEU A1086     6592   3786   8970   -225   1616    577       N  
ATOM   2455  CA  LEU A1086     132.459 167.828 -23.868  1.00 48.27           C  
ANISOU 2455  CA  LEU A1086     6256   3477   8607   -221   1599    378       C  
ATOM   2456  C   LEU A1086     131.521 167.237 -24.909  1.00 49.98           C  
ANISOU 2456  C   LEU A1086     6569   3603   8820   -235   1751    224       C  
ATOM   2457  O   LEU A1086     131.215 166.040 -24.860  1.00 51.99           O  
ANISOU 2457  O   LEU A1086     6797   3849   9107   -236   1843     36       O  
ATOM   2458  CB  LEU A1086     131.675 168.273 -22.633  1.00 44.17           C  
ANISOU 2458  CB  LEU A1086     5734   3045   8002   -227   1342    343       C  
ATOM   2459  CG  LEU A1086     132.478 168.457 -21.342  1.00 42.60           C  
ANISOU 2459  CG  LEU A1086     5447   2924   7815   -213   1231    405       C  
ATOM   2460  CD1 LEU A1086     131.807 169.478 -20.443  1.00 40.34           C  
ANISOU 2460  CD1 LEU A1086     5181   2684   7461   -227   1018    401       C  
ATOM   2461  CD2 LEU A1086     132.617 167.128 -20.623  1.00 42.77           C  
ANISOU 2461  CD2 LEU A1086     5412   2974   7864   -191   1294    335       C  
ATOM   2462  N   GLU A1087     131.063 168.057 -25.860  1.00 51.24           N  
ANISOU 2462  N   GLU A1087     6837   3682   8951   -245   1788    296       N  
ATOM   2463  CA  GLU A1087     130.203 167.556 -26.927  1.00 53.78           C  
ANISOU 2463  CA  GLU A1087     7283   3882   9268   -252   1963    106       C  
ATOM   2464  C   GLU A1087     130.960 166.607 -27.851  1.00 54.50           C  
ANISOU 2464  C   GLU A1087     7338   4096   9274   -230   2204    -15       C  
ATOM   2465  O   GLU A1087     130.412 165.584 -28.278  1.00 54.17           O  
ANISOU 2465  O   GLU A1087     7282   4132   9167   -219   2273   -332       O  
ATOM   2466  CB  GLU A1087     129.623 168.730 -27.715  1.00 56.98           C  
ANISOU 2466  CB  GLU A1087     7750   4468   9432   -214   1818    249       C  
ATOM   2467  CG  GLU A1087     128.491 168.359 -28.654  1.00 61.17           C  
ANISOU 2467  CG  GLU A1087     8320   5246   9675   -168   1762     -5       C  
ATOM   2468  CD  GLU A1087     128.163 169.477 -29.620  1.00 65.38           C  
ANISOU 2468  CD  GLU A1087     8905   6009   9928   -104   1648    205       C  
ATOM   2469  OE1 GLU A1087     129.099 169.991 -30.268  1.00 67.76           O  
ANISOU 2469  OE1 GLU A1087     9208   6409  10130    -83   1760    476       O  
ATOM   2470  OE2 GLU A1087     126.975 169.849 -29.725  1.00 66.56           O  
ANISOU 2470  OE2 GLU A1087     9082   6235   9971    -70   1451    117       O  
ATOM   2471  N   GLU A1088     132.218 166.927 -28.175  1.00 53.77           N  
ANISOU 2471  N   GLU A1088     7208   4022   9202   -225   2342    209       N  
ATOM   2472  CA  GLU A1088     133.005 166.042 -29.031  1.00 54.83           C  
ANISOU 2472  CA  GLU A1088     7287   4281   9266   -201   2587     80       C  
ATOM   2473  C   GLU A1088     133.344 164.740 -28.318  1.00 52.54           C  
ANISOU 2473  C   GLU A1088     6916   3771   9275   -217   2707   -122       C  
ATOM   2474  O   GLU A1088     133.375 163.674 -28.943  1.00 46.53           O  
ANISOU 2474  O   GLU A1088     6106   3084   8488   -196   2866   -404       O  
ATOM   2475  CB  GLU A1088     134.289 166.737 -29.485  1.00 59.33           C  
ANISOU 2475  CB  GLU A1088     7817   4909   9818   -198   2719    385       C  
ATOM   2476  CG  GLU A1088     134.086 167.977 -30.338  1.00 64.34           C  
ANISOU 2476  CG  GLU A1088     8515   5763  10169   -174   2652    641       C  
ATOM   2477  CD  GLU A1088     135.401 168.605 -30.770  1.00 67.64           C  
ANISOU 2477  CD  GLU A1088     8871   6214  10616   -184   2822    957       C  
ATOM   2478  OE1 GLU A1088     136.312 167.856 -31.183  1.00 68.92           O  
ANISOU 2478  OE1 GLU A1088     8956   6437  10793   -177   3056    868       O  
ATOM   2479  OE2 GLU A1088     135.528 169.845 -30.686  1.00 67.88           O  
ANISOU 2479  OE2 GLU A1088     8912   6191  10690   -200   2731   1287       O  
ATOM   2480  N   LYS A1089     133.605 164.806 -27.012  1.00 50.44           N  
ANISOU 2480  N   LYS A1089     6573   3428   9165   -224   2546      9       N  
ATOM   2481  CA  LYS A1089     134.054 163.622 -26.289  1.00 49.68           C  
ANISOU 2481  CA  LYS A1089     6330   3368   9178   -202   2554    -91       C  
ATOM   2482  C   LYS A1089     132.912 162.636 -26.081  1.00 50.49           C  
ANISOU 2482  C   LYS A1089     6420   3488   9275   -220   2504   -341       C  
ATOM   2483  O   LYS A1089     133.049 161.442 -26.371  1.00 52.89           O  
ANISOU 2483  O   LYS A1089     6645   3749   9701   -224   2663   -533       O  
ATOM   2484  CB  LYS A1089     134.668 164.028 -24.948  1.00 47.38           C  
ANISOU 2484  CB  LYS A1089     5938   3194   8870   -170   2320    111       C  
ATOM   2485  CG  LYS A1089     135.350 162.893 -24.199  1.00 48.21           C  
ANISOU 2485  CG  LYS A1089     5904   3310   9106   -136   2357     87       C  
ATOM   2486  CD  LYS A1089     135.992 163.404 -22.921  1.00 47.95           C  
ANISOU 2486  CD  LYS A1089     5802   3369   9047   -103   2149    260       C  
ATOM   2487  CE  LYS A1089     136.687 162.290 -22.159  1.00 51.36           C  
ANISOU 2487  CE  LYS A1089     6105   3787   9621    -61   2196    270       C  
ATOM   2488  NZ  LYS A1089     137.393 162.798 -20.950  1.00 52.87           N  
ANISOU 2488  NZ  LYS A1089     6236   4047   9805    -30   2022    420       N  
ATOM   2489  N   HIS A1090     131.778 163.116 -25.582  1.00 49.87           N  
ANISOU 2489  N   HIS A1090     6397   3478   9072   -235   2282   -345       N  
ATOM   2490  CA  HIS A1090     130.657 162.259 -25.229  1.00 47.90           C  
ANISOU 2490  CA  HIS A1090     6114   3267   8820   -257   2211   -537       C  
ATOM   2491  C   HIS A1090     129.562 162.348 -26.285  1.00 47.17           C  
ANISOU 2491  C   HIS A1090     6118   3140   8664   -280   2251   -803       C  
ATOM   2492  O   HIS A1090     129.247 163.433 -26.781  1.00 46.88           O  
ANISOU 2492  O   HIS A1090     6207   3072   8531   -272   2208   -760       O  
ATOM   2493  CB  HIS A1090     130.097 162.639 -23.856  1.00 47.65           C  
ANISOU 2493  CB  HIS A1090     6065   3341   8698   -250   1957   -397       C  
ATOM   2494  CG  HIS A1090     131.136 162.720 -22.778  1.00 49.76           C  
ANISOU 2494  CG  HIS A1090     6260   3661   8986   -212   1891   -188       C  
ATOM   2495  ND1 HIS A1090     131.641 161.605 -22.143  1.00 51.33           N  
ANISOU 2495  ND1 HIS A1090     6351   3850   9302   -189   1965   -174       N  
ATOM   2496  CD2 HIS A1090     131.760 163.786 -22.219  1.00 49.97           C  
ANISOU 2496  CD2 HIS A1090     6299   3743   8946   -193   1755     -7       C  
ATOM   2497  CE1 HIS A1090     132.532 161.981 -21.242  1.00 51.01           C  
ANISOU 2497  CE1 HIS A1090     6272   3857   9254   -152   1878      2       C  
ATOM   2498  NE2 HIS A1090     132.623 163.299 -21.267  1.00 50.05           N  
ANISOU 2498  NE2 HIS A1090     6216   3781   9020   -159   1748     88       N  
ATOM   2499  N   GLY A1091     128.985 161.197 -26.624  1.00 47.60           N  
ANISOU 2499  N   GLY A1091     6101   3207   8778   -301   2322  -1086       N  
ATOM   2500  CA  GLY A1091     127.885 161.133 -27.562  1.00 49.50           C  
ANISOU 2500  CA  GLY A1091     6392   3489   8926   -306   2318  -1423       C  
ATOM   2501  C   GLY A1091     126.524 161.458 -26.993  1.00 50.13           C  
ANISOU 2501  C   GLY A1091     6483   3633   8931   -327   2087  -1440       C  
ATOM   2502  O   GLY A1091     125.547 161.509 -27.744  1.00 52.38           O  
ANISOU 2502  O   GLY A1091     6798   3982   9121   -321   2045  -1728       O  
ATOM   2503  N   ASN A1092     126.424 161.673 -25.681  1.00 48.29           N  
ANISOU 2503  N   ASN A1092     6215   3421   8710   -336   1937  -1175       N  
ATOM   2504  CA  ASN A1092     125.165 162.032 -25.042  1.00 44.96           C  
ANISOU 2504  CA  ASN A1092     5802   3064   8218   -350   1740  -1182       C  
ATOM   2505  C   ASN A1092     125.130 163.491 -24.607  1.00 43.24           C  
ANISOU 2505  C   ASN A1092     5681   2857   7892   -328   1570   -969       C  
ATOM   2506  O   ASN A1092     124.260 163.875 -23.815  1.00 41.11           O  
ANISOU 2506  O   ASN A1092     5405   2644   7568   -334   1405   -930       O  
ATOM   2507  CB  ASN A1092     124.891 161.112 -23.849  1.00 42.00           C  
ANISOU 2507  CB  ASN A1092     5310   2721   7925   -366   1724  -1106       C  
ATOM   2508  CG  ASN A1092     126.050 161.058 -22.878  1.00 39.96           C  
ANISOU 2508  CG  ASN A1092     5022   2462   7700   -336   1749   -840       C  
ATOM   2509  OD1 ASN A1092     127.213 161.129 -23.274  1.00 41.59           O  
ANISOU 2509  OD1 ASN A1092     5233   2628   7940   -315   1846   -765       O  
ATOM   2510  ND2 ASN A1092     125.738 160.927 -21.595  1.00 38.43           N  
ANISOU 2510  ND2 ASN A1092     4791   2313   7498   -329   1670   -715       N  
ATOM   2511  N   VAL A1093     126.052 164.310 -25.106  1.00 44.53           N  
ANISOU 2511  N   VAL A1093     5921   2958   8042   -307   1622   -828       N  
ATOM   2512  CA  VAL A1093     126.055 165.751 -24.879  1.00 44.26           C  
ANISOU 2512  CA  VAL A1093     5961   2913   7945   -291   1466   -621       C  
ATOM   2513  C   VAL A1093     125.799 166.441 -26.211  1.00 46.65           C  
ANISOU 2513  C   VAL A1093     6391   3095   8239   -273   1543   -702       C  
ATOM   2514  O   VAL A1093     126.438 166.116 -27.219  1.00 48.06           O  
ANISOU 2514  O   VAL A1093     6592   3328   8340   -249   1716   -747       O  
ATOM   2515  CB  VAL A1093     127.379 166.230 -24.259  1.00 36.73           C  
ANISOU 2515  CB  VAL A1093     4973   1983   6999   -276   1455   -341       C  
ATOM   2516  CG1 VAL A1093     127.437 167.752 -24.243  1.00 36.35           C  
ANISOU 2516  CG1 VAL A1093     4980   1919   6912   -267   1306   -147       C  
ATOM   2517  CG2 VAL A1093     127.537 165.678 -22.854  1.00 35.31           C  
ANISOU 2517  CG2 VAL A1093     4699   1909   6806   -273   1372   -288       C  
ATOM   2518  N   LYS A1094     124.863 167.387 -26.213  1.00 46.74           N  
ANISOU 2518  N   LYS A1094     6454   3086   8221   -261   1368   -693       N  
ATOM   2519  CA  LYS A1094     124.533 168.183 -27.387  1.00 47.07           C  
ANISOU 2519  CA  LYS A1094     6539   3369   7977   -190   1260   -630       C  
ATOM   2520  C   LYS A1094     124.467 169.643 -26.974  1.00 46.47           C  
ANISOU 2520  C   LYS A1094     6487   3218   7950   -173   1078   -334       C  
ATOM   2521  O   LYS A1094     123.802 169.980 -25.988  1.00 45.72           O  
ANISOU 2521  O   LYS A1094     6371   2969   8033   -203    949   -377       O  
ATOM   2522  CB  LYS A1094     123.201 167.742 -28.004  1.00 49.02           C  
ANISOU 2522  CB  LYS A1094     6765   3795   8065   -161   1160   -968       C  
ATOM   2523  CG  LYS A1094     122.735 168.592 -29.178  1.00 52.94           C  
ANISOU 2523  CG  LYS A1094     7296   4590   8228    -64   1005   -885       C  
ATOM   2524  CD  LYS A1094     123.532 168.296 -30.441  1.00 56.78           C  
ANISOU 2524  CD  LYS A1094     7801   5352   8422    -10   1154   -853       C  
ATOM   2525  CE  LYS A1094     123.067 169.169 -31.602  1.00 60.56           C  
ANISOU 2525  CE  LYS A1094     8315   6168   8526    103    998   -716       C  
ATOM   2526  NZ  LYS A1094     123.808 168.888 -32.864  1.00 64.43           N  
ANISOU 2526  NZ  LYS A1094     8818   6992   8671    164   1153   -686       N  
ATOM   2527  N   VAL A1095     125.154 170.503 -27.721  1.00 47.94           N  
ANISOU 2527  N   VAL A1095     6703   3508   8002   -127   1082    -39       N  
ATOM   2528  CA  VAL A1095     125.212 171.932 -27.436  1.00 47.78           C  
ANISOU 2528  CA  VAL A1095     6685   3385   8085   -110    930    266       C  
ATOM   2529  C   VAL A1095     124.588 172.684 -28.604  1.00 52.17           C  
ANISOU 2529  C   VAL A1095     7274   4177   8370    -14    800    389       C  
ATOM   2530  O   VAL A1095     124.955 172.457 -29.764  1.00 55.21           O  
ANISOU 2530  O   VAL A1095     7691   4820   8468     39    904    452       O  
ATOM   2531  CB  VAL A1095     126.655 172.405 -27.185  1.00 46.18           C  
ANISOU 2531  CB  VAL A1095     6461   3043   8044   -144   1055    571       C  
ATOM   2532  CG1 VAL A1095     126.672 173.889 -26.850  1.00 46.93           C  
ANISOU 2532  CG1 VAL A1095     6527   2987   8318   -135    896    849       C  
ATOM   2533  CG2 VAL A1095     127.292 171.593 -26.070  1.00 42.96           C  
ANISOU 2533  CG2 VAL A1095     5997   2517   7810   -211   1139    444       C  
ATOM   2534  N   ILE A1096     123.649 173.575 -28.296  1.00 53.06           N  
ANISOU 2534  N   ILE A1096     7372   4220   8570     18    574    424       N  
ATOM   2535  CA  ILE A1096     122.957 174.385 -29.292  1.00 56.85           C  
ANISOU 2535  CA  ILE A1096     7869   4899   8831    127    411    575       C  
ATOM   2536  C   ILE A1096     123.291 175.842 -29.014  1.00 58.19           C  
ANISOU 2536  C   ILE A1096     8012   4862   9235    143    312    958       C  
ATOM   2537  O   ILE A1096     122.986 176.358 -27.931  1.00 55.50           O  
ANISOU 2537  O   ILE A1096     7616   4257   9214    100    196    908       O  
ATOM   2538  CB  ILE A1096     121.438 174.153 -29.263  1.00 55.58           C  
ANISOU 2538  CB  ILE A1096     7684   4830   8606    168    214    258       C  
ATOM   2539  CG1 ILE A1096     121.120 172.692 -29.590  1.00 46.22           C  
ANISOU 2539  CG1 ILE A1096     6496   3826   7238    144    323   -144       C  
ATOM   2540  CG2 ILE A1096     120.735 175.093 -30.233  1.00 48.96           C  
ANISOU 2540  CG2 ILE A1096     6849   4190   7563    300     14    453       C  
ATOM   2541  CD1 ILE A1096     119.745 172.250 -29.147  1.00 48.96           C  
ANISOU 2541  CD1 ILE A1096     6785   4156   7660    132    180   -522       C  
ATOM   2542  N   THR A1097     123.923 176.503 -29.985  1.00 62.19           N  
ANISOU 2542  N   THR A1097     8543   5490   9598    203    368   1334       N  
ATOM   2543  CA  THR A1097     124.319 177.897 -29.838  1.00 64.41           C  
ANISOU 2543  CA  THR A1097     8778   5548  10145    216    302   1733       C  
ATOM   2544  C   THR A1097     123.489 178.858 -30.677  1.00 69.74           C  
ANISOU 2544  C   THR A1097     9454   6346  10698    348    110   1982       C  
ATOM   2545  O   THR A1097     123.568 180.072 -30.456  1.00 67.97           O  
ANISOU 2545  O   THR A1097     9169   5880  10776    365     16   2281       O  
ATOM   2546  CB  THR A1097     125.803 178.069 -30.199  1.00 65.50           C  
ANISOU 2546  CB  THR A1097     8914   5659  10313    174    538   2058       C  
ATOM   2547  OG1 THR A1097     126.089 177.365 -31.413  1.00 67.98           O  
ANISOU 2547  OG1 THR A1097     9296   6350  10185    227    696   2088       O  
ATOM   2548  CG2 THR A1097     126.690 177.542 -29.080  1.00 48.35           C  
ANISOU 2548  CG2 THR A1097     6699   3250   8423     50    669   1894       C  
ATOM   2549  N   GLU A1098     122.701 178.358 -31.625  1.00 76.28           N  
ANISOU 2549  N   GLU A1098    10331   7537  11113    446     43   1860       N  
ATOM   2550  CA  GLU A1098     121.908 179.227 -32.478  1.00 79.95           C  
ANISOU 2550  CA  GLU A1098    10792   8165  11420    595   -155   2117       C  
ATOM   2551  C   GLU A1098     120.685 179.750 -31.732  1.00 80.33           C  
ANISOU 2551  C   GLU A1098    10770   8007  11746    622   -428   1937       C  
ATOM   2552  O   GLU A1098     120.299 179.240 -30.679  1.00 79.15           O  
ANISOU 2552  O   GLU A1098    10587   7680  11808    532   -456   1550       O  
ATOM   2553  CB  GLU A1098     121.475 178.493 -33.748  1.00 83.53           C  
ANISOU 2553  CB  GLU A1098    11304   9130  11305    703   -155   2010       C  
ATOM   2554  CG  GLU A1098     122.570 178.368 -34.788  1.00 88.40           C  
ANISOU 2554  CG  GLU A1098    11976  10023  11590    729     83   2316       C  
ATOM   2555  CD  GLU A1098     122.019 178.229 -36.192  1.00 94.72           C  
ANISOU 2555  CD  GLU A1098    12811  11361  11818    892      8   2378       C  
ATOM   2556  OE1 GLU A1098     122.216 177.161 -36.809  1.00 96.30           O  
ANISOU 2556  OE1 GLU A1098    13041  11912  11638    893    144   2097       O  
ATOM   2557  OE2 GLU A1098     121.382 179.189 -36.677  1.00 98.07           O  
ANISOU 2557  OE2 GLU A1098    13220  11863  12178   1027   -193   2697       O  
ATOM   2558  N   MET A1099     120.078 180.791 -32.299  1.00 82.02           N  
ANISOU 2558  N   MET A1099    10950   8250  11962    757   -622   2242       N  
ATOM   2559  CA  MET A1099     118.892 181.395 -31.707  1.00 81.56           C  
ANISOU 2559  CA  MET A1099    10805   8003  12182    806   -890   2096       C  
ATOM   2560  C   MET A1099     117.692 180.478 -31.909  1.00 79.73           C  
ANISOU 2560  C   MET A1099    10573   8057  11664    852  -1025   1641       C  
ATOM   2561  O   MET A1099     117.423 180.034 -33.029  1.00 81.84           O  
ANISOU 2561  O   MET A1099    10886   8736  11474    954  -1049   1647       O  
ATOM   2562  CB  MET A1099     118.630 182.762 -32.334  1.00 88.08           C  
ANISOU 2562  CB  MET A1099    11581   8769  13116    952  -1055   2589       C  
ATOM   2563  CG  MET A1099     117.436 183.501 -31.753  1.00 91.82           C  
ANISOU 2563  CG  MET A1099    11940   9017  13931   1018  -1337   2461       C  
ATOM   2564  SD  MET A1099     117.811 184.314 -30.188  1.00 92.04           S  
ANISOU 2564  SD  MET A1099    11848   8451  14672    883  -1329   2385       S  
ATOM   2565  CE  MET A1099     116.271 185.170 -29.866  1.00 93.72           C  
ANISOU 2565  CE  MET A1099    11916   8504  15191   1008  -1670   2252       C  
ATOM   2566  N   LEU A1100     116.972 180.189 -30.829  1.00 78.89           N  
ANISOU 2566  N   LEU A1100    10400   7749  11824    777  -1108   1232       N  
ATOM   2567  CA  LEU A1100     115.870 179.237 -30.864  1.00 79.64           C  
ANISOU 2567  CA  LEU A1100    10470   8058  11730    787  -1202    757       C  
ATOM   2568  C   LEU A1100     114.528 179.956 -30.875  1.00 81.43           C  
ANISOU 2568  C   LEU A1100    10592   8267  12081    907  -1503    697       C  
ATOM   2569  O   LEU A1100     114.359 180.991 -30.224  1.00 86.16           O  
ANISOU 2569  O   LEU A1100    11115   8549  13072    918  -1613    840       O  
ATOM   2570  CB  LEU A1100     115.931 178.282 -29.671  1.00 51.94           C  
ANISOU 2570  CB  LEU A1100     6950   4368   8417    619  -1059    337       C  
ATOM   2571  CG  LEU A1100     117.025 177.218 -29.708  1.00 54.05           C  
ANISOU 2571  CG  LEU A1100     7303   4706   8529    513   -776    275       C  
ATOM   2572  CD1 LEU A1100     116.706 176.130 -28.706  1.00 51.58           C  
ANISOU 2572  CD1 LEU A1100     6959   4283   8356    385   -680   -170       C  
ATOM   2573  CD2 LEU A1100     117.172 176.639 -31.107  1.00 56.52           C  
ANISOU 2573  CD2 LEU A1100     7676   5432   8368    596   -724    304       C  
ATOM   2574  N   SER A1101     113.575 179.397 -31.618  1.00 77.12           N  
ANISOU 2574  N   SER A1101    10020   8062  11218    999  -1639    455       N  
ATOM   2575  CA  SER A1101     112.249 179.988 -31.700  1.00 78.76           C  
ANISOU 2575  CA  SER A1101    10110   8291  11524   1125  -1938    366       C  
ATOM   2576  C   SER A1101     111.458 179.707 -30.429  1.00 75.14           C  
ANISOU 2576  C   SER A1101     9548   7571  11432   1015  -1972    -83       C  
ATOM   2577  O   SER A1101     111.716 178.737 -29.709  1.00 73.88           O  
ANISOU 2577  O   SER A1101     9413   7339  11321    858  -1778   -398       O  
ATOM   2578  CB  SER A1101     111.489 179.447 -32.912  1.00 82.09           C  
ANISOU 2578  CB  SER A1101    10517   9198  11477   1263  -2086    218       C  
ATOM   2579  OG  SER A1101     112.261 179.570 -34.095  1.00 85.67           O  
ANISOU 2579  OG  SER A1101    11071   9964  11518   1361  -2021    605       O  
ATOM   2580  N   ARG A1102     110.487 180.581 -30.156  1.00 75.05           N  
ANISOU 2580  N   ARG A1102     9411   7420  11686   1107  -2214    -93       N  
ATOM   2581  CA  ARG A1102     109.644 180.430 -28.975  1.00 71.94           C  
ANISOU 2581  CA  ARG A1102     8895   6803  11635   1018  -2253   -511       C  
ATOM   2582  C   ARG A1102     108.965 179.065 -28.958  1.00 67.70           C  
ANISOU 2582  C   ARG A1102     8329   6482  10911    943  -2195  -1017       C  
ATOM   2583  O   ARG A1102     108.939 178.383 -27.927  1.00 63.71           O  
ANISOU 2583  O   ARG A1102     7804   5820  10584    786  -2032  -1326       O  
ATOM   2584  CB  ARG A1102     108.611 181.559 -28.947  1.00 77.90           C  
ANISOU 2584  CB  ARG A1102     9498   7439  12661   1163  -2545   -454       C  
ATOM   2585  CG  ARG A1102     107.975 181.846 -27.597  1.00 79.26           C  
ANISOU 2585  CG  ARG A1102     9532   7298  13286   1080  -2571   -771       C  
ATOM   2586  CD  ARG A1102     106.860 182.873 -27.766  1.00 84.63           C  
ANISOU 2586  CD  ARG A1102    10042   7906  14208   1248  -2877   -745       C  
ATOM   2587  NE  ARG A1102     106.230 183.247 -26.504  1.00 84.69           N  
ANISOU 2587  NE  ARG A1102     9895   7625  14660   1183  -2904  -1058       N  
ATOM   2588  CZ  ARG A1102     105.218 184.103 -26.401  1.00 87.70           C  
ANISOU 2588  CZ  ARG A1102    10093   7887  15341   1307  -3147  -1126       C  
ATOM   2589  NH1 ARG A1102     104.713 184.676 -27.486  1.00 90.88           N  
ANISOU 2589  NH1 ARG A1102    10451   8429  15652   1513  -3399   -871       N  
ATOM   2590  NH2 ARG A1102     104.707 184.385 -25.211  1.00 87.60           N  
ANISOU 2590  NH2 ARG A1102     9935   7637  15713   1234  -3136  -1447       N  
ATOM   2591  N   GLU A1103     108.425 178.641 -30.105  1.00 68.41           N  
ANISOU 2591  N   GLU A1103     8406   6943  10644   1057  -2322  -1101       N  
ATOM   2592  CA  GLU A1103     107.748 177.350 -30.175  1.00 66.92           C  
ANISOU 2592  CA  GLU A1103     8158   6951  10318    987  -2277  -1612       C  
ATOM   2593  C   GLU A1103     108.727 176.190 -30.041  1.00 64.23           C  
ANISOU 2593  C   GLU A1103     7931   6629   9843    832  -1964  -1721       C  
ATOM   2594  O   GLU A1103     108.337 175.100 -29.605  1.00 63.12           O  
ANISOU 2594  O   GLU A1103     7735   6477   9771    712  -1844  -2142       O  
ATOM   2595  CB  GLU A1103     106.966 177.230 -31.486  1.00 70.62           C  
ANISOU 2595  CB  GLU A1103     8562   7844  10427   1160  -2514  -1700       C  
ATOM   2596  CG  GLU A1103     105.988 178.367 -31.768  1.00 73.31           C  
ANISOU 2596  CG  GLU A1103     8778   8202  10874   1348  -2852  -1556       C  
ATOM   2597  CD  GLU A1103     106.654 179.574 -32.408  1.00 76.37           C  
ANISOU 2597  CD  GLU A1103     9253   8596  11168   1502  -2944   -929       C  
ATOM   2598  OE1 GLU A1103     106.787 180.613 -31.729  1.00 75.91           O  
ANISOU 2598  OE1 GLU A1103     9171   8180  11493   1507  -2979   -671       O  
ATOM   2599  OE2 GLU A1103     107.051 179.481 -33.590  1.00 79.71           O  
ANISOU 2599  OE2 GLU A1103     9757   9385  11145   1616  -2971   -698       O  
ATOM   2600  N   PHE A1104     109.993 176.401 -30.408  1.00 62.00           N  
ANISOU 2600  N   PHE A1104     7794   6359   9403    833  -1822  -1340       N  
ATOM   2601  CA  PHE A1104     110.981 175.331 -30.310  1.00 58.39           C  
ANISOU 2601  CA  PHE A1104     7434   5912   8840    700  -1527  -1427       C  
ATOM   2602  C   PHE A1104     111.305 175.020 -28.853  1.00 54.49           C  
ANISOU 2602  C   PHE A1104     6938   5052   8712    526  -1337  -1542       C  
ATOM   2603  O   PHE A1104     111.349 173.851 -28.452  1.00 52.59           O  
ANISOU 2603  O   PHE A1104     6689   4785   8508    404  -1152  -1848       O  
ATOM   2604  CB  PHE A1104     112.245 175.713 -31.079  1.00 60.03           C  
ANISOU 2604  CB  PHE A1104     7777   6232   8799    753  -1424   -979       C  
ATOM   2605  CG  PHE A1104     113.157 174.553 -31.358  1.00 60.93           C  
ANISOU 2605  CG  PHE A1104     7970   6465   8717    661  -1155  -1101       C  
ATOM   2606  CD1 PHE A1104     113.045 173.835 -32.537  1.00 65.94           C  
ANISOU 2606  CD1 PHE A1104     8604   7502   8948    732  -1157  -1276       C  
ATOM   2607  CD2 PHE A1104     114.127 174.181 -30.442  1.00 56.98           C  
ANISOU 2607  CD2 PHE A1104     7527   5684   8440    514   -909  -1058       C  
ATOM   2608  CE1 PHE A1104     113.882 172.770 -32.795  1.00 66.51           C  
ANISOU 2608  CE1 PHE A1104     8726   7666   8878    652   -905  -1421       C  
ATOM   2609  CE2 PHE A1104     114.965 173.117 -30.694  1.00 57.49           C  
ANISOU 2609  CE2 PHE A1104     7646   5833   8365    441   -666  -1167       C  
ATOM   2610  CZ  PHE A1104     114.844 172.411 -31.871  1.00 62.46           C  
ANISOU 2610  CZ  PHE A1104     8270   6836   8627    507   -656  -1356       C  
ATOM   2611  N   VAL A1105     111.536 176.058 -28.045  1.00 54.94           N  
ANISOU 2611  N   VAL A1105     6991   4830   9053    518  -1380  -1300       N  
ATOM   2612  CA  VAL A1105     111.754 175.861 -26.616  1.00 52.81           C  
ANISOU 2612  CA  VAL A1105     6701   4264   9099    373  -1232  -1422       C  
ATOM   2613  C   VAL A1105     110.523 175.242 -25.972  1.00 55.53           C  
ANISOU 2613  C   VAL A1105     6918   4586   9593    314  -1262  -1864       C  
ATOM   2614  O   VAL A1105     110.636 174.457 -25.021  1.00 56.06           O  
ANISOU 2614  O   VAL A1105     6972   4568   9760    177  -1057  -2022       O  
ATOM   2615  CB  VAL A1105     112.138 177.194 -25.946  1.00 50.17           C  
ANISOU 2615  CB  VAL A1105     6352   3669   9042    393  -1309  -1131       C  
ATOM   2616  CG1 VAL A1105     112.653 176.957 -24.538  1.00 42.98           C  
ANISOU 2616  CG1 VAL A1105     5436   2518   8376    250  -1136  -1222       C  
ATOM   2617  CG2 VAL A1105     113.178 177.928 -26.782  1.00 47.22           C  
ANISOU 2617  CG2 VAL A1105     6072   3326   8544    470  -1308   -669       C  
ATOM   2618  N   ARG A1106     109.332 175.576 -26.475  1.00 57.28           N  
ANISOU 2618  N   ARG A1106     7031   4937   9796    417  -1496  -2019       N  
ATOM   2619  CA  ARG A1106     108.116 174.933 -25.990  1.00 55.82           C  
ANISOU 2619  CA  ARG A1106     6702   4753   9753    361  -1517  -2462       C  
ATOM   2620  C   ARG A1106     108.137 173.436 -26.283  1.00 54.45           C  
ANISOU 2620  C   ARG A1106     6533   4721   9433    266  -1326  -2744       C  
ATOM   2621  O   ARG A1106     107.721 172.624 -25.448  1.00 52.71           O  
ANISOU 2621  O   ARG A1106     6226   4617   9184    144  -1081  -2749       O  
ATOM   2622  CB  ARG A1106     106.898 175.599 -26.630  1.00 58.67           C  
ANISOU 2622  CB  ARG A1106     6931   5254  10107    510  -1826  -2559       C  
ATOM   2623  CG  ARG A1106     105.557 175.210 -26.044  1.00 57.86           C  
ANISOU 2623  CG  ARG A1106     6637   5167  10181    462  -1850  -2942       C  
ATOM   2624  CD  ARG A1106     104.450 176.037 -26.669  1.00 58.89           C  
ANISOU 2624  CD  ARG A1106     6633   5369  10371    633  -2209  -3046       C  
ATOM   2625  NE  ARG A1106     104.345 175.792 -28.104  1.00 60.84           N  
ANISOU 2625  NE  ARG A1106     6900   5961  10256    762  -2359  -3027       N  
ATOM   2626  CZ  ARG A1106     103.494 176.418 -28.907  1.00 62.10           C  
ANISOU 2626  CZ  ARG A1106     6952   6312  10330    943  -2668  -3021       C  
ATOM   2627  NH1 ARG A1106     102.672 177.336 -28.418  1.00 61.58           N  
ANISOU 2627  NH1 ARG A1106     6748   6087  10562   1014  -2856  -3033       N  
ATOM   2628  NH2 ARG A1106     103.466 176.128 -30.200  1.00 65.17           N  
ANISOU 2628  NH2 ARG A1106     7360   7069  10332   1064  -2794  -3009       N  
ATOM   2629  N   GLU A1107     108.641 173.054 -27.461  1.00 55.56           N  
ANISOU 2629  N   GLU A1107     6753   5094   9265    329  -1325  -2686       N  
ATOM   2630  CA  GLU A1107     108.735 171.640 -27.813  1.00 54.82           C  
ANISOU 2630  CA  GLU A1107     6648   5113   9069    246  -1146  -2991       C  
ATOM   2631  C   GLU A1107     109.723 170.908 -26.911  1.00 48.74           C  
ANISOU 2631  C   GLU A1107     5957   4156   8406     93   -818  -2867       C  
ATOM   2632  O   GLU A1107     109.518 169.736 -26.575  1.00 46.38           O  
ANISOU 2632  O   GLU A1107     5595   3957   8068    -12   -598  -2923       O  
ATOM   2633  CB  GLU A1107     109.140 171.499 -29.281  1.00 61.34           C  
ANISOU 2633  CB  GLU A1107     7533   6283   9491    361  -1209  -2926       C  
ATOM   2634  CG  GLU A1107     109.069 170.082 -29.828  1.00 67.83           C  
ANISOU 2634  CG  GLU A1107     8300   7265  10209    300  -1070  -3329       C  
ATOM   2635  CD  GLU A1107     109.693 169.961 -31.206  1.00 74.94           C  
ANISOU 2635  CD  GLU A1107     9271   8526  10675    410  -1092  -3247       C  
ATOM   2636  OE1 GLU A1107     110.797 169.385 -31.313  1.00 75.24           O  
ANISOU 2636  OE1 GLU A1107     9404   8543  10641    350   -857  -3161       O  
ATOM   2637  OE2 GLU A1107     109.086 170.454 -32.180  1.00 79.70           O  
ANISOU 2637  OE2 GLU A1107     9827   9455  11002    564  -1344  -3261       O  
ATOM   2638  N   LEU A1108     110.803 171.585 -26.510  1.00 48.08           N  
ANISOU 2638  N   LEU A1108     5998   3890   8381     91   -768  -2541       N  
ATOM   2639  CA  LEU A1108     111.791 170.966 -25.631  1.00 46.04           C  
ANISOU 2639  CA  LEU A1108     5807   3565   8122    -31   -472  -2315       C  
ATOM   2640  C   LEU A1108     111.235 170.774 -24.225  1.00 45.23           C  
ANISOU 2640  C   LEU A1108     5624   3527   8034   -115   -358  -2190       C  
ATOM   2641  O   LEU A1108     111.389 169.703 -23.627  1.00 44.92           O  
ANISOU 2641  O   LEU A1108     5573   3546   7947   -196   -160  -2158       O  
ATOM   2642  CB  LEU A1108     113.063 171.815 -25.594  1.00 44.69           C  
ANISOU 2642  CB  LEU A1108     5762   3191   8027     -1   -473  -2016       C  
ATOM   2643  CG  LEU A1108     113.860 171.918 -26.895  1.00 47.34           C  
ANISOU 2643  CG  LEU A1108     6190   3738   8058     86   -472  -1810       C  
ATOM   2644  CD1 LEU A1108     114.722 173.166 -26.891  1.00 47.61           C  
ANISOU 2644  CD1 LEU A1108     6299   3689   8101    141   -527  -1367       C  
ATOM   2645  CD2 LEU A1108     114.716 170.682 -27.089  1.00 47.40           C  
ANISOU 2645  CD2 LEU A1108     6244   3771   7993     12   -214  -1900       C  
ATOM   2646  N   TYR A1109     110.589 171.811 -23.679  1.00 44.59           N  
ANISOU 2646  N   TYR A1109     5476   3428   8037    -78   -498  -2131       N  
ATOM   2647  CA  TYR A1109     110.018 171.713 -22.338  1.00 44.21           C  
ANISOU 2647  CA  TYR A1109     5345   3457   7996   -136   -402  -2065       C  
ATOM   2648  C   TYR A1109     109.035 170.554 -22.236  1.00 46.83           C  
ANISOU 2648  C   TYR A1109     5566   3909   8318   -184   -308  -2255       C  
ATOM   2649  O   TYR A1109     108.984 169.863 -21.213  1.00 47.65           O  
ANISOU 2649  O   TYR A1109     5640   4050   8415   -250   -144  -2184       O  
ATOM   2650  CB  TYR A1109     109.330 173.025 -21.962  1.00 45.12           C  
ANISOU 2650  CB  TYR A1109     5369   3547   8226    -72   -581  -2049       C  
ATOM   2651  CG  TYR A1109     110.272 174.157 -21.614  1.00 44.20           C  
ANISOU 2651  CG  TYR A1109     5319   3314   8161    -45   -631  -1814       C  
ATOM   2652  CD1 TYR A1109     111.487 173.911 -20.991  1.00 43.26           C  
ANISOU 2652  CD1 TYR A1109     5302   3183   7952   -103   -466  -1617       C  
ATOM   2653  CD2 TYR A1109     109.940 175.475 -21.905  1.00 44.64           C  
ANISOU 2653  CD2 TYR A1109     5314   3268   8381     49   -860  -1789       C  
ATOM   2654  CE1 TYR A1109     112.347 174.945 -20.669  1.00 43.57           C  
ANISOU 2654  CE1 TYR A1109     5374   3137   8045    -82   -508  -1418       C  
ATOM   2655  CE2 TYR A1109     110.794 176.515 -21.588  1.00 39.96           C  
ANISOU 2655  CE2 TYR A1109     4753   2563   7868     69   -897  -1562       C  
ATOM   2656  CZ  TYR A1109     111.996 176.246 -20.971  1.00 38.30           C  
ANISOU 2656  CZ  TYR A1109     4636   2370   7548     -3   -711  -1388       C  
ATOM   2657  OH  TYR A1109     112.849 177.279 -20.653  1.00 38.13           O  
ANISOU 2657  OH  TYR A1109     4618   2263   7606     13   -743  -1187       O  
ATOM   2658  N   GLY A1110     108.249 170.324 -23.284  1.00 42.46           N  
ANISOU 2658  N   GLY A1110     4934   3414   7783   -141   -425  -2508       N  
ATOM   2659  CA  GLY A1110     107.293 169.237 -23.280  1.00 43.52           C  
ANISOU 2659  CA  GLY A1110     4934   3656   7948   -186   -340  -2699       C  
ATOM   2660  C   GLY A1110     107.862 167.937 -23.810  1.00 65.05           C  
ANISOU 2660  C   GLY A1110     7692   6400  10624   -238   -186  -2770       C  
ATOM   2661  O   GLY A1110     107.128 167.107 -24.356  1.00 70.53           O  
ANISOU 2661  O   GLY A1110     8261   7182  11356   -250   -174  -3004       O  
ATOM   2662  N   SER A1111     109.172 167.749 -23.658  1.00 59.53           N  
ANISOU 2662  N   SER A1111     7136   5619   9863   -266    -68  -2580       N  
ATOM   2663  CA  SER A1111     109.824 166.533 -24.124  1.00 57.76           C  
ANISOU 2663  CA  SER A1111     6929   5396   9620   -308     88  -2638       C  
ATOM   2664  C   SER A1111     110.857 166.053 -23.113  1.00 54.14           C  
ANISOU 2664  C   SER A1111     6541   4856   9173   -362    273  -2370       C  
ATOM   2665  O   SER A1111     110.799 164.907 -22.657  1.00 54.38           O  
ANISOU 2665  O   SER A1111     6489   4885   9287   -419    432  -2374       O  
ATOM   2666  CB  SER A1111     110.473 166.762 -25.492  1.00 58.59           C  
ANISOU 2666  CB  SER A1111     7121   5514   9625   -249      5  -2782       C  
ATOM   2667  OG  SER A1111     109.496 166.916 -26.506  1.00 61.81           O  
ANISOU 2667  OG  SER A1111     7432   6059   9995   -184   -177  -3100       O  
ATOM   2668  N   VAL A1112     111.796 166.930 -22.745  1.00 52.18           N  
ANISOU 2668  N   VAL A1112     6423   4539   8865   -339    245  -2145       N  
ATOM   2669  CA  VAL A1112     112.878 166.534 -21.849  1.00 48.27           C  
ANISOU 2669  CA  VAL A1112     5983   3995   8360   -372    388  -1909       C  
ATOM   2670  C   VAL A1112     112.323 166.153 -20.476  1.00 46.29           C  
ANISOU 2670  C   VAL A1112     5641   3778   8168   -412    468  -1839       C  
ATOM   2671  O   VAL A1112     111.206 166.524 -20.092  1.00 47.45           O  
ANISOU 2671  O   VAL A1112     5704   3972   8352   -412    403  -1924       O  
ATOM   2672  CB  VAL A1112     113.924 167.653 -21.724  1.00 44.75           C  
ANISOU 2672  CB  VAL A1112     5666   3483   7853   -336    323  -1700       C  
ATOM   2673  CG1 VAL A1112     114.490 168.005 -23.093  1.00 43.39           C  
ANISOU 2673  CG1 VAL A1112     5576   3245   7664   -295    274  -1773       C  
ATOM   2674  CG2 VAL A1112     113.316 168.879 -21.059  1.00 44.38           C  
ANISOU 2674  CG2 VAL A1112     5601   3450   7809   -311    187  -1644       C  
ATOM   2675  N   ASP A1113     113.125 165.393 -19.730  1.00 44.42           N  
ANISOU 2675  N   ASP A1113     5408   3513   7958   -442    617  -1695       N  
ATOM   2676  CA  ASP A1113     112.718 164.923 -18.411  1.00 45.86           C  
ANISOU 2676  CA  ASP A1113     5501   3706   8218   -479    724  -1640       C  
ATOM   2677  C   ASP A1113     113.023 165.932 -17.311  1.00 43.87           C  
ANISOU 2677  C   ASP A1113     5300   3471   7898   -459    663  -1489       C  
ATOM   2678  O   ASP A1113     112.193 166.145 -16.422  1.00 44.11           O  
ANISOU 2678  O   ASP A1113     5252   3534   7974   -475    672  -1530       O  
ATOM   2679  CB  ASP A1113     113.401 163.590 -18.095  1.00 50.03           C  
ANISOU 2679  CB  ASP A1113     5988   4178   8843   -513    922  -1572       C  
ATOM   2680  CG  ASP A1113     112.844 162.447 -18.913  1.00 56.36           C  
ANISOU 2680  CG  ASP A1113     6678   4959   9776   -549   1014  -1763       C  
ATOM   2681  OD1 ASP A1113     111.646 162.499 -19.264  1.00 59.13           O  
ANISOU 2681  OD1 ASP A1113     6940   5352  10175   -561    958  -1950       O  
ATOM   2682  OD2 ASP A1113     113.601 161.499 -19.206  1.00 58.89           O  
ANISOU 2682  OD2 ASP A1113     6983   5222  10170   -562   1141  -1741       O  
ATOM   2683  N   PHE A1114     114.197 166.556 -17.344  1.00 40.80           N  
ANISOU 2683  N   PHE A1114     5021   3060   7419   -428    611  -1337       N  
ATOM   2684  CA  PHE A1114     114.581 167.501 -16.308  1.00 39.53           C  
ANISOU 2684  CA  PHE A1114     4890   2918   7214   -412    553  -1222       C  
ATOM   2685  C   PHE A1114     115.231 168.720 -16.940  1.00 40.57           C  
ANISOU 2685  C   PHE A1114     5115   3027   7271   -369    410  -1153       C  
ATOM   2686  O   PHE A1114     115.947 168.605 -17.938  1.00 41.63           O  
ANISOU 2686  O   PHE A1114     5319   3115   7382   -356    409  -1116       O  
ATOM   2687  CB  PHE A1114     115.545 166.874 -15.290  1.00 32.28           C  
ANISOU 2687  CB  PHE A1114     3971   1979   6316   -427    681  -1079       C  
ATOM   2688  CG  PHE A1114     114.963 165.720 -14.522  1.00 41.09           C  
ANISOU 2688  CG  PHE A1114     4986   3077   7549   -470    856  -1117       C  
ATOM   2689  CD1 PHE A1114     115.059 164.428 -15.008  1.00 41.06           C  
ANISOU 2689  CD1 PHE A1114     4941   3027   7632   -492    997  -1133       C  
ATOM   2690  CD2 PHE A1114     114.333 165.925 -13.307  1.00 41.31           C  
ANISOU 2690  CD2 PHE A1114     4946   3118   7632   -493    902  -1147       C  
ATOM   2691  CE1 PHE A1114     114.530 163.364 -14.300  1.00 42.86           C  
ANISOU 2691  CE1 PHE A1114     5064   3209   8012   -534   1183  -1154       C  
ATOM   2692  CE2 PHE A1114     113.803 164.864 -12.595  1.00 41.70           C  
ANISOU 2692  CE2 PHE A1114     4900   3121   7821   -540   1101  -1169       C  
ATOM   2693  CZ  PHE A1114     113.901 163.583 -13.093  1.00 35.44           C  
ANISOU 2693  CZ  PHE A1114     4069   2269   7126   -558   1243  -1160       C  
ATOM   2694  N   VAL A1115     114.979 169.884 -16.349  1.00 41.39           N  
ANISOU 2694  N   VAL A1115     5204   3151   7370   -350    306  -1145       N  
ATOM   2695  CA  VAL A1115     115.613 171.132 -16.753  1.00 40.64           C  
ANISOU 2695  CA  VAL A1115     5166   3016   7259   -313    187  -1063       C  
ATOM   2696  C   VAL A1115     116.491 171.606 -15.604  1.00 39.66           C  
ANISOU 2696  C   VAL A1115     5034   2907   7128   -313    193   -956       C  
ATOM   2697  O   VAL A1115     116.050 171.641 -14.448  1.00 37.75           O  
ANISOU 2697  O   VAL A1115     4718   2709   6915   -326    214  -1011       O  
ATOM   2698  CB  VAL A1115     114.575 172.197 -17.152  1.00 40.40           C  
ANISOU 2698  CB  VAL A1115     5083   2980   7289   -281     48  -1167       C  
ATOM   2699  CG1 VAL A1115     113.525 172.370 -16.065  1.00 41.52           C  
ANISOU 2699  CG1 VAL A1115     5109   3193   7471   -289     41  -1278       C  
ATOM   2700  CG2 VAL A1115     115.262 173.516 -17.459  1.00 38.43           C  
ANISOU 2700  CG2 VAL A1115     4857   2661   7084   -242    -61  -1061       C  
ATOM   2701  N   ILE A1116     117.735 171.959 -15.917  1.00 39.42           N  
ANISOU 2701  N   ILE A1116     5065   2834   7079   -300    182   -820       N  
ATOM   2702  CA  ILE A1116     118.731 172.329 -14.919  1.00 37.11           C  
ANISOU 2702  CA  ILE A1116     4753   2553   6796   -299    187   -732       C  
ATOM   2703  C   ILE A1116     118.934 173.837 -14.959  1.00 39.01           C  
ANISOU 2703  C   ILE A1116     4956   2763   7102   -271     64   -715       C  
ATOM   2704  O   ILE A1116     119.240 174.404 -16.016  1.00 41.31           O  
ANISOU 2704  O   ILE A1116     5287   2989   7419   -252     16   -645       O  
ATOM   2705  CB  ILE A1116     120.057 171.584 -15.149  1.00 34.18           C  
ANISOU 2705  CB  ILE A1116     4437   2161   6391   -303    273   -597       C  
ATOM   2706  CG1 ILE A1116     119.831 170.073 -15.064  1.00 33.32           C  
ANISOU 2706  CG1 ILE A1116     4324   2065   6270   -326    405   -618       C  
ATOM   2707  CG2 ILE A1116     121.097 172.033 -14.140  1.00 31.84           C  
ANISOU 2707  CG2 ILE A1116     4102   1868   6127   -298    263   -523       C  
ATOM   2708  CD1 ILE A1116     121.038 169.254 -15.457  1.00 32.90           C  
ANISOU 2708  CD1 ILE A1116     4301   1988   6210   -322    498   -504       C  
ATOM   2709  N   ILE A1117     118.764 174.483 -13.809  1.00 38.81           N  
ANISOU 2709  N   ILE A1117     4836   2769   7140   -268     19   -784       N  
ATOM   2710  CA  ILE A1117     118.958 175.925 -13.672  1.00 38.24           C  
ANISOU 2710  CA  ILE A1117     4680   2666   7185   -239    -98   -794       C  
ATOM   2711  C   ILE A1117     119.944 176.179 -12.536  1.00 38.83           C  
ANISOU 2711  C   ILE A1117     4687   2751   7316   -245    -97   -789       C  
ATOM   2712  O   ILE A1117     119.524 176.497 -11.413  1.00 39.64           O  
ANISOU 2712  O   ILE A1117     4685   2891   7486   -243   -128   -927       O  
ATOM   2713  CB  ILE A1117     117.626 176.648 -13.419  1.00 36.63           C  
ANISOU 2713  CB  ILE A1117     4372   2482   7063   -218   -187   -947       C  
ATOM   2714  CG1 ILE A1117     116.532 176.095 -14.330  1.00 33.67           C  
ANISOU 2714  CG1 ILE A1117     4045   2109   6638   -218   -177   -993       C  
ATOM   2715  CG2 ILE A1117     117.785 178.143 -13.645  1.00 39.55           C  
ANISOU 2715  CG2 ILE A1117     4644   2784   7598   -179   -319   -937       C  
ATOM   2716  CD1 ILE A1117     115.218 175.885 -13.625  1.00 32.30           C  
ANISOU 2716  CD1 ILE A1117     3784   2008   6480   -223   -172  -1163       C  
ATOM   2717  N   PRO A1118     121.259 176.054 -12.776  1.00 38.37           N  
ANISOU 2717  N   PRO A1118     4240   2973   7365   -766   1096   -666       N  
ATOM   2718  CA  PRO A1118     122.271 176.244 -11.729  1.00 39.83           C  
ANISOU 2718  CA  PRO A1118     4414   3194   7527   -749   1161   -698       C  
ATOM   2719  C   PRO A1118     122.704 177.699 -11.558  1.00 39.82           C  
ANISOU 2719  C   PRO A1118     4420   3192   7518   -747   1208   -701       C  
ATOM   2720  O   PRO A1118     123.891 178.025 -11.607  1.00 39.45           O  
ANISOU 2720  O   PRO A1118     4390   3165   7434   -755   1238   -731       O  
ATOM   2721  CB  PRO A1118     123.421 175.349 -12.207  1.00 39.38           C  
ANISOU 2721  CB  PRO A1118     4382   3160   7421   -763   1145   -732       C  
ATOM   2722  CG  PRO A1118     123.203 175.176 -13.703  1.00 37.42           C  
ANISOU 2722  CG  PRO A1118     4176   2888   7152   -796   1087   -718       C  
ATOM   2723  CD  PRO A1118     121.870 175.760 -14.078  1.00 31.69           C  
ANISOU 2723  CD  PRO A1118     3451   2122   6467   -799   1051   -673       C  
ATOM   2724  N   SER A1119     121.726 178.571 -11.327  1.00 40.02           N  
ANISOU 2724  N   SER A1119     4427   3190   7590   -736   1214   -675       N  
ATOM   2725  CA  SER A1119     121.956 180.007 -11.271  1.00 39.82           C  
ANISOU 2725  CA  SER A1119     4412   3150   7567   -737   1244   -672       C  
ATOM   2726  C   SER A1119     122.591 180.421  -9.950  1.00 38.89           C  
ANISOU 2726  C   SER A1119     4268   3056   7451   -713   1310   -706       C  
ATOM   2727  O   SER A1119     122.258 179.889  -8.888  1.00 38.21           O  
ANISOU 2727  O   SER A1119     4152   2982   7385   -692   1334   -717       O  
ATOM   2728  CB  SER A1119     120.637 180.757 -11.467  1.00 40.49           C  
ANISOU 2728  CB  SER A1119     4483   3189   7713   -732   1217   -637       C  
ATOM   2729  OG  SER A1119     120.057 180.461 -12.723  1.00 41.00           O  
ANISOU 2729  OG  SER A1119     4582   3221   7776   -758   1141   -606       O  
ATOM   2730  N   TYR A1120     123.518 181.379 -10.022  1.00 38.15           N  
ANISOU 2730  N   TYR A1120     4193   2964   7337   -723   1338   -723       N  
ATOM   2731  CA  TYR A1120     124.014 182.015  -8.808  1.00 35.34           C  
ANISOU 2731  CA  TYR A1120     3815   2619   6994   -704   1389   -755       C  
ATOM   2732  C   TYR A1120     123.048 183.079  -8.314  1.00 33.75           C  
ANISOU 2732  C   TYR A1120     3593   2384   6846   -688   1403   -738       C  
ATOM   2733  O   TYR A1120     122.950 183.318  -7.104  1.00 31.75           O  
ANISOU 2733  O   TYR A1120     3315   2135   6613   -667   1442   -761       O  
ATOM   2734  CB  TYR A1120     125.385 182.651  -9.052  1.00 34.41           C  
ANISOU 2734  CB  TYR A1120     3714   2509   6851   -722   1413   -786       C  
ATOM   2735  CG  TYR A1120     126.525 181.687  -9.288  1.00 37.01           C  
ANISOU 2735  CG  TYR A1120     4047   2872   7142   -733   1413   -823       C  
ATOM   2736  CD1 TYR A1120     126.798 181.199 -10.559  1.00 40.33           C  
ANISOU 2736  CD1 TYR A1120     4498   3293   7532   -763   1391   -813       C  
ATOM   2737  CD2 TYR A1120     127.345 181.288  -8.244  1.00 37.52           C  
ANISOU 2737  CD2 TYR A1120     4087   2962   7206   -718   1432   -870       C  
ATOM   2738  CE1 TYR A1120     127.852 180.327 -10.780  1.00 42.14           C  
ANISOU 2738  CE1 TYR A1120     4724   3552   7737   -772   1394   -856       C  
ATOM   2739  CE2 TYR A1120     128.398 180.420  -8.452  1.00 39.19           C  
ANISOU 2739  CE2 TYR A1120     4295   3199   7396   -726   1425   -909       C  
ATOM   2740  CZ  TYR A1120     128.648 179.941  -9.720  1.00 42.39           C  
ANISOU 2740  CZ  TYR A1120     4721   3609   7778   -751   1410   -905       C  
ATOM   2741  OH  TYR A1120     129.700 179.076  -9.920  1.00 45.00           O  
ANISOU 2741  OH  TYR A1120     5039   3962   8097   -758   1407   -953       O  
ATOM   2742  N   PHE A1121     122.327 183.713  -9.238  1.00 34.41           N  
ANISOU 2742  N   PHE A1121     3693   2429   6952   -701   1367   -700       N  
ATOM   2743  CA  PHE A1121     121.464 184.847  -8.930  1.00 39.02           C  
ANISOU 2743  CA  PHE A1121     4258   2971   7595   -688   1370   -686       C  
ATOM   2744  C   PHE A1121     120.264 184.814  -9.865  1.00 42.48           C  
ANISOU 2744  C   PHE A1121     4703   3369   8071   -696   1308   -643       C  
ATOM   2745  O   PHE A1121     120.418 184.971 -11.080  1.00 42.91           O  
ANISOU 2745  O   PHE A1121     4813   3396   8094   -729   1257   -612       O  
ATOM   2746  CB  PHE A1121     122.238 186.158  -9.068  1.00 39.36           C  
ANISOU 2746  CB  PHE A1121     4332   2991   7632   -704   1382   -691       C  
ATOM   2747  CG  PHE A1121     121.396 187.378  -8.882  1.00 41.85           C  
ANISOU 2747  CG  PHE A1121     4636   3253   8011   -694   1372   -676       C  
ATOM   2748  CD1 PHE A1121     120.944 187.738  -7.622  1.00 43.23           C  
ANISOU 2748  CD1 PHE A1121     4760   3428   8236   -662   1414   -706       C  
ATOM   2749  CD2 PHE A1121     121.056 188.172  -9.965  1.00 42.36           C  
ANISOU 2749  CD2 PHE A1121     4751   3259   8084   -721   1317   -632       C  
ATOM   2750  CE1 PHE A1121     120.164 188.866  -7.445  1.00 43.18           C  
ANISOU 2750  CE1 PHE A1121     4740   3371   8298   -651   1404   -700       C  
ATOM   2751  CE2 PHE A1121     120.278 189.303  -9.800  1.00 42.30           C  
ANISOU 2751  CE2 PHE A1121     4737   3193   8143   -710   1297   -620       C  
ATOM   2752  CZ  PHE A1121     119.831 189.652  -8.535  1.00 42.81           C  
ANISOU 2752  CZ  PHE A1121     4732   3261   8273   -671   1346   -659       C  
ATOM   2753  N   GLU A1122     119.077 184.604  -9.290  1.00 45.79           N  
ANISOU 2753  N   GLU A1122     5065   3776   8558   -671   1313   -643       N  
ATOM   2754  CA  GLU A1122     117.825 184.542 -10.045  1.00 45.59           C  
ANISOU 2754  CA  GLU A1122     5021   3703   8597   -673   1254   -614       C  
ATOM   2755  C   GLU A1122     116.708 185.020  -9.122  1.00 43.08           C  
ANISOU 2755  C   GLU A1122     4616   3352   8402   -639   1303   -636       C  
ATOM   2756  O   GLU A1122     116.229 184.259  -8.267  1.00 42.48           O  
ANISOU 2756  O   GLU A1122     4483   3296   8363   -621   1355   -658       O  
ATOM   2757  CB  GLU A1122     117.536 183.137 -10.568  1.00 49.11           C  
ANISOU 2757  CB  GLU A1122     5466   4168   9026   -683   1216   -603       C  
ATOM   2758  CG  GLU A1122     116.250 183.023 -11.373  1.00 53.97           C  
ANISOU 2758  CG  GLU A1122     6047   4723   9737   -685   1155   -584       C  
ATOM   2759  CD  GLU A1122     116.382 183.589 -12.773  1.00 60.09           C  
ANISOU 2759  CD  GLU A1122     6900   5444  10489   -717   1076   -552       C  
ATOM   2760  OE1 GLU A1122     117.091 182.976 -13.601  1.00 62.48           O  
ANISOU 2760  OE1 GLU A1122     7273   5763  10705   -749   1042   -540       O  
ATOM   2761  OE2 GLU A1122     115.781 184.651 -13.041  1.00 61.83           O  
ANISOU 2761  OE2 GLU A1122     7117   5595  10780   -712   1050   -541       O  
ATOM   2762  N   PRO A1123     116.280 186.272  -9.258  1.00 42.13           N  
ANISOU 2762  N   PRO A1123     4483   3173   8352   -632   1292   -634       N  
ATOM   2763  CA  PRO A1123     115.214 186.825  -8.408  1.00 41.68           C  
ANISOU 2763  CA  PRO A1123     4329   3075   8432   -599   1344   -666       C  
ATOM   2764  C   PRO A1123     113.804 186.693  -8.967  1.00 43.35           C  
ANISOU 2764  C   PRO A1123     4467   3224   8781   -588   1301   -661       C  
ATOM   2765  O   PRO A1123     112.880 187.262  -8.380  1.00 46.88           O  
ANISOU 2765  O   PRO A1123     4821   3625   9366   -561   1341   -694       O  
ATOM   2766  CB  PRO A1123     115.614 188.307  -8.320  1.00 41.55           C  
ANISOU 2766  CB  PRO A1123     4343   3021   8425   -599   1343   -670       C  
ATOM   2767  CG  PRO A1123     116.552 188.562  -9.524  1.00 41.28           C  
ANISOU 2767  CG  PRO A1123     4422   2981   8280   -638   1267   -625       C  
ATOM   2768  CD  PRO A1123     116.753 187.255 -10.244  1.00 42.14           C  
ANISOU 2768  CD  PRO A1123     4563   3131   8316   -659   1232   -603       C  
ATOM   2769  N   PHE A1124     113.608 185.988 -10.063  1.00 41.17           N  
ANISOU 2769  N   PHE A1124     4221   2938   8484   -608   1219   -630       N  
ATOM   2770  CA  PHE A1124     112.256 185.864 -10.601  1.00 41.85           C  
ANISOU 2770  CA  PHE A1124     4227   2956   8719   -595   1165   -632       C  
ATOM   2771  C   PHE A1124     111.887 184.440 -10.983  1.00 42.84           C  
ANISOU 2771  C   PHE A1124     4330   3103   8846   -605   1136   -626       C  
ATOM   2772  O   PHE A1124     110.739 184.044 -10.784  1.00 43.35           O  
ANISOU 2772  O   PHE A1124     4283   3133   9056   -586   1144   -650       O  
ATOM   2773  CB  PHE A1124     112.088 186.781 -11.818  1.00 42.27           C  
ANISOU 2773  CB  PHE A1124     4342   2925   8792   -608   1055   -601       C  
ATOM   2774  CG  PHE A1124     112.528 188.191 -11.574  1.00 38.12           C  
ANISOU 2774  CG  PHE A1124     3860   2368   8256   -604   1068   -599       C  
ATOM   2775  CD1 PHE A1124     111.694 189.093 -10.937  1.00 38.94           C  
ANISOU 2775  CD1 PHE A1124     3869   2416   8510   -567   1092   -634       C  
ATOM   2776  CD2 PHE A1124     113.782 188.613 -11.979  1.00 40.36           C  
ANISOU 2776  CD2 PHE A1124     4272   2671   8390   -638   1058   -567       C  
ATOM   2777  CE1 PHE A1124     112.108 190.393 -10.714  1.00 43.35           C  
ANISOU 2777  CE1 PHE A1124     4472   2939   9060   -564   1096   -634       C  
ATOM   2778  CE2 PHE A1124     114.199 189.907 -11.760  1.00 40.62           C  
ANISOU 2778  CE2 PHE A1124     4347   2668   8419   -637   1066   -565       C  
ATOM   2779  CZ  PHE A1124     113.364 190.798 -11.127  1.00 42.61           C  
ANISOU 2779  CZ  PHE A1124     4515   2865   8811   -600   1081   -597       C  
ATOM   2780  N   GLY A1125     112.820 183.667 -11.529  1.00 42.74           N  
ANISOU 2780  N   GLY A1125     4412   3140   8689   -635   1105   -601       N  
ATOM   2781  CA  GLY A1125     112.546 182.281 -11.872  1.00 40.96           C  
ANISOU 2781  CA  GLY A1125     4170   2933   8459   -647   1073   -597       C  
ATOM   2782  C   GLY A1125     111.545 182.086 -12.993  1.00 40.62           C  
ANISOU 2782  C   GLY A1125     4096   2815   8521   -652    968   -590       C  
ATOM   2783  O   GLY A1125     110.687 181.199 -12.905  1.00 38.88           O  
ANISOU 2783  O   GLY A1125     3790   2583   8399   -643    959   -606       O  
ATOM   2784  N   LEU A1126     111.644 182.878 -14.062  1.00 41.90           N  
ANISOU 2784  N   LEU A1126     4334   2917   8670   -666    882   -567       N  
ATOM   2785  CA  LEU A1126     110.695 182.732 -15.160  1.00 38.55           C  
ANISOU 2785  CA  LEU A1126     3893   2405   8352   -667    764   -565       C  
ATOM   2786  C   LEU A1126     110.907 181.425 -15.913  1.00 41.45           C  
ANISOU 2786  C   LEU A1126     4303   2790   8657   -695    709   -559       C  
ATOM   2787  O   LEU A1126     109.947 180.850 -16.438  1.00 41.49           O  
ANISOU 2787  O   LEU A1126     4244   2742   8779   -686    629   -574       O  
ATOM   2788  CB  LEU A1126     110.803 183.925 -16.107  1.00 53.25           C  
ANISOU 2788  CB  LEU A1126     5855   4178  10199   -677    682   -538       C  
ATOM   2789  CG  LEU A1126     109.730 184.033 -17.189  1.00 51.71           C  
ANISOU 2789  CG  LEU A1126     5648   3864  10135   -665    541   -541       C  
ATOM   2790  CD1 LEU A1126     108.341 184.081 -16.568  1.00 50.40           C  
ANISOU 2790  CD1 LEU A1126     5293   3663  10196   -616    536   -586       C  
ATOM   2791  CD2 LEU A1126     109.980 185.260 -18.044  1.00 41.25           C  
ANISOU 2791  CD2 LEU A1126     4460   2442   8770   -675    466   -507       C  
ATOM   2792  N   VAL A1127     112.148 180.937 -15.966  1.00 42.36           N  
ANISOU 2792  N   VAL A1127     4516   2975   8603   -724    744   -545       N  
ATOM   2793  CA  VAL A1127     112.426 179.684 -16.662  1.00 42.40           C  
ANISOU 2793  CA  VAL A1127     4563   2996   8550   -750    695   -546       C  
ATOM   2794  C   VAL A1127     111.753 178.514 -15.953  1.00 41.07           C  
ANISOU 2794  C   VAL A1127     4281   2861   8462   -732    720   -569       C  
ATOM   2795  O   VAL A1127     111.257 177.582 -16.598  1.00 37.58           O  
ANISOU 2795  O   VAL A1127     3820   2389   8068   -741    646   -579       O  
ATOM   2796  CB  VAL A1127     113.945 179.468 -16.791  1.00 42.10           C  
ANISOU 2796  CB  VAL A1127     4637   3023   8334   -781    736   -535       C  
ATOM   2797  CG1 VAL A1127     114.234 178.315 -17.738  1.00 36.26           C  
ANISOU 2797  CG1 VAL A1127     3953   2277   7545   -810    673   -543       C  
ATOM   2798  CG2 VAL A1127     114.631 180.744 -17.260  1.00 43.13           C  
ANISOU 2798  CG2 VAL A1127     4869   3120   8397   -801    740   -512       C  
ATOM   2799  N   ALA A1128     111.721 178.542 -14.618  1.00 41.30           N  
ANISOU 2799  N   ALA A1128     4241   2942   8508   -710    825   -578       N  
ATOM   2800  CA  ALA A1128     111.091 177.458 -13.868  1.00 42.62           C  
ANISOU 2800  CA  ALA A1128     4317   3128   8747   -700    863   -595       C  
ATOM   2801  C   ALA A1128     109.591 177.407 -14.134  1.00 49.06           C  
ANISOU 2801  C   ALA A1128     5009   3867   9766   -682    813   -615       C  
ATOM   2802  O   ALA A1128     109.025 176.331 -14.360  1.00 51.85           O  
ANISOU 2802  O   ALA A1128     5312   4203  10184   -690    773   -625       O  
ATOM   2803  CB  ALA A1128     111.372 177.617 -12.374  1.00 38.16           C  
ANISOU 2803  CB  ALA A1128     3725   2616   8158   -682    991   -603       C  
ATOM   2804  N   LEU A1129     108.929 178.569 -14.115  1.00 50.43           N  
ANISOU 2804  N   LEU A1129     5124   3985  10053   -658    809   -626       N  
ATOM   2805  CA  LEU A1129     107.500 178.614 -14.413  1.00 51.06           C  
ANISOU 2805  CA  LEU A1129     5068   3979  10352   -636    749   -655       C  
ATOM   2806  C   LEU A1129     107.216 178.123 -15.828  1.00 52.14           C  
ANISOU 2806  C   LEU A1129     5237   4058  10517   -649    593   -654       C  
ATOM   2807  O   LEU A1129     106.234 177.407 -16.061  1.00 52.16           O  
ANISOU 2807  O   LEU A1129     5132   4015  10671   -640    536   -682       O  
ATOM   2808  CB  LEU A1129     106.966 180.036 -14.225  1.00 49.93           C  
ANISOU 2808  CB  LEU A1129     4867   3781  10325   -605    756   -671       C  
ATOM   2809  CG  LEU A1129     106.790 180.559 -12.799  1.00 48.18           C  
ANISOU 2809  CG  LEU A1129     4564   3585  10157   -581    905   -695       C  
ATOM   2810  CD1 LEU A1129     106.552 182.060 -12.813  1.00 49.54           C  
ANISOU 2810  CD1 LEU A1129     4714   3701  10406   -555    892   -707       C  
ATOM   2811  CD2 LEU A1129     105.640 179.843 -12.112  1.00 47.72           C  
ANISOU 2811  CD2 LEU A1129     4348   3500  10284   -564    966   -737       C  
ATOM   2812  N   GLU A1130     108.072 178.490 -16.784  1.00 51.70           N  
ANISOU 2812  N   GLU A1130     5330   3994  10320   -672    525   -628       N  
ATOM   2813  CA  GLU A1130     107.853 178.089 -18.170  1.00 51.96           C  
ANISOU 2813  CA  GLU A1130     5418   3956  10369   -685    375   -632       C  
ATOM   2814  C   GLU A1130     108.033 176.586 -18.353  1.00 49.09           C  
ANISOU 2814  C   GLU A1130     5057   3631   9964   -706    359   -641       C  
ATOM   2815  O   GLU A1130     107.294 175.959 -19.120  1.00 48.03           O  
ANISOU 2815  O   GLU A1130     4878   3434   9937   -701    242   -667       O  
ATOM   2816  CB  GLU A1130     108.800 178.862 -19.090  1.00 53.41           C  
ANISOU 2816  CB  GLU A1130     5781   4111  10399   -710    331   -601       C  
ATOM   2817  CG  GLU A1130     108.487 180.349 -19.194  1.00 56.24           C  
ANISOU 2817  CG  GLU A1130     6156   4398  10815   -688    304   -590       C  
ATOM   2818  CD  GLU A1130     109.656 181.154 -19.729  1.00 58.93           C  
ANISOU 2818  CD  GLU A1130     6683   4730  10976   -722    318   -549       C  
ATOM   2819  OE1 GLU A1130     110.786 180.622 -19.743  1.00 59.28           O  
ANISOU 2819  OE1 GLU A1130     6817   4848  10859   -759    380   -536       O  
ATOM   2820  OE2 GLU A1130     109.448 182.316 -20.133  1.00 61.48           O  
ANISOU 2820  OE2 GLU A1130     7063   4967  11330   -710    266   -532       O  
ATOM   2821  N   ALA A1131     109.002 175.989 -17.655  1.00 47.14           N  
ANISOU 2821  N   ALA A1131     4859   3480   9572   -726    462   -626       N  
ATOM   2822  CA  ALA A1131     109.268 174.563 -17.828  1.00 46.00           C  
ANISOU 2822  CA  ALA A1131     4729   3366   9381   -746    441   -634       C  
ATOM   2823  C   ALA A1131     108.283 173.703 -17.044  1.00 44.20           C  
ANISOU 2823  C   ALA A1131     4359   3138   9296   -733    472   -651       C  
ATOM   2824  O   ALA A1131     107.821 172.673 -17.547  1.00 44.21           O  
ANISOU 2824  O   ALA A1131     4326   3109   9364   -740    395   -670       O  
ATOM   2825  CB  ALA A1131     110.702 174.239 -17.414  1.00 44.98           C  
ANISOU 2825  CB  ALA A1131     4707   3327   9055   -769    522   -615       C  
ATOM   2826  N   MET A1132     107.959 174.105 -15.811  1.00 42.47           N  
ANISOU 2826  N   MET A1132     4062   2946   9130   -715    589   -649       N  
ATOM   2827  CA  MET A1132     107.025 173.335 -14.994  1.00 41.08           C  
ANISOU 2827  CA  MET A1132     3761   2758   9092   -709    642   -665       C  
ATOM   2828  C   MET A1132     105.621 173.330 -15.588  1.00 43.42           C  
ANISOU 2828  C   MET A1132     3918   2960   9618   -689    549   -701       C  
ATOM   2829  O   MET A1132     104.900 172.335 -15.456  1.00 42.70           O  
ANISOU 2829  O   MET A1132     3741   2844   9641   -695    538   -718       O  
ATOM   2830  CB  MET A1132     106.999 173.884 -13.567  1.00 40.20           C  
ANISOU 2830  CB  MET A1132     3609   2680   8985   -694    795   -662       C  
ATOM   2831  CG  MET A1132     108.282 173.640 -12.788  1.00 38.85           C  
ANISOU 2831  CG  MET A1132     3553   2594   8613   -710    881   -635       C  
ATOM   2832  SD  MET A1132     108.435 174.652 -11.302  1.00 38.55           S  
ANISOU 2832  SD  MET A1132     3499   2584   8562   -688   1037   -640       S  
ATOM   2833  CE  MET A1132     107.001 174.127 -10.368  1.00 39.90           C  
ANISOU 2833  CE  MET A1132     3525   2701   8935   -685   1126   -666       C  
ATOM   2834  N   CYS A1133     105.217 174.421 -16.245  1.00 45.68           N  
ANISOU 2834  N   CYS A1133     4182   3188   9988   -665    472   -715       N  
ATOM   2835  CA  CYS A1133     103.906 174.458 -16.882  1.00 48.16           C  
ANISOU 2835  CA  CYS A1133     4359   3402  10537   -639    354   -758       C  
ATOM   2836  C   CYS A1133     103.773 173.423 -17.992  1.00 49.85           C  
ANISOU 2836  C   CYS A1133     4596   3579  10765   -652    206   -773       C  
ATOM   2837  O   CYS A1133     102.649 173.052 -18.345  1.00 53.03           O  
ANISOU 2837  O   CYS A1133     4864   3907  11376   -631    112   -816       O  
ATOM   2838  CB  CYS A1133     103.621 175.855 -17.441  1.00 50.83           C  
ANISOU 2838  CB  CYS A1133     4694   3674  10943   -609    274   -768       C  
ATOM   2839  SG  CYS A1133     102.942 177.038 -16.247  1.00 54.41           S  
ANISOU 2839  SG  CYS A1133     5010   4113  11549   -571    401   -792       S  
ATOM   2840  N   LEU A1134     104.885 172.948 -18.551  1.00 48.47           N  
ANISOU 2840  N   LEU A1134     4581   3449  10387   -683    179   -747       N  
ATOM   2841  CA  LEU A1134     104.854 171.971 -19.632  1.00 48.45           C  
ANISOU 2841  CA  LEU A1134     4614   3408  10386   -695     39   -769       C  
ATOM   2842  C   LEU A1134     105.341 170.591 -19.204  1.00 47.28           C  
ANISOU 2842  C   LEU A1134     4490   3321  10152   -725     97   -759       C  
ATOM   2843  O   LEU A1134     105.481 169.705 -20.053  1.00 47.88           O  
ANISOU 2843  O   LEU A1134     4611   3374  10208   -737     -8   -779       O  
ATOM   2844  CB  LEU A1134     105.671 172.472 -20.825  1.00 48.92           C  
ANISOU 2844  CB  LEU A1134     4844   3442  10301   -705    -59   -762       C  
ATOM   2845  CG  LEU A1134     104.929 173.410 -21.779  1.00 50.86           C  
ANISOU 2845  CG  LEU A1134     5080   3576  10667   -671   -213   -786       C  
ATOM   2846  CD1 LEU A1134     105.076 174.864 -21.357  1.00 51.16           C  
ANISOU 2846  CD1 LEU A1134     5141   3613  10683   -659   -144   -758       C  
ATOM   2847  CD2 LEU A1134     105.417 173.199 -23.195  1.00 51.51           C  
ANISOU 2847  CD2 LEU A1134     5321   3600  10650   -681   -359   -801       C  
ATOM   2848  N   GLY A1135     105.602 170.385 -17.915  1.00 47.37           N  
ANISOU 2848  N   GLY A1135     4483   3402  10115   -736    253   -732       N  
ATOM   2849  CA  GLY A1135     105.883 169.072 -17.374  1.00 48.36           C  
ANISOU 2849  CA  GLY A1135     4619   3566  10190   -763    302   -721       C  
ATOM   2850  C   GLY A1135     107.309 168.860 -16.913  1.00 48.05           C  
ANISOU 2850  C   GLY A1135     4720   3615   9923   -785    383   -687       C  
ATOM   2851  O   GLY A1135     107.555 167.938 -16.124  1.00 48.58           O  
ANISOU 2851  O   GLY A1135     4795   3716   9948   -805    448   -672       O  
ATOM   2852  N   ALA A1136     108.253 169.677 -17.375  1.00 45.59           N  
ANISOU 2852  N   ALA A1136     4518   3331   9471   -784    377   -677       N  
ATOM   2853  CA  ALA A1136     109.651 169.472 -17.020  1.00 38.89           C  
ANISOU 2853  CA  ALA A1136     3790   2560   8425   -801    441   -656       C  
ATOM   2854  C   ALA A1136     109.850 169.617 -15.515  1.00 38.30           C  
ANISOU 2854  C   ALA A1136     3695   2542   8316   -797    579   -631       C  
ATOM   2855  O   ALA A1136     109.268 170.496 -14.873  1.00 65.85           O  
ANISOU 2855  O   ALA A1136     7117   6022  11880   -778    645   -628       O  
ATOM   2856  CB  ALA A1136     110.541 170.459 -17.774  1.00 38.33           C  
ANISOU 2856  CB  ALA A1136     3828   2498   8235   -803    420   -653       C  
ATOM   2857  N   ILE A1137     110.665 168.734 -14.955  1.00 37.65           N  
ANISOU 2857  N   ILE A1137     3671   2507   8127   -814    617   -619       N  
ATOM   2858  CA  ILE A1137     110.972 168.727 -13.526  1.00 42.45           C  
ANISOU 2858  CA  ILE A1137     4284   3159   8688   -813    734   -598       C  
ATOM   2859  C   ILE A1137     112.289 169.456 -13.331  1.00 41.75           C  
ANISOU 2859  C   ILE A1137     4289   3131   8444   -804    774   -592       C  
ATOM   2860  O   ILE A1137     113.322 168.998 -13.846  1.00 43.14           O  
ANISOU 2860  O   ILE A1137     4544   3332   8515   -814    732   -599       O  
ATOM   2861  CB  ILE A1137     111.050 167.298 -12.974  1.00 42.83           C  
ANISOU 2861  CB  ILE A1137     4342   3206   8725   -840    739   -588       C  
ATOM   2862  CG1 ILE A1137     109.708 166.591 -13.136  1.00 44.46           C  
ANISOU 2862  CG1 ILE A1137     4446   3346   9101   -853    706   -595       C  
ATOM   2863  CG2 ILE A1137     111.473 167.320 -11.514  1.00 37.05           C  
ANISOU 2863  CG2 ILE A1137     3629   2502   7947   -842    858   -569       C  
ATOM   2864  CD1 ILE A1137     109.797 165.109 -12.923  1.00 38.97           C  
ANISOU 2864  CD1 ILE A1137     3773   2636   8399   -886    681   -585       C  
ATOM   2865  N   PRO A1138     112.321 170.567 -12.599  1.00 40.23           N  
ANISOU 2865  N   PRO A1138     4083   2958   8246   -785    855   -586       N  
ATOM   2866  CA  PRO A1138     113.546 171.366 -12.521  1.00 41.41           C  
ANISOU 2866  CA  PRO A1138     4309   3155   8271   -775    886   -587       C  
ATOM   2867  C   PRO A1138     114.490 170.951 -11.403  1.00 40.49           C  
ANISOU 2867  C   PRO A1138     4224   3076   8083   -773    963   -589       C  
ATOM   2868  O   PRO A1138     114.089 170.666 -10.272  1.00 41.39           O  
ANISOU 2868  O   PRO A1138     4307   3183   8234   -774   1033   -582       O  
ATOM   2869  CB  PRO A1138     113.009 172.786 -12.286  1.00 35.06           C  
ANISOU 2869  CB  PRO A1138     3461   2336   7522   -753    930   -586       C  
ATOM   2870  CG  PRO A1138     111.615 172.606 -11.726  1.00 38.81           C  
ANISOU 2870  CG  PRO A1138     3827   2765   8153   -746    965   -591       C  
ATOM   2871  CD  PRO A1138     111.231 171.153 -11.805  1.00 40.22           C  
ANISOU 2871  CD  PRO A1138     3987   2926   8368   -770    928   -588       C  
ATOM   2872  N   ILE A1139     115.772 170.915 -11.751  1.00 38.56           N  
ANISOU 2872  N   ILE A1139     4048   2866   7737   -775    947   -601       N  
ATOM   2873  CA  ILE A1139     116.868 170.780 -10.800  1.00 38.32           C  
ANISOU 2873  CA  ILE A1139     4054   2871   7633   -768   1007   -611       C  
ATOM   2874  C   ILE A1139     117.558 172.136 -10.762  1.00 39.34           C  
ANISOU 2874  C   ILE A1139     4206   3029   7714   -751   1048   -622       C  
ATOM   2875  O   ILE A1139     118.384 172.446 -11.627  1.00 41.03           O  
ANISOU 2875  O   ILE A1139     4461   3259   7869   -757   1016   -634       O  
ATOM   2876  CB  ILE A1139     117.844 169.670 -11.197  1.00 32.96           C  
ANISOU 2876  CB  ILE A1139     3424   2204   6895   -782    956   -628       C  
ATOM   2877  CG1 ILE A1139     117.083 168.382 -11.515  1.00 38.75           C  
ANISOU 2877  CG1 ILE A1139     4139   2899   7686   -802    896   -618       C  
ATOM   2878  CG2 ILE A1139     118.867 169.452 -10.094  1.00 36.56           C  
ANISOU 2878  CG2 ILE A1139     3912   2684   7293   -775   1007   -639       C  
ATOM   2879  CD1 ILE A1139     117.883 167.390 -12.323  1.00 38.56           C  
ANISOU 2879  CD1 ILE A1139     4160   2876   7616   -814    822   -642       C  
ATOM   2880  N   ALA A1140     117.224 172.953  -9.767  1.00 38.94           N  
ANISOU 2880  N   ALA A1140     4128   2979   7687   -735   1122   -619       N  
ATOM   2881  CA  ALA A1140     117.633 174.348  -9.749  1.00 32.50           C  
ANISOU 2881  CA  ALA A1140     3322   2178   6848   -720   1156   -627       C  
ATOM   2882  C   ALA A1140     118.322 174.691  -8.437  1.00 32.20           C  
ANISOU 2882  C   ALA A1140     3299   2164   6773   -706   1234   -643       C  
ATOM   2883  O   ALA A1140     118.191 173.988  -7.432  1.00 32.33           O  
ANISOU 2883  O   ALA A1140     3316   2176   6792   -710   1270   -642       O  
ATOM   2884  CB  ALA A1140     116.434 175.282  -9.968  1.00 32.97           C  
ANISOU 2884  CB  ALA A1140     3334   2204   6989   -711   1155   -613       C  
ATOM   2885  N   SER A1141     119.061 175.797  -8.465  1.00 31.90           N  
ANISOU 2885  N   SER A1141     3279   2144   6699   -696   1257   -658       N  
ATOM   2886  CA  SER A1141     119.689 176.319  -7.262  1.00 40.95           C  
ANISOU 2886  CA  SER A1141     4437   3307   7817   -683   1323   -680       C  
ATOM   2887  C   SER A1141     118.636 176.865  -6.302  1.00 41.45           C  
ANISOU 2887  C   SER A1141     4464   3346   7941   -671   1384   -674       C  
ATOM   2888  O   SER A1141     117.571 177.336  -6.710  1.00 41.96           O  
ANISOU 2888  O   SER A1141     4485   3384   8074   -666   1377   -661       O  
ATOM   2889  CB  SER A1141     120.689 177.420  -7.620  1.00 40.67           C  
ANISOU 2889  CB  SER A1141     4422   3289   7743   -679   1329   -699       C  
ATOM   2890  OG  SER A1141     121.560 177.008  -8.660  1.00 40.16           O  
ANISOU 2890  OG  SER A1141     4386   3240   7632   -695   1283   -706       O  
ATOM   2891  N   ALA A1142     118.944 176.804  -5.008  1.00 40.63           N  
ANISOU 2891  N   ALA A1142     4381   3246   7812   -669   1442   -689       N  
ATOM   2892  CA  ALA A1142     118.032 177.299  -3.979  1.00 41.32           C  
ANISOU 2892  CA  ALA A1142     4443   3308   7948   -663   1515   -691       C  
ATOM   2893  C   ALA A1142     118.222 178.803  -3.775  1.00 42.25           C  
ANISOU 2893  C   ALA A1142     4545   3423   8085   -643   1553   -716       C  
ATOM   2894  O   ALA A1142     118.585 179.283  -2.701  1.00 43.11           O  
ANISOU 2894  O   ALA A1142     4668   3526   8187   -639   1619   -745       O  
ATOM   2895  CB  ALA A1142     118.236 176.532  -2.681  1.00 41.01           C  
ANISOU 2895  CB  ALA A1142     4442   3254   7884   -679   1574   -698       C  
ATOM   2896  N   VAL A1143     117.976 179.549  -4.846  1.00 41.16           N  
ANISOU 2896  N   VAL A1143     4384   3282   7974   -635   1505   -705       N  
ATOM   2897  CA  VAL A1143     118.090 180.997  -4.824  1.00 32.59           C  
ANISOU 2897  CA  VAL A1143     3285   2184   6915   -621   1526   -721       C  
ATOM   2898  C   VAL A1143     116.696 181.602  -5.000  1.00 39.73           C  
ANISOU 2898  C   VAL A1143     4115   3038   7944   -608   1549   -720       C  
ATOM   2899  O   VAL A1143     115.740 180.919  -5.366  1.00 39.81           O  
ANISOU 2899  O   VAL A1143     4084   3027   8017   -610   1534   -705       O  
ATOM   2900  CB  VAL A1143     119.085 181.518  -5.884  1.00 32.23           C  
ANISOU 2900  CB  VAL A1143     3277   2156   6815   -630   1465   -714       C  
ATOM   2901  CG1 VAL A1143     120.450 180.874  -5.677  1.00 31.77           C  
ANISOU 2901  CG1 VAL A1143     3260   2135   6676   -640   1463   -734       C  
ATOM   2902  CG2 VAL A1143     118.569 181.248  -7.288  1.00 41.63           C  
ANISOU 2902  CG2 VAL A1143     4464   3330   8024   -643   1393   -682       C  
ATOM   2903  N   GLY A1144     116.604 182.915  -4.763  1.00 40.88           N  
ANISOU 2903  N   GLY A1144     4237   3158   8137   -594   1579   -740       N  
ATOM   2904  CA  GLY A1144     115.325 183.540  -4.438  1.00 40.68           C  
ANISOU 2904  CA  GLY A1144     4127   3077   8254   -575   1634   -760       C  
ATOM   2905  C   GLY A1144     114.198 183.210  -5.398  1.00 40.60           C  
ANISOU 2905  C   GLY A1144     4059   3031   8335   -574   1580   -737       C  
ATOM   2906  O   GLY A1144     113.139 182.721  -4.991  1.00 40.75           O  
ANISOU 2906  O   GLY A1144     4005   3018   8461   -567   1633   -753       O  
ATOM   2907  N   GLY A1145     114.397 183.494  -6.686  1.00 40.86           N  
ANISOU 2907  N   GLY A1145     4126   3060   8340   -585   1477   -704       N  
ATOM   2908  CA  GLY A1145     113.336 183.252  -7.653  1.00 42.54           C  
ANISOU 2908  CA  GLY A1145     4287   3227   8650   -587   1410   -687       C  
ATOM   2909  C   GLY A1145     112.954 181.787  -7.761  1.00 43.24           C  
ANISOU 2909  C   GLY A1145     4359   3330   8738   -598   1399   -677       C  
ATOM   2910  O   GLY A1145     111.771 181.446  -7.843  1.00 40.44           O  
ANISOU 2910  O   GLY A1145     3918   2932   8517   -590   1401   -687       O  
ATOM   2911  N   LEU A1146     113.951 180.900  -7.757  1.00 43.95           N  
ANISOU 2911  N   LEU A1146     4527   3477   8694   -617   1383   -662       N  
ATOM   2912  CA  LEU A1146     113.690 179.472  -7.890  1.00 48.02           C  
ANISOU 2912  CA  LEU A1146     5038   4004   9202   -632   1361   -650       C  
ATOM   2913  C   LEU A1146     113.294 178.825  -6.568  1.00 53.18           C  
ANISOU 2913  C   LEU A1146     5659   4657   9893   -629   1461   -669       C  
ATOM   2914  O   LEU A1146     112.497 177.879  -6.565  1.00 54.58           O  
ANISOU 2914  O   LEU A1146     5792   4810  10135   -639   1462   -663       O  
ATOM   2915  CB  LEU A1146     114.917 178.773  -8.471  1.00 33.74           C  
ANISOU 2915  CB  LEU A1146     3324   2247   7249   -654   1299   -631       C  
ATOM   2916  CG  LEU A1146     115.421 179.416  -9.765  1.00 33.58           C  
ANISOU 2916  CG  LEU A1146     3356   2221   7181   -667   1219   -614       C  
ATOM   2917  CD1 LEU A1146     116.877 179.065 -10.040  1.00 33.82           C  
ANISOU 2917  CD1 LEU A1146     3463   2297   7090   -683   1209   -617       C  
ATOM   2918  CD2 LEU A1146     114.535 179.015 -10.937  1.00 34.16           C  
ANISOU 2918  CD2 LEU A1146     3406   2248   7323   -680   1134   -598       C  
ATOM   2919  N   ARG A1147     113.830 179.309  -5.442  1.00 56.14           N  
ANISOU 2919  N   ARG A1147     6057   5046  10229   -620   1547   -692       N  
ATOM   2920  CA  ARG A1147     113.454 178.736  -4.153  1.00 58.45           C  
ANISOU 2920  CA  ARG A1147     6335   5322  10552   -626   1654   -709       C  
ATOM   2921  C   ARG A1147     111.984 178.984  -3.843  1.00 61.19           C  
ANISOU 2921  C   ARG A1147     6575   5605  11070   -614   1729   -733       C  
ATOM   2922  O   ARG A1147     111.339 178.157  -3.187  1.00 60.11           O  
ANISOU 2922  O   ARG A1147     6414   5441  10984   -631   1799   -736       O  
ATOM   2923  CB  ARG A1147     114.330 179.302  -3.033  1.00 58.57           C  
ANISOU 2923  CB  ARG A1147     6402   5354  10498   -621   1730   -735       C  
ATOM   2924  CG  ARG A1147     114.143 178.600  -1.689  1.00 63.39           C  
ANISOU 2924  CG  ARG A1147     7032   5942  11110   -640   1840   -748       C  
ATOM   2925  CD  ARG A1147     114.550 179.486  -0.517  1.00 67.96           C  
ANISOU 2925  CD  ARG A1147     7633   6509  11679   -633   1942   -790       C  
ATOM   2926  NE  ARG A1147     115.998 179.618  -0.374  1.00 71.52           N  
ANISOU 2926  NE  ARG A1147     8166   7004  12003   -636   1892   -791       N  
ATOM   2927  CZ  ARG A1147     116.696 180.686  -0.751  1.00 74.45           C  
ANISOU 2927  CZ  ARG A1147     8541   7400  12347   -619   1848   -804       C  
ATOM   2928  NH1 ARG A1147     118.011 180.716  -0.576  1.00 74.51           N  
ANISOU 2928  NH1 ARG A1147     8614   7442  12254   -626   1807   -810       N  
ATOM   2929  NH2 ARG A1147     116.080 181.723  -1.301  1.00 76.05           N  
ANISOU 2929  NH2 ARG A1147     8680   7582  12632   -599   1842   -812       N  
ATOM   2930  N   ASP A1148     111.438 180.112  -4.302  1.00 66.94           N  
ANISOU 2930  N   ASP A1148     7236   6301  11898   -590   1716   -751       N  
ATOM   2931  CA  ASP A1148     110.019 180.381  -4.093  1.00 72.16           C  
ANISOU 2931  CA  ASP A1148     7774   6892  12750   -575   1780   -785       C  
ATOM   2932  C   ASP A1148     109.150 179.417  -4.889  1.00 69.49           C  
ANISOU 2932  C   ASP A1148     7379   6528  12495   -587   1714   -766       C  
ATOM   2933  O   ASP A1148     108.139 178.917  -4.383  1.00 70.84           O  
ANISOU 2933  O   ASP A1148     7472   6652  12792   -591   1791   -788       O  
ATOM   2934  CB  ASP A1148     109.693 181.824  -4.483  1.00 81.19           C  
ANISOU 2934  CB  ASP A1148     8857   8001  13990   -546   1760   -809       C  
ATOM   2935  CG  ASP A1148     110.345 182.837  -3.566  1.00 84.86           C  
ANISOU 2935  CG  ASP A1148     9356   8476  14412   -535   1841   -839       C  
ATOM   2936  OD1 ASP A1148     110.965 182.428  -2.561  1.00 85.80           O  
ANISOU 2936  OD1 ASP A1148     9539   8624  14439   -548   1923   -848       O  
ATOM   2937  OD2 ASP A1148     110.230 184.048  -3.852  1.00 86.17           O  
ANISOU 2937  OD2 ASP A1148     9485   8615  14639   -517   1817   -855       O  
ATOM   2938  N   ILE A1149     109.536 179.141  -6.133  1.00 62.43           N  
ANISOU 2938  N   ILE A1149     6524   5659  11536   -596   1576   -729       N  
ATOM   2939  CA  ILE A1149     108.675 178.385  -7.036  1.00 58.41           C  
ANISOU 2939  CA  ILE A1149     5953   5116  11125   -605   1495   -719       C  
ATOM   2940  C   ILE A1149     108.793 176.888  -6.780  1.00 56.36           C  
ANISOU 2940  C   ILE A1149     5730   4879  10805   -637   1501   -696       C  
ATOM   2941  O   ILE A1149     107.785 176.178  -6.685  1.00 56.26           O  
ANISOU 2941  O   ILE A1149     5637   4821  10916   -648   1522   -705       O  
ATOM   2942  CB  ILE A1149     109.009 178.736  -8.497  1.00 56.53           C  
ANISOU 2942  CB  ILE A1149     5752   4881  10846   -607   1349   -693       C  
ATOM   2943  CG1 ILE A1149     108.869 180.242  -8.715  1.00 56.40           C  
ANISOU 2943  CG1 ILE A1149     5708   4830  10892   -582   1338   -709       C  
ATOM   2944  CG2 ILE A1149     108.120 177.950  -9.447  1.00 56.86           C  
ANISOU 2944  CG2 ILE A1149     5730   4879  10996   -616   1255   -690       C  
ATOM   2945  CD1 ILE A1149     109.384 180.720 -10.047  1.00 56.64           C  
ANISOU 2945  CD1 ILE A1149     5814   4856  10851   -593   1208   -677       C  
ATOM   2946  N   ILE A1150     110.018 176.385  -6.673  1.00 56.49           N  
ANISOU 2946  N   ILE A1150     6368   4574  10523      1   2130   -391       N  
ATOM   2947  CA  ILE A1150     110.239 174.948  -6.557  1.00 55.07           C  
ANISOU 2947  CA  ILE A1150     6238   4372  10313    -31   2168   -363       C  
ATOM   2948  C   ILE A1150     110.089 174.529  -5.100  1.00 56.19           C  
ANISOU 2948  C   ILE A1150     6565   4399  10384    -67   2383   -353       C  
ATOM   2949  O   ILE A1150     110.718 175.105  -4.205  1.00 55.76           O  
ANISOU 2949  O   ILE A1150     6714   4302  10172    -46   2371   -326       O  
ATOM   2950  CB  ILE A1150     111.619 174.567  -7.116  1.00 50.40           C  
ANISOU 2950  CB  ILE A1150     5735   3851   9565      7   1952   -284       C  
ATOM   2951  CG1 ILE A1150     111.702 174.931  -8.602  1.00 48.36           C  
ANISOU 2951  CG1 ILE A1150     5326   3681   9365     46   1791   -289       C  
ATOM   2952  CG2 ILE A1150     111.891 173.087  -6.901  1.00 50.04           C  
ANISOU 2952  CG2 ILE A1150     5763   3767   9483    -22   1987   -251       C  
ATOM   2953  CD1 ILE A1150     112.935 175.721  -8.975  1.00 47.86           C  
ANISOU 2953  CD1 ILE A1150     5336   3680   9169     98   1627   -224       C  
ATOM   2954  N   THR A1151     109.246 173.528  -4.861  1.00 58.45           N  
ANISOU 2954  N   THR A1151     6797   4615  10797   -121   2586   -380       N  
ATOM   2955  CA  THR A1151     108.958 173.013  -3.532  1.00 62.03           C  
ANISOU 2955  CA  THR A1151     7442   4935  11193   -158   2853   -360       C  
ATOM   2956  C   THR A1151     109.609 171.642  -3.352  1.00 64.60           C  
ANISOU 2956  C   THR A1151     7912   5223  11411   -170   2826   -279       C  
ATOM   2957  O   THR A1151     110.439 171.210  -4.163  1.00 63.71           O  
ANISOU 2957  O   THR A1151     7767   5193  11246   -144   2585   -241       O  
ATOM   2958  CB  THR A1151     107.444 172.957  -3.307  1.00 63.29           C  
ANISOU 2958  CB  THR A1151     7425   5014  11610   -215   3164   -450       C  
ATOM   2959  OG1 THR A1151     106.816 172.317  -4.424  1.00 63.68           O  
ANISOU 2959  OG1 THR A1151     7186   5106  11904   -239   3108   -513       O  
ATOM   2960  CG2 THR A1151     106.872 174.359  -3.146  1.00 63.89           C  
ANISOU 2960  CG2 THR A1151     7424   5090  11761   -206   3221   -516       C  
ATOM   2961  N   ASN A1152     109.226 170.952  -2.274  1.00 66.54           N  
ANISOU 2961  N   ASN A1152     8330   5330  11623   -206   3096   -246       N  
ATOM   2962  CA  ASN A1152     109.789 169.643  -1.968  1.00 65.17           C  
ANISOU 2962  CA  ASN A1152     8323   5092  11345   -216   3093   -153       C  
ATOM   2963  C   ASN A1152     109.180 168.531  -2.811  1.00 64.47           C  
ANISOU 2963  C   ASN A1152     8005   5017  11473   -257   3129   -194       C  
ATOM   2964  O   ASN A1152     109.813 167.482  -2.983  1.00 64.88           O  
ANISOU 2964  O   ASN A1152     8132   5057  11461   -257   3027   -127       O  
ATOM   2965  CB  ASN A1152     109.606 169.334  -0.481  1.00 70.73           C  
ANISOU 2965  CB  ASN A1152     9343   5621  11910   -230   3390    -84       C  
ATOM   2966  CG  ASN A1152     110.218 168.004  -0.080  1.00 77.35           C  
ANISOU 2966  CG  ASN A1152    10389   6376  12625   -231   3383     38       C  
ATOM   2967  OD1 ASN A1152     111.434 167.832  -0.127  1.00 78.90           O  
ANISOU 2967  OD1 ASN A1152    10723   6596  12658   -184   3110    115       O  
ATOM   2968  ND2 ASN A1152     109.375 167.058   0.319  1.00 80.90           N  
ANISOU 2968  ND2 ASN A1152    10851   6711  13177   -279   3689     53       N  
ATOM   2969  N   GLU A1153     107.977 168.733  -3.344  1.00 63.12           N  
ANISOU 2969  N   GLU A1153     7553   4855  11576   -289   3259   -313       N  
ATOM   2970  CA  GLU A1153     107.318 167.741  -4.183  1.00 62.25           C  
ANISOU 2970  CA  GLU A1153     7203   4735  11715   -324   3273   -387       C  
ATOM   2971  C   GLU A1153     107.303 168.119  -5.658  1.00 57.16           C  
ANISOU 2971  C   GLU A1153     6298   4221  11201   -300   3001   -472       C  
ATOM   2972  O   GLU A1153     106.724 167.380  -6.462  1.00 55.98           O  
ANISOU 2972  O   GLU A1153     5938   4055  11277   -325   2979   -561       O  
ATOM   2973  CB  GLU A1153     105.883 167.505  -3.696  1.00 67.66           C  
ANISOU 2973  CB  GLU A1153     7743   5289  12677   -374   3633   -481       C  
ATOM   2974  CG  GLU A1153     105.785 166.631  -2.457  1.00 74.10           C  
ANISOU 2974  CG  GLU A1153     8809   5941  13405   -405   3939   -395       C  
ATOM   2975  CD  GLU A1153     104.352 166.394  -2.022  1.00 80.97           C  
ANISOU 2975  CD  GLU A1153     9525   6661  14580   -442   4323   -500       C  
ATOM   2976  OE1 GLU A1153     103.575 167.371  -1.971  1.00 82.74           O  
ANISOU 2976  OE1 GLU A1153     9592   6880  14964   -432   4448   -602       O  
ATOM   2977  OE2 GLU A1153     104.000 165.230  -1.737  1.00 83.29           O  
ANISOU 2977  OE2 GLU A1153     9846   6827  14974   -478   4504   -484       O  
ATOM   2978  N   THR A1154     107.913 169.243  -6.038  1.00 53.21           N  
ANISOU 2978  N   THR A1154     5819   3830  10569   -249   2796   -452       N  
ATOM   2979  CA  THR A1154     107.929 169.699  -7.425  1.00 50.26           C  
ANISOU 2979  CA  THR A1154     5249   3563  10286   -218   2553   -512       C  
ATOM   2980  C   THR A1154     109.331 170.117  -7.843  1.00 48.66           C  
ANISOU 2980  C   THR A1154     5200   3463   9826   -154   2297   -420       C  
ATOM   2981  O   THR A1154     109.550 171.218  -8.351  1.00 50.78           O  
ANISOU 2981  O   THR A1154     5431   3807  10056   -111   2163   -422       O  
ATOM   2982  CB  THR A1154     106.966 170.863  -7.656  1.00 49.70           C  
ANISOU 2982  CB  THR A1154     4983   3500  10400   -220   2589   -601       C  
ATOM   2983  OG1 THR A1154     107.428 172.015  -6.939  1.00 49.72           O  
ANISOU 2983  OG1 THR A1154     5146   3527  10218   -188   2599   -539       O  
ATOM   2984  CG2 THR A1154     105.563 170.510  -7.194  1.00 51.82           C  
ANISOU 2984  CG2 THR A1154     5064   3653  10973   -283   2870   -707       C  
ATOM   2985  N   GLY A1155     110.309 169.240  -7.641  1.00 44.09           N  
ANISOU 2985  N   GLY A1155     4788   2878   9087   -146   2235   -338       N  
ATOM   2986  CA  GLY A1155     111.651 169.469  -8.134  1.00 38.66           C  
ANISOU 2986  CA  GLY A1155     4202   2275   8211    -89   2007   -265       C  
ATOM   2987  C   GLY A1155     112.695 169.287  -7.055  1.00 48.74           C  
ANISOU 2987  C   GLY A1155     5726   3510   9281    -76   1992   -162       C  
ATOM   2988  O   GLY A1155     112.395 169.036  -5.888  1.00 40.01           O  
ANISOU 2988  O   GLY A1155     4758   2304   8142   -106   2157   -135       O  
ATOM   2989  N   ILE A1156     113.952 169.435  -7.469  1.00 46.61           N  
ANISOU 2989  N   ILE A1156     5520   3304   8885    -26   1794   -106       N  
ATOM   2990  CA  ILE A1156     115.109 169.218  -6.610  1.00 43.49           C  
ANISOU 2990  CA  ILE A1156     5337   2859   8329     -4   1714    -18       C  
ATOM   2991  C   ILE A1156     115.901 170.517  -6.519  1.00 42.11           C  
ANISOU 2991  C   ILE A1156     5197   2732   8071     39   1581     -5       C  
ATOM   2992  O   ILE A1156     116.216 171.133  -7.544  1.00 41.58           O  
ANISOU 2992  O   ILE A1156     5002   2764   8032     68   1482    -21       O  
ATOM   2993  CB  ILE A1156     115.998 168.078  -7.138  1.00 40.32           C  
ANISOU 2993  CB  ILE A1156     4958   2461   7900     13   1604     27       C  
ATOM   2994  CG1 ILE A1156     115.165 166.816  -7.369  1.00 40.06           C  
ANISOU 2994  CG1 ILE A1156     4865   2374   7981    -33   1730     -4       C  
ATOM   2995  CG2 ILE A1156     117.141 167.808  -6.175  1.00 39.62           C  
ANISOU 2995  CG2 ILE A1156     5083   2291   7679     41   1510    116       C  
ATOM   2996  CD1 ILE A1156     115.397 166.188  -8.720  1.00 37.42           C  
ANISOU 2996  CD1 ILE A1156     4400   2098   7718    -17   1637    -43       C  
ATOM   2997  N   LEU A1157     116.224 170.927  -5.296  1.00 41.81           N  
ANISOU 2997  N   LEU A1157     5345   2604   7939     44   1587     23       N  
ATOM   2998  CA  LEU A1157     116.994 172.136  -5.053  1.00 40.38           C  
ANISOU 2998  CA  LEU A1157     5209   2432   7703     80   1457     20       C  
ATOM   2999  C   LEU A1157     118.376 171.779  -4.523  1.00 40.53           C  
ANISOU 2999  C   LEU A1157     5387   2376   7636    115   1287     82       C  
ATOM   3000  O   LEU A1157     118.546 170.793  -3.800  1.00 41.78           O  
ANISOU 3000  O   LEU A1157     5710   2426   7738    115   1303    135       O  
ATOM   3001  CB  LEU A1157     116.282 173.062  -4.062  1.00 41.67           C  
ANISOU 3001  CB  LEU A1157     5464   2519   7848     68   1577    -26       C  
ATOM   3002  CG  LEU A1157     115.023 173.783  -4.557  1.00 41.94           C  
ANISOU 3002  CG  LEU A1157     5319   2618   7998     47   1719    -98       C  
ATOM   3003  CD1 LEU A1157     114.310 174.484  -3.410  1.00 44.21           C  
ANISOU 3003  CD1 LEU A1157     5728   2803   8267     34   1887   -146       C  
ATOM   3004  CD2 LEU A1157     115.356 174.777  -5.662  1.00 40.30           C  
ANISOU 3004  CD2 LEU A1157     4942   2528   7842     79   1585   -114       C  
ATOM   3005  N   VAL A1158     119.365 172.592  -4.896  1.00 36.49           N  
ANISOU 3005  N   VAL A1158     4820   1907   7136    149   1130     79       N  
ATOM   3006  CA  VAL A1158     120.756 172.396  -4.515  1.00 36.98           C  
ANISOU 3006  CA  VAL A1158     4982   1896   7174    189    953    120       C  
ATOM   3007  C   VAL A1158     121.367 173.750  -4.169  1.00 42.52           C  
ANISOU 3007  C   VAL A1158     5692   2564   7901    208    847     78       C  
ATOM   3008  O   VAL A1158     120.722 174.795  -4.282  1.00 43.58           O  
ANISOU 3008  O   VAL A1158     5759   2741   8060    191    914     25       O  
ATOM   3009  CB  VAL A1158     121.573 171.703  -5.625  1.00 36.07           C  
ANISOU 3009  CB  VAL A1158     4723   1870   7111    207    887    158       C  
ATOM   3010  CG1 VAL A1158     121.131 170.262  -5.792  1.00 36.26           C  
ANISOU 3010  CG1 VAL A1158     4776   1884   7116    193    963    190       C  
ATOM   3011  CG2 VAL A1158     121.438 172.463  -6.937  1.00 35.93           C  
ANISOU 3011  CG2 VAL A1158     4485   2001   7168    201    923    131       C  
ATOM   3012  N   LYS A1159     122.625 173.721  -3.735  1.00 44.07           N  
ANISOU 3012  N   LYS A1159     5961   2667   8117    247    678     96       N  
ATOM   3013  CA  LYS A1159     123.376 174.943  -3.491  1.00 44.80           C  
ANISOU 3013  CA  LYS A1159     6022   2715   8286    262    562     45       C  
ATOM   3014  C   LYS A1159     123.822 175.538  -4.820  1.00 46.30           C  
ANISOU 3014  C   LYS A1159     5935   3058   8599    245    577     53       C  
ATOM   3015  O   LYS A1159     124.175 174.811  -5.752  1.00 48.12           O  
ANISOU 3015  O   LYS A1159     6041   3379   8864    250    600    104       O  
ATOM   3016  CB  LYS A1159     124.588 174.660  -2.604  1.00 46.77           C  
ANISOU 3016  CB  LYS A1159     6411   2794   8565    316    369     52       C  
ATOM   3017  CG  LYS A1159     125.247 175.915  -2.053  1.00 51.40           C  
ANISOU 3017  CG  LYS A1159     6991   3284   9254    327    235    -35       C  
ATOM   3018  CD  LYS A1159     126.609 175.621  -1.448  1.00 56.80           C  
ANISOU 3018  CD  LYS A1159     7705   3825  10052    387      3    -39       C  
ATOM   3019  CE  LYS A1159     127.270 176.893  -0.937  1.00 61.41           C  
ANISOU 3019  CE  LYS A1159     8229   4312  10793    385   -165   -157       C  
ATOM   3020  NZ  LYS A1159     127.318 177.955  -1.981  1.00 62.17           N  
ANISOU 3020  NZ  LYS A1159     8038   4557  11028    317    -73   -175       N  
ATOM   3021  N   ALA A1160     123.813 176.872  -4.898  1.00 44.12           N  
ANISOU 3021  N   ALA A1160     5579   2793   8393    231    576      4       N  
ATOM   3022  CA  ALA A1160     124.005 177.547  -6.180  1.00 43.37           C  
ANISOU 3022  CA  ALA A1160     5250   2824   8403    218    635     26       C  
ATOM   3023  C   ALA A1160     125.409 177.334  -6.742  1.00 45.68           C  
ANISOU 3023  C   ALA A1160     5394   3120   8841    229    561     68       C  
ATOM   3024  O   ALA A1160     125.566 177.061  -7.938  1.00 46.32           O  
ANISOU 3024  O   ALA A1160     5333   3303   8963    231    643    119       O  
ATOM   3025  CB  ALA A1160     123.705 179.038  -6.034  1.00 43.12           C  
ANISOU 3025  CB  ALA A1160     5184   2774   8428    204    653    -29       C  
ATOM   3026  N   GLY A1161     126.439 177.451  -5.915  1.00 47.56           N  
ANISOU 3026  N   GLY A1161     5658   3232   9183    240    407     39       N  
ATOM   3027  CA  GLY A1161     127.766 177.360  -6.482  1.00 52.76           C  
ANISOU 3027  CA  GLY A1161     6116   3886  10046    244    349     71       C  
ATOM   3028  C   GLY A1161     128.442 176.013  -6.394  1.00 55.78           C  
ANISOU 3028  C   GLY A1161     6518   4238  10438    279    277    115       C  
ATOM   3029  O   GLY A1161     129.644 175.922  -6.675  1.00 59.90           O  
ANISOU 3029  O   GLY A1161     6864   4725  11171    287    206    130       O  
ATOM   3030  N   ASP A1162     127.709 174.962  -6.026  1.00 54.74           N  
ANISOU 3030  N   ASP A1162     6580   4107  10111    300    302    138       N  
ATOM   3031  CA  ASP A1162     128.313 173.670  -5.744  1.00 53.89           C  
ANISOU 3031  CA  ASP A1162     6534   3938  10003    345    220    181       C  
ATOM   3032  C   ASP A1162     128.113 172.730  -6.925  1.00 50.16           C  
ANISOU 3032  C   ASP A1162     5974   3591   9494    342    356    234       C  
ATOM   3033  O   ASP A1162     126.966 172.356  -7.219  1.00 48.28           O  
ANISOU 3033  O   ASP A1162     5817   3425   9102    323    474    236       O  
ATOM   3034  CB  ASP A1162     127.704 173.074  -4.475  1.00 55.82           C  
ANISOU 3034  CB  ASP A1162     7082   4057  10070    378    164    181       C  
ATOM   3035  CG  ASP A1162     128.509 171.910  -3.929  1.00 60.63           C  
ANISOU 3035  CG  ASP A1162     7785   4551  10702    448     31    232       C  
ATOM   3036  OD1 ASP A1162     129.536 171.550  -4.547  1.00 62.37           O  
ANISOU 3036  OD1 ASP A1162     7807   4800  11090    466    -21    256       O  
ATOM   3037  OD2 ASP A1162     128.115 171.354  -2.880  1.00 63.46           O  
ANISOU 3037  OD2 ASP A1162     8421   4774  10917    493    -11    256       O  
ATOM   3038  N   PRO A1163     129.176 172.339  -7.636  1.00 48.02           N  
ANISOU 3038  N   PRO A1163     5527   3334   9383    358    345    265       N  
ATOM   3039  CA  PRO A1163     129.015 171.419  -8.768  1.00 45.99           C  
ANISOU 3039  CA  PRO A1163     5211   3172   9090    362    473    300       C  
ATOM   3040  C   PRO A1163     128.816 169.991  -8.298  1.00 48.36           C  
ANISOU 3040  C   PRO A1163     5672   3419   9282    397    438    325       C  
ATOM   3041  O   PRO A1163     128.201 169.170  -8.984  1.00 47.11           O  
ANISOU 3041  O   PRO A1163     5536   3325   9039    392    543    333       O  
ATOM   3042  CB  PRO A1163     130.334 171.575  -9.542  1.00 46.78           C  
ANISOU 3042  CB  PRO A1163     5079   3267   9429    369    483    323       C  
ATOM   3043  CG  PRO A1163     130.988 172.816  -8.974  1.00 48.71           C  
ANISOU 3043  CG  PRO A1163     5216   3440   9851    349    383    293       C  
ATOM   3044  CD  PRO A1163     130.541 172.878  -7.554  1.00 49.41           C  
ANISOU 3044  CD  PRO A1163     5515   3437   9821    365    232    255       C  
ATOM   3045  N   GLY A1164     129.376 169.685  -7.126  1.00 49.71           N  
ANISOU 3045  N   GLY A1164     5960   3453   9473    441    280    338       N  
ATOM   3046  CA  GLY A1164     129.235 168.353  -6.564  1.00 46.68           C  
ANISOU 3046  CA  GLY A1164     5763   2987   8988    486    245    381       C  
ATOM   3047  C   GLY A1164     127.838 168.074  -6.053  1.00 45.98           C  
ANISOU 3047  C   GLY A1164     5893   2887   8689    456    330    381       C  
ATOM   3048  O   GLY A1164     127.351 166.944  -6.150  1.00 47.00           O  
ANISOU 3048  O   GLY A1164     6112   3004   8742    457    395    410       O  
ATOM   3049  N   GLU A1165     127.170 169.097  -5.517  1.00 46.77           N  
ANISOU 3049  N   GLU A1165     6065   2981   8726    422    342    343       N  
ATOM   3050  CA  GLU A1165     125.790 168.934  -5.076  1.00 45.92           C  
ANISOU 3050  CA  GLU A1165     6121   2862   8463    382    451    337       C  
ATOM   3051  C   GLU A1165     124.837 168.874  -6.262  1.00 41.41           C  
ANISOU 3051  C   GLU A1165     5392   2454   7889    324    614    305       C  
ATOM   3052  O   GLU A1165     123.753 168.289  -6.155  1.00 41.24           O  
ANISOU 3052  O   GLU A1165     5440   2431   7800    290    721    303       O  
ATOM   3053  CB  GLU A1165     125.416 170.074  -4.131  1.00 50.22           C  
ANISOU 3053  CB  GLU A1165     6788   3333   8962    373    419    297       C  
ATOM   3054  CG  GLU A1165     124.239 169.772  -3.220  1.00 57.13           C  
ANISOU 3054  CG  GLU A1165     7892   4116   9699    351    513    308       C  
ATOM   3055  CD  GLU A1165     124.019 170.850  -2.176  1.00 63.47           C  
ANISOU 3055  CD  GLU A1165     8854   4804  10459    360    474    261       C  
ATOM   3056  OE1 GLU A1165     125.017 171.389  -1.648  1.00 66.64           O  
ANISOU 3056  OE1 GLU A1165     9309   5100  10911    418    302    242       O  
ATOM   3057  OE2 GLU A1165     122.844 171.160  -1.884  1.00 64.34           O  
ANISOU 3057  OE2 GLU A1165     9017   4922  10508    314    625    233       O  
ATOM   3058  N   LEU A1166     125.222 169.469  -7.394  1.00 39.48           N  
ANISOU 3058  N   LEU A1166     4935   2329   7735    319    637    283       N  
ATOM   3059  CA  LEU A1166     124.434 169.337  -8.615  1.00 39.24           C  
ANISOU 3059  CA  LEU A1166     4780   2423   7706    291    766    257       C  
ATOM   3060  C   LEU A1166     124.635 167.966  -9.252  1.00 44.03           C  
ANISOU 3060  C   LEU A1166     5368   3029   8330    308    793    275       C  
ATOM   3061  O   LEU A1166     123.696 167.404  -9.830  1.00 46.15           O  
ANISOU 3061  O   LEU A1166     5620   3337   8579    285    886    246       O  
ATOM   3062  CB  LEU A1166     124.800 170.447  -9.603  1.00 35.64           C  
ANISOU 3062  CB  LEU A1166     4151   2060   7329    292    790    244       C  
ATOM   3063  CG  LEU A1166     124.099 170.428 -10.964  1.00 33.32           C  
ANISOU 3063  CG  LEU A1166     3758   1865   7036    287    901    225       C  
ATOM   3064  CD1 LEU A1166     122.587 170.462 -10.794  1.00 32.94           C  
ANISOU 3064  CD1 LEU A1166     3756   1836   6925    255    969    181       C  
ATOM   3065  CD2 LEU A1166     124.574 171.588 -11.826  1.00 33.03           C  
ANISOU 3065  CD2 LEU A1166     3598   1881   7070    296    932    237       C  
ATOM   3066  N   ALA A1167     125.851 167.417  -9.152  1.00 44.42           N  
ANISOU 3066  N   ALA A1167     5414   3022   8444    352    711    313       N  
ATOM   3067  CA  ALA A1167     126.112 166.073  -9.658  1.00 42.61           C  
ANISOU 3067  CA  ALA A1167     5181   2769   8239    375    734    328       C  
ATOM   3068  C   ALA A1167     125.329 165.030  -8.872  1.00 43.92           C  
ANISOU 3068  C   ALA A1167     5520   2846   8322    361    752    344       C  
ATOM   3069  O   ALA A1167     124.801 164.075  -9.454  1.00 44.78           O  
ANISOU 3069  O   ALA A1167     5614   2961   8439    346    830    324       O  
ATOM   3070  CB  ALA A1167     127.610 165.775  -9.608  1.00 37.38           C  
ANISOU 3070  CB  ALA A1167     4465   2048   7691    432    641    368       C  
ATOM   3071  N   ASN A1168     125.236 165.198  -7.550  1.00 45.33           N  
ANISOU 3071  N   ASN A1168     5871   2920   8431    364    690    380       N  
ATOM   3072  CA  ASN A1168     124.427 164.285  -6.749  1.00 47.22           C  
ANISOU 3072  CA  ASN A1168     6291   3054   8596    343    741    412       C  
ATOM   3073  C   ASN A1168     122.954 164.379  -7.125  1.00 44.03           C  
ANISOU 3073  C   ASN A1168     5826   2721   8183    268    901    356       C  
ATOM   3074  O   ASN A1168     122.262 163.358  -7.211  1.00 42.70           O  
ANISOU 3074  O   ASN A1168     5680   2511   8032    236    997    355       O  
ATOM   3075  CB  ASN A1168     124.618 164.581  -5.260  1.00 53.35           C  
ANISOU 3075  CB  ASN A1168     7300   3681   9291    373    651    470       C  
ATOM   3076  CG  ASN A1168     126.049 164.382  -4.805  1.00 59.62           C  
ANISOU 3076  CG  ASN A1168     8163   4370  10118    469    473    523       C  
ATOM   3077  OD1 ASN A1168     126.684 163.380  -5.134  1.00 60.29           O  
ANISOU 3077  OD1 ASN A1168     8227   4424  10257    514    442    557       O  
ATOM   3078  ND2 ASN A1168     126.567 165.343  -4.048  1.00 63.37           N  
ANISOU 3078  ND2 ASN A1168     8710   4781  10588    510    354    523       N  
ATOM   3079  N   ALA A1169     122.460 165.598  -7.359  1.00 42.14           N  
ANISOU 3079  N   ALA A1169     5496   2574   7940    242    933    306       N  
ATOM   3080  CA  ALA A1169     121.052 165.776  -7.701  1.00 39.98           C  
ANISOU 3080  CA  ALA A1169     5146   2357   7686    184   1077    247       C  
ATOM   3081  C   ALA A1169     120.720 165.181  -9.062  1.00 38.87           C  
ANISOU 3081  C   ALA A1169     4851   2291   7628    177   1127    193       C  
ATOM   3082  O   ALA A1169     119.593 164.721  -9.275  1.00 40.09           O  
ANISOU 3082  O   ALA A1169     4962   2435   7837    132   1237    145       O  
ATOM   3083  CB  ALA A1169     120.686 167.257  -7.675  1.00 37.72           C  
ANISOU 3083  CB  ALA A1169     4801   2142   7391    174   1085    208       C  
ATOM   3084  N   ILE A1170     121.673 165.194  -9.995  1.00 37.48           N  
ANISOU 3084  N   ILE A1170     4591   2171   7478    221   1058    194       N  
ATOM   3085  CA  ILE A1170     121.450 164.560 -11.287  1.00 38.98           C  
ANISOU 3085  CA  ILE A1170     4680   2398   7734    226   1099    142       C  
ATOM   3086  C   ILE A1170     121.488 163.046 -11.154  1.00 40.94           C  
ANISOU 3086  C   ILE A1170     4990   2550   8015    222   1119    150       C  
ATOM   3087  O   ILE A1170     120.873 162.333 -11.956  1.00 41.15           O  
ANISOU 3087  O   ILE A1170     4960   2566   8110    205   1173     84       O  
ATOM   3088  CB  ILE A1170     122.478 165.101 -12.294  1.00 39.96           C  
ANISOU 3088  CB  ILE A1170     4717   2591   7875    278   1052    150       C  
ATOM   3089  CG1 ILE A1170     122.167 166.573 -12.573  1.00 33.76           C  
ANISOU 3089  CG1 ILE A1170     3866   1888   7075    274   1060    137       C  
ATOM   3090  CG2 ILE A1170     122.486 164.288 -13.586  1.00 41.64           C  
ANISOU 3090  CG2 ILE A1170     4880   2804   8139    303   1086    102       C  
ATOM   3091  CD1 ILE A1170     123.300 167.326 -13.203  1.00 41.25           C  
ANISOU 3091  CD1 ILE A1170     4747   2879   8046    315   1033    173       C  
ATOM   3092  N   LEU A1171     122.177 162.532 -10.136  1.00 43.05           N  
ANISOU 3092  N   LEU A1171     5387   2726   8244    240   1068    225       N  
ATOM   3093  CA  LEU A1171     122.123 161.102  -9.862  1.00 44.13           C  
ANISOU 3093  CA  LEU A1171     5608   2748   8412    234   1097    248       C  
ATOM   3094  C   LEU A1171     120.789 160.715  -9.234  1.00 46.14           C  
ANISOU 3094  C   LEU A1171     5912   2935   8683    162   1222    235       C  
ATOM   3095  O   LEU A1171     120.241 159.647  -9.535  1.00 47.57           O  
ANISOU 3095  O   LEU A1171     6074   3051   8947    130   1300    202       O  
ATOM   3096  CB  LEU A1171     123.289 160.705  -8.956  1.00 43.87           C  
ANISOU 3096  CB  LEU A1171     5717   2615   8338    292    991    344       C  
ATOM   3097  CG  LEU A1171     124.670 160.602  -9.613  1.00 43.31           C  
ANISOU 3097  CG  LEU A1171     5570   2568   8317    365    899    355       C  
ATOM   3098  CD1 LEU A1171     125.752 160.702  -8.556  1.00 44.20           C  
ANISOU 3098  CD1 LEU A1171     5803   2587   8402    429    766    440       C  
ATOM   3099  CD2 LEU A1171     124.792 159.298 -10.383  1.00 44.32           C  
ANISOU 3099  CD2 LEU A1171     5667   2648   8523    381    942    329       C  
ATOM   3100  N   LYS A1172     120.247 161.572  -8.362  1.00 46.71           N  
ANISOU 3100  N   LYS A1172     6042   3010   8697    134   1259    254       N  
ATOM   3101  CA  LYS A1172     118.947 161.294  -7.759  1.00 46.65           C  
ANISOU 3101  CA  LYS A1172     6062   2934   8728     63   1423    241       C  
ATOM   3102  C   LYS A1172     117.824 161.367  -8.784  1.00 45.02           C  
ANISOU 3102  C   LYS A1172     5656   2796   8652     16   1514    121       C  
ATOM   3103  O   LYS A1172     116.860 160.599  -8.700  1.00 45.31           O  
ANISOU 3103  O   LYS A1172     5660   2756   8801    -42   1649     83       O  
ATOM   3104  CB  LYS A1172     118.679 162.268  -6.613  1.00 48.20           C  
ANISOU 3104  CB  LYS A1172     6372   3107   8833     53   1458    283       C  
ATOM   3105  CG  LYS A1172     119.573 162.071  -5.403  1.00 50.86           C  
ANISOU 3105  CG  LYS A1172     6952   3319   9054     97   1373    401       C  
ATOM   3106  CD  LYS A1172     119.406 163.208  -4.412  1.00 52.67           C  
ANISOU 3106  CD  LYS A1172     7298   3524   9191    100   1384    422       C  
ATOM   3107  CE  LYS A1172     120.081 162.898  -3.087  1.00 55.53           C  
ANISOU 3107  CE  LYS A1172     7945   3712   9441    150   1316    544       C  
ATOM   3108  NZ  LYS A1172     119.399 161.779  -2.380  1.00 58.23           N  
ANISOU 3108  NZ  LYS A1172     8436   3914   9776    117   1503    623       N  
ATOM   3109  N   ALA A1173     117.927 162.282  -9.753  1.00 44.73           N  
ANISOU 3109  N   ALA A1173     5490   2884   8622     43   1441     61       N  
ATOM   3110  CA  ALA A1173     116.909 162.373 -10.794  1.00 46.98           C  
ANISOU 3110  CA  ALA A1173     5604   3211   9036     15   1487    -56       C  
ATOM   3111  C   ALA A1173     116.895 161.129 -11.672  1.00 50.02           C  
ANISOU 3111  C   ALA A1173     5941   3541   9522     11   1479   -117       C  
ATOM   3112  O   ALA A1173     115.835 160.738 -12.172  1.00 51.28           O  
ANISOU 3112  O   ALA A1173     5987   3664   9835    -35   1540   -223       O  
ATOM   3113  CB  ALA A1173     117.132 163.625 -11.643  1.00 36.94           C  
ANISOU 3113  CB  ALA A1173     4247   2061   7729     59   1400    -86       C  
ATOM   3114  N   LEU A1174     118.053 160.496 -11.866  1.00 52.42           N  
ANISOU 3114  N   LEU A1174     6323   3827   9769     60   1402    -65       N  
ATOM   3115  CA  LEU A1174     118.099 159.247 -12.619  1.00 52.91           C  
ANISOU 3115  CA  LEU A1174     6362   3816   9927     60   1403   -125       C  
ATOM   3116  C   LEU A1174     117.445 158.113 -11.838  1.00 53.99           C  
ANISOU 3116  C   LEU A1174     6543   3814  10155     -6   1516   -114       C  
ATOM   3117  O   LEU A1174     116.645 157.348 -12.390  1.00 56.39           O  
ANISOU 3117  O   LEU A1174     6758   4051  10617    -52   1571   -219       O  
ATOM   3118  CB  LEU A1174     119.547 158.904 -12.964  1.00 52.46           C  
ANISOU 3118  CB  LEU A1174     6369   3764   9797    136   1311    -68       C  
ATOM   3119  CG  LEU A1174     119.831 157.472 -13.417  1.00 55.74           C  
ANISOU 3119  CG  LEU A1174     6808   4074  10297    147   1319   -101       C  
ATOM   3120  CD1 LEU A1174     119.253 157.213 -14.798  1.00 57.15           C  
ANISOU 3120  CD1 LEU A1174     6888   4252  10574    147   1314   -252       C  
ATOM   3121  CD2 LEU A1174     121.325 157.205 -13.393  1.00 55.56           C  
ANISOU 3121  CD2 LEU A1174     6856   4044  10212    226   1245    -19       C  
ATOM   3122  N   GLU A1175     117.773 157.995 -10.546  1.00 52.20           N  
ANISOU 3122  N   GLU A1175     6464   3526   9842     -9   1553      9       N  
ATOM   3123  CA  GLU A1175     117.174 156.960  -9.706  1.00 53.49           C  
ANISOU 3123  CA  GLU A1175     6705   3539  10081    -68   1690     47       C  
ATOM   3124  C   GLU A1175     115.657 157.091  -9.663  1.00 53.28           C  
ANISOU 3124  C   GLU A1175     6548   3489  10206   -154   1850    -45       C  
ATOM   3125  O   GLU A1175     114.937 156.085  -9.679  1.00 55.96           O  
ANISOU 3125  O   GLU A1175     6840   3711  10709   -215   1968    -92       O  
ATOM   3126  CB  GLU A1175     117.753 157.032  -8.291  1.00 56.29           C  
ANISOU 3126  CB  GLU A1175     7276   3823  10290    -45   1694    202       C  
ATOM   3127  CG  GLU A1175     117.343 155.880  -7.381  1.00 62.45           C  
ANISOU 3127  CG  GLU A1175     8188   4420  11122    -89   1841    279       C  
ATOM   3128  CD  GLU A1175     118.119 154.610  -7.666  1.00 68.47           C  
ANISOU 3128  CD  GLU A1175     9011   5080  11924    -53   1777    314       C  
ATOM   3129  OE1 GLU A1175     119.268 154.714  -8.147  1.00 69.13           O  
ANISOU 3129  OE1 GLU A1175     9103   5221  11941     26   1606    324       O  
ATOM   3130  OE2 GLU A1175     117.582 153.511  -7.414  1.00 72.97           O  
ANISOU 3130  OE2 GLU A1175     9612   5504  12610   -104   1911    327       O  
ATOM   3131  N   LEU A1176     115.153 158.324  -9.606  1.00 50.54           N  
ANISOU 3131  N   LEU A1176     6129   3241   9832   -159   1861    -77       N  
ATOM   3132  CA  LEU A1176     113.711 158.536  -9.577  1.00 50.28           C  
ANISOU 3132  CA  LEU A1176     5946   3185   9975   -231   2013   -175       C  
ATOM   3133  C   LEU A1176     113.078 158.288 -10.940  1.00 50.00           C  
ANISOU 3133  C   LEU A1176     5696   3167  10134   -249   1955   -345       C  
ATOM   3134  O   LEU A1176     111.890 157.957 -11.019  1.00 51.13           O  
ANISOU 3134  O   LEU A1176     5687   3239  10502   -317   2072   -453       O  
ATOM   3135  CB  LEU A1176     113.407 159.957  -9.103  1.00 44.34           C  
ANISOU 3135  CB  LEU A1176     5183   2521   9142   -220   2037   -161       C  
ATOM   3136  CG  LEU A1176     112.001 160.264  -8.588  1.00 54.98           C  
ANISOU 3136  CG  LEU A1176     6422   3818  10651   -286   2247   -224       C  
ATOM   3137  CD1 LEU A1176     111.765 159.594  -7.244  1.00 57.96           C  
ANISOU 3137  CD1 LEU A1176     6965   4049  11007   -328   2464   -123       C  
ATOM   3138  CD2 LEU A1176     111.793 161.765  -8.486  1.00 55.85           C  
ANISOU 3138  CD2 LEU A1176     6489   4033  10699   -260   2224   -239       C  
ATOM   3139  N   SER A1177     113.846 158.438 -12.018  1.00 47.86           N  
ANISOU 3139  N   SER A1177     5413   2976   9797   -186   1777   -380       N  
ATOM   3140  CA  SER A1177     113.294 158.276 -13.356  1.00 48.82           C  
ANISOU 3140  CA  SER A1177     5372   3100  10076   -189   1693   -552       C  
ATOM   3141  C   SER A1177     113.097 156.819 -13.747  1.00 53.26           C  
ANISOU 3141  C   SER A1177     5904   3532  10799   -228   1716   -635       C  
ATOM   3142  O   SER A1177     112.547 156.557 -14.821  1.00 54.21           O  
ANISOU 3142  O   SER A1177     5893   3627  11075   -235   1636   -808       O  
ATOM   3143  CB  SER A1177     114.194 158.953 -14.385  1.00 47.19           C  
ANISOU 3143  CB  SER A1177     5201   3003   9726    -97   1522   -557       C  
ATOM   3144  OG  SER A1177     115.471 158.346 -14.397  1.00 48.30           O  
ANISOU 3144  OG  SER A1177     5481   3133   9739    -46   1477   -466       O  
ATOM   3145  N   ARG A1178     113.540 155.868 -12.921  1.00 56.96           N  
ANISOU 3145  N   ARG A1178     6501   3903  11239   -248   1807   -526       N  
ATOM   3146  CA  ARG A1178     113.263 154.468 -13.214  1.00 63.54           C  
ANISOU 3146  CA  ARG A1178     7301   4591  12253   -295   1851   -604       C  
ATOM   3147  C   ARG A1178     111.812 154.111 -12.919  1.00 74.30           C  
ANISOU 3147  C   ARG A1178     8496   5850  13885   -397   2008   -709       C  
ATOM   3148  O   ARG A1178     111.316 153.099 -13.425  1.00 75.99           O  
ANISOU 3148  O   ARG A1178     8610   5946  14317   -446   2023   -837       O  
ATOM   3149  CB  ARG A1178     114.210 153.563 -12.421  1.00 60.22           C  
ANISOU 3149  CB  ARG A1178     7077   4079  11726   -275   1896   -446       C  
ATOM   3150  CG  ARG A1178     115.669 153.975 -12.518  1.00 55.23           C  
ANISOU 3150  CG  ARG A1178     6587   3542  10857   -172   1755   -336       C  
ATOM   3151  CD  ARG A1178     116.585 153.000 -11.794  1.00 55.95           C  
ANISOU 3151  CD  ARG A1178     6854   3521  10883   -144   1771   -200       C  
ATOM   3152  NE  ARG A1178     117.939 153.532 -11.662  1.00 54.95           N  
ANISOU 3152  NE  ARG A1178     6842   3480  10558    -47   1641    -92       N  
ATOM   3153  CZ  ARG A1178     118.873 153.439 -12.602  1.00 55.12           C  
ANISOU 3153  CZ  ARG A1178     6849   3548  10546     28   1526   -128       C  
ATOM   3154  NH1 ARG A1178     118.604 152.832 -13.750  1.00 56.89           N  
ANISOU 3154  NH1 ARG A1178     6984   3738  10895     23   1514   -271       N  
ATOM   3155  NH2 ARG A1178     120.077 153.956 -12.395  1.00 53.00           N  
ANISOU 3155  NH2 ARG A1178     6656   3347  10135    110   1429    -31       N  
ATOM   3156  N   SER A1179     111.127 154.918 -12.116  1.00 81.50           N  
ANISOU 3156  N   SER A1179     9367   6793  14806   -426   2132   -668       N  
ATOM   3157  CA  SER A1179     109.701 154.780 -11.892  1.00 89.92           C  
ANISOU 3157  CA  SER A1179    10236   7772  16159   -512   2294   -784       C  
ATOM   3158  C   SER A1179     108.954 155.799 -12.749  1.00 97.46           C  
ANISOU 3158  C   SER A1179    10973   8825  17231   -499   2177   -950       C  
ATOM   3159  O   SER A1179     109.546 156.554 -13.524  1.00103.60           O  
ANISOU 3159  O   SER A1179    11780   9728  17855   -427   1982   -964       O  
ATOM   3160  CB  SER A1179     109.377 154.947 -10.407  1.00 93.18           C  
ANISOU 3160  CB  SER A1179    10755   8125  16525   -546   2543   -639       C  
ATOM   3161  OG  SER A1179     110.098 154.006  -9.628  1.00 98.05           O  
ANISOU 3161  OG  SER A1179    11596   8635  17024   -547   2625   -481       O  
ATOM   3162  N   ASP A1180     107.629 155.784 -12.623  1.00102.91           N  
ANISOU 3162  N   ASP A1180    11442   9443  18216   -564   2304  -1078       N  
ATOM   3163  CA  ASP A1180     106.783 156.722 -13.406  1.00103.44           C  
ANISOU 3163  CA  ASP A1180    11272   9577  18454   -549   2183  -1256       C  
ATOM   3164  C   ASP A1180     106.859 158.110 -12.772  1.00101.01           C  
ANISOU 3164  C   ASP A1180    11018   9384  17976   -508   2230  -1147       C  
ATOM   3165  O   ASP A1180     106.478 158.262 -11.611  1.00101.78           O  
ANISOU 3165  O   ASP A1180    11136   9435  18099   -541   2466  -1068       O  
ATOM   3166  CB  ASP A1180     105.340 156.246 -13.562  1.00107.99           C  
ANISOU 3166  CB  ASP A1180    11558  10019  19453   -625   2293  -1451       C  
ATOM   3167  CG  ASP A1180     104.670 156.844 -14.785  1.00110.39           C  
ANISOU 3167  CG  ASP A1180    11593  10368  19983   -596   2072  -1692       C  
ATOM   3168  OD1 ASP A1180     105.277 157.717 -15.397  1.00109.13           O  
ANISOU 3168  OD1 ASP A1180    11502  10333  19630   -520   1834  -1702       O  
ATOM   3169  OD2 ASP A1180     103.555 156.417 -15.124  1.00113.74           O  
ANISOU 3169  OD2 ASP A1180    11739  10690  20786   -641   2130  -1878       O  
ATOM   3170  N   LEU A1181     107.410 159.059 -13.516  1.00 95.26           N  
ANISOU 3170  N   LEU A1181    11284   8010  16899   -169   1554  -1446       N  
ATOM   3171  CA  LEU A1181     107.509 160.443 -13.081  1.00 84.19           C  
ANISOU 3171  CA  LEU A1181     9900   6750  15337   -163   1519  -1334       C  
ATOM   3172  C   LEU A1181     106.219 161.229 -13.280  1.00 80.16           C  
ANISOU 3172  C   LEU A1181     9170   6266  15020   -252   1407  -1472       C  
ATOM   3173  O   LEU A1181     106.185 162.413 -12.932  1.00 77.34           O  
ANISOU 3173  O   LEU A1181     8818   6022  14546   -255   1377  -1390       O  
ATOM   3174  CB  LEU A1181     108.647 161.142 -13.829  1.00 80.33           C  
ANISOU 3174  CB  LEU A1181     9556   6390  14577    -50   1334  -1320       C  
ATOM   3175  CG  LEU A1181     110.072 160.712 -13.492  1.00 85.37           C  
ANISOU 3175  CG  LEU A1181    10389   7035  15015     61   1442  -1138       C  
ATOM   3176  CD1 LEU A1181     111.046 161.268 -14.515  1.00 52.95           C  
ANISOU 3176  CD1 LEU A1181     6365   3018  10736    185   1281  -1163       C  
ATOM   3177  CD2 LEU A1181     110.435 161.189 -12.101  1.00 91.25           C  
ANISOU 3177  CD2 LEU A1181    11208   7812  15650     76   1598   -905       C  
ATOM   3178  N   SER A1182     105.166 160.602 -13.817  1.00 79.82           N  
ANISOU 3178  N   SER A1182     8923   6115  15289   -316   1333  -1683       N  
ATOM   3179  CA  SER A1182     103.958 161.335 -14.189  1.00 77.12           C  
ANISOU 3179  CA  SER A1182     8348   5798  15155   -372   1165  -1852       C  
ATOM   3180  C   SER A1182     103.323 162.043 -12.999  1.00 77.11           C  
ANISOU 3180  C   SER A1182     8255   5811  15233   -436   1399  -1685       C  
ATOM   3181  O   SER A1182     102.688 163.090 -13.172  1.00 60.18           O  
ANISOU 3181  O   SER A1182     5995   3752  13118   -455   1262  -1748       O  
ATOM   3182  CB  SER A1182     102.945 160.392 -14.839  1.00 82.42           C  
ANISOU 3182  CB  SER A1182     8784   6316  16217   -414   1053  -2107       C  
ATOM   3183  OG  SER A1182     103.406 159.937 -16.100  1.00 80.71           O  
ANISOU 3183  OG  SER A1182     8680   6094  15890   -322    760  -2307       O  
ATOM   3184  N   LYS A1183     103.476 161.494 -11.792  1.00 74.67           N  
ANISOU 3184  N   LYS A1183     8022   5410  14940   -445   1755  -1473       N  
ATOM   3185  CA  LYS A1183     102.907 162.145 -10.616  1.00 73.06           C  
ANISOU 3185  CA  LYS A1183     7796   5197  14768   -464   2005  -1303       C  
ATOM   3186  C   LYS A1183     103.610 163.465 -10.327  1.00 68.81           C  
ANISOU 3186  C   LYS A1183     7446   4834  13865   -413   1902  -1167       C  
ATOM   3187  O   LYS A1183     102.965 164.449  -9.944  1.00 68.30           O  
ANISOU 3187  O   LYS A1183     7309   4819  13823   -437   1918  -1136       O  
ATOM   3188  CB  LYS A1183     102.992 161.217  -9.403  1.00 75.91           C  
ANISOU 3188  CB  LYS A1183     8268   5401  15172   -435   2419  -1104       C  
ATOM   3189  CG  LYS A1183     101.891 161.426  -8.373  1.00 79.05           C  
ANISOU 3189  CG  LYS A1183     8546   5688  15800   -455   2749  -1005       C  
ATOM   3190  CD  LYS A1183     100.730 160.475  -8.619  1.00 85.46           C  
ANISOU 3190  CD  LYS A1183     9021   6306  17144   -528   2896  -1162       C  
ATOM   3191  CE  LYS A1183      99.634 160.639  -7.578  1.00 89.77           C  
ANISOU 3191  CE  LYS A1183     9429   6711  17967   -526   3294  -1052       C  
ATOM   3192  NZ  LYS A1183      98.888 161.919  -7.735  1.00 90.11           N  
ANISOU 3192  NZ  LYS A1183     9314   6853  18069   -554   3137  -1119       N  
ATOM   3193  N   PHE A1184     104.932 163.507 -10.516  1.00 65.72           N  
ANISOU 3193  N   PHE A1184     7280   4526  13165   -336   1798  -1091       N  
ATOM   3194  CA  PHE A1184     105.676 164.742 -10.284  1.00 62.01           C  
ANISOU 3194  CA  PHE A1184     6956   4204  12402   -280   1688   -974       C  
ATOM   3195  C   PHE A1184     105.378 165.781 -11.357  1.00 55.67           C  
ANISOU 3195  C   PHE A1184     6025   3529  11597   -308   1396  -1139       C  
ATOM   3196  O   PHE A1184     105.309 166.980 -11.063  1.00 51.87           O  
ANISOU 3196  O   PHE A1184     5556   3147  11007   -308   1345  -1074       O  
ATOM   3197  CB  PHE A1184     107.177 164.451 -10.227  1.00 65.25           C  
ANISOU 3197  CB  PHE A1184     7589   4645  12559   -173   1662   -857       C  
ATOM   3198  CG  PHE A1184     107.603 163.682  -9.007  1.00 70.71           C  
ANISOU 3198  CG  PHE A1184     8472   5228  13167    -98   1917   -668       C  
ATOM   3199  CD1 PHE A1184     107.556 162.294  -8.992  1.00 74.09           C  
ANISOU 3199  CD1 PHE A1184     8910   5523  13717    -98   2080   -684       C  
ATOM   3200  CD2 PHE A1184     108.061 164.344  -7.879  1.00 71.27           C  
ANISOU 3200  CD2 PHE A1184     8738   5318  13025     -3   1979   -481       C  
ATOM   3201  CE1 PHE A1184     107.950 161.579  -7.874  1.00 74.72           C  
ANISOU 3201  CE1 PHE A1184     9198   5498  13695     -2   2324   -506       C  
ATOM   3202  CE2 PHE A1184     108.458 163.636  -6.757  1.00 72.94           C  
ANISOU 3202  CE2 PHE A1184     9180   5418  13117    115   2187   -318       C  
ATOM   3203  CZ  PHE A1184     108.402 162.249  -6.755  1.00 74.30           C  
ANISOU 3203  CZ  PHE A1184     9367   5466  13399    118   2373   -324       C  
ATOM   3204  N   ARG A1185     105.188 165.345 -12.594  1.00 55.01           N  
ANISOU 3204  N   ARG A1185     5849   3436  11616   -309   1196  -1356       N  
ATOM   3205  CA  ARG A1185     104.884 166.289 -13.693  1.00 52.41           C  
ANISOU 3205  CA  ARG A1185     5445   3209  11260   -291    910  -1531       C  
ATOM   3206  C   ARG A1185     103.578 167.008 -13.381  1.00 65.71           C  
ANISOU 3206  C   ARG A1185     6929   4908  13129   -367    899  -1586       C  
ATOM   3207  O   ARG A1185     103.519 168.204 -13.622  1.00 64.92           O  
ANISOU 3207  O   ARG A1185     6828   4925  12914   -354    772  -1589       O  
ATOM   3208  CB  ARG A1185     104.666 165.578 -15.027  1.00 54.12           C  
ANISOU 3208  CB  ARG A1185     5641   3374  11549   -237    686  -1780       C  
ATOM   3209  CG  ARG A1185     105.644 164.465 -15.347  1.00 54.33           C  
ANISOU 3209  CG  ARG A1185     5837   3337  11470   -167    752  -1738       C  
ATOM   3210  CD  ARG A1185     107.006 164.978 -15.692  1.00 53.03           C  
ANISOU 3210  CD  ARG A1185     5861   3251  11035    -15    603  -1756       C  
ATOM   3211  NE  ARG A1185     107.638 164.141 -16.686  1.00 53.67           N  
ANISOU 3211  NE  ARG A1185     6093   3259  11042     74    653  -1745       N  
ATOM   3212  CZ  ARG A1185     108.938 164.097 -16.858  1.00 56.42           C  
ANISOU 3212  CZ  ARG A1185     6615   3651  11172    217    674  -1647       C  
ATOM   3213  NH1 ARG A1185     109.719 164.728 -16.007  1.00 55.32           N  
ANISOU 3213  NH1 ARG A1185     6507   3621  10892    279    654  -1549       N  
ATOM   3214  NH2 ARG A1185     109.456 163.432 -17.868  1.00 53.34           N  
ANISOU 3214  NH2 ARG A1185     6351   3186  10729    304    736  -1635       N  
ATOM   3215  N   GLU A1186     102.558 166.280 -12.920  1.00 67.41           N  
ANISOU 3215  N   GLU A1186     6964   4994  13656   -437   1055  -1624       N  
ATOM   3216  CA  GLU A1186     101.283 166.904 -12.583  1.00 65.43           C  
ANISOU 3216  CA  GLU A1186     6494   4730  13636   -492   1089  -1666       C  
ATOM   3217  C   GLU A1186     101.420 167.862 -11.407  1.00 59.10           C  
ANISOU 3217  C   GLU A1186     5808   3988  12658   -496   1293  -1426       C  
ATOM   3218  O   GLU A1186     100.729 168.885 -11.361  1.00 56.57           O  
ANISOU 3218  O   GLU A1186     5388   3731  12373   -513   1230  -1449       O  
ATOM   3219  CB  GLU A1186     100.236 165.835 -12.278  1.00 70.74           C  
ANISOU 3219  CB  GLU A1186     6927   5212  14740   -545   1273  -1742       C  
ATOM   3220  CG  GLU A1186      98.804 166.345 -12.307  1.00 75.78           C  
ANISOU 3220  CG  GLU A1186     7262   5807  15723   -577   1240  -1868       C  
ATOM   3221  CD  GLU A1186      98.331 166.675 -13.711  1.00 79.11           C  
ANISOU 3221  CD  GLU A1186     7538   6289  16232   -538    797  -2167       C  
ATOM   3222  OE1 GLU A1186      98.478 165.814 -14.604  1.00 82.02           O  
ANISOU 3222  OE1 GLU A1186     7886   6602  16678   -506    595  -2354       O  
ATOM   3223  OE2 GLU A1186      97.820 167.794 -13.923  1.00 79.13           O  
ANISOU 3223  OE2 GLU A1186     7473   6389  16206   -519    641  -2219       O  
ATOM   3224  N   ASN A1187     102.304 167.554 -10.455  1.00 57.35           N  
ANISOU 3224  N   ASN A1187     5813   3739  12236   -461   1514  -1204       N  
ATOM   3225  CA  ASN A1187     102.573 168.494  -9.371  1.00 52.05           C  
ANISOU 3225  CA  ASN A1187     5311   3119  11348   -428   1645   -992       C  
ATOM   3226  C   ASN A1187     103.251 169.753  -9.893  1.00 55.64           C  
ANISOU 3226  C   ASN A1187     5841   3748  11550   -402   1384   -997       C  
ATOM   3227  O   ASN A1187     102.944 170.863  -9.440  1.00 48.36           O  
ANISOU 3227  O   ASN A1187     4932   2890  10553   -406   1381   -928       O  
ATOM   3228  CB  ASN A1187     103.433 167.829  -8.298  1.00 59.87           C  
ANISOU 3228  CB  ASN A1187     6561   4025  12162   -352   1881   -780       C  
ATOM   3229  CG  ASN A1187     102.709 166.702  -7.594  1.00 63.15           C  
ANISOU 3229  CG  ASN A1187     6928   4250  12816   -360   2217   -734       C  
ATOM   3230  OD1 ASN A1187     101.485 166.721  -7.467  1.00 65.02           O  
ANISOU 3230  OD1 ASN A1187     6949   4408  13347   -415   2353   -792       O  
ATOM   3231  ND2 ASN A1187     103.462 165.714  -7.126  1.00 63.94           N  
ANISOU 3231  ND2 ASN A1187     7218   4265  12813   -291   2369   -627       N  
ATOM   3232  N   CYS A1188     104.174 169.600 -10.847  1.00 54.07           N  
ANISOU 3232  N   CYS A1188     5697   3612  11233   -364   1186  -1073       N  
ATOM   3233  CA  CYS A1188     104.867 170.757 -11.407  1.00 49.38           C  
ANISOU 3233  CA  CYS A1188     5162   3158  10441   -322    982  -1073       C  
ATOM   3234  C   CYS A1188     103.897 171.680 -12.131  1.00 47.43           C  
ANISOU 3234  C   CYS A1188     4757   2986  10278   -355    805  -1232       C  
ATOM   3235  O   CYS A1188     103.938 172.904 -11.957  1.00 45.23           O  
ANISOU 3235  O   CYS A1188     4500   2801   9882   -352    749  -1169       O  
ATOM   3236  CB  CYS A1188     105.976 170.297 -12.356  1.00 47.46           C  
ANISOU 3236  CB  CYS A1188     5003   2929  10099   -245    862  -1126       C  
ATOM   3237  SG  CYS A1188     107.357 169.442 -11.563  1.00 46.11           S  
ANISOU 3237  SG  CYS A1188     5023   2697   9800   -173   1021   -928       S  
ATOM   3238  N   LYS A1189     103.019 171.110 -12.958  1.00 48.20           N  
ANISOU 3238  N   LYS A1189     4695   3035  10584   -374    692  -1448       N  
ATOM   3239  CA  LYS A1189     102.030 171.927 -13.651  1.00 56.88           C  
ANISOU 3239  CA  LYS A1189     5644   4192  11777   -376    488  -1623       C  
ATOM   3240  C   LYS A1189     101.118 172.643 -12.661  1.00 57.16           C  
ANISOU 3240  C   LYS A1189     5575   4231  11913   -441    639  -1520       C  
ATOM   3241  O   LYS A1189     100.757 173.807 -12.867  1.00 47.70           O  
ANISOU 3241  O   LYS A1189     4344   3127  10654   -433    519  -1548       O  
ATOM   3242  CB  LYS A1189     101.205 171.060 -14.602  1.00 59.80           C  
ANISOU 3242  CB  LYS A1189     5849   4478  12394   -360    312  -1889       C  
ATOM   3243  CG  LYS A1189     102.026 170.293 -15.628  1.00 60.59           C  
ANISOU 3243  CG  LYS A1189     6088   4554  12378   -266    156  -2010       C  
ATOM   3244  CD  LYS A1189     101.159 169.312 -16.407  1.00 65.41           C  
ANISOU 3244  CD  LYS A1189     6539   5057  13255   -247    -25  -2273       C  
ATOM   3245  CE  LYS A1189     101.968 168.558 -17.451  1.00 66.69           C  
ANISOU 3245  CE  LYS A1189     6890   5189  13260   -122   -187  -2400       C  
ATOM   3246  NZ  LYS A1189     101.116 167.617 -18.228  1.00 70.61           N  
ANISOU 3246  NZ  LYS A1189     7241   5574  14012    -87   -411  -2676       N  
ATOM   3247  N   LYS A1190     100.737 171.963 -11.577  1.00 58.69           N  
ANISOU 3247  N   LYS A1190     5737   4307  12255   -486    926  -1397       N  
ATOM   3248  CA  LYS A1190      99.828 172.576 -10.617  1.00 50.21           C  
ANISOU 3248  CA  LYS A1190     4589   3201  11287   -517   1115  -1297       C  
ATOM   3249  C   LYS A1190     100.530 173.628  -9.771  1.00 58.12           C  
ANISOU 3249  C   LYS A1190     5815   4288  11980   -493   1184  -1083       C  
ATOM   3250  O   LYS A1190      99.884 174.566  -9.291  1.00 60.04           O  
ANISOU 3250  O   LYS A1190     6028   4556  12230   -503   1234  -1030       O  
ATOM   3251  CB  LYS A1190      99.201 171.506  -9.724  1.00 52.73           C  
ANISOU 3251  CB  LYS A1190     4831   3333  11871   -538   1447  -1227       C  
ATOM   3252  CG  LYS A1190      98.202 170.613 -10.434  1.00 55.77           C  
ANISOU 3252  CG  LYS A1190     4914   3601  12673   -566   1391  -1453       C  
ATOM   3253  CD  LYS A1190      97.586 169.611  -9.472  1.00 67.27           C  
ANISOU 3253  CD  LYS A1190     6277   4850  14433   -580   1785  -1363       C  
ATOM   3254  CE  LYS A1190      96.491 168.793 -10.141  1.00 72.30           C  
ANISOU 3254  CE  LYS A1190     6553   5342  15575   -603   1727  -1602       C  
ATOM   3255  NZ  LYS A1190      95.781 167.903  -9.177  1.00 75.96           N  
ANISOU 3255  NZ  LYS A1190     6880   5576  16406   -608   2167  -1511       N  
ATOM   3256  N   ARG A1191     101.843 173.494  -9.575  1.00 54.70           N  
ANISOU 3256  N   ARG A1191     5600   3886  11296   -448   1173   -966       N  
ATOM   3257  CA  ARG A1191     102.573 174.467  -8.770  1.00 50.51           C  
ANISOU 3257  CA  ARG A1191     5271   3414  10505   -404   1190   -784       C  
ATOM   3258  C   ARG A1191     102.910 175.720  -9.572  1.00 47.92           C  
ANISOU 3258  C   ARG A1191     4914   3239  10054   -403    939   -844       C  
ATOM   3259  O   ARG A1191     102.857 176.833  -9.038  1.00 46.24           O  
ANISOU 3259  O   ARG A1191     4760   3079   9731   -397    931   -753       O  
ATOM   3260  CB  ARG A1191     103.843 173.830  -8.203  1.00 50.12           C  
ANISOU 3260  CB  ARG A1191     5443   3315  10285   -328   1254   -647       C  
ATOM   3261  CG  ARG A1191     104.662 174.756  -7.319  1.00 49.68           C  
ANISOU 3261  CG  ARG A1191     5598   3286   9990   -248   1220   -482       C  
ATOM   3262  CD  ARG A1191     103.985 174.989  -5.977  1.00 50.40           C  
ANISOU 3262  CD  ARG A1191     5838   3277  10036   -202   1437   -346       C  
ATOM   3263  NE  ARG A1191     104.714 175.951  -5.157  1.00 47.78           N  
ANISOU 3263  NE  ARG A1191     5730   2956   9468    -97   1345   -220       N  
ATOM   3264  CZ  ARG A1191     104.415 177.243  -5.079  1.00 46.88           C  
ANISOU 3264  CZ  ARG A1191     5597   2916   9301   -115   1248   -213       C  
ATOM   3265  NH1 ARG A1191     103.394 177.732  -5.771  1.00 48.51           N  
ANISOU 3265  NH1 ARG A1191     5577   3198   9657   -230   1239   -316       N  
ATOM   3266  NH2 ARG A1191     105.133 178.047  -4.307  1.00 45.23           N  
ANISOU 3266  NH2 ARG A1191     5595   2693   8897     -1   1136   -114       N  
ATOM   3267  N   ALA A1192     103.256 175.563 -10.851  1.00 48.16           N  
ANISOU 3267  N   ALA A1192     4876   3324  10097   -390    746   -996       N  
ATOM   3268  CA  ALA A1192     103.531 176.731 -11.680  1.00 48.67           C  
ANISOU 3268  CA  ALA A1192     4931   3505  10056   -362    547  -1055       C  
ATOM   3269  C   ALA A1192     102.257 177.518 -11.970  1.00 51.98           C  
ANISOU 3269  C   ALA A1192     5207   3969  10573   -397    465  -1171       C  
ATOM   3270  O   ALA A1192     102.281 178.753 -12.016  1.00 51.96           O  
ANISOU 3270  O   ALA A1192     5224   4052  10465   -389    391  -1136       O  
ATOM   3271  CB  ALA A1192     104.214 176.303 -12.978  1.00 47.50           C  
ANISOU 3271  CB  ALA A1192     4806   3359   9883   -287    401  -1188       C  
ATOM   3272  N   MET A1193     101.134 176.823 -12.172  1.00 54.75           N  
ANISOU 3272  N   MET A1193     5396   4252  11154   -427    473  -1312       N  
ATOM   3273  CA  MET A1193      99.865 177.520 -12.352  1.00 55.29           C  
ANISOU 3273  CA  MET A1193     5299   4345  11366   -444    398  -1420       C  
ATOM   3274  C   MET A1193      99.434 178.213 -11.066  1.00 52.61           C  
ANISOU 3274  C   MET A1193     4984   3994  11010   -486    612  -1232       C  
ATOM   3275  O   MET A1193      98.978 179.362 -11.095  1.00 51.66           O  
ANISOU 3275  O   MET A1193     4834   3948  10845   -487    543  -1234       O  
ATOM   3276  CB  MET A1193      98.785 176.543 -12.817  1.00 60.96           C  
ANISOU 3276  CB  MET A1193     5797   4960  12405   -450    351  -1619       C  
ATOM   3277  CG  MET A1193      98.952 176.055 -14.245  1.00 65.96           C  
ANISOU 3277  CG  MET A1193     6415   5602  13046   -372     56  -1865       C  
ATOM   3278  SD  MET A1193      97.705 174.835 -14.700  1.00 73.90           S  
ANISOU 3278  SD  MET A1193     7138   6460  14479   -368    -32  -2109       S  
ATOM   3279  CE  MET A1193      98.013 174.683 -16.456  1.00 75.75           C  
ANISOU 3279  CE  MET A1193     7464   6740  14579   -213   -470  -2407       C  
ATOM   3280  N   SER A1194      99.569 177.526  -9.927  1.00 52.33           N  
ANISOU 3280  N   SER A1194     5034   3853  10998   -501    879  -1070       N  
ATOM   3281  CA  SER A1194      99.242 178.147  -8.647  1.00 52.97           C  
ANISOU 3281  CA  SER A1194     5213   3892  11022   -500   1096   -886       C  
ATOM   3282  C   SER A1194     100.119 179.360  -8.377  1.00 52.91           C  
ANISOU 3282  C   SER A1194     5393   3993  10718   -474    993   -766       C  
ATOM   3283  O   SER A1194      99.661 180.331  -7.764  1.00 52.56           O  
ANISOU 3283  O   SER A1194     5389   3961  10621   -472   1050   -684       O  
ATOM   3284  CB  SER A1194      99.378 177.129  -7.514  1.00 54.67           C  
ANISOU 3284  CB  SER A1194     5557   3949  11265   -474   1400   -735       C  
ATOM   3285  OG  SER A1194      99.288 177.758  -6.246  1.00 55.08           O  
ANISOU 3285  OG  SER A1194     5804   3947  11177   -426   1596   -542       O  
ATOM   3286  N   PHE A1195     101.376 179.327  -8.827  1.00 51.51           N  
ANISOU 3286  N   PHE A1195     5316   3879  10377   -446    848   -755       N  
ATOM   3287  CA  PHE A1195     102.261 180.469  -8.643  1.00 48.78           C  
ANISOU 3287  CA  PHE A1195     5096   3617   9820   -415    735   -656       C  
ATOM   3288  C   PHE A1195     101.937 181.592  -9.617  1.00 47.90           C  
ANISOU 3288  C   PHE A1195     4869   3630   9701   -435    554   -763       C  
ATOM   3289  O   PHE A1195     102.127 182.768  -9.286  1.00 47.13           O  
ANISOU 3289  O   PHE A1195     4830   3590   9488   -430    510   -681       O  
ATOM   3290  CB  PHE A1195     103.718 180.038  -8.798  1.00 46.76           C  
ANISOU 3290  CB  PHE A1195     4944   3361   9463   -363    663   -606       C  
ATOM   3291  CG  PHE A1195     104.702 181.021  -8.232  1.00 46.45           C  
ANISOU 3291  CG  PHE A1195     5028   3350   9272   -311    576   -479       C  
ATOM   3292  CD1 PHE A1195     105.339 181.939  -9.050  1.00 35.67           C  
ANISOU 3292  CD1 PHE A1195     3593   2135   7825   -297    413   -494       C  
ATOM   3293  CD2 PHE A1195     104.984 181.030  -6.877  1.00 47.34           C  
ANISOU 3293  CD2 PHE A1195     5339   3363   9284   -240    649   -342       C  
ATOM   3294  CE1 PHE A1195     106.243 182.842  -8.529  1.00 34.99           C  
ANISOU 3294  CE1 PHE A1195     3571   2107   7616   -246    315   -383       C  
ATOM   3295  CE2 PHE A1195     105.885 181.931  -6.349  1.00 46.71           C  
ANISOU 3295  CE2 PHE A1195     5361   3320   9068   -166    500   -257       C  
ATOM   3296  CZ  PHE A1195     106.516 182.839  -7.176  1.00 46.30           C  
ANISOU 3296  CZ  PHE A1195     5175   3435   8983   -186    326   -283       C  
ATOM   3297  N   SER A1196     101.454 181.255 -10.815  1.00 48.72           N  
ANISOU 3297  N   SER A1196     4830   3760   9923   -438    433   -956       N  
ATOM   3298  CA  SER A1196     101.029 182.290 -11.751  1.00 50.34           C  
ANISOU 3298  CA  SER A1196     4962   4053  10114   -421    257  -1079       C  
ATOM   3299  C   SER A1196      99.772 182.995 -11.253  1.00 52.92           C  
ANISOU 3299  C   SER A1196     5195   4392  10521   -458    304  -1080       C  
ATOM   3300  O   SER A1196      99.596 184.196 -11.485  1.00 53.53           O  
ANISOU 3300  O   SER A1196     5273   4548  10519   -451    215  -1084       O  
ATOM   3301  CB  SER A1196     100.795 181.680 -13.133  1.00 52.45           C  
ANISOU 3301  CB  SER A1196     5153   4304  10472   -360     76  -1321       C  
ATOM   3302  OG  SER A1196     101.974 181.061 -13.622  1.00 53.67           O  
ANISOU 3302  OG  SER A1196     5421   4476  10496   -288     62  -1292       O  
ATOM   3303  N   LYS A 294      98.887 182.263 -10.568  1.00 55.03           N  
ANISOU 3303  N   LYS A 294     5379   4560  10969   -489    470  -1069       N  
ATOM   3304  CA  LYS A 294      97.703 182.887  -9.986  1.00 55.63           C  
ANISOU 3304  CA  LYS A 294     5366   4609  11160   -509    573  -1045       C  
ATOM   3305  C   LYS A 294      98.089 183.924  -8.940  1.00 53.61           C  
ANISOU 3305  C   LYS A 294     5293   4377  10698   -512    681   -839       C  
ATOM   3306  O   LYS A 294      97.465 184.989  -8.851  1.00 52.10           O  
ANISOU 3306  O   LYS A 294     5069   4230  10495   -518    661   -831       O  
ATOM   3307  CB  LYS A 294      96.796 181.820  -9.376  1.00 60.39           C  
ANISOU 3307  CB  LYS A 294     5848   5055  12043   -524    798  -1048       C  
ATOM   3308  CG  LYS A 294      95.549 182.381  -8.713  1.00 64.79           C  
ANISOU 3308  CG  LYS A 294     6299   5542  12777   -528    964  -1011       C  
ATOM   3309  CD  LYS A 294      94.820 181.306  -7.932  1.00 69.44           C  
ANISOU 3309  CD  LYS A 294     6791   5937  13656   -525   1275   -966       C  
ATOM   3310  CE  LYS A 294      93.576 181.860  -7.257  1.00 71.48           C  
ANISOU 3310  CE  LYS A 294     6933   6096  14129   -510   1489   -918       C  
ATOM   3311  NZ  LYS A 294      93.893 182.966  -6.311  1.00 69.56           N  
ANISOU 3311  NZ  LYS A 294     6944   5895  13590   -494   1605   -710       N  
ATOM   3312  N   GLN A 295      99.121 183.631  -8.142  1.00 53.64           N  
ANISOU 3312  N   GLN A 295     5501   4339  10542   -491    773   -682       N  
ATOM   3313  CA  GLN A 295      99.588 184.584  -7.139  1.00 52.99           C  
ANISOU 3313  CA  GLN A 295     5624   4250  10261   -459    817   -510       C  
ATOM   3314  C   GLN A 295     100.104 185.858  -7.796  1.00 47.99           C  
ANISOU 3314  C   GLN A 295     4978   3755   9500   -466    602   -534       C  
ATOM   3315  O   GLN A 295      99.765 186.970  -7.374  1.00 45.20           O  
ANISOU 3315  O   GLN A 295     4672   3425   9077   -464    603   -473       O  
ATOM   3316  CB  GLN A 295     100.676 183.941  -6.275  1.00 56.66           C  
ANISOU 3316  CB  GLN A 295     6314   4621  10592   -393    883   -379       C  
ATOM   3317  CG  GLN A 295     100.240 182.662  -5.575  1.00 62.74           C  
ANISOU 3317  CG  GLN A 295     7138   5239  11461   -365   1135   -332       C  
ATOM   3318  CD  GLN A 295      99.100 182.889  -4.600  1.00 69.58           C  
ANISOU 3318  CD  GLN A 295     8059   5995  12382   -336   1394   -241       C  
ATOM   3319  OE1 GLN A 295      98.140 182.119  -4.558  1.00 73.88           O  
ANISOU 3319  OE1 GLN A 295     8458   6453  13162   -361   1600   -275       O  
ATOM   3320  NE2 GLN A 295      99.205 183.948  -3.806  1.00 70.39           N  
ANISOU 3320  NE2 GLN A 295     8368   6087  12290   -267   1394   -124       N  
ATOM   3321  N   ILE A 296     100.925 185.709  -8.838  1.00 47.58           N  
ANISOU 3321  N   ILE A 296     4872   3780   9428   -462    441   -615       N  
ATOM   3322  CA  ILE A 296     101.435 186.868  -9.567  1.00 47.08           C  
ANISOU 3322  CA  ILE A 296     4800   3903   9185   -422    282   -611       C  
ATOM   3323  C   ILE A 296     100.285 187.677 -10.148  1.00 46.60           C  
ANISOU 3323  C   ILE A 296     4630   3911   9166   -433    229   -714       C  
ATOM   3324  O   ILE A 296     100.267 188.912 -10.062  1.00 46.32           O  
ANISOU 3324  O   ILE A 296     4630   3974   8997   -415    190   -651       O  
ATOM   3325  CB  ILE A 296     102.416 186.416 -10.664  1.00 46.77           C  
ANISOU 3325  CB  ILE A 296     4742   3942   9086   -364    187   -661       C  
ATOM   3326  CG1 ILE A 296     103.522 185.555 -10.064  1.00 33.82           C  
ANISOU 3326  CG1 ILE A 296     3186   2222   7442   -352    233   -568       C  
ATOM   3327  CG2 ILE A 296     103.016 187.614 -11.379  1.00 32.96           C  
ANISOU 3327  CG2 ILE A 296     3005   2344   7176   -297    103   -619       C  
ATOM   3328  CD1 ILE A 296     104.323 184.817 -11.097  1.00 41.81           C  
ANISOU 3328  CD1 ILE A 296     4172   3265   8450   -296    193   -621       C  
ATOM   3329  N   ARG A 297      99.304 186.994 -10.740  1.00 47.21           N  
ANISOU 3329  N   ARG A 297     4563   3920   9456   -455    208   -889       N  
ATOM   3330  CA  ARG A 297      98.166 187.689 -11.329  1.00 47.10           C  
ANISOU 3330  CA  ARG A 297     4425   3953   9520   -443    111  -1023       C  
ATOM   3331  C   ARG A 297      97.312 188.368 -10.263  1.00 46.39           C  
ANISOU 3331  C   ARG A 297     4320   3797   9507   -501    258   -925       C  
ATOM   3332  O   ARG A 297      96.717 189.419 -10.528  1.00 48.02           O  
ANISOU 3332  O   ARG A 297     4485   4086   9672   -481    187   -955       O  
ATOM   3333  CB  ARG A 297      97.333 186.706 -12.154  1.00 50.61           C  
ANISOU 3333  CB  ARG A 297     4695   4307  10226   -433      4  -1267       C  
ATOM   3334  CG  ARG A 297      96.630 187.312 -13.357  1.00 54.29           C  
ANISOU 3334  CG  ARG A 297     5082   4863  10683   -331   -244  -1479       C  
ATOM   3335  CD  ARG A 297      95.898 186.238 -14.142  1.00 60.87           C  
ANISOU 3335  CD  ARG A 297     5755   5591  11780   -288   -410  -1747       C  
ATOM   3336  NE  ARG A 297      94.523 186.627 -14.427  1.00 67.26           N  
ANISOU 3336  NE  ARG A 297     6380   6394  12783   -241   -541  -1907       N  
ATOM   3337  CZ  ARG A 297      94.133 187.219 -15.550  1.00 70.28           C  
ANISOU 3337  CZ  ARG A 297     6760   6829  13113   -103   -851  -2140       C  
ATOM   3338  NH1 ARG A 297      95.015 187.487 -16.503  1.00 70.80           N  
ANISOU 3338  NH1 ARG A 297     7064   7034  12802     69   -988  -2156       N  
ATOM   3339  NH2 ARG A 297      92.858 187.540 -15.720  1.00 71.60           N  
ANISOU 3339  NH2 ARG A 297     6741   6978  13486    -50   -974  -2279       N  
ATOM   3340  N   ALA A 298      97.255 187.802  -9.054  1.00 44.01           N  
ANISOU 3340  N   ALA A 298     4099   3391   9232   -518    477   -782       N  
ATOM   3341  CA  ALA A 298      96.518 188.443  -7.969  1.00 43.51           C  
ANISOU 3341  CA  ALA A 298     4090   3263   9178   -522    657   -657       C  
ATOM   3342  C   ALA A 298      97.274 189.651  -7.428  1.00 43.23           C  
ANISOU 3342  C   ALA A 298     4251   3273   8900   -509    619   -514       C  
ATOM   3343  O   ALA A 298      96.685 190.718  -7.217  1.00 41.71           O  
ANISOU 3343  O   ALA A 298     4063   3105   8681   -510    632   -482       O  
ATOM   3344  CB  ALA A 298      96.237 187.435  -6.854  1.00 38.08           C  
ANISOU 3344  CB  ALA A 298     3474   2410   8586   -506    933   -549       C  
ATOM   3345  N   ARG A 299      98.582 189.498  -7.188  1.00 43.77           N  
ANISOU 3345  N   ARG A 299     4474   3365   8790   -475    556   -431       N  
ATOM   3346  CA  ARG A 299      99.400 190.638  -6.781  1.00 44.30           C  
ANISOU 3346  CA  ARG A 299     4694   3533   8603   -424    452   -321       C  
ATOM   3347  C   ARG A 299      99.385 191.740  -7.829  1.00 42.69           C  
ANISOU 3347  C   ARG A 299     4384   3518   8321   -426    302   -382       C  
ATOM   3348  O   ARG A 299      99.501 192.923  -7.488  1.00 40.63           O  
ANISOU 3348  O   ARG A 299     4199   3313   7925   -403    262   -308       O  
ATOM   3349  CB  ARG A 299     100.844 190.199  -6.523  1.00 45.10           C  
ANISOU 3349  CB  ARG A 299     4910   3628   8596   -377    364   -263       C  
ATOM   3350  CG  ARG A 299     101.102 189.605  -5.150  1.00 49.70           C  
ANISOU 3350  CG  ARG A 299     5724   4033   9125   -302    468   -156       C  
ATOM   3351  CD  ARG A 299     102.591 189.360  -4.949  1.00 54.34           C  
ANISOU 3351  CD  ARG A 299     6401   4627   9617   -236    305   -125       C  
ATOM   3352  NE  ARG A 299     102.903 188.833  -3.623  1.00 59.35           N  
ANISOU 3352  NE  ARG A 299     7312   5088  10149   -107    355    -37       N  
ATOM   3353  CZ  ARG A 299     104.129 188.506  -3.224  1.00 61.76           C  
ANISOU 3353  CZ  ARG A 299     7726   5356  10385    -13    195    -22       C  
ATOM   3354  NH1 ARG A 299     105.156 188.650  -4.050  1.00 61.88           N  
ANISOU 3354  NH1 ARG A 299     7556   5481  10473    -60     14    -75       N  
ATOM   3355  NH2 ARG A 299     104.328 188.033  -2.002  1.00 62.78           N  
ANISOU 3355  NH2 ARG A 299     8159   5314  10380    154    227     48       N  
ATOM   3356  N   ARG A 300      99.246 191.374  -9.105  1.00 44.41           N  
ANISOU 3356  N   ARG A 300     4455   3814   8603   -424    219   -519       N  
ATOM   3357  CA  ARG A 300      99.282 192.368 -10.172  1.00 43.68           C  
ANISOU 3357  CA  ARG A 300     4321   3882   8393   -368    102   -567       C  
ATOM   3358  C   ARG A 300      98.058 193.274 -10.114  1.00 44.25           C  
ANISOU 3358  C   ARG A 300     4344   3983   8488   -372    109   -601       C  
ATOM   3359  O   ARG A 300      98.172 194.497 -10.265  1.00 45.01           O  
ANISOU 3359  O   ARG A 300     4489   4179   8434   -334     74   -545       O  
ATOM   3360  CB  ARG A 300      99.381 191.669 -11.532  1.00 45.88           C  
ANISOU 3360  CB  ARG A 300     4529   4211   8693   -302      7   -715       C  
ATOM   3361  CG  ARG A 300      99.934 192.547 -12.645  1.00 46.98           C  
ANISOU 3361  CG  ARG A 300     4722   4486   8641   -179    -62   -710       C  
ATOM   3362  CD  ARG A 300     100.001 191.824 -13.988  1.00 49.47           C  
ANISOU 3362  CD  ARG A 300     5045   4828   8923    -52   -152   -858       C  
ATOM   3363  NE  ARG A 300     101.023 190.780 -14.029  1.00 49.87           N  
ANISOU 3363  NE  ARG A 300     5122   4822   9005    -58   -107   -823       N  
ATOM   3364  CZ  ARG A 300     100.786 189.512 -14.349  1.00 52.66           C  
ANISOU 3364  CZ  ARG A 300     5435   5103   9470    -55   -158   -959       C  
ATOM   3365  NH1 ARG A 300      99.558 189.123 -14.665  1.00 54.49           N  
ANISOU 3365  NH1 ARG A 300     5572   5293   9838    -51   -273  -1158       N  
ATOM   3366  NH2 ARG A 300     101.779 188.633 -14.365  1.00 53.55           N  
ANISOU 3366  NH2 ARG A 300     5585   5168   9595    -54   -104   -910       N  
ATOM   3367  N   LYS A 301      96.878 192.692  -9.878  1.00 45.39           N  
ANISOU 3367  N   LYS A 301     4372   4016   8857   -419    173   -690       N  
ATOM   3368  CA  LYS A 301      95.648 193.479  -9.870  1.00 45.56           C  
ANISOU 3368  CA  LYS A 301     4304   4044   8962   -418    181   -737       C  
ATOM   3369  C   LYS A 301      95.613 194.440  -8.691  1.00 43.99           C  
ANISOU 3369  C   LYS A 301     4247   3820   8645   -435    313   -555       C  
ATOM   3370  O   LYS A 301      95.078 195.549  -8.800  1.00 44.47           O  
ANISOU 3370  O   LYS A 301     4304   3958   8634   -408    287   -545       O  
ATOM   3371  CB  LYS A 301      94.436 192.546  -9.848  1.00 48.99           C  
ANISOU 3371  CB  LYS A 301     4531   4310   9773   -470    240   -879       C  
ATOM   3372  CG  LYS A 301      94.277 191.731 -11.120  1.00 51.83           C  
ANISOU 3372  CG  LYS A 301     4743   4685  10266   -426     34  -1118       C  
ATOM   3373  CD  LYS A 301      93.275 190.605 -10.943  1.00 56.60           C  
ANISOU 3373  CD  LYS A 301     5148   5120  11238   -453    108  -1232       C  
ATOM   3374  CE  LYS A 301      93.116 189.812 -12.232  1.00 61.30           C  
ANISOU 3374  CE  LYS A 301     5616   5720  11957   -380   -153  -1499       C  
ATOM   3375  NZ  LYS A 301      92.204 188.646 -12.074  1.00 66.06           N  
ANISOU 3375  NZ  LYS A 301     6026   6173  12900   -369    -80  -1593       N  
ATOM   3376  N   THR A 302      96.186 194.035  -7.556  1.00 41.87           N  
ANISOU 3376  N   THR A 302     4137   3436   8334   -450    441   -416       N  
ATOM   3377  CA  THR A 302      96.246 194.930  -6.406  1.00 32.22           C  
ANISOU 3377  CA  THR A 302     3115   2172   6954   -418    527   -258       C  
ATOM   3378  C   THR A 302      97.178 196.107  -6.671  1.00 41.16           C  
ANISOU 3378  C   THR A 302     4331   3455   7850   -384    360   -214       C  
ATOM   3379  O   THR A 302      96.874 197.241  -6.286  1.00 41.14           O  
ANISOU 3379  O   THR A 302     4408   3481   7743   -361    366   -152       O  
ATOM   3380  CB  THR A 302      96.690 194.160  -5.163  1.00 37.56           C  
ANISOU 3380  CB  THR A 302     4000   2670   7603   -381    668   -141       C  
ATOM   3381  OG1 THR A 302      95.816 193.044  -4.957  1.00 41.30           O  
ANISOU 3381  OG1 THR A 302     4380   2966   8346   -411    883   -168       O  
ATOM   3382  CG2 THR A 302      96.642 195.055  -3.935  1.00 33.06           C  
ANISOU 3382  CG2 THR A 302     3694   2026   6843   -294    740      2       C  
ATOM   3383  N   ALA A 303      98.315 195.860  -7.329  1.00 39.99           N  
ANISOU 3383  N   ALA A 303     4158   3382   7652   -378    235   -240       N  
ATOM   3384  CA  ALA A 303      99.225 196.954  -7.654  1.00 40.34           C  
ANISOU 3384  CA  ALA A 303     4236   3525   7567   -349    123   -194       C  
ATOM   3385  C   ALA A 303      98.592 197.914  -8.652  1.00 40.86           C  
ANISOU 3385  C   ALA A 303     4217   3721   7587   -322    103   -244       C  
ATOM   3386  O   ALA A 303      98.713 199.136  -8.509  1.00 41.43           O  
ANISOU 3386  O   ALA A 303     4344   3833   7564   -302     87   -181       O  
ATOM   3387  CB  ALA A 303     100.541 196.405  -8.203  1.00 39.78           C  
ANISOU 3387  CB  ALA A 303     4127   3467   7521   -338     50   -201       C  
ATOM   3388  N   ARG A 304      97.904 197.376  -9.662  1.00 41.47           N  
ANISOU 3388  N   ARG A 304     4174   3853   7732   -300     86   -371       N  
ATOM   3389  CA  ARG A 304      97.258 198.220 -10.661  1.00 40.30           C  
ANISOU 3389  CA  ARG A 304     3981   3820   7511   -221     35   -441       C  
ATOM   3390  C   ARG A 304      96.217 199.131 -10.021  1.00 36.52           C  
ANISOU 3390  C   ARG A 304     3510   3336   7031   -240     82   -408       C  
ATOM   3391  O   ARG A 304      96.064 200.291 -10.422  1.00 34.85           O  
ANISOU 3391  O   ARG A 304     3334   3214   6695   -179     62   -385       O  
ATOM   3392  CB  ARG A 304      96.624 197.337 -11.739  1.00 45.61           C  
ANISOU 3392  CB  ARG A 304     4543   4513   8272   -160    -55   -626       C  
ATOM   3393  CG  ARG A 304      95.994 198.077 -12.912  1.00 49.80           C  
ANISOU 3393  CG  ARG A 304     5073   5157   8693    -12   -163   -735       C  
ATOM   3394  CD  ARG A 304      94.912 197.215 -13.550  1.00 54.29           C  
ANISOU 3394  CD  ARG A 304     5500   5689   9439     36   -310   -968       C  
ATOM   3395  NE  ARG A 304      93.872 196.875 -12.581  1.00 57.72           N  
ANISOU 3395  NE  ARG A 304     5774   6000  10157    -98   -242   -994       N  
ATOM   3396  CZ  ARG A 304      93.169 195.747 -12.599  1.00 61.19           C  
ANISOU 3396  CZ  ARG A 304     6035   6310  10905   -145   -284  -1152       C  
ATOM   3397  NH1 ARG A 304      93.397 194.835 -13.533  1.00 62.58           N  
ANISOU 3397  NH1 ARG A 304     6182   6482  11114    -70   -443  -1319       N  
ATOM   3398  NH2 ARG A 304      92.245 195.526 -11.673  1.00 62.42           N  
ANISOU 3398  NH2 ARG A 304     6044   6314  11357   -257   -144  -1137       N  
ATOM   3399  N   MET A 305      95.502 198.627  -9.012  1.00 36.58           N  
ANISOU 3399  N   MET A 305     3501   3219   7180   -309    182   -389       N  
ATOM   3400  CA  MET A 305      94.506 199.441  -8.322  1.00 36.69           C  
ANISOU 3400  CA  MET A 305     3535   3196   7209   -313    274   -337       C  
ATOM   3401  C   MET A 305      95.167 200.527  -7.484  1.00 35.17           C  
ANISOU 3401  C   MET A 305     3542   3006   6816   -301    295   -184       C  
ATOM   3402  O   MET A 305      94.742 201.688  -7.507  1.00 34.76           O  
ANISOU 3402  O   MET A 305     3522   3013   6671   -270    296   -151       O  
ATOM   3403  CB  MET A 305      93.624 198.558  -7.443  1.00 38.63           C  
ANISOU 3403  CB  MET A 305     3731   3258   7690   -363    448   -329       C  
ATOM   3404  CG  MET A 305      92.466 199.309  -6.813  1.00 42.44           C  
ANISOU 3404  CG  MET A 305     4211   3673   8241   -352    591   -273       C  
ATOM   3405  SD  MET A 305      91.805 198.478  -5.362  1.00 47.24           S  
ANISOU 3405  SD  MET A 305     4894   3996   9058   -367    922   -152       S  
ATOM   3406  CE  MET A 305      93.130 198.766  -4.192  1.00 48.15           C  
ANISOU 3406  CE  MET A 305     5404   4080   8813   -298    926     29       C  
ATOM   3407  N   LEU A 306      96.201 200.163  -6.720  1.00 35.20           N  
ANISOU 3407  N   LEU A 306     3681   2930   6762   -312    286   -105       N  
ATOM   3408  CA  LEU A 306      96.906 201.147  -5.906  1.00 29.00           C  
ANISOU 3408  CA  LEU A 306     3079   2115   5824   -282    236     -3       C  
ATOM   3409  C   LEU A 306      97.565 202.211  -6.775  1.00 35.84           C  
ANISOU 3409  C   LEU A 306     3890   3101   6628   -271    135     -9       C  
ATOM   3410  O   LEU A 306      97.615 203.388  -6.397  1.00 36.04           O  
ANISOU 3410  O   LEU A 306     4003   3123   6566   -249    114     47       O  
ATOM   3411  CB  LEU A 306      97.945 200.452  -5.026  1.00 29.34           C  
ANISOU 3411  CB  LEU A 306     3264   2036   5847   -263    180     38       C  
ATOM   3412  CG  LEU A 306      97.441 199.445  -3.990  1.00 31.19           C  
ANISOU 3412  CG  LEU A 306     3639   2109   6104   -227    326     82       C  
ATOM   3413  CD1 LEU A 306      98.612 198.707  -3.362  1.00 33.78           C  
ANISOU 3413  CD1 LEU A 306     4107   2338   6389   -176    225     99       C  
ATOM   3414  CD2 LEU A 306      96.599 200.131  -2.922  1.00 31.09           C  
ANISOU 3414  CD2 LEU A 306     3834   1993   5987   -150    456    174       C  
ATOM   3415  N   MET A 307      98.070 201.819  -7.948  1.00 34.57           N  
ANISOU 3415  N   MET A 307     3601   3021   6513   -266    100    -68       N  
ATOM   3416  CA  MET A 307      98.738 202.781  -8.820  1.00 34.39           C  
ANISOU 3416  CA  MET A 307     3548   3070   6448   -223     81    -45       C  
ATOM   3417  C   MET A 307      97.752 203.789  -9.396  1.00 34.80           C  
ANISOU 3417  C   MET A 307     3599   3220   6403   -165    123    -57       C  
ATOM   3418  O   MET A 307      98.102 204.957  -9.599  1.00 37.18           O  
ANISOU 3418  O   MET A 307     3938   3539   6650   -130    147      4       O  
ATOM   3419  CB  MET A 307      99.482 202.053  -9.940  1.00 35.56           C  
ANISOU 3419  CB  MET A 307     3612   3253   6644   -185     85    -86       C  
ATOM   3420  CG  MET A 307     100.708 201.292  -9.470  1.00 38.03           C  
ANISOU 3420  CG  MET A 307     3912   3467   7071   -231     42    -57       C  
ATOM   3421  SD  MET A 307     101.524 200.396 -10.801  1.00 42.59           S  
ANISOU 3421  SD  MET A 307     4407   4072   7704   -168     88    -90       S  
ATOM   3422  CE  MET A 307     102.530 199.254  -9.857  1.00 44.04           C  
ANISOU 3422  CE  MET A 307     4574   4131   8027   -242     13    -79       C  
ATOM   3423  N   VAL A 308      96.518 203.361  -9.665  1.00 33.91           N  
ANISOU 3423  N   VAL A 308     3428   3153   6304   -146    130   -145       N  
ATOM   3424  CA  VAL A 308      95.506 204.300 -10.138  1.00 34.58           C  
ANISOU 3424  CA  VAL A 308     3505   3322   6311    -74    139   -174       C  
ATOM   3425  C   VAL A 308      95.164 205.302  -9.044  1.00 35.76           C  
ANISOU 3425  C   VAL A 308     3751   3423   6413   -113    196    -72       C  
ATOM   3426  O   VAL A 308      95.023 206.503  -9.304  1.00 35.96           O  
ANISOU 3426  O   VAL A 308     3826   3503   6333    -59    215    -30       O  
ATOM   3427  CB  VAL A 308      94.255 203.545 -10.627  1.00 35.59           C  
ANISOU 3427  CB  VAL A 308     3501   3471   6549    -43     90   -325       C  
ATOM   3428  CG1 VAL A 308      93.099 204.509 -10.857  1.00 35.74           C  
ANISOU 3428  CG1 VAL A 308     3499   3551   6531     30     81   -360       C  
ATOM   3429  CG2 VAL A 308      94.565 202.783 -11.902  1.00 30.06           C  
ANISOU 3429  CG2 VAL A 308     2757   2828   5839     52    -10   -451       C  
ATOM   3430  N   VAL A 309      95.031 204.823  -7.803  1.00 37.02           N  
ANISOU 3430  N   VAL A 309     3971   3464   6630   -179    239    -26       N  
ATOM   3431  CA  VAL A 309      94.752 205.710  -6.675  1.00 28.10           C  
ANISOU 3431  CA  VAL A 309     2997   2260   5418   -177    292     73       C  
ATOM   3432  C   VAL A 309      95.829 206.782  -6.570  1.00 33.03           C  
ANISOU 3432  C   VAL A 309     3718   2881   5950   -166    215    134       C  
ATOM   3433  O   VAL A 309      95.539 207.967  -6.366  1.00 34.76           O  
ANISOU 3433  O   VAL A 309     4014   3110   6082   -137    233    181       O  
ATOM   3434  CB  VAL A 309      94.636 204.899  -5.372  1.00 28.69           C  
ANISOU 3434  CB  VAL A 309     3198   2174   5529   -191    367    124       C  
ATOM   3435  CG1 VAL A 309      94.430 205.825  -4.181  1.00 28.99           C  
ANISOU 3435  CG1 VAL A 309     3471   2115   5428   -135    414    226       C  
ATOM   3436  CG2 VAL A 309      93.502 203.892  -5.474  1.00 29.53           C  
ANISOU 3436  CG2 VAL A 309     3166   2236   5818   -210    498     71       C  
ATOM   3437  N   VAL A 310      97.091 206.378  -6.726  1.00 33.93           N  
ANISOU 3437  N   VAL A 310     3806   2960   6125   -190    131    127       N  
ATOM   3438  CA  VAL A 310      98.197 207.330  -6.654  1.00 35.62           C  
ANISOU 3438  CA  VAL A 310     4046   3119   6366   -190     57    166       C  
ATOM   3439  C   VAL A 310      98.113 208.332  -7.800  1.00 37.10           C  
ANISOU 3439  C   VAL A 310     4162   3403   6532   -148    142    185       C  
ATOM   3440  O   VAL A 310      98.251 209.546  -7.599  1.00 35.21           O  
ANISOU 3440  O   VAL A 310     3975   3126   6277   -135    149    232       O  
ATOM   3441  CB  VAL A 310      99.545 206.585  -6.646  1.00 33.39           C  
ANISOU 3441  CB  VAL A 310     3700   2755   6231   -221    -37    146       C  
ATOM   3442  CG1 VAL A 310     100.702 207.565  -6.731  1.00 34.17           C  
ANISOU 3442  CG1 VAL A 310     3746   2763   6476   -227    -98    170       C  
ATOM   3443  CG2 VAL A 310      99.663 205.726  -5.396  1.00 32.16           C  
ANISOU 3443  CG2 VAL A 310     3678   2485   6055   -219   -132    134       C  
ATOM   3444  N   LEU A 311      97.892 207.839  -9.022  1.00 37.98           N  
ANISOU 3444  N   LEU A 311     4181   3621   6628    -97    206    144       N  
ATOM   3445  CA  LEU A 311      97.773 208.727 -10.175  1.00 35.52           C  
ANISOU 3445  CA  LEU A 311     3867   3389   6241      7    305    166       C  
ATOM   3446  C   LEU A 311      96.648 209.738  -9.979  1.00 35.42           C  
ANISOU 3446  C   LEU A 311     3925   3434   6098     47    332    180       C  
ATOM   3447  O   LEU A 311      96.813 210.932 -10.252  1.00 34.94           O  
ANISOU 3447  O   LEU A 311     3914   3366   5994     99    409    246       O  
ATOM   3448  CB  LEU A 311      97.542 207.903 -11.442  1.00 33.19           C  
ANISOU 3448  CB  LEU A 311     3531   3190   5892    112    325     90       C  
ATOM   3449  CG  LEU A 311      97.304 208.689 -12.730  1.00 34.21           C  
ANISOU 3449  CG  LEU A 311     3731   3395   5871    299    425    102       C  
ATOM   3450  CD1 LEU A 311      98.618 209.116 -13.363  1.00 36.22           C  
ANISOU 3450  CD1 LEU A 311     4007   3561   6195    362    591    211       C  
ATOM   3451  CD2 LEU A 311      96.480 207.858 -13.689  1.00 34.41           C  
ANISOU 3451  CD2 LEU A 311     3761   3524   5790    436    339    -38       C  
ATOM   3452  N   VAL A 312      95.496 209.274  -9.486  1.00 36.00           N  
ANISOU 3452  N   VAL A 312     3993   3543   6144     26    295    126       N  
ATOM   3453  CA  VAL A 312      94.377 210.172  -9.219  1.00 34.61           C  
ANISOU 3453  CA  VAL A 312     3866   3405   5878     64    332    142       C  
ATOM   3454  C   VAL A 312      94.720 211.145  -8.097  1.00 34.03           C  
ANISOU 3454  C   VAL A 312     3922   3231   5778     14    345    240       C  
ATOM   3455  O   VAL A 312      94.313 212.313  -8.134  1.00 35.26           O  
ANISOU 3455  O   VAL A 312     4143   3410   5844     63    395    285       O  
ATOM   3456  CB  VAL A 312      93.111 209.349  -8.910  1.00 33.97           C  
ANISOU 3456  CB  VAL A 312     3706   3332   5869     49    324     65       C  
ATOM   3457  CG1 VAL A 312      91.970 210.245  -8.457  1.00 34.49           C  
ANISOU 3457  CG1 VAL A 312     3810   3404   5891     81    388     99       C  
ATOM   3458  CG2 VAL A 312      92.696 208.545 -10.138  1.00 33.20           C  
ANISOU 3458  CG2 VAL A 312     3474   3322   5817    126    250    -75       C  
ATOM   3459  N   PHE A 313      95.480 210.696  -7.094  1.00 31.60           N  
ANISOU 3459  N   PHE A 313     3673   2798   5536    -58    277    259       N  
ATOM   3460  CA  PHE A 313      95.959 211.608  -6.058  1.00 30.00           C  
ANISOU 3460  CA  PHE A 313     3618   2473   5309    -70    220    314       C  
ATOM   3461  C   PHE A 313      96.867 212.679  -6.648  1.00 31.16           C  
ANISOU 3461  C   PHE A 313     3719   2592   5529    -65    221    341       C  
ATOM   3462  O   PHE A 313      96.818 213.844  -6.233  1.00 31.14           O  
ANISOU 3462  O   PHE A 313     3808   2531   5492    -49    218    379       O  
ATOM   3463  CB  PHE A 313      96.694 210.822  -4.970  1.00 31.02           C  
ANISOU 3463  CB  PHE A 313     3838   2459   5487    -98     93    298       C  
ATOM   3464  CG  PHE A 313      97.369 211.684  -3.934  1.00 31.24           C  
ANISOU 3464  CG  PHE A 313     4032   2331   5507    -73    -53    307       C  
ATOM   3465  CD1 PHE A 313      98.669 212.129  -4.119  1.00 32.68           C  
ANISOU 3465  CD1 PHE A 313     4121   2419   5876   -106   -183    273       C  
ATOM   3466  CD2 PHE A 313      96.711 212.030  -2.766  1.00 33.21           C  
ANISOU 3466  CD2 PHE A 313     4533   2496   5591      2    -61    339       C  
ATOM   3467  CE1 PHE A 313      99.291 212.915  -3.172  1.00 34.96           C  
ANISOU 3467  CE1 PHE A 313     4538   2534   6211    -74   -377    237       C  
ATOM   3468  CE2 PHE A 313      97.333 212.815  -1.812  1.00 36.10           C  
ANISOU 3468  CE2 PHE A 313     5088   2701   5928     61   -247    317       C  
ATOM   3469  CZ  PHE A 313      98.624 213.256  -2.017  1.00 36.51           C  
ANISOU 3469  CZ  PHE A 313     5019   2661   6192     18   -435    248       C  
ATOM   3470  N   ALA A 314      97.713 212.300  -7.610  1.00 31.89           N  
ANISOU 3470  N   ALA A 314     3674   2698   5745    -69    253    331       N  
ATOM   3471  CA  ALA A 314      98.632 213.260  -8.211  1.00 29.63           C  
ANISOU 3471  CA  ALA A 314     3325   2334   5598    -54    330    379       C  
ATOM   3472  C   ALA A 314      97.878 214.319  -9.004  1.00 29.78           C  
ANISOU 3472  C   ALA A 314     3396   2447   5474     43    493    433       C  
ATOM   3473  O   ALA A 314      98.184 215.512  -8.915  1.00 31.31           O  
ANISOU 3473  O   ALA A 314     3615   2548   5732     50    553    487       O  
ATOM   3474  CB  ALA A 314      99.639 212.532  -9.103  1.00 29.14           C  
ANISOU 3474  CB  ALA A 314     3125   2247   5702    -49    395    380       C  
ATOM   3475  N   ILE A 315      96.878 213.899  -9.781  1.00 28.34           N  
ANISOU 3475  N   ILE A 315     3228   2429   5111    134    548    404       N  
ATOM   3476  CA  ILE A 315      96.151 214.836 -10.630  1.00 28.66           C  
ANISOU 3476  CA  ILE A 315     3338   2562   4990    274    675    438       C  
ATOM   3477  C   ILE A 315      95.224 215.722  -9.804  1.00 39.38           C  
ANISOU 3477  C   ILE A 315     4785   3932   6247    257    649    458       C  
ATOM   3478  O   ILE A 315      94.967 216.875 -10.171  1.00 39.99           O  
ANISOU 3478  O   ILE A 315     4935   4020   6240    342    758    516       O  
ATOM   3479  CB  ILE A 315      95.387 214.062 -11.720  1.00 28.90           C  
ANISOU 3479  CB  ILE A 315     3360   2745   4876    411    666    357       C  
ATOM   3480  CG1 ILE A 315      96.360 213.211 -12.532  1.00 29.45           C  
ANISOU 3480  CG1 ILE A 315     3384   2786   5020    453    709    349       C  
ATOM   3481  CG2 ILE A 315      94.637 215.012 -12.639  1.00 29.61           C  
ANISOU 3481  CG2 ILE A 315     3558   2925   4768    610    759    373       C  
ATOM   3482  CD1 ILE A 315      95.685 212.262 -13.481  1.00 35.86           C  
ANISOU 3482  CD1 ILE A 315     4203   3721   5703    592    633    231       C  
ATOM   3483  N   CYS A 316      94.723 215.219  -8.674  1.00 37.79           N  
ANISOU 3483  N   CYS A 316     4604   3710   6046    168    539    425       N  
ATOM   3484  CA  CYS A 316      93.764 215.987  -7.887  1.00 36.44           C  
ANISOU 3484  CA  CYS A 316     4542   3537   5768    179    552    456       C  
ATOM   3485  C   CYS A 316      94.433 217.054  -7.031  1.00 38.23           C  
ANISOU 3485  C   CYS A 316     4882   3615   6028    138    525    513       C  
ATOM   3486  O   CYS A 316      93.852 218.124  -6.819  1.00 38.77           O  
ANISOU 3486  O   CYS A 316     5051   3685   5996    184    582    559       O  
ATOM   3487  CB  CYS A 316      92.942 215.054  -7.003  1.00 33.73           C  
ANISOU 3487  CB  CYS A 316     4209   3183   5423    139    512    423       C  
ATOM   3488  SG  CYS A 316      91.690 214.119  -7.899  1.00 36.15           S  
ANISOU 3488  SG  CYS A 316     4350   3631   5755    198    531    327       S  
ATOM   3489  N   TYR A 317      95.636 216.782  -6.553  1.00 38.34           N  
ANISOU 3489  N   TYR A 317     4879   3487   6202     63    413    493       N  
ATOM   3490  CA  TYR A 317      96.340 217.756  -5.694  1.00 38.64           C  
ANISOU 3490  CA  TYR A 317     5002   3347   6333     35    319    500       C  
ATOM   3491  C   TYR A 317      97.316 218.583  -6.523  1.00 41.60           C  
ANISOU 3491  C   TYR A 317     5256   3637   6914     28    413    532       C  
ATOM   3492  O   TYR A 317      97.853 219.469  -5.963  1.00 43.59           O  
ANISOU 3492  O   TYR A 317     5543   3722   7296      7    351    528       O  
ATOM   3493  CB  TYR A 317      97.074 217.036  -4.569  1.00 40.67           C  
ANISOU 3493  CB  TYR A 317     5312   3451   6689    -11     93    431       C  
ATOM   3494  CG  TYR A 317      96.233 216.518  -3.430  1.00 43.45           C  
ANISOU 3494  CG  TYR A 317     5882   3795   6831     39     34    430       C  
ATOM   3495  CD1 TYR A 317      95.222 215.600  -3.631  1.00 43.40           C  
ANISOU 3495  CD1 TYR A 317     5855   3920   6716     52    164    453       C  
ATOM   3496  CD2 TYR A 317      96.495 216.895  -2.132  1.00 46.01           C  
ANISOU 3496  CD2 TYR A 317     6445   3945   7090     99   -141    401       C  
ATOM   3497  CE1 TYR A 317      94.464 215.110  -2.584  1.00 43.55           C  
ANISOU 3497  CE1 TYR A 317     6068   3885   6595    111    190    479       C  
ATOM   3498  CE2 TYR A 317      95.754 216.411  -1.076  1.00 46.59           C  
ANISOU 3498  CE2 TYR A 317     6777   3978   6946    194   -131    429       C  
ATOM   3499  CZ  TYR A 317      94.739 215.511  -1.298  1.00 45.54           C  
ANISOU 3499  CZ  TYR A 317     6600   3964   6738    194     69    483       C  
ATOM   3500  OH  TYR A 317      94.015 215.034  -0.254  1.00 47.10           O  
ANISOU 3500  OH  TYR A 317     7046   4079   6772    299    158    537       O  
ATOM   3501  N   ALA A 318      97.523 218.292  -7.803  1.00 41.54           N  
ANISOU 3501  N   ALA A 318     5122   3709   6951     66    577    564       N  
ATOM   3502  CA  ALA A 318      98.445 219.072  -8.628  1.00 30.99           C  
ANISOU 3502  CA  ALA A 318     3687   2251   5838     89    754    627       C  
ATOM   3503  C   ALA A 318      98.033 220.532  -8.775  1.00 38.08           C  
ANISOU 3503  C   ALA A 318     4676   3114   6677    152    898    698       C  
ATOM   3504  O   ALA A 318      98.891 221.410  -8.574  1.00 39.82           O  
ANISOU 3504  O   ALA A 318     4830   3119   7181    105    932    716       O  
ATOM   3505  CB  ALA A 318      98.607 218.405  -9.999  1.00 31.16           C  
ANISOU 3505  CB  ALA A 318     3642   2368   5828    185    944    666       C  
ATOM   3506  N   PRO A 319      96.782 220.873  -9.115  1.00 35.95           N  
ANISOU 3506  N   PRO A 319     4539   3025   6096    259    981    730       N  
ATOM   3507  CA  PRO A 319      96.468 222.301  -9.295  1.00 36.73           C  
ANISOU 3507  CA  PRO A 319     4732   3079   6145    331   1135    806       C  
ATOM   3508  C   PRO A 319      96.549 223.097  -8.007  1.00 39.57           C  
ANISOU 3508  C   PRO A 319     5158   3290   6588    237    980    777       C  
ATOM   3509  O   PRO A 319      97.068 224.219  -8.011  1.00 43.56           O  
ANISOU 3509  O   PRO A 319     5653   3622   7275    230   1073    816       O  
ATOM   3510  CB  PRO A 319      95.041 222.284  -9.870  1.00 34.00           C  
ANISOU 3510  CB  PRO A 319     4501   2970   5448    477   1194    817       C  
ATOM   3511  CG  PRO A 319      94.813 220.883 -10.336  1.00 32.35           C  
ANISOU 3511  CG  PRO A 319     4222   2900   5169    499   1114    746       C  
ATOM   3512  CD  PRO A 319      95.607 220.030  -9.401  1.00 33.02           C  
ANISOU 3512  CD  PRO A 319     4213   2879   5456    328    939    689       C  
ATOM   3513  N   ILE A 320      96.073 222.546  -6.903  1.00 38.49           N  
ANISOU 3513  N   ILE A 320     5108   3187   6329    185    757    707       N  
ATOM   3514  CA  ILE A 320      96.060 223.336  -5.644  1.00 39.72           C  
ANISOU 3514  CA  ILE A 320     5407   3197   6489    156    598    674       C  
ATOM   3515  C   ILE A 320      97.442 223.377  -5.002  1.00 41.17           C  
ANISOU 3515  C   ILE A 320     5503   3118   7020     66    392    584       C  
ATOM   3516  O   ILE A 320      97.659 224.284  -4.213  1.00 41.65           O  
ANISOU 3516  O   ILE A 320     5636   2991   7199     59    278    543       O  
ATOM   3517  CB  ILE A 320      94.995 222.800  -4.684  1.00 41.38           C  
ANISOU 3517  CB  ILE A 320     5795   3499   6429    186    485    653       C  
ATOM   3518  CG1 ILE A 320      94.729 223.782  -3.546  1.00 41.22           C  
ANISOU 3518  CG1 ILE A 320     6005   3339   6318    223    375    643       C  
ATOM   3519  CG2 ILE A 320      95.366 221.421  -4.189  1.00 42.47           C  
ANISOU 3519  CG2 ILE A 320     5898   3618   6622    137    321    583       C  
ATOM   3520  CD1 ILE A 320      94.394 225.167  -4.018  1.00 41.63           C  
ANISOU 3520  CD1 ILE A 320     6110   3418   6290    278    552    720       C  
ATOM   3521  N   SER A 321      98.290 222.374  -5.229  1.00 41.50           N  
ANISOU 3521  N   SER A 321     5382   3126   7258      8    317    536       N  
ATOM   3522  CA  SER A 321      99.644 222.439  -4.682  1.00 43.12           C  
ANISOU 3522  CA  SER A 321     5459   3062   7861    -67     94    429       C  
ATOM   3523  C   SER A 321     100.507 223.419  -5.465  1.00 45.12           C  
ANISOU 3523  C   SER A 321     5500   3125   8518   -103    287    471       C  
ATOM   3524  O   SER A 321     101.290 224.172  -4.876  1.00 48.17           O  
ANISOU 3524  O   SER A 321     5812   3288   9201   -147    116    373       O  
ATOM   3525  CB  SER A 321     100.288 221.051  -4.672  1.00 43.31           C  
ANISOU 3525  CB  SER A 321     5365   3101   7990   -110    -31    370       C  
ATOM   3526  OG  SER A 321     100.051 220.381  -3.445  1.00 43.64           O  
ANISOU 3526  OG  SER A 321     5605   3136   7840    -78   -319    281       O  
ATOM   3527  N   ILE A 322     100.381 223.422  -6.793  1.00 42.90           N  
ANISOU 3527  N   ILE A 322     5131   2953   8215    -58    646    603       N  
ATOM   3528  CA  ILE A 322     101.139 224.369  -7.604  1.00 37.79           C  
ANISOU 3528  CA  ILE A 322     4316   2138   7902    -53    922    675       C  
ATOM   3529  C   ILE A 322     100.658 225.791  -7.354  1.00 53.26           C  
ANISOU 3529  C   ILE A 322     6397   4042   9798    -21    986    702       C  
ATOM   3530  O   ILE A 322     101.466 226.720  -7.225  1.00 55.04           O  
ANISOU 3530  O   ILE A 322     6474   4114  10325    -66    987    652       O  
ATOM   3531  CB  ILE A 322     101.045 223.990  -9.093  1.00 43.00           C  
ANISOU 3531  CB  ILE A 322     4950   2903   8484     57   1317    829       C  
ATOM   3532  CG1 ILE A 322     101.918 222.767  -9.381  1.00 44.89           C  
ANISOU 3532  CG1 ILE A 322     5009   3139   8909     14   1275    791       C  
ATOM   3533  CG2 ILE A 322     101.435 225.171  -9.976  1.00 43.77           C  
ANISOU 3533  CG2 ILE A 322     4984   2930   8718    137   1677    930       C  
ATOM   3534  CD1 ILE A 322     101.802 222.249 -10.796  1.00 46.31           C  
ANISOU 3534  CD1 ILE A 322     5225   3411   8960    160   1629    929       C  
ATOM   3535  N   LEU A 323      99.339 225.985  -7.275  1.00 51.07           N  
ANISOU 3535  N   LEU A 323     6368   3946   9092     63   1026    763       N  
ATOM   3536  CA  LEU A 323      98.792 227.325  -7.093  1.00 51.51           C  
ANISOU 3536  CA  LEU A 323     6560   3949   9061    110   1117    808       C  
ATOM   3537  C   LEU A 323      99.197 227.926  -5.754  1.00 53.29           C  
ANISOU 3537  C   LEU A 323     6820   3947   9480     29    783    666       C  
ATOM   3538  O   LEU A 323      99.397 229.143  -5.656  1.00 55.21           O  
ANISOU 3538  O   LEU A 323     7055   4077   9847     24    830    654       O  
ATOM   3539  CB  LEU A 323      97.268 227.295  -7.227  1.00 35.20           C  
ANISOU 3539  CB  LEU A 323     4727   2188   6458    226   1181    872       C  
ATOM   3540  CG  LEU A 323      96.706 227.476  -8.639  1.00 34.98           C  
ANISOU 3540  CG  LEU A 323     4738   2328   6225    383   1533   1008       C  
ATOM   3541  CD1 LEU A 323      95.234 227.103  -8.696  1.00 33.28           C  
ANISOU 3541  CD1 LEU A 323     4684   2411   5551    487   1490   1012       C  
ATOM   3542  CD2 LEU A 323      96.906 228.908  -9.094  1.00 49.40           C  
ANISOU 3542  CD2 LEU A 323     6596   3987   8187    448   1809   1109       C  
ATOM   3543  N   ASN A 324      99.388 227.094  -4.732  1.00 53.10           N  
ANISOU 3543  N   ASN A 324     6857   3913   9404     -9    418    533       N  
ATOM   3544  CA  ASN A 324      99.771 227.595  -3.380  1.00 56.63           C  
ANISOU 3544  CA  ASN A 324     7396   4147   9972    -28     43    367       C  
ATOM   3545  C   ASN A 324     101.275 227.837  -3.310  1.00 57.38           C  
ANISOU 3545  C   ASN A 324     7195   4084  10522   -117   -105    226       C  
ATOM   3546  O   ASN A 324     101.714 228.511  -2.391  1.00 56.64           O  
ANISOU 3546  O   ASN A 324     7122   3828  10570   -120   -355     86       O  
ATOM   3547  CB  ASN A 324      99.277 226.719  -2.231  1.00 58.45           C  
ANISOU 3547  CB  ASN A 324     7863   4444   9901     26   -278    280       C  
ATOM   3548  CG  ASN A 324      98.063 227.307  -1.552  1.00 62.20           C  
ANISOU 3548  CG  ASN A 324     8698   4967   9969    138   -353    290       C  
ATOM   3549  OD1 ASN A 324      97.401 228.168  -2.105  1.00 62.32           O  
ANISOU 3549  OD1 ASN A 324     8842   5221   9614    194   -112    424       O  
ATOM   3550  ND2 ASN A 324      97.763 226.855  -0.352  1.00 65.37           N  
ANISOU 3550  ND2 ASN A 324     9265   5119  10455    190   -700    136       N  
ATOM   3551  N   VAL A 325     102.032 227.204  -4.192  1.00 57.15           N  
ANISOU 3551  N   VAL A 325     6883   4094  10737   -171     47    259       N  
ATOM   3552  CA  VAL A 325     103.458 227.502  -4.263  1.00 45.51           C  
ANISOU 3552  CA  VAL A 325     5065   2466   9762   -238    -19    158       C  
ATOM   3553  C   VAL A 325     103.691 228.815  -4.997  1.00 58.21           C  
ANISOU 3553  C   VAL A 325     6524   3982  11612   -242    310    243       C  
ATOM   3554  O   VAL A 325     104.472 229.665  -4.552  1.00 62.77           O  
ANISOU 3554  O   VAL A 325     6928   4373  12550   -279    169    127       O  
ATOM   3555  CB  VAL A 325     104.219 226.341  -4.928  1.00 45.47           C  
ANISOU 3555  CB  VAL A 325     4814   2522   9940   -267     70    182       C  
ATOM   3556  CG1 VAL A 325     105.622 226.783  -5.319  1.00 48.80           C  
ANISOU 3556  CG1 VAL A 325     4830   2782  10930   -307    154    139       C  
ATOM   3557  CG2 VAL A 325     104.283 225.149  -3.991  1.00 49.81           C  
ANISOU 3557  CG2 VAL A 325     5467   3111  10346   -266   -326     53       C  
ATOM   3558  N   LEU A 326     103.012 229.001  -6.131  1.00 55.75           N  
ANISOU 3558  N   LEU A 326     6283   3795  11105   -181    753    444       N  
ATOM   3559  CA  LEU A 326     103.132 230.252  -6.870  1.00 55.14           C  
ANISOU 3559  CA  LEU A 326     6118   3641  11193   -146   1114    546       C  
ATOM   3560  C   LEU A 326     102.629 231.435  -6.053  1.00 53.26           C  
ANISOU 3560  C   LEU A 326     6055   3306  10875   -150    955    484       C  
ATOM   3561  O   LEU A 326     103.147 232.549  -6.188  1.00 55.71           O  
ANISOU 3561  O   LEU A 326     6210   3460  11496   -167   1082    475       O  
ATOM   3562  CB  LEU A 326     102.362 230.157  -8.188  1.00 52.95           C  
ANISOU 3562  CB  LEU A 326     5971   3542  10607    -18   1585    764       C  
ATOM   3563  CG  LEU A 326     102.764 229.045  -9.158  1.00 50.77           C  
ANISOU 3563  CG  LEU A 326     5581   3356  10354     30   1798    845       C  
ATOM   3564  CD1 LEU A 326     101.774 228.952 -10.307  1.00 47.42           C  
ANISOU 3564  CD1 LEU A 326     5392   3117   9506    210   2172   1031       C  
ATOM   3565  CD2 LEU A 326     104.171 229.278  -9.680  1.00 55.38           C  
ANISOU 3565  CD2 LEU A 326     5806   3766  11469     12   2005    841       C  
ATOM   3566  N   LYS A 327     101.628 231.212  -5.199  1.00 50.69           N  
ANISOU 3566  N   LYS A 327     6052   3056  10151   -121    699    445       N  
ATOM   3567  CA  LYS A 327     101.047 232.300  -4.421  1.00 53.06           C  
ANISOU 3567  CA  LYS A 327     6576   3267  10318    -93    566    399       C  
ATOM   3568  C   LYS A 327     101.881 232.617  -3.186  1.00 57.26           C  
ANISOU 3568  C   LYS A 327     7053   3583  11121   -146    108    160       C  
ATOM   3569  O   LYS A 327     102.208 233.782  -2.931  1.00 59.11           O  
ANISOU 3569  O   LYS A 327     7231   3651  11578   -163     77     96       O  
ATOM   3570  CB  LYS A 327      99.617 231.948  -4.008  1.00 50.01           C  
ANISOU 3570  CB  LYS A 327     6563   3035   9403      1    521    470       C  
ATOM   3571  CG  LYS A 327      98.956 233.006  -3.139  1.00 51.34           C  
ANISOU 3571  CG  LYS A 327     7005   3108   9394     58    388    431       C  
ATOM   3572  CD  LYS A 327      97.665 232.500  -2.516  1.00 50.88           C  
ANISOU 3572  CD  LYS A 327     7296   3174   8864    168    313    489       C  
ATOM   3573  CE  LYS A 327      97.032 233.564  -1.628  1.00 53.42           C  
ANISOU 3573  CE  LYS A 327     7913   3384   8998    253    200    460       C  
ATOM   3574  NZ  LYS A 327      95.793 233.088  -0.950  1.00 53.53           N  
ANISOU 3574  NZ  LYS A 327     8263   3633   8443    374    149    511       N  
ATOM   3575  N   ARG A 328     102.227 231.597  -2.403  1.00 57.99           N  
ANISOU 3575  N   ARG A 328     7168   3680  11185   -151   -260     20       N  
ATOM   3576  CA  ARG A 328     102.849 231.826  -1.107  1.00 60.20           C  
ANISOU 3576  CA  ARG A 328     7478   3794  11603   -135   -750   -219       C  
ATOM   3577  C   ARG A 328     104.367 231.892  -1.178  1.00 62.35           C  
ANISOU 3577  C   ARG A 328     7302   3914  12474   -212   -891   -355       C  
ATOM   3578  O   ARG A 328     104.994 232.507  -0.307  1.00 65.54           O  
ANISOU 3578  O   ARG A 328     7639   4141  13122   -195  -1250   -550       O  
ATOM   3579  CB  ARG A 328     102.438 230.724  -0.126  1.00 59.69           C  
ANISOU 3579  CB  ARG A 328     7702   3813  11162    -45  -1091   -304       C  
ATOM   3580  CG  ARG A 328     100.940 230.642   0.140  1.00 60.19           C  
ANISOU 3580  CG  ARG A 328     8201   3999  10671     64   -983   -180       C  
ATOM   3581  CD  ARG A 328     100.497 231.628   1.223  1.00 64.15           C  
ANISOU 3581  CD  ARG A 328     9018   4390  10967    177  -1202   -275       C  
ATOM   3582  NE  ARG A 328      99.049 231.613   1.440  1.00 65.61           N  
ANISOU 3582  NE  ARG A 328     9593   4695  10643    299  -1048   -128       N  
ATOM   3583  CZ  ARG A 328      98.412 232.413   2.292  1.00 69.69           C  
ANISOU 3583  CZ  ARG A 328    10432   5166  10882    425  -1145   -155       C  
ATOM   3584  NH1 ARG A 328      99.091 233.294   3.013  1.00 74.31           N  
ANISOU 3584  NH1 ARG A 328    11009   5574  11649    444  -1429   -340       N  
ATOM   3585  NH2 ARG A 328      97.094 232.334   2.423  1.00 68.58           N  
ANISOU 3585  NH2 ARG A 328    10604   5170  10281    538   -959      6       N  
ATOM   3586  N   VAL A 329     104.982 231.277  -2.183  1.00 64.46           N  
ANISOU 3586  N   VAL A 329     7079   4815  12598  -1686   1431  -1141       N  
ATOM   3587  CA  VAL A 329     106.436 231.234  -2.211  1.00 66.86           C  
ANISOU 3587  CA  VAL A 329     7129   5188  13088  -1833   1531  -1297       C  
ATOM   3588  C   VAL A 329     106.943 232.216  -3.248  1.00 68.49           C  
ANISOU 3588  C   VAL A 329     7431   5201  13392  -1969   1858  -1167       C  
ATOM   3589  O   VAL A 329     107.769 233.084  -2.947  1.00 71.99           O  
ANISOU 3589  O   VAL A 329     7756   5574  14022  -2101   1940  -1296       O  
ATOM   3590  CB  VAL A 329     106.950 229.817  -2.505  1.00 59.00           C  
ANISOU 3590  CB  VAL A 329     5960   4385  12071  -1803   1486  -1335       C  
ATOM   3591  CG1 VAL A 329     108.454 229.847  -2.670  1.00 66.62           C  
ANISOU 3591  CG1 VAL A 329     6664   5410  13240  -1944   1619  -1491       C  
ATOM   3592  CG2 VAL A 329     106.548 228.877  -1.381  1.00 56.54           C  
ANISOU 3592  CG2 VAL A 329     5551   4260  11672  -1676   1148  -1470       C  
ATOM   3593  N   PHE A 330     106.469 232.068  -4.482  1.00 67.76           N  
ANISOU 3593  N   PHE A 330     7557   5018  13169  -1935   2048   -911       N  
ATOM   3594  CA  PHE A 330     106.879 232.958  -5.556  1.00 70.65           C  
ANISOU 3594  CA  PHE A 330     8064   5198  13582  -2051   2374   -747       C  
ATOM   3595  C   PHE A 330     106.127 234.283  -5.553  1.00 75.05           C  
ANISOU 3595  C   PHE A 330     8877   5523  14115  -2033   2404   -620       C  
ATOM   3596  O   PHE A 330     106.549 235.212  -6.247  1.00 77.67           O  
ANISOU 3596  O   PHE A 330     9314   5679  14519  -2146   2654   -510       O  
ATOM   3597  CB  PHE A 330     106.693 232.269  -6.906  1.00 68.99           C  
ANISOU 3597  CB  PHE A 330     8016   4988  13210  -2007   2572   -515       C  
ATOM   3598  CG  PHE A 330     107.662 231.153  -7.160  1.00 69.88           C  
ANISOU 3598  CG  PHE A 330     7870   5293  13389  -2064   2634   -634       C  
ATOM   3599  CD1 PHE A 330     108.912 231.411  -7.701  1.00 74.36           C  
ANISOU 3599  CD1 PHE A 330     8289   5857  14108  -2230   2906   -689       C  
ATOM   3600  CD2 PHE A 330     107.318 229.844  -6.875  1.00 66.81           C  
ANISOU 3600  CD2 PHE A 330     7382   5083  12918  -1945   2421   -696       C  
ATOM   3601  CE1 PHE A 330     109.801 230.381  -7.948  1.00 74.91           C  
ANISOU 3601  CE1 PHE A 330     8105   6114  14244  -2266   2961   -817       C  
ATOM   3602  CE2 PHE A 330     108.201 228.812  -7.119  1.00 66.98           C  
ANISOU 3602  CE2 PHE A 330     7158   5283  13010  -1983   2463   -815       C  
ATOM   3603  CZ  PHE A 330     109.444 229.080  -7.656  1.00 70.96           C  
ANISOU 3603  CZ  PHE A 330     7503   5794  13662  -2138   2733   -881       C  
ATOM   3604  N   GLY A 331     105.030 234.396  -4.809  1.00 76.25           N  
ANISOU 3604  N   GLY A 331     9131   5668  14173  -1893   2163   -634       N  
ATOM   3605  CA  GLY A 331     104.372 235.680  -4.669  1.00 79.78           C  
ANISOU 3605  CA  GLY A 331     9781   5903  14630  -1873   2165   -561       C  
ATOM   3606  C   GLY A 331     103.535 236.097  -5.855  1.00 80.30           C  
ANISOU 3606  C   GLY A 331    10195   5789  14525  -1778   2301   -247       C  
ATOM   3607  O   GLY A 331     103.314 237.297  -6.062  1.00 82.79           O  
ANISOU 3607  O   GLY A 331    10686   5889  14884  -1803   2385   -154       O  
ATOM   3608  N   MET A 332     103.050 235.138  -6.635  1.00 79.70           N  
ANISOU 3608  N   MET A 332    10236   5793  14254  -1657   2310    -85       N  
ATOM   3609  CA  MET A 332     102.275 235.454  -7.820  1.00 81.56           C  
ANISOU 3609  CA  MET A 332    10817   5877  14294  -1539   2421    217       C  
ATOM   3610  C   MET A 332     100.856 235.869  -7.442  1.00 83.29           C  
ANISOU 3610  C   MET A 332    11223   6020  14403  -1339   2194    272       C  
ATOM   3611  O   MET A 332     100.428 235.763  -6.287  1.00 82.43           O  
ANISOU 3611  O   MET A 332    10977   5996  14348  -1290   1969     82       O  
ATOM   3612  CB  MET A 332     102.253 234.268  -8.783  1.00 78.28           C  
ANISOU 3612  CB  MET A 332    10464   5577  13703  -1465   2503    356       C  
ATOM   3613  CG  MET A 332     103.522 234.127  -9.614  1.00 79.29           C  
ANISOU 3613  CG  MET A 332    10518   5717  13890  -1644   2819    392       C  
ATOM   3614  SD  MET A 332     103.314 233.034 -11.033  1.00 78.18           S  
ANISOU 3614  SD  MET A 332    10578   5644  13482  -1530   2976    627       S  
ATOM   3615  CE  MET A 332     104.864 233.282 -11.899  1.00 81.40           C  
ANISOU 3615  CE  MET A 332    10900   6041  13988  -1774   3399    649       C  
ATOM   3616  N   PHE A 333     100.129 236.360  -8.447  1.00 85.56           N  
ANISOU 3616  N   PHE A 333    11833   6150  14526  -1215   2257    533       N  
ATOM   3617  CA  PHE A 333      98.745 236.817  -8.347  1.00 85.37           C  
ANISOU 3617  CA  PHE A 333    12015   6036  14388  -1000   2057    616       C  
ATOM   3618  C   PHE A 333      98.583 238.039  -7.453  1.00 91.00           C  
ANISOU 3618  C   PHE A 333    12703   6602  15270  -1049   1983    488       C  
ATOM   3619  O   PHE A 333      97.450 238.459  -7.188  1.00 90.59           O  
ANISOU 3619  O   PHE A 333    12779   6481  15161   -877   1805    506       O  
ATOM   3620  CB  PHE A 333      97.812 235.696  -7.857  1.00 78.36           C  
ANISOU 3620  CB  PHE A 333    11047   5340  13384   -814   1805    539       C  
ATOM   3621  CG  PHE A 333      98.017 234.385  -8.556  1.00 74.52           C  
ANISOU 3621  CG  PHE A 333    10541   5007  12767   -771   1852    615       C  
ATOM   3622  CD1 PHE A 333      97.700 234.240  -9.893  1.00 74.70           C  
ANISOU 3622  CD1 PHE A 333    10834   4969  12580   -651   1953    872       C  
ATOM   3623  CD2 PHE A 333      98.509 233.291  -7.862  1.00 71.78           C  
ANISOU 3623  CD2 PHE A 333     9915   4863  12497   -837   1779    425       C  
ATOM   3624  CE1 PHE A 333      97.884 233.030 -10.535  1.00 73.21           C  
ANISOU 3624  CE1 PHE A 333    10625   4953  12237   -596   1980    922       C  
ATOM   3625  CE2 PHE A 333      98.695 232.078  -8.501  1.00 70.70           C  
ANISOU 3625  CE2 PHE A 333     9741   4924  12198   -779   1782    476       C  
ATOM   3626  CZ  PHE A 333      98.383 231.949  -9.838  1.00 71.32           C  
ANISOU 3626  CZ  PHE A 333    10073   4986  12041   -657   1874    711       C  
ATOM   3627  N   ALA A 334      99.688 238.617  -6.980  1.00 97.29           N  
ANISOU 3627  N   ALA A 334    13330   7350  16285  -1272   2111    344       N  
ATOM   3628  CA  ALA A 334      99.610 239.785  -6.111  1.00102.71           C  
ANISOU 3628  CA  ALA A 334    13989   7890  17148  -1325   2046    202       C  
ATOM   3629  C   ALA A 334      99.007 240.972  -6.852  1.00111.06           C  
ANISOU 3629  C   ALA A 334    15361   8667  18170  -1252   2103    421       C  
ATOM   3630  O   ALA A 334      97.980 241.525  -6.440  1.00111.88           O  
ANISOU 3630  O   ALA A 334    15575   8680  18256  -1103   1929    402       O  
ATOM   3631  CB  ALA A 334     101.000 240.128  -5.567  1.00103.79           C  
ANISOU 3631  CB  ALA A 334    13873   8030  17531  -1577   2177      5       C  
ATOM   3632  N   HIS A 335      99.634 241.378  -7.953  1.00117.63           N  
ANISOU 3632  N   HIS A 335    16343   9359  18991  -1352   2349    628       N  
ATOM   3633  CA  HIS A 335      99.099 242.431  -8.809  1.00122.70           C  
ANISOU 3633  CA  HIS A 335    17317   9734  19571  -1274   2407    876       C  
ATOM   3634  C   HIS A 335      98.201 241.767  -9.845  1.00125.49           C  
ANISOU 3634  C   HIS A 335    17914  10142  19622  -1043   2345   1123       C  
ATOM   3635  O   HIS A 335      98.683 241.044 -10.724  1.00125.51           O  
ANISOU 3635  O   HIS A 335    17958  10243  19486  -1071   2509   1258       O  
ATOM   3636  CB  HIS A 335     100.225 243.231  -9.462  1.00124.47           C  
ANISOU 3636  CB  HIS A 335    17592   9776  19925  -1498   2713    983       C  
ATOM   3637  CG  HIS A 335     101.159 243.875  -8.481  1.00124.12           C  
ANISOU 3637  CG  HIS A 335    17290   9678  20193  -1722   2768    726       C  
ATOM   3638  ND1 HIS A 335     102.193 243.191  -7.878  1.00122.54           N  
ANISOU 3638  ND1 HIS A 335    16753   9680  20126  -1886   2820    495       N  
ATOM   3639  CD2 HIS A 335     101.213 245.140  -7.998  1.00126.60           C  
ANISOU 3639  CD2 HIS A 335    17633   9756  20715  -1800   2763    655       C  
ATOM   3640  CE1 HIS A 335     102.844 244.008  -7.068  1.00124.38           C  
ANISOU 3640  CE1 HIS A 335    16815   9813  20629  -2048   2839    288       C  
ATOM   3641  NE2 HIS A 335     102.269 245.196  -7.122  1.00127.10           N  
ANISOU 3641  NE2 HIS A 335    17378   9889  21026  -2006   2813    380       N  
ATOM   3642  N   THR A 336      96.898 242.002  -9.736  1.00127.62           N  
ANISOU 3642  N   THR A 336    18337  10357  19794   -808   2105   1164       N  
ATOM   3643  CA  THR A 336      95.915 241.271 -10.523  1.00129.59           C  
ANISOU 3643  CA  THR A 336    18768  10699  19773   -555   1974   1337       C  
ATOM   3644  C   THR A 336      95.567 242.013 -11.809  1.00136.88           C  
ANISOU 3644  C   THR A 336    20053  11412  20542   -447   2043   1650       C  
ATOM   3645  O   THR A 336      95.325 243.226 -11.794  1.00140.62           O  
ANISOU 3645  O   THR A 336    20670  11639  21119   -442   2024   1706       O  
ATOM   3646  CB  THR A 336      94.646 241.027  -9.700  1.00126.56           C  
ANISOU 3646  CB  THR A 336    18319  10398  19368   -341   1661   1189       C  
ATOM   3647  OG1 THR A 336      94.301 242.221  -8.985  1.00128.13           O  
ANISOU 3647  OG1 THR A 336    18538  10404  19742   -344   1578   1085       O  
ATOM   3648  CG2 THR A 336      94.864 239.891  -8.712  1.00122.60           C  
ANISOU 3648  CG2 THR A 336    17502  10167  18913   -395   1588    945       C  
ATOM   3649  N   GLU A 337      95.559 241.277 -12.918  1.00140.01           N  
ANISOU 3649  N   GLU A 337    20604  11907  20685   -355   2121   1851       N  
ATOM   3650  CA  GLU A 337      94.946 241.733 -14.157  1.00144.58           C  
ANISOU 3650  CA  GLU A 337    21544  12352  21037   -169   2108   2148       C  
ATOM   3651  C   GLU A 337      93.454 241.426 -14.170  1.00143.34           C  
ANISOU 3651  C   GLU A 337    21465  12259  20739    154   1760   2152       C  
ATOM   3652  O   GLU A 337      92.646 242.272 -14.569  1.00147.20           O  
ANISOU 3652  O   GLU A 337    22167  12571  21192    322   1621   2284       O  
ATOM   3653  CB  GLU A 337      95.633 241.077 -15.360  1.00146.18           C  
ANISOU 3653  CB  GLU A 337    21892  12651  20997   -206   2357   2349       C  
ATOM   3654  CG  GLU A 337      95.276 241.676 -16.712  1.00150.80           C  
ANISOU 3654  CG  GLU A 337    22876  13092  21329    -59   2413   2674       C  
ATOM   3655  CD  GLU A 337      95.775 240.824 -17.862  1.00152.91           C  
ANISOU 3655  CD  GLU A 337    23296  13512  21290    -41   2620   2844       C  
ATOM   3656  OE1 GLU A 337      95.637 239.584 -17.778  1.00150.55           O  
ANISOU 3656  OE1 GLU A 337    22873  13452  20878     39   2537   2744       O  
ATOM   3657  OE2 GLU A 337      96.314 241.386 -18.839  1.00157.79           O  
ANISOU 3657  OE2 GLU A 337    24162  14011  21780   -108   2873   3073       O  
ATOM   3658  N   ASP A 338      93.078 240.228 -13.731  1.00130.53           N  
ANISOU 3658  N   ASP A 338    19653  10884  19058    243   1612   2000       N  
ATOM   3659  CA  ASP A 338      91.680 239.885 -13.497  1.00121.24           C  
ANISOU 3659  CA  ASP A 338    18460   9791  17814    522   1276   1934       C  
ATOM   3660  C   ASP A 338      91.645 238.869 -12.367  1.00110.14           C  
ANISOU 3660  C   ASP A 338    16730   8609  16509    479   1181   1663       C  
ATOM   3661  O   ASP A 338      92.281 237.815 -12.460  1.00110.58           O  
ANISOU 3661  O   ASP A 338    16672   8843  16500    394   1291   1634       O  
ATOM   3662  CB  ASP A 338      91.010 239.336 -14.761  1.00120.00           C  
ANISOU 3662  CB  ASP A 338    18531   9718  17345    774   1176   2143       C  
ATOM   3663  CG  ASP A 338      91.706 238.106 -15.305  1.00112.51           C  
ANISOU 3663  CG  ASP A 338    17565   8976  16208    722   1333   2183       C  
ATOM   3664  OD1 ASP A 338      92.953 238.056 -15.248  1.00110.76           O  
ANISOU 3664  OD1 ASP A 338    17276   8745  16063    465   1623   2177       O  
ATOM   3665  OD2 ASP A 338      91.008 237.188 -15.783  1.00108.59           O  
ANISOU 3665  OD2 ASP A 338    17106   8651  15503    939   1160   2204       O  
ATOM   3666  N   ARG A 339      90.933 239.196 -11.288  1.00 97.66           N  
ANISOU 3666  N   ARG A 339    15005   7015  15085    534    991   1463       N  
ATOM   3667  CA  ARG A 339      90.888 238.303 -10.139  1.00 90.90           C  
ANISOU 3667  CA  ARG A 339    13849   6373  14315    487    914   1208       C  
ATOM   3668  C   ARG A 339      89.865 237.191 -10.309  1.00 86.93           C  
ANISOU 3668  C   ARG A 339    13298   6070  13662    719    700   1188       C  
ATOM   3669  O   ARG A 339      89.920 236.200  -9.572  1.00 85.05           O  
ANISOU 3669  O   ARG A 339    12824   6035  13458    678    663   1023       O  
ATOM   3670  CB  ARG A 339      90.581 239.092  -8.865  1.00 89.69           C  
ANISOU 3670  CB  ARG A 339    13568   6147  14363    446    835    989       C  
ATOM   3671  CG  ARG A 339      89.189 239.699  -8.842  1.00 90.02           C  
ANISOU 3671  CG  ARG A 339    13727   6091  14384    701    604    984       C  
ATOM   3672  CD  ARG A 339      88.955 240.543  -7.596  1.00 89.21           C  
ANISOU 3672  CD  ARG A 339    13520   5908  14468    658    570    762       C  
ATOM   3673  NE  ARG A 339      88.936 239.750  -6.368  1.00 84.95           N  
ANISOU 3673  NE  ARG A 339    12688   5604  13987    597    545    515       N  
ATOM   3674  CZ  ARG A 339      87.887 239.050  -5.946  1.00 81.58           C  
ANISOU 3674  CZ  ARG A 339    12145   5354  13497    771    388    409       C  
ATOM   3675  NH1 ARG A 339      86.769 239.032  -6.657  1.00 81.13           N  
ANISOU 3675  NH1 ARG A 339    12232   5275  13319   1026    235    509       N  
ATOM   3676  NH2 ARG A 339      87.955 238.362  -4.815  1.00 79.55           N  
ANISOU 3676  NH2 ARG A 339    11621   5302  13301    690    380    201       N  
ATOM   3677  N   GLU A 340      88.939 237.336 -11.259  1.00 87.99           N  
ANISOU 3677  N   GLU A 340    13635   6153  13644    961    546   1347       N  
ATOM   3678  CA  GLU A 340      87.915 236.319 -11.465  1.00 86.26           C  
ANISOU 3678  CA  GLU A 340    13350   6123  13302   1191    321   1312       C  
ATOM   3679  C   GLU A 340      88.544 234.982 -11.836  1.00 81.55           C  
ANISOU 3679  C   GLU A 340    12685   5726  12575   1137    416   1336       C  
ATOM   3680  O   GLU A 340      88.234 233.947 -11.234  1.00 80.05           O  
ANISOU 3680  O   GLU A 340    12277   5727  12410   1165    317   1183       O  
ATOM   3681  CB  GLU A 340      86.935 236.784 -12.545  1.00 91.63           C  
ANISOU 3681  CB  GLU A 340    14236   6718  13861   1449    148   1487       C  
ATOM   3682  CG  GLU A 340      85.579 236.095 -12.507  1.00 94.32           C  
ANISOU 3682  CG  GLU A 340    14420   7223  14192   1698   -126   1391       C  
ATOM   3683  CD  GLU A 340      85.560 234.785 -13.268  1.00 98.14           C  
ANISOU 3683  CD  GLU A 340    14910   7936  14444   1790   -163   1441       C  
ATOM   3684  OE1 GLU A 340      86.152 234.724 -14.366  1.00101.68           O  
ANISOU 3684  OE1 GLU A 340    15602   8370  14663   1793    -55   1635       O  
ATOM   3685  OE2 GLU A 340      84.952 233.815 -12.767  1.00 97.72           O  
ANISOU 3685  OE2 GLU A 340    14626   8078  14425   1860   -290   1280       O  
ATOM   3686  N   THR A 341      89.451 234.991 -12.817  1.00 77.86           N  
ANISOU 3686  N   THR A 341    12403   5211  11968   1054    624   1526       N  
ATOM   3687  CA  THR A 341      90.097 233.753 -13.242  1.00 74.41           C  
ANISOU 3687  CA  THR A 341    11929   4944  11401   1014    731   1549       C  
ATOM   3688  C   THR A 341      90.931 233.147 -12.120  1.00 70.67           C  
ANISOU 3688  C   THR A 341    11142   4575  11134    781    839   1348       C  
ATOM   3689  O   THR A 341      90.990 231.921 -11.972  1.00 68.70           O  
ANISOU 3689  O   THR A 341    10692   4607  10805    776    745   1233       O  
ATOM   3690  CB  THR A 341      90.964 234.014 -14.475  1.00 78.31           C  
ANISOU 3690  CB  THR A 341    12695   5353  11705    955    976   1784       C  
ATOM   3691  OG1 THR A 341      90.160 234.590 -15.512  1.00 81.10           O  
ANISOU 3691  OG1 THR A 341    13338   5630  11845   1181    849   1971       O  
ATOM   3692  CG2 THR A 341      91.578 232.716 -14.983  1.00 78.41           C  
ANISOU 3692  CG2 THR A 341    12649   5596  11547    925   1055   1775       C  
ATOM   3693  N   VAL A 342      91.575 233.990 -11.312  1.00 69.45           N  
ANISOU 3693  N   VAL A 342    10888   4305  11194    568    962   1257       N  
ATOM   3694  CA  VAL A 342      92.403 233.483 -10.222  1.00 66.57           C  
ANISOU 3694  CA  VAL A 342    10222   4050  11023    350   1035   1050       C  
ATOM   3695  C   VAL A 342      91.535 232.888  -9.119  1.00 63.32           C  
ANISOU 3695  C   VAL A 342     9579   3796  10682    438    799    847       C  
ATOM   3696  O   VAL A 342      91.849 231.825  -8.570  1.00 51.90           O  
ANISOU 3696  O   VAL A 342     7897   2601   9223    367    740    706       O  
ATOM   3697  CB  VAL A 342      93.323 234.597  -9.688  1.00 58.75           C  
ANISOU 3697  CB  VAL A 342     9190   2910  10221    112   1206    988       C  
ATOM   3698  CG1 VAL A 342      94.186 234.078  -8.551  1.00 56.93           C  
ANISOU 3698  CG1 VAL A 342     8642   2814  10176    -95   1243    754       C  
ATOM   3699  CG2 VAL A 342      94.188 235.148 -10.811  1.00 61.71           C  
ANISOU 3699  CG2 VAL A 342     9777   3140  10529      8   1465   1197       C  
ATOM   3700  N   TYR A 343      90.432 233.557  -8.776  1.00 54.70           N  
ANISOU 3700  N   TYR A 343     8537   2644   9604    586    633    809       N  
ATOM   3701  CA  TYR A 343      89.546 233.015  -7.752  1.00 52.52           C  
ANISOU 3701  CA  TYR A 343     8047   2526   9382    668    441    620       C  
ATOM   3702  C   TYR A 343      88.732 231.841  -8.279  1.00 54.17           C  
ANISOU 3702  C   TYR A 343     8220   2913   9447    856    271    653       C  
ATOM   3703  O   TYR A 343      88.286 230.995  -7.493  1.00 48.85           O  
ANISOU 3703  O   TYR A 343     7324   2446   8791    865    147    499       O  
ATOM   3704  CB  TYR A 343      88.625 234.111  -7.215  1.00 53.81           C  
ANISOU 3704  CB  TYR A 343     8262   2577   9606    766    344    548       C  
ATOM   3705  CG  TYR A 343      89.226 234.897  -6.073  1.00 54.28           C  
ANISOU 3705  CG  TYR A 343     8212   2571   9841    577    438    386       C  
ATOM   3706  CD1 TYR A 343      90.049 235.991  -6.310  1.00 62.51           C  
ANISOU 3706  CD1 TYR A 343     9385   3406  10959    439    593    450       C  
ATOM   3707  CD2 TYR A 343      88.976 234.540  -4.756  1.00 52.58           C  
ANISOU 3707  CD2 TYR A 343     7761   2504   9712    537    371    165       C  
ATOM   3708  CE1 TYR A 343      90.603 236.710  -5.264  1.00 62.82           C  
ANISOU 3708  CE1 TYR A 343     9311   3390  11168    272    660    280       C  
ATOM   3709  CE2 TYR A 343      89.521 235.250  -3.706  1.00 58.70           C  
ANISOU 3709  CE2 TYR A 343     8443   3227  10632    382    439      2       C  
ATOM   3710  CZ  TYR A 343      90.333 236.334  -3.964  1.00 60.85           C  
ANISOU 3710  CZ  TYR A 343     8836   3296  10989    253    575     51       C  
ATOM   3711  OH  TYR A 343      90.875 237.038  -2.913  1.00 61.64           O  
ANISOU 3711  OH  TYR A 343     8830   3349  11242    104    624   -133       O  
ATOM   3712  N   ALA A 344      88.525 231.770  -9.597  1.00 55.35           N  
ANISOU 3712  N   ALA A 344     8590   3032   9410   1000    252    839       N  
ATOM   3713  CA  ALA A 344      87.855 230.613 -10.181  1.00 52.47           C  
ANISOU 3713  CA  ALA A 344     8183   2889   8864   1161     71    841       C  
ATOM   3714  C   ALA A 344      88.753 229.383 -10.126  1.00 52.48           C  
ANISOU 3714  C   ALA A 344     8018   3126   8798   1012    130    780       C  
ATOM   3715  O   ALA A 344      88.330 228.315  -9.667  1.00 52.39           O  
ANISOU 3715  O   ALA A 344     7802   3322   8781   1036    -10    656       O  
ATOM   3716  CB  ALA A 344      87.435 230.915 -11.620  1.00 53.30           C  
ANISOU 3716  CB  ALA A 344     8589   2897   8764   1369     20   1045       C  
ATOM   3717  N   TRP A 345      90.002 229.517 -10.586  1.00 52.60           N  
ANISOU 3717  N   TRP A 345     8110   3100   8775    854    346    865       N  
ATOM   3718  CA  TRP A 345      90.946 228.404 -10.521  1.00 49.74           C  
ANISOU 3718  CA  TRP A 345     7577   2948   8375    715    408    792       C  
ATOM   3719  C   TRP A 345      91.166 227.948  -9.085  1.00 47.14           C  
ANISOU 3719  C   TRP A 345     6958   2734   8219    578    361    592       C  
ATOM   3720  O   TRP A 345      91.343 226.752  -8.826  1.00 45.04           O  
ANISOU 3720  O   TRP A 345     6516   2677   7918    554    285    502       O  
ATOM   3721  CB  TRP A 345      92.280 228.801 -11.157  1.00 52.08           C  
ANISOU 3721  CB  TRP A 345     7981   3158   8650    553    679    895       C  
ATOM   3722  CG  TRP A 345      92.364 228.543 -12.635  1.00 56.06           C  
ANISOU 3722  CG  TRP A 345     8714   3688   8899    666    737   1065       C  
ATOM   3723  CD1 TRP A 345      92.269 229.465 -13.637  1.00 59.44           C  
ANISOU 3723  CD1 TRP A 345     9461   3922   9201    746    846   1274       C  
ATOM   3724  CD2 TRP A 345      92.564 227.276 -13.275  1.00 56.21           C  
ANISOU 3724  CD2 TRP A 345     8678   3938   8741    720    687   1037       C  
ATOM   3725  NE1 TRP A 345      92.396 228.852 -14.860  1.00 60.72           N  
ANISOU 3725  NE1 TRP A 345     9779   4200   9094    850    871   1378       N  
ATOM   3726  CE2 TRP A 345      92.578 227.508 -14.665  1.00 58.75           C  
ANISOU 3726  CE2 TRP A 345     9295   4212   8817    835    773   1222       C  
ATOM   3727  CE3 TRP A 345      92.732 225.969 -12.808  1.00 54.62           C  
ANISOU 3727  CE3 TRP A 345     8221   3969   8565    688    577    874       C  
ATOM   3728  CZ2 TRP A 345      92.752 226.480 -15.592  1.00 59.11           C  
ANISOU 3728  CZ2 TRP A 345     9374   4448   8636    920    751   1224       C  
ATOM   3729  CZ3 TRP A 345      92.904 224.950 -13.730  1.00 54.29           C  
ANISOU 3729  CZ3 TRP A 345     8206   4095   8329    769    552    880       C  
ATOM   3730  CH2 TRP A 345      92.913 225.212 -15.105  1.00 56.39           C  
ANISOU 3730  CH2 TRP A 345     8755   4322   8347    884    638   1042       C  
ATOM   3731  N   PHE A 346      91.199 228.896  -8.165  1.00 47.69           N  
ANISOU 3731  N   PHE A 346     6988   2663   8470    495    402    518       N  
ATOM   3732  CA  PHE A 346      91.383 228.509  -6.750  1.00 46.95           C  
ANISOU 3732  CA  PHE A 346     6648   2681   8508    378    354    327       C  
ATOM   3733  C   PHE A 346      90.146 227.743  -6.289  1.00 47.78           C  
ANISOU 3733  C   PHE A 346     6638   2937   8581    513    148    243       C  
ATOM   3734  O   PHE A 346      90.302 226.702  -5.758  1.00 46.09           O  
ANISOU 3734  O   PHE A 346     6235   2905   8371    453     84    135       O  
ATOM   3735  CB  PHE A 346      91.694 229.728  -5.890  1.00 46.29           C  
ANISOU 3735  CB  PHE A 346     6567   2404   8616    262    449    252       C  
ATOM   3736  CG  PHE A 346      93.146 229.887  -5.535  1.00 51.09           C  
ANISOU 3736  CG  PHE A 346     7067   3004   9341     32    602    173       C  
ATOM   3737  CD1 PHE A 346      94.015 230.535  -6.381  1.00 53.65           C  
ANISOU 3737  CD1 PHE A 346     7516   3158   9713    -78    810    280       C  
ATOM   3738  CD2 PHE A 346      93.637 229.413  -4.340  1.00 49.06           C  
ANISOU 3738  CD2 PHE A 346     6581   2909   9150    -73    539    -10       C  
ATOM   3739  CE1 PHE A 346      95.340 230.699  -6.040  1.00 54.44           C  
ANISOU 3739  CE1 PHE A 346     7479   3251   9957   -297    951    183       C  
ATOM   3740  CE2 PHE A 346      94.961 229.576  -4.000  1.00 45.95           C  
ANISOU 3740  CE2 PHE A 346     6066   2515   8880   -270    648   -107       C  
ATOM   3741  CZ  PHE A 346      95.809 230.218  -4.853  1.00 53.46           C  
ANISOU 3741  CZ  PHE A 346     7106   3297   9910   -387    855    -23       C  
ATOM   3742  N   ALA A 347      88.946 228.236  -6.546  1.00 50.82           N  
ANISOU 3742  N   ALA A 347     7130   3239   8942    698     46    293       N  
ATOM   3743  CA  ALA A 347      87.732 227.518  -6.112  1.00 47.58           C  
ANISOU 3743  CA  ALA A 347     6590   2965   8524    823   -132    208       C  
ATOM   3744  C   ALA A 347      87.641 226.154  -6.805  1.00 49.47           C  
ANISOU 3744  C   ALA A 347     6777   3391   8630    884   -232    236       C  
ATOM   3745  O   ALA A 347      87.221 225.214  -6.166  1.00 48.69           O  
ANISOU 3745  O   ALA A 347     6502   3449   8550    883   -329    141       O  
ATOM   3746  CB  ALA A 347      86.537 228.367  -6.422  1.00 45.03           C  
ANISOU 3746  CB  ALA A 347     6374   2498   8237   1016   -224    233       C  
ATOM   3747  N   PHE A 348      87.981 226.068  -8.086  1.00 51.01           N  
ANISOU 3747  N   PHE A 348     7128   3565   8689    933   -199    364       N  
ATOM   3748  CA  PHE A 348      87.896 224.779  -8.810  1.00 50.38           C  
ANISOU 3748  CA  PHE A 348     7006   3656   8480    995   -294    371       C  
ATOM   3749  C   PHE A 348      88.869 223.761  -8.236  1.00 50.18           C  
ANISOU 3749  C   PHE A 348     6799   3782   8485    830   -246    288       C  
ATOM   3750  O   PHE A 348      88.471 222.653  -7.968  1.00 50.36           O  
ANISOU 3750  O   PHE A 348     6670   3949   8515    848   -365    211       O  
ATOM   3751  CB  PHE A 348      88.346 224.951 -10.255  1.00 43.32           C  
ANISOU 3751  CB  PHE A 348     6345   2708   7406   1088   -249    519       C  
ATOM   3752  CG  PHE A 348      88.681 223.660 -10.947  1.00 42.67           C  
ANISOU 3752  CG  PHE A 348     6225   2799   7189   1109   -293    507       C  
ATOM   3753  CD1 PHE A 348      87.688 222.778 -11.321  1.00 42.27           C  
ANISOU 3753  CD1 PHE A 348     6129   2858   7075   1269   -503    457       C  
ATOM   3754  CD2 PHE A 348      89.987 223.329 -11.234  1.00 42.68           C  
ANISOU 3754  CD2 PHE A 348     6222   2847   7147    969   -126    526       C  
ATOM   3755  CE1 PHE A 348      87.989 221.597 -11.971  1.00 45.70           C  
ANISOU 3755  CE1 PHE A 348     6528   3437   7398   1292   -549    426       C  
ATOM   3756  CE2 PHE A 348      90.289 222.145 -11.880  1.00 47.70           C  
ANISOU 3756  CE2 PHE A 348     6819   3637   7668    999   -165    496       C  
ATOM   3757  CZ  PHE A 348      89.290 221.283 -12.247  1.00 46.20           C  
ANISOU 3757  CZ  PHE A 348     6599   3546   7408   1162   -379    446       C  
ATOM   3758  N   SER A 349      90.104 224.173  -7.989  1.00 50.34           N  
ANISOU 3758  N   SER A 349     6828   3762   8539    668    -75    300       N  
ATOM   3759  CA  SER A 349      91.139 223.256  -7.461  1.00 47.48           C  
ANISOU 3759  CA  SER A 349     6288   3537   8215    529    -47    213       C  
ATOM   3760  C   SER A 349      90.777 222.762  -6.070  1.00 47.45           C  
ANISOU 3760  C   SER A 349     6104   3612   8313    478   -140     92       C  
ATOM   3761  O   SER A 349      91.248 221.699  -5.729  1.00 47.10           O  
ANISOU 3761  O   SER A 349     5919   3705   8272    428   -196     30       O  
ATOM   3762  CB  SER A 349      92.481 223.863  -7.501  1.00 46.70           C  
ANISOU 3762  CB  SER A 349     6203   3367   8176    363    150    220       C  
ATOM   3763  OG  SER A 349      92.412 225.211  -7.124  1.00 47.37           O  
ANISOU 3763  OG  SER A 349     6330   3288   8379    295    228    207       O  
ATOM   3764  N   HIS A 350      90.051 223.570  -5.301  1.00 48.47           N  
ANISOU 3764  N   HIS A 350     6246   3652   8518    495   -151     58       N  
ATOM   3765  CA  HIS A 350      89.659 223.265  -3.903  1.00 45.65           C  
ANISOU 3765  CA  HIS A 350     5742   3380   8224    463   -223    -53       C  
ATOM   3766  C   HIS A 350      88.592 222.190  -3.897  1.00 43.63           C  
ANISOU 3766  C   HIS A 350     5406   3245   7927    565   -362    -59       C  
ATOM   3767  O   HIS A 350      88.550 221.419  -2.969  1.00 41.09           O  
ANISOU 3767  O   HIS A 350     4957   3047   7609    508   -409   -110       O  
ATOM   3768  CB  HIS A 350      89.041 224.501  -3.275  1.00 46.56           C  
ANISOU 3768  CB  HIS A 350     5897   3370   8425    481   -194   -101       C  
ATOM   3769  CG  HIS A 350      90.024 225.401  -2.624  1.00 49.87           C  
ANISOU 3769  CG  HIS A 350     6311   3707   8929    336    -82   -169       C  
ATOM   3770  ND1 HIS A 350      90.133 225.492  -1.267  1.00 51.19           N  
ANISOU 3770  ND1 HIS A 350     6377   3965   9109    194    -53   -232       N  
ATOM   3771  CD2 HIS A 350      90.922 226.256  -3.133  1.00 52.63           C  
ANISOU 3771  CD2 HIS A 350     6738   3885   9375    314     -7   -203       C  
ATOM   3772  CE1 HIS A 350      91.047 226.370  -0.966  1.00 52.03           C  
ANISOU 3772  CE1 HIS A 350     6486   3968   9317     86     32   -312       C  
ATOM   3773  NE2 HIS A 350      91.558 226.831  -2.081  1.00 53.30           N  
ANISOU 3773  NE2 HIS A 350     6758   3962   9533    149     68   -294       N  
ATOM   3774  N   TRP A 351      87.716 222.236  -4.883  1.00 44.20           N  
ANISOU 3774  N   TRP A 351     5554   3272   7967    718   -436     -8       N  
ATOM   3775  CA  TRP A 351      86.643 221.223  -5.038  1.00 44.15           C  
ANISOU 3775  CA  TRP A 351     5457   3365   7952    813   -574    -32       C  
ATOM   3776  C   TRP A 351      87.255 219.865  -5.376  1.00 42.72           C  
ANISOU 3776  C   TRP A 351     5224   3296   7712    778   -613    -21       C  
ATOM   3777  O   TRP A 351      86.807 218.862  -4.826  1.00 41.94           O  
ANISOU 3777  O   TRP A 351     4999   3289   7647    775   -697    -66       O  
ATOM   3778  CB  TRP A 351      85.654 221.661  -6.117  1.00 37.19           C  
ANISOU 3778  CB  TRP A 351     4674   2411   7044    999   -668      7       C  
ATOM   3779  CG  TRP A 351      84.715 220.579  -6.539  1.00 42.67           C  
ANISOU 3779  CG  TRP A 351     5275   3200   7737   1100   -824    -31       C  
ATOM   3780  CD1 TRP A 351      83.601 220.165  -5.885  1.00 42.59           C  
ANISOU 3780  CD1 TRP A 351     5108   3237   7837   1135   -905   -117       C  
ATOM   3781  CD2 TRP A 351      84.822 219.758  -7.712  1.00 44.27           C  
ANISOU 3781  CD2 TRP A 351     5525   3458   7837   1173   -909     -1       C  
ATOM   3782  NE1 TRP A 351      83.000 219.157  -6.576  1.00 44.04           N  
ANISOU 3782  NE1 TRP A 351     5227   3489   8016   1215  -1044   -147       N  
ATOM   3783  CE2 TRP A 351      83.730 218.880  -7.696  1.00 44.17           C  
ANISOU 3783  CE2 TRP A 351     5373   3515   7895   1247  -1060    -83       C  
ATOM   3784  CE3 TRP A 351      85.733 219.675  -8.767  1.00 43.83           C  
ANISOU 3784  CE3 TRP A 351     5611   3403   7640   1179   -862     73       C  
ATOM   3785  CZ2 TRP A 351      83.533 217.932  -8.691  1.00 42.55           C  
ANISOU 3785  CZ2 TRP A 351     5169   3372   7628   1334  -1188   -104       C  
ATOM   3786  CZ3 TRP A 351      85.532 218.750  -9.757  1.00 37.64           C  
ANISOU 3786  CZ3 TRP A 351     4839   2696   6769   1274   -977     57       C  
ATOM   3787  CH2 TRP A 351      84.445 217.889  -9.714  1.00 39.88           C  
ANISOU 3787  CH2 TRP A 351     4984   3040   7128   1353  -1150    -37       C  
ATOM   3788  N   LEU A 352      88.302 219.883  -6.202  1.00 42.60           N  
ANISOU 3788  N   LEU A 352     5301   3265   7619    748   -541     34       N  
ATOM   3789  CA  LEU A 352      89.033 218.703  -6.724  1.00 40.96           C  
ANISOU 3789  CA  LEU A 352     5043   3158   7361    728   -570     26       C  
ATOM   3790  C   LEU A 352      89.649 217.912  -5.576  1.00 40.79           C  
ANISOU 3790  C   LEU A 352     4869   3219   7408    601   -570    -35       C  
ATOM   3791  O   LEU A 352      89.812 216.733  -5.744  1.00 41.26           O  
ANISOU 3791  O   LEU A 352     4856   3359   7462    603   -636    -57       O  
ATOM   3792  CB  LEU A 352      90.080 219.169  -7.736  1.00 35.90           C  
ANISOU 3792  CB  LEU A 352     4530   2483   6627    715   -452     89       C  
ATOM   3793  CG  LEU A 352      90.483 218.159  -8.803  1.00 39.54           C  
ANISOU 3793  CG  LEU A 352     5013   3027   6984    780   -489     91       C  
ATOM   3794  CD1 LEU A 352      89.283 217.414  -9.337  1.00 39.72           C  
ANISOU 3794  CD1 LEU A 352     5028   3090   6974    931   -673     66       C  
ATOM   3795  CD2 LEU A 352      91.215 218.835  -9.938  1.00 37.65           C  
ANISOU 3795  CD2 LEU A 352     4954   2732   6618    799   -345    178       C  
ATOM   3796  N   VAL A 353      90.084 218.573  -4.513  1.00 41.19           N  
ANISOU 3796  N   VAL A 353     4880   3249   7521    502   -509    -69       N  
ATOM   3797  CA  VAL A 353      90.660 217.897  -3.319  1.00 40.88           C  
ANISOU 3797  CA  VAL A 353     4722   3292   7519    401   -528   -122       C  
ATOM   3798  C   VAL A 353      89.600 217.010  -2.661  1.00 39.95           C  
ANISOU 3798  C   VAL A 353     4521   3234   7423    428   -626   -136       C  
ATOM   3799  O   VAL A 353      89.935 215.901  -2.288  1.00 31.95           O  
ANISOU 3799  O   VAL A 353     3433   2289   6416    400   -688   -141       O  
ATOM   3800  CB  VAL A 353      91.226 218.945  -2.349  1.00 33.46           C  
ANISOU 3800  CB  VAL A 353     3777   2317   6620    295   -443   -173       C  
ATOM   3801  CG1 VAL A 353      91.545 218.362  -0.992  1.00 33.56           C  
ANISOU 3801  CG1 VAL A 353     3684   2425   6642    215   -495   -230       C  
ATOM   3802  CG2 VAL A 353      92.460 219.590  -2.928  1.00 35.15           C  
ANISOU 3802  CG2 VAL A 353     4051   2456   6847    240   -326   -162       C  
ATOM   3803  N   TYR A 354      88.364 217.485  -2.548  1.00 39.43           N  
ANISOU 3803  N   TYR A 354     4463   3134   7383    481   -632   -143       N  
ATOM   3804  CA  TYR A 354      87.273 216.680  -1.944  1.00 38.17           C  
ANISOU 3804  CA  TYR A 354     4213   3022   7266    503   -696   -157       C  
ATOM   3805  C   TYR A 354      86.767 215.680  -2.976  1.00 36.22           C  
ANISOU 3805  C   TYR A 354     3939   2786   7037    587   -800   -143       C  
ATOM   3806  O   TYR A 354      86.160 214.710  -2.576  1.00 37.02           O  
ANISOU 3806  O   TYR A 354     3947   2923   7195    573   -854   -153       O  
ATOM   3807  CB  TYR A 354      86.134 217.556  -1.425  1.00 33.08           C  
ANISOU 3807  CB  TYR A 354     3560   2341   6669    540   -660   -194       C  
ATOM   3808  CG  TYR A 354      86.577 218.662  -0.514  1.00 34.68           C  
ANISOU 3808  CG  TYR A 354     3803   2517   6857    473   -564   -233       C  
ATOM   3809  CD1 TYR A 354      87.080 218.391   0.733  1.00 35.48           C  
ANISOU 3809  CD1 TYR A 354     3865   2690   6926    373   -530   -265       C  
ATOM   3810  CD2 TYR A 354      86.498 219.976  -0.908  1.00 36.42           C  
ANISOU 3810  CD2 TYR A 354     4114   2632   7094    517   -515   -242       C  
ATOM   3811  CE1 TYR A 354      87.505 219.405   1.564  1.00 36.89           C  
ANISOU 3811  CE1 TYR A 354     4079   2851   7088    318   -460   -329       C  
ATOM   3812  CE2 TYR A 354      86.928 220.999  -0.097  1.00 36.96           C  
ANISOU 3812  CE2 TYR A 354     4212   2658   7172    452   -433   -300       C  
ATOM   3813  CZ  TYR A 354      87.428 220.711   1.145  1.00 36.00           C  
ANISOU 3813  CZ  TYR A 354     4036   2624   7019    353   -410   -356       C  
ATOM   3814  OH  TYR A 354      87.844 221.708   1.954  1.00 36.07           O  
ANISOU 3814  OH  TYR A 354     4073   2596   7035    295   -346   -441       O  
ATOM   3815  N   ALA A 355      86.920 215.992  -4.259  1.00 36.15           N  
ANISOU 3815  N   ALA A 355     4015   2742   6977    673   -825   -123       N  
ATOM   3816  CA  ALA A 355      86.571 215.023  -5.289  1.00 38.05           C  
ANISOU 3816  CA  ALA A 355     4238   3005   7213    760   -938   -135       C  
ATOM   3817  C   ALA A 355      87.473 213.800  -5.228  1.00 42.88           C  
ANISOU 3817  C   ALA A 355     4795   3669   7827    699   -964   -141       C  
ATOM   3818  O   ALA A 355      87.053 212.703  -5.610  1.00 46.65           O  
ANISOU 3818  O   ALA A 355     5211   4164   8351    738  -1066   -173       O  
ATOM   3819  CB  ALA A 355      86.649 215.659  -6.675  1.00 36.99           C  
ANISOU 3819  CB  ALA A 355     4242   2833   6978    877   -952   -108       C  
ATOM   3820  N   ASN A 356      88.716 213.970  -4.768  1.00 42.84           N  
ANISOU 3820  N   ASN A 356     4804   3681   7791    610   -884   -126       N  
ATOM   3821  CA  ASN A 356      89.605 212.825  -4.603  1.00 43.02           C  
ANISOU 3821  CA  ASN A 356     4764   3749   7834    566   -922   -141       C  
ATOM   3822  C   ASN A 356      89.040 211.838  -3.590  1.00 41.43           C  
ANISOU 3822  C   ASN A 356     4471   3558   7711    522   -987   -137       C  
ATOM   3823  O   ASN A 356      89.155 210.619  -3.765  1.00 42.01           O  
ANISOU 3823  O   ASN A 356     4494   3635   7834    534  -1069   -148       O  
ATOM   3824  CB  ASN A 356      90.995 213.298  -4.171  1.00 47.61           C  
ANISOU 3824  CB  ASN A 356     5351   4348   8392    482   -836   -146       C  
ATOM   3825  CG  ASN A 356      91.921 212.150  -3.828  1.00 51.36           C  
ANISOU 3825  CG  ASN A 356     5744   4866   8904    450   -895   -171       C  
ATOM   3826  OD1 ASN A 356      92.077 211.205  -4.602  1.00 53.39           O  
ANISOU 3826  OD1 ASN A 356     5979   5133   9175    507   -958   -194       O  
ATOM   3827  ND2 ASN A 356      92.533 212.220  -2.650  1.00 52.41           N  
ANISOU 3827  ND2 ASN A 356     5838   5023   9055    371   -890   -177       N  
ATOM   3828  N   SER A 357      88.427 212.348  -2.516  1.00 40.96           N  
ANISOU 3828  N   SER A 357     4399   3496   7667    471   -939   -120       N  
ATOM   3829  CA  SER A 357      87.776 211.473  -1.547  1.00 40.80           C  
ANISOU 3829  CA  SER A 357     4313   3483   7707    422   -964    -97       C  
ATOM   3830  C   SER A 357      86.558 210.781  -2.146  1.00 39.76           C  
ANISOU 3830  C   SER A 357     4116   3318   7672    474  -1031   -118       C  
ATOM   3831  O   SER A 357      86.234 209.654  -1.756  1.00 39.67           O  
ANISOU 3831  O   SER A 357     4044   3289   7741    436  -1070    -99       O  
ATOM   3832  CB  SER A 357      87.380 212.270  -0.304  1.00 43.44           C  
ANISOU 3832  CB  SER A 357     4657   3837   8011    360   -872    -89       C  
ATOM   3833  OG  SER A 357      88.524 212.816   0.337  1.00 44.86           O  
ANISOU 3833  OG  SER A 357     4883   4049   8114    308   -835    -93       O  
ATOM   3834  N   ALA A 358      85.877 211.435  -3.090  1.00 37.69           N  
ANISOU 3834  N   ALA A 358     3868   3039   7415    565  -1054   -160       N  
ATOM   3835  CA  ALA A 358      84.778 210.789  -3.800  1.00 35.11           C  
ANISOU 3835  CA  ALA A 358     3465   2687   7190    632  -1152   -212       C  
ATOM   3836  C   ALA A 358      85.279 209.726  -4.771  1.00 34.27           C  
ANISOU 3836  C   ALA A 358     3356   2573   7092    679  -1260   -244       C  
ATOM   3837  O   ALA A 358      84.605 208.711  -4.976  1.00 36.27           O  
ANISOU 3837  O   ALA A 358     3519   2794   7466    686  -1347   -290       O  
ATOM   3838  CB  ALA A 358      83.949 211.836  -4.537  1.00 33.19           C  
ANISOU 3838  CB  ALA A 358     3248   2429   6932    743  -1175   -254       C  
ATOM   3839  N   ALA A 359      86.466 209.921  -5.349  1.00 32.33           N  
ANISOU 3839  N   ALA A 359     3199   2352   6735    705  -1247   -234       N  
ATOM   3840  CA  ALA A 359      86.935 209.049  -6.423  1.00 32.61           C  
ANISOU 3840  CA  ALA A 359     3242   2392   6758    774  -1339   -289       C  
ATOM   3841  C   ALA A 359      87.471 207.718  -5.906  1.00 36.11           C  
ANISOU 3841  C   ALA A 359     3615   2812   7292    712  -1381   -289       C  
ATOM   3842  O   ALA A 359      87.272 206.685  -6.552  1.00 37.14           O  
ANISOU 3842  O   ALA A 359     3704   2921   7488    754  -1483   -357       O  
ATOM   3843  CB  ALA A 359      88.011 209.756  -7.244  1.00 32.61           C  
ANISOU 3843  CB  ALA A 359     3355   2429   6608    820  -1276   -281       C  
ATOM   3844  N   ASN A 360      88.165 207.715  -4.765  1.00 35.78           N  
ANISOU 3844  N   ASN A 360     3571   2776   7247    617  -1314   -221       N  
ATOM   3845  CA  ASN A 360      88.845 206.492  -4.336  1.00 32.21           C  
ANISOU 3845  CA  ASN A 360     3080   2294   6865    583  -1370   -209       C  
ATOM   3846  C   ASN A 360      87.899 205.317  -4.120  1.00 37.29           C  
ANISOU 3846  C   ASN A 360     3652   2855   7663    561  -1447   -210       C  
ATOM   3847  O   ASN A 360      88.235 204.203  -4.559  1.00 38.30           O  
ANISOU 3847  O   ASN A 360     3753   2941   7858    585  -1534   -255       O  
ATOM   3848  CB  ASN A 360      89.682 206.759  -3.082  1.00 37.32           C  
ANISOU 3848  CB  ASN A 360     3749   2966   7465    503  -1310   -136       C  
ATOM   3849  CG  ASN A 360      90.931 207.546  -3.381  1.00 38.52           C  
ANISOU 3849  CG  ASN A 360     3935   3179   7522    515  -1257   -165       C  
ATOM   3850  OD1 ASN A 360      91.479 207.471  -4.479  1.00 40.84           O  
ANISOU 3850  OD1 ASN A 360     4232   3489   7795    579  -1266   -229       O  
ATOM   3851  ND2 ASN A 360      91.390 208.319  -2.405  1.00 37.75           N  
ANISOU 3851  ND2 ASN A 360     3859   3116   7368    450  -1191   -131       N  
ATOM   3852  N   PRO A 361      86.744 205.457  -3.455  1.00 36.61           N  
ANISOU 3852  N   PRO A 361     3525   2742   7642    502  -1404   -173       N  
ATOM   3853  CA  PRO A 361      85.818 204.313  -3.383  1.00 37.09           C  
ANISOU 3853  CA  PRO A 361     3499   2709   7884    467  -1461   -188       C  
ATOM   3854  C   PRO A 361      85.303 203.868  -4.742  1.00 41.22           C  
ANISOU 3854  C   PRO A 361     3971   3220   8472    549  -1577   -323       C  
ATOM   3855  O   PRO A 361      84.934 202.696  -4.894  1.00 45.08           O  
ANISOU 3855  O   PRO A 361     4394   3631   9104    518  -1648   -365       O  
ATOM   3856  CB  PRO A 361      84.683 204.829  -2.483  1.00 34.44           C  
ANISOU 3856  CB  PRO A 361     3120   2377   7589    387  -1352   -140       C  
ATOM   3857  CG  PRO A 361      85.296 205.902  -1.672  1.00 33.70           C  
ANISOU 3857  CG  PRO A 361     3112   2363   7327    360  -1247    -71       C  
ATOM   3858  CD  PRO A 361      86.292 206.564  -2.588  1.00 35.00           C  
ANISOU 3858  CD  PRO A 361     3343   2584   7372    449  -1286   -120       C  
ATOM   3859  N   ILE A 362      85.284 204.754  -5.739  1.00 40.91           N  
ANISOU 3859  N   ILE A 362     3981   3272   8291    636  -1589   -393       N  
ATOM   3860  CA  ILE A 362      84.894 204.337  -7.083  1.00 35.11           C  
ANISOU 3860  CA  ILE A 362     3241   2565   7534    713  -1701   -528       C  
ATOM   3861  C   ILE A 362      86.005 203.530  -7.742  1.00 42.79           C  
ANISOU 3861  C   ILE A 362     4260   3549   8447    749  -1751   -578       C  
ATOM   3862  O   ILE A 362      85.732 202.603  -8.514  1.00 44.30           O  
ANISOU 3862  O   ILE A 362     4417   3716   8697    779  -1858   -694       O  
ATOM   3863  CB  ILE A 362      84.509 205.568  -7.921  1.00 35.12           C  
ANISOU 3863  CB  ILE A 362     3310   2645   7390    818  -1704   -565       C  
ATOM   3864  CG1 ILE A 362      83.358 206.313  -7.245  1.00 39.36           C  
ANISOU 3864  CG1 ILE A 362     3779   3165   8010    790  -1661   -538       C  
ATOM   3865  CG2 ILE A 362      84.134 205.164  -9.348  1.00 36.21           C  
ANISOU 3865  CG2 ILE A 362     3467   2816   7476    926  -1841   -706       C  
ATOM   3866  CD1 ILE A 362      83.110 207.682  -7.811  1.00 35.28           C  
ANISOU 3866  CD1 ILE A 362     3350   2706   7348    891  -1647   -538       C  
ATOM   3867  N   ILE A 363      87.263 203.862  -7.447  1.00 40.99           N  
ANISOU 3867  N   ILE A 363     4096   3354   8125    750  -1680   -512       N  
ATOM   3868  CA  ILE A 363      88.384 203.069  -7.938  1.00 41.30           C  
ANISOU 3868  CA  ILE A 363     4151   3400   8140    785  -1716   -568       C  
ATOM   3869  C   ILE A 363      88.361 201.679  -7.317  1.00 42.36           C  
ANISOU 3869  C   ILE A 363     4221   3440   8433    710  -1776   -561       C  
ATOM   3870  O   ILE A 363      88.624 200.676  -7.993  1.00 42.89           O  
ANISOU 3870  O   ILE A 363     4272   3482   8544    745  -1859   -663       O  
ATOM   3871  CB  ILE A 363      89.709 203.796  -7.649  1.00 39.04           C  
ANISOU 3871  CB  ILE A 363     3911   3158   7764    798  -1626   -509       C  
ATOM   3872  CG1 ILE A 363      89.702 205.190  -8.274  1.00 33.68           C  
ANISOU 3872  CG1 ILE A 363     3304   2530   6963    872  -1559   -502       C  
ATOM   3873  CG2 ILE A 363      90.886 202.995  -8.170  1.00 34.46           C  
ANISOU 3873  CG2 ILE A 363     3320   2588   7184    847  -1658   -588       C  
ATOM   3874  CD1 ILE A 363      90.763 206.100  -7.716  1.00 33.08           C  
ANISOU 3874  CD1 ILE A 363     3262   2492   6815    823  -1434   -431       C  
ATOM   3875  N   TYR A 364      88.041 201.595  -6.023  1.00 40.96           N  
ANISOU 3875  N   TYR A 364     4016   3197   8352    616  -1735   -439       N  
ATOM   3876  CA  TYR A 364      87.963 200.298  -5.362  1.00 39.49           C  
ANISOU 3876  CA  TYR A 364     3787   2891   8326    551  -1785   -399       C  
ATOM   3877  C   TYR A 364      86.835 199.450  -5.932  1.00 42.35           C  
ANISOU 3877  C   TYR A 364     4065   3170   8855    536  -1869   -496       C  
ATOM   3878  O   TYR A 364      86.946 198.220  -5.981  1.00 42.22           O  
ANISOU 3878  O   TYR A 364     4014   3059   8967    515  -1942   -527       O  
ATOM   3879  CB  TYR A 364      87.772 200.481  -3.856  1.00 38.10           C  
ANISOU 3879  CB  TYR A 364     3622   2649   8204    469  -1713   -230       C  
ATOM   3880  CG  TYR A 364      88.820 201.346  -3.194  1.00 37.04           C  
ANISOU 3880  CG  TYR A 364     3557   2586   7929    484  -1655   -152       C  
ATOM   3881  CD1 TYR A 364      90.113 201.425  -3.699  1.00 38.53           C  
ANISOU 3881  CD1 TYR A 364     3772   2850   8016    545  -1679   -213       C  
ATOM   3882  CD2 TYR A 364      88.514 202.085  -2.061  1.00 37.24           C  
ANISOU 3882  CD2 TYR A 364     3614   2613   7922    426  -1567    -35       C  
ATOM   3883  CE1 TYR A 364      91.069 202.219  -3.092  1.00 39.75           C  
ANISOU 3883  CE1 TYR A 364     3958   3058   8086    556  -1639   -164       C  
ATOM   3884  CE2 TYR A 364      89.460 202.881  -1.449  1.00 38.30           C  
ANISOU 3884  CE2 TYR A 364     3809   2839   7906    422  -1519      8       C  
ATOM   3885  CZ  TYR A 364      90.736 202.945  -1.966  1.00 39.38           C  
ANISOU 3885  CZ  TYR A 364     3947   3023   7993    491  -1568    -57       C  
ATOM   3886  OH  TYR A 364      91.680 203.739  -1.355  1.00 39.37           O  
ANISOU 3886  OH  TYR A 364     3979   3107   7875    477  -1526    -36       O  
ATOM   3887  N   ASN A 365      85.748 200.087  -6.371  1.00 45.24           N  
ANISOU 3887  N   ASN A 365     4387   3564   9238    551  -1870   -555       N  
ATOM   3888  CA  ASN A 365      84.633 199.342  -6.945  1.00 50.05           C  
ANISOU 3888  CA  ASN A 365     4890   4094  10035    542  -1970   -679       C  
ATOM   3889  C   ASN A 365      84.954 198.866  -8.357  1.00 52.47           C  
ANISOU 3889  C   ASN A 365     5221   4445  10270    638  -2093   -859       C  
ATOM   3890  O   ASN A 365      84.580 197.753  -8.744  1.00 55.09           O  
ANISOU 3890  O   ASN A 365     5475   4680  10775    625  -2202   -969       O  
ATOM   3891  CB  ASN A 365      83.371 200.209  -6.941  1.00 49.75           C  
ANISOU 3891  CB  ASN A 365     4782   4076  10044    542  -1948   -704       C  
ATOM   3892  CG  ASN A 365      82.127 199.434  -7.327  1.00 50.72           C  
ANISOU 3892  CG  ASN A 365     4753   4096  10424    516  -2051   -840       C  
ATOM   3893  OD1 ASN A 365      81.528 198.748  -6.500  1.00 51.07           O  
ANISOU 3893  OD1 ASN A 365     4682   3991  10731    415  -2017   -785       O  
ATOM   3894  ND2 ASN A 365      81.725 199.550  -8.588  1.00 52.86           N  
ANISOU 3894  ND2 ASN A 365     5026   4431  10627    609  -2175  -1019       N  
ATOM   3895  N   PHE A 366      85.656 199.691  -9.136  1.00 52.47           N  
ANISOU 3895  N   PHE A 366     5327   4579  10032    742  -2074   -893       N  
ATOM   3896  CA  PHE A 366      85.957 199.330 -10.517  1.00 51.37           C  
ANISOU 3896  CA  PHE A 366     5225   4488   9806    860  -2179  -1063       C  
ATOM   3897  C   PHE A 366      87.135 198.372 -10.624  1.00 48.32           C  
ANISOU 3897  C   PHE A 366     4855   4074   9432    872  -2197  -1096       C  
ATOM   3898  O   PHE A 366      87.183 197.563 -11.556  1.00 48.39           O  
ANISOU 3898  O   PHE A 366     4849   4066   9473    941  -2310  -1261       O  
ATOM   3899  CB  PHE A 366      86.251 200.584 -11.345  1.00 54.54           C  
ANISOU 3899  CB  PHE A 366     5736   5027   9960    986  -2142  -1072       C  
ATOM   3900  CG  PHE A 366      85.022 201.325 -11.797  1.00 59.24           C  
ANISOU 3900  CG  PHE A 366     6326   5658  10523   1036  -2196  -1117       C  
ATOM   3901  CD1 PHE A 366      83.782 201.074 -11.229  1.00 62.51           C  
ANISOU 3901  CD1 PHE A 366     6622   5994  11135    947  -2233  -1130       C  
ATOM   3902  CD2 PHE A 366      85.111 202.271 -12.808  1.00 61.49           C  
ANISOU 3902  CD2 PHE A 366     6724   6046  10594   1185  -2214  -1150       C  
ATOM   3903  CE1 PHE A 366      82.656 201.761 -11.653  1.00 65.07           C  
ANISOU 3903  CE1 PHE A 366     6927   6356  11442   1003  -2293  -1191       C  
ATOM   3904  CE2 PHE A 366      83.993 202.960 -13.238  1.00 63.79           C  
ANISOU 3904  CE2 PHE A 366     7022   6370  10844   1250  -2286  -1191       C  
ATOM   3905  CZ  PHE A 366      82.762 202.705 -12.661  1.00 65.72           C  
ANISOU 3905  CZ  PHE A 366     7135   6550  11286   1157  -2329  -1221       C  
ATOM   3906  N   LEU A 367      88.088 198.439  -9.695  1.00 46.17           N  
ANISOU 3906  N   LEU A 367     4607   3797   9139    819  -2101   -960       N  
ATOM   3907  CA  LEU A 367      89.347 197.720  -9.840  1.00 45.84           C  
ANISOU 3907  CA  LEU A 367     4581   3751   9086    855  -2113   -999       C  
ATOM   3908  C   LEU A 367      89.586 196.636  -8.797  1.00 45.91           C  
ANISOU 3908  C   LEU A 367     4546   3633   9264    764  -2138   -915       C  
ATOM   3909  O   LEU A 367      90.638 195.990  -8.837  1.00 47.90           O  
ANISOU 3909  O   LEU A 367     4805   3874   9521    799  -2161   -948       O  
ATOM   3910  CB  LEU A 367      90.521 198.710  -9.820  1.00 44.28           C  
ANISOU 3910  CB  LEU A 367     4445   3664   8717    907  -2003   -944       C  
ATOM   3911  CG  LEU A 367      90.645 199.630 -11.036  1.00 42.19           C  
ANISOU 3911  CG  LEU A 367     4239   3510   8282   1035  -1975  -1030       C  
ATOM   3912  CD1 LEU A 367      91.811 200.582 -10.855  1.00 41.54           C  
ANISOU 3912  CD1 LEU A 367     4188   3499   8098   1066  -1851   -964       C  
ATOM   3913  CD2 LEU A 367      90.805 198.819 -12.313  1.00 41.53           C  
ANISOU 3913  CD2 LEU A 367     4154   3437   8187   1152  -2074  -1226       C  
ATOM   3914  N   SER A 368      88.669 196.423  -7.864  1.00 49.40           N  
ANISOU 3914  N   SER A 368     5558   3643   9568    851  -1345  -1745       N  
ATOM   3915  CA  SER A 368      88.879 195.344  -6.868  1.00 50.62           C  
ANISOU 3915  CA  SER A 368     5717   3722   9794    817  -1409  -1676       C  
ATOM   3916  C   SER A 368      87.586 194.555  -6.690  1.00 52.60           C  
ANISOU 3916  C   SER A 368     5978   3850  10157    737  -1513  -1605       C  
ATOM   3917  O   SER A 368      86.623 195.138  -6.234  1.00 51.72           O  
ANISOU 3917  O   SER A 368     5841   3708  10102    610  -1428  -1468       O  
ATOM   3918  CB  SER A 368      89.355 195.898  -5.567  1.00 50.84           C  
ANISOU 3918  CB  SER A 368     5772   3740   9804    705  -1271  -1490       C  
ATOM   3919  OG  SER A 368      89.201 194.972  -4.507  1.00 44.41           O  
ANISOU 3919  OG  SER A 368     5033   2822   9020    693  -1335  -1422       O  
ATOM   3920  N   GLY A 369      87.592 193.268  -7.038  1.00 55.67           N  
ANISOU 3920  N   GLY A 369     6384   4157  10611    822  -1713  -1713       N  
ATOM   3921  CA  GLY A 369      86.417 192.424  -6.915  1.00 49.26           C  
ANISOU 3921  CA  GLY A 369     5555   3183   9980    733  -1840  -1648       C  
ATOM   3922  C   GLY A 369      85.985 192.209  -5.479  1.00 52.29           C  
ANISOU 3922  C   GLY A 369     5975   3434  10458    567  -1708  -1417       C  
ATOM   3923  O   GLY A 369      84.789 192.077  -5.201  1.00 49.90           O  
ANISOU 3923  O   GLY A 369     5608   3011  10340    437  -1682  -1304       O  
ATOM   3924  N   LYS A 370      86.943 192.164  -4.550  1.00 52.81           N  
ANISOU 3924  N   LYS A 370     6150   3505  10411    583  -1628  -1357       N  
ATOM   3925  CA  LYS A 370      86.597 192.000  -3.141  1.00 52.77           C  
ANISOU 3925  CA  LYS A 370     6266   3355  10428    456  -1490  -1140       C  
ATOM   3926  C   LYS A 370      85.815 193.200  -2.621  1.00 51.20           C  
ANISOU 3926  C   LYS A 370     6035   3200  10218    340  -1245   -984       C  
ATOM   3927  O   LYS A 370      84.878 193.042  -1.829  1.00 51.84           O  
ANISOU 3927  O   LYS A 370     6147   3133  10416    218  -1124   -823       O  
ATOM   3928  CB  LYS A 370      87.861 191.781  -2.312  1.00 54.61           C  
ANISOU 3928  CB  LYS A 370     6657   3583  10510    537  -1503  -1138       C  
ATOM   3929  CG  LYS A 370      88.121 190.333  -1.934  1.00 60.76           C  
ANISOU 3929  CG  LYS A 370     7576   4170  11341    574  -1692  -1155       C  
ATOM   3930  CD  LYS A 370      89.296 190.234  -0.974  1.00 65.03           C  
ANISOU 3930  CD  LYS A 370     8284   4692  11731    661  -1713  -1144       C  
ATOM   3931  CE  LYS A 370      89.540 188.803  -0.528  1.00 70.01           C  
ANISOU 3931  CE  LYS A 370     9096   5106  12398    704  -1921  -1154       C  
ATOM   3932  NZ  LYS A 370      90.692 188.712   0.414  1.00 71.21           N  
ANISOU 3932  NZ  LYS A 370     9415   5235  12407    810  -1984  -1164       N  
ATOM   3933  N   PHE A 371      86.186 194.408  -3.054  1.00 48.86           N  
ANISOU 3933  N   PHE A 371     5680   3087   9797    382  -1172  -1033       N  
ATOM   3934  CA  PHE A 371      85.441 195.598  -2.657  1.00 43.98           C  
ANISOU 3934  CA  PHE A 371     5038   2513   9160    303   -986   -913       C  
ATOM   3935  C   PHE A 371      84.104 195.682  -3.383  1.00 56.49           C  
ANISOU 3935  C   PHE A 371     6449   4071  10943    248  -1016   -941       C  
ATOM   3936  O   PHE A 371      83.100 196.105  -2.798  1.00 60.31           O  
ANISOU 3936  O   PHE A 371     6876   4493  11546    165   -875   -828       O  
ATOM   3937  CB  PHE A 371      86.269 196.855  -2.928  1.00 49.49           C  
ANISOU 3937  CB  PHE A 371     5747   3377   9680    356   -941   -953       C  
ATOM   3938  CG  PHE A 371      87.116 197.289  -1.765  1.00 47.31           C  
ANISOU 3938  CG  PHE A 371     5624   3098   9254    368   -861   -855       C  
ATOM   3939  CD1 PHE A 371      86.527 197.733  -0.593  1.00 41.35           C  
ANISOU 3939  CD1 PHE A 371     5003   2266   8443    322   -714   -693       C  
ATOM   3940  CD2 PHE A 371      88.498 197.273  -1.848  1.00 47.28           C  
ANISOU 3940  CD2 PHE A 371     5625   3152   9187    448   -949   -946       C  
ATOM   3941  CE1 PHE A 371      87.299 198.139   0.481  1.00 44.89           C  
ANISOU 3941  CE1 PHE A 371     5643   2689   8723    366   -681   -619       C  
ATOM   3942  CE2 PHE A 371      89.276 197.680  -0.777  1.00 46.73           C  
ANISOU 3942  CE2 PHE A 371     5687   3062   9008    469   -931   -873       C  
ATOM   3943  CZ  PHE A 371      88.673 198.113   0.389  1.00 44.69           C  
ANISOU 3943  CZ  PHE A 371     5615   2722   8642    433   -808   -708       C  
ATOM   3944  N   ARG A 372      84.074 195.283  -4.656  1.00 55.98           N  
ANISOU 3944  N   ARG A 372     6298   4040  10934    316  -1212  -1109       N  
ATOM   3945  CA  ARG A 372      82.857 195.416  -5.451  1.00 56.32           C  
ANISOU 3945  CA  ARG A 372     6184   4053  11162    295  -1308  -1169       C  
ATOM   3946  C   ARG A 372      81.728 194.560  -4.886  1.00 56.70           C  
ANISOU 3946  C   ARG A 372     6105   3902  11534    178  -1312  -1075       C  
ATOM   3947  O   ARG A 372      80.594 195.029  -4.739  1.00 57.23           O  
ANISOU 3947  O   ARG A 372     6005   3922  11817    106  -1239  -1026       O  
ATOM   3948  CB  ARG A 372      83.147 195.049  -6.907  1.00 57.05           C  
ANISOU 3948  CB  ARG A 372     6281   4190  11206    428  -1555  -1383       C  
ATOM   3949  CG  ARG A 372      81.967 195.235  -7.841  1.00 48.49           C  
ANISOU 3949  CG  ARG A 372     5075   3069  10278    444  -1723  -1476       C  
ATOM   3950  CD  ARG A 372      82.374 195.063  -9.294  1.00 49.38           C  
ANISOU 3950  CD  ARG A 372     5289   3234  10241    619  -1957  -1695       C  
ATOM   3951  NE  ARG A 372      83.039 193.787  -9.548  1.00 55.86           N  
ANISOU 3951  NE  ARG A 372     6169   3998  11056    713  -2124  -1799       N  
ATOM   3952  CZ  ARG A 372      84.318 193.665  -9.888  1.00 55.60           C  
ANISOU 3952  CZ  ARG A 372     6270   4059  10797    853  -2107  -1909       C  
ATOM   3953  NH1 ARG A 372      85.077 194.745 -10.019  1.00 53.27           N  
ANISOU 3953  NH1 ARG A 372     6047   3901  10292    894  -1918  -1913       N  
ATOM   3954  NH2 ARG A 372      84.837 192.464 -10.106  1.00 57.88           N  
ANISOU 3954  NH2 ARG A 372     6604   4291  11095    964  -2292  -2027       N  
ATOM   3955  N   GLU A 373      82.022 193.301  -4.553  1.00 57.94           N  
ANISOU 3955  N   GLU A 373     6331   3920  11763    156  -1400  -1050       N  
ATOM   3956  CA  GLU A 373      80.988 192.433  -3.999  1.00 60.46           C  
ANISOU 3956  CA  GLU A 373     6547   4008  12419     14  -1396   -932       C  
ATOM   3957  C   GLU A 373      80.579 192.878  -2.599  1.00 57.69           C  
ANISOU 3957  C   GLU A 373     6229   3578  12113   -116  -1066   -707       C  
ATOM   3958  O   GLU A 373      79.397 192.816  -2.245  1.00 59.89           O  
ANISOU 3958  O   GLU A 373     6313   3716  12726   -246   -952   -603       O  
ATOM   3959  CB  GLU A 373      81.472 190.984  -3.984  1.00 65.75           C  
ANISOU 3959  CB  GLU A 373     7342   4520  13120     23  -1597   -954       C  
ATOM   3960  CG  GLU A 373      81.929 190.481  -5.341  1.00 70.78           C  
ANISOU 3960  CG  GLU A 373     7973   5219  13702    191  -1932  -1194       C  
ATOM   3961  CD  GLU A 373      80.787 190.329  -6.320  1.00 77.97           C  
ANISOU 3961  CD  GLU A 373     8669   6060  14896    191  -2155  -1294       C  
ATOM   3962  OE1 GLU A 373      79.745 189.759  -5.933  1.00 82.58           O  
ANISOU 3962  OE1 GLU A 373     9107   6433  15837     43  -2177  -1184       O  
ATOM   3963  OE2 GLU A 373      80.928 190.784  -7.475  1.00 78.86           O  
ANISOU 3963  OE2 GLU A 373     8770   6310  14883    340  -2314  -1482       O  
ATOM   3964  N   GLU A 374      81.540 193.328  -1.789  1.00 54.72           N  
ANISOU 3964  N   GLU A 374     6089   3275  11426    -71   -913   -634       N  
ATOM   3965  CA  GLU A 374      81.202 193.819  -0.457  1.00 56.79           C  
ANISOU 3965  CA  GLU A 374     6447   3453  11679   -149   -613   -430       C  
ATOM   3966  C   GLU A 374      80.457 195.144  -0.522  1.00 55.76           C  
ANISOU 3966  C   GLU A 374     6139   3429  11620   -138   -454   -433       C  
ATOM   3967  O   GLU A 374      79.683 195.463   0.389  1.00 57.55           O  
ANISOU 3967  O   GLU A 374     6320   3540  12007   -212   -190   -279       O  
ATOM   3968  CB  GLU A 374      82.462 193.955   0.393  1.00 58.02           C  
ANISOU 3968  CB  GLU A 374     6935   3638  11471    -63   -564   -379       C  
ATOM   3969  CG  GLU A 374      82.981 192.633   0.926  1.00 63.64           C  
ANISOU 3969  CG  GLU A 374     7875   4154  12150    -88   -658   -321       C  
ATOM   3970  CD  GLU A 374      82.093 192.057   2.011  1.00 68.64           C  
ANISOU 3970  CD  GLU A 374     8610   4508  12963   -253   -457    -80       C  
ATOM   3971  OE1 GLU A 374      81.616 192.834   2.866  1.00 69.66           O  
ANISOU 3971  OE1 GLU A 374     8780   4606  13081   -282   -181     72       O  
ATOM   3972  OE2 GLU A 374      81.869 190.828   2.009  1.00 71.27           O  
ANISOU 3972  OE2 GLU A 374     8987   4638  13456   -355   -566    -32       O  
ATOM   3973  N   PHE A 375      80.685 195.931  -1.575  1.00 53.36           N  
ANISOU 3973  N   PHE A 375     5753   3323  11198    -40   -598   -602       N  
ATOM   3974  CA  PHE A 375      79.858 197.112  -1.795  1.00 51.84           C  
ANISOU 3974  CA  PHE A 375     5395   3200  11103    -21   -519   -635       C  
ATOM   3975  C   PHE A 375      78.432 196.715  -2.144  1.00 51.99           C  
ANISOU 3975  C   PHE A 375     5080   3079  11595   -105   -546   -661       C  
ATOM   3976  O   PHE A 375      77.476 197.358  -1.695  1.00 53.99           O  
ANISOU 3976  O   PHE A 375     5150   3268  12094   -134   -359   -615       O  
ATOM   3977  CB  PHE A 375      80.454 197.983  -2.902  1.00 49.77           C  
ANISOU 3977  CB  PHE A 375     5182   3146  10584     89   -692   -793       C  
ATOM   3978  CG  PHE A 375      81.628 198.808  -2.463  1.00 45.72           C  
ANISOU 3978  CG  PHE A 375     4912   2759   9703    151   -619   -750       C  
ATOM   3979  CD1 PHE A 375      81.887 199.018  -1.118  1.00 46.32           C  
ANISOU 3979  CD1 PHE A 375     5151   2774   9674    146   -431   -602       C  
ATOM   3980  CD2 PHE A 375      82.470 199.381  -3.400  1.00 42.00           C  
ANISOU 3980  CD2 PHE A 375     4511   2436   9013    220   -746   -856       C  
ATOM   3981  CE1 PHE A 375      82.969 199.782  -0.715  1.00 43.93           C  
ANISOU 3981  CE1 PHE A 375     5061   2566   9065    211   -422   -577       C  
ATOM   3982  CE2 PHE A 375      83.552 200.144  -3.006  1.00 41.05           C  
ANISOU 3982  CE2 PHE A 375     4560   2399   8638    254   -694   -812       C  
ATOM   3983  CZ  PHE A 375      83.802 200.345  -1.660  1.00 41.35           C  
ANISOU 3983  CZ  PHE A 375     4740   2386   8584    250   -557   -679       C  
ATOM   3984  N   LYS A 376      78.266 195.656  -2.942  1.00 52.67           N  
ANISOU 3984  N   LYS A 376     5066   3095  11852   -129   -788   -747       N  
ATOM   3985  CA  LYS A 376      76.923 195.216  -3.301  1.00 55.77           C  
ANISOU 3985  CA  LYS A 376     5117   3331  12742   -206   -870   -778       C  
ATOM   3986  C   LYS A 376      76.208 194.600  -2.104  1.00 59.32           C  
ANISOU 3986  C   LYS A 376     5449   3557  13532   -392   -582   -552       C  
ATOM   3987  O   LYS A 376      74.986 194.730  -1.972  1.00 62.93           O  
ANISOU 3987  O   LYS A 376     5568   3898  14446   -477   -465   -521       O  
ATOM   3988  CB  LYS A 376      76.981 194.215  -4.459  1.00 57.00           C  
ANISOU 3988  CB  LYS A 376     5243   3446  12969   -159  -1251   -930       C  
ATOM   3989  CG  LYS A 376      77.347 194.827  -5.799  1.00 60.98           C  
ANISOU 3989  CG  LYS A 376     5814   4129  13225     14  -1517  -1151       C  
ATOM   3990  CD  LYS A 376      77.059 193.874  -6.954  1.00 63.49           C  
ANISOU 3990  CD  LYS A 376     6062   4356  13706     84  -1909  -1313       C  
ATOM   3991  CE  LYS A 376      78.076 192.743  -7.027  1.00 63.14           C  
ANISOU 3991  CE  LYS A 376     6236   4278  13476    113  -2026  -1321       C  
ATOM   3992  NZ  LYS A 376      77.728 191.756  -8.091  1.00 65.75           N  
ANISOU 3992  NZ  LYS A 376     6509   4485  13988    197  -2436  -1482       N  
ATOM   3993  N   ALA A 377      76.949 193.925  -1.221  1.00 60.26           N  
ANISOU 3993  N   ALA A 377     5848   3601  13446   -459   -456   -386       N  
ATOM   3994  CA  ALA A 377      76.312 193.274  -0.081  1.00 62.63           C  
ANISOU 3994  CA  ALA A 377     6109   3675  14014   -660   -162   -127       C  
ATOM   3995  C   ALA A 377      75.889 194.287   0.975  1.00 62.85           C  
ANISOU 3995  C   ALA A 377     6102   3701  14077   -677    281     30       C  
ATOM   3996  O   ALA A 377      74.898 194.069   1.681  1.00 77.48           O  
ANISOU 3996  O   ALA A 377     7741   5402  16298   -848    609    228       O  
ATOM   3997  CB  ALA A 377      77.249 192.225   0.519  1.00 63.04           C  
ANISOU 3997  CB  ALA A 377     6541   3614  13798   -708   -208     -7       C  
ATOM   3998  N   ALA A 378      76.624 195.394   1.101  1.00 95.57           N  
ANISOU 3998  N   ALA A 378    10454   8012  17845   -501    315    -43       N  
ATOM   3999  CA  ALA A 378      76.230 196.445   2.031  1.00 93.96           C  
ANISOU 3999  CA  ALA A 378    10251   7785  17663   -455    704     74       C  
ATOM   4000  C   ALA A 378      75.086 197.285   1.481  1.00 99.70           C  
ANISOU 4000  C   ALA A 378    10555   8531  18797   -431    747    -63       C  
ATOM   4001  O   ALA A 378      74.243 197.757   2.251  1.00107.76           O  
ANISOU 4001  O   ALA A 378    11396   9435  20111   -470   1156     65       O  
ATOM   4002  CB  ALA A 378      77.432 197.329   2.365  1.00 92.46           C  
ANISOU 4002  CB  ALA A 378    10463   7748  16919   -255    653     32       C  
ATOM   4003  N   PHE A 379      75.038 197.479   0.160  1.00 93.58           N  
ANISOU 4003  N   PHE A 379     9629   7886  18042   -355    347   -322       N  
ATOM   4004  CA  PHE A 379      73.913 198.188  -0.441  1.00 96.16           C  
ANISOU 4004  CA  PHE A 379     9563   8198  18777   -316    294   -492       C  
ATOM   4005  C   PHE A 379      72.635 197.361  -0.371  1.00101.04           C  
ANISOU 4005  C   PHE A 379     9720   8634  20038   -511    409   -423       C  
ATOM   4006  O   PHE A 379      71.555 197.904  -0.111  1.00102.38           O  
ANISOU 4006  O   PHE A 379     9502   8746  20651   -553    637   -440       O  
ATOM   4007  CB  PHE A 379      74.230 198.553  -1.892  1.00 95.14           C  
ANISOU 4007  CB  PHE A 379     9474   8251  18424   -174   -185   -760       C  
ATOM   4008  CG  PHE A 379      74.634 199.987  -2.085  1.00 93.93           C  
ANISOU 4008  CG  PHE A 379     9525   8279  17884      1   -241   -870       C  
ATOM   4009  CD1 PHE A 379      73.757 201.014  -1.770  1.00 95.56           C  
ANISOU 4009  CD1 PHE A 379     9550   8442  18315     97   -104   -939       C  
ATOM   4010  CD2 PHE A 379      75.882 200.310  -2.596  1.00 91.79           C  
ANISOU 4010  CD2 PHE A 379     9624   8217  17037     81   -430   -903       C  
ATOM   4011  CE1 PHE A 379      74.119 202.334  -1.948  1.00 94.19           C  
ANISOU 4011  CE1 PHE A 379     9623   8455  17710    276   -208  -1027       C  
ATOM   4012  CE2 PHE A 379      76.251 201.630  -2.779  1.00 90.38           C  
ANISOU 4012  CE2 PHE A 379     9651   8193  16496    210   -489   -964       C  
ATOM   4013  CZ  PHE A 379      75.367 202.644  -2.453  1.00 91.42           C  
ANISOU 4013  CZ  PHE A 379     9660   8296  16780    306   -405  -1021       C  
ATOM   4014  N   SER A 380      72.733 196.048  -0.608  1.00102.37           N  
ANISOU 4014  N   SER A 380     9908   8728  20258   -631    243   -350       N  
ATOM   4015  CA  SER A 380      71.546 195.199  -0.561  1.00103.38           C  
ANISOU 4015  CA  SER A 380     9638   8696  20945   -819    310   -262       C  
ATOM   4016  C   SER A 380      70.987 195.086   0.849  1.00105.42           C  
ANISOU 4016  C   SER A 380     9777   8888  21390  -1025    913     64       C  
ATOM   4017  O   SER A 380      69.767 194.989   1.022  1.00117.83           O  
ANISOU 4017  O   SER A 380    10902  10431  23436  -1151   1122    125       O  
ATOM   4018  CB  SER A 380      71.856 193.809  -1.116  1.00 73.10           C  
ANISOU 4018  CB  SER A 380     5927   4759  17089   -890    -42   -255       C  
ATOM   4019  OG  SER A 380      71.902 193.823  -2.531  1.00 84.99           O  
ANISOU 4019  OG  SER A 380     7392   6312  18587   -710   -554   -546       O  
ATOM   4020  N   TRP A 381      71.852 195.089   1.864  1.00 94.89           N  
ANISOU 4020  N   TRP A 381     8853   7550  19650  -1042   1207    284       N  
ATOM   4021  CA  TRP A 381      71.365 195.096   3.239  1.00 96.56           C  
ANISOU 4021  CA  TRP A 381     9023   7726  19938  -1194   1847    625       C  
ATOM   4022  C   TRP A 381      70.735 196.438   3.589  1.00 96.43           C  
ANISOU 4022  C   TRP A 381     8719   7855  20063  -1088   2229    584       C  
ATOM   4023  O   TRP A 381      69.714 196.490   4.286  1.00102.69           O  
ANISOU 4023  O   TRP A 381     9156   8763  21099  -1179   2726    763       O  
ATOM   4024  CB  TRP A 381      72.507 194.776   4.204  1.00 94.46           C  
ANISOU 4024  CB  TRP A 381     9365   7385  19142  -1175   2003    854       C  
ATOM   4025  CG  TRP A 381      72.096 194.797   5.650  1.00100.38           C  
ANISOU 4025  CG  TRP A 381    10199   8100  19842  -1280   2692   1239       C  
ATOM   4026  CD1 TRP A 381      71.557 193.766   6.362  1.00107.31           C  
ANISOU 4026  CD1 TRP A 381    11050   8891  20832  -1530   2993   1554       C  
ATOM   4027  CD2 TRP A 381      72.194 195.903   6.559  1.00100.82           C  
ANISOU 4027  CD2 TRP A 381    10470   8356  19483  -1032   3109   1317       C  
ATOM   4028  NE1 TRP A 381      71.310 194.159   7.656  1.00110.99           N  
ANISOU 4028  NE1 TRP A 381    11669   9410  21092  -1515   3676   1876       N  
ATOM   4029  CE2 TRP A 381      71.693 195.467   7.803  1.00106.91           C  
ANISOU 4029  CE2 TRP A 381    11322   9113  20187  -1161   3729   1709       C  
ATOM   4030  CE3 TRP A 381      72.655 197.218   6.442  1.00 97.06           C  
ANISOU 4030  CE3 TRP A 381    10175   8132  18572   -661   2964   1071       C  
ATOM   4031  CZ2 TRP A 381      71.641 196.299   8.920  1.00108.07           C  
ANISOU 4031  CZ2 TRP A 381    11743   9508  19812   -883   4201   1834       C  
ATOM   4032  CZ3 TRP A 381      72.602 198.042   7.553  1.00 97.94           C  
ANISOU 4032  CZ3 TRP A 381    10543   8458  18213   -404   3381   1187       C  
ATOM   4033  CH2 TRP A 381      72.099 197.579   8.775  1.00103.27           C  
ANISOU 4033  CH2 TRP A 381    11310   9131  18796   -492   3992   1551       C  
ATOM   4034  N   TRP A 382      71.322 197.532   3.103  1.00 89.05           N  
ANISOU 4034  N   TRP A 382     8005   7099  18730   -770   1946    315       N  
ATOM   4035  CA  TRP A 382      70.898 198.860   3.530  1.00 85.66           C  
ANISOU 4035  CA  TRP A 382     7518   6981  18047   -483   2187    232       C  
ATOM   4036  C   TRP A 382      69.526 199.213   2.967  1.00 88.36           C  
ANISOU 4036  C   TRP A 382     7200   7423  18949   -488   2179     45       C  
ATOM   4037  O   TRP A 382      68.718 199.862   3.643  1.00 91.44           O  
ANISOU 4037  O   TRP A 382     7344   8045  19352   -354   2590     82       O  
ATOM   4038  CB  TRP A 382      71.954 199.879   3.102  1.00 78.72           C  
ANISOU 4038  CB  TRP A 382     7079   6201  16630   -189   1820     13       C  
ATOM   4039  CG  TRP A 382      71.641 201.309   3.389  1.00 78.42           C  
ANISOU 4039  CG  TRP A 382     7061   6427  16309    131   1920   -119       C  
ATOM   4040  CD1 TRP A 382      70.830 201.809   4.367  1.00 81.54           C  
ANISOU 4040  CD1 TRP A 382     7303   7019  16660    267   2400    -18       C  
ATOM   4041  CD2 TRP A 382      72.148 202.435   2.673  1.00 75.36           C  
ANISOU 4041  CD2 TRP A 382     6882   6121  15629    372   1513   -379       C  
ATOM   4042  NE1 TRP A 382      70.802 203.183   4.300  1.00 80.68           N  
ANISOU 4042  NE1 TRP A 382     7306   7097  16253    607   2266   -232       N  
ATOM   4043  CE2 TRP A 382      71.605 203.591   3.267  1.00 77.27           C  
ANISOU 4043  CE2 TRP A 382     7105   6579  15674    653   1713   -439       C  
ATOM   4044  CE3 TRP A 382      73.012 202.579   1.583  1.00 71.23           C  
ANISOU 4044  CE3 TRP A 382     6574   5510  14979    380   1012   -557       C  
ATOM   4045  CZ2 TRP A 382      71.899 204.874   2.806  1.00 75.24           C  
ANISOU 4045  CZ2 TRP A 382     7060   6406  15121    917   1376   -665       C  
ATOM   4046  CZ3 TRP A 382      73.302 203.848   1.127  1.00 68.92           C  
ANISOU 4046  CZ3 TRP A 382     6477   5323  14386    614    740   -748       C  
ATOM   4047  CH2 TRP A 382      72.748 204.980   1.736  1.00 70.77           C  
ANISOU 4047  CH2 TRP A 382     6710   5726  14452    867    896   -797       C  
ATOM   4048  N   TRP A 383      69.236 198.784   1.740  1.00 87.56           N  
ANISOU 4048  N   TRP A 383     6808   7146  19316   -609   1698   -176       N  
ATOM   4049  CA  TRP A 383      67.979 199.109   1.081  1.00 91.56           C  
ANISOU 4049  CA  TRP A 383     6694   7700  20394   -588   1562   -410       C  
ATOM   4050  C   TRP A 383      66.952 197.987   1.182  1.00 98.67           C  
ANISOU 4050  C   TRP A 383     7261   8478  21752   -839   1681   -258       C  
ATOM   4051  O   TRP A 383      65.788 198.235   1.514  1.00104.41           O  
ANISOU 4051  O   TRP A 383     7570   9347  22755   -835   1955   -254       O  
ATOM   4052  CB  TRP A 383      68.243 199.455  -0.391  1.00 88.92           C  
ANISOU 4052  CB  TRP A 383     6437   7263  20086   -442    855   -785       C  
ATOM   4053  CG  TRP A 383      68.983 200.745  -0.594  1.00 71.90           C  
ANISOU 4053  CG  TRP A 383     4733   5292  17294    -98    679   -952       C  
ATOM   4054  CD1 TRP A 383      70.272 200.897  -1.013  1.00 72.18           C  
ANISOU 4054  CD1 TRP A 383     5321   5286  16819    -16    399   -988       C  
ATOM   4055  CD2 TRP A 383      68.473 202.066  -0.376  1.00 78.50           C  
ANISOU 4055  CD2 TRP A 383     5493   6369  17965    199    762  -1100       C  
ATOM   4056  NE1 TRP A 383      70.595 202.233  -1.077  1.00 70.24           N  
ANISOU 4056  NE1 TRP A 383     5346   5221  16122    271    305  -1120       N  
ATOM   4057  CE2 TRP A 383      69.507 202.971  -0.690  1.00 73.65           C  
ANISOU 4057  CE2 TRP A 383     5432   5812  16741    421    496  -1198       C  
ATOM   4058  CE3 TRP A 383      67.241 202.570   0.051  1.00 81.67           C  
ANISOU 4058  CE3 TRP A 383     5397   6942  18692    308   1030  -1166       C  
ATOM   4059  CZ2 TRP A 383      69.346 204.352  -0.590  1.00 66.82           C  
ANISOU 4059  CZ2 TRP A 383     4688   5125  15577    735    444  -1351       C  
ATOM   4060  CZ3 TRP A 383      67.082 203.941   0.150  1.00 80.20           C  
ANISOU 4060  CZ3 TRP A 383     5366   6966  18140    653    972  -1345       C  
ATOM   4061  CH2 TRP A 383      68.129 204.817  -0.170  1.00 71.04           C  
ANISOU 4061  CH2 TRP A 383     4784   5813  16392    865    664  -1435       C  
ATOM   4062  N   LEU A 384      67.362 196.751   0.909  1.00 98.53           N  
ANISOU 4062  N   LEU A 384     7451   8232  21752  -1021   1455   -140       N  
ATOM   4063  CA  LEU A 384      66.448 195.616   0.904  1.00104.33           C  
ANISOU 4063  CA  LEU A 384     7901   8836  22903  -1249   1471     -4       C  
ATOM   4064  C   LEU A 384      66.577 194.727   2.134  1.00109.91           C  
ANISOU 4064  C   LEU A 384     8738   9510  23512  -1517   1983    429       C  
ATOM   4065  O   LEU A 384      65.575 194.157   2.577  1.00112.67           O  
ANISOU 4065  O   LEU A 384     8746   9852  24211  -1729   2266    616       O  
ATOM   4066  CB  LEU A 384      66.665 194.768  -0.354  1.00 90.96           C  
ANISOU 4066  CB  LEU A 384     6318   6925  21319  -1226    799   -196       C  
ATOM   4067  CG  LEU A 384      66.289 195.392  -1.697  1.00 89.66           C  
ANISOU 4067  CG  LEU A 384     6024   6724  21317   -975    250   -605       C  
ATOM   4068  CD1 LEU A 384      67.367 195.097  -2.724  1.00 84.92           C  
ANISOU 4068  CD1 LEU A 384     5836   6064  20366   -805   -288   -774       C  
ATOM   4069  CD2 LEU A 384      64.945 194.859  -2.172  1.00105.04           C  
ANISOU 4069  CD2 LEU A 384     7524   8521  23866  -1064     77   -683       C  
ATOM   4070  N   GLY A 385      67.771 194.604   2.710  1.00113.62           N  
ANISOU 4070  N   GLY A 385     9719   9951  23500  -1514   2100    597       N  
ATOM   4071  CA  GLY A 385      67.968 193.661   3.793  1.00125.16           C  
ANISOU 4071  CA  GLY A 385    11422  11325  24810  -1752   2487    996       C  
ATOM   4072  C   GLY A 385      68.011 192.243   3.286  1.00133.86           C  
ANISOU 4072  C   GLY A 385    12597  12194  26070  -1958   2089   1044       C  
ATOM   4073  O   GLY A 385      67.650 191.312   4.016  1.00144.64           O  
ANISOU 4073  O   GLY A 385    13969  13460  27527  -2233   2375   1364       O  
ATOM   4074  N   VAL A 386      68.459 192.049   2.046  1.00129.83           N  
ANISOU 4074  N   VAL A 386    12167  11602  25562  -1820   1438    739       N  
ATOM   4075  CA  VAL A 386      68.294 190.775   1.359  1.00137.99           C  
ANISOU 4075  CA  VAL A 386    13173  12423  26834  -1965   1006    719       C  
ATOM   4076  C   VAL A 386      69.446 189.793   1.535  1.00141.64           C  
ANISOU 4076  C   VAL A 386    14197  12773  26848  -1989    795    805       C  
ATOM   4077  O   VAL A 386      69.243 188.572   1.496  1.00143.89           O  
ANISOU 4077  O   VAL A 386    14553  12849  27269  -2188    605    919       O  
ATOM   4078  CB  VAL A 386      67.962 191.003  -0.130  1.00135.81           C  
ANISOU 4078  CB  VAL A 386    12652  12119  26829  -1761    422    335       C  
ATOM   4079  CG1 VAL A 386      69.104 191.705  -0.860  1.00129.10           C  
ANISOU 4079  CG1 VAL A 386    12221  11298  25534  -1513    -77     97       C  
ATOM   4080  CG2 VAL A 386      67.643 189.682  -0.792  1.00142.05           C  
ANISOU 4080  CG2 VAL A 386    13117  12689  28165  -1961    193    367       C  
ATOM   4081  N   HIS A 387      70.661 190.311   1.730  1.00143.92           N  
ANISOU 4081  N   HIS A 387    14891  13184  26606  -1783    802    737       N  
ATOM   4082  CA  HIS A 387      71.786 189.438   2.049  1.00149.96           C  
ANISOU 4082  CA  HIS A 387    16200  13859  26920  -1781    629    806       C  
ATOM   4083  C   HIS A 387      71.953 189.118   3.534  1.00164.05           C  
ANISOU 4083  C   HIS A 387    18261  15528  28544  -1997   1105   1199       C  
ATOM   4084  O   HIS A 387      72.344 188.008   3.909  1.00170.99           O  
ANISOU 4084  O   HIS A 387    19437  16200  29332  -2160    976   1347       O  
ATOM   4085  CB  HIS A 387      73.090 190.105   1.609  1.00139.30           C  
ANISOU 4085  CB  HIS A 387    15176  12693  25058  -1476    439    580       C  
ATOM   4086  CG  HIS A 387      73.225 190.248   0.124  1.00130.26           C  
ANISOU 4086  CG  HIS A 387    14146  11579  23767  -1308   -134    293       C  
ATOM   4087  ND1 HIS A 387      72.655 191.290  -0.575  1.00125.87           N  
ANISOU 4087  ND1 HIS A 387    13354  11158  23312  -1117   -439      0       N  
ATOM   4088  CD2 HIS A 387      73.862 189.480  -0.791  1.00127.34           C  
ANISOU 4088  CD2 HIS A 387    14116  11121  23146  -1285   -438    256       C  
ATOM   4089  CE1 HIS A 387      72.938 191.155  -1.859  1.00123.82           C  
ANISOU 4089  CE1 HIS A 387    13282  10913  22852   -986   -871   -184       C  
ATOM   4090  NE2 HIS A 387      73.669 190.066  -2.016  1.00125.04           N  
ANISOU 4090  NE2 HIS A 387    13762  10937  22810  -1079   -877    -46       N  
ATOM   4091  N   HIS A 388      71.633 190.088   4.384  1.00169.73           N  
ANISOU 4091  N   HIS A 388    18926  16364  29198  -1982   1653   1373       N  
ATOM   4092  CA  HIS A 388      71.826 189.951   5.825  1.00176.19           C  
ANISOU 4092  CA  HIS A 388    20095  17098  29753  -2118   2152   1761       C  
ATOM   4093  C   HIS A 388      70.709 190.604   6.634  1.00182.87           C  
ANISOU 4093  C   HIS A 388    20583  18080  30821  -2205   2838   1995       C  
ATOM   4094  O   HIS A 388      69.535 190.278   6.467  1.00186.58           O  
ANISOU 4094  O   HIS A 388    20554  18564  31772  -2410   2968   2058       O  
ATOM   4095  CB  HIS A 388      73.190 190.454   6.309  1.00173.03           C  
ANISOU 4095  CB  HIS A 388    20284  16718  28742  -1865   2114   1730       C  
ATOM   4096  CG  HIS A 388      73.235 190.791   7.768  1.00177.41           C  
ANISOU 4096  CG  HIS A 388    21171  17252  28985  -1860   2715   2081       C  
ATOM   4097  ND1 HIS A 388      73.046 189.849   8.757  1.00183.58           N  
ANISOU 4097  ND1 HIS A 388    22232  17856  29666  -2090   2994   2452       N  
ATOM   4098  CD2 HIS A 388      73.451 191.968   8.404  1.00176.14           C  
ANISOU 4098  CD2 HIS A 388    21166  17214  28544  -1624   3089   2123       C  
ATOM   4099  CE1 HIS A 388      73.141 190.435   9.938  1.00185.04           C  
ANISOU 4099  CE1 HIS A 388    22739  18083  29485  -1971   3531   2708       C  
ATOM   4100  NE2 HIS A 388      73.386 191.719   9.752  1.00180.36           N  
ANISOU 4100  NE2 HIS A 388    22083  17667  28780  -1676   3601   2511       N  
TER    4101      HIS A 388                                                      
HETATM 4102  N1  NU8 A1201      97.663 224.946   1.439  1.00 70.55           N  
HETATM 4103  N3  NU8 A1201      95.304 224.865   1.478  1.00 74.02           N  
HETATM 4104  C4  NU8 A1201      96.541 224.880   2.149  1.00 72.48           C  
HETATM 4105  C5  NU8 A1201      94.196 225.461   1.921  1.00 74.65           C  
HETATM 4106  C6  NU8 A1201      96.518 224.796   3.535  1.00 72.07           C  
HETATM 4107  C7  NU8 A1201      90.742 227.504   4.947  0.29 65.34           C  
HETATM 4108  C8  NU8 A1201      90.628 226.165   4.470  0.75 66.09           C  
HETATM 4109  C10 NU8 A1201      92.942 226.242   3.792  1.00 69.24           C  
HETATM 4110  C13 NU8 A1201      97.193 220.476  -0.280  1.00 78.71           C  
HETATM 4111  C15 NU8 A1201      95.276 221.771   0.438  1.00 78.48           C  
HETATM 4112  C17 NU8 A1201      97.192 222.845  -0.500  1.00 78.90           C  
HETATM 4113  C20 NU8 A1201      89.373 224.170   4.079  1.00 65.67           C  
HETATM 4114  C1  NU8 A1201      97.721 224.797   4.215  1.00 71.80           C  
HETATM 4115  C11 NU8 A1201      92.990 227.572   4.273  0.64 67.68           C  
HETATM 4116  C12 NU8 A1201      95.306 224.339   0.143  1.00 76.44           C  
HETATM 4117  C14 NU8 A1201      95.917 220.545   0.275  1.00 78.60           C  
HETATM 4118  C16 NU8 A1201      95.928 222.948   0.040  1.00 78.66           C  
HETATM 4119  C18 NU8 A1201      97.824 221.633  -0.662  1.00 78.51           C  
HETATM 4120  C19 NU8 A1201      89.806 229.530   6.026  1.00 61.68           C  
HETATM 4121  C2  NU8 A1201      98.888 224.880   3.486  1.00 71.02           C  
HETATM 4122  C3  NU8 A1201      98.807 224.954   2.108  1.00 70.64           C  
HETATM 4123  C9  NU8 A1201      91.742 225.551   3.898  0.60 67.22           C  
HETATM 4124  F1  NU8 A1201      97.848 219.318  -0.459  1.00 79.41           F  
HETATM 4125  F2  NU8 A1201      94.048 221.813   0.962  1.00 77.18           F  
HETATM 4126  F3  NU8 A1201      97.814 223.933  -0.881  1.00 78.92           F  
HETATM 4127  N2  NU8 A1201      91.916 228.200   4.840  0.87 67.10           N  
HETATM 4128  N4  NU8 A1201      94.073 225.580   3.334  1.00 72.37           N  
HETATM 4129  O1  NU8 A1201      93.336 225.900   1.216  1.00 74.92           O  
HETATM 4130  O2  NU8 A1201      95.053 225.403   5.607  1.00 71.90           O  
HETATM 4131  O3  NU8 A1201      94.467 223.388   4.239  1.00 73.29           O  
HETATM 4132  O4  NU8 A1201      89.705 228.212   5.545  1.00 62.85           O  
HETATM 4133  O5  NU8 A1201      89.448 225.483   4.588  1.00 65.83           O  
HETATM 4134  S1  NU8 A1201      95.011 224.701   4.363  1.00 73.64           S  
HETATM 4135  N   NO3 A1202     137.767 178.784 -28.087  1.00 92.32           N  
HETATM 4136  O1  NO3 A1202     136.816 178.416 -28.726  1.00 92.29           O  
HETATM 4137  O2  NO3 A1202     137.979 180.138 -27.954  1.00 92.36           O  
HETATM 4138  O3  NO3 A1202     138.400 177.933 -27.200  1.00 92.15           O  
HETATM 4139  N   NO3 A1203     107.613 158.786 -17.858  1.00100.04           N  
HETATM 4140  O1  NO3 A1203     106.805 158.053 -18.385  1.00 99.85           O  
HETATM 4141  O2  NO3 A1203     107.644 160.143 -18.191  1.00 99.66           O  
HETATM 4142  O3  NO3 A1203     108.295 158.325 -16.741  1.00 99.98           O  
HETATM 4143  O1  PG4 A1204      93.864 233.079   1.529  1.00 73.32           O  
HETATM 4144  C1  PG4 A1204      92.719 233.855   1.162  1.00 72.58           C  
HETATM 4145  C2  PG4 A1204      92.103 233.258  -0.095  1.00 72.06           C  
HETATM 4146  O2  PG4 A1204      92.998 233.424  -1.194  1.00 71.46           O  
HETATM 4147  C3  PG4 A1204      92.578 232.631  -2.300  1.00 71.87           C  
HETATM 4148  C4  PG4 A1204      92.847 233.371  -3.604  1.00 72.68           C  
HETATM 4149  O3  PG4 A1204      94.121 234.012  -3.566  1.00 73.04           O  
HETATM 4150  C5  PG4 A1204      94.688 234.069  -4.874  1.00 74.07           C  
HETATM 4151  C6  PG4 A1204      95.329 235.429  -5.129  1.00 75.35           C  
HETATM 4152  O4  PG4 A1204      96.205 235.775  -4.058  1.00 75.69           O  
HETATM 4153  C7  PG4 A1204      96.727 237.095  -4.208  1.00 75.87           C  
HETATM 4154  C8  PG4 A1204      96.962 237.712  -2.833  1.00 77.02           C  
HETATM 4155  O5  PG4 A1204      97.865 236.898  -2.075  1.00 78.47           O  
HETATM 4156  O1  PG4 A1205     121.938 181.560   2.659  1.00 53.42           O  
HETATM 4157  C1  PG4 A1205     121.119 180.757   3.516  1.00 55.19           C  
HETATM 4158  C2  PG4 A1205     119.799 180.420   2.828  1.00 59.21           C  
HETATM 4159  O2  PG4 A1205     118.968 181.577   2.753  1.00 63.32           O  
HETATM 4160  C3  PG4 A1205     117.586 181.222   2.710  1.00 64.12           C  
HETATM 4161  C4  PG4 A1205     116.734 182.463   2.944  1.00 64.39           C  
HETATM 4162  O3  PG4 A1205     116.938 183.376   1.870  1.00 65.91           O  
HETATM 4163  C5  PG4 A1205     116.134 184.546   2.005  1.00 66.41           C  
HETATM 4164  C6  PG4 A1205     116.218 185.349   0.713  1.00 67.47           C  
HETATM 4165  O4  PG4 A1205     117.573 185.741   0.502  1.00 69.92           O  
HETATM 4166  C7  PG4 A1205     117.871 185.911  -0.882  1.00 71.01           C  
HETATM 4167  C8  PG4 A1205     119.383 185.989  -1.050  1.00 70.46           C  
HETATM 4168  O5  PG4 A1205     119.976 184.791  -0.536  1.00 70.12           O  
HETATM 4169  C1  OLA A1206      76.282 220.382 -13.138  1.00 68.76           C  
HETATM 4170  O1  OLA A1206      76.519 221.057 -14.163  1.00 69.00           O  
HETATM 4171  O2  OLA A1206      75.274 220.565 -12.421  1.00 70.15           O  
HETATM 4172  C2  OLA A1206      77.255 219.296 -12.743  1.00 66.75           C  
HETATM 4173  C3  OLA A1206      77.988 219.693 -11.466  1.00 64.41           C  
HETATM 4174  C4  OLA A1206      79.198 220.574 -11.760  1.00 61.90           C  
HETATM 4175  C5  OLA A1206      80.504 219.825 -11.511  1.00 59.37           C  
HETATM 4176  C6  OLA A1206      81.703 220.755 -11.664  1.00 59.12           C  
HETATM 4177  C7  OLA A1206      82.205 221.244 -10.309  1.00 60.12           C  
HETATM 4178  C8  OLA A1206      82.373 222.759 -10.282  1.00 61.39           C  
HETATM 4179  C9  OLA A1206      83.765 223.110  -9.809  1.00 62.22           C  
HETATM 4180  C10 OLA A1206      84.291 224.303 -10.082  1.00 61.96           C  
HETATM 4181  C11 OLA A1206      83.498 225.328 -10.856  1.00 61.34           C  
HETATM 4182  C1  OLA A1207      95.050 220.762  18.727  1.00 68.33           C  
HETATM 4183  O1  OLA A1207      93.825 220.517  18.683  1.00 68.05           O  
HETATM 4184  O2  OLA A1207      95.853 220.101  19.420  1.00 67.24           O  
HETATM 4185  C2  OLA A1207      95.584 221.917  17.914  1.00 69.00           C  
HETATM 4186  C3  OLA A1207      95.429 223.197  18.727  1.00 67.89           C  
HETATM 4187  C4  OLA A1207      96.466 224.244  18.338  1.00 65.96           C  
HETATM 4188  C5  OLA A1207      96.296 225.484  19.205  1.00 64.66           C  
HETATM 4189  C6  OLA A1207      97.478 226.436  19.065  1.00 64.67           C  
HETATM 4190  C7  OLA A1207      97.098 227.664  18.247  1.00 64.17           C  
HETATM 4191  C8  OLA A1207      97.820 228.900  18.770  1.00 64.09           C  
HETATM 4192  C1  OLA A1208     105.634 200.777   7.447  1.00 73.22           C  
HETATM 4193  O1  OLA A1208     105.311 199.696   7.984  1.00 74.28           O  
HETATM 4194  O2  OLA A1208     105.225 201.128   6.318  1.00 74.32           O  
HETATM 4195  C2  OLA A1208     106.554 201.706   8.201  1.00 70.53           C  
HETATM 4196  C3  OLA A1208     105.743 202.449   9.254  1.00 68.84           C  
HETATM 4197  C4  OLA A1208     106.452 203.717   9.712  1.00 66.52           C  
HETATM 4198  C5  OLA A1208     105.461 204.868   9.855  1.00 63.82           C  
HETATM 4199  C6  OLA A1208     105.836 206.029   8.940  1.00 60.84           C  
HETATM 4200  C7  OLA A1208     105.321 207.342   9.517  1.00 57.32           C  
HETATM 4201  C8  OLA A1208     105.975 208.561   8.873  1.00 54.37           C  
HETATM 4202  C9  OLA A1208     106.794 209.285   9.919  1.00 50.99           C  
HETATM 4203  C10 OLA A1208     107.520 210.359   9.616  1.00 47.03           C  
HETATM 4204  C11 OLA A1208     107.543 210.915   8.214  1.00 44.70           C  
HETATM 4205  C12 OLA A1208     106.981 212.331   8.252  1.00 45.32           C  
HETATM 4206  C13 OLA A1208     107.907 213.321   7.558  1.00 47.37           C  
HETATM 4207  C14 OLA A1208     107.580 214.750   7.974  1.00 50.04           C  
HETATM 4208  C15 OLA A1208     108.844 215.482   8.410  1.00 52.93           C  
HETATM 4209  C16 OLA A1208     108.677 216.995   8.323  1.00 54.23           C  
HETATM 4210  C17 OLA A1208     109.938 217.643   7.757  1.00 53.87           C  
HETATM 4211  C18 OLA A1208     109.724 219.108   7.442  1.00 53.41           C  
HETATM 4212  C1  OLA A1209     116.175 197.771   3.582  1.00 74.38           C  
HETATM 4213  O1  OLA A1209     116.542 196.645   3.982  1.00 74.39           O  
HETATM 4214  O2  OLA A1209     116.051 198.756   4.342  1.00 75.18           O  
HETATM 4215  C2  OLA A1209     115.860 197.939   2.114  1.00 72.99           C  
HETATM 4216  C3  OLA A1209     116.196 199.357   1.667  1.00 72.21           C  
HETATM 4217  C4  OLA A1209     114.937 200.131   1.294  1.00 71.40           C  
HETATM 4218  C5  OLA A1209     115.278 201.310   0.390  1.00 71.00           C  
HETATM 4219  C6  OLA A1209     114.020 201.897  -0.241  1.00 69.85           C  
HETATM 4220  C7  OLA A1209     113.820 201.427  -1.678  1.00 68.73           C  
HETATM 4221  C8  OLA A1209     114.498 202.360  -2.678  1.00 68.21           C  
HETATM 4222  C9  OLA A1209     113.762 202.282  -3.994  1.00 68.33           C  
HETATM 4223  C10 OLA A1209     114.396 202.532  -5.137  1.00 68.86           C  
HETATM 4224  C11 OLA A1209     115.866 202.876  -5.129  1.00 69.09           C  
HETATM 4225  O   HOH A1301      89.508 215.074   0.798  1.00 51.24           O  
HETATM 4226  O   HOH A1302     124.283 173.707  -8.003  1.00 55.21           O  
HETATM 4227  O   HOH A1303     137.192 176.001  -9.160  1.00 43.34           O  
HETATM 4228  O   HOH A1304     132.584 158.280 -19.465  1.00 30.00           O  
HETATM 4229  O   HOH A1305     128.194 164.755 -29.341  1.00 39.84           O  
HETATM 4230  O   HOH A1306      83.936 228.990  16.297  1.00 32.47           O  
HETATM 4231  O   HOH A1307      90.477 241.842 -10.984  1.00 34.89           O  
HETATM 4232  O   HOH A1308     114.927 181.707 -27.596  1.00 62.26           O  
HETATM 4233  O   HOH A1309      89.922 208.489   0.040  1.00 38.65           O  
HETATM 4234  O   HOH A1310      90.623 223.275   0.513  1.00 38.80           O  
HETATM 4235  O   HOH A1311     130.567 158.515 -24.293  1.00 42.92           O  
HETATM 4236  O   HOH A1312      93.823 228.523  -0.885  1.00 31.07           O  
HETATM 4237  O   HOH A1313     122.090 178.350  -2.739  1.00 24.42           O  
HETATM 4238  O   HOH A1314      96.014 238.304 -11.975  1.00 49.91           O  
HETATM 4239  O   HOH A1315      91.593 192.888  -3.897  1.00 32.36           O  
HETATM 4240  O   HOH A1316     116.968 154.619 -16.087  1.00 52.95           O  
HETATM 4241  O   HOH A1317     105.202 221.165   8.231  1.00 50.79           O  
HETATM 4242  O   HOH A1318     102.311 189.628  -0.025  1.00 48.96           O  
HETATM 4243  O   HOH A1319     138.795 183.237 -27.448  1.00 55.08           O  
HETATM 4244  O   HOH A1320     139.009 180.523 -24.142  1.00 33.49           O  
HETATM 4245  O   HOH A1321     140.676 176.656 -29.184  1.00 30.77           O  
HETATM 4246  O   HOH A1322      81.494 240.758  -1.813  1.00 41.63           O  
HETATM 4247  O   HOH A1323     125.094 164.029 -29.869  1.00 39.83           O  
HETATM 4248  O   HOH A1324     125.228 157.483 -25.403  1.00 41.84           O  
HETATM 4249  O   HOH A1325      93.017 236.927  -0.330  1.00 34.31           O  
HETATM 4250  O   HOH A1326     137.156 172.684 -31.495  1.00 56.17           O  
HETATM 4251  O   HOH A1327      91.740 211.807   0.749  1.00 90.07           O  
HETATM 4252  O   HOH A1328      90.072 186.056 -14.253  1.00 65.98           O  
HETATM 4253  O   HOH A1329     125.153 163.714 -33.961  1.00 35.29           O  
HETATM 4254  O   HOH A1330      97.831 191.304  -2.614  1.00 37.90           O  
HETATM 4255  O   HOH A1331     112.242 175.562  -0.932  1.00 33.77           O  
HETATM 4256  O   HOH A1332      75.442 198.469   5.842  1.00 44.58           O  
HETATM 4257  O   HOH A1333      94.771 194.075  -1.084  1.00 37.92           O  
HETATM 4258  O   HOH A1334     120.224 180.552 -27.300  1.00 50.59           O  
HETATM 4259  O   HOH A1335     119.646 173.560  -1.044  1.00 31.27           O  
HETATM 4260  O   HOH A1336      87.996 234.035   4.011  1.00 22.17           O  
HETATM 4261  O   HOH A1337      79.675 246.421   9.961  1.00 38.62           O  
HETATM 4262  O   HOH A1338      84.930 235.249  -9.362  1.00 35.90           O  
HETATM 4263  O   HOH A1339     129.940 187.567 -18.247  1.00 37.69           O  
HETATM 4264  O   HOH A1340     133.112 172.019 -32.756  1.00 41.01           O  
HETATM 4265  O   HOH A1341      90.012 190.221  -6.512  1.00 46.60           O  
HETATM 4266  O   HOH A1342     130.028 162.901 -31.261  1.00 19.31           O  
HETATM 4267  O   HOH A1343     135.176 187.773 -20.073  1.00 25.40           O  
HETATM 4268  O   HOH A1344     112.773 194.926 -11.434  1.00 42.98           O  
HETATM 4269  O   HOH A1345     128.719 166.985 -33.201  1.00 30.00           O  
HETATM 4270  O   HOH A1346     119.917 157.249 -33.705  1.00 23.19           O  
CONECT  783 1392                                                                
CONECT 1392  783                                                                
CONECT 1781 1787                                                                
CONECT 1787 1781 1788                                                           
CONECT 1788 1787 1789 1795                                                      
CONECT 1789 1788 1790                                                           
CONECT 1790 1789 1791                                                           
CONECT 1791 1790 1792                                                           
CONECT 1792 1791 1793 1794                                                      
CONECT 1793 1792                                                                
CONECT 1794 1792                                                                
CONECT 1795 1788 1796 1797                                                      
CONECT 1796 1795                                                                
CONECT 1797 1795                                                                
CONECT 4102 4104 4122                                                           
CONECT 4103 4104 4105 4116                                                      
CONECT 4104 4102 4103 4106                                                      
CONECT 4105 4103 4128 4129                                                      
CONECT 4106 4104 4114 4134                                                      
CONECT 4107 4108 4127 4132                                                      
CONECT 4108 4107 4123 4133                                                      
CONECT 4109 4115 4123 4128                                                      
CONECT 4110 4117 4119 4124                                                      
CONECT 4111 4117 4118 4125                                                      
CONECT 4112 4118 4119 4126                                                      
CONECT 4113 4133                                                                
CONECT 4114 4106 4121                                                           
CONECT 4115 4109 4127                                                           
CONECT 4116 4103 4118                                                           
CONECT 4117 4110 4111                                                           
CONECT 4118 4111 4112 4116                                                      
CONECT 4119 4110 4112                                                           
CONECT 4120 4132                                                                
CONECT 4121 4114 4122                                                           
CONECT 4122 4102 4121                                                           
CONECT 4123 4108 4109                                                           
CONECT 4124 4110                                                                
CONECT 4125 4111                                                                
CONECT 4126 4112                                                                
CONECT 4127 4107 4115                                                           
CONECT 4128 4105 4109 4134                                                      
CONECT 4129 4105                                                                
CONECT 4130 4134                                                                
CONECT 4131 4134                                                                
CONECT 4132 4107 4120                                                           
CONECT 4133 4108 4113                                                           
CONECT 4134 4106 4128 4130 4131                                                 
CONECT 4135 4136 4137 4138                                                      
CONECT 4136 4135                                                                
CONECT 4137 4135                                                                
CONECT 4138 4135                                                                
CONECT 4139 4140 4141 4142                                                      
CONECT 4140 4139                                                                
CONECT 4141 4139                                                                
CONECT 4142 4139                                                                
CONECT 4143 4144                                                                
CONECT 4144 4143 4145                                                           
CONECT 4145 4144 4146                                                           
CONECT 4146 4145 4147                                                           
CONECT 4147 4146 4148                                                           
CONECT 4148 4147 4149                                                           
CONECT 4149 4148 4150                                                           
CONECT 4150 4149 4151                                                           
CONECT 4151 4150 4152                                                           
CONECT 4152 4151 4153                                                           
CONECT 4153 4152 4154                                                           
CONECT 4154 4153 4155                                                           
CONECT 4155 4154                                                                
CONECT 4156 4157                                                                
CONECT 4157 4156 4158                                                           
CONECT 4158 4157 4159                                                           
CONECT 4159 4158 4160                                                           
CONECT 4160 4159 4161                                                           
CONECT 4161 4160 4162                                                           
CONECT 4162 4161 4163                                                           
CONECT 4163 4162 4164                                                           
CONECT 4164 4163 4165                                                           
CONECT 4165 4164 4166                                                           
CONECT 4166 4165 4167                                                           
CONECT 4167 4166 4168                                                           
CONECT 4168 4167                                                                
CONECT 4169 4170 4171 4172                                                      
CONECT 4170 4169                                                                
CONECT 4171 4169                                                                
CONECT 4172 4169 4173                                                           
CONECT 4173 4172 4174                                                           
CONECT 4174 4173 4175                                                           
CONECT 4175 4174 4176                                                           
CONECT 4176 4175 4177                                                           
CONECT 4177 4176 4178                                                           
CONECT 4178 4177 4179                                                           
CONECT 4179 4178 4180                                                           
CONECT 4180 4179 4181                                                           
CONECT 4181 4180                                                                
CONECT 4182 4183 4184 4185                                                      
CONECT 4183 4182                                                                
CONECT 4184 4182                                                                
CONECT 4185 4182 4186                                                           
CONECT 4186 4185 4187                                                           
CONECT 4187 4186 4188                                                           
CONECT 4188 4187 4189                                                           
CONECT 4189 4188 4190                                                           
CONECT 4190 4189 4191                                                           
CONECT 4191 4190                                                                
CONECT 4192 4193 4194 4195                                                      
CONECT 4193 4192                                                                
CONECT 4194 4192                                                                
CONECT 4195 4192 4196                                                           
CONECT 4196 4195 4197                                                           
CONECT 4197 4196 4198                                                           
CONECT 4198 4197 4199                                                           
CONECT 4199 4198 4200                                                           
CONECT 4200 4199 4201                                                           
CONECT 4201 4200 4202                                                           
CONECT 4202 4201 4203                                                           
CONECT 4203 4202 4204                                                           
CONECT 4204 4203 4205                                                           
CONECT 4205 4204 4206                                                           
CONECT 4206 4205 4207                                                           
CONECT 4207 4206 4208                                                           
CONECT 4208 4207 4209                                                           
CONECT 4209 4208 4210                                                           
CONECT 4210 4209 4211                                                           
CONECT 4211 4210                                                                
CONECT 4212 4213 4214 4215                                                      
CONECT 4213 4212                                                                
CONECT 4214 4212                                                                
CONECT 4215 4212 4216                                                           
CONECT 4216 4215 4217                                                           
CONECT 4217 4216 4218                                                           
CONECT 4218 4217 4219                                                           
CONECT 4219 4218 4220                                                           
CONECT 4220 4219 4221                                                           
CONECT 4221 4220 4222                                                           
CONECT 4222 4221 4223                                                           
CONECT 4223 4222 4224                                                           
CONECT 4224 4223                                                                
MASTER      611    0   10   21    8    0   14    6 4269    1  137   44          
END